WO2007134262A2 - Crystal structure of prostasin and uses thereof - Google Patents

Abstract

The invention provides a crystallized prostasin molecule. The three-dimensional coordinates of the crystal structure of prostasin are obtained by X-ray diffraction. The coordinates can be used for studying the prostasin structure and designing, screening and developing compounds that modulate prostasin activity.

Description

CRYSTAL STRUCTURE OF PROSTASIN AND USES THEREOF

CROSS-REFERENCE TO RELATED APPLICATIONS

[0001] This application claims the benefit of priority to U.S. Provisional Patent

Application Number 60/799,839 filed 11 May 2006. The full disclosure of this application is incorporated herein by reference in its entirety and for all purposes

BACKGROUND OF THE INVENTION

Field of the Invention

[0002] The invention provides a crystallized prostasin molecule. The three- dimensional coordinates of the crystal structure of prostasin are obtained by X-ray diffraction. The coordinates can be used for studying the prostasin structure and designing, screening and developing compounds that modulate prostasin activity.

Background

[0003] Prostasin or human channel activating protein (h-CAP) is a type-1 membrane associated serine protease initially found in semen and subsequently in kidneys and the lining of the lung. In the epithelial cell lung lining Prostasin has been implicated in the activation of ENaC (endothelial cell Sodium channel). Inhibition of prostasin activity provides a potential mechanism of selectively inhibiting ENaC activation in the lung, thereby decreasing sodium hyper-absorption and mucociliary clearance in cystic fibrosis (CF) and possibly other lung disorders such as chronic obstructive pulmonary disease (COPD) and asthma.

[0004] The prostasin three dimensional coordinates of the invention can be used to design, screen and develop compounds that associate with and inhibit the activity of prostasin.

Summary of the Invention

[0005] The present invention provides the three-dimensional structure of prostasin thereby enabling identification and design of ligands or low molecular weight molecules that specifically bind to and modulate (inhibit) the activity of prostasin.

[0006] The present invention relates to: [0007] (i) a crystal of the prostasin polypeptide comprising the catalytic site with or without a ligand or low molecular weight compound;

[0008] (ii) a method of crystallizing the prostasin polypeptide; and

[0009] (iii) methods of using the three dimensional coordinates derived from said prostasin polypeptide crystal to identify/design small molecules capable of modulating prostasin activity.

BRIEF DESCRIPTION OF FIGURES

[0010] FIG. 1 : A ribbon diagram of prostasin detailing the overall fold of the molecule, colored from green to red dependant on the position of carbon alpha atoms within the molecule. A ball and stick representation of an inhibitor (DFFK-chloromethyl- ketone) is displayed to indicate the binding site.

[0011] FIG. 2: A representation of the electrostatic surface of the prostasin substrate binding site. Surface is colored red, blue and white to indicate electronegative, electropositive and charge neutral areas, respectively.

[0012] FIG. 3 : A structure alignment of prostasin with thrombin, trypsin and hepsin.

DETAILED DESCRIPTION OF THE INVENTION

Definitions

[0013] The term "binding partner" according to the invention refers to a ligand or low molecular weight molecule that associates with prostasin and either enhances the ability of prostasin to crystallize or modulates the activity of prostasin.

[0014] The term "space group" according to the invention refers to the arrangement of symmetry elements of the crystal.

[0015] The term "structure coordinates" or "three-dimensional coordinates" refers to mathematical coordinates derived from the placement of a polypeptide chain

(and the individual atoms thereof) in an electron density map. The electron density map is derived from mathematical equations related to the pattern obtained on diffraction of a monochromatic beam of X-rays by the atoms of a crystal of the invention. [0016] The term "unit cell" according to the invention, refers to the basic shape block. The entire volume of a crystal can be constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit cell pattern, the repetition of which builds the crystal.

Embodiments

[0017] The present invention relates to a prostasin polypeptide, a method of crystallizing a prostasin polypeptide and a prostasin polypeptide crystal. The invention further relates to the X-ray coordinates (also referred to as three dimensional or structural coordinates) of the structure of a prostasin polypeptide elucidated from a prostasin polypeptide crystal. Still further, the present invention relates to using the coordinates of a prostasin polypeptide to design and developing compounds that modulate the activity of said prostasin polypeptide.

[001 S] The full length sequence of human prostasin is known and is set forth in

Genbank Accession Number gi:2833277 and SwissProt Accession Number Q16651, which are incorporated herein by reference. As used herein, the prostasin polypeptide refers to that of SEQ. ID. No.: 1. The sequence has two truncations: the light chain (the first 44 residues; at the N-fermtnus; and 38 residues at the C -terminus. In addition, there are three point mutations: Cysteine 154 to Serine; Asparagine 159 to Glutamine; and Cysteine 203 to Serine.

[0019] SEP. ID. No.: 1:

>gil2833277lsplQ16651IPRSS8_HUMAN Prostasin:

ITGGSSAVAGQWPWQVSITYEGVHVCGGSLVSEQWVLS AAHCFPSEHHKEA YEV KLGAHQLDSYSEDAKVSTLKDIIPHPSYLQEGSQGDIALLQLSRPITFSRYIRPISLP AAQASFPNGLHCTVTGWGHV APSVSLLTPKPLQQLEVPLISRETSNCLYNID AKP EEPHFVQEDMVCAGYVEGGKDACQGDSGGPLSCPVEGLWYLTGIVSWGDACGA RNRPGVYTLASSYASWIQSKVTELQPRVVPQTQESQPDSNL

[0020] According to the invention, cDNA encoding prostasin (i.e., amino acid residues detailed in SEQ. ID No: 1) is inserted into a suitable expression vector and expressed in a suitable cell line. The cDNA also can include other regions that facilitate expression or achieve other objects, such as flanking regions, that otherwise do not depart from the essence of the invention. The cDNAs encoding the prostasin polypeptide, or functional portions thereof, can be altered by addition, substitution, deletion, or insertion.

Such alterations can be made, for example, to prevent glycosolation, prevent formation of incorrect or undesired disulfide bridges, and to enhance expression, purification and/or crystallization.

[0021] Recombinant expression vectors containing the nucleotide sequence encoding prostasin, or a portion thereof, can be prepared using methods known to those of skill in the art. Suitable host cells for expression of prostasin polypeptides include prokaryotic, yeast, and higher eukaryotic cells. Further examples of suitable expression systems that can be employed to express recombinant prostasin according to the present invention including mammalian or insect host cell culture expression systems, including baculo virus systems in insect cells and mammalian cell lines.

[0022] In one aspect of the invention, there is provided a composition comprising a polypeptide in crystalline form, wherein the polypeptide is a prostasin polypeptide.

[0023] In a further embodiment, the prostasin polypeptide is the expression product of a polynucleotide encoded by the amino acid residues of SEQ. ID No.: 1, or fragments and/or homologs thereof.

[0024] In a further embodiment of the invention, the composition above further comprises an optional binding partner suitable for co-crystallization with prostasin.

[0025] In a further embodiment, the binding partner is a small molecule or polypeptide binding partner.

[0026] In a further embodiment, the binding partner is a small molecule.

[0027] One aspect of the invention relates to a method of crystallizing a prostasin polypeptide with or without a binding partner. Crystals can be grown or formed by any suitable crystallization method such as vapor diffusion, sitting drop and the like (see Ducruix and Giege "Crystallization of Nucleic Acids and Proteins: A Practical Approach", Oxford University Press, 1992) and can be set up manually or automatically (using robotics) known in the art. The crystallization buffer can optionally comprise a number of elements that include, without limitation, buffers, salts, organics, additives, precipitating agents, etc. The pH can range, for example from about 4.0 to about 9.0. The claimed invention can encompass any and all methods of crystallization. One skilled in the art can choose any such methods and vary the parameters such that the chosen method results in the desired crystals. Crystals of the invention are screened for their ability to diffract X-rays to a resolution of 3.0 A or better and a complete data set can be collected from one or more crystals.

[0028] In a further aspect of the invention, is provided a method for crystallizing a prostasin polypeptide, comprising mixing a solution comprising a prostasin polypeptide, a binding partner and a crystallization buffer, or soaking an existing binding partner into the preformed prostasin crystals.

[0029] In a further embodiment, the method of crystallization is by sitting drop, the crystallization precipitant can be PEG-6000, PEG-4000 or PEG-ME 5000 at concentration between 16 and 26% with no buffer or in a MES, CITRATE or HEPES buffer between pH 5.0 and pH 7.0 with or without additional salts such as 0.2M Ammonium Sulphate, Potassium hydrogen phosphate. The prostasin polypeptide is at a final concentration of 20 mg/mL and the crystals are prepared in a temperature ranging from 4 to 20 ⁰C. A detailed description of the crystallization of the prostasin polypeptide of the invention is described in Example 1, infra.

[0030] In a further aspect, the above prostasin crystal diffracts X-rays to a resolution of at least 3.0 A, is of space group P2₁2₁2₁ with unit cell dimensions: a=52.9 ±5 A, b=54.8 ±5 A, c=83.0 ±5 A, α =90 degrees, β =90 degrees and γ =90 degrees. Depending on the particular conditions for crystallization, the parameters characterizing the unit cell can vary with a limited range, for example, a, b, and c each vary by up to 1OA and α, β and γ vary by up to 10 degrees.

[0031] Another aspect of the invention relates to the atomic structure of prostasin. The structure of prostasin can be determined utilizing a crystal comprising a prostasin polypeptide as described above. According to the present invention, the structure of prostasin is determined using X-ray crystallography. Any suitable X-ray diffraction method for obtaining three-dimensional structural coordinates of a polypeptide can be used (see, for example, International Tables for Crystallography: Volume F: Crystallography of biological macromolecules, editor M. G. Rossmann. For the present invention, see Example 2 {infra) for a detailed description of the structure determination of prostasin. [0032] In a further embodiment of the invention, the crystalline prostasin polypeptide has a three-dimensional structure characterized by the atomic structure coordinates given in Table 1, infra.

[0033] In another aspect of the invention is provided a computer-readable medium (such as, for example, a floppy disc, a hard disc, computer tape, RAM, ROM, CD, DVD, a magnetic disk, an optical disk, and the like) having recorded thereon structural coordinate data for prostasin (such as set forth in Table 1), or a portion thereof. [0034] In one embodiment, the computer-readable medium has recorded thereon machine-readable data, wherein the computer-readable medium, when used in conjunction with a machine programmed with instructions for using the data, is capable of generating image signals for depicting a graphical, three-dimensional representation of the prostasin polypeptide, or portion thereof.

[0035] In a further embodiment of the invention, there is provided a system for studying a prostasin polypeptide, said system comprising (a) a memory capable of storing information representing at least a portion of the prostasin polypeptide, wherein said memory comprises at least one first-type storage region, including a set of spatial coordinates specifying a location in a three dimensional space, and at least one second- type storage region comprising information representing a characteristic of one of a plurality of amino acids, said second-type storage regions being logically associated with said first-type storage regions in said memory to represent a geometric arrangement of at least one characteristic of said prostasin peptide in said three dimensional space; (b) a processor coupled to said memory to access said first-type storage regions and said second-type storage regions, wherein the processor generates image signals for depicting a visual image representing three dimensional image of said prostasin polypeptide in said three dimensional space based on data from said memory; and (c) a display coupled to said processor to receive said image signals, wherein the display depicts a visual three dimensional image of said prostasin polypeptide in said three dimensional space based on said image signals.

[0036] The use of X-ray structure determination, molecular design and selection and synthesis of compounds that associate with other polypeptides is known in the art. This invention, however, for the first time allows the use of structural coordinates from the prostasin polypeptide of SEQ. ID. No.: 1 for molecular design, and selection and synthesis of compounds that associate with prostasin.

[0037] In one aspect of the invention, the structure coordinates of the invention can be displayed as, or converted to, a graphical representation, including three-dimensional shape representations. This can be accomplished using commercially available computer programs capable of generating graphical representations of molecules, or parts thereof, from a set of structural coordinates. Examples of computer programs capable of generating graphical representations of molecules, or parts thereof, from a set of structural coordinates are O (Alwyn Jones), Xfit, PyMOL, RasMol, and the like.

[0038] In another aspect of the invention, the structure of prostasin can be compared to, or superimposed over, other similar molecules, such as prostasin-like molecules. Comparison of prostasin and other molecules for which a graphical structure or three- dimensional structural coordinates are available can be carried out with the aide of available software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations, Inc., Waltham, Mass.).

[0039] Compounds that associate with prostasin can also be computationally evaluated and designed by screening and selecting chemical entities or fragments for their ability to associate with prostasin. Several methods can be used to accomplish this aspect of the invention.

[0040] In one embodiment, one may visually inspect a computer-generated model of prostasin based on the structure coordinates described herein. Computer generated models of chemical entities or specific chemical moieties can then be positioned in or around the catalytic domain and evaluated based on energy minimization and molecular dynamics, using, for example, available programs such as CHARMM or AMBER. Positioning of the chemical entity or fragment can be accomplished, for example, with docking software such as Quanta and Sybyl. Additionally, known and commercially available computer programs can be used in selecting chemical entities or fragments. Once suitable chemical entities or fragments are selected, they can be assembled into a single compound, such as an inhibitor, mediator, or other regulatory compound. Known and commercially available model building software may assist in assembly. [0041] In one aspect of the invention, compounds that associate with prostasin can be designed as a whole, rather than by assembly of specific chemical moieties or chemical entities. This embodiment can be carried out using computer programs such as LUDI (Biosym Technologies, San Diego, Calif.), LEGEND (Molecular Simulations, Burlington, Mass.), and Leap Frog (Tripos Associates, St. Louis, Mo.).

[0042] In one embodiment, a candidate compound is chosen based upon the desired sites of interaction with prostasin and the candidate compound in light of the sites of interaction identified previously. Once the specific candidate compound-prostasin interactions are determined, docking studies, using commercially available docking software, are performed to provide preliminary "modeled" complexes of selected candidate compound with prostasin.

[0043] Constrained conformational analysis is performed using, for example, molecular dynamics (MD) to check the integrity of the modeled prostasin-inhibitor complex. Once the complex reaches its most favorable conformational state, the structure as proposed by the MD study is analyzed visually to ensure that the modeled complex complies with known experimental SAR/QSAR (structure-activity relationship/quantitative structure- activity relationship) based on measured binding affinities.

[0044] Other modeling techniques can also be used in accordance with the invention. Examples of these techniques are disclosed in Cohen et al., "Molecular Modeling Software and Methods for Medicinal Chemistry," J. Med. Chem., 33:883-894 (1990) and Navia et al., "The Use of Structural Information in Drug Design," Current Opinions in Structural Biology, 2:202-210 (1992), "Structure Based Drug Design", editor Verapandian herein incorporated by reference in the entirety.

[0045] Compounds developed or designed to associate with prostasin can be optimized or the efficiency of association can be tested using a number of methods known in the art. For example, the deformation energy and electrostatic interactions can be determined and optimized. Known and commercially available software and hardware systems can be used. Structure-based analoging for optimization of the inhibitor potency, selectivity and physical drug-like properties in an iterative manner can also be performed by one skilled in the art of drug design.

[0046] Substitutions can also be made to selected or designed compounds. These substitutions can be made to improve or modify the association properties of the compound. Such substitutions can be made, for example, in side groups or particular atoms of the compounds. Generally, one should begin with conservative substitutions that have approximately the same size, shape, charge and other characteristics of the original group or atom. Substituted compounds can be further analyzed and optimized as described above. [0047] In a further aspect of the invention, the potential inhibitory, mediatory, regulatory, or other binding effect of a compound can be analyzed and evaluated, using, for example, commercially available computer software, prior to actual synthesis and testing of such compound. In this way, one can evaluate the probability of synthesizing and testing of inoperative compounds.

[0048] In a further aspect of the invention, there is provided a method of identifying a compound that associates with prostasin, comprising: (a) designing an associating compound for said polypeptide that forms a bond with a site on the prostasin molecule based on all or part of the coordinates of a prostasin polypeptide crystal (Table 1); (b) synthesizing said compound; and (c) determining the capability of said compound to modulate the activity of said prostasin polypeptide.

[0049] In on embodiment, the identified compound interacts with a site on prostasin defined by at least one of the amino acids listed in Table 2. [0050] As used herein, "associate" means that the compounds may bind to or interact with prostasin ionically, covalently, via hydrogen bonding, Van der Waals interactions, salt bridges, steric interactions, hydrophilic interactions and/or hydrophobic interactions. Moreover, the term "associate" encompasses associations with any portion of prostasin. For example, compounds that associate with prostasin can be compounds that act as competitive inhibitors, un-competitive inhibitors, and non-competitive inhibitors. Compounds that associate with prostasin can also be compounds that act as mediators or other regulatory compounds. Compounds that associate with prostasin can also be compounds that isomerize to short-lived reaction intermediates in the chemical reaction of a substrate with prostasin. In particular, compounds designed to associate with prostasin can be used therapeutically as modulators of prostasin activity, such as inhibitors, mediators and other regulatory compounds.

[0051] In vitro procedures for measuring the effect of compounds have on modulating the activity of prostasin generally are known in the art. Description of Prostasin Structure

[0052] The three dimensional prostasin molecule of the invention can be described, with reference to the Figures.

[0053] FIG. 1 is a ribbon diagram of prostasin: Ribbon diagram of prostasin molecule detailing the overall fold of the molecule, colored from green to red dependant on the position of carbon alpha atoms within the molecule. A ball and stick representation of an inhibitor (DFFK-chloromethylketone)is displayed to indicate the binding site.

Figure produced with BobScript and Raster3D [Esnouf, 1997 #319; Kraulis, 1991 #329;

Merritt, 1994 #332]

[0054] FIG. 2 is a surface representation: Electrostatic surface representation of prostasin substrate binding site. Surface is colored red, blue and white to indicate electronegativity, electropositivity and neutrality respectively. Figure produced with

PYMOL and APBS [Baker, 2000 #2280]

[0055] FIG. 3 is a structure alignment: Structure alignment of the superposition of the structure of prostasin with related serine proteases, thrombin, trypsin and hepsin.

Figure produced by STAMP and ALSCRIPT [Russell, 1992 #984:Barton, 1993 #992]

[0056] In designing and developing compounds that modulate prostasin activity, such as inhibitors, mediators and other compounds having activities with biological significance, that associate with prostasin, it is desirable to select compounds with a view toward the particular surface contour, charge, shape, and other physical characteristics of prostasin. Generally, the compounds should be capable of physically and structurally associating with prostasin.

[0057] The prostasin crystal structure of the invention demonstrates several structural peculiarities regarding surface contour, charge and shape, which facilitates the design of potent selective modulators of prostasin activity, particularly modulators that associate with the residues described in Table 2.

Examples:

[0058] The following examples serve to illustrate the present invention but should not be construed as a limitation thereof. Example 1

Expression and Crystallization of Prostasin

[0059] The DNA sequence encoding prostasin residues 45 to 305 is amplified from a full length construct in a mammalian expression vector by PCR. The 3' primer incorporates a stop codon and an overhanging Pad site. The PCR product is digested with Pad before ligating into the MHBa plasmid which has been prepared by digestion with PmII and Pad. Cloning into the MH4Ba plasmid adds the sequence MKFLVNVALVFMVVYISYIYA to the N-terminus of the translated construct (which comprises the first 21 N-terminal residues of honeybee melittin and serves as a secretion signal), and HHHHHH to the C-terminus.

[0060] The resultant plasmid is transfected into DHlOBac , plated on LB plates with 7μg/ml gentamycin, 50μg/ml kanamycin, lOμg/ml tetracycline, lOOμg/ml bluo-gal, and 40μg/ml IPTG. Bacmid- positive colonies are transfected into SF9 cells using standard Cellfectin protocol, and amplified to >= lxl0^Λ8 virus/ml. [0061] The resultant prostasin construct is expressed in 2xlOL of Sf9 cells in

Wave Bioreactors (Wave) infected at a cell density of 0.8xl0^Λ6 cells/ml and an MOI of 0.1. Cells are then incubated at 27°C.

[0062] Cells are removed by centrifugation for 10 minutes at 1500 x g, and the pH of the supernatant is adjusted to 7.5 by adding ION NaOH. The pH-adjusted supernatant is placed at 4-10⁰C for 2-16 hours, then centrifuged again at 4200xg for 10- 15 minutes to clarify. Further clarification is achieved by pumping the pH adjusted supernatant through a Sartoban P Sterile Capsule 0.45+0.2 um (Sartorius). The final clarified supernatant is then concentrated to about IL by ultrafiltration using a Slice ultrafiltration unit (Sartorius) loaded with Slice Crossflow 1OK MWCO Membrane. The IL of concentrate is then diafiltered at constant volume against approximately 20 volumes of 50 mM potassium phosphate pH 7.5, 200 mM NaCl until the diafiltrate is clear (without color). The buffer exchanged concentrate is further concentrated to 500 ml and harvested from the unit to a final volume of approximately 2L once the system is washed with buffer to recover all possible protein.

[0063] The diafiltered concentrate is loaded onto a 10 ml Sepharose Fast Flow column (Amersham) previously charged with NiCl₂ and equilibrated with 50 mM potassium phosphate pH 7.5, 300 mM NaCl, 5%v glycerol. The column is washed with the above buffer until no additional protein flowed through as judged by online OD(280) absorbance. The column is then eluted with imidazole spiked in the above buffer in three steps, 10 mM, 25 mM, and 150 mM.

[0064] The prostasin eluted in the 150 mM step fraction- appropriate fractions as judged by SDS-PAGE gel are pooled. The pooled fractions are dialyzed against 20 mM TrisCl pH 7.9 (adjusted at RT), 50 mM NaCl, 5% glycerol, then loaded onto a 6 ml Resource Q column (Amersham). The column is eluted with a 30 CV gradient from the above buffer to the above buffer containing IM NaCl.

[0065] Appropriate fractions as judged by SDS-PAGE gel are pooled and dialyzed against a 2OmM Tris buffer with 15OmM NaCL at pH 7.0 , concentrated to 20mg/ml (as assayed by Bradford against BSA std) using 10,000 MWCO spin concentrators [0066] Sitting drop vapour diffusion crystallization plates are set up in low profile

Greiner 96 well crystallization plates. A reservoir of 50μl of crystallization solution is added to the well reservoir whilst equal volumes of protein and crystallization solution (20OnI) are added to the crystallization shelf. Crystals formed within 3 weeks in a variety of conditions all involving 16-26% w/v PEG-4000 and a pH of less than 7.0

Example 2

Structure Determination of Prostasin

[0067] Data for the prostasin structure is collected at a synchrotron X-ray source or on a rotating anode system. Data are processed with standard data reduction packages such as Mosflm or HKL2000 and diffract in excess of 2.0A resolution. The initial structure is solved by the molecular replacement technique using the coordinates of a homologous protein (human Beta Tryptase PDB code IAOL) and refined until convergence with the crystallographic refinement program Refmac5. [0068] The structure coordinates obtained from prostasin crystal of the invention are detailed in Table 1 , infra.

Table Ia

Structure Coordinates for APO (open version of Prostasin)

REMARK 3 REFINEMENT.

REMARK 3 PROGRAM : REFMAC 5.2.0005

REMARK 3 AUTHORS : MURSHUDOV, VAGIN, DODSON REMARK

REMARK REFINEMENT TARGET MAXIMUM LIKELIHOOD

REMARK

REMARK DATA USED IN REFINEMENT.

REMARK RESOLUTION RANGE HIGH (ANGSTROMS) 1.60

REMARK RESOLUTION RANGE LOW (ANGSTROMS) 45.18

REMARK DATA CUTOFF (SIGMA(F)) NONE

REMARK COMPLETENESS FOR RANGE (%) 90.34

REMARK NUMBER OF REFLECTIONS 27807

REMARK

REMARK FIT TO DATA USED IN REFINEMENT.

REMARK CROSS-VALIDATION METHOD THROUGHOUT

REMARK FREE R VALUE TEST SET SELECTION RANDOM

REMARK R VALUE (WORKING + TEST SET) 0.17827

REMARK R VALUE (WORKING 3ET) 0.17590

REMARK FREE R VALUE 0.22424

REMARK FREE R VALUE TEST 3ET SIZE (%) 5.0

REMARK FREE R VALUE TEST 3ET COUNT 1459

REMARK

REMARK FIT IN THE HIGHEST RESOLUTION BIN.

REMARK TOTAL NUMBER OF BINS USED 20

REMARK BIN RESOLUTION RANGE HIGH 1.600

REMARK BIN RESOLUTION RANGE LOW 1.642

REMARK REFLECTION IN BIN (WORKING SET) 1160

REMARK BIN COMPLETENESS (WORKING+TEST) (%) 51.41

REMARK BIN R VALUE (WORKING SET) 0.376

REMARK BIN FREE R VALUE 3ET COUNT 58

REMARK BIN FREE R VALUE 0.533

REMARK

REMARK NUMBER OF NON-HYDROGEN ATOME USED IN REFINEMENT.

REMARK ALL ATOMS : 2121

REMARK

REMARK B VALUES .

REMARK FROM WILSON PLOT (A**2) NULL

REMARK MEAN B VALUE (OVERALL, A**2) 17.076

REMARK OVERALL ANISOTROPIC B VALUE.

REMARK BIl (A**2) 0. 39

REMARK B22 (A**2) 0.

REMARK B33 (A**2) -1. 27

REMARK B12 (A**2) 0.00

REMARK B13 (A**2) 0.00

REMARK B23 (A**2) 0.00

REMARK

REMARK ESTIMATED OVERALL COORDINATE ERROR.

REMARK ESU BASED ON R VALUE (A)

0.098

REMARK ESU BASED ON FREE R VALUE (A)

0.104

REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A)

0.075

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

2.219

REMARK

REMARK 3 CORRELATION COEFFICIENTS.

REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965

REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945

REMARK 3

REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS

WEIGHT

REMARK BOND LENGTHS REFINED ATOMS (A) : 1952 ; 0.014; 0.021 REMARK 3 BOND LENGTHS OTHERS (A) 1707 ; 0.001 ;

0.020

REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES) 2665 ; 1.523 ;

1.955

REMARK 3 BOND ANGLES OTHERS (DEGREES) 3996 ; 0.768 ;

3.000

REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES) 246 ; 5.809 ;

5.000

REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES) 79 ;32.463

;24.430

REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES) 290 ;12.483

;15.000

REMARK TORSION ANGLES, PERIOD 4 (DEGREES) 7 ;22.991

;15.000

REMARK CHIRAL-CENTER RESTRAINTS (A**3) 288 ; 0.084 ;

0.200

REMARK GENERAL PLANES REFINED ATOMS (A) 2175 ; 0.007 ;

0.020

REMARK GENERAL PLANES OTHERS (A) 369 ; 0.001 ;

0.020

REMARK NON-BONDED CONTACTS REFINED ATOMS (A) 440 ; 0.202 ;

0.200

REMARK NON-BONDED CONTACTS OTHERS (A) 1888 ; 0.183 ;

0.200

REMARK NON-BONDED TORSION REFINED ATOMS (A) 979 ; 0.187 ;

0.200

REMARK NON-BONDED TORSION OTHERS (A) 1181 ; 0.091 ;

0.200

REMARK 3 H-BOND (X... Y) REFINED ATOMS (A) 182 ; 0.159 ;

0.200

REMARK 3 SYMMETRY VDW REFINED ATOMS (A) 19 ; 0.170 ;

0.200

REMARK 3 SYMMETRY VDW OTHERS (A) 82 ; 0.191 ;

0.200

REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A) 20 ; 0.165 ;

0.200

REMARK 3

REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS

WEIGHT

REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2) 1536 ; 1.713 ;

2.000

REMARK MAIN-CHAIN BOND OTHER ATOMS (A**2) 501 ; 0.350 ;

2.000

REMARK MAIN-CHAIN ANGLE REFINED ATOMS (A**2) 1981 ; 2.049 ;

3.000

REMARK SIDE-CHAIN BOND REFINED ATOMS (A**2) 851 ; 3.850 ;

5.000

REMARK SIDE-CHAIN ANGLE REFINED ATOMS (A**2) 684 ; 5.422 ;

8.000

REMARK

REMARK 3 NCS RESTRAINTS STATISTICS

REMARK 3 NUMBER OF NCS GROUPS : NULL

REMARK 3

REMARK 3

REMARK 3 TLS DETAILS

REMARK 3 NUMBER OF TLS GROUPS : NULL

REMARK 3

REMARK 3

REMARK 3 BULK SOLVENT MODELLING.

REMARK 3 METHOD USED : BABINET MODEL WITH MASK

REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20

REMARK 3 ION PROBE RADIUS : 0. 80

REMARK 3 SHRINKAGE RADIUS : 0. 80

REMARK 3

REMARK 3 OTHER REFINEMENT REMARKS:

REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITION S

REMARK 3

SSBOND 1 CYS B 70 CYS B 86

SSBOND 2 CYS B 168 CYS B 244

SSBOND 3 CYS B 201 CYS B 223

SSBOND 4 CYS B 234 CYS B 262

CISPEP 1 THR B 184 PRO B 185 0.00

CRYSTl 53 .556 54.071 82.678 90. 00 90.00 90.00 P 21 21 21

SCALEl 0.018672 0.000000 0.000000 0.00000

SCALE2 0.000000 0.018494 0.000000 0.00000

SCALE3 0.000000 0.000000 0.012095 0.00000

ATOM 1 N ILE B 45 3.904 32.536 4.482 1.00 13.68

ATOM 2 CA ILE B 45 3.480 32.154 3.109 1.00 13.87

ATOM 4 CB ILE B 45 2.947 30.703 3.051 1.00 13.84

ATOM 6 CGl ILE B 45 3.987 29.742 3.592 1.00 13.87

ATOM 9 CDl ILE B 45 5.160 29.460 2.666 1.00 17.37

ATOM 13 CG2 ILE B 45 2.445 30.353 1.654 1.00 14.25

ATOM 17 C ILE B 45 2.322 33.041 2.726 1.00 15.74

ATOM 18 O ILE B 45 1.268 33.036 3.397 1.00 15.32

ATOM 22 N THR B 46 2.494 33.786 1.647 1.00 14.74

ATOM 23 CA THR B 46 1.381 34.600 1.153 1.00 15.84

ATOM 25 CB THR B 46 1.798 36.021 0.803 1.00 17.30

ATOM 27 OGl THR B 46 0.610 36.803 0.646 1.00 19.67

ATOM 29 CG2 THR B 46 2.575 36.059 -0.469 1.00 21.00

ATOM 33 C THR B 46 0.754 33.944 -0.052 1.00 16.36

ATOM 34 O THR B 46 1.460 33.428 -0.936 1.00 14.86

ATOM 36 N GLY B 47 -0.574 33.958 -0.086 1.00 18.36

ATOM 37 CA GLY B 47 -1.324 33.430 -1.215 1.00 18.42

ATOM 40 C GLY B 47 -1.443 31.917 -1.269 1.00 19.12

ATOM 41 O GLY B 47 -1.728 31.347 -2.321 1.00 20.33

ATOM 43 N GLY B 48 -1.239 31.261 -0.138 1.00 19.17

ATOM 44 CA GLY B 48 -1.260 29.810 -0.076 1.00 18.78

ATOM 47 C GLY B 48 -2.533 29.368 0.590 1.00 19.54

ATOM 48 O GLY B 48 -3.543 30.063 0.508 1.00 20.69

ATOM 50 N SER B 49 -2.479 28.239 1.269 1.00 17.74

ATOM 51 CA SER B 49 -3.598 27.714 2.024 1.00 19.69

ATOM 53 CB SER B 49 -4.358 26.686 1.202 1.00 19.42

ATOM 56 OG SER B 49 -3.475 25.663 0.806 1.00 22.01

ATOM 58 C SER B 49 -3.103 27.024 3.284 1.00 19.62

ATOM 59 O 49 -1.925 26.701 3.392 1.00 20.24

ATOM 61 N Q-C¹P P, 50 -4.009 26.760 4.210 1.00 18.74

ATOM 62 CA SER B 50 -3.668 26.040 5.409 1.00 19.38

ATOM 64 CB SER B 50 -4.777 26.156 6.449 1.00 19.22

ATOM 67 OG SER B 50 -4.880 27.489 6.913 1.00 19.24

ATOM 69 C QfT¹P R 50 -3.455 24.573 5.075 1.00 19.83

ATOM 70 O SER B 50 -4.297 23.948 4.423 1.00 18.35

ATOM 72 N ALA B 51 -2.321 24.024 5.512 1.00 19.20

ATOM 73 CA ALA B 51 -2.066 22.608 5.431 1.00 19.72

ATOM 75 CB ALA B 51 -0.578 22.314 5.670 1.00 18.79

ATOM 79 C ALA B 51 -2.922 21.954 6.496 1.00 20.09

ATOM 80 O ALA B 51 -3.487 22.643 7.340 1.00 21.34

ATOM 82 N VAL B 52 -3.040 20.637 6.466 1.00 19.56

ATOM 83 CA VAL B 52 -3.711 19.950 7.555 1.00 21.40

ATOM 85 CB VAL B 52 -4.794 18.940 7.033 1.00 22.27

ATOM 87 CGl VAL B 52 -5.789 19.635 6.141 1.00 27.78

ATOM 91 CG2 VAL B 52 -4.199 17.825 6.311 1.00 26.21 ATOM 95 C VAL B 52 -2.638 19.274 8.427 1.00 20.36

ATOM 96 O VAL B 52 -1.553 18.997 7.961 1.00 20.34

ATOM 98 N ALA B 53 -2.943 19.016 9.694 1.00 18.80

ATOM 99 CA ALA B 53 -2.040 18.330 10.583 1.00 18.70

ATOM 101 CB ALA B 53 -2.726 18.032 11.898 1.00 19.09

ATOM 105 C ALA B 53 -1.537 17.050 9.958 1.00 18.90

ATOM 106 O ALA B 53 -2.309 16.310 9.347 1.00 18.31

ATOM 108 N GLY B 54 -0.233 16.801 10.085 1.00 18.95

ATOM 109 CA GLY B 54 0.382 15.582 9.524 1.00 18.91

ATOM 112 C GLY B 54 0.788 15.645 8.051 1.00 17.68

ATOM 113 O GLY B 54 1.477 14.744 7.564 1.00 16.91

ATOM 115 N GLN B 55 0.376 16.690 7.338 1.00 17.57

ATOM 116 CA GLN B 55 0.587 16.753 5.915 1.00 15.66

ATOM 118 CB GLN B 55 -0.253 17.897 5.319 1.00 15.52

ATOM 121 CG GLN B 55 -0.258 17.856 3.834 1.00 15.96

ATOM 124 CD GLN B 55 -1.242 18.815 3.199 1.00 18.22

ATOM 125 OEl GLN B 55 -1.292 18.945 1.967 1.00 24.22

ATOM 126 NE2 GLN B 55 -2.036 19.455 4.016 1.00 16.26

ATOM 129 C GLN B 55 2.063 16.908 5.525 1.00 15.74

ATOM 130 O GLN B 55 2.515 16.332 4.538 1.00 16.82

ATOM 132 N TRP B 56 2.789 17.721 6.287 1.00 14.98

ATOM 133 CA TRP B 56 4.204 18.044 5.973 1.00 13.66

ATOM 135 CB TRP B 56 4.353 19.519 5.565 1.00 11.95

ATOM 138 CG TRP B 56 3.502 19.833 4.383 1.00 11.65

ATOM 139 CDl TRP B 56 2.354 20.524 4.395 1.00 11.45

ATOM 141 NEl TRP B 56 1.823 20.599 3.130 1.00 13.41

ATOM 143 CE2 TRP B 56 2.658 19.954 2.264 1.00 12.26

ATOM 144 CD2 TRP B 56 3.742 19.464 3.030 1.00 12.90

ATOM 145 CE3 TRP B 56 4.757 18.776 2.383 1.00 13.48

ATOM 147 CZ3 TRP B 56 4.649 18.562 1.011 1.00 13.29

ATOM 149 CH2 TRP B 56 3.565 19.065 0.286 1.00 14.33

ATOM 151 CZ2 TRP B 56 2.563 19.759 0.888 1.00 14.78

ATOM 153 C TRP B 56 4.995 17.743 7.226 1.00 13.94

ATOM 154 O TRP B 56 5.500 18.659 7.878 1.00 11.61

ATOM 156 N PRO B 57 5.077 16.442 7.583 1.00 13.85

ATOM 157 CA PRO B 57 5.567 16.071 8.917 1.00 12.72

ATOM 159 CB PRO B 57 5.217 14.587 9.027 1.00 14.27

ATOM 162 CG PRO B 57 5.251 14.094 7.619 1.00 14.85

ATOM 165 CD PRO B 57 4.627 15.247 6.831 1.00 14.50

ATOM 168 C PRO B 57 7.042 16.337 9.179 1.00 11.86

ATOM 169 O PRO B 57 7.482 16.161 10.310 1.00 10.54

ATOM 170 N TRP B 58 7.768 16.788 8.152 1.00 10.50

ATOM 171 CA TRP B 58 9.175 17.150 8.292 1.00 9.58

ATOM 173 CB TRP B 58 9.942 16.861 7.011 1.00 11.45

ATOM 176 CG TRP B 58 9.223 17.168 5.766 1.00 9.66

ATOM 177 CDl TRP B 58 9.198 18.341 5.080 1.00 12.64

ATOM 179 NEl TRP B 58 8.442 18.214 3.942 1.00 12.64

ATOM 181 CE2 TRP B 58 7.928 16.944 3.901 1.00 12.53

ATOM 182 CD2 TRP B 58 8.391 16.267 5.040 1.00 9.11

ATOM 183 CE3 TRP B 58 8.063 14.920 5.203 1.00 12.58

ATOM 185 CZ3 TRP B 58 7.284 14.326 4.283 1.00 13.84

ATOM 187 CH2 TRP B 58 6.807 15.020 3.170 1.00 13.97

ATOM 189 CZ2 TRP B 58 7.127 16.323 2.951 1.00 17.12

ATOM 191 C TRP B 58 9.316 18.619 8.635 1.00 10.22

ATOM 192 O TRP B 58 10.388 19.088 9.025 1.00 10.51

ATOM 194 N GLN B 59 8.229 19.374 8.510 1.00 10.22

ATOM 195 CA GLN B 59 8.351 20.804 8.782 1.00 10.99

ATOM 197 CB GLN B 59 7.086 21.523 8.314 1.00 11.13

ATOM 200 CG GLN B 59 6.986 22.997 8.700 1.00 12.75

ATOM 203 CD GLN B 59 7.735 23.964 7.791 1.00 10.44

ATOM 204 OEl GLN B 59 7.546 23.966 6.559 1.00 10.59 ATOM 205 NE2 GLN B 59 8.566 24.847 8.404 1.00 11.71

ATOM 208 C GLN B 59 8.507 21.035 10.280 1.00 11.27

ATOM 209 O GLN B 59 7.716 20.527 11.090 1.00 11.23

ATOM 211 N VAL B 60 9.474 21.880 10.607 1.00 10.58

ATOM 212 CA VAL B 60 9.693 22.264 11.981 1.00 11.91

ATOM 214 CB VAL B 60 10.993 21.672 12.580 1.00 13.07

ATOM 216 CGl VAL B 60 11.067 20.165 12.357 1.00 13.38

ATOM 220 CG2 VAL B 60 12.193 22.357 12.034 1.00 14.48

ATOM 224 C VAL B 60 9.678 23.770 12.079 1.00 11.28

ATOM 225 O VAL B 60 9.878 24.512 11.104 1.00 11.61

ATOM 227 N SER B 61 9.390 24.210 13.291 1.00 11.15

ATOM 228 CA SER B 61 9.546 25.622 13.663 1.00 11.82

ATOM 230 CB SER B 61 8.279 26.089 14.398 1.00 12.58

ATOM 233 OG SER B 61 8.511 27.265 15.174 1.00 11.41

ATOM 235 C SER B 61 10.766 25.834 14.513 1.00 12.08

ATOM 236 O SER B 61 10.989 25.140 15.494 1.00 11.81

ATOM 238 N ILE B 62 11.539 26.851 14.152 1.00 12.24

ATOM 239 CA ILE B 62 12.722 27.212 14.887 1.00 13.39

ATOM 241 CB ILE B 62 13.888 27.358 13.927 1.00 15.19

ATOM 243 CGl ILE B 62 14.148 25.983 13.306 1.00 17.39

ATOM 246 CDl ILE B 62 15.196 25.980 12.289 1.00 19.67

ATOM 250 CG2 ILE B 62 15.112 27.882 14.668 1.00 14.69

ATOM 254 C ILE B 62 12.412 28.504 15.614 1.00 13.34

ATOM 255 O ILE B 62 12.022 29.465 14.986 1.00 11.83

ATOM 257 N THR B 63 12.581 28.498 16.928 1.00 13.00

ATOM 258 CA THR B 63 12.343 29.686 17.754 1.00 12.22

ATOM 260 CB THR B 63 11.321 29.408 18.838 1.00 12.27

ATOM 262 OGl THR B 63 11.872 28.494 19.787 1.00 11.51

ATOM 264 CG2 THR B 63 10.050 28.794 18.235 1.00 14.63

ATOM 268 C THR B 63 13.662 30.169 18.381 1.00 13.72

ATOM 269 O THR B 63 14.596 29.393 18.593 1.00 13.40

ATOM 271 N TYR B 64 13.739 31.467 18.603 1.00 13.79

ATOM 272 CA TYR B 64 14.830 32.052 19.331 1.00 13.61

ATOM 274 CB TYR B 64 15.674 32.949 18.447 1.00 14.77

ATOM 277 CG TYR B 64 16.848 33.462 19.196 1.00 13.86

ATOM 278 CDl TYR B 64 17.900 32.628 19.473 1.00 12.31

ATOM 280 CEl TYR B 64 18.987 33.059 20.185 1.00 18.48

ATOM 282 CZ TYR B 64 19.023 34.358 20.624 1.00 18.07

ATOM 283 OH TYR B 64 20.124 34.781 21.326 1.00 21.37

ATOM 285 CE2 TYR B 64 17.988 35.233 20.364 1.00 17.14

ATOM 287 CD2 TYR B 64 16.894 34.780 19.645 1.00 22.57

ATOM 289 C TYR B 64 14.213 32.856 20.458 1.00 15.40

ATOM 290 O TYR B 64 13.365 33.717 20.214 1.00 14.46

ATOM 292 N GLU B 65 14.608 32.527 21.688 1.00 15.10

ATOM 293 CA GLU B 65 14.024 33.180 22.867 1.00 15.20

ATOM 295 CB GLU B 65 14.585 34.599 22.995 1.00 14.27

ATOM 298 CG GLU B 65 15.999 34.547 23.384 1.00 14.89

ATOM 301 CD GLU B 65 16.557 35.912 23.716 1.00 19.66

ATOM 302 OEl GLU B 65 15.999 36.920 23.280 1.00 24.81

ATOM 303 OE2 GLU B 65 17.559 35.930 24.424 1.00 21.81

ATOM 304 C GLU B 65 12.502 33.120 22.807 1.00 15.76

ATOM 305 O GLU B 65 11.784 34.076 23.130 1.00 17.03

ATOM 307 N GLY B 66 12.002 31.962 22.396 1.00 16.22

ATOM 308 CA GLY B 66 10.573 31.673 22.392 1.00 15.56

ATOM 311 C GLY B 66 9.763 32.151 21.207 1.00 15.75

ATOM 312 O GLY B 66 8.597 31.833 21.112 1.00 17.74

ATOM 314 N VAL B 67 10.396 32.887 20.292 1.00 16.38

ATOM 315 CA VAL B 67 9.716 33.493 19.154 1.00 15.58

ATOM 317 CB VAL B 67 10.098 34.956 19.000 1.00 16.85

ATOM 319 CGl VAL B 67 9.225 35.597 17.922 1.00 19.17

ATOM 323 CG2 VAL B 67 9.912 35.696 20.306 1.00 19.38 ATOM 327 C VAL B 67 10.108 32.741 17.873 1.00 15.22

ATOM 328 O VAL B 67 11.278 32.486 17.641 1.00 15.16

ATOM 330 N HIS B 68 9.114 32.341 17.092 1.00 15.63

ATOM 331 CA HIS B 68 9.362 31.684 15.812 1.00 14.99

ATOM 333 CB HIS B 68 8.042 31.367 15.127 1.00 14.35

ATOM 336 CG HIS B 68 8.207 30.775 13.778 1.00 15.11

ATOM 337 NDl HIS B 68 8.280 31.525 12.624 1.00 19.44

ATOM 339 CEl HIS B 68 8.489 30.715 11.595 1.00 12.40

ATOM 341 NE2 HIS B 68 8.571 29.479 12.049 1.00 15.78

ATOM 343 CD2 HIS B 68 8.429 29.496 13.410 1.00 8.54

ATOM 345 C HIS B 68 10.140 32.621 14.938 1.00 14.88

ATOM 346 O HIS B 68 9.657 33.742 14.683 1.00 14.79

ATOM 348 N VAL B 69 11.288 32.155 14.437 1.00 13.21

ATOM 349 CA VAL B 69 12.118 32.946 13.539 1.00 14.07

ATOM 351 CB VAL B 69 13.495 33.255 14.131 1.00 14.39

ATOM 353 CGl VAL B 69 13.350 34.177 15.341 1.00 15.80

ATOM 357 CG2 VAL B 69 14.278 32.015 14.495 1.00 14.78

ATOM 361 C VAL B 69 12.310 32.353 12.137 1.00 14.00

ATOM 362 O VAL B 69 12.520 33.072 11.173 1.00 16.03

ATOM 364 N CYS B 70 12.238 31.030 12.053 1.00 13.61

ATOM 365 CA CYS B 70 12.530 30.325 10.819 1.00 13.21

ATOM 367 CB CYS B 70 14.018 30.082 10.675 1.00 14.05

ATOM 370 SG CYS B 70 14.965 31.549 10.216 1.00 18.51

ATOM 372 C CYS B 70 11.852 28.965 10.816 1.00 12.52

ATOM 373 O CYS B 70 11.479 28.445 11.861 1.00 13.60

ATOM 375 N GLY B 71 11.703 28.421 9.616 1.00 11.80

ATOM 376 CA GLY B 71 11.399 27.022 9.411 1.00 11.78

ATOM 379 C GLY B 71 12.648 26.164 9.320 1.00 12.46

ATOM 380 O GLY B 71 13.780 26.648 9.280 1.00 11.03

ATOM 382 N GLY B 72 12.414 24.860 9.272 1.00 10.53

ATOM 383 CA GLY B 72 13.479 23.851 9.094 1.00 9.73

ATOM 386 C GLY B 72 12.838 22.568 8.617 1.00 10.24

ATOM 387 O GLY B 72 11.611 22.462 8.581 1.00 10.60

ATOM 389 N SER B 73 13.668 21.575 8.313 1.00 11.06

ATOM 390 CA SER B 73 13.161 20.290 7.807 1.00 10.07

ATOM 392 CB SER B 73 13.425 20.153 6.322 1.00 10.58

ATOM 395 OG SER B 73 12.799 21.210 5.629 1.00 9.62

ATOM 397 C SER B 73 13.886 19.188 8.561 1.00 10.26

ATOM 398 O SER B 73 15.119 19.174 8.595 1.00 10.16

ATOM 400 N LEU B 74 13.123 18.304 9.175 1.00 12.41

ATOM 401 CA LEU B 74 13.666 17.143 9.824 1.00 10.24

ATOM 403 CB LEU B 74 12.564 16.431 10.630 1.00 9.66

ATOM 406 CG LEU B 74 13.017 15.334 11.559 1.00 11.59

ATOM 408 CDl LEU B 74 13.932 15.834 12.633 1.00 9.91

ATOM 412 CD2 LEU B 74 11.762 14.671 12.112 1.00 11.60

ATOM 416 C LEU B 74 14.216 16.172 8.786 1.00 10.13

ATOM 417 O LEU B 74 13.541 15.791 7.845 1.00 11.64

ATOM 419 N VAL B 75 15.448 15.752 8.986 1.00 11.41

ATOM 420 CA VAL B 75 16.062 14.841 8.035 1.00 12.66

ATOM 422 CB VAL B 75 17.226 15.534 7.260 1.00 12.93

ATOM 424 CGl VAL B 75 16.665 16.726 6.471 1.00 13.24

ATOM 428 CG2 VAL B 75 18.347 15.979 8.174 1.00 12.08

ATOM 432 C VAL B 75 16.509 13.537 8.650 1.00 14.24

ATOM 433 O VAL B 75 16.813 12.595 7.928 1.00 15.20

ATOM 435 N SER B 76 16.521 13.440 9.963 1.00 13.72

ATOM 436 CA SER B 76 16.798 12.162 10.621 1.00 13.22

ATOM 438 CB SER B 76 18.299 11.858 10.625 1.00 14.96

ATOM 441 OG SER B 76 18.985 12.743 11.472 1.00 16.39

ATOM 443 C SER B 76 16.236 12.284 12.053 1.00 14.85

ATOM 444 O SER B 76 15.585 13.253 12.360 1.00 14.99

ATOM 446 N GLU B 77 16.486 11.295 12.910 1.00 14.63 ATOM 447 CA GLU B 77 15.982 11.291 14.268 1.00 15.63

ATOM 449 CB GLU B 77 16.339 9.958 14.967 1.00 16.48

ATOM 452 CG GLU B 77 15.591 8.755 14.434 1.00 22.14

ATOM 455 CD GLU B 77 16.290 8.051 13.264 1.00 29.77

ATOM 456 OEl GLU B 77 17.182 8.661 12.644 1.00 26.89

ATOM 457 OE2 GLU B 77 15.918 6.883 12.952 1.00 36.29

ATOM 458 C GLU B 77 16.567 12.455 15.085 1.00 15.42

ATOM 459 O GLU B 77 15.973 12.896 16.077 1.00 16.94

ATOM 461 N GLN B 78 17.729 12.961 14.696 1.00 14.58

ATOM 462 CA GLN B 78 18.351 14.007 15.507 1.00 14.85

ATOM 464 CB GLN B 78 19.496 13.396 16.351 1.00 16.24

ATOM 467 CG GLN B 78 19.813 14.176 17.633 1.00 15.57

ATOM 470 CD GLN B 78 20.570 13.383 18.675 1.00 17.71

ATOM 471 OEl GLN B 78 20.721 12.169 18.543 1.00 20.80

ATOM 472 NE2 GLN B 78 21.072 14.077 19.708 1.00 18.10

ATOM 475 C GLN B 78 18.871 15.180 14.727 1.00 12.49

ATOM 476 O GLN B 78 19.544 16.017 15.312 1.00 12.88

ATOM 478 N TRP B 79 18.542 15.296 13.427 1.00 12.04

ATOM 479 CA TRP B 79 19.081 16.363 12.605 1.00 12.35

ATOM 481 CB TRP B 79 20.163 15.867 11.650 1.00 13.14

ATOM 484 CG TRP B 79 21.357 15.398 12.381 1.00 12.80

ATOM 485 CDl TRP B 79 21.534 14.155 12.925 1.00 17.13

ATOM 487 NEl TRP B 79 22.759 14.074 13.536 1.00 17.28

ATOM 489 CE2 TRP B 79 23.411 15.275 13.408 1.00 13.53

ATOM 490 CD2 TRP B 79 22.559 16.138 12.670 1.00 13.45

ATOM 491 CE3 TRP B 79 23.003 17.426 12.387 1.00 14.38

ATOM 493 CZ3 TRP B 79 24.264 17.815 12.836 1.00 15.49

ATOM 495 CH2 TRP B 79 25.095 16.929 13.532 1.00 16.53

ATOM 497 CZ2 TRP B 79 24.677 15.662 13.833 1.00 16.28

ATOM 499 C TRP B 79 18.007 17.050 11.790 1.00 11.55

ATOM 500 O TRP B 79 17.055 16.410 11.301 1.00 11.55

ATOM 502 N VAL B 80 18.144 18.372 11.761 1.00 11.14

ATOM 503 CA VAL B 80 17.312 19.248 11.011 1.00 10.88

ATOM 505 CB VAL B 80 16.563 20.174 11.970 1.00 12.42

ATOM 507 CGl VAL B 80 15.888 21.379 11.245 1.00 12.70

ATOM 511 CG2 VAL B 80 15.565 19.343 12.823 1.00 13.53

ATOM 515 C VAL B 80 18.166 20.114 10.099 1.00 10.76

ATOM 516 O VAL B 80 19.252 20.580 10.487 1.00 11.01

ATOM 518 N LEU B 81 17.637 20.374 8.919 1.00 10.45

ATOM 519 CA LEU B 81 18.236 21.355 8.003 1.00 10.05

ATOM 521 CB LEU B 81 18.277 20.817 6.577 1.00 11.11

ATOM 524 CG LEU B 81 19.393 19.873 6.163 1.00 15.98

ATOM 526 CDl LEU B 81 19.128 19.325 4.755 1.00 16.63

ATOM 530 CD2 LEU B 81 20.702 20.598 6.171 1.00 15.02

ATOM 534 C LEU B 81 17.449 22.640 7.973 1.00 10.31

ATOM 535 O LEU B 81 16.247 22.641 7.849 1.00 9.22

ATOM 537 N SER B 82 18.154 23.753 8.023 1.00 9.60

ATOM 538 CA SER B 82 17.525 25.059 7.960 1.00 10.03

ATOM 540 CB SER B 82 17.178 25.565 9.347 1.00 10.19

ATOM 543 OG SER B 82 16.492 26.819 9.302 1.00 9.82

ATOM 545 C SER B 82 18.516 25.932 7.207 1.00 9.54

ATOM 546 O SER B 82 19.388 25.402 6.485 1.00 10.65

ATOM 548 N ALA B 83 18.335 27.253 7.297 1.00 10.56

ATOM 549 CA ALA B 83 19.167 28.199 6.552 1.00 10.87

ATOM 551 CB ALA B 83 18.293 29.326 6.002 1.00 10.78

ATOM 555 C ALA B 83 20.181 28.785 7.480 1.00 11.64

ATOM 556 O ALA B 83 19.848 29.083 8.635 1.00 11.48

ATOM 558 N ALA B 84 21.392 29.023 6.972 1.00 12.52

ATOM 559 CA ALA B 84 22.447 29.566 7.831 1.00 13.38

ATOM 561 CB ALA B 84 23.781 29.603 7.127 1.00 14.52

ATOM 565 C ALA B 84 22.096 30.940 8.360 1.00 14.29 ATOM 566 O ALA B 84 22.435 31.289 9.483 1.00 13.69

ATOM 568 N HIS B 85 21.406 31.707 7.552 1.00 14.30

ATOM 569 CA HIS B 85 21.101 33.068 7.922 1.00 14.30

ATOM 571 CB HIS B 85 20.510 33.829 6.725 1.00 15.08

ATOM 574 CG HIS B 85 19.066 33.525 6.449 1.00 14.51

ATOM 575 NDl HIS B 85 18.655 32.838 5.325 1.00 15.07

ATOM 577 CEl HIS B 85 17.341 32.737 5.331 1.00 16.57

ATOM 579 NE 2 HIS B 85 16.874 33.388 6.387 1.00 15.91

ATOM 581 CD2 HIS B 85 17.936 33.909 7.089 1.00 19.55

ATOM 583 C HIS B 85 20.214 33.133 9.167 1.00 14.98

ATOM 584 O HIS B 85 20.138 34.164 9.787 1.00 16.49

ATOM 586 N CYS B 86 19.531 32.040 9.510 1.00 13.37

ATOM 587 CA CYS B 86 18.686 32.005 10.698 1.00 14.38

ATOM 589 CB CYS B 86 17.748 30.802 10.643 1.00 13.49

ATOM 592 SG CYS B 86 16.626 30.811 9.280 1.00 17.45

ATOM 594 C CYS B 86 19.478 31.905 11.997 1.00 15.97

ATOM 595 O CYS B 86 18.883 31.952 13.074 1.00 15.90

ATOM 597 N PHE B 87 20.802 31.723 11.892 1.00 14.36

ATOM 598 CA PHE B 87 21.667 31.469 13.045 1.00 15.57

ATOM 600 CB PHE B 87 22.115 30.022 13.029 1.00 15.92

ATOM 603 CG PHE B 87 20.974 29.088 13.006 1.00 14.08

ATOM 604 CDl PHE B 87 20.297 28.788 14.171 1.00 19.43

ATOM 606 CEl PHE B 87 19.150 27.956 14.130 1.00 15.15

ATOM 608 CZ PHE B 87 18.715 27.487 12.918 1.00 14.87

ATOM 610 CE 2 PHE B 87 19.371 27.802 11.766 1.00 15.79

ATOM 612 CD2 PHE B 87 20.484 28.610 11.803 1.00 15.60

ATOM 614 C PHE B 87 22.850 32.418 13.084 1.00 16.94

ATOM 615 O PHE B 87 24.003 31.999 12.962 1.00 16.68

ATOM 617 N PRO B 88 22.562 33.680 13.332 1.00 19.59

ATOM 618 CA PRO B 88 23.665 34.619 13.427 1.00 22.47

ATOM 620 CB PRO B 88 22.966 35.969 13.625 1.00 22.55

ATOM 623 CG PRO B 88 21.594 35.647 14.088 1.00 22.80

ATOM 626 CD PRO B 88 21.254 34.316 13.527 1.00 20.65

ATOM 629 C PRO B 88 24.564 34.265 14.604 1.00 24.07

ATOM 630 O PRO B 88 24.108 33.695 15.599 1.00 23.07

ATOM 631 N SER B 89 25.844 34.599 14.471 1.00 25.46

ATOM 632 CA SER B 89 26.855 34.328 15.489 1.00 26.84

ATOM 634 CB SER B 89 28.192 34.891 15.009 1.00 28.26

ATOM 637 OG SER B 89 27.991 36.266 14.711 1.00 34.33

ATOM 639 C SER B 89 26.513 34.962 16.844 1.00 26.59

ATOM 640 O SER B 89 26.892 34.436 17.874 1.00 27.84

ATOM 642 N GLU B 90 25.803 36.087 16.839 1.00 27.26

ATOM 643 CA GLU B 90 25.467 36.794 18.086 1.00 28.06

ATOM 645 CB GLU B 90 24.787 38.136 17.805 1.00 29.51

ATOM 648 CG GLU B 90 25.701 39.194 17.167 1.00 36.68

ATOM 651 CD GLU B 90 25.641 39.197 15.637 1.00 47.20

ATOM 652 OEl GLU B 90 24.962 38.306 15.055 1.00 47.90

ATOM 653 OE 2 GLU B 90 26.288 40.095 15.030 1.00 53.11

ATOM 654 C GLU B 90 24.525 36.009 18.984 1.00 27.96

ATOM 655 O GLU B 90 24.485 36.224 20.195 1.00 27.60

ATOM 657 N HIS B 91 23.721 35.145 18.376 1.00 25.93

ATOM 658 CA HIS B 91 22.724 34.400 19.103 1.00 24.44

ATOM 660 CB HIS B 91 21.687 33.840 18.124 1.00 23.39

ATOM 663 CG HIS B 91 20.685 34.855 17.662 1.00 22.96

ATOM 664 NDl HIS B 91 19.604 34.532 16.870 1.00 24.02

ATOM 666 CEl HIS B 91 18.885 35.616 16.646 1.00 24.06

ATOM 668 NE 2 HIS B 91 19.453 36.626 17.276 1.00 24.34

ATOM 670 CD2 HIS B 91 20.586 36.178 17.907 1.00 24.09

ATOM 672 C HIS B 91 23.336 33.282 19.910 1.00 23.07

ATOM 673 O HIS B 91 24.355 32.699 19.539 1.00 22.86

ATOM 675 N HIS B 92 22.663 32.951 21.007 1.00 23.86 ATOM 676 CA HIS B 92 23.134 31.934 21.944 .00 23.21

ATOM 678 CB HIS B 92 22.839 32.417 23.370 .00 25.14

ATOM 681 CG HIS B 92 23.188 33.861 23.593 .00 29.78

ATOM 682 NDl HIS B 92 22.310 34.768 24.143 1.00 34.80

ATOM 684 CEl HIS B 92 22.883 35.958 24.199 1 .00 36.78

ATOM 686 NE 2 HIS B 92 24.100 35.858 23.694 1.00 33.65

ATOM 688 CD2 HIS B 92 24.313 34.561 23.300 1.00 33.02

ATOM 690 C HIS B 92 22.435 30.613 21.626 1.00 21.68

ATOM 691 O HIS B 92 21.232 30.589 21.505 1.00 21.87

ATOM 693 N LYS B 93 23.198 29.533 21.480 1.00 20.19

ATOM 694 CA LYS B 93 22.664 28.251 21.075 1.00 19.90

ATOM 696 CB LYS B 93 23.749 27.150 21.119 1.00 18.57

ATOM 699 CG LYS B 93 23.296 25.828 20.531 1.00 21.28

ATOM 702 CD LYS B 93 24.439 24.870 20.274 1.00 24.19

ATOM 705 CE LYS B 93 25.050 24.341 21.553 1.00 29.78

ATOM 708 NZ LYS B 93 26.338 23.713 21.209 1.00 30.97

ATOM 712 C LYS B 93 21.515 27.809 21.982 1.00 17.42

ATOM 713 O LYS B 93 20.517 27.290 21.518 1.00 16.42

ATOM 715 N GLU B 94 21.692 28.039 23.283 1.00 18.36

ATOM 716 CA GLU B 94 20.765 27.574 24.319 1.00 17.74

ATOM 718 CB GLU B 94 21.342 27.896 25.695 1.00 16.56

ATOM 721 CG GLU B 94 22.549 27.161 26.051 1.00 22.05

ATOM 724 CD GLU B 94 23.447 27.942 27.023 1.00 24.03

ATOM 725 OEl GLU B 94 23.608 29.216 26.832 1.00 29.87

ATOM 726 OE 2 GLU B 94 24.034 27.237 27.913 1.00 32.33

ATOM 727 C GLU B 94 19.403 28.271 24.270 1.00 16.08

ATOM 728 O GLU B 94 18.481 27.899 25.002 1.00 15.32

ATOM 730 N ALA B 95 19.310 29.332 23.483 1.00 13.84

ATOM 731 CA ALA B 95 18.097 30.096 23.368 1.00 14.36

ATOM 733 CB ALA B 95 18.405 31.554 23.233 1.00 14.36

ATOM 737 C ALA B 95 17.245 29.632 22.207 1.00 13.95

ATOM 738 O ALA B 95 16.155 30.128 22.042 1.00 12.05

ATOM 740 N TYR B 96 17.719 28.665 21.427 1.00 12.50

ATOM 741 CA TYR B 96 16.911 28.151 20.313 1.00 12.62

ATOM 743 CB TYR B 96 17.792 27.656 19.172 1.00 12.61

ATOM 746 CG TYR B 96 18.396 28.745 18.350 1.00 13.46

ATOM 747 CDl TYR B 96 17.702 29.328 17.303 1.00 15.12

ATOM 749 CEl TYR B 96 18.283 30.367 16.547 1.00 15.69

ATOM 751 CZ TYR B 96 19.544 30.793 16.881 1.00 17.20

ATOM 752 OH TYR B 96 20.160 31.818 16.169 1.00 18.56

ATOM 754 CE 2 TYR B 96 20.225 30.216 17.920 1.00 14.98

ATOM 756 CD2 TYR B 96 19.657 29.224 18.656 1.00 14.22

ATOM 758 C TYR B 96 16.065 26.975 20.757 1.00 11.83

ATOM 759 O TYR B 96 16.465 26.225 21.618 1.00 11.45

ATOM 761 N GLU B 97 14.940 26.769 20.081 .00 12.65

ATOM 762 CA GLU B 97 14.219 25.517 20.187 .00 12.64

ATOM 764 CB GLU B 97 13.035 25.594 21.146 .00 13.79

ATOM 767 CG GLU B 97 13.433 25.816 22.577 .00 15.70

ATOM 770 CD GLU B 97 12.268 25.709 23.531 1.00 12.82

ATOM 771 OEl GLU B 97 11.187 26.286 23.259 1 .00 13.88

ATOM 772 OE 2 GLU B 97 12.462 25.030 24.547 1.00 15.06

ATOM 773 C GLU B 97 13.727 25.163 18.818 1.00 13.85

ATOM 774 O GLU B 97 13.618 26.023 17.930 1.00 10.65

ATOM 776 N VAL B 98 13.415 23.893 18.677 1.00 12.57

ATOM 111 CA VAL B 98 12.833 23.355 17.465 1.00 11.68

ATOM 779 CB VAL B 98 13.738 22.315 16.821 1.00 11.16

ATOM 781 CGl VAL B 98 13.077 21.737 15.592 1.00 14.42

ATOM 785 CG2 VAL B 98 15.077 22.970 16.417 1.00 17.77

ATOM 789 C VAL B 98 11.545 22.673 17.883 1.00 11.47

ATOM 790 O VAL B 98 11.518 21.872 18.821 1.00 10.91

ATOM 792 N LYS B 99 10.472 23.002 17.191 1.00 12.35 ATOM 793 CA LYS B 99 9.183 22.395 17.484 1.00 13.24

ATOM 795 CB LYS B 99 8.092 23.443 17.697 1.00 13.51

ATOM 798 CG LYS B 99 6.740 22.847 18.127 1.00 17.91

ATOM 801 CD LYS B 99 5.918 23.903 18.891 1.00 19.52

ATOM 804 CE LYS B 99 4.460 23.554 19.068 1.00 27.86

ATOM 807 NZ LYS B 99 3.711 24.662 19.765 1.00 25.59

ATOM 811 C LYS B 99 8.792 21.551 16.306 1.00 13.15

ATOM 812 O LYS B 99 8.711 22.035 15.179 1.00 11.31

ATOM 814 N LEU B 100 8.517 20.302 16.609 1.00 13.52

ATOM 815 CA LEU B 100 8.266 19.305 15.607 1.00 13.24

ATOM 817 CB LEU B 100 9.266 18.159 15.793 1.00 14.31

ATOM 820 CG LEU B 100 10.744 18.535 15.697 1.00 15.23

ATOM 822 CDl LEU B 100 11.453 17.516 14.841 1.00 17.06

ATOM 826 CD2 LEU B 100 11.407 18.612 17.082 1.00 18.24

ATOM 830 C LEU B 100 6.860 18.773 15.850 1.00 13.25

ATOM 831 O LEU B 100 6.415 18.732 16.993 1.00 12.09

ATOM 833 N GLY B 101 6.205 18.321 14.792 1.00 14.83

ATOM 834 CA GLY B 101 4.916 17.687 14.934 1.00 15.82

ATOM 837 C GLY B 101 3.815 18.695 15.173 1.00 17.22

ATOM 838 O GLY B 101 2.715 18.320 15.537 1.00 17.58

ATOM 840 N ALA B 102 4. Ill 19.964 14.922 1.00 18.39

ATOM 841 CA ALA B 102 3.167 21.062 15.125 1.00 19.30

ATOM 843 CB ALA B 102 3.910 22.301 15.534 1.00 20.18

ATOM 847 C ALA B 102 2.425 21.358 13.856 1.00 20.45

ATOM 848 O ALA B 102 3.011 21.356 12.761 1.00 21.60

ATOM 850 N HIS B 103 1.134 21.628 13.990 1.00 20.05

ATOM 851 CA HIS B 103 0.346 22.108 12.870 1.00 19.22

ATOM 853 CB HIS B 103 -0.907 21.232 12.698 1.00 21.23

ATOM 856 CG HIS B 103 -1.936 21.832 11.800 1.00 21.61

ATOM 857 NDl HIS B 103 -1.633 22.297 10.539 1.00 28.87

ATOM 859 CEl HIS B 103 -2.721 22.797 9.987 1.00 27.54

ATOM 861 NE 2 HIS B 103 -3.721 22.653 10.835 1.00 25.40

ATOM 863 CD2 HIS B 103 -3.258 22.055 11.979 1.00 26.34

ATOM 865 C HIS B 103 0.024 23.584 13.133 1.00 19.05

ATOM 866 O HIS B 103 0.379 24.449 12.340 1.00 15.69

ATOM 868 N GLN B 104 -0.612 23.842 14.274 1.00 17.57

ATOM 869 CA GLN B 104 -0.941 25.189 14.727 1.00 20.64

ATOM 871 CB GLN B 104 -2.381 25.214 15.261 1.00 19.70

ATOM 874 CG GLN B 104 -3.397 25.286 14.163 1.00 22.95

ATOM 877 CD GLN B 104 -4.819 25.050 14.615 1.00 25.15

ATOM 878 OEl GLN B 104 -5.111 24.915 15.807 1.00 28.63

ATOM 879 NE 2 GLN B 104 -5.722 25.014 13.648 1.00 29.11

ATOM 882 C GLN B 104 0.055 25.544 15.821 1.00 21.07

ATOM 883 O GLN B 104 0.058 24.916 16.894 1.00 18.68

ATOM 885 N LEU B 105 0.921 26.530 15.562 1.00 20.58

ATOM 886 CA LEU B 105 1.972 26.883 16.518 1.00 22.40

ATOM 888 CB LEU B 105 2.831 28.028 15.987 1.00 22.55

ATOM 891 CG LEU B 105 3.862 27.700 14.926 1.00 20.77

ATOM 893 CDl LEU B 105 4.786 28.864 14.739 1.00 22.00

ATOM 897 CD2 LEU B 105 4.644 26.431 15.281 1.00 18.30

ATOM 901 C LEU B 105 1.447 27.304 17.882 1.00 24.77

ATOM 902 O LEU B 105 2.061 26.994 18.906 1.00 26.42

ATOM 904 N ASP B 106 0.332 28.030 17.888 1.00 25.44

ATOM 905 CA ASP B 106 -0.232 28.548 19.139 1.00 27.80

ATOM 907 CB ASP B 106 -1.053 29.805 18.862 1.00 27.88

ATOM 910 CG ASP B 106 -0.195 30.996 18.496 1.00 29.06

ATOM 911 ODl ASP B 106 1.039 30.938 18.699 1.00 34.21

ATOM 912 OD2 ASP B 106 -0.752 31.989 17.982 1.00 33.63

ATOM 913 C ASP B 106 -1.096 27.540 19.886 1.00 30.14

ATOM 914 O ASP B 106 -1.533 27.832 21.009 1.00 31.23

ATOM 916 N SER B 107 -1.356 26.379 19.285 1.00 30.76 ATOM 917 CA SER B 107 -2.231 25.367 19.889 1.00 31.86

ATOM 919 CB SER B 107 -3.048 24.655 18.823 1.00 31.52

ATOM 922 OG SER B 107 -3.908 25.580 18.190 1.00 33.53

ATOM 924 C SER B 107 -1.431 24.340 20.669 1.00 33.68

ATOM 925 O SER B 107 -0.278 24.052 20.332 1.00 33.43

ATOM 927 N TYR B 108 -2.031 23.789 21.722 1.00 35.40

ATOM 928 CA TYR B 108 -1.403 22.669 22.382 1.00 35.11

ATOM 930 CB TYR B 108 -1.887 22.425 23.804 1.00 38.47

ATOM 933 CG TYR B 108 -1.164 21.220 24.387 1.00 40.20

ATOM 934 CDl TYR B 108 0.226 21.252 24.597 1.00 44.32

ATOM 936 CEl TYR B 108 0.909 20.137 25.099 1.00 45.46

ATOM 938 CZ TYR B 108 0.195 18.968 25.379 1.00 45.94

ATOM 939 OH TYR B 108 0.854 17.859 25.878 1.00 46.04

ATOM 941 CE2 TYR B 108 -1.185 18.912 25.159 1.00 44.79

ATOM 943 CD2 TYR B 108 -1.852 20.027 24.658 1.00 44.96

ATOM 945 C TYR B 108 -1.673 21.437 21.567 1.00 34.20

ATOM 946 O TYR B 108 -2.778 21.237 21.055 1.00 34.52

ATOM 948 N SER B 109 -0.647 20.615 21.436 1.00 32.33

ATOM 949 CA SER B 109 -0.792 19.351 20.802 1.00 31.48

ATOM 951 CB SER B 109 -0.222 19.380 19.392 1.00 31.07

ATOM 954 OG SER B 109 -0.205 18.059 18.888 1.00 31.23

ATOM 956 C SER B 109 -0.018 18.347 21.596 1.00 30.60

ATOM 957 O SER B 109 1.123 18.604 21.973 1.00 31.30

ATOM 959 N GLU B 110 -0.619 17.181 21.803 1.00 29.95

ATOM 960 CA GLU B 110 0.101 16.075 22.390 1.00 29.51

ATOM 962 CB GLU B 110 -0.862 15.103 23.072 1.00 30.55

ATOM 965 CG GLU B 110 -1.390 15.679 24.403 1.00 35.53

ATOM 968 CD GLU B 110 -2.115 14.657 25.287 1.00 37.10

ATOM 969 OEl GLU B 110 -1.609 13.507 25.447 1.00 48.31

ATOM 970 OE2 GLU B 110 -3.186 15.027 25.836 1.00 47.79

ATOM 971 C GLU B 110 0.994 15.359 21.374 1.00 26.45

ATOM 972 O GLU B 110 1.787 14.531 21.762 1.00 26.39

ATOM 974 N ASP B 111 0.900 15.710 20.093 1.00 24.81

ATOM 975 CA ASP B 111 1.786 15.144 19.067 1.00 24.03

ATOM 977 CB ASP B 111 1.033 15.004 17.756 1.00 25.30

ATOM 980 CG ASP B 111 -0.229 14.188 17.924 1.00 23.78

ATOM 981 ODl ASP B 111 -0.113 13.026 18.369 1.00 23.20

ATOM 982 OD2 ASP B 111 -1.305 14.740 17.668 1.00 28.81

ATOM 983 C ASP B 111 3.076 15.939 18.825 1.00 22.74

ATOM 984 O ASP B 111 4.031 15.399 18.287 1.00 21.48

ATOM 986 N ALA B 112 3.091 17.196 19.239 1.00 19.17

ATOM 987 CA ALA B 112 4.235 18.067 19.014 1.00 18.65

ATOM 989 CB ALA B 112 3.841 19.529 19.114 1.00 18.83

ATOM 993 C ALA B 112 5.285 17.721 20.024 1.00 18.10

ATOM 994 O ALA B 112 4.978 17.216 21.123 1.00 18.74

ATOM 996 N LYS B 113 6.540 17.920 19.636 1.00 17.10

ATOM 997 CA LYS B 113 7.659 17.768 20.539 1.00 15.34

ATOM 999 CB LYS B 113 8.484 16.523 20.216 1.00 14.89

ATOM 1002 CG LYS B 113 7.663 15.193 20.253 1.00 21.31

ATOM 1005 CD LYS B 113 7.268 14.863 21.705 1.00 31.01

ATOM 1008 CE LYS B 113 6.203 13.738 21.845 1.00 32.53

ATOM 1011 NZ LYS B 113 4.826 14.248 21.520 1.00 34.46

ATOM 1015 C LYS B 113 8.521 19.009 20.360 1.00 13.46

ATOM 1016 O LYS B 113 8.693 19.482 19.257 1.00 13.37

ATOM 1018 N VAL B 114 9.069 19.495 21.449 1.00 13.86

ATOM 1019 CA VAL B 114 9.975 20.619 21.416 1.00 14.14

ATOM 1021 CB VAL B 114 9.412 21.833 22.203 1.00 14.58

ATOM 1023 CGl VAL B 114 10.330 23.037 22.058 1.00 14.49

ATOM 1027 CG2 VAL B 114 8.013 22.175 21.695 1.00 15.66

ATOM 1031 C VAL B 114 11.341 20.192 21.956 1.00 13.17

ATOM 1032 O VAL B 114 11.471 19.385 22.894 1.00 10.97 ATOM 1034 N SER B 115 12.376 20.697 21.299 1.00 13.55

ATOM 1035 CA SER B 115 13.738 20.294 21.587 1.00 14.47

ATOM 1037 CB SER B 115 14.221 19.261 20.571 1.00 17.27

ATOM 1040 OG SER B 115 15.532 18.884 20.920 1.00 20.04

ATOM 1042 C SER B 115 14.681 21.467 21.555 1.00 14.87

ATOM 1043 O SER B 115 14.461 22.400 20.785 1.00 14.52

ATOM 1045 N THR B 116 15.696 21.427 22.414 1.00 13.16

ATOM 1046 CA THR B 116 16.830 22.319 22.267 1.00 13.76

ATOM 1048 CB THR B 116 17.504 22.553 23.634 1.00 13.66

ATOM 1050 OGl THR B 116 17.691 21.282 24.256 1.00 15.33

ATOM 1052 CG2 THR B 116 16.605 23.413 24.496 1.00 16.88

ATOM 1056 C THR B 116 17.828 21.726 21.269 1.00 13.45

ATOM 1057 O THR B 116 17.622 20.603 20.766 1.00 12.13

ATOM 1059 N LEU B 117 18.886 22.481 20.981 1.00 12.70

ATOM 1060 CA LEU B 117 19.919 22.076 20.029 1.00 15.15

ATOM 1062 CB LEU B 117 20.148 23.211 19.059 1.00 16.02

ATOM 1065 CG LEU B 117 18.929 23.552 18.203 1.00 15.53

ATOM 1067 CDl LEU B 117 19.282 24.657 17.247 1.00 19.24

ATOM 1071 CD2 LEU B 117 18.448 22.294 17.447 1.00 14.14

ATOM 1075 C LEU B 117 21.254 21.761 20.733 1.00 16.36

ATOM 1076 O LEU B 117 21.703 22.542 21.544 1.00 17.68

ATOM 1078 N LYS B 118 21.877 20.649 20.365 1.00 17.31

ATOM 1079 CA LYS B 118 23.221 20.269 20.782 1.00 17.49

ATOM 1081 CB LYS B 118 23.339 18.749 20.659 1.00 17.77

ATOM 1084 CG LYS B 118 24.694 18.161 20.823 1.00 22.11

ATOM 1087 CD LYS B 118 24.558 16.659 21.083 1.00 21.73

ATOM 1090 CE LYS B 118 25.898 16.002 21.136 1.00 29.98

ATOM 1093 NZ LYS B 118 26.612 16.141 19.830 1.00 36.58

ATOM 1097 C LYS B 118 24.258 20.952 19.909 1.00 17.44

ATOM 1098 O LYS B 118 25.344 21.270 20.367 1.00 16.87

ATOM 1100 N ASP B 119 23.931 21.181 18.639 1.00 16.84

ATOM 1101 CA ASP B 119 24.903 21.759 17.731 1.00 16.68

ATOM 1103 CB ASP B 119 25.780 20.644 17.161 1.00 17.43

ATOM 1106 CG ASP B 119 27.153 21.145 16.663 1.00 18.38

ATOM 1107 ODl ASP B 119 27.443 22.351 16.764 1.00 23.21

ATOM 1108 OD2 ASP B 119 27.929 20.295 16.197 1.00 23.45

ATOM 1109 C ASP B 119 24.205 22.504 16.604 1.00 17.06

ATOM 1110 O ASP B 119 23.096 22.183 16.227 1.00 14.50

ATOM 1112 N ILE B 120 24.864 23.540 16.121 1.00 17.11

ATOM 1113 CA ILE B 120 24.349 24.339 15.021 1.00 16.65

ATOM 1115 CB ILE B 120 23.934 25.754 15.463 1.00 17.15

ATOM 1117 CGl ILE B 120 22.701 25.708 16.379 1.00 18.55

ATOM 1120 CDl ILE B 120 22.406 27.028 17.102 1.00 18.52

ATOM 1124 CG2 ILE B 120 23.662 26.624 14.247 1.00 17.42

ATOM 1128 C ILE B 120 25.516 24.463 14.089 1.00 15.94

ATOM 1129 O ILE B 120 26.537 25.009 14.481 1.00 15.55

ATOM 1131 N ILE B 121 25.380 23.969 12.862 1.00 13.98

ATOM 1132 CA ILE B 121 26.483 23.946 11.934 1.00 14.94

ATOM 1134 CB ILE B 121 26.898 22.512 11.638 1.00 13.61

ATOM 1136 CGl ILE B 121 27.050 21.744 12.962 1.00 15.71

ATOM 1139 CDl ILE B 121 27.437 20.252 12.809 1.00 17.78

ATOM 1143 CG2 ILE B 121 28.182 22.517 10.760 1.00 14.03

ATOM 1147 C ILE B 121 26.150 24.653 10.628 1.00 14.25

ATOM 1148 O ILE B 121 25.595 24.035 9.727 1.00 15.76

ATOM 1150 N PRO B 122 26.438 25.964 10.539 1.00 17.30

ATOM 1151 CA PRO B 122 26.232 26.645 9.278 1.00 17.38

ATOM 1153 CB PRO B 122 26.516 28.114 9.602 1.00 18.66

ATOM 1156 CG PRO B 122 27.453 28.056 10.751 1.00 22.55

ATOM 1159 CD PRO B 122 27.014 26.857 11.554 1.00 17.50

ATOM 1162 C PRO B 122 27.260 26.156 8.285 1.00 18.02

ATOM 1163 O PRO B 122 28.374 25.861 8.660 1.00 16.83 ATOM 1164 N HIS B 123 26.925 26.077 7.012 1.00 17.41

ATOM 1165 CA HIS B 123 27.930 25.698 6.048 1.00 16.43

ATOM 1167 CB HIS B 123 27.365 25.633 4.649 1.00 16.95

ATOM 1170 CG HIS B 123 28.283 24.949 3.693 1.00 16.68

ATOM 1171 NDl HIS B 123 29.287 25.613 3.032 1.00 17.59

ATOM 1173 CEl HIS B 123 29.954 24.757 2.278 1.00 18.08

ATOM 1175 NE2 HIS B 123 29.412 23.560 2.427 1.00 20.44

ATOM 1177 CD2 HIS B 123 28.364 23.656 3.305 1.00 18.93

ATOM 1179 C HIS B 123 29.036 26.759 6.082 1.00 16.72

ATOM 1180 O HIS B 123 28.720 27.905 6.196 1.00 15.76

ATOM 1182 N PRO B 124 30.312 26.356 6.038 1.00 18.35

ATOM 1183 CA PRO B 124 31.375 27.379 6.203 1.00 19.04

ATOM 1185 CB PRO B 124 32.669 26.568 6.289 1.00 20.46

ATOM 1188 CG PRO B 124 32.347 25.216 5.916 1.00 21.57

ATOM 1191 CD PRO B 124 30.862 25.003 5.926 1.00 19.11

ATOM 1194 C PRO B 124 31.467 28.443 5.106 1.00 20.13

ATOM 1195 O PRO B 124 32.120 29.466 5.322 1.00 21.29

ATOM 1196 N SER B 125 30.836 28.224 3.953 1.00 19.34

ATOM 1197 CA SER B 125 30.887 29.221 2.866 1.00 19.69

ATOM 1199 CB SER B 125 30.636 28.572 1.536 1.00 18.79

ATOM 1202 OG SER B 125 29.348 27.998 1.502 1.00 21.46

ATOM 1204 C SER B 125 29.902 30.340 3.061 1.00 19.72

ATOM 1205 O SER B 125 29.923 31.334 2.322 1.00 20.61

ATOM 1207 N TYR B 126 29.013 30.209 4.039 1.00 18.97

ATOM 1208 CA TYR B 126 28.049 31.262 4.258 1.00 21.37

ATOM 1210 CB TYR B 126 26.860 30.803 5.095 1.00 19.88

ATOM 1213 CG TYR B 126 25.794 31.877 5.090 1.00 18.37

ATOM 1214 CDl TYR B 126 25.105 32.163 3.938 1.00 17.08

ATOM 1216 CEl TYR B 126 24.149 33.182 3.896 1.00 19.51

ATOM 1218 CZ TYR B 126 23.894 33.916 5.033 1.00 21.18

ATOM 1219 OH TYR B 126 22.941 34.895 4.979 1.00 22.95

ATOM 1221 CE2 TYR B 126 24.562 33.632 6.192 1.00 19.82

ATOM 1223 CD2 TYR B 126 25.512 32.627 6.216 1.00 19.85

ATOM 1225 C TYR B 126 28.692 32.447 4.968 1.00 23.37

ATOM 1226 O TYR B 126 28.927 32.375 6.164 1.00 23.13

ATOM 1228 N LEU B 127 28.936 33.530 4.240 1.00 25.56

ATOM 1229 CA LEU B 127 29.693 34.655 4.809 1.00 28.47

ATOM 1231 CB LEU B 127 30.821 35.085 3.863 1.00 29.66

ATOM 1234 CG LEU B 127 31.885 33.995 3.675 1.00 33.19

ATOM 1236 CDl LEU B 127 32.993 34.440 2.707 1.00 38.39

ATOM 1240 CD2 LEU B 127 32.469 33.548 5.034 1.00 36.16

ATOM 1244 C LEU B 127 28.827 35.841 5.174 1.00 30.44

ATOM 1245 O LEU B 127 29.172 36.584 6.110 1.00 33.04

ATOM 1247 N GLN B 128 27.716 36.022 4.472 1.00 30.50

ATOM 1248 CA GLN B 128 26.896 37.215 4.634 1.00 32.99

ATOM 1250 CB GLN B 128 27.674 38.477 4.189 1.00 33.84

ATOM 1253 CG GLN B 128 28.278 38.383 2.802 1.00 34.86

ATOM 1256 CD GLN B 128 28.845 39.708 2.287 1.00 34.06

ATOM 1257 OEl GLN B 128 28.373 40.806 2.631 1.00 39.52

ATOM 1258 NE2 GLN B 128 29.845 39.603 1.446 1.00 28.17

ATOM 1261 C GLN B 128 25.574 37.094 3.873 1.00 34.23

ATOM 1262 O GLN B 128 25.369 36.142 3.129 1.00 35.73

ATOM 1264 N GLU B 129 24.674 38.050 4.081 1.00 35.15

ATOM 1265 CA GLU B 129 23.344 38.026 3.455 1.00 35.52

ATOM 1267 CB GLU B 129 22.533 39.265 3.844 1.00 36.24

ATOM 1270 CG GLU B 129 21.102 39.257 3.308 1.00 37.21

ATOM 1273 CD GLU B 129 20.219 40.356 3.906 1.00 40.46

ATOM 1274 OEl GLU B 129 20.664 41.035 4.869 1.00 50.34

ATOM 1275 OE2 GLU B 129 19.074 40.538 3.412 1.00 44.85

ATOM 1276 C GLU B 129 23.474 37.944 1.941 1.00 34.84

ATOM 1277 O GLU B 129 24.342 38.603 1.357 1.00 34.77 ATOM 1279 N GLY B 130 22.619 37.122 1.327 1.00 33.61

ATOM 1280 CA GLY B 130 22.726 36.775 -0.095 1.00 32.16

ATOM 1283 C GLY B 130 23.777 35.717 -0.472 1.00 30.55

ATOM 1284 O GLY B 130 23.776 35.225 -1.620 1.00 30.75

ATOM 1286 N SER B 131 24.669 35.364 0.459 1.00 27.92

ATOM 1287 CA SER B 131 25.817 34.479 0.153 1.00 26.77

ATOM 1289 CB SER B 131 26.733 34.330 1.376 1.00 25.67

ATOM 1292 OG SER B 131 27.802 33.419 1.178 1.00 25.10

ATOM 1294 C SER B 131 25.352 33.097 -0.256 1.00 25.34

ATOM 1295 O SER B 131 24.223 32.682 0.064 1.00 25.50

ATOM 1297 N GLN B 132 26.233 32.375 -0.936 1.00 24.09

ATOM 1298 CA GLN B 132 26.003 30.961 -1.174 1.00 23.72

ATOM 1300 CB GLN B 132 26.877 30.409 -2.315 1.00 23.59

ATOM 1303 CG GLN B 132 28.325 30.222 -2.004 1.00 28.47

ATOM 1306 CD GLN B 132 29.103 29.643 -3.204 1.00 32.02

ATOM 1307 OEl GLN B 132 28.519 29.328 -4.259 1.00 41.33

ATOM 1308 NE2 GLN B 132 30.429 29.500 -3.037 1.00 43.61

ATOM 1311 C GLN B 132 26.248 30.241 0.148 1.00 20.53

ATOM 1312 O GLN B 132 26.751 30.849 1.096 1.00 19.31

ATOM 1314 N GLY B 133 25.887 28.957 0.207 1.00 17.56

ATOM 1315 CA GLY B 133 26.038 28.164 1.414 1.00 15.82

ATOM 1318 C GLY B 133 25.031 28.494 2.506 1.00 13.74

ATOM 1319 O GLY B 133 25.309 28.272 3.677 1.00 14.45

ATOM 1321 N ASP B 134 23.872 29.015 2.129 1.00 12.11

ATOM 1322 CA ASP B 134 22.865 29.393 3.090 1.00 12.34

ATOM 1324 CB ASP B 134 21.932 30.472 2.571 1.00 12.14

ATOM 1327 CG ASP B 134 21.046 31.027 3.650 1.00 11.90

ATOM 1328 ODl ASP B 134 21.311 30.795 4.873 1.00 11.10

ATOM 1329 OD2 ASP B 134 20.074 31.720 3.295 1.00 16.52

ATOM 1330 C ASP B 134 22.092 28.155 3.545 1.00 12.75

ATOM 1331 O ASP B 134 20.931 27.952 3.199 1.00 13.36

ATOM 1333 N ILE B 135 22.770 27.347 4.353 1.00 12.23

ATOM 1334 CA ILE B 135 22.253 26.096 4.827 1.00 11.91

ATOM 1336 CB ILE B 135 22.485 24.968 3.772 1.00 12.89

ATOM 1338 CGl ILE B 135 21.729 23.711 4.172 1.00 15.51

ATOM 1341 CDl ILE B 135 21.742 22.642 3.138 1.00 13.78

ATOM 1345 CG2 ILE B 135 23.965 24.700 3.552 1.00 15.78

ATOM 1349 C ILE B 135 22.941 25.799 6.156 1.00 11.65

ATOM 1350 O ILE B 135 24.093 26.207 6.393 1.00 11.92

ATOM 1352 N ALA B 136 22.223 25.163 7.067 1.00 11.73

ATOM 1353 CA ALA B 136 22.801 24.799 8.350 1.00 11.68

ATOM 1355 CB ALA B 136 22.479 25.830 9.409 1.00 11.95

ATOM 1359 C ALA B 136 22.226 23.468 8.786 1.00 12.50

ATOM 1360 O ALA B 136 21.025 23.240 8.644 1.00 12.48

ATOM 1362 N LEU B 137 23.078 22.636 9.354 1.00 12.73

ATOM 1363 CA LEU B 137 22.640 21.426 10.022 1.00 12.13

ATOM 1365 CB LEU B 137 23.690 20.313 9.906 1.00 12.47

ATOM 1368 CG LEU B 137 23.623 19.471 8.674 1.00 14.12

ATOM 1370 CDl LEU B 137 24.996 18.802 8.464 1.00 14.97

ATOM 1374 CD2 LEU B 137 22.471 18.477 8.769 1.00 16.51

ATOM 1378 C LEU B 137 22.474 21.728 11.486 1.00 12.60

ATOM 1379 O LEU B 137 23.362 22.323 12.093 1.00 13.51

ATOM 1381 N LEU B 138 21.345 21.322 12.066 1.00 12.90

ATOM 1382 CA LEU B 138 21.138 21.496 13.494 1.00 11.80

ATOM 1384 CB LEU B 138 19.849 22.282 13.724 1.00 12.59

ATOM 1387 CG LEU B 138 19.642 23.496 12.836 1.00 13.87

ATOM 1389 CDl LEU B 138 18.305 24.188 13.127 1.00 20.52

ATOM 1393 CD2 LEU B 138 20.815 24.421 13.030 1.00 11.03

ATOM 1397 C LEU B 138 20.990 20.121 14.101 1.00 12.82

ATOM 1398 O LEU B 138 20.236 19.319 13.583 1.00 13.72

ATOM 1400 N GLN B 139 21.708 19.845 15.182 1.00 12.35 ATOM 1401 CA GLN B 139 21.584 18.560 15.837 1.00 13.32

ATOM 1403 CB GLN B 139 22.942 17.996 16.242 1.00 13.60

ATOM 1406 CG GLN B 139 22.882 16.591 16.809 1.00 14.97

ATOM 1409 CD GLN B 139 24.224 16.098 17.324 1.00 15.13

ATOM 1410 OEl GLN B 139 25.078 16.889 17.716 1.00 17.74

ATOM 1411 NE 2 GLN B 139 24.405 14.789 17.324 1.00 18.80

ATOM 1414 C GLN B 139 20.751 18.817 17.067 1.00 12.27

ATOM 1415 O GLN B 139 21.108 19.642 17.913 1.00 12.32

ATOM 1417 N LEU B 140 19.647 18.106 17.188 1.00 12.50

ATOM 1418 CA LEU B 140 18.807 18.242 18.357 1.00 12.47

ATOM 1420 CB LEU B 140 17.501 17.434 18.217 1.00 12.74

ATOM 1423 CG LEU B 140 16.677 17.694 16.933 1.00 15.12

ATOM 1425 CDl LEU B 140 15.418 16.844 16.956 1.00 18.19

ATOM 1429 CD2 LEU B 140 16.406 19.153 16.766 1.00 17.85

ATOM 1433 C LEU B 140 19.550 17.752 19.592 1.00 13.90

ATOM 1434 O LEU B 140 20.460 16.904 19.486 1.00 12.92

ATOM 1436 N SER B 141 19.167 18.270 20.756 1.00 13.74

ATOM 1437 CA SER B 141 19.788 17.832 22.006 1.00 15.01

ATOM 1439 CB SER B 141 19.192 18.604 23.182 1.00 15.77

ATOM 1442 OG SER B 141 19.684 19.907 23.106 1.00 17.67

ATOM 1444 C SER B 141 19.641 16.332 22.224 1.00 15.05

ATOM 1445 O SER B 141 20.552 15.668 22.721 1.00 16.04

ATOM 1447 N ARG B 142 18.502 15.793 21.845 1.00 16.90

ATOM 1448 CA ARG B 142 18.271 14.385 21.965 1.00 17.04

ATOM 1450 CB ARG B 142 17.415 14.105 23.206 1.00 17.51

ATOM 1453 CG ARG B 142 18.130 14.379 24.513 1.00 19.58

ATOM 1456 CD ARG B 142 19.193 13.352 24.775 1.00 14.12

ATOM 1459 NE ARG B 142 19.788 13.554 26.090 1.00 17.88

ATOM 1461 CZ ARG B 142 21.074 13.411 26.404 1.00 18.70

ATOM 1462 NHl ARG B 142 21.976 13.095 25.493 1.00 23.10

ATOM 1465 NH2 ARG B 142 21.470 13.641 27.655 1.00 22.74

ATOM 1468 C ARG B 142 17.538 13.942 20.722 1.00 17.98

ATOM 1469 O ARG B 142 16.844 14.748 20.116 1.00 17.87

ATOM 1471 N PRO B 143 17.653 12.659 20.365 1.00 19.10

ATOM 1472 CA PRO B 143 16.943 12.143 19.202 1.00 19.02

ATOM 1474 CB PRO B 143 17.477 10.719 19.051 1.00 19.90

ATOM 1477 CG PRO B 143 17.953 10.329 20.393 1.00 22.44

ATOM 1480 CD PRO B 143 18.442 11.619 21.035 1.00 18.80

ATOM 1483 C PRO B 143 15.483 12.125 19.475 1.00 19.35

ATOM 1484 O PRO B 143 15.100 11.950 20.634 1.00 21.42

ATOM 1485 N ILE B 144 14.658 12.315 18.456 1.00 19.11

ATOM 1486 CA ILE B 144 13.232 12.175 18.658 1.00 19.22

ATOM 1488 CB ILE B 144 12.409 13.410 18.133 1.00 20.18

ATOM 1490 CGl ILE B 144 12.734 13.760 16.692 1.00 18.87

ATOM 1493 CDl ILE B 144 12.503 12.674 15.705 1.00 20.13

ATOM 1497 CG2 ILE B 144 12.676 14.649 18.999 1.00 25.70

ATOM 1501 C ILE B 144 12.766 10.848 18.070 1.00 18.39

ATOM 1502 O ILE B 144 13.510 10.175 17.320 1.00 21.15

ATOM 1504 N THR B 145 11.564 10.452 18.457 1.00 18.66

ATOM 1505 CA THR B 145 10.906 9.325 17.869 1.00 18.27

ATOM 1507 CB THR B 145 10.117 8.549 18.955 1.00 18.25

ATOM 1509 OGl THR B 145 11.016 8.181 20.006 1.00 23.30

ATOM 1511 CG2 THR B 145 9.518 7.292 18.330 1.00 19.50

ATOM 1515 C THR B 145 9.941 9.749 16.785 1.00 18.10

ATOM 1516 O THR B 145 9.099 10.619 17.008 1.00 18.67

ATOM 1518 N PHE B 146 10.053 9.141 15.613 1.00 17.74

ATOM 1519 CA PHE B 146 9.150 9.442 14.503 1.00 18.16

ATOM 1521 CB PHE B 146 9.590 8.734 13.231 1.00 17.89

ATOM 1524 CG PHE B 146 10.942 9.140 12.744 1.00 18.40

ATOM 1525 CDl PHE B 146 11.445 10.410 12.993 1.00 17.11

ATOM 1527 CEl PHE B 146 12.713 10.785 12.517 1.00 16.01 ATOM 1529 CZ PHE B 146 13.446 9.897 11.772 1.00 16.76

ATOM 1531 CE2 PHE B 146 12.954 8.642 11.526 1.00 18.34

ATOM 1533 CD2 PHE B 146 11.698 8.266 11.996 1.00 17.85

ATOM 1535 C PHE B 146 7.753 8.973 14.843 1.00 19.52

ATOM 1536 O PHE B 146 7.569 8.029 15.628 1.00 20.81

ATOM 1538 N SER B 147 6.773 9.627 14.252 1.00 16.73

ATOM 1539 CA SER B 147 5.388 9.347 14.551 1.00 18.94

ATOM 1541 CB SER B 147 4.947 10.245 15.709 1.00 18.45

ATOM 1544 OG SER B 147 4.806 11.606 15.300 1.00 18.27

ATOM 1546 C SER B 147 4.593 9.708 13.312 1.00 17.89

ATOM 1547 O SER B 147 5.165 10.038 12.284 1.00 18.61

ATOM 1549 N ARG B 148 3.276 9.704 13.417 1.00 19.02

ATOM 1550 CA ARG B 148 2.438 10.125 12.314 1.00 20.54

ATOM 1552 CB ARG B 148 0.964 9.861 12.643 1.00 21.29

ATOM 1555 CG ARG B 148 0.632 8.381 12.734 1.00 26.76

ATOM 1558 CD ARG B 148 -0.859 8.123 12.964 1.00 31.58

ATOM 1561 NE ARG B 148 -1.395 8.748 14.175 1.00 39.90

ATOM 1563 CZ ARG B 148 -2.487 9.529 14.241 1.00 48.12

ATOM 1564 NHl ARG B 148 -2.876 10.014 15.428 1.00 48.44

ATOM 1567 NH2 ARG B 148 -3.208 9.839 13.155 1.00 48.64

ATOM 1570 C ARG B 148 2.608 11.601 11.984 1.00 19.34

ATOM 1571 O ARG B 148 2.270 12.018 10.885 1.00 19.74

ATOM 1573 N TYR B 149 3.080 12.397 12.941 1.00 16.68

ATOM 1574 CA TYR B 149 3.179 13.834 12.766 1.00 16.52

ATOM 1576 CB TYR B 149 2.467 14.549 13.924 1.00 16.96

ATOM 1579 CG TYR B 149 1.015 14.223 13.927 1.00 17.20

ATOM 1580 CDl TYR B 149 0.151 14.812 13.015 1.00 18.57

ATOM 1582 CEl TYR B 149 -1.190 14.438 12.963 1.00 15.48

ATOM 1584 CZ TYR B 149 -1.661 13.507 13.836 1.00 22.52

ATOM 1585 OH TYR B 149 -2.983 13.129 13.802 1.00 23.20

ATOM 1587 CE2 TYR B 149 -0.809 12.897 14.731 1.00 22.30

ATOM 1589 CD2 TYR B 149 0.509 13.248 14.768 1.00 23.24

ATOM 1591 C TYR B 149 4.632 14.321 12.657 1.00 14.10

ATOM 1592 O TYR B 149 4.850 15.486 12.433 1.00 15.29

ATOM 1594 N ILE B 150 5.599 13.417 12.821 1.00 14.16

ATOM 1595 CA ILE B 150 7.011 13.753 12.847 1.00 13.66

ATOM 1597 CB ILE B 150 7.574 13.733 14.282 1.00 13.12

ATOM 1599 CGl ILE B 150 6.793 14.724 15.176 1.00 11.37

ATOM 1602 CDl ILE B 150 7.239 14.723 16.600 1.00 15.60

ATOM 1606 CG2 ILE B 150 9.046 14.073 14.255 1.00 14.82

ATOM 1610 C ILE B 150 7.771 12.736 12.018 1.00 12.93

ATOM 1611 O ILE B 150 7.920 11.580 12.414 1.00 14.96

ATOM 1613 N ARG B 151 8.229 13.164 10.847 1.00 13.18

ATOM 1614 CA ARG B 151 8.846 12.244 9.911 1.00 13.91

ATOM 1616 CB ARG B 151 7.793 11.628 8.974 1.00 14.18

ATOM 1619 CG ARG B 151 6.849 10.676 9.702 1.00 18.91

ATOM 1622 CD ARG B 151 5.765 10.160 8.819 1.00 24.72

ATOM 1625 NE ARG B 151 6.246 9.153 7.879 1.00 40.91

ATOM 1627 CZ ARG B 151 5.451 8.373 7.141 1.00 45.70

ATOM 1628 NHl ARG B 151 4.123 8.475 7.256 1.00 49.14

ATOM 1631 NH2 ARG B 151 5.978 7.480 6.291 1.00 46.49

ATOM 1634 C ARG B 151 9.874 12.981 9.096 1.00 12.01

ATOM 1635 O ARG B 151 9.718 14.170 8.810 1.00 12.99

ATOM 1637 N PRO B 152 10.961 12.292 8.750 1.00 11.63

ATOM 1638 CA PRO B 152 11.994 13.000 8.022 1.00 11.16

ATOM 1640 CB PRO B 152 13.231 12.108 8.232 1.00 10.87

ATOM 1643 CG PRO B 152 12.649 10.733 8.292 1.00 13.69

ATOM 1646 CD PRO B 152 11.321 10.881 8.964 1.00 13.42

ATOM 1649 C PRO B 152 11.658 13.076 6.557 1.00 12.44

ATOM 1650 O PRO B 152 10.920 12.239 6.050 1.00 13.24

ATOM 1651 N ILE B 153 12.241 14.050 5.867 1.00 11.49 ATOM 1652 CA ILE B 153 12.132 14.143 4.412 1.00 11.69

ATOM 1654 CB ILE B 153 11.837 15.605 3.958 1.00 10.82

ATOM 1656 CGl ILE B 153 11.597 15.669 2.445 1.00 12.07

ATOM 1659 CDl ILE B 153 11.030 16.948 1.939 1.00 12.20

ATOM 1663 CG2 ILE B 153 12.956 16.539 4.381 1.00 11.21

ATOM 1667 C ILE B 153 13.412 13.645 3.753 1.00 11.68

ATOM 1668 O ILE B 153 14.512 13.847 4.251 1.00 12.50

ATOM 1670 N SER B 154 13.248 12.930 2.655 1.00 13.96

ATOM 1671 CA SER B 154 14.336 12.343 1.951 1.00 12.80

ATOM 1673 CB SER B 154 13.831 11.409 0.851 1.00 13.34

ATOM 1676 OG SER B 154 13.222 10.270 1.460 1.00 17.01

ATOM 1678 C SER B 154 15.161 13.439 1.327 1.00 11.74

ATOM 1679 O SER B 154 14.597 14.399 0.769 1.00 9.98

ATOM 1681 N LEU B 155 16.475 13.292 1.411 1.00 13.51

ATOM 1682 CA LEU B 155 17.386 14.241 0.780 1.00 13.12

ATOM 1684 CB LEU B 155 18.623 14.432 1.629 1.00 13.59

ATOM 1687 CG LEU B 155 18.433 15.135 2.969 1.00 15.48

ATOM 1689 CDl LEU B 155 19.714 15.037 3.769 1.00 15.88

ATOM 1693 CD2 LEU B 155 18.053 16.587 2.737 1.00 18.20

ATOM 1697 C LEU B 155 17.775 13.802 -0.649 1.00 13.75

ATOM 1698 O LEU B 155 18.000 12.628 -0.899 1.00 14.10

ATOM 1700 N PRO B 156 17.882 14.760 -1.582 1.00 13.32

ATOM 1701 CA PRO B 156 18.279 14.390 -2.940 1.00 14.19

ATOM 1703 CB PRO B 156 17.910 15.636 -3.773 1.00 15.39

ATOM 1706 CG PRO B 156 17.963 16.746 -2.822 1.00 14.86

ATOM 1709 CD PRO B 156 17.662 16.214 -1.446 1.00 12.45

ATOM 1712 C PRO B 156 19.760 14.127 -3.032 1.00 15.21

ATOM 1713 O PRO B 156 20.566 14.674 -2.236 1.00 14.86

ATOM 1714 N ALA B 157 20.132 13.362 -4.042 1.00 17.24

ATOM 1715 CA ALA B 157 21.525 13.129 -4.328 1.00 19.04

ATOM 1717 CB ALA B 157 21.660 12.014 -5.317 1.00 20.95

ATOM 1721 C ALA B 157 22.141 14.396 -4.909 1.00 18.33

ATOM 1722 O ALA B 157 21.431 15.273 -5.417 1.00 17.97

ATOM 1724 N ALA B 158 23.464 14.459 -4.880 1.00 19.38

ATOM 1725 CA ALA B 158 24.210 15.619 -5.357 1.00 19.82

ATOM 1727 CB ALA B 158 25.684 15.369 -5.266 1.00 21.72

ATOM 1731 C ALA B 158 23.823 16.011 -6.783 1.00 21.39

ATOM 1732 O ALA B 158 23.768 17.194 -7.115 1.00 21.52

ATOM 1734 N GLN B 159 23.535 15.031 -7.632 1.00 20.37

ATOM 1735 CA GLN B 159 23.186 15.339 -9.028 1.00 21.86

ATOM 1737 CB GLN B 159 24.113 14.562 -9.978 1.00 22.37

ATOM 1740 CG GLN B 159 25.570 14.893 -9.779 1.00 22.60

ATOM 1743 CD GLN B 159 25.840 16.381 -9.775 1.00 27.40

ATOM 1744 OEl GLN B 159 25.163 17.144 -10.461 1.00 30.22

ATOM 1745 NE2 GLN B 159 26.817 16.801 -9.004 1.00 22.41

ATOM 1748 C GLN B 159 21.710 15.110 -9.392 1.00 21.70

ATOM 1749 O GLN B 159 21.365 14.947 -10.560 1.00 23.96

ATOM 1751 N ALA B 160 20.835 15.118 -8.396 1.00 20.18

ATOM 1752 CA ALA B 160 19.426 15.029 -8.645 1.00 20.95

ATOM 1754 CB ALA B 160 18.670 14.884 -7.337 1.00 19.71

ATOM 1758 C ALA B 160 19.042 16.317 -9.345 1.00 20.69

ATOM 1759 O ALA B 160 19.483 17.387 -8.961 1.00 19.23

ATOM 1761 N SER B 161 18.245 16.214 -10.390 1.00 21.96

ATOM 1762 CA SER B 161 17.793 17.419 -11.089 1.00 23.44

ATOM 1764 CB SER B 161 18.190 17.433 -12.573 1.00 25.74

ATOM 1767 OG SER B 161 19.515 17.940 -12.722 1.00 30.81

ATOM 1769 C SER B 161 16.307 17.429 -10.908 1.00 22.84

ATOM 1770 O SER B 161 15.639 16.387 -10.983 1.00 25.44

ATOM 1772 N PHE B 162 15.797 18.592 -10.545 1.00 18.07

ATOM 1773 CA PHE B 162 14.406 18.765 -10.397 1.00 16.59

ATOM 1775 CB PHE B 162 14.093 19.308 -9.014 1.00 15.63 ATOM 1778 CG PHE B 162 14.366 18.313 -7.916 1.00 14.67

ATOM 1779 CDl PHE B 162 13.394 17.409 -7.518 1.00 12.99

ATOM 1781 CEl PHE B 162 13.654 16.476 -6.532 1.00 15.26

ATOM 1783 CZ PHE B 162 14.854 16.491 -5.902 1.00 13.77

ATOM 1785 CE2 PHE B 162 15.828 17.388 -6.271 1.00 14.82

ATOM 1787 CD2 PHE B 162 15.603 18.265 -7.303 1.00 11.70

ATOM 1789 C PHE B 162 14.108 19.755 -11.512 1.00 15.48

ATOM 1790 O PHE B 162 14.678 20.845 -11.544 1.00 15.78

ATOM 1792 N PRO B 163 13.273 19.347 -12.454 1.00 14.34

ATOM 1793 CA PRO B 163 13.215 20.129 -13.670 1.00 13.51

ATOM 1795 CB PRO B 163 12.421 19.250 -14.611 1.00 14.71

ATOM 1798 CG PRO B 163 11.609 18.401 -13.726 1.00 17.10

ATOM 1801 CD PRO B 163 12.391 18.162 -12.507 1.00 15.68

ATOM 1804 C PRO B 163 12.470 21.454 -13.517 1.00 12.76

ATOM 1805 O PRO B 163 11.561 21.559 -12.673 1.00 11.19

ATOM 1806 N ASN B 164 12.831 22.420 -14.354 1.00 11.43

ATOM 1807 CA ASN B 164 12.063 23.637 -14.470 1.00 12.06

ATOM 1809 CB ASN B 164 12.516 24.411 -15.716 1.00 11.54

ATOM 1812 CG ASN B 164 13.952 24.894 -15.602 1.00 14.46

ATOM 1813 ODl ASN B 164 14.502 24.968 -14.498 1.00 17.61

ATOM 1814 ND2 ASN B 164 14.566 25.211 -16.733 1.00 11.37

ATOM 1817 C ASN B 164 10.606 23.343 -14.595 1.00 12.14

ATOM 1818 O ASN B 164 10.208 22.453 -15.353 1.00 12.00

ATOM 1820 N GLY B 165 9.808 24.090 -13.841 1.00 12.03

ATOM 1821 CA GLY B 165 8.376 23.963 -13.908 1.00 12.53

ATOM 1824 C GLY B 165 7.783 22.905 -13.009 1.00 11.55

ATOM 1825 O GLY B 165 6.570 22.825 -12.899 1.00 12.74

ATOM 1827 N LEU B 166 8.592 22.072 -12.361 1.00 12.11

ATOM 1828 CA LEU B 166 8.039 21.096 -11.429 1.00 10.72

ATOM 1830 CB LEU B 166 9.152 20.248 -10.849 1.00 10.33

ATOM 1833 CG LEU B 166 8.688 19.126 -9.906 1.00 11.87

ATOM 1835 CDl LEU B 166 7.810 18.095 -10.624 1.00 16.26

ATOM 1839 CD2 LEU B 166 9.914 18.481 -9.225 1.00 12.58

ATOM 1843 C LEU B 166 7.299 21.799 -10.300 1.00 10.11

ATOM 1844 O LEU B 166 7.771 22.816 -9.773 1.00 10.90

ATOM 1846 N HIS B 167 6.094 21.323 -10.023 1.00 11.34

ATOM 1847 CA HIS B 167 5.274 21.902 -8.959 1.00 10.02

ATOM 1849 CB HIS B 167 3.793 21.663 -9.203 1.00 10.20

ATOM 1852 CG HIS B 167 3.243 22.498 -10.298 1.00 9.76

ATOM 1853 NDl HIS B 167 2.030 23.147 -10.222 1.00 14.82

ATOM 1855 CEl HIS B 167 1.832 23.827 -11.337 1.00 15.51

ATOM 1857 NE2 HIS B 167 2.877 23.665 -12.124 1.00 16.85

ATOM 1859 CD2 HIS B 167 3.796 22.867 -11.476 1.00 11.38

ATOM 1861 C HIS B 167 5.647 21.364 -7.611 1.00 11.92

ATOM 1862 O HIS B 167 5.192 20.243 -7.225 1.00 12.42

ATOM 1864 N CYS B 168 6.466 22.138 -6.906 1.00 9.91

ATOM 1865 CA CYS B 168 6.829 21.811 -5.542 1.00 9.21

ATOM 1867 CB CYS B 168 8.315 22.034 -5.369 1.00 11.09

ATOM 1870 SG CYS B 168 9.219 21.150 -6.678 1.00 12.12

ATOM 1872 C CYS B 168 5.986 22.608 -4.560 1.00 10.69

ATOM 1873 O CYS B 168 5.168 23.426 -4.976 1.00 11.61

ATOM 1875 N THR B 169 6.159 22.347 -3.273 1.00 10.76

ATOM 1876 CA THR B 169 5.405 23.067 -2.258 1.00 10.20

ATOM 1878 CB THR B 169 4.351 22.170 -1.609 1.00 11.68

ATOM 1880 OGl THR B 169 3.423 21.739 -2.623 1.00 11.88

ATOM 1882 CG2 THR B 169 3.603 22.894 -0.531 1.00 11.93

ATOM 1886 C THR B 169 6.343 23.657 -1.230 1.00 11.59

ATOM 1887 O THR B 169 7.258 22.987 -0.757 1.00 9.71

ATOM 1889 N VAL B 170 6.119 24.920 -0.920 1.00 12.26

ATOM 1890 CA VAL B 170 6.836 25.548 0.165 1.00 12.18

ATOM 1892 CB VAL B 170 7.512 26.871 -0.239 1.00 11.17 ATOM 1894 CGl VAL B 170 6.514 27.879 -0.734 1.00 9.18

ATOM 1898 CG2 VAL B 170 8.302 27.420 0.902 1.00 11.70

ATOM 1902 C VAL B 170 5.833 25.730 1.300 1.00 11.28

ATOM 1903 O VAL B 170 4.656 26.036 1.079 1.00 13.61

ATOM 1905 N THR B 171 6.301 25.483 2.516 1.00 12.75

ATOM 1906 CA THR B 171 5.462 25.534 3.705 1.00 12.00

ATOM 1908 CB THR B 171 5.233 24.125 4.248 1.00 12.72

ATOM 1910 OGl THR B 171 6.486 23.393 4.298 1.00 11.61

ATOM 1912 CG2 THR B 171 4.247 23.391 3.370 1.00 13.48

ATOM 1916 C THR B 171 6.095 26.412 4.776 1.00 13.15

ATOM 1917 O THR B 171 7.313 26.613 4.803 1.00 10.31

ATOM 1919 N GLY B 172 5.272 26.936 5.686 1.00 12.86

ATOM 1920 CA GLY B 172 5.828 27.705 6.766 1.00 11.74

ATOM 1923 C GLY B 172 4.805 28.506 7.510 1.00 12.36

ATOM 1924 O GLY B 172 3.633 28.552 7.102 1.00 12.64

ATOM 1926 N TRP B 173 5.279 29.125 8.597 1.00 12.67

ATOM 1927 CA TRP B 173 4.416 29.902 9.490 1.00 13.43

ATOM 1929 CB TRP B 173 4.560 29.412 10.952 1.00 13.09

ATOM 1932 CG TRP B 173 3.956 28.072 11.236 1.00 12.17

ATOM 1933 CDl TRP B 173 2.644 27.803 11.494 1.00 13.02

ATOM 1935 NEl TRP B 173 2.461 26.455 11.756 1.00 14.83

ATOM 1937 CE 2 TRP B 173 3.688 25.838 11.733 1.00 13.00

ATOM 1938 CD2 TRP B 173 4.663 26.831 11.426 1.00 12.62

ATOM 1939 CE 3 TRP B 173 5.997 26.447 11.288 1.00 12.53

ATOM 1941 CZ3 TRP B 173 6.328 25.116 11.525 1.00 10.72

ATOM 1943 CH2 TRP B 173 5.321 24.154 11.819 1.00 11.37

ATOM 1945 CZ2 TRP B 173 4.010 24.513 11.928 1.00 12.67

ATOM 1947 C TRP B 173 4.781 31.367 9.440 1.00 13.54

ATOM 1948 O TRP B 173 4.490 32.113 10.380 1.00 14.69

ATOM 1950 N GLY B 174 5.408 31.780 8.348 1.00 13.68

ATOM 1951 CA GLY B 174 5.853 33.157 8.168 1.00 14.16

ATOM 1954 C GLY B 174 4.671 34.031 7.842 1.00 13.55

ATOM 1955 O GLY B 174 3.498 33.587 7.814 1.00 13.18

ATOM 1957 N HIS B 175 4.951 35.284 7.571 1.00 15.79

ATOM 1958 CA HIS B 175 3.879 36.257 7.353 1.00 16.69

ATOM 1960 CB HIS B 175 4.478 37.631 7.078 1.00 17.61

ATOM 1963 CG HIS B 175 5.117 38.248 8.277 1.00 19.39

ATOM 1964 NDl HIS B 175 5.912 39.374 8.196 1.00 21.45

ATOM 1966 CEl HIS B 175 6.346 39.681 9.405 1.00 23.89

ATOM 1968 NE 2 HIS B 175 5.882 38.788 10.260 1.00 24.02

ATOM 1970 CD2 HIS B 175 5.104 37.881 9.581 1.00 21.70

ATOM 1972 C HIS B 175 3.023 35.856 6.193 1.00 17.79

ATOM 1973 O HIS B 175 3.504 35.193 5.250 1.00 16.87

ATOM 1975 N VAL B 176 1.751 36.254 6.250 1.00 19.47

ATOM 1976 CA VAL B 176 0.780 35.929 5.190 1.00 18.97

ATOM 1978 CB VAL B 176 0.589 35.464 5.746 1.00 20.34

ATOM 1980 CGl VAL B 176 0.456 34.128 6.419 1.00 20.86

ATOM 1984 CG2 VAL B 176 1.169 36.486 6.727 1.00 20.58

ATOM 1988 C VAL B 176 0.597 37.073 4.160 1.00 19.33

ATOM 1989 O VAL B 176 0.148 36.919 3.219 1.00 17.27

ATOM 1991 N ALA B 177 1.286 38.199 4.386 1.00 19.35

ATOM 1992 CA ALA B 177 1.371 39.355 3.481 1.00 20.82

ATOM 1994 CB ALA B 177 0.091 40.126 3.481 1.00 21.04

ATOM 1998 C ALA B 177 2.504 40.218 4.030 1.00 21.63

ATOM 1999 O ALA B 177 3.015 39.949 5.131 1.00 21.69

ATOM 2001 N PRO B 178 2.981 41.199 3.254 1.00 21.51

ATOM 2002 CA PRO B 178 4.073 42.003 3.803 1.00 23.79

ATOM 2004 CB PRO B 178 4.352 43.030 2.694 1.00 23.64

ATOM 2007 CG PRO B 178 3.878 42.350 1.450 1.00 24.29

ATOM 2010 CD PRO B 178 2.702 41.523 1.852 1.00 23.51

ATOM 2013 C PRO B 178 3.756 42.636 5.160 1.00 25.43 ATOM 2014 O PRO B 178 2.725 43.272 5.321 1.00 26.67

ATOM 2015 N SER B 179 4.621 42.368 6.140 1.00 26.65

ATOM 2016 CA SER B 179 4.439 42.792 7.541 1.00 26.98

ATOM 2018 CB SER B 179 4.680 44.310 7.683 1.00 27.70

ATOM 2021 OG SER B 179 6.004 44.662 7.282 1.00 32.47

ATOM 2023 C SER B 179 3.098 42.416 8.170 1.00 27.20

ATOM 2024 O SER B 179 2.672 43.058 9.128 1.00 28.53

ATOM 2026 N VAL B 180 2.448 41.371 7.659 1.00 25.80

ATOM 2027 CA VAL B 180 1.242 40.850 8.266 1.00 25.81

ATOM 2029 CB VAL B 180 0.089 40.849 7.304 1.00 25.52

ATOM 2031 CGl VAL B 180 1.146 40.201 7.939 1.00 25.20

ATOM 2035 CG2 VAL B 180 0.177 42.280 6.869 1.00 27.16

ATOM 2039 C VAL B 180 1.471 39.434 8.749 1.00 26.05

ATOM 2040 O VAL B 180 1.576 38.494 7.948 1.00 24.28

ATOM 2042 N SER B 181 1.552 39.310 10.071 1.00 25.49

ATOM 2043 CA SER B 181 1.671 38.033 10.741 1.00 24.75

ATOM 2045 CB SER B 181 1.779 38.249 12.253 1.00 25.36

ATOM 2048 OG SER B 181 3.141 38.395 12.587 1.00 33.88

ATOM 2050 C SER B 181 0.534 37.056 10.468 1.00 22.94

ATOM 2051 O SER B 181 0.634 37.435 10.398 1.00 21.90

ATOM 2053 N LEU B 182 0.902 35.778 10.350 1.00 21.07

ATOM 2054 CA LEU B 182 0.055 34.673 10.336 1.00 20.80

ATOM 2056 CB LEU B 182 0.693 33.338 10.215 1.00 19.66

ATOM 2059 CG LEU B 182 0.142 32.059 10.300 1.00 19.83

ATOM 2061 CDl LEU B 182 1.085 31.975 9.116 1.00 16.83

ATOM 2065 CD2 LEU B 182 0.779 30.853 10.366 1.00 19.17

ATOM 2069 C LEU B 182 0.863 34.706 11.635 1.00 20.63

ATOM 2070 O LEU B 182 0.304 34.704 12.726 1.00 19.07

ATOM 2072 N LEU B 183 2.178 34.766 11.488 1.00 22.11

ATOM 2073 CA LEU B 183 3.062 34.933 12.623 1.00 23.02

ATOM 2075 CB LEU B 183 4.439 35.351 12.134 1.00 24.33

ATOM 2078 CG LEU B 183 5.436 35.914 13.144 1.00 25.22

ATOM 2080 CDl LEU B 183 5.112 37.359 13.429 1.00 32.82

ATOM 2084 CD2 LEU B 183 6.862 35.773 12.614 1.00 25.69

ATOM 2088 C LEU B 183 3.121 33.656 13.463 1.00 23.38

ATOM 2089 O LEU B 183 3.151 32.534 12.940 1.00 21.80

ATOM 2091 N THR B 184 3.120 33.851 14.775 1.00 23.20

ATOM 2092 CA THR B 184 3.303 32.767 15.714 1.00 22.62

ATOM 2094 CB THR B 184 3.401 33.307 17.161 1.00 24.37

ATOM 2096 OGl THR B 184 3.417 32.223 18.099 1.00 24.99

ATOM 2098 CG2 THR B 184 4.643 34.178 17.335 1.00 27.21

ATOM 2102 C THR B 184 4.559 31.981 15.345 1.00 21.60

ATOM 2103 O THR B 184 5.554 32.557 14.879 1.00 22.52

ATOM 2105 N PRO B 185 4.538 30.659 15.537 1.00 19.24

ATOM 2106 CA PRO B 185 3.569 29.754 16.157 1.00 18.60

ATOM 2108 CB PRO B 185 4.419 28.538 16.486 1.00 17.50

ATOM 2111 CG PRO B 185 5.405 28.502 15.439 1.00 20.57

ATOM 2114 CD PRO B 185 5.719 29.915 15.064 1.00 19.69

ATOM 2117 C PRO B 185 2.396 29.334 15.258 1.00 17.49

ATOM 2118 O PRO B 185 1.613 28.436 15.628 1.00 16.97

ATOM 2119 N LYS B 186 2.264 29.978 14.107 1.00 18.77

ATOM 2120 CA LYS B 186 1.084 29.782 13.257 1.00 18.26

ATOM 2122 CB LYS B 186 0.197 30.180 13.989 1.00 18.26

ATOM 2125 CG LYS B 186 0.313 31.686 14.216 1.00 21.30

ATOM 2128 CD LYS B 186 1.433 32.051 15.137 1.00 22.48

ATOM 2131 CE LYS B 186 1.543 33.599 15.232 1.00 24.07

ATOM 2134 NZ LYS B 186 2.024 34.257 13.948 1.00 26.36

ATOM 2138 C LYS B 186 0.978 28.383 12.668 1.00 17.05

ATOM 2139 O LYS B 186 0.014 27.692 12.867 1.00 17.52

ATOM 2141 N PRO B 187 1.979 27.988 11.869 1.00 16.77

ATOM 2142 CA PRO B 187 1.921 26.741 11.125 1.00 16.05 ATOM 2144 CB PRO B 187 3.306 26.649 10.498 1.00 16.67

ATOM 2147 CG PRO B 187 3.690 28.074 10.325 1.00 16.64

ATOM 2150 CD PRO B 187 3.189 28.755 11.523 1.00 16.15

ATOM 2153 C PRO B 187 0.855 26.854 10.030 1.00 15.94

ATOM 2154 O PRO B 187 0.711 27.903 9.376 1.00 15.57

ATOM 2155 N LEU B 188 0.072 25.801 9.878 1.00 13.41

ATOM 2156 CA LEU B 188 0.952 25.790 8.841 1.00 12.99

ATOM 2158 CB LEU B 188 1.579 24.405 8.736 1.00 13.52

ATOM 2161 CG LEU B 188 2.760 24.215 7.765 1.00 10.49

ATOM 2163 CDl LEU B 188 3.919 25.065 8.169 1.00 12.02

ATOM 2167 CD2 LEU B 188 3.110 22.725 7.715 1.00 12.24

ATOM 2171 C LEU B 188 0.352 26.119 7.495 1.00 13.61

ATOM 2172 O LEU B 188 0.645 25.519 7.086 1.00 12.09

ATOM 2174 N GLN B 189 0.992 27.034 6.789 1.00 12.92

ATOM 2175 CA GLN B 189 0.594 27.354 5.415 1.00 12.94

ATOM 2177 CB GLN B 189 0.771 28.830 5.192 1.00 15.30

ATOM 2180 CG GLN B 189 0.064 29.665 6.124 1.00 14.52

ATOM 2183 CD GLN B 189 1.530 29.424 5.862 1.00 19.33

ATOM 2184 OEl GLN B 189 2.034 29.830 4.816 1.00 18.44

ATOM 2185 NE2 GLN B 189 2.210 28.716 6.784 1.00 13.44

ATOM 2188 C GLN B 189 1.437 26.608 4.389 1.00 13.76

ATOM 2189 O GLN B 189 2.596 26.305 4.629 1.00 11.73

ATOM 2191 N GLN B 190 0.854 26.399 3.229 1.00 14.47

ATOM 2192 CA GLN B 190 1.495 25.674 2.130 1.00 14.99

ATOM 2194 CB GLN B 190 0.936 24.261 2.024 1.00 16.06

ATOM 2197 CG GLN B 190 0.570 24.236 1.871 1.00 16.60

ATOM 2200 CD GLN B 190 1.185 22.883 1.707 1.00 18.22

ATOM 2201 OEl GLN B 190 0.529 21.843 1.787 1.00 16.16

ATOM 2202 NE2 GLN B 190 2.503 22.886 1.539 1.00 20.40

ATOM 2205 C GLN B 190 1.181 26.441 0.863 1.00 15.54

ATOM 2206 O GLN B 190 0.125 27.088 0.767 1.00 14.54

ATOM 2208 N LEU B 191 2.090 26.377 -0.108 1.00 14.02

ATOM 2209 CA LEU B 191 1.913 27.025 -1.389 1.00 14.37

ATOM 2211 CB LEU B 191 2.469 28.436 -1.389 1.00 15.32

ATOM 2214 CG LEU B 191 2.497 29.149 -2.751 1.00 15.21

ATOM 2216 CDl LEU B 191 1.126 29.491 -3.214 1.00 19.35

ATOM 2220 CD2 LEU B 191 3.318 30.363 -2.664 1.00 14.64

ATOM 2224 C LEU B 191 2.607 26.191 -2.448 1.00 15.62

ATOM 2225 O LEU B 191 3.795 25.882 -2.316 1.00 13.48

ATOM 2227 N GLU B 192 1.865 25.870 -3.508 1.00 14.48

ATOM 2228 CA GLU B 192 2.408 25.123 -4.637 1.00 14.43

ATOM 2230 CB GLU B 192 1.284 24.421 -5.383 1.00 14.38

ATOM 2233 CG GLU B 192 1.731 23.577 -6.519 1.00 16.09

ATOM 2236 CD GLU B 192 0.666 22.595 -6.968 1.00 22.00

ATOM 2237 OEl GLU B 192 0.116 21.847 -6.103 1.00 35.68

ATOM 2238 OE2 GLU B 192 0.417 22.543 -8.177 1.00 21.46

ATOM 2239 C GLU B 192 3.072 26.159 -5.516 1.00 13.51

ATOM 2240 O GLU B 192 2.465 27.199 -5.810 1.00 15.29

ATOM 2242 N VAL B 193 4.311 25.871 -5.904 1.00 12.42

ATOM 2243 CA VAL B 193 5.147 26.754 -6.663 1.00 12.66

ATOM 2245 CB VAL B 193 6.092 27.530 -5.763 1.00 13.79

ATOM 2247 CGl VAL B 193 5.326 28.543 -4.973 1.00 15.94

ATOM 2251 CG2 VAL B 193 6.960 26.608 -4.844 1.00 13.03

ATOM 2255 C VAL B 193 5.950 25.980 -7.696 1.00 12.12

ATOM 2256 O VAL B 193 6.635 24.984 -7.348 1.00 12.57

ATOM 2258 N PRO B 194 5.853 26.406 -8.961 1.00 11.01

ATOM 2259 CA PRO B 194 6.709 25.824 -9.964 1.00 11.56

ATOM 2261 CB PRO B 194 6.113 26.322 -11.278 1.00 12.34

ATOM 2264 CG PRO B 194 5.421 27.534 -10.956 1.00 16.80

ATOM 2267 CD PRO B 194 4.995 27.478 -9.527 1.00 12.35

ATOM 2270 C PRO B 194 8.175 26.256 -9.846 1.00 10.03 ATOM 2271 O PRO B 194 8.487 27.435 -9.538 1.00 10.89

ATOM 2272 N LEU B 195 9.081 25.319 -10.057 1.00 11.35

ATOM 2273 CA LEU B 195 10.470 25.664 -10.072 1.00 10.37

ATOM 2275 CB LEU B 195 11.337 24.419 -10.210 1.00 9.68

ATOM 2278 CG LEU B 195 11.190 23.424 -9.031 1.00 10.94

ATOM 2280 CDl LEU B 195 12.165 22.280 -9.243 1.00 12.20

ATOM 2284 CD2 LEU B 195 11.433 24.121 -7.676 1.00 11.31

ATOM 2288 C LEU B 195 10.787 26.602 -11.213 1.00 9.94

ATOM 2289 O LEU B 195 10.345 26.388 -12.345 1.00 11.99

ATOM 2291 N ILE B 196 11.684 27.534 -10.917 1.00 12.95

ATOM 2292 CA ILE B 196 12.154 28.533 -11.874 1.00 12.38

ATOM 2294 CB ILE B 196 11.603 29.948 -11.505 1.00 14.30

ATOM 2296 CGl ILE B 196 10.106 29.984 -11.594 1.00 13.78

ATOM 2299 CDl ILE B 196 9.482 31.345 -11.156 1.00 13.93

ATOM 2303 CG2 ILE B 196 12.191 31.020 -12.397 1.00 14.17

ATOM 2307 C ILE B 196 13.669 28.534 -11. 1.00 12.56

ATOM 2308 O ILE B 196 14.253 28.650 -10.710 1.00 11.51

ATOM 2310 N SER B 197 14.311 28.403 -12.972 1.00 12.48

ATOM 2311 CA SER B 197 15.760 28.220 -13.050 1.00 13.52

ATOM 2313 CB SER B 197 16.234 28.048 -14.481 1.00 13.35

ATOM 2316 OG SER B 197 16.207 29.284 -15.155 1.00 14.07

ATOM 2318 C SER B 197 16.421 29.449 -12.472 1.00 11.97

ATOM 2319 O SER B 197 15.829 30.525 -12.453 1.00 13.29

ATOM 2321 N ARG B 198 17.632 29.289 -11.976 1.00 13.57

ATOM 2322 CA ARG B 198 18.318 30.441 -11.416 1.00 14.37

ATOM 2324 CB ARG B 198 19.635 30.071 -10.748 1.00 14.61

ATOM 2327 CG ARG B 198 20.593 29.318 -11.602 1.00 18.66

ATOM 2330 CD ARG B 198 21.844 29.029 -10.815 1.00 17.77

ATOM 2333 NE ARG B 198 22.600 30.252 -10.491 1.00 26.26

ATOM 2335 CZ ARG B 198 23.398 30.907 -11.335 1.00 26.68

ATOM 2336 NHl ARG B 198 23.516 30.535 -12.611 1.00 31.53

ATOM 2339 NH2 ARG B 198 24.058 31.977 -10.920 1.00 26.51

ATOM 2342 C ARG B 198 18.528 31.509 -12.477 1.00 14.36

ATOM 2343 O ARG B 198 18.508 32.700 -12.155 1.00 15.99

ATOM 2345 N GLU B 199 18.655 31.081 -13.736 1.00 14.18

ATOM 2346 CA GLU B 199 18.907 32.032 -14.829 1.00 14.23

ATOM 2348 CB GLU B 199 19.323 31.319 -16.093 1.00 13.14

ATOM 2351 CG GLU B 199 20.703 30.648 -15.969 1.00 13.26

ATOM 2354 CD GLU B 199 20.683 29.300 -15.267 1.00 27.52

ATOM 2355 OEl GLU B 199 19.585 28.754 -14.959 1.00 22.35

ATOM 2356 OE2 GLU B 199 21.799 28.794 -15.004 1.00 33.10

ATOM 2357 C GLU B 199 17.689 32.908 -15.077 1.00 13.70

ATOM 2358 O GLU B 199 17.805 34.137 -15.195 1.00 15.24

ATOM 2360 N THR B 200 16.515 32.274 -15.177 1.00 13.48

ATOM 2361 CA THR B 200 15.295 33.048 -15.303 1.00 13.84

ATOM 2363 CB THR B 200 14.054 32.164 -15.450 1.00 14.24

ATOM 2365 OGl THR B 200 14.068 31.539 -16.742 1.00 16.11

ATOM 2367 CG2 THR B 200 12.814 32.997 -15.350 1.00 13.86

ATOM 2371 C THR B 200 15.129 33.946 -14.093 1.00 14.20

ATOM 2372 O THR B 200 14.812 35.119 -14.195 1.00 15.47

ATOM 2374 N CYS B 201 15.341 33.379 -12.918 1.00 14.11

ATOM 2375 CA CYS B 201 15.140 34.079 -11.678 1.00 13.94

ATOM 2377 CB CYS B 201 15.443 33.135 -10.542 1.00 14.48

ATOM 2380 SG CYS B 201 14.813 33.688 -9.042 1.00 15.71

ATOM 2382 C CYS B 201 16.016 35.337 -11.595 1.00 14.37

ATOM 2383 O CYS B 201 15.543 36.409 -11.217 1.00 17.18

ATOM 2385 N ASN B 202 17.263 35.208 -11.988 1.00 16.21

ATOM 2386 CA ASN B 202 18.173 36.362 -12.027 1.00 16.99

ATOM 2388 CB ASN B 202 19.581 35.931 -12.427 1.00 18.29

ATOM 2391 CG ASN B 202 20.356 35.350 -11.282 1.00 16.05

ATOM 2392 ODl ASN B 202 21.069 34.345 -11.446 1.00 20.23 ATOM 2393 ND2 ASN B 202 20.216 35.957 -10.113 1.00 13.58

ATOM 2396 C ASN B 202 17.662 37.447 -12.975 1.00 18.49

ATOM 2397 O ASN B 202 17.718 38.622 -12.647 1.00 19.88

ATOM 2399 N SER B 203 17.131 37.059 -14.133 1.00 18.72

ATOM 2400 CA SER B 203 16.531 38.049 -15.025 1.00 19.06

ATOM 2402 CB SER B 203 16.162 37.419 -16.350 1.00 21.84

ATOM 2405 OG SER B 203 17.350 37.114 -17.046 1.00 29.25

ATOM 2407 C SER B 203 15.346 38.761 -14.419 1.00 18.88

ATOM 2408 O SER B 203 15.187 39.961 -14.587 1.00 20.07

ATOM 2410 N LEU B 204 14.509 38.022 -13.706 1.00 17.36

ATOM 2411 CA LEU B 204 13.373 38.601 -13.022 1.00 17.55

ATOM 2413 CB LEU B 204 12.497 37.518 -12.407 1.00 16.25

ATOM 2416 CG LEU B 204 11.807 36.598 -13.413 1.00 15.96

ATOM 2418 CDl LEU B 204 11.023 35.515 -12.682 1.00 18.64

ATOM 2422 CD2 LEU B 204 10.905 37.417 -14.375 1.00 17.85

ATOM 2426 C LEU B 204 13.821 39.568 -11.958 1.00 17.15

ATOM 2427 O LEU B 204 13.285 40.686 -11.868 1.00 17.17

ATOM 2429 N TYR B 205 14.806 39.159 -11.160 1.00 17.68

ATOM 2430 CA TYR B 205 15.260 39.995 -10.067 1.00 19.03

ATOM 2432 CB TYR B 205 16.218 39.253 -9. Ill 1.00 18.73

ATOM 2435 CG TYR B 205 15.471 38.590 -7.978 1.00 19.32

ATOM 2436 CDl TYR B 205 15.180 39.283 -6.800 1.00 17.55

ATOM 2438 CEl TYR B 205 14.460 38.700 -5.766 1.00 19.73

ATOM 2440 CZ TYR B 205 14.000 37.398 -5.910 1.00 21.40

ATOM 2441 OH TYR B 205 13.284 36.823 -4.898 1.00 19.29

ATOM 2443 CE2 TYR B 205 14.253 36.702 -7.077 1.00 20.14

ATOM 2445 CD2 TYR B 205 14.977 37.297 -8.106 1.00 19.56

ATOM 2447 C TYR B 205 15.876 41.290 -10.569 1.00 19.65

ATOM 2448 O TYR B 205 15.885 42.255 -9.840 1.00 20.24

ATOM 2450 N ASN B 206 16.386 41.284 -11.796 .00 21.25

ATOM 2451 CA ASN B 206 16.920 42.488 -12.457 .00 22.38

ATOM 2453 CB ASN B 206 17.731 42.100 -13.691 .00 22.69

ATOM 2456 CG ASN B 206 19.013 41.387 -13.346 .00 24.98

ATOM 2457 ODl ASN B 206 19.466 41.422 -12.210 1.00 25.48

ATOM 2458 ND2 ASN B 206 19.603 40.728 -14.327 1 00 25.70

ATOM 2461 C ASN B 206 15.855 43.518 -12.844 1 00 24.43

ATOM 2462 O ASN B 206 16.177 44.687 -13.062 1.00 26.60

ATOM 2464 N ILE B 207 14.599 43.100 -12.923 1.00 23.03

ATOM 2465 CA ILE B 207 13.509 43.996 -13.297 1.00 23.67

ATOM 2467 CB ILE B 207 12.261 43.198 -13.677 1.00 23.22

ATOM 2469 CGl ILE B 207 12.574 42.302 -14.882 1.00 20.94

ATOM 2472 CDl ILE B 207 11.439 41.341 -15.267 1.00 21.80

ATOM 2476 CG2 ILE B 207 11.079 44.142 -13.921 1.00 21.60

ATOM 2480 C ILE B 207 13.209 44.985 -12.167 1.00 24.97

ATOM 2481 O ILE B 207 12.921 44.586 -11.040 1.00 22.22

ATOM 2483 N ASP B 208 13.303 46.283 -12.470 1.00 26.74

ATOM 2484 CA ASP B 208 13.114 47.344 -11.470 1.00 28.41

ATOM 2486 CB ASP B 208 11.652 47.469 -11.032 1.00 29.52

ATOM 2489 CG ASP B 208 10.709 47.638 -12.185 1.00 35.24

ATOM 2490 ODl ASP B 208 11.073 48.384 -13.121 1.00 41.20

ATOM 2491 OD2 ASP B 208 9.607 47.029 -12.154 1.00 40.30

ATOM 2492 C ASP B 208 13.971 47.101 -10.247 1.00 29.16

ATOM 2493 O ASP B 208 13.547 47.344 -9.121 1.00 30.88

ATOM 2495 N ALA B 209 15.180 46.603 -10.467 1.00 30.23

ATOM 2496 CA ALA B 209 16.073 46.285 -9.370 1.00 31.48

ATOM 2498 CB ALA B 209 17.171 45.386 -9.831 1.00 31.35

ATOM 2502 C ALA B 209 16.665 47.566 -8.794 1.00 32.38

ATOM 2503 O ALA B 209 16.940 48.521 -9.533 1.00 31.05

ATOM 2505 N LYS B 210 16.837 47.574 -7.478 1.00 33.34

ATOM 2506 CA LYS B 210 17.561 48.641 -6.820 1.00 35.54

ATOM 2508 CB LYS B 210 17.202 48.709 -5.345 1.00 36.08 ATOM 2511 CG LYS B 210 15.818 49.290 -5.091 1.00 39.29

ATOM 2514 CD LYS B 210 15.190 48.706 -3.802 1.00 39.88

ATOM 2517 CE LYS B 210 13.696 49.071 -3.677 1.00 45.99

ATOM 2520 NZ LYS B 210 13.446 50.546 -3.830 1.00 48.72

ATOM 2524 C LYS B 210 19.035 48.313 -6.998 1.00 35.23

ATOM 2525 O LYS B 210 19.467 47.254 -6.561 1.00 34.03

ATOM 2527 N PRO B 211 19.804 49.227 -7.630 1.00 37.05

ATOM 2528 CA PRO B 211 21.216 49.038 -7.951 1.00 37.81

ATOM 2530 CB PRO B 211 21.677 50.445 -8.316 1.00 38.70

ATOM 2533 CG PRO B 211 20.460 51.108 -8.822 1.00 39.43

ATOM 2536 CD PRO B 211 19.333 50.559 -8.043 1.00 37.21

ATOM 2539 C PRO B 211 22.009 48.564 -6.761 1.00 38.65

ATOM 2540 O PRO B 211 22.831 47.666 -6.873 1.00 38.44

ATOM 2541 N GLU B 212 21.727 49.156 -5.616 1.00 40.18

ATOM 2542 CA GLU B 212 22.490 48.900 -4.417 1.00 42.45

ATOM 2544 CB GLU B 212 22.222 49.994 -3.374 1.00 43.19

ATOM 2547 CG GLU B 212 20.797 50.031 -2.814 1.00 44.39

ATOM 2550 CD GLU B 212 19.856 50.945 -3.593 1.00 47.82

ATOM 2551 OEl GLU B 212 20.113 51.280 -4.776 1.00 45.09

ATOM 2552 OE 2 GLU B 212 18.831 51.333 -3.003 1.00 53.15

ATOM 2553 C GLU B 212 22.173 47.574 -3.791 1.00 43.72

ATOM 2554 O GLU B 212 22.950 47.064 -2.984 1.00 44.60

ATOM 2556 N GLU B 213 21.019 47.032 -4.143 1.00 45.95

ATOM 2557 CA GLU B 213 20.383 45.989 -3.356 1.00 46.23

ATOM 2559 CB GLU B 213 19.017 46.481 -2.912 1.00 46.61

ATOM 2562 CG GLU B 213 18.327 45.578 -1.938 1.00 48.11

ATOM 2565 CD GLU B 213 16.844 45.821 -1.940 1.00 50.11

ATOM 2566 OEl GLU B 213 16.434 46.972 -1.652 1.00 56.66

ATOM 2567 OE 2 GLU B 213 16.095 44.869 -2.251 1.00 58.24

ATOM 2568 C GLU B 213 20.277 44.720 -4.194 1.00 45.77

ATOM 2569 O GLU B 213 19.202 44.394 -4.734 1.00 46.49

ATOM 2571 N PRO B 214 21.399 43.988 -4.296 1.00 44.34

ATOM 2572 CA PRO B 214 21.474 42.930 -5.265 1.00 43.05

ATOM 2574 CB PRO B 214 22.958 42.592 -5.293 1.00 42.97

ATOM 2577 CG PRO B 214 23.379 42.810 -3.896 1.00 44.23

ATOM 2580 CD PRO B 214 22.628 44.054 -3.484 1.00 44.55

ATOM 2583 C PRO B 214 20.695 41.717 -4.811 1.00 40.17

ATOM 2584 O PRO B 214 20.429 41.521 -3.615 1.00 38.88

ATOM 2585 N HIS B 215 20.374 40.911 -5.800 1.00 37.22

ATOM 2586 CA HIS B 215 19.560 39.748 -5.633 1.00 34.57

ATOM 2588 CB HIS B 215 18.077 40.083 -5.870 1.00 36.07

ATOM 2591 CG HIS B 215 17.369 40.661 -4.678 1.00 38.54

ATOM 2592 NDl HIS B 215 17.389 40.063 -3.434 1.00 44.99

ATOM 2594 CEl HIS B 215 16.675 40.790 -2.588 1.00 43.28

ATOM 2596 NE 2 HIS B 215 16.184 41.831 -3.238 1.00 40.35

ATOM 2598 CD2 HIS B 215 16.589 41.766 -4.549 1.00 42.29

ATOM 2600 C HIS B 215 20.108 38.809 -6.694 1.00 32.87

ATOM 2601 O HIS B 215 19.484 38.598 -7.744 1.00 33.98

ATOM 2603 N PHE B 216 21.300 38.279 -6.423 1.00 28.82

ATOM 2604 CA PHE B 216 21.943 37.324 -7.310 1.00 27.22

ATOM 2606 CB PHE B 216 23.434 37.550 -7.405 1.00 26.86

ATOM 2609 CG PHE B 216 24.119 36.590 -8.337 1.00 28.23

ATOM 2610 CDl PHE B 216 23.860 36.623 -9.698 1.00 24.77

ATOM 2612 CEl PHE B 216 24.465 35.745 -10.558 1.00 25.16

ATOM 2614 CZ PHE B 216 25.341 34.815 -10.072 1.00 25.89

ATOM 2616 CE 2 PHE B 216 25.616 34.763 -8.713 1.00 26.42

ATOM 2618 CD2 PHE B 216 25.006 35.635 -7.853 1.00 29.60

ATOM 2620 C PHE B 216 21.699 35.904 -6.840 1.00 24.47

ATOM 2621 O PHE B 216 22.075 35.522 -5.727 1.00 24.55

ATOM 2623 N VAL B 217 21.066 35.119 -7.697 1.00 21.46

ATOM 2624 CA VAL B 217 20.770 33.735 -7.402 1.00 19.68 ATOM 2626 CB VAL B 217 19.534 33.268 -8.154 1.00 18.04

ATOM 2628 CGl VAL B 217 19.182 31.844 -7.774 1.00 16.17

ATOM 2632 CG2 VAL B 217 18.349 34.215 -7.861 1.00 18.71

ATOM 2636 C VAL B 217 21.984 32.915 -7.775 1.00 18.11

ATOM 2637 O VAL B 217 22.341 32.735 -8.945 1.00 16.71

ATOM 2639 N GLN B 218 22.626 32.412 -6.736 1.00 19.42

ATOM 2640 CA GLN B 218 23.909 31.728 -6.832 1.00 19.73

ATOM 2642 CB GLN B 218 24.439 31.547 -5.417 1.00 21.21

ATOM 2645 CG GLN B 218 24.534 32.830 -4.571 1.00 24.90

ATOM 2648 CD GLN B 218 25.826 33.603 -4.780 1.00 20.74

ATOM 2649 OEl GLN B 218 26.710 33.187 -5.525 1.00 23.63

ATOM 2650 NE2 GLN B 218 25.945 34.738 -4.072 1.00 25.91

ATOM 2653 C GLN B 218 23.765 30.373 -7.478 1.00 20.33

ATOM 2654 O GLN B 218 22.639 29.884 -7.636 1.00 17.83

ATOM 2656 N GLU B 219 24.889 29.716 -7.797 1.00 18.49

ATOM 2657 CA GLU B 219 24.854 28.403 -8.451 1.00 20.45

ATOM 2659 CB GLU B 219 26.240 28.026 -8.951 1.00 21.21

ATOM 2662 CG GLU B 219 26.691 28.892 -10.151 1.00 28.49

ATOM 2665 CD GLU B 219 28.094 28.522 -10.694 1.00 28.41

ATOM 2666 OEl GLU B 219 28.557 27.367 -10.455 1.00 40.13

ATOM 2667 OE2 GLU B 219 28.701 29.408 -11.372 1.00 42.77

ATOM 2668 C GLU B 219 24.303 27.254 -7.590 1.00 17.57

ATOM 2669 O GLU B 219 23.879 26.229 -8.128 1.00 16.79

ATOM 2671 N ASP B 220 24.313 27.438 -6.268 1.00 16.95

ATOM 2672 CA ASP B 220 23.710 26.472 -5.328 1.00 16.31

ATOM 2674 CB ASP B 220 24.539 26.408 -4.036 1.00 16.66

ATOM 2677 CG ASP B 220 24.494 27.716 -3.215 1.00 14.15

ATOM 2678 ODl ASP B 220 24.212 28.790 -3.754 1.00 17.34

ATOM 2679 OD2 ASP B 220 24.756 27.674 -1.987 1.00 13.87

ATOM 2680 C ASP B 220 22.253 26.828 -4.981 1.00 15.67

ATOM 2681 O ASP B 220 21.758 26.428 -3.935 1.00 15.61

ATOM 2683 N MET B 221 21.604 27.641 -5.806 1.00 13.13

ATOM 2684 CA MET B 221 20.250 28.061 -5.543 1.00 14.54

ATOM 2686 CB MET B 221 20.210 29.552 -5.216 1.00 16.59

ATOM 2689 CG MET B 221 20.936 29.929 -3.943 1.00 17.42

ATOM 2692 SD MET B 221 21.042 31.745 -3.797 1.00 19.24

ATOM 2693 CE MET B 221 21.725 31.893 -2.137 1.00 24.64

ATOM 2697 C MET B 221 19.322 27.771 -6.737 1.00 14.56

ATOM 2698 O MET B 221 19.761 27.645 -7.899 1.00 12.57

ATOM 2700 N VAL B 222 18.028 27.717 -6.436 1.00 11.95

ATOM 2701 CA VAL B 222 16.982 27.663 -7.426 1.00 12.43

ATOM 2703 CB VAL B 222 16.473 26.240 -7.611 1.00 13.45

ATOM 2705 CGl VAL B 222 15.750 25.754 -6.337 1.00 14.24

ATOM 2709 CG2 VAL B 222 15.587 26.117 -8.838 1.00 13.71

ATOM 2713 C VAL B 222 15.865 28.588 -6.940 1.00 13.54

ATOM 2714 O VAL B 222 15.852 28.961 -5.781 1.00 13.08

ATOM 2716 N CYS B 223 14.987 28.998 -7.839 1.00 10.82

ATOM 2717 CA CYS B 223 13.832 29.738 -7.429 1.00 11.19

ATOM 2719 CB CYS B 223 13.724 30.997 -8.237 1.00 13.23

ATOM 2722 SG CYS B 223 15.136 32.052 -7.853 1.00 14.77

ATOM 2724 C CYS B 223 12.581 28.914 -7.616 1.00 12.21

ATOM 2725 O CYS B 223 12.592 27.900 -8.279 1.00 10.85

ATOM 2727 N ALA B 224 11.485 29.438 -7.096 1.00 11.10

ATOM 2728 CA ALA B 224 10.155 28.847 -7.328 1.00 12.32

ATOM 2730 CB ALA B 224 9.924 27.713 -6.444 1.00 13.11

ATOM 2734 C ALA B 224 9.129 29.917 -7.082 1.00 13.20

ATOM 2735 O ALA B 224 9.285 30.719 -6.176 1.00 14.47

ATOM 2737 N GLY B 225 8.086 29.930 -7.892 1.00 14.02

ATOM 2738 CA GLY B 225 6.984 30.873 -7.637 1.00 15.32

ATOM 2741 C GLY B 225 6.434 31.330 -8.957 1.00 15.87

ATOM 2742 O GLY B 225 6.379 30.545 -9.898 1.00 16.42 ATOM 2744 N TYR B 226 6.055 32.605 -8.997 1.00 16.33

ATOM 2745 CA TYR B 226 5.251 33.170 -10.053 1.00 18.58

ATOM 2747 CB TYR B 226 3.813 33.265 -9.595 1.00 19.24

ATOM 2750 CG TYR B 226 3.239 31.913 -9.213 1.00 16.36

ATOM 2751 CDl TYR B 226 2.648 31.098 -10.145 1.00 17.85

ATOM 2753 CEl TYR B 226 2.126 29.824 -9.774 1.00 19.00

ATOM 2755 CZ TYR B 226 2.237 29.378 -8.465 1.00 18.79

ATOM 2756 OH TYR B 226 1.720 28.137 -8.141 1.00 21.93

ATOM 2758 CE2 TYR B 226 2.835 30.173 -7.515 1.00 19.13

ATOM 2760 CD2 TYR B 226 3.338 31.446 -7.889 1.00 18.22

ATOM 2762 C TYR B 226 5.782 34.531 -10.427 1.00 18.80

ATOM 2763 O TYR B 226 6.055 35.388 -9.570 1.00 19.25

ATOM 2765 N VAL B 227 5.940 34.730 -11.722 1.00 19.56

ATOM 2766 CA VAL B 227 6.372 35.996 -12.265 1.00 21.14

ATOM 2768 CB VAL B 227 6.403 35.890 -13.799 1.00 21.14

ATOM 2770 CGl VAL B 227 6.436 37.249 -14.451 1.00 23.47

ATOM 2774 CG2 VAL B 227 7.623 35.041 -14.228 1.00 24.10

ATOM 2778 C VAL B 227 5.469 37.146 -11.812 1.00 20.98

ATOM 2779 O VAL B 227 5.949 38.250 -11.512 1.00 18.60

ATOM 2781 N GLU B 228 4.167 36.877 -11.741 1.00 21.56

ATOM 2782 CA GLU B 228 3.182 37.907 -11.497 1.00 24.83

ATOM 2784 CB GLU B 228 1.849 37.564 -12.192 1.00 26.06

ATOM 2787 CG GLU B 228 1.926 37.375 -13.730 1.00 30.14

ATOM 2790 CD GLU B 228 2.158 38.676 -14.545 1.00 38.40

ATOM 2791 OEl GLU B 228 2.320 39.771 -13.950 1.00 41.88

ATOM 2792 OE2 GLU B 228 2.186 38.587 -15.807 1.00 36.33

ATOM 2793 C GLU B 228 2.931 38.146 -10.013 1.00 26.06

ATOM 2794 O GLU B 228 2.128 39.007 -9.652 1.00 28.35

ATOM 2796 N GLY B 229 3.605 37.427 -9.128 1.00 25.50

ATOM 2797 CA GLY B 229 3.515 37.820 -7.720 1.00 26.04

ATOM 2800 C GLY B 229 2.222 37.394 -7.034 1.00 25.56

ATOM 2801 O GLY B 229 1.426 36.659 -7.606 1.00 26.26

ATOM 2803 N GLY B 230 2.057 37.844 -5.791 1.00 24.96

ATOM 2804 CA GLY B 230 0.932 37.465 -4.935 1.00 24.12

ATOM 2807 C GLY B 230 1.051 36.117 -4.224 1.00 23.62

ATOM 2808 O GLY B 230 0.211 35.780 -3.383 1.00 22.79

ATOM 2810 N LYS B 231 2.070 35.334 -4.568 1.00 21.42

ATOM 2811 CA LYS B 231 2.170 33.975 -4.062 1.00 21.79

ATOM 2813 CB LYS B 231 1.546 32.996 -5.050 1.00 23.14

ATOM 2816 CG LYS B 231 0.027 33.051 -5.152 1.00 20.51

ATOM 2819 CD LYS B 231 0.462 31.946 -6.127 1.00 27.34

ATOM 2822 CE LYS B 231 1.575 32.420 -7.088 1.00 36.03

ATOM 2825 NZ LYS B 231 1.041 33.191 -8.285 1.00 39.12

ATOM 2829 C LYS B 231 3.631 33.606 -3.828 1.00 21.43

ATOM 2830 O LYS B 231 4.355 33.284 -4.765 1.00 19.60

ATOM 2832 N ASP B 232 4.053 33.674 -2.574 1.00 18.94

ATOM 2833 CA ASP B 232 5.416 33.357 -2.209 1.00 18.03

ATOM 2835 CB ASP B 232 6.428 34.366 -2.777 1.00 15.91

ATOM 2838 CG ASP B 232 7.654 33.650 -3.356 1.00 18.36

ATOM 2839 ODl ASP B 232 8.431 33.088 -2.560 1.00 19.25

ATOM 2840 OD2 ASP B 232 7.820 33.578 -4.596 1.00 20.56

ATOM 2841 C ASP B 232 5.599 33.225 -0.705 1.00 17.55

ATOM 2842 O ASP B 232 4.658 33.344 0.061 1.00 16.54

ATOM 2844 N ALA B 233 6.819 32.885 -0.321 1.00 18.74

ATOM 2845 CA ALA B 233 7.204 32.809 1.063 1.00 18.36

ATOM 2847 CB ALA B 233 8.508 32.033 1.166 1.00 18.60

ATOM 2851 C ALA B 233 7.396 34.244 1.605 1.00 18.88

ATOM 2852 O ALA B 233 7.761 35.156 0.854 1.00 17.95

ATOM 2854 N CYS B 234 7.195 34.425 2.908 1.00 18.82

ATOM 2855 CA CYS B 234 7.424 35.707 3.560 1.00 19.78

ATOM 2857 CB CYS B 234 6.120 36.370 3.959 1.00 21.28 ATOM 2860 SG CYS B 234 4.895 36.464 2.639 1.00 24.01

ATOM 2862 C CYS B 234 8.284 35.531 4.799 1.00 20.48

ATOM 2863 O CYS B 234 8.699 34.416 5.137 1.00 22.11

ATOM 2865 N GLN B 235 8.590 36.649 5.452 1.00 20.28

ATOM 2866 CA GLN B 235 9.398 36.636 6.657 1.00 20.22

ATOM 2868 CB GLN B 235 9.374 38.019 7.317 1.00 21.46

ATOM 2871 CG GLN B 235 10.212 38.134 8.598 1.00 23.77

ATOM 2874 CD GLN B 235 9.763 39.308 9.455 1.00 26.54

ATOM 2875 OEl GLN B 235 9.411 40.370 8.929 1.00 38.80

ATOM 2876 NE2 GLN B 235 9.758 39.121 10.777 1.00 37.39

ATOM 2879 C GLN B 235 8.901 35.578 7.643 1.00 18.76

ATOM 2880 O GLN B 235 7.730 35.535 7.999 1.00 18.89

ATOM 2882 N GLY B 236 9.814 34.719 8.079 1.00 17.75

ATOM 2883 CA GLY B 236 9.445 33.671 8.991 1.00 15.72

ATOM 2886 C GLY B 236 9.384 32.311 8.309 1.00 15.47

ATOM 2887 O GLY B 236 9.372 31.287 8.998 1.00 14.46

ATOM 2889 N ASP B 237 9.347 32.291 6.979 1.00 11.47

ATOM 2890 CA ASP B 237 9.349 31.019 6.225 1.00 13.25

ATOM 2892 CB ASP B 237 8.613 31.180 4.916 1.00 12.34

ATOM 2895 CG ASP B 237 7.099 31.374 5.110 1.00 10.46

ATOM 2896 ODl ASP B 237 6.542 30.752 6.064 1.00 14.60

ATOM 2897 OD2 ASP B 237 6.478 32.138 4.332 1.00 15.78

ATOM 2898 C ASP B 237 10.751 30.528 5.926 1.00 11.43

ATOM 2899 O ASP B 237 10.954 29.366 5.560 1.00 14.32

ATOM 2901 N SER B 238 11.728 31.433 5.981 1.00 13.43

ATOM 2902 CA SER B 238 13.044 31.062 5.581 1.00 12.33

ATOM 2904 CB SER B 238 13.989 32.281 5.552 1.00 14.49

ATOM 2907 OG SER B 238 14.174 32.753 6.833 1.00 17.18

ATOM 2909 C SER B 238 13.559 29.915 6.442 1.00 11.82

ATOM 2910 O SER B 238 13.103 29.697 7.573 1.00 12.85

ATOM 2912 N GLY B 239 14.446 29.143 5.848 1.00 10.18

ATOM 2913 CA GLY B 239 14.965 27.914 6.438 1.00 10.76

ATOM 2916 C GLY B 239 14.057 26.722 6.216 1.00 11.65

ATOM 2917 O GLY B 239 14.455 25.579 6.405 1.00 12.97

ATOM 2919 N GLY B 240 12.821 26.962 5.839 1.00 11.00

ATOM 2920 CA GLY B 240 11.885 25.866 5.673 1.00 10.59

ATOM 2923 C GLY B 240 12.012 25.147 4.331 1.00 11.00

ATOM 2924 O GLY B 240 12.776 25.584 3.453 1.00 12.39

ATOM 2926 N PRO B 241 11.232 24.057 4.164 1.00 10.43

ATOM 2927 CA PRO B 241 11.359 23.193 2.989 1.00 11.05

ATOM 2929 CB PRO B 241 10.683 21.915 3.441 1.00 10.17

ATOM 2932 CG PRO B 241 9.551 22.496 4.357 1.00 9.32

ATOM 2935 CD PRO B 241 10.254 23.511 5.135 1.00 11.28

ATOM 2938 C PRO B 241 10.647 23.625 1.722 1.00 11.08

ATOM 2939 O PRO B 241 9.521 24.188 1.754 1.00 10.73

ATOM 2940 N LEU B 242 11.309 23.315 0.610 1.00 9.78

ATOM 2941 CA LEU B 242 10.699 23.276 -0.678 1.00 11.19

ATOM 2943 CB LEU B 242 11.515 24.055 -1.691 1.00 9.97

ATOM 2946 CG LEU B 242 11.025 23.971 -3.144 1.00 11.81

ATOM 2948 CDl LEU B 242 9.707 24.698 -3.275 1.00 8.80

ATOM 2952 CD2 LEU B 242 12.042 24.537 -4.102 1.00 13.38

ATOM 2956 C LEU B 242 10.652 21.799 -0.996 1.00 11.27

ATOM 2957 O LEU B 242 11.697 21.142 -1.228 1.00 9.93

ATOM 2959 N SER B 243 9.459 21.234 -0.931 1.00 11.20

ATOM 2960 CA SER B 243 9.302 19.795 -1.043 1.00 10.09

ATOM 2962 CB SER B 243 8.290 19.299 0.006 1.00 10.79

ATOM 2965 OG SER B 243 8.581 19.687 1.360 1.00 9.54

ATOM 2967 C SER B 243 8.795 19.511 -2.450 1.00 10.16

ATOM 2968 O SER B 243 7.746 20.037 -2.847 1.00 9.57

ATOM 2970 N CYS B 244 9.539 18.693 -3.201 1.00 10.54

ATOM 2971 CA CYS B 244 9.186 18.374 -4.596 1.00 11.64 ATOM 2973 CB CYS B 244 10.366 18.644 -5.524 1.00 12.71

ATOM 2976 SG CYS B 244 10.831 20.376 -5.695 1.00 11.93

ATOM 2978 C CYS B 244 8.821 16.912 -4.763 1.00 11.91

ATOM 2979 O CYS B 244 9.481 16.035 -4.193 1.00 11.68

ATOM 2981 N PRO B 245 7.797 16.638 -5.577 1.00 11.87

ATOM 2982 CA PRO B 245 7.317 15.284 -5.768 1.00 13.60

ATOM 2984 CB PRO B 245 5.906 15.493 -6.278 1.00 13.76

ATOM 2987 CG PRO B 245 5.962 16.809 -7.006 1.00 13.73

ATOM 2990 CD PRO B 245 6.945 17.636 -6.244 1.00 11.29

ATOM 2993 C PRO B 245 8.143 14.586 -6.842 1.00 13.61

ATOM 2994 O PRO B 245 8.285 15.118 -7.948 1.00 15.79

ATOM 2995 N VAL B 246 8.657 13.419 -6.538 1.00 15.19

ATOM 2996 CA VAL B 246 9.376 12.653 -7.552 1.00 16.58

ATOM 2998 CB VAL B 246 10.888 12.862 -7.489 1.00 19.49

ATOM 3000 CGl VAL B 246 11.590 12.030 -8.598 1.00 23.50

ATOM 3004 CG2 VAL B 246 11.239 14.334 -7.635 1.00 22.84

ATOM 3008 C VAL B 246 9.104 11.173 -7.299 1.00 15.61

ATOM 3009 O VAL B 246 9.285 10.702 -6.214 1.00 14.50

ATOM 3011 N GLU B 247 8.592 10.484 -8.302 1.00 16.00

ATOM 3012 CA GLU B 247 8.433 9.035 -8.214 1.00 17.08

ATOM 3014 CB GLU B 247 9.793 8.355 -8.080 1.00 19.50

ATOM 3017 CG GLU B 247 10.738 8.637 -9.210 1.00 27.71

ATOM 3020 CD GLU B 247 10.557 7.663 -10.323 1.00 36.77

ATOM 3021 OEl GLU B 247 9.724 7.933 -11.230 1.00 43.82

ATOM 3022 OE2 GLU B 247 11.224 6.609 -10.250 1.00 45.14

ATOM 3023 C GLU B 247 7.578 8.645 -7.042 1.00 14.95

ATOM 3024 O GLU B 247 7.868 7.664 -6.376 1.00 17.13

ATOM 3026 N GLY B 248 6.527 9.425 -6.786 1.00 13.54

ATOM 3027 CA GLY B 248 5.595 9.133 -5.703 1.00 14.02

ATOM 3030 C GLY B 248 6.045 9.537 -4.333 1.00 14.32

ATOM 3031 O GLY B 248 5.296 9.399 -3.356 1.00 13.63

ATOM 3033 N LEU B 249 7.266 10.068 -4.244 1.00 12.70

ATOM 3034 CA LEU B 249 7.851 10.455 -2.964 1.00 12.93

ATOM 3036 CB LEU B 249 9.252 9.847 -2.783 1.00 15.81

ATOM 3039 CG LEU B 249 9.326 8.333 -2.867 1.00 19.26

ATOM 3041 CDl LEU B 249 10.766 7.908 -2.681 1.00 23.24

ATOM 3045 CD2 LEU B 249 8.435 7.675 -1.861 1.00 21.54

ATOM 3049 C LEU B 249 7.967 11.986 -2.955 1.00 12.10

ATOM 3050 O LEU B 249 7.578 12.634 -3.913 1.00 11.23

ATOM 3052 N TRP B 250 8.404 12.532 -1.821 1.00 10.74

ATOM 3053 CA TRP B 250 8.752 13.953 -1.687 1.00 13.07

ATOM 3055 CB TRP B 250 7.866 14.628 -0.619 1.00 13.71

ATOM 3058 CG TRP B 250 6.442 14.569 -1.008 1.00 13.23

ATOM 3059 CDl TRP B 250 5.586 13.536 -0.806 1.00 14.22

ATOM 3061 NEl TRP B 250 4.360 13.827 -1.356 1.00 13.56

ATOM 3063 CE2 TRP B 250 4.421 15.059 -1.955 1.00 12.47

ATOM 3064 CD2 TRP B 250 5.739 15.537 -1.784 1.00 10.89

ATOM 3065 CE3 TRP B 250 6.076 16.788 -2.311 1.00 13.92

ATOM 3067 CZ3 TRP B 250 5.085 17.518 -3.007 1.00 12.09

ATOM 3069 CH2 TRP B 250 3.802 16.980 -3.196 1.00 12.33

ATOM 3071 CZ2 TRP B 250 3.450 15.770 -2.664 1.00 13.19

ATOM 3073 C TRP B 250 10.213 14.048 -1.309 1.00 11.36

ATOM 3074 O TRP B 250 10.691 13.301 -0.453 1.00 10.92

ATOM 3076 N TYR B 251 10.915 14.988 -1.937 1.00 11.85

ATOM 3077 CA TYR B 251 12.312 15.255 -1.640 1.00 12.11

ATOM 3079 CB TYR B 251 13.166 15.016 -2.871 1.00 14.35

ATOM 3082 CG TYR B 251 13.349 13.568 -3.135 1.00 18.44

ATOM 3083 CDl TYR B 251 14.427 12.892 -2.637 1.00 18.96

ATOM 3085 CEl TYR B 251 14.572 11.521 -2.865 1.00 21.28

ATOM 3087 CZ TYR B 251 13.617 10.855 -3.604 1.00 22.50

ATOM 3088 OH TYR B 251 13.771 9.520 -3.859 1.00 29.42 ATOM 3090 CE2 TYR B 251 12.530 11.510 -4.126 1.00 24.59

ATOM 3092 CD2 TYR B 251 12.390 12.862 -3.887 1.00 22.49

ATOM 3094 C TYR B 251 12.495 16.684 -1.233 1.00 10.80

ATOM 3095 O TYR B 251 11.773 17.572 -1.684 1.00 11.86

ATOM 3097 N LEU B 252 13.467 16.914 -0.374 1.00 9.05

ATOM 3098 CA LEU B 252 13.831 18.269 -0.006 1.00 8.91

ATOM 3100 CB LEU B 252 14.579 18.275 1.303 1.00 8.94

ATOM 3103 CG LEU B 252 14.863 19.635 1.904 1.00 8.47

ATOM 3105 CDl LEU B 252 13.567 20.378 2.313 1.00 10.20

ATOM 3109 CD2 LEU B 252 15.785 19.506 3.084 1.00 12.33

ATOM 3113 C LEU B 252 14.683 18.880 -1.101 1.00 10.33

ATOM 3114 O LEU B 252 15.904 18.664 -1.170 1.00 11.55

ATOM 3116 N THR B 253 14.025 19.589 -2.006 1.00 9.25

ATOM 3117 CA THR B 253 14.728 20.168 -3.104 1.00 10.92

ATOM 3119 CB THR B 253 13.790 20.497 -4.219 1.00 10.76

ATOM 3121 OGl THR B 253 13.229 19.292 -4.729 1.00 13.35

ATOM 3123 CG2 THR B 253 14.529 21.218 -5.332 1.00 12.09

ATOM 3127 C THR B 253 15.458 21.403 -2.650 1.00 10.13

ATOM 3128 O THR B 253 16.539 21.704 -3.119 1.00 9.38

ATOM 3130 N GLY B 254 14.787 22.170 -1.783 1.00 10.14

ATOM 3131 CA GLY B 254 15.280 23.499 -1.427 1.00 10.62

ATOM 3134 C GLY B 254 15.017 23.866 0.013 1.00 8.96

ATOM 3135 O GLY B 254 14.184 23.269 0.691 1.00 10.03

ATOM 3137 N ILE B 255 15.835 24.786 0.493 1.00 11.65

ATOM 3138 CA ILE B 255 15.707 25.386 1.813 1.00 11.56

ATOM 3140 CB ILE B 255 17.006 25.175 2.602 1.00 12.51

ATOM 3142 CGl ILE B 255 17.148 23.682 2.902 1.00 13.03

ATOM 3145 CDl ILE B 255 18.442 23.247 3.340 1.00 16.52

ATOM 3149 CG2 ILE B 255 17.012 26.003 3.890 1.00 14.65

ATOM 3153 C ILE B 255 15.505 26.878 1.557 1.00 11.27

ATOM 3154 O ILE B 255 16.318 27.487 0.862 1.00 10.34

ATOM 3156 N VAL B 256 14.435 27.449 2.080 1.00 10.98

ATOM 3157 CA VAL B 256 14.108 28.853 1.755 1.00 11.62

ATOM 3159 CB VAL B 256 12.779 29.347 2.425 1.00 12.55

ATOM 3161 CGl VAL B 256 12.512 30.792 2.091 1.00 11.51

ATOM 3165 CG2 VAL B 256 11.555 28.471 2.043 1.00 13.15

ATOM 3169 C VAL B 256 15.276 29.708 2.182 1.00 12.86

ATOM 3170 O VAL B 256 15.665 29.664 3.345 1.00 13.03

ATOM 3172 N SER B 257 15.827 30.479 1.253 1.00 13.02

ATOM 3173 CA SER B 257 16.979 31.330 1.519 1.00 15.31

ATOM 3175 CB SER B 257 18.097 31.114 0.514 1.00 15.29

ATOM 3178 OG SER B 257 19.218 31.944 0.829 1.00 15.78

ATOM 3180 C SER B 257 16.599 32.795 1.510 1.00 18.64

ATOM 3181 O SER B 257 16.858 33.502 2.476 1.00 19.08

ATOM 3183 N TRP B 258 16.012 33.266 0.411 1.00 20.11

ATOM 3184 CA TRP B 258 15.442 34.635 0.402 1.00 22.29

ATOM 3186 CB TRP B 258 15.872 35.508 -0.769 1.00 24.59

ATOM 3189 CG TRP B 258 17.302 35.335 -1.231 1.00 29.56

ATOM 3190 CDl TRP B 258 18.342 34.721 -0.575 1.00 31.59

ATOM 3192 NEl TRP B 258 19.480 34.771 -1.344 1.00 32.67

ATOM 3194 CE2 TRP B 258 19.190 35.442 -2.503 1.00 26.77

ATOM 3195 CD2 TRP B 258 17.834 35.816 -2.454 1.00 30.89

ATOM 3196 CE3 TRP B 258 17.286 36.514 -3.526 1.00 32.59

ATOM 3198 CZ3 TRP B 258 18.073 36.817 -4.573 1.00 30.93

ATOM 3200 CH2 TRP B 258 19.411 36.422 -4.606 1.00 30.92

ATOM 3202 CZ2 TRP B 258 19.991 35.743 -3.572 1.00 29.25

ATOM 3204 C TRP B 258 13.947 34.436 0.398 1.00 24.25

ATOM 3205 O TRP B 258 13.326 34.074 -0.624 1.00 23.46

ATOM 3207 N GLY B 259 13.398 34.648 1.584 1.00 25.14

ATOM 3208 CA GLY B 259 12.036 34.269 1.890 1.00 26.85

ATOM 3211 C GLY B 259 11.231 35.473 2.325 1.00 27.51 ATOM 3212 O GLY B 259 10.272 35.314 3.073 1.00 24.96

ATOM 3214 N ASP B 260 11.637 36.663 1.876 1.00 27.92

ATOM 3215 CA ASP B 260 10.942 37.906 2.205 1.00 30.36

ATOM 3217 CB ASP B 260 11.907 38.880 2.891 1.00 31.15

ATOM 3220 CG ASP B 260 12.448 38.333 4.199 1.00 37.45

ATOM 3221 ODl ASP B 260 11.914 37.307 4.687 1.00 44.38

ATOM 3222 OD2 ASP B 260 13.420 38.904 4.736 1.00 45.72

ATOM 3223 C ASP B 260 10.344 38.556 0.963 1.00 31.16

ATOM 3224 O ASP B 260 9.924 39.699 1.014 1.00 31.80

ATOM 3226 N ALA B 261 10.276 37.825 -0.146 1.00 30.41

ATOM 3227 CA ALA B 261 9.742 38.416 -1.380 1.00 29.80

ATOM 3229 CB ALA B 261 9.854 37.424 -2.529 1.00 29.37

ATOM 3233 C ALA B 261 8.287 38.793 -1.121 1.00 28.47

ATOM 3234 O ALA B 261 7.802 39.882 -1.485 1.00 28.56

ATOM 3236 N CYS B 262 7.599 37.843 -0.496 1.00 26.76

ATOM 3237 CA CYS B 262 6.252 38.016 -0.004 1.00 25.77

ATOM 3239 CB CYS B 262 6.238 38.853 1.264 1.00 24.47

ATOM 3242 SG CYS B 262 4.784 38.469 2.232 1.00 24.85

ATOM 3244 C CYS B 262 5.305 38.570 -1.034 1.00 23.74

ATOM 3245 O CYS B 262 4.516 39.465 -0.755 1.00 25.38

ATOM 3247 N GLY B 263 5.366 37.989 -2.220 1.00 21.74

ATOM 3248 CA GLY B 263 4.349 38.210 -3.232 1.00 22.02

ATOM 3251 C GLY B 263 4.609 39.337 -4.193 1.00 21.38

ATOM 3252 O GLY B 263 3.782 39.594 -5.049 1.00 23.81

ATOM 3254 N ALA B 264 5.752 39.991 -4.069 1.00 21.15

ATOM 3255 CA ALA B 264 6.155 41.008 -5.031 1.00 21.98

ATOM 3257 CB ALA B 264 7.464 41.635 -4.591 1.00 21.67

ATOM 3261 C ALA B 264 6.314 40.365 -6.404 1.00 21.98

ATOM 3262 O ALA B 264 6.840 39.238 -6.523 1.00 21.20

ATOM 3264 N ARG B 265 5.880 41.072 -7.448 1.00 20.59

ATOM 3265 CA ARG B 265 6.090 40.601 -8.825 1.00 22.48

ATOM 3267 CB ARG B 265 5.482 41.585 -9.831 1.00 23.31

ATOM 3270 CG ARG B 265 4.005 41.762 -9.710 1.00 31.61

ATOM 3273 CD ARG B 265 3.381 42.422 -10.961 1.00 34.00

ATOM 3276 NE ARG B 265 2.247 41.600 -11.422 1.00 48.13

ATOM 3278 CZ ARG B 265 1.058 41.511 -10.812 1.00 48.34

ATOM 3279 NHl ARG B 265 0.118 40.721 -11.324 1.00 48.23

ATOM 3282 NH2 ARG B 265 0.797 42.198 -9.698 1.00 51.80

ATOM 3285 C ARG B 265 7.554 40.536 -9.142 1.00 19.37

ATOM 3286 O ARG B 265 8.347 41.328 -8.634 1.00 17.55

ATOM 3288 N ASN B 266 7.926 39.625 -10.042 1.00 17.12

ATOM 3289 CA ASN B 266 9.322 39.491 -10.436 1.00 17.82

ATOM 3291 CB ASN B 266 9.788 40.738 -11.189 1.00 17.86

ATOM 3294 CG ASN B 266 8.924 41.012 -12.375 1.00 13.31

ATOM 3295 ODl ASN B 266 8.471 40.062 -13.034 1.00 15.81

ATOM 3296 ND2 ASN B 266 8.657 42.295 -12.661 1.00 19.00

ATOM 3299 C ASN B 266 10.309 39.182 -9.317 1.00 17.38

ATOM 3300 O ASN B 266 11.481 39.470 -9.435 1.00 18.89

ATOM 3302 N ARG B 267 9.818 38.596 -8.241 1.00 17.37

ATOM 3303 CA ARG B 267 10.637 38.298 -7.093 1.00 17.87

ATOM 3305 CB ARG B 267 10.436 39.377 -6.040 1.00 18.59

ATOM 3308 CG ARG B 267 10.756 40.780 -6.507 1.00 21.66

ATOM 3311 CD ARG B 267 12.247 40.977 -6.647 1.00 22.39

ATOM 3314 NE ARG B 267 12.581 42.378 -6.922 1.00 24.16

ATOM 3316 CZ ARG B 267 12.702 42.916 -8.130 1.00 24.15

ATOM 3317 NHl ARG B 267 12.513 42.202 -9.231 1.00 18.43

ATOM 3320 NH2 ARG B 267 13.020 44.200 -8.234 1.00 27.17

ATOM 3323 C ARG B 267 10.242 36.915 -6.523 1.00 16.91

ATOM 3324 O ARG B 267 9.783 36.810 -5.399 1.00 17.82

ATOM 3326 N PRO B 268 10.464 35.846 -7.297 1.00 16.90

ATOM 3327 CA PRO B 268 10.115 34.523 -6.794 1.00 16.59 ATOM 3329 CB PRO B 268 10.311 33.616 -8.001 1.00 16.43

ATOM 3332 CG PRO B 268 11.094 34.372 -8.973 1.00 16.78

ATOM 3335 CD PRO B 268 11.034 35.800 -8.644 1.00 16.90

ATOM 3338 C PRO B 268 11.044 34.116 -5.647 1.00 15.02

ATOM 3339 O PRO B 268 12.196 34.577 -5.571 1.00 14.61

ATOM 3340 N GLY B 269 10.541 33.261 -4.767 1.00 14.17

ATOM 3341 CA GLY B 269 11.356 32.787 -3.667 1.00 14.89

ATOM 3344 C GLY B 269 12.640 32.161 -4.170 1.00 13.81

ATOM 3345 O GLY B 269 12.666 31.575 -5.251 1.00 12.49

ATOM 3347 N VAL B 270 13.699 32.305 -3.389 1.00 13.71

ATOM 3348 CA VAL B 270 15.028 31.757 -3.694 1.00 12.65

ATOM 3350 CB VAL B 270 16.152 32.830 -3.686 1.00 13.89

ATOM 3352 CGl VAL B 270 17.511 32.236 -4.081 1.00 16.01

ATOM 3356 CG2 VAL B 270 15.758 33.982 -4.646 1.00 16.79

ATOM 3360 C VAL B 270 15.377 30.748 -2.630 1.00 12.87

ATOM 3361 O VAL B 270 15.227 31.014 -1.449 1.00 12.90

ATOM 3363 N TYR B 271 15.901 29.624 -3.076 1.00 11.34

ATOM 3364 CA TYR B 271 16.105 28.487 -2.229 1.00 10.95

ATOM 3366 CB TYR B 271 15.129 27.372 -2.620 1.00 10.64

ATOM 3369 CG TYR B 271 13.680 27.744 -2.473 1.00 9.27

ATOM 3370 CDl TYR B 271 12.959 27.337 -1.356 1.00 11.46

ATOM 3372 CEl TYR B 271 11.651 27.656 -1.210 1.00 10.39

ATOM 3374 CZ TYR B 271 11.030 28.421 -2.173 1.00 9.60

ATOM 3375 OH TYR B 271 9.715 28.765 -2.048 1.00 12.11

ATOM 3377 CE2 TYR B 271 11.706 28.825 -3.302 1.00 11.94

ATOM 3379 CD2 TYR B 271 13.031 28.484 -3.442 1.00 10.22

ATOM 3381 C TYR B 271 17.488 27.948 -2.425 1.00 10.67

ATOM 3382 O TYR B 271 17.968 27.870 -3.556 1.00 11.19

ATOM 3384 N THR B 272 18.110 27.551 -1.322 1.00 8.96

ATOM 3385 CA THR B 272 19.317 26.766 -1.391 1.00 9.89

ATOM 3387 CB THR B 272 20.038 26.754 -0.059 1.00 12.04

ATOM 3389 OGl THR B 272 20.374 28.101 0.289 1.00 11.19

ATOM 3391 CG2 THR B 272 21.305 25.900 -0.143 1.00 12.42

ATOM 3395 C THR B 272 18.976 25.355 -1.820 1.00 9.96

ATOM 3396 O THR B 272 18.102 24.744 -1.239 1.00 10.14

ATOM 3398 N LEU B 273 19.696 24.854 -2.819 1.00 11.54

ATOM 3399 CA LEU B 273 19.515 23.500 -3.301 1.00 10.32

ATOM 3401 CB LEU B 273 20.184 23.349 -4.663 1.00 11.25

ATOM 3404 CG LEU B 273 19.405 23.893 -5.857 1.00 11.89

ATOM 3406 CDl LEU B 273 20.311 24.000 -7.052 1.00 13.23

ATOM 3410 CD2 LEU B 273 18.230 22.984 -6.188 1.00 14.78

ATOM 3414 C LEU B 273 20.132 22.527 -2.337 1.00 10.52

ATOM 3415 O LEU B 273 21.300 22.595 -2.042 1.00 11.31

ATOM 3417 N ALA B 274 19.329 21.611 -1.828 1.00 10.88

ATOM 3418 CA ALA B 274 19.869 20.582 -0.945 1.00 10.77

ATOM 3420 CB ALA B 274 18.737 19.737 -0.324 1.00 10.39

ATOM 3424 C ALA B 274 20.847 19.674 -1.674 1.00 11.20

ATOM 3425 O ALA B 274 21.799 19.164 -1.067 1.00 11.41

ATOM 3427 N SER B 275 20.625 19.477 -2.978 1.00 10.37

ATOM 3428 CA SER B 275 21.530 18.644 -3.781 1.00 10.13

ATOM 3430 CB SER B 275 21.067 18.566 -5.219 1.00 10.88

ATOM 3433 OG SER B 275 20.899 19.878 -5.763 1.00 11.99

ATOM 3435 C SER B 275 22.949 19.189 -3.723 1.00 9.78

ATOM 3436 O SER B 275 23.913 18.402 -3.712 1.00 13.12

ATOM 3438 N SER B 276 23.086 20.516 -3.739 1.00 10.29

ATOM 3439 CA SER B 276 24.404 21.167 -3.662 1.00 10.41

ATOM 3441 CB SER B 276 24.267 22.659 -3.780 1.00 12.56

ATOM 3444 OG SER B 276 23.921 23.012 -5.110 1.00 13.44

ATOM 3446 C SER B 276 25.172 20.846 -2.391 1.00 12.06

ATOM 3447 O SER B 276 26.407 20.959 -2.371 1.00 14.04

ATOM 3449 N TYR B 277 24.455 20.417 -1.360 1.00 11.18 ATOM 3450 CA TYR B 277 25.044 20.084 -0.048 1.00 11.74

ATOM 3452 CB TYR B 277 24.496 21.069 1.014 1.00 13.20

ATOM 3455 CG TYR B 277 24.885 22.436 0.600 1.00 11.93

ATOM 3456 CDl TYR B 277 26.167 22.911 0.872 1.00 17.47

ATOM 3458 CEl TYR B 277 26.599 24.109 0.394 1.00 15.85

ATOM 3460 CZ TYR B 277 25.747 24.891 -0.358 1.00 17.05

ATOM 3461 OH TYR B 277 26.167 26.111 -0.853 1.00 14.91

ATOM 3463 CE2 TYR B 277 24.487 24.446 -0.660 1.00 12.48

ATOM 3465 CD2 TYR B 277 24.054 23.218 -0.195 1.00 13.36

ATOM 3467 C TYR B 277 24.864 18.624 0.371 1.00 12.78

ATOM 3468 O TYR B 277 25.171 18.300 1.522 1.00 12.12

ATOM 3470 N ALA B 278 24.366 17.762 -0.523 1.00 13.19

ATOM 3471 CA ALA B 278 24.174 16.345 -0.217 1.00 14.10

ATOM 3473 CB ALA B 278 23.759 15.591 -1.484 1.00 14.69

ATOM 3477 C ALA B 278 25.468 15.752 0.355 1.00 14.44

ATOM 3478 O ALA B 278 25.507 15.107 1.412 1.00 14.17

ATOM 3480 N SER B 279 26.555 16.023 -0.333 1.00 14.21

ATOM 3481 CA SER B 279 27.838 15.406 0.041 1.00 14.27

ATOM 3483 CB SER B 279 28.886 15.741 -1.005 1.00 15.73

ATOM 3486 OG SER B 279 30.160 15.365 -0.548 1.00 14.15

ATOM 3488 C SER B 279 28.304 15.873 1.419 1.00 13.60

ATOM 3489 O SER B 279 28.705 15.047 2.242 1.00 14.89

ATOM 3491 N TRP B 280 28.176 17.182 1.661 1.00 12.76

ATOM 3492 CA TRP B 280 28.574 17.828 2.922 1.00 13.42

ATOM 3494 CB TRP B 280 28.439 19.324 2.813 1.00 14.80

ATOM 3497 CG TRP B 280 28.763 20.096 4.045 1.00 14.43

ATOM 3498 CDl TRP B 280 30.002 20.383 4.524 1.00 16.77

ATOM 3500 NEl TRP B 280 29.901 21.117 5.688 1.00 19.00

ATOM 3502 CE2 TRP B 280 28.576 21.354 5.946 1.00 17.40

ATOM 3503 CD2 TRP B 280 27.831 20.717 4.933 1.00 15.90

ATOM 3504 CE3 TRP B 280 26.433 20.835 4.950 1.00 17.15

ATOM 3506 CZ3 TRP B 280 25.832 21.568 5.983 1.00 18.34

ATOM 3508 CH2 TRP B 280 26.597 22.179 6.969 1.00 16.67

ATOM 3510 CZ2 TRP B 280 27.973 22.081 6.971 1.00 20.30

ATOM 3512 C TRP B 280 27.702 17.331 4.059 1.00 12.73

ATOM 3513 O TRP B 280 28.195 16.951 5.131 1.00 11.39

ATOM 3515 N ILE B 281 26.388 17.306 3.825 1.00 13.86

ATOM 3516 CA ILE B 281 25.469 16.843 4.852 1.00 12.62

ATOM 3518 CB ILE B 281 24.004 16.911 4.379 1.00 14.90

ATOM 3520 CGl ILE B 281 23.569 18.362 4.233 1.00 11.62

ATOM 3523 CDl ILE B 281 22.371 18.504 3.411 1.00 11.94

ATOM 3527 CG2 ILE B 281 23.081 16.208 5.347 1.00 13.68

ATOM 3531 C ILE B 281 25.798 15.406 5.198 1.00 12.37

ATOM 3532 O ILE B 281 25.870 15.055 6.383 1.00 13.16

ATOM 3534 N GLN B 282 25.980 14.569 4.177 1.00 12.71

ATOM 3535 CA GLN B 282 26.339 13.152 4.440 1.00 13.36

ATOM 3537 CB GLN B 282 26.411 12.310 3.175 1.00 12.66

ATOM 3540 CG GLN B 282 26.547 10.805 3.503 1.00 15.08

ATOM 3543 CD GLN B 282 26.540 9.923 2.270 1.00 18.26

ATOM 3544 OEl GLN B 282 26.974 8.757 2.311 1.00 19.88

ATOM 3545 NE2 GLN B 282 26.074 10.470 1.163 1.00 17.77

ATOM 3548 C GLN B 282 27.645 13.038 5.200 1.00 11.92

ATOM 3549 O GLN B 282 27.763 12.264 6.126 1.00 11.30

ATOM 3551 N SER B 283 28.624 13.853 4.837 1.00 12.19

ATOM 3552 CA SER B 283 29.915 13.766 5.498 1.00 12.14

ATOM 3554 CB SER B 283 30.936 14.663 4.803 1.00 11.71

ATOM 3557 OG SER B 283 32.089 14.716 5.608 1.00 12.50

ATOM 3559 C SER B 283 29.797 14.163 6.965 1.00 12.46

ATOM 3560 O SER B 283 30.278 13.481 7.855 1.00 13.32

ATOM 3562 N LYS B 284 29.119 15.276 7.227 1.00 11.58

ATOM 3563 CA LYS B 284 29.038 15.808 8.607 1.00 12.43 ATOM 3565 CB LYS B 284 28.386 17.187 8.608 1.00 12.92

ATOM 3568 CG LYS B 284 29.130 18.271 7.885 1.00 13.38

ATOM 3571 CD LYS B 284 30.478 18.646 8.577 1.00 17.96

ATOM 3574 CE LYS B 284 30.326 19.105 9.990 1.00 18.19

ATOM 3577 NZ LYS B 284 31.664 19.661 10.477 1.00 20.19

ATOM 3581 C LYS B 284 28.240 14.885 9.504 1.00 12.97

ATOM 3582 O LYS B 284 28.667 14.581 10.640 1.00 13.94

ATOM 3584 N VAL B 285 27.103 14.413 9.006 1.00 12.70

ATOM 3585 CA VAL B 285 26.257 13.531 9.846 1.00 13.90

ATOM 3587 CB VAL B 285 24.848 13.390 9.299 1.00 16.02

ATOM 3589 CGl VAL B 285 24.015 12.484 10.207 1.00 16.77

ATOM 3593 CG2 VAL B 285 24.187 14.794 9.227 1.00 15.42

ATOM 3597 C VAL B 285 26.910 12.168 10.054 1.00 14.53

ATOM 3598 O VAL B 285 26.903 11.630 11.159 1.00 14.87

ATOM 3600 N THR B 286 27.584 11.652 9.031 1.00 13.93

ATOM 3601 CA THR B 286 28.237 10.352 9.162 1.00 12.69

ATOM 3603 CB THR B 286 28.741 9.847 7.819 1.00 11.94

ATOM 3605 OGl THR B 286 27.619 9.702 6.928 1.00 10.00

ATOM 3607 CG2 THR B 286 29.399 8.457 7.938 1.00 14.36

ATOM 3611 C THR B 286 29.376 10.418 10.169 1.00 13.11

ATOM 3612 O THR B 286 29.568 9.514 10.985 1.00 15.63

ATOM 3614 N GLU B 287 30.149 11.487 10.094 1.00 14.25

ATOM 3615 CA GLU B 287 31.265 11.638 10.982 1.00 14.86

ATOM 3617 CB GLU B 287 32.110 12.836 10.600 1.00 14.97

ATOM 3620 CG GLU B 287 33.312 12.859 11.457 1.00 15.91

ATOM 3623 CD GLU B 287 34.269 13.964 11.123 1.00 18.50

ATOM 3624 OEl GLU B 287 33.902 14.898 10.370 1.00 22.20

ATOM 3625 OE2 GLU B 287 35.396 13.903 11.661 1.00 24.37

ATOM 3626 C GLU B 287 30.798 11.862 12.388 1.00 15.90

ATOM 3627 O GLU B 287 31.320 11.283 13.329 1.00 15.71

ATOM 3629 N LEU B 288 29.824 12.746 12.542 1.00 14.46

ATOM 3630 CA LEU B 288 29.403 13.191 13.889 1.00 15.36

ATOM 3632 CB LEU B 288 28.789 14.564 13.822 1.00 14.18

ATOM 3635 CG LEU B 288 29.789 15.627 13.426 1.00 17.42

ATOM 3637 CDl LEU B 288 29.099 16.981 13.292 1.00 18.04

ATOM 3641 CD2 LEU B 288 30.911 15.699 14.446 1.00 21.15

ATOM 3645 C LEU B 288 28.413 12.278 14.563 1.00 16.28

ATOM 3646 O LEU B 288 28.344 12.225 15.807 1.00 17.94

ATOM 3648 N GLN B 289 27.611 11.579 13.785 1.00 17.82

ATOM 3649 CA GLN B 289 26.644 10.692 14.392 1.00 19.25

ATOM 3651 CB GLN B 289 25.394 11.472 14.805 1.00 19.34

ATOM 3654 CG GLN B 289 24.468 10.599 15.656 1.00 19.71

ATOM 3657 CD GLN B 289 23.340 11.365 16.331 1.00 22.77

ATOM 3658 OEl GLN B 289 23.007 12.496 15.963 1.00 24.96

ATOM 3659 NE2 GLN B 289 22.744 10.736 17.339 1.00 30.39

ATOM 3662 C GLN B 289 26.312 9.552 13.453 1.00 19.52

ATOM 3663 O GLN B 289 25.221 9.500 12.920 1.00 17.23

ATOM 3665 N PRO B 290 27.266 8.617 13.245 1.00 19.84

ATOM 3666 CA PRO B 290 26.998 7.531 12.312 1.00 22.37

ATOM 3668 CB PRO B 290 28.305 6.716 12.306 1.00 22.87

ATOM 3671 CG PRO B 290 28.951 7.039 13.604 1.00 21.30

ATOM 3674 CD PRO B 290 28.594 8.494 13.867 1.00 21.45

ATOM 3677 C PRO B 290 25.890 6.643 12.818 1.00 23.80

ATOM 3678 O PRO B 290 25.694 6.567 14.035 1.00 22.71

ATOM 3679 N ARG B 291 25.217 5.956 11.895 1.00 26.70

ATOM 3680 CA ARG B 291 24.232 4.936 12.246 1.00 29.62

ATOM 3682 CB ARG B 291 23.251 4.676 11.090 1.00 31.94

ATOM 3685 CG ARG B 291 22.769 5.952 10.383 1.00 35.69

ATOM 3688 CD ARG B 291 21.640 5.725 9.365 1.00 37.61

ATOM 3691 NE ARG B 291 21.430 6.935 8.543 1.00 44.92

ATOM 3693 CZ ARG B 291 20.379 7.160 7.744 1.00 50.44 ATOM 3694 NHl ARG B 291 19.400 6.255 7.637 1.00 53.11

ATOM 3697 NH2 ARG B 291 20.297 8.303 7.049 1.00 50.82

ATOM 3700 C ARG B 291 24.987 3.661 12.591 1.00 30.19

ATOM 3701 O ARG B 291 24.805 3.123 13.680 1.00 33.30

ATOM 3703 03 GOL G 1 30.683 13.201 -2.123 1.00 24.51

ATOM 3705 C3 GOL G 1 30.388 11.863 -1.690 1.00 26.57

ATOM 3708 C2 GOL G 1 28.950 11.449 -1.893 1.00 32.36

ATOM 3710 02 GOL G 1 28.313 12.306 -2.809 1.00 35.74

ATOM 3712 Cl GOL G 1 28.097 11.429 -0.653 1.00 34.06

ATOM 3715 Ol GOL G 1 27.133 10.428 -0.900 1.00 36.17

ATOM 3717 03 GOL G 2 37.879 17.496 -2.730 1.00 39.09

ATOM 3719 C3 GOL G 36.779 16.771 -3.232 1.00 38.69

ATOM 3722 C2 GOL G 36.306 15.781 -2.191 1.00 31.70

ATOM 3724 02 GOL G 37.391 14.975 -1.775 1.00 16.33

ATOM 3726 Cl GOL G 2 35.830 16.610 -1.005 1.00 31.37

ATOM 3729 Ol GOL G 2 34.697 15.967 -0.509 1.00 24.03

ATOM 3731 03 GOL G 3 -0.974 26.733 -3.325 1.00 27.14

ATOM 3733 C3 GOL G 3 -1.069 25.441 -2.841 1.00 34.20

ATOM 3736 C2 GOL G 3 -2.488 25.306 -2.399 1.00 42.72

ATOM 3738 02 GOL G 3 -2.652 26.257 -1.370 1.00 44.44

ATOM 3740 Cl GOL G 3 -2.709 23.860 -1.976 1.00 46.95

ATOM 3743 Ol GOL G 3 -1.461 23.300 -1.622 1.00 51.05

ATOM 3745 OH2 HOH W 1 9.166 27.500 6.690 1.00 10.78

ATOM 3748 OH2 HOH W 2 18.680 19.705 -7.287 1.00 13.95

ATOM 3751 OH2 HOH W 3 7.274 22.028 1.976 1.00 12.47

ATOM 3754 OH2 HOH W 4 31.650 7.863 11.593 1.00 13.87

ATOM 3757 OH2 HOH W 5 8.132 28.762 8.929 1.00 10.96

ATOM 3760 OH2 HOH W 6 13.331 29.483 21.888 1.00 12.76

ATOM 3763 OH2 HOH W 7 18.168 19.803 -4.456 1.00 12.14

ATOM 3766 OH2 HOH W 8 15.218 21.840 -15.773 1.00 17.70

ATOM 3769 OH2 HOH W 9 2.724 31.251 6.677 1.00 11.96

ATOM 3772 OH2 HOH W 10 14.629 23.032 5.497 1.00 13.77

ATOM 3775 OH2 HOH W 11 14.315 25.893 26.129 1.00 14.05

ATOM 3778 OH2 HOH W 12 22.736 29.104 -0.538 1.00 14.77

ATOM 3781 OH2 HOH W 13 28.133 19.179 -0.667 1.00 15.24

ATOM 3784 OH2 HOH W 14 18.885 25.102 22.043 1.00 15.95

ATOM 3787 OH2 HOH W 15 32.444 15.439 8.321 1.00 14.30

ATOM 3790 OH2 HOH W 16 3.860 20.181 -4.681 1.00 12.50

ATOM 3793 OH2 HOH W 17 3.648 34.945 10.762 1.00 21.32

ATOM 3796 OH2 HOH W 18 7.263 27.211 17.549 1.00 18.46

ATOM 3799 OH2 HOH W 19 20.958 16.481 -0.013 1.00 21.56

ATOM 3802 OH2 HOH W 20 8.618 30.542 -3.563 1.00 16.53

ATOM 3805 OH2 HOH W 21 18.140 27.899 -17.057 1.00 16.87

ATOM 3808 OH2 HOH W 22 28.025 7.911 4.889 1.00 14.07

ATOM 3811 OH2 HOH W 23 22.965 21.183 -6.891 1.00 18.28

ATOM 3814 OH2 HOH W 24 19.069 35.307 -17.330 1.00 16.53

ATOM 3817 OH2 HOH W 25 26.608 17.639 -2.849 1.00 13.86

ATOM 3820 OH2 HOH W 26 10.049 27.793 21.444 1.00 18.31

ATOM 3823 OH2 HOH W 27 24.660 12.553 -7.179 1.00 18.24

ATOM 3826 OH2 HOH W 28 7.606 18.082 12.372 1.00 13.59

ATOM 3829 OH2 HOH W 29 18.398 26.494 -12.059 1.00 15.54

ATOM 3832 OH2 HOH W 30 4.355 13.029 17.494 1.00 19.92

ATOM 3835 OH2 HOH W 31 -0.900 31.488 2.829 1.00 18.30

ATOM 3838 OH2 HOH W 32 11.654 34.502 5.468 1.00 25.42

ATOM 3841 OH2 HOH W 33 7.194 37.243 -4.445 1.00 19.56

ATOM 3844 OH2 HOH W 34 6.377 34.130 -6.695 1.00 18.47

ATOM 3847 OH2 HOH W 35 6.504 21.372 13.690 1.00 20.31

ATOM 3850 OH2 HOH W 36 23.108 46.257 -9.094 1.00 25.60

ATOM 3853 OH2 HOH W 37 17.773 33.636 14.905 1.00 22.15

ATOM 3856 OH2 HOH W 38 8.610 20.297 -15.054 1.00 19.26

ATOM 3859 OH2 HOH W 39 5.372 22.059 -15.064 1.00 27.58 ATOM 3862 OH2 HOH W 40 16.365 12.317 5.212 1.00 16.25

ATOM 3865 OH2 HOH W 41 20.124 25.959 -9.827 1.00 20.48

ATOM 3868 OH2 HOH W 42 -O.785 20.507 -9.217 1.00 21.47

ATOM 3871 OH2 HOH W 43 15.288 16.319 21.447 1.00 28.05

ATOM 3874 OH2 HOH W 44 12.480 33.606 8.456 1.00 19.45

ATOM 3877 OH2 HOH W 45 7.289 37.001 -7.936 1.00 18.91

ATOM 3880 OH2 HOH W 46 2.028 12.237 8.190 1.00 22.39

ATOM 3883 OH2 HOH W 47 3.209 17.409 11.484 1.00 25.83

ATOM 3886 OH2 HOH W 48 5.465 30.279 -12.380 1.00 22.85

ATOM 3889 OH2 HOH W 49 22.982 31.407 16.105 1.00 22.99

ATOM 3892 OH2 HOH W 50 24.742 45.646 -1.834 1.00 27.69

ATOM 3895 OH2 HOH W 51 2.855 34.508 -12.669 1.00 29.18

ATOM 3898 OH2 HOH W 52 27.130 31.410 -7.401 1.00 21.83

ATOM 3901 OH2 HOH W 53 6.533 33.029 17.866 1.00 23.08

ATOM 3904 OH2 HOH W 54 7.168 43.849 -14.726 1.00 24.30

ATOM 3907 OH2 HOH W 55 9.653 9.952 6.151 1.00 29.92

ATOM 3910 OH2 HOH W 56 17.527 26.562 26.826 1.00 25.29

ATOM 3913 OH2 HOH W 57 31.108 20.934 12.859 1.00 23.94

ATOM 3916 OH2 HOH W 58 25.097 19.426 -6.903 1.00 25.73

ATOM 3919 OH2 HOH W 59 4.055 37.151 -17.075 1.00 22.24

ATOM 3922 OH2 HOH W 60 30.811 21.627 0.903 1.00 28.34

ATOM 3925 OH2 HOH W 61 8.041 13.655 24.435 1.00 33.26

ATOM 3928 OH2 HOH W 62 10.203 34.664 -0.919 1.00 32.67

ATOM 3931 OH2 HOH W 63 0.787 21.818 -2.474 1.00 22.36

ATOM 3934 OH2 HOH W 64 8.278 26.115 19.878 1.00 25.79

ATOM 3937 OH2 HOH W 65 8.084 39.231 4.138 1.00 30.02

ATOM 3940 OH2 HOH W 66 21.688 12.649 -0.060 1.00 34.13

ATOM 3943 OH2 HOH W 67 17.732 20.720 -9.545 1.00 24.08

ATOM 3946 OH2 HOH W 68 15.758 18.751 23.791 1.00 30.14

ATOM 3949 OH2 HOH W 69 19.842 53.713 -3.904 1.00 36.48

ATOM 3952 OH2 HOH W 70 21.818 33.539 0.594 1.00 30.68

ATOM 3955 OH2 HOH W 71 22.875 13.810 2.166 1.00 26.21

ATOM 3958 OH2 HOH W 72 31.677 17.137 0.649 1.00 25.94

ATOM 3961 OH2 HOH W 73 17.702 11.343 3.065 1.00 17.06

ATOM 3964 OH2 HOH W 74 O.778 41.731 11.827 1.00 35.02

ATOM 3967 OH2 HOH W 75 -0.698 20.410 -0.675 1.00 23.31

ATOM 3970 OH2 HOH W 76 19.556 38.814 -10.469 1.00 26.20

ATOM 3973 OH2 HOH W 77 4.450 32.708 13.071 1.00 24.43

ATOM 3976 OH2 HOH W 78 1.052 18.358 12.276 1.00 34.72

ATOM 3979 OH2 HOH W 79 11.832 6.851 15.414 1.00 30.11

ATOM 3982 OH2 HOH W 80 4.586 32.608 -13.395 1.00 33.70

ATOM 3985 OH2 HOH W 81 22.062 34.132 -14.209 1.00 21.98

ATOM 3988 OH2 HOH W 82 20.146 10.905 13.559 1.00 33.56

ATOM 3991 OH2 HOH W 83 27.558 17.467 16.706 1.00 26.60

ATOM 3994 OH2 HOH W 84 16.395 45.178 -6.175 1.00 30.76

ATOM 3997 OH2 HOH W 85 28.889 26.973 -1.045 1.00 30.80

ATOM 4000 OH2 HOH W 86 6.740 40.727 6.077 1.00 25.10

ATOM 4003 OH2 HOH W 87 4.651 20.004 11.014 1.00 28.93

ATOM 4006 OH2 HOH W 88 19.925 26.259 -14.193 1.00 28.49

ATOM 4009 OH2 HOH W 89 32.933 17.501 11.128 1.00 29.39

ATOM 4012 OH2 HOH W 90 22.117 19.486 24.116 1.00 29.72

ATOM 4015 OH2 HOH W 91 16.563 42.717 -7.537 1.00 38.33

ATOM 4018 OH2 HOH W 92 10.585 11.488 20.926 1.00 28.39

ATOM 4021 OH2 HOH W 93 32.153 21.984 7.770 1.00 37.67

ATOM 4024 OH2 HOH W 94 19.838 24.340 26.802 1.00 32.22

ATOM 4027 OH2 HOH W 95 21.135 23.974 24.266 1.00 32.86

ATOM 4030 OH2 HOH W 96 17.957 11.867 -5.395 1.00 30.06

ATOM 4033 OH2 HOH W 97 0.953 20.261 8.008 1.00 41.09

ATOM 4036 OH2 HOH W 98 32.062 37.265 6.823 1.00 30.65

ATOM 4039 OH2 HOH W 99 14.742 23.673 -11.816 1.00 23.19

ATOM 4042 OH2 HOH W 100 -5.742 19.592 10.594 1.00 29.15 ATOM 4045 OH2 HOH W 101 17.866 9.888 24.166 1.00 32.36

ATOM 4048 OH2 HOH W 102 -5.043 15.461 9.612 1.00 32.25

ATOM 4051 OH2 HOH W 103 1.455 9.372 16.114 1.00 29.97

ATOM 4054 OH2 HOH W 104 16.690 22.823 -10.497 1.00 38.29

ATOM 4057 OH2 HOH W 105 15.984 27.047 24.287 1.00 27.58

ATOM 4060 OH2 HOH W 106 29.067 30.034 7.947 1.00 30.09

ATOM 4063 OH2 HOH W 107 26.873 13.684 18.289 1.00 30.30

ATOM 4066 OH2 HOH W 108 26.611 35.649 11.995 1.00 30.43

ATOM 4069 OH2 HOH W 109 17.645 25.226 -16.842 1.00 30.04

ATOM 4072 OH2 HOH W 110 21.298 10.927 23.220 1.00 39.36

ATOM 4075 OH2 HOH W 111 -3.755 20.234 1.273 1.00 35.21

ATOM 4078 OH2 HOH W 112 16.849 35.173 12.810 1.00 40.15

ATOM 4081 OH2 HOH W 113 32.680 8.857 13.943 1.00 32.58

ATOM 4084 OH2 HOH W 114 13.401 38.319 -2.260 1.00 37.10

ATOM 4087 OH2 HOH W 115 25.947 38.794 -0.457 1.00 33.15

ATOM 4090 OH2 HOH W 116 3.045 36.679 15.657 1.00 38.38

ATOM 4093 OH2 HOH W 117 28.634 17.418 -4.461 1.00 27.64

ATOM 4096 OH2 HOH W 118 13.195 17.931 24.435 1.00 31.39

ATOM 4099 OH2 HOH W 119 24.218 30.053 18.129 1.00 35.53

ATOM 4102 OH2 HOH W 120 30.332 20.582 15.574 1.00 35.53

ATOM 4105 OH2 HOH W 121 9.403 44.536 -10.706 1.00 35.40

ATOM 4108 OH2 HOH W 122 30.488 25.100 9.901 1.00 33.98

ATOM 4111 OH2 HOH W 123 15.784 12.389 -6.525 1.00 43.55

ATOM 4114 OH2 HOH W 124 7.688 11.687 19.060 1.00 36.87

ATOM 4117 OH2 HOH W 125 -3.912 32.863 0.241 1.00 30.58

ATOM 4120 OH2 HOH W 126 14.714 9.545 5.346 1.00 30.45

ATOM 4123 OH2 HOH W 127 17.279 23.551 -14.954 1.00 35.71

ATOM 4126 OH2 HOH W 128 -2.467 36.346 15.921 1.00 42.28

ATOM 4129 OH2 HOH W 129 -3.300 17.162 20.997 1.00 40.02

ATOM 4132 OH2 HOH W 130 14.917 7.632 18.357 1.00 38.85

ATOM 4135 OH2 HOH W 131 13.916 47.035 -14.990 1.00 42.89

ATOM 4138 OH2 HOH W 132 6.831 25.776 22.177 1.00 27.21

ATOM 4141 OH2 HOH W 133 4.483 6.781 12.443 1.00 39.57

ATOM 4144 OH2 HOH W 134 27.504 19.574 -6.046 1.00 31.34

ATOM 4147 OH2 HOH W 135 27.222 37.371 -3.488 1.00 36.87

ATOM 4150 OH2 HOH W 136 26.328 23.713 -6.285 1.00 30.37

ATOM 4153 OH2 HOH W 137 9.900 5.416 -5.773 1.00 42.95

ATOM 4156 OH2 HOH W 138 19.302 42.237 -8.390 1.00 47.29

ATOM 4159 OH2 HOH W 139 27.974 24.430 -4.232 1.00 37.77

ATOM 4162 OH2 HOH W 140 -0.411 22.132 16.514 1.00 36.68

ATOM 4165 OH2 HOH W 141 28.981 15.448 17.768 1.00 39.88

ATOM 4168 OH2 HOH W 142 7.596 35.277 11.339 1.00 34.57

ATOM 4171 OH2 HOH W 143 10.487 13.988 22.355 1.00 42.95

ATOM 4174 OH2 HOH W 144 21.560 34.054 -17.435 1.00 29.46

ATOM 4177 OH2 HOH W 145 13.715 14.679 -10.482 1.00 43.27

ATOM 4180 OH2 HOH W 146 1.935 11.547 18.248 1.00 40.18

ATOM 4183 OH2 HOH W 147 3.393 17.712 23.189 1.00 33.07

ATOM 4186 OH2 HOH W 148 -3.496 36.740 -0.124 1.00 47.29

ATOM 4189 OH2 HOH W 149 22.254 22.228 -9.526 1.00 38.26

ATOM 4192 OH2 HOH W 150 3.195 7.573 9.719 1.00 40.89

ATOM 4195 OH2 HOH W 151 -7.121 16.750 10.286 1.00 42.26

ATOM 4198 OH2 HOH W 152 16.161 8.774 9.578 1.00 41.94

ATOM 4201 OH2 HOH W 153 16.092 35.277 10.412 1.00 42.26

ATOM 4204 OH2 HOH W 154 26.133 30.721 14.238 1.00 45.33

ATOM 4207 OH2 HOH W 155 24.524 0.768 13.585 1.00 38.75

ATOM 4210 OH2 HOH W 156 31.083 31.795 0.067 1.00 36.20

ATOM 4213 OH2 HOH W 157 3.167 21.515 22.429 1.00 36.00

ATOM 4216 OH2 HOH W 158 24.801 33.964 9.921 1.00 45.48

ATOM 4219 OH2 HOH W 159 -3.493 32.134 -4.498 1.00 42.32

ATOM 4222 OH2 HOH W 160 12.768 14.064 -13.158 1.00 46.22

ATOM 4225 OH2 HOH W 161 12.666 38.337 -17.657 1.00 36.30 ATOM 4228 OH2 HOH W 162 15.370 13.648 -8.783 1.00 45.53

ATOM 4231 OH2 HOH W 163 36.549 11.808 12.902 1.00 35.47

ATOM 4234 OH2 HOH W 164 24.222 24.289 27.671 1.00 31.43

ATOM 4237 OH2 HOH W 165 12.153 35.795 11.204 1.00 41.20

ATOM 4240 OH2 HOH W 166 9.700 36.766 11.913 1.00 39.29

ATOM 4243 OH2 HOH W 167 11.543 16.643 21.740 1.00 43.82

ATOM 4246 OH2 HOH W 168 23.124 4.374 6.956 1.00 45.07

ATOM 4249 OH2 HOH W 169 4.770 26.940 19.244 1.00 43.32

ATOM 4252 OH2 HOH W 171 29.445 23.775 15.949 1.00 41.74

ATOM 4255 OH2 HOH W 172 33.619 20.957 9.469 1.00 35.28

ATOM 4258 OH2 HOH W 173 4.589 35.695 -6.166 1.00 43.92

ATOM 4261 OH2 HOH W 174 22.229 12.974 22.170 1.00 29.78

ATOM 4264 OH2 HOH W 175 22.749 36.545 7.072 1.00 32.48

ATOM 4267 OH2 HOH W 176 22.768 12.143 4.126 1.00 34.54

ATOM 4270 OH2 HOH W 177 20.396 11.626 6.932 1.00 40.14

ATOM 4273 OH2 HOH W 178 19.949 37.352 6.938 1.00 43.05

ATOM 4276 OH2 HOH W 179 0.318 34.055 -10.167 1.00 37.51

ATOM 4279 OH2 HOH W 180 27.777 26.561 -5.580 1.00 38.70

ATOM 4282 OH2 HOH W 181 -7.821 33.694 15.658 1.00 43.77

ATOM 4285 OH2 HOH W 182 -1.174 17.500 15.475 1.00 44.52

ATOM 4288 OH2 HOH W 183 21.613 18.685 -8.904 1.00 37.57

ATOM 4291 OH2 HOH W 184 18.530 10.217 -2.679 1.00 43.00

ATOM 4294 OH2 HOH W 185 -2.070 39.118 11.910 1.00 44.15

ATOM 4297 OH2 HOH W 186 -5.845 26.909 19.878 1.00 48.94

ATOM 4300 OH2 HOH W 187 -4.797 27.850 -3.050 1.00 49.09

ATOM 4303 OH2 HOH W 188 21.283 35.111 2.806 1.00 28.83

ATOM 4306 OH2 HOH W 189 18.741 35.515 3.236 1.00 36.23

ATOM 4309 OH2 HOH W 190 -2.385 36.331 -3.442 1.00 42.61

ATOM 4312 OH2 HOH W 191 12.897 13.429 23.065 1.00 47.11

ATOM 4315 OH2 HOH W 192 11.734 51.930 -2.413 1.00 48.51

ATOM 4318 OH2 HOH W 193 27.495 4.321 15.536 1.00 37.55

ATOM 4321 OH2 HOH W 194 1.360 22.823 18.157 1.00 44.43

ATOM 4324 OH2 HOH W 195 30.702 35.970 17.204 1.00 56.42

ATOM 4327 OH2 HOH W 196 15.854 8.709 1.293 1.00 41.56

ATOM 4330 OH2 HOH W 197 7.603 41.670 3.075 1.00 51.02

ATOM 4333 OH2 HOH W 198 20.289 10.918 2.624 1.00 39.89

ATOM 4336 OH2 HOH W 199 24.813 12.186 -4.391 1.00 31.75

ATOM 4339 OH2 HOH W 200 25.698 12.916 -2.334 1.00 34.86

ATOM 4342 OH2 HOH W 201 10.148 15.062 -10.418 1.00 42.93

ATOM 4345 OH2 HOH W 202 2.551 18.776 8.755 1.00 38.89

ATOM 4348 OH2 HOH W 203 5.727 31.066 18.521 1.00 40.86

ATOM 4351 OH2 HOH W 205 22.290 25.210 -10.050 1.00 36.35

ATOM 4354 OH2 HOH W 206 27.494 25.373 18.119 1.00 43.80

ATOM 4357 OH2 HOH W 207 19.704 38.102 -16.736 1.00 42.96

ATOM 4360 OH2 HOH W 208 31.448 37.858 2.208 1.00 49.68

ATOM 4363 OH2 HOH W 209 22.129 49.138 -11.083 1.00 52.80

ATOM 4366 OH2 HOH W 211 17.218 13.335 -10.543 1.00 49.10

ATOM 4369 OH2 HOH W 212 23.140 27.375 -13.205 1.00 45.56

ATOM 4372 OH2 HOH W 213 22.259 35.803 9.828 1.00 37.67

ATOM 4375 OH2 HOH W 214 5.278 33.991 14.876 1.00 51.67

ATOM 4378 OH2 HOH W 215 27.663 36.926 -0.953 1.00 41.76

ATOM 4381 OH2 HOH W 217 14.502 35.566 4.101 1.00 45.42

ATOM 4384 OH2 HOH W 218 26.326 29.701 21.539 1.00 38.49

ATOM 4387 OH2 HOH W 219 8.476 5.105 15.999 1.00 43.06

ATOM 4390 OH2 HOH W 220 27.189 34.442 24.885 1.00 36.98

ATOM 4393 OH2 HOH W 221 20.649 45.763 -8.645 1.00 43.89

ATOM 4396 OH2 HOH W 223 7.448 35.230 14.873 1.00 35.81

ATOM 4399 OH2 HOH W 224 -7.954 27.430 6.637 1.00 51.06

ATOM 4402 OH2 HOH W 226 2.926 32.535 18.042 1.00 49.53

ATOM 4405 OH2 HOH W 227 23.072 40.040 -1.900 1.00 48.81

ATOM 4408 OH2 HOH W 229 5.317 35.724 12.637 1.00 50.79 ATOM 4411 OH2 HOH W 231 15 . 097 37 . 872 20 . 843 1 . 00 49 . 88

ATOM 44 14 OH2 HOH W 232 - 3 . 341 12 . 532 17 . 990 1 . 00 45 . 83

Table Ib

Coordinates of DFFK-chloromethyl ketone inhibited Prostasin

HEADER XX-XXX-XX COMPND REMARK REMARK REFINEMENT. REMARK PROGRAM REFMAC 5.2.0005 REMARK AUTHORS MURSHUDOV, VAGIN, DODSON REMARK REMARK REFINEMENT TARGET MAXIMUM LIKELIHOOD REMARK REMARK DATA USED IN REFINEMENT. REMARK RESOLUTION RANGE HIGH (ANGSTROMS 1.70 REMARK RESOLUTION RANGE LOW (ANGSTROMS 34.10 REMARK DATA CUTOFF (SIGMA(F) NONE REMARK COMPLETENESS FOR RANGE (% 98.29 REMARK NUMBER OF REFLECTIONS 24009 REMARK REMARK FIT TO DATA USED IN REFINEMENT. REMARK CROSS-VALIDATION METHOD THROUGHOUT REMARK FREE R VALUE TEST SET SELECTION RANDOM REMARK R VALUE (WORKING + TEST SET) 0.15694 REMARK R VALUE (WORKING SET) 0.15521 REMARK FREE R VALUE 0.19000 REMARK FREE R VALUE TEST SET SIZE (%) 5.0 REMARK FREE R VALUE TEST SET COUNT 1256 REMARK REMARK FIT IN THE HIGHEST RESOLUTION BIN. REMARK TOTAL NUMBER OF BINS USED 20 REMARK BIN RESOLUTION RANGE HIGH 1. 700 REMARK BIN RESOLUTION RANGE LOW 1. 744 REMARK REFLECTION IN BIN (WORKING SET) 1549 REMARK BIN COMPLETENESS (WORKING+TEST) (%) 87 .93 REMARK BIN R VALUE (WORKING SET) 0. 210 REMARK BIN FREE R VALUE SET COUNT 76 REMARK BIN FREE R VALUE 0. 314 REMARK REMARK NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK ALL ATOMS : 2243 REMARK REMARK B VALUES . REMARK FROM WILSON PLOT (A**2) NULL REMARK MEAN B VALUE (OVERALL, A**2) 13.238 REMARK OVERALL ANISOTROPIC B VALUE. REMARK BIl (A**2) -0.14 REMARK B22 (A**2) 0.08 REMARK B33 (A**2) 0.05 REMARK B12 (A**2) 0.00 REMARK B13 (A**2) 0.00 REMARK B23 (A**2) 0.00 REMARK REMARK ESTIMATED OVERALL COORDINATE ERROR. REMARK ESU BASED ON R VALUE (A) 0.104 REMARK 3 ESU BASED ON FREE R VALUE (A) :

0.101

REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A) :

0.064

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

1.903

REMARK 3

REMARK 3 3 CORRELATION COEFFICIENTS.

REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963

REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943

REMARK 3

REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS

WEIGHT

REMARK 3 BOND LENGTHS REFINED ATOMS (A) 2044 ; 0.012

0.021

REMARK 3 BOND LENGTHS OTHERS (A) 1785 ; 0.001

0.020

REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES) 2797 ; 1.427

1.963

REMARK 3 BOND ANGLES OTHERS (DEGREES) 4181 ; 0.797

3.000

REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES) 260 ; 5.706

5.000

REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES) 82 ; 34.094

;24.512

REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES) 299 ; 11.716

;15.000

REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES) 7 ; 12.785

;15.000

REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3) 301 ; 0.087

0.200

REMARK 3 GENERAL PLANES REFINED ATOMS (A) 2277 ; 0.006

0.020

REMARK 3 GENERAL PLANES OTHERS (A) 392 ; 0.001

0.020

REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A) 445 ; 0.238

0.200

REMARK 3 NON-BONDED CONTACTS OTHERS (A) 1991 ; 0.189

0.200

REMARK 3 NON-BONDED TORSION REFINED ATOMS (A) 1022 ; 0.184

0.200

REMARK 3 NON-BONDED TORSION OTHERS (A) 1228 ; 0.089

0.200

REMARK 3 H-BOND (X... Y) REFINED ATOMS (A) 200 ; 0.134

0.200

REMARK 3 SYMMETRY VDW REFINED ATOMS (A) 24 ; 0.257

0.200

REMARK 3 SYMMETRY VDW OTHERS (A) 71 ; 0.202

0.200

REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A) 33 ; 0.176

0.200

REMARK 3

REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS

WEIGHT

REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2) 1606 ; 1.454

2.000

REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2) 520 ; 0.293

2.000

REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2) : 2065 ; 1.900

3.000 REMARK SIDE-CHAIN BOND REFINED ATOMS (A**2) 902 ; 3.772 ;

5.000

REMARK SIDE-CHAIN ANGLE REFINED ATOMS (A**2) 728 ; 5.332 ;

8.000

REMARK

REMARK NCS RESTRAINTS STATISTICS

REMARK NUMBER OF NCS GROUPS : NULL

REMARK

REMARK

REMARK TLS DETAILS

REMARK NUMBER OF TLS GROUPS : NULL

REMARK

REMARK

REMARK BULK SOLVENT MODELLING.

REMARK METHOD USED : BABINET MODEL WITH MASK

REMARK PARAMETERS FOR MASK CALCULATION

REMARK VDW PROBE RADIUS : 1.20

REMARK ION PROBE RADIUS : 0.80

REMARK SHRINKAGE RADIUS : 0.80

REMARK

REMARK OTHER REFINEMENT REMARKS:

REMARK HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

REMARK

LINK SG ACYS B 70 2.031 SG CYΞ 86

SS

SSBOND 1 CYS B 168 CYS B 244

SSBOND 2 CYS B 201 CYS B 223

SSBOND 3 CYS B 234 CYS B 262

CISPEP 1 THR B 184 PRO B 185 0. 00

CRYSTl 37.677 75.880 79.179 90.00 90.00 90.00 P 21 21 21

SCALEl 0.026541 0. 000000 0.000000 0.00000

SCALE 2 0.000000 0. 013179 0.000000 0.00000

SCALE 3 0.000000 0. 000000 0.012630 0.00000

ATOM 1 N N ILE B 45 32.479 -5.195 23.924 .00 9.17

ATOM 2 C CAA ILE B 45 33.132 -5.340 22.601 .00 9.29

ATOM 4 C CBB ILE B 45 34.625 -5.035 22.693 .00 9.55

ATOM 6 C CGGll ILE B 45 34.867 -3.645 23.300 .00 9.89

ATOM 9 C CDDll ILE B 45 34.555 -2.503 22.388 .00 8.38

ATOM 13 C CGG22 ILE B 45 35.292 -5.199 21.320 .00 10.21

ATOM 17 C C ILE B 45 32.963 -6.782 22.124 .00 9.78

ATOM 18 O O ILE B 45 33.283 -7.697 22.854 .00 9.53

ATOM 22 N N THR B 46 32.457 -6.965 20.906 .00 10.46

ATOM 23 C CAA THR B 46 32.315 -8.299 20.347 .00 10.82

ATOM 25 C CBB THR B 46 30.855 -8.647 19.940 .00 11.76

ATOM 27 OGl THR B 46 30.791 10.010 19.497 .00 12.56

ATOM 29 CG2 THR B 46 30.328 -7.725 18.849 .00 11.19

ATOM 33 C C THR B 46 33.277 -8.388 19.170 .00 10.97

ATOM 34 O O THR B 46 33.442 -7.442 18.421 .00 9.92

ATOM 36 N N GLY B 47 33.928 -9.535 19.035 .00 11.26

ATOM 37 C CAA GLY B 47 34.768 -9.769 17.893 .00 11.78

ATOM 40 C C GLY B 47 36.179 -9.270 18.035 .00 11.94

ATOM 41 O O GLY B 47 36.955 -9.311 17.065 .00 13.39

ATOM 43 N N GLY B 48 36.520 -8.808 19.236 .00 11.14

ATOM 44 C CAA GLY B 48 37.821 -8.262 19.475 .00 11.73

ATOM 47 C C GLY B 48 38.717 -9.204 20.238 .00 13.16

ATOM 48 O O GLY B 48 38.516 10.420 20.232 .00 14.99

ATOM 50 N N SER B 49 39.709 -8.632 20.903 .00 12.87

ATOM 51 C CAA SER B 49 40.656 -9.417 21.692 .00 12.60

ATOM 53 C CBB SER B 49 41.957 -9.592 20.925 .00 13.49

ATOM 56 O OGG SER B 49 42.593 -8.338 20.673 .00 13.97

ATOM 58 C C SER B 49 40.924 -8.722 23.000 .00 12.95 ATOM 59 O SER B 49 40.588 -7.542 23.166 1.00 11.06

ATOM 61 N SER B 50 41.603 -9.423 23.903 1.00 12.13

ATOM 62 CA SER B 50 42.010 -8.823 25.164 1.00 11.45

ATOM 64 CB SER B 50 42.311 -9.887 26.223 1.00 12.37

ATOM 67 OG SER B 50 41.116 -10.552 26.572 1.00 13.76

ATOM 69 C SER B 50 43.225 -7.963 24.958 1.00 11.63

ATOM 70 O SER B 50 44.252 -8.414 24.427 1.00 10.93

ATOM 72 N ALA B 51 43.107 -6.712 25.369 1.00 10.73

ATOM 73 CA ALA B 51 44.255 -5.821 25.425 1.00 11.39

ATOM 75 CB ALA B 51 43.800 -4.430 25.754 1.00 12.04

ATOM 79 C ALA B 51 45.289 -6.304 26.449 1.00 13.55

ATOM 80 O ALA B 51 44.968 -7.029 27.380 1.00 13.28

ATOM 82 N VAL B 52 46.534 -5.919 26.249 1.00 15.71

ATOM 83 CA VAL B 52 47.563 -6.103 27.268 1.00 16.99

ATOM 85 CB VAL B 52 48.976 -6.234 26.636 1.00 18.95

ATOM 87 CGl VAL B 52 48.967 -7.228 25.483 1.00 21.60

ATOM 91 CG2 VAL B 52 49.489 -4.913 26.162 1.00 22.01

ATOM 95 C VAL B 52 47.517 -4.918 28.232 1.00 18.20

ATOM 96 O VAL B 52 47.108 -3.823 27.856 1.00 17.03

ATOM 98 N ALA B 53 47.931 -5.124 29.484 1.00 18.54

ATOM 99 CA ALA B 53 47.899 -4.048 30.478 1.00 18.91

ATOM 101 CB ALA B 53 48.369 -4.542 31.856 1.00 19.66

ATOM 105 C ALA B 53 48.770 -2.892 29.997 1.00 19.25

ATOM 106 O ALA B 53 49.836 -3.106 29.416 1.00 20.00

ATOM 108 N GLY B 54 48.286 -1.670 30.186 1.00 19.50

ATOM 109 CA GLY B 54 49.036 -0.487 29.770 1.00 18.55

ATOM 112 C GLY B 54 48.804 -0.093 28.327 1.00 17.21

ATOM 113 O GLY B 54 49.225 0.985 27.911 1.00 16.53

ATOM 115 N GLN B 55 48.115 -0.945 27.559 1.00 17.42

ATOM 116 CA GLN B 55 47.915 -0.677 26.137 1.00 16.31

ATOM 118 CB GLN B 55 47.368 -1.918 25.429 1.00 17.19

ATOM 121 CG GLN B 55 47.572 -1.870 23.956 1.00 18.92

ATOM 124 CD GLN B 55 47.344 -3.193 23.219 1.00 19.86

ATOM 125 OEl GLN B 55 47.518 -3.233 22.006 1.00 31.16

ATOM 126 NE2 GLN B 55 46.925 -4.244 23.915 1.00 11.50

ATOM 129 C GLN B 55 47.050 0.557 25.827 1.00 16.65

ATOM 130 O GLN B 55 47.363 1.310 24.911 1.00 18.78

ATOM 132 N TRP B 56 45.978 0.761 26.572 1.00 13.82

ATOM 133 CA TRP B 56 45.029 1.863 26.285 1.00 12.36

ATOM 135 CB TRP B 56 43.721 1.300 25.746 1.00 12.22

ATOM 138 CG TRP B 56 43.922 0.411 24.581 1.00 10.21

ATOM 139 CDl TRP B 56 43.906 -0.943 24.573 1.00 10.51

ATOM 141 NEl TRP B 56 44.143 -1.412 23.313 1.00 12.67

ATOM 143 CE2 TRP B 56 44.334 -0.351 22.478 1.00 9.43

ATOM 144 CD2 TRP B 56 44.212 0.817 23.255 1.00 8.35

ATOM 145 CE3 TRP B 56 44.324 2.052 22.627 1.00 10.75

ATOM 147 CZ3 TRP B 56 44.599 2.085 21.280 1.00 11.94

ATOM 149 CH2 TRP B 56 44.732 0.912 20.543 1.00 9.85

ATOM 151 CZ2 TRP B 56 44.587 -0.311 21.115 1.00 10.27

ATOM 153 C TRP B 56 44.821 2.610 27.597 1.00 10.47

ATOM 154 O TRP B 56 43.774 2.501 28.239 1.00 8.57

ATOM 156 N PRO B 57 45.863 3.328 28.036 1.00 10.15

ATOM 157 CA PRO B 57 45.894 3.845 29.394 1.00 10.34

ATOM 159 CB PRO B 57 47.343 4.295 29.563 1.00 11.49

ATOM 162 CG PRO B 57 47.796 4.627 28.174 1.00 10.27

ATOM 165 CD PRO B 57 47.080 3.662 27.270 1.00 10.75

ATOM 168 C PRO B 57 44.900 4.979 29.677 1.00 8.95

ATOM 169 O PRO B 57 44.784 5.441 30.821 1.00 10.15

ATOM 170 N TRP B 58 44.232 5.455 28.633 1.00 9.52

ATOM 171 CA TRP B 58 43.203 6.463 28.764 1.00 8.97

ATOM 173 CB TRP B 58 43.143 7.383 27.548 1.00 9.77 ATOM 176 CG TRP B 58 43.314 6.679 26.240 1.00 6.25

ATOM 177 CDl TRP B 58 42.336 6.108 25.460 1.00 7.31

ATOM 179 NEl TRP B 58 42.901 5.582 24.331 1.00 9.26

ATOM 181 CE2 TRP B 58 44.248 5.798 24.347 1.00 6.32

ATOM 182 CD2 TRP B 58 44.547 6.481 25.542 1.00 6.70

ATOM 183 CE3 TRP B 58 45.861 6.859 25.786 1.00 8.15

ATOM 185 CZ3 TRP B 58 46.843 6.517 24.867 1.00 11.45

ATOM 187 CH2 TRP B 58 46.514 5.819 23.700 1.00 9.47

ATOM 189 CZ2 TRP B 58 45.235 5.465 23.415 1.00 9.66

ATOM 191 C TRP B 58 41.846 5.827 28.977 1.00 9.07

ATOM 192 O TRP B 58 40.912 6.529 29.331 1.00 7.83

ATOM 194 N GLN B 59 41.729 4.504 28.803 1.00 8.10

ATOM 195 CA GLN B 59 40.431 3.855 29.014 1.00 8.57

ATOM 197 CB GLN B 59 40.473 2.400 28.541 1.00 8.43

ATOM 200 CG GLN B 59 39.190 1.579 28.883 1.00 8.42

ATOM 203 CD GLN B 59 38.037 1.874 27.957 1.00 7.28

ATOM 204 OEl GLN B 59 38.165 1.748 26.753 1.00 10.12

ATOM 205 NE2 GLN B 59 36.891 2.243 28.513 1.00 6.24

ATOM 208 C GLN B 59 40.097 3.809 30.480 1.00 8.44

ATOM 209 O GLN B 59 40.921 3.315 31.276 1.00 9.52

ATOM 211 N VAL B 60 38.891 4.274 30.839 1.00 7.50

ATOM 212 CA VAL B 60 38.410 4.203 32.215 1.00 8.18

ATOM 214 CB VAL B 60 38.331 5.599 32.900 1.00 8.76

ATOM 216 CGl VAL B 60 39.666 6.344 32.785 1.00 8.93

ATOM 220 CG2 VAL B 60 37.223 6.416 32.345 1.00 8.10

ATOM 224 C VAL B 60 37.062 3.505 32.270 1.00 8.21

ATOM 225 O VAL B 60 36.366 3.388 31.263 1.00 7.57

ATOM 227 N SER B 61 36.716 3.037 33.454 1.00 7.37

ATOM 228 CA SER B 61 35.449 2.378 33.708 1.00 8.91

ATOM 230 CB SER B 61 35.664 1.021 34.385 1.00 10.09

ATOM 233 OG SER B 61 34.485 0.598 35.069 1.00 12.50

ATOM 235 C SER B 61 34.636 3.286 34.608 1.00 8.47

ATOM 236 O SER B 61 35.174 3.845 35.546 1.00 9.55

ATOM 238 N ILE B 62 33.353 3.448 34.282 1.00 10.10

ATOM 239 CA ILE B 62 32.450 4.274 35.052 1.00 10.71

ATOM 241 CB ILE B 62 31.650 5.223 34.171 1.00 11.81

ATOM 243 CGl ILE B 62 32.555 5.982 33.169 1.00 17.41

ATOM 246 CDl ILE B 62 33.432 6.947 33.753 1.00 17.75

ATOM 250 CG2 ILE B 62 30.816 6.164 35.026 1.00 14.08

ATOM 254 C ILE B 62 31.459 3.322 35.688 1.00 10.01

ATOM 255 O ILE B 62 30.827 2.526 34.985 1.00 9.85

ATOM 257 N THR B 63 31.338 3.408 37.007 1.00 9.99

ATOM 258 CA THR B 63 30.339 2.638 37.711 1.00 10.14

ATOM 260 CB THR B 63 30.951 1.844 38.876 1.00 11.87

ATOM 262 OGl THR B 63 31.561 2.771 39.791 1.00 10.61

ATOM 264 CG2 THR B 63 31.973 0.821 38.383 1.00 11.83

ATOM 268 C THR B 63 29.269 3.558 38.270 1.00 10.15

ATOM 269 O THR B 63 29.526 4.736 38.578 1.00 9.94

ATOM 271 N TYR B 64 28.060 3.018 38.408 1.00 10.29

ATOM 272 CA TYR B 64 26.971 3.716 39.079 1.00 11.32

ATOM 274 CB TYR B 64 25.840 4.104 38.124 1.00 13.72

ATOM 277 CG TYR B 64 24.827 4.977 38.821 1.00 14.21

ATOM 278 CDl TYR B 64 25.140 6.281 39.150 1.00 19.62

ATOM 280 CEl TYR B 64 24.247 7.083 39.824 1.00 20.24

ATOM 282 CZ TYR B 64 23.026 6.595 40.186 1.00 21.27

ATOM 283 OH TYR B 64 22.171 7.450 40.861 1.00 23.48

ATOM 285 CE2 TYR B 64 22.681 5.284 39.875 1.00 21.08

ATOM 287 CD2 TYR B 64 23.589 4.486 39.202 1.00 20.15

ATOM 289 C TYR B 64 26.464 2.787 40.155 1.00 11.98

ATOM 290 O TYR B 64 26.115 1.640 39.874 1.00 10.44

ATOM 292 N GLU B 65 26.465 3.290 41.385 1.00 12.11 ATOM 293 CA GLU B 65 26.220 2.466 42.581 1.00 12.71

ATOM 295 CB GLU B 65 24.721 2.272 42.788 1.00 14.23

ATOM 298 CG GLU B 65 24.002 3.568 43.096 1.00 18.18

ATOM 301 CD GLU B 65 24.183 4.085 44.544 1.00 23.84

ATOM 302 OEl GLU B 65 24.901 3.491 45.399 1.00 22.83

ATOM 303 OE2 GLU B 65 23.564 5.124 44.822 1.00 30.44

ATOM 304 C GLU B 65 27.004 1.145 42.552 1.00 12.51

ATOM 305 O GLU B 65 26.492 0.095 42.895 1.00 13.46

ATOM 307 N GLY B 66 28.272 1.219 42.133 1.00 10.24

ATOM 308 CA GLY B 66 29.179 0.070 42.120 1.00 10.92

ATOM 311 C GLY B 66 29.145 -0.812 40.897 1.00 10.69

ATOM 312 O GLY B 66 29.970 -1.728 40.776 1.00 12.90

ATOM 314 N VAL B 67 28.182 -0.565 40.009 1.00 10.81

ATOM 315 CA VAL B 67 27.983 -1.397 38.810 1.00 11.66

ATOM 317 CB VAL B 67 26.492 -1.662 38.531 1.00 12.62

ATOM 319 CGl VAL B 67 26.335 -2.541 37.295 1.00 14.89

ATOM 323 CG2 VAL B 67 25.835 -2.326 39.739 1.00 14.97

ATOM 327 C VAL B 67 28.594 -0.710 37.594 1.00 10.83

ATOM 328 O VAL B 67 28.317 0.453 37.360 1.00 10.50

ATOM 330 N HIS B 68 29.415 -1.433 36.829 1.00 12.71

ATOM 331 CA HIS B 68 30.009 -0.870 35.633 1.00 11.69

ATOM 333 CB HIS B 68 30.988 -1.819 34.944 1.00 12.00

ATOM 336 CG HIS B 68 31.452 -1.325 33.603 1.00 13.35

ATOM 337 NDl HIS B 68 30.873 -1.727 32.418 1.00 17.97

ATOM 339 CEl HIS B 68 31.473 -1.116 31.409 1.00 11.85

ATOM 341 NE2 HIS B 68 32.411 -0.328 31.899 1.00 16.47

ATOM 343 CD2 HIS B 68 32.415 -0.437 33.267 1.00 9.69

ATOM 345 C HIS B 68 28.884 -0.602 34.679 1.00 11.96

ATOM 346 O HIS B 68 28.068 -1.494 34.391 1.00 12.69

ATOM 348 N VAL B 69 28.815 0.623 34.200 1.00 10.66

ATOM 349 CA VAL B 69 27.785 1.005 33.254 1.00 10.31

ATOM 351 CB VAL B 69 26.799 2.021 33.852 1.00 10.94

ATOM 353 CGl VAL B 69 26.064 1.421 35.038 1.00 13.01

ATOM 357 CG2 VAL B 69 27.475 3.328 34.251 1.00 11.61

ATOM 361 C VAL B 69 28.305 1.536 31.935 1.00 10.93

ATOM 362 O VAL B 69 27.610 1.476 30.913 1.00 9.35

ATOM 364 N CYS B 70 29.486 2.117 31.935 1.00 9.71

ATOM 365 CA ACYS B 70 30.005 2.751 30.731 0.50 8.82

ATOM 366 CA BCYS B 70 30.019 2.662 30.700 0.50 9.67

ATOM 369 CB ACYS B 70 29.369 4.152 30.560 0.50 8.59

ATOM 370 CB BCYS B 70 29.326 3.988 30.384 0.50 10.29

ATOM 375 SG ACYS B 70 27.685 4.105 29.896 0.50 8.19

ATOM 376 SG BCYS B 70 29.651 5.234 31.583 0.50 17.28

ATOM 379 C CYS B 70 31.519 2.862 30.791 1.00 9.18

ATOM 380 O CYS B 70 32.139 2.630 31.848 1.00 9.99

ATOM 382 N GLY B 71 32.105 3.241 29.670 1.00 8.46

ATOM 383 CA GLY B 71 33.509 3.564 29.627 1.00 8.24

ATOM 386 C GLY B 71 33.655 5.073 29.599 1.00 8.42

ATOM 387 O GLY B 71 32.663 5.849 29.587 1.00 7.41

ATOM 389 N GLY B 72 34.915 5.495 29.559 1.00 7.48

ATOM 390 CA GLY B 72 35.245 6.891 29.343 1.00 7.59

ATOM 393 C GLY B 72 36.672 6.951 28.896 1.00 6.58

ATOM 394 O GLY B 72 37.384 5.917 28.930 1.00 5.30

ATOM 396 N SER B 73 37. Ill 8.145 28.539 1.00 8.28

ATOM 397 CA SER B 73 38.482 8.370 28. Ill 1.00 8.49

ATOM 399 CB SER B 73 38.525 8.742 26.625 1.00 10.54

ATOM 402 OG SER B 73 37.889 7.755 25.862 1.00 15.90

ATOM 404 C SER B 73 39.067 9.484 28.935 1.00 8.02

ATOM 405 O SER B 73 38.474 10.571 28.978 1.00 9.10

ATOM 407 N LEU B 74 40.184 9.209 29.588 1.00 10.03

ATOM 408 CA LEU B 74 40.919 10.224 30.330 1.00 9.58 ATOM 410 CB LEU B 74 42.036 9.594 31.136 1.00 10.17

ATOM 413 CG LEU B 74 42.768 10.486 32.107 1.00 12.06

ATOM 415 CDl LEU B 74 41.814 10.945 33.229 1.00 10.87

ATOM 419 CD2 LEU B 74 43.983 9.754 32.646 1.00 11.94

ATOM 423 C LEU B 74 41.484 11.201 29.327 1.00 9.06

ATOM 424 O LEU B 74 42.176 10.802 28.402 1.00 8.19

ATOM 426 N VAL B 75 41.208 12.481 29.519 1.00 9.02

ATOM 427 CA VAL B 75 41.738 13.496 28.609 1.00 10.15

ATOM 429 CB VAL B 75 40.613 14.165 27.810 1.00 9.49

ATOM 431 CGl VAL B 75 39.960 13.139 26.897 1.00 9.97

ATOM 435 CG2 VAL B 75 39.560 14.791 28.720 1.00 10.50

ATOM 439 C VAL B 75 42.634 14.521 29.293 1.00 11.27

ATOM 440 O VAL B 75 43.228 15.369 28.611 1.00 11.11

ATOM 442 N SER B 76 42.735 14.457 30.612 1.00 11.31

ATOM 443 CA SER B 76 43.695 15.255 31.347 1.00 12.22

ATOM 445 CB SER B 76 43.210 16.701 31.469 1.00 11.14

ATOM 448 OG SER B 76 42.112 16.833 32.365 1.00 11.80

ATOM 450 C SER B 76 43.858 14.625 32.723 1.00 12.93

ATOM 451 O SER B 76 43.263 13.593 33.001 1.00 12.80

ATOM 453 N GLU B 77 44.631 15.254 33.601 1.00 13.77

ATOM 454 CA GLU B 77 44.768 14.729 34.966 1.00 14.29

ATOM 456 CB GLU B 77 45.811 15.525 35.773 1.00 15.67

ATOM 459 CG GLU B 77 45.590 17.027 35.772 1.00 20.84

ATOM 462 CD GLU B 77 46.377 17.763 34.675 1.00 32.43

ATOM 463 OEl GLU B 77 46.260 17.427 33.459 1.00 33.73

ATOM 464 OE 2 GLU B 77 47.121 18.710 35.039 1.00 40.84

ATOM 465 C GLU B 77 43.449 14.739 35.735 1.00 13.25

ATOM 466 O GLU B 77 43.344 14.056 36.733 1.00 14.00

ATOM 468 N GLN B 78 42.455 15.510 35.312 1.00 12.75

ATOM 469 CA GLN B 78 41.192 15.563 36.066 1.00 13.45

ATOM 471 CB GLN B 78 41.166 16.807 36.951 1.00 13.87

ATOM 474 CG GLN B 78 40.400 16.611 38.242 1.00 15.92

ATOM 477 CD GLN B 78 40.392 17.881 39.056 1.00 19.08

ATOM 478 OEl GLN B 78 41.026 18.888 38.646 1.00 24.44

ATOM 479 NE 2 GLN B 78 39.676 17.870 40.203 1.00 18.62

ATOM 482 C GLN B 78 39.898 15.485 35.288 1.00 11.76

ATOM 483 O GLN B 78 38.827 15.580 35.881 1.00 12.05

ATOM 485 N TRP B 79 39.977 15.322 33.975 1.00 10.49

ATOM 486 CA TRP B 79 38.784 15.263 33.162 1.00 10.79

ATOM 488 CB TRP B 79 38.638 16.472 32.256 1.00 11.62

ATOM 491 CG TRP B 79 38.348 17.730 33.018 1.00 12.37

ATOM 492 CDl TRP B 79 39.255 18.566 33.570 1.00 13.69

ATOM 494 NEl TRP B 79 38.612 19.625 34.211 1.00 12.86

ATOM 496 CE 2 TRP B 79 37.260 19.463 34.062 1.00 11.15

ATOM 497 CD2 TRP B 79 37.058 18.272 33.314 1.00 10.97

ATOM 498 CE 3 TRP B 79 35.747 17.875 33.023 1.00 12.61

ATOM 500 CZ3 TRP B 79 34.707 18.659 33.463 1.00 12.77

ATOM 502 CH2 TRP B 79 34.940 19.835 34.184 1.00 12.20

ATOM 504 CZ2 TRP B 79 36.201 20.246 34.501 1.00 14.82

ATOM 506 C TRP B 79 38.757 14.002 32.326 1.00 10.38

ATOM 507 O TRP B 79 39.787 13.516 31.831 1.00 8.55

ATOM 509 N VAL B 80 37.536 13.510 32.179 1.00 10.09

ATOM 510 CA VAL B 80 37.235 12.314 31.427 1.00 9.31

ATOM 512 CB VAL B 80 36.779 11.194 32.375 1.00 9.66

ATOM 514 CGl VAL B 80 36.160 10.047 31.589 1.00 10.05

ATOM 518 CG2 VAL B 80 37.941 10.713 33.211 1.00 10.10

ATOM 522 C VAL B 80 36.092 12.690 30.485 1.00 9.15

ATOM 523 O VAL B 80 35.165 13.412 30.884 1.00 9.58

ATOM 525 N LEU B 81 36.142 12.196 29.246 1.00 8.45

ATOM 526 CA LEU B 81 35.051 12.366 28.291 1.00 8.66

ATOM 528 CB LEU B 81 35.605 12.780 26.922 1.00 9.29 ATOM 531 CG LEU B 81 34.715 13.573 25.973 1.00 14.28

ATOM 533 CDl LEU B 81 34.233 14.836 26.588 1.00 12.95

ATOM 537 CD2 LEU B 81 35.515 13.870 24.713 1.00 14.40

ATOM 541 C LEU B 81 34.333 11.042 28.190 1.00 7.89

ATOM 542 O LEU B 81 34.970 9.974 28.102 1.00 9.57

ATOM 544 N SER B 82 33.008 11.099 28.249 1.00 8.40

ATOM 545 CA SER B 82 32.182 9.909 28.160 1.00 8.70

ATOM 547 CB SER B 82 31.880 9.387 29.563 1.00 8.93

ATOM 550 OG SER B 82 31.235 8.151 29.510 1.00 9.40

ATOM 552 C SER B 82 30.928 10.261 27.364 1.00 8.06

ATOM 553 O SER B 82 30.901 11.287 26.690 1.00 9.36

ATOM 555 N ALA B 83 29.919 9.397 27.400 1.00 8.24

ATOM 556 CA ALA B 83 28.696 9.605 26.646 1.00 7.75

ATOM 558 CB ALA B 83 28.223 8.309 26.031 1.00 7.21

ATOM 562 C ALA B 83 27.633 10.114 27.592 1.00 8.53

ATOM 563 O ALA B 83 27.450 9.571 28.668 1.00 9.74

ATOM 565 N ALA B 84 26.893 11.122 27.161 1.00 8.67

ATOM 566 CA ALA B 84 25.837 11.697 27.989 1.00 8.06

ATOM 568 CB ALA B 84 25.203 12.888 27.279 1.00 8.74

ATOM 572 C ALA B 84 24.760 10.697 28.374 1.00 8.44

ATOM 573 O ALA B 84 24.151 10.810 29.438 1.00 7.14

ATOM 575 N HIS B 85 24.505 9.701 27.530 1.00 8.21

ATOM 576 CA HIS B 85 23.388 8.819 27.828 1.00 8.40

ATOM 578 CB HIS B 85 22.964 8.027 26.601 1.00 8.89

ATOM 581 CG HIS B 85 23.825 6.850 26.314 1.00 6.98

ATOM 582 NDl HIS B 85 24.745 6.859 25.297 1.00 9.21

ATOM 584 CEl HIS B 85 25.355 5.692 25.249 1.00 10.84

ATOM 586 NE2 HIS B 85 24.848 4.918 26.195 1.00 8.56

ATOM 588 CD2 HIS B 85 23.892 5.625 26.880 1.00 8.25

ATOM 590 C HIS B 85 23.687 7.917 29.024 1.00 8.70

ATOM 591 O HIS B 85 22.774 7.291 29.565 1.00 10.05

ATOM 593 N CYS B 86 24.942 7.884 29.454 1.00 9.80

ATOM 594 CA CYS B 86 25.358 7.163 30.653 1.00 10.13

ATOM 596 CB CYS B 86 26.843 6.881 30.609 1.00 10.99

ATOM 599 SG CYS B 86 27.366 5.985 29.139 1.00 14.49

ATOM 601 C CYS B 86 25.095 7.932 31.933 1.00 10.66

ATOM 602 O CYS B 86 25.268 7.366 32.992 1.00 9.11

ATOM 604 N PHE B 87 24.679 9.192 31.819 1.00 11.29

ATOM 605 CA PHE B 87 24.511 10.086 32.964 1.00 12.13

ATOM 607 CB PHE B 87 25.617 11.141 32.958 1.00 11.98

ATOM 610 CG PHE B 87 26.974 10.533 32.973 1.00 10.13

ATOM 611 CDl PHE B 87 27.546 10.131 34.144 1.00 11.34

ATOM 613 CEl PHE B 87 28.772 9.509 34.144 1.00 11.37

ATOM 615 CZ PHE B 87 29.395 9.245 32.960 1.00 11.68

ATOM 617 CE2 PHE B 87 28.818 9.617 31.786 1.00 12.39

ATOM 619 CD2 PHE B 87 27.610 10.236 31.791 1.00 8.75

ATOM 621 C PHE B 87 23.130 10.717 32.918 1.00 13.46

ATOM 622 O PHE B 87 23.010 11.924 32.776 1.00 15.81

ATOM 624 N PRO B 88 22.092 9.894 33.054 1.00 15.12

ATOM 625 CA PRO B 88 20.745 10.443 33.051 1.00 16.94

ATOM 627 CB PRO B 88 19.859 9.211 33.199 1.00 16.07

ATOM 630 CG PRO B 88 20.711 8.150 33.757 1.00 17.81

ATOM 633 CD PRO B 88 22.090 8.438 33.239 1.00 15.85

ATOM 636 C PRO B 88 20.549 11.404 34.223 1.00 17.79

ATOM 637 O PRO B 88 21.177 11.253 35.277 1.00 17.93

ATOM 638 N SER B 89 19.690 12.391 34.018 1.00 19.34

ATOM 639 CA SER B 89 19.523 13.478 34.981 1.00 21.43

ATOM 641 CB SER B 89 18.439 14.454 34.488 1.00 22.60

ATOM 644 OG SER B 89 18.895 15.122 33.319 1.00 30.68

ATOM 646 C SER B 89 19.157 12.974 36.374 1.00 21.74

ATOM 647 O SER B 89 19.546 13.569 37.373 1.00 23.67 ATOM 649 N GLU B 90 18.403 11.884 36.435 1.00 21.52

ATOM 650 CA GLU B 90 17.929 11.357 37.714 1.00 21.61

ATOM 652 CB GLU B 90 16.789 10.345 37.524 1.00 23.11

ATOM 655 CG GLU B 90 17.118 9.143 36.644 1.00 25.91

ATOM 658 CD GLU B 90 16.814 9.376 35.173 1.00 27.88

ATOM 659 OEl GLU B 90 16.644 10.549 34.748 1.00 25.73

ATOM 660 OE 2 GLU B 90 16.763 8.368 34.437 1.00 31.58

ATOM 661 C GLU B 90 19.016 10.715 38.545 1.00 20.90

ATOM 662 O GLU B 90 18.834 10.501 39.746 1.00 20.34

ATOM 664 N HIS B 91 20.150 10.387 37.925 1.00 19.75

ATOM 665 CA HIS B 91 21.222 9.753 38.675 1.00 19.91

ATOM 667 CB HIS B 91 22.176 9.002 37.750 1.00 19.22

ATOM 670 CG HIS B 91 21.647 7.679 37.308 1.00 21.40

ATOM 671 NDl HIS B 91 22.386 6.794 36.550 1.00 21.88

ATOM 673 CEl HIS B 91 21.662 5.709 36.324 1.00 22.81

ATOM 675 NE 2 HIS B 91 20.485 5.859 36.909 1.00 23.94

ATOM 677 CD2 HIS B 91 20.455 7.077 37.540 1.00 22.99

ATOM 679 C HIS B 91 21.962 10.771 39.519 1.00 20.04

ATOM 680 O HIS B 91 21.993 11.956 39.187 1.00 21.75

ATOM 682 N HIS B 92 22.506 10.307 40.632 1.00 19.58

ATOM 683 CA HIS B 92 23.211 11.178 41.540 1.00 19.93

ATOM 685 CB HIS B 92 23.066 10.700 42.978 1.00 22.06

ATOM 688 CG HIS B 92 21.651 10.459 43.394 1.00 25.78

ATOM 689 NDl HIS B 92 21.259 9.314 44.050 1.00 33.54

ATOM 691 CEl HIS B 92 19.961 9.376 44.292 1.00 34.36

ATOM 693 NE 2 HIS B 92 19.500 10.517 43.811 1.00 32.08

ATOM 695 CD2 HIS B 92 20.539 11.212 43.242 1.00 28.89

ATOM 697 C HIS B 92 24.688 11.177 41.168 1.00 18.29

ATOM 698 O HIS B 92 25.319 10.128 41.091 1.00 18.83

ATOM 700 N LYS B 93 25.235 12.360 40.963 1.00 17.69

ATOM 701 CA LYS B 93 26.656 12.508 40.686 1.00 17.05

ATOM 703 CB LYS B 93 27.039 13.979 40.762 1.00 17.84

ATOM 706 CG LYS B 93 28.508 14.253 40.737 1.00 17.38

ATOM 709 CD LYS B 93 28.766 15.768 40.770 1.00 20.05

ATOM 712 CE LYS B 93 28.550 16.360 42.145 1.00 23.13

ATOM 715 NZ LYS B 93 29.110 17.737 42.275 1.00 22.40

ATOM 719 C LYS B 93 27.500 11.722 41.680 1.00 14.97

ATOM 720 O LYS B 93 28.462 11.089 41.297 1.00 12.90

ATOM 722 N GLU B 94 27.128 11.766 42.961 1.00 14.27

ATOM 723 CA GLU B 94 27.913 11.112 44.028 1.00 13.94

ATOM 725 CB GLU B 94 27.447 11.601 45.409 1.00 15.16

ATOM 728 CG GLU B 94 27.629 13.093 45.625 1.00 20.36

ATOM 731 CD GLU B 94 26.600 13.940 44.875 1.00 27.45

ATOM 732 OEl GLU B 94 25.566 13.391 44.385 1.00 28.28

ATOM 733 OE 2 GLU B 94 26.830 15.164 44.757 1.00 35.53

ATOM 734 C GLU B 94 27.848 9.587 44.005 1.00 13.15

ATOM 735 O GLU B 94 28.586 8.929 44.747 1.00 14.05

ATOM 737 N ALA B 95 26.992 9.023 43.154 1.00 12.26

ATOM 738 CA ALA B 95 26.923 7.564 43.058 1.00 12.50

ATOM 740 CB ALA B 95 25.506 7.103 42.878 1.00 12.59

ATOM 744 C ALA B 95 27.818 7.002 41.964 1.00 12.02

ATOM 745 O ALA B 95 27.876 5.801 41.803 1.00 12.03

ATOM 747 N TYR B 96 28.540 7.869 41.252 1.00 10.01

ATOM 748 CA TYR B 96 29.444 7.404 40.199 1.00 10.56

ATOM 750 CB TYR B 96 29.464 8.414 39.078 1.00 10.99

ATOM 753 CG TYR B 96 28.223 8.428 38.265 1.00 9.89

ATOM 754 CDl TYR B 96 28.039 7.506 37.231 1.00 11.57

ATOM 756 CEl TYR B 96 26.885 7.537 36.441 1.00 9.09

ATOM 758 CZ TYR B 96 25.891 8.460 36.702 1.00 12.15

ATOM 759 OH TYR B 96 24.763 8.459 35.902 1.00 13.52

ATOM 761 CE 2 TYR B 96 26.055 9.387 37.724 1.00 10.30 ATOM 763 CD2 TYR B 96 27.212 9.358 38.505 1.00 12.13

ATOM 765 C TYR B 96 30.861 7.232 40.718 1.00 11.63

ATOM 766 O TYR B 96 31.316 8.001 41.577 1.00 12.00

ATOM 768 N GLU B 97 31.582 6.241 40.194 1.00 11.76

ATOM 769 CA GLU B 97 33.009 6.142 40.430 1.00 12.52

ATOM 771 CB GLU B 97 33.377 4.992 41.335 1.00 13.64

ATOM 774 CG GLU B 97 33.098 5.175 42.778 1.00 20.40

ATOM 111 CD GLU B 97 33.942 4.210 43.626 1.00 18.99

ATOM 778 OEl GLU B 97 33.615 3.018 43.677 1.00 26.71

ATOM 779 OE2 GLU B 97 34.951 4.662 44.230 1.00 32.19

ATOM 780 C GLU B 97 33.677 5.906 39.092 1.00 12.38

ATOM 781 O GLU B 97 33.058 5.380 38.188 1.00 12.99

ATOM 783 N VAL B 98 34.930 6.312 38.983 1.00 11.10

ATOM 784 CA VAL B 98 35.740 6.082 37.790 1.00 10.88

ATOM 786 CB VAL B 98 36.285 7.400 37.210 1.00 11.82

ATOM 788 CGl VAL B 98 37.130 7.131 35.983 1.00 11.78

ATOM 792 CG2 VAL B 98 35.138 8.310 36.872 1.00 10.44

ATOM 796 C VAL B 98 36.907 5.234 38.212 1.00 11.52

ATOM 797 O VAL B 98 37.586 5.580 39.191 1.00 11.29

ATOM 799 N LYS B 99 37.125 4.114 37.512 1.00 10.42

ATOM 800 CA LYS B 99 38.310 3.307 37.756 1.00 9.94

ATOM 802 CB LYS B 99 38.012 1.833 38.060 1.00 9.41

ATOM 805 CG LYS B 99 39.311 1.052 38.310 1.00 11.45

ATOM 808 CD LYS B 99 39.115 -0.170 39.155 1.00 11.29

ATOM 811 CE LYS B 99 38.333 -1.261 38.409 1.00 13.27

ATOM 814 NZ LYS B 99 38.176 -2.537 39.259 1.00 10.84

ATOM 818 C LYS B 99 39.264 3.455 36.577 1.00 9.07

ATOM 819 O LYS B 99 38.881 3.246 35.430 1.00 9.85

ATOM 821 N LEU B 100 40.506 3.819 36.901 1.00 9.76

ATOM 822 CA LEU B 100 41.583 4.063 35.942 1.00 9.92

ATOM 824 CB LEU B 100 42.125 5.495 36.115 1.00 10.43

ATOM 827 CG LEU B 100 41.103 6.651 36.189 1.00 10.72

ATOM 829 CDl LEU B 100 40.733 7.035 37.618 1.00 10.35

ATOM 833 CD2 LEU B 100 41.654 7.841 35.458 1.00 10.99

ATOM 837 C LEU B 100 42.711 3.084 36.220 1.00 11.05

ATOM 838 O LEU B 100 42.873 2.607 37.352 1.00 9.80

ATOM 840 N GLY B 101 43.483 2.777 35.188 1.00 10.90

ATOM 841 CA GLY B 101 44.666 1.942 35.320 1.00 11.62

ATOM 844 C GLY B 101 44.408 0.456 35.453 1.00 12.72

ATOM 845 O GLY B 101 45.353 -0.295 35.700 1.00 14.57

ATOM 847 N ALA B 102 43.157 0.013 35.294 1.00 12.50

ATOM 848 CA ALA B 102 42.852 -1.401 35.442 1.00 15.01

ATOM 850 CB ALA B 102 41.652 -1.599 36.341 1.00 17.11

ATOM 854 C ALA B 102 42.587 -1.996 34.070 1.00 16.52

ATOM 855 O ALA B 102 41.900 -1.384 33.253 1.00 18.21

ATOM 857 N HIS B 103 43.182 -3.153 33.793 1.00 16.64

ATOM 858 CA HIS B 103 42.861 -3.903 32.581 1.00 17.25

ATOM 860 CB HIS B 103 44.118 -4.515 31.946 1.00 20.06

ATOM 863 CG HIS B 103 44.812 -5.508 32.809 1.00 25.87

ATOM 864 NDl HIS B 103 45.404 -5.172 34.011 1.00 32.25

ATOM 866 CEl HIS B 103 45.940 -6.255 34.548 1.00 36.34

ATOM 868 NE2 HIS B 103 45.735 -7.274 33.729 1.00 33.95

ATOM 870 CD2 HIS B 103 45.037 -6.833 32.632 1.00 30.18

ATOM 872 C HIS B 103 41.793 -4.964 32.858 1.00 16.67

ATOM 873 O HIS B 103 40.886 -5.157 32.046 1.00 15.43

ATOM 875 N GLN B 104 41.882 -5.641 34.009 1.00 15.55

ATOM 876 CA GLN B 104 40.845 -6.595 34.398 1.00 16.28

ATOM 878 CB GLN B 104 41.439 -7.873 34.978 1.00 16.05

ATOM 881 CG GLN B 104 41.798 -8.858 33.887 1.00 19.68

ATOM 884 CD GLN B 104 42.644 -10.010 34.346 1.00 20.01

ATOM 885 OEl GLN B 104 42.726 -10.329 35.538 1.00 18.63 ATOM 886 NE2 GLN B 104 43.296 -10.646 33.392 1.00 23.76

ATOM 889 C GLN B 104 39.943 -5.918 35.394 1.00 14.77

ATOM 890 O GLN B 104 40.360 -5.595 36.501 1.00 14.21

ATOM 892 N LEU B 105 38.702 -5.681 35.011 1.00 13.86

ATOM 893 CA LEU B 105 37.799 -4.935 35.883 1.00 15.37

ATOM 895 CB LEU B 105 36.437 -4.682 35.227 1.00 16.28

ATOM 898 CG LEU B 105 36.189 -3.393 34.492 1.00 19.71

ATOM 900 CDl LEU B 105 34.687 -3.214 34.318 1.00 17.96

ATOM 904 CD2 LEU B 105 36.821 -2.180 35.142 1.00 16.61

ATOM 908 C LEU B 105 37.540 -5.635 37.193 1.00 14.43

ATOM 909 O LEU B 105 37.280 -4.969 38.180 1.00 14.94

ATOM 911 N ASP B 106 37.574 -6.968 37.199 1.00 13.24

ATOM 912 CA ASP B 106 37.254 -7.745 38.390 1.00 14.46

ATOM 914 CB ASP B 106 36.281 -8.878 38.054 1.00 14.78

ATOM 917 CG ASP B 106 34.911 -8.387 37.654 1.00 18.62

ATOM 918 ODl ASP B 106 34.609 -7.190 37.852 1.00 21.82

ATOM 919 OD2 ASP B 106 34.119 -9.224 37.137 1.00 21.94

ATOM 920 C ASP B 106 38.490 -8.315 39.082 1.00 14.27

ATOM 921 O ASP B 106 38.385 -9.269 39.849 1.00 14.03

ATOM 923 N SER B 107 39.652 -7.722 38.830 1.00 13.64

ATOM 924 CA SER B 107 40.885 -8.095 39.520 1.00 14.39

ATOM 926 CB SER B 107 41.936 -8.661 38.573 1.00 15.87

ATOM 929 OG SER B 107 41.455 -9.764 37.826 1.00 19.18

ATOM 931 C SER B 107 41.471 -6.871 40.190 1.00 13.29

ATOM 932 O SER B 107 41.605 -5.781 39.583 1.00 13.05

ATOM 934 N TYR B 108 41.844 -7.046 41.454 1.00 12.38

ATOM 935 CA TYR B 108 42.542 -6.020 42.155 1.00 13.19

ATOM 937 CB TYR B 108 42.876 -6.458 43.576 1.00 14.45

ATOM 940 CG TYR B 108 43.810 -5.497 44.246 1.00 15.21

ATOM 941 CDl TYR B 108 43.329 -4.351 44.849 1.00 16.14

ATOM 943 CEl TYR B 108 44.190 -3.436 45.443 1.00 16.91

ATOM 945 CZ TYR B 108 45.552 -3.682 45.421 1.00 15.28

ATOM 946 OH TYR B 108 46.403 -2.796 46.022 1.00 14.96

ATOM 948 CE2 TYR B 108 46.045 -4.806 44.832 1.00 15.77

ATOM 950 CD2 TYR B 108 45.184 -5.714 44.241 1.00 18.78

ATOM 952 C TYR B 108 43.836 -5.714 41.408 1.00 13.94

ATOM 953 O TYR B 108 44.497 -6.615 40.901 1.00 14.12

ATOM 955 N SER B 109 44.171 -4.434 41.325 1.00 13.27

ATOM 956 CA SER B 109 45.442 -4.018 40.786 1.00 13.92

ATOM 958 CB SER B 109 45.325 -3.623 39.311 1.00 14.22

ATOM 961 OG SER B 109 46.559 -3.089 38.896 1.00 15.21

ATOM 963 C SER B 109 46.002 -2.871 41.572 1.00 14.30

ATOM 964 O SER B 109 45.312 -1.888 41.845 1.00 12.76

ATOM 966 N GLU B 110 47.272 -2.997 41.957 1.00 16.45

ATOM 967 CA GLU B 110 47.933 -1.914 42.632 1.00 18.35

ATOM 969 CB GLU B 110 49.289 -2.357 43.157 1.00 19.79

ATOM 972 CG GLU B 110 49.798 -1.409 44.215 1.00 23.06

ATOM 975 CD GLU B 110 51.002 -1.946 44.934 1.00 24.18

ATOM 976 OEl GLU B 110 51.646 -2.880 44.400 1.00 33.47

ATOM 977 OE2 GLU B 110 51.295 -1.410 46.028 1.00 36.07

ATOM 978 C GLU B 110 48.112 -0.703 41.720 1.00 17.47

ATOM 979 O GLU B 110 48.364 0.393 42.193 1.00 18.68

ATOM 981 N ASP B 111 47.999 -0.903 40.410 1.00 16.58

ATOM 982 CA ASP B 111 48.122 0.197 39.472 1.00 15.44

ATOM 984 CB ASP B 111 48.610 -0.318 38.145 1.00 15.22

ATOM 987 CG ASP B 111 49.935 -1.032 38.255 1.00 18.57

ATOM 988 ODl ASP B 111 50.806 -0.500 38.955 1.00 19.89

ATOM 989 OD2 ASP B 111 50.095 -2.105 37.652 1.00 23.10

ATOM 990 C ASP B 111 46.803 0.956 39.238 1.00 15.13

ATOM 991 O ASP B 111 46.798 2.040 38.643 1.00 14.89

ATOM 993 N ALA B 112 45.709 0.383 39.723 1.00 14.20 ATOM 994 CA ALA B 112 44.384 0.949 39.526 1.00 14.25

ATOM 996 CB ALA B 112 43.318 -0.113 39.751 1.00 14.44

ATOM 1000 C ALA B 112 44.170 2.110 40.471 1.00 14.12

ATOM 1001 O ALA B 112 44.659 2.087 41.605 1.00 13.92

ATOM 1003 N LYS B 113 43.441 3.116 40.004 1.00 13.92

ATOM 1004 CA LYS B 113 42.999 4.216 40.844 1.00 14.81

ATOM 1006 CB LYS B 113 43.719 5.497 40.472 1.00 14.81

ATOM 1009 CG LYS B 113 45.240 5.402 40.640 1.00 18.60

ATOM 1012 CD LYS B 113 45.950 6.684 40.223 1.00 20.37

ATOM 1015 CE LYS B 113 47.421 6.673 40.660 1.00 27.12

ATOM 1018 NZ LYS B 113 48.315 7.305 39.663 1.00 30.63

ATOM 1022 C LYS B 113 41.507 4.400 40.663 1.00 14.81

ATOM 1023 O LYS B 113 40.959 4.232 39.557 1.00 14.13

ATOM 1025 N VAL B 114 40.836 4.734 41.750 1.00 14.23

ATOM 1026 CA VAL B 114 39.402 4.933 41.686 1.00 14.59

ATOM 1028 CB VAL B 114 38.668 3.836 42.474 1.00 14.49

ATOM 1030 CGl VAL B 114 37.184 4.031 42.382 1.00 19.63

ATOM 1034 CG2 VAL B 114 39.074 2.464 41.950 1.00 16.75

ATOM 1038 C VAL B 114 39.127 6.333 42.187 1.00 15.19

ATOM 1039 O VAL B 114 39.705 6.776 43.195 1.00 17.79

ATOM 1041 N SER B 115 38.265 7.047 41.474 1.00 13.47

ATOM 1042 CA ASER B 115 37.986 8.442 41.760 0.50 13.60

ATOM 1043 CA BSER B 115 37.969 8.430 41.801 0.50 13.66

ATOM 1046 CB ASER B 115 38.644 9.333 40.701 0.50 13.95

ATOM 1047 CB BSER B 115 38.657 9.378 40.825 0.50 13.99

ATOM 1052 OG ASER B 115 40.045 9.089 40.579 0.50 12.26

ATOM 1053 OG BSER B 115 38.290 10.725 41.088 0.50 12.89

ATOM 1056 C SER B 115 36.482 8.668 41.747 1.00 13.17

ATOM 1057 O SER B 115 35.767 7.997 41.023 1.00 14.11

ATOM 1059 N THR B 116 36.028 9.631 42.540 1.00 11.86

ATOM 1060 CA THR B 116 34.670 10.106 42.488 1.00 12.36

ATOM 1062 CB THR B 116 34.159 10.537 43.853 1.00 14.30

ATOM 1064 OGl THR B 116 35.078 11.458 44.454 1.00 15.52

ATOM 1066 CG2 THR B 116 33.984 9.342 44.713 1.00 14.85

ATOM 1070 C THR B 116 34.634 11.279 41.541 1.00 12.14

ATOM 1071 O THR B 116 35.679 11.681 41.063 1.00 11.25

ATOM 1073 N LEU B 117 33.434 11.811 41.277 1.00 11.97

ATOM 1074 CA LEU B 117 33.239 12.897 40.328 1.00 12.43

ATOM 1076 CB LEU B 117 32.134 12.532 39.355 1.00 13.23

ATOM 1079 CG LEU B 117 32.410 11.360 38.417 1.00 13.07

ATOM 1081 CDl LEU B 117 31.251 11.205 37.424 1.00 14.18

ATOM 1085 CD2 LEU B 117 33.731 11.609 37.706 1.00 11.89

ATOM 1089 C LEU B 117 32.817 14.170 41.037 1.00 13.87

ATOM 1090 O LEU B 117 31.949 14.136 41.922 1.00 14.30

ATOM 1092 N LYS B 118 33.377 15.295 40.618 1.00 14.86

ATOM 1093 CA LYS B 118 32.917 16.573 41.143 1.00 15.25

ATOM 1095 CB LYS B 118 34.068 17.427 41.634 1.00 16.97

ATOM 1098 CG LYS B 118 35.028 17.864 40.607 1.00 17.32

ATOM 1101 CD LYS B 118 36.068 18.807 41.201 1.00 19.66

ATOM 1104 CE LYS B 118 35.441 20.152 41.574 1.00 24.45

ATOM 1107 NZ LYS B 118 36.431 21.174 41.987 1.00 26.82

ATOM 1111 C LYS B 118 32.038 17.353 40.184 1.00 15.72

ATOM 1112 O LYS B 118 31.366 18.289 40.599 1.00 14.32

ATOM 1114 N ASP B 119 31.985 16.947 38.921 1.00 14.58

ATOM 1115 CA ASP B 119 31. Ill 17.598 37.973 1.00 14.81

ATOM 1117 CB ASP B 119 31.822 18.825 37.391 1.00 15.71

ATOM 1120 CG ASP B 119 30.857 19.920 36.947 1.00 19.90

ATOM 1121 ODl ASP B 119 29.612 19.784 37.087 1.00 22.87

ATOM 1122 OD2 ASP B 119 31.366 20.945 36.470 1.00 26.95

ATOM 1123 C ASP B 119 30.805 16.619 36.845 1.00 13.37

ATOM 1124 O ASP B 119 31.659 15.816 36.462 1.00 13.20 ATOM 1126 N ILE B 120 29.592 16.696 36.328 1.00 13.84

ATOM 1127 CA ILE B 120 29.205 15.994 35.104 1.00 12.46

ATOM 1129 CB ILE B 120 28.177 14.888 35.413 1.00 13.40

ATOM 1131 CGl ILE B 120 28.754 13.872 36.394 1.00 12.05

ATOM 1134 CDl ILE B 120 27.725 12.850 36.896 1.00 12.28

ATOM 1138 CG2 ILE B 120 27.676 14.220 34.133 1.00 13.45

ATOM 1142 C ILE B 120 28.562 17.030 34.214 1.00 12.55

ATOM 1143 O ILE B 120 27.644 17.704 34.636 1.00 12.65

ATOM 1145 N ILE B 121 29.061 17.199 33.006 1.00 11.88

ATOM 1146 CA ILE B 121 28.569 18.237 32.132 1.00 12.10

ATOM 1148 CB ILE B 121 29.624 19.307 31.871 1.00 12.62

ATOM 1150 CGl ILE B 121 30.249 19.784 33.189 1.00 14.19

ATOM 1153 CDl ILE B 121 31.274 20.856 33.033 1.00 14.41

ATOM 1157 CG2 ILE B 121 28.996 20.438 31.088 1.00 14.25

ATOM 1161 C ILE B 121 28.186 17.573 30.825 1.00 11.55

ATOM 1162 O ILE B 121 29.067 17.346 29.963 1.00 10.67

ATOM 1164 N PRO B 122 26.903 17.230 30.676 1.00 11.79

ATOM 1165 CA PRO B 122 26.482 16.686 29.382 1.00 11.87

ATOM 1167 CB PRO B 122 25.110 16.109 29.678 1.00 13.55

ATOM 1170 CG PRO B 122 24.575 16.978 30.754 1.00 16.06

ATOM 1173 CD PRO B 122 25.768 17.309 31.617 1.00 12.06

ATOM 1176 C PRO B 122 26.372 17.809 28.384 1.00 13.87

ATOM 1177 O PRO B 122 26.135 18.972 28.783 1.00 13.02

ATOM 1178 N HIS B 123 26.485 17.480 27.102 1.00 12.29

ATOM 1179 CA HIS B 123 26.230 18.476 26.096 1.00 14.15

ATOM 1181 CB HIS B 123 26.555 17.989 24.691 1.00 13.72

ATOM 1184 CG HIS B 123 26.669 19.119 23.731 1.00 13.39

ATOM 1185 NDl HIS B 123 25.577 19.637 23.070 1.00 16.48

ATOM 1187 CEl HIS B 123 25.965 20.673 22.346 1.00 17.76

ATOM 1189 NE2 HIS B 123 27.256 20.863 22.543 1.00 16.96

ATOM 1191 CD2 HIS B 123 27.713 19.917 23.426 1.00 16.10

ATOM 1193 C HIS B 123 24.781 18.942 26.197 1.00 13.70

ATOM 1194 O HIS B 123 23.877 18.133 26.413 1.00 12.78

ATOM 1196 N PRO B 124 24.565 20.262 26.119 1.00 15.92

ATOM 1197 CA PRO B 124 23.198 20.763 26.293 1.00 17.01

ATOM 1199 CB PRO B 124 23.375 22.285 26.247 1.00 18.56

ATOM 1202 CG PRO B 124 24.663 22.507 25.576 1.00 20.06

ATOM 1205 CD PRO B 124 25.528 21.358 25.967 1.00 16.05

ATOM 1208 C PRO B 124 22.206 20.284 25.224 1.00 17.86

ATOM 1209 O PRO B 124 21.011 20.202 25.511 1.00 18.46

ATOM 1210 N SER B 125 22.699 19.934 24.033 1.00 16.16

ATOM 1211 CA SER B 125 21.848 19.408 22.986 1.00 16.55

ATOM 1213 CB SER B 125 22.586 19.407 21.648 1.00 16.26

ATOM 1216 OG SER B 125 23.590 18.410 21.636 1.00 14.15

ATOM 1218 C SER B 125 21.320 18.005 23.303 1.00 17.81

ATOM 1219 O SER B 125 20.392 17.504 22.638 1.00 18.52

ATOM 1221 N TYR B 126 21.899 17.354 24.309 1.00 17.71

ATOM 1222 CA TYR B 126 21.519 15.975 24.589 1.00 18.37

ATOM 1224 CB TYR B 126 22.508 15.314 25.537 1.00 17.27

ATOM 1227 CG TYR B 126 22.099 13.890 25.776 1.00 17.59

ATOM 1228 CDl TYR B 126 22.161 12.962 24.747 1.00 17.78

ATOM 1230 CEl TYR B 126 21.744 11.658 24.935 1.00 18.27

ATOM 1232 CZ TYR B 126 21.247 11.276 26.160 1.00 19.90

ATOM 1233 OH TYR B 126 20.814 9.985 26.344 1.00 23.31

ATOM 1235 CE2 TYR B 126 21.149 12.184 27.194 1.00 19.29

ATOM 1237 CD2 TYR B 126 21.569 13.490 26.995 1.00 19.13

ATOM 1239 C TYR B 126 20.106 15.808 25.178 1.00 20.44

ATOM 1240 O TYR B 126 19.789 16.401 26.199 1.00 21.22

ATOM 1242 N LEU B 127 19.301 14.966 24.538 1.00 21.28

ATOM 1243 CA LEU B 127 18.005 14.552 25.060 1.00 23.66

ATOM 1245 CB LEU B 127 16.896 14.995 24.121 1.00 25.75 ATOM 1248 CG LEU B 127 16.769 16.493 23.803 1.00 30.62

ATOM 1250 CDl LEU B 127 17.244 17.439 24.948 1.00 33.76

ATOM 1254 CD2 LEU B 127 17.503 16.811 22.518 1.00 33.53

ATOM 1258 C LEU B 127 17.983 13.026 25.204 1.00 24.23

ATOM 1259 O LEU B 127 18.363 12.312 24.285 1.00 21.78

ATOM 1261 N GLN B 128 17.522 12.536 26.351 1.00 24.83

ATOM 1262 CA GLN B 128 17.488 11.092 26.605 1.00 25.07

ATOM 1264 CB GLN B 128 16.902 10.795 27.991 1.00 25.99

ATOM 1267 CG GLN B 128 17.334 9.464 28.588 1.00 27.48

ATOM 1270 CD GLN B 128 18.820 9.391 28.964 1.00 32.13

ATOM 1271 OEl GLN B 128 19.481 8.387 28.709 1.00 37.47

ATOM 1272 NE2 GLN B 128 19.333 10.439 29.584 1.00 32.36

ATOM 1275 C GLN B 128 16.681 10.361 25.516 1.00 24.91

ATOM 1276 O GLN B 128 15.607 10.816 25.129 1.00 25.90

ATOM 1278 N GLU B 129 17.225 9.239 25.042 1.00 24.79

ATOM 1279 CA GLU B 129 16.650 8.417 23.954 1.00 25.09

ATOM 1281 CB GLU B 129 15.180 8.061 24.230 1.00 26.51

ATOM 1284 CG GLU B 129 14.940 7.447 25.594 1.00 30.92

ATOM 1287 CD GLU B 129 15.923 6.340 25.910 1.00 38.17

ATOM 1288 OEl GLU B 129 16.149 5.476 25.035 1.00 43.50

ATOM 1289 OE2 GLU B 129 16.479 6.342 27.034 1.00 45.82

ATOM 1290 C GLU B 129 16.809 9.014 22.542 1.00 23.83

ATOM 1291 O GLU B 129 16.335 8.442 21.554 1.00 21.76

ATOM 1293 N GLY B 130 17.497 10.146 22.458 1.00 22.12

ATOM 1294 CA GLY B 130 17.806 10.793 21.190 1.00 21.77

ATOM 1297 C GLY B 130 19.289 10.611 20.908 1.00 21.57

ATOM 1298 O GLY B 130 20.083 10.339 21.835 1.00 19.94

ATOM 1300 N SER B 131 19.672 10.756 19.634 1.00 19.01

ATOM 1301 CA SER B 131 21.041 10.516 19.217 1.00 17.52

ATOM 1303 CB SER B 131 21.066 9.996 17.767 1.00 15.77

ATOM 1306 OG SER B 131 20.521 10.964 16.898 1.00 15.45

ATOM 1308 C SER B 131 21.955 11.742 19.384 1.00 15.88

ATOM 1309 O SER B 131 23.099 11.589 19.731 1.00 15.14

ATOM 1311 N GLN B 132 21.437 12.939 19.156 1.00 16.27

ATOM 1312 CA GLN B 132 22.243 14.160 19.154 1.00 15.80

ATOM 1314 CB GLN B 132 21.335 15.353 18.855 1.00 18.55

ATOM 1317 CG GLN B 132 22.058 16.643 18.608 1.00 21.23

ATOM 1320 CD GLN B 132 22.675 16.714 17.227 1.00 29.67

ATOM 1321 OEl GLN B 132 21.969 16.877 16.211 1.00 40.28

ATOM 1322 NE2 GLN B 132 23.991 16.607 17.170 1.00 36.72

ATOM 1325 C GLN B 132 22.968 14.449 20.472 1.00 13.65

ATOM 1326 O GLN B 132 22.394 14.302 21.532 1.00 13.79

ATOM 1328 N GLY B 133 24.220 14.874 20.387 1.00 12.91

ATOM 1329 CA GLY B 133 24.948 15.390 21.541 1.00 12.30

ATOM 1332 C GLY B 133 25.318 14.383 22.619 1.00 10.22

ATOM 1333 O GLY B 133 25.378 14.739 23.796 1.00 9.21

ATOM 1335 N ASP B 134 25.600 13.136 22.229 1.00 9.93

ATOM 1336 CA ASP B 134 25.841 12.074 23.215 1.00 9.92

ATOM 1338 CB ASP B 134 25.549 10.697 22.640 1.00 9.71

ATOM 1341 CG ASP B 134 25.414 9.651 23.716 1.00 8.48

ATOM 1342 ODl ASP B 134 25.431 10.055 24.900 1.00 8.87

ATOM 1343 OD2 ASP B 134 25.279 8.438 23.376 1.00 8.92

ATOM 1344 C ASP B 134 27.275 12.141 23.724 1.00 9.89

ATOM 1345 O ASP B 134 28.130 11.350 23.362 1.00 8.03

ATOM 1347 N ILE B 135 27.530 13.118 24.581 1.00 8.97

ATOM 1348 CA ILE B 135 28.869 13.404 25.040 1.00 9.12

ATOM 1350 CB ILE B 135 29.673 14.219 23.978 1.00 10.25

ATOM 1352 CGl ILE B 135 31.099 14.470 24.446 1.00 10.06

ATOM 1355 CDl ILE B 135 31.953 15.031 23.334 1.00 9.26

ATOM 1359 CG2 ILE B 135 28.957 15.524 23.611 1.00 12.55

ATOM 1363 C ILE B 135 28.748 14.181 26.328 1.00 7.64 ATOM 1364 O ILE B 135 27.822 14.973 26.489 1.00 9.41

ATOM 1366 N ALA B 136 29.643 13.881 27.253 1.00 7.95

ATOM 1367 CA ALA B 136 29.646 14.480 28.562 1.00 8.58

ATOM 1369 CB ALA B 136 28.837 13.657 29.511 1.00 9.36

ATOM 1373 C ALA B 136 31.057 14.591 29.072 1.00 9.01

ATOM 1374 O ALA B 136 31.861 13.682 28. 1.00 10.16

ATOM 1376 N LEU B 137 31.341 15.718 29.702 1.00 8.26

ATOM 1377 CA LEU B 137 32.604 15.932 30.419 1.00 9.17

ATOM 1379 CB LEU B 137 33.044 17.398 30.323 1.00 9.97

ATOM 1382 CG LEU B 137 33.625 17.804 28.961 1.00 11.87

ATOM 1384 CDl LEU B 137 33.508 19.300 28.765 1.00 13.80

ATOM 1388 CD2 LEU B 137 35.065 17.328 28.848 1.00 14.21

ATOM 1392 C LEU B 137 32.429 15.589 31.881 1.00 9.32

ATOM 1393 O LEU B 137 31.437 16.004 32.500 1.00 9.54

ATOM 1395 N LEU B 138 33.377 14.833 32.421 1.00 8.56

ATOM 1396 CA LEU B 138 33.352 14.404 33.813 1.00 9.09

ATOM 1398 CB LEU B 138 33.374 12.893 33.917 1.00 8.73

ATOM 1401 CG LEU B 138 32.395 12.134 33.018 1.00 10.72

ATOM 1403 CDl LEU B 138 32.589 10.641 33.307 1.00 10.61

ATOM 1407 CD2 LEU B 138 30.964 12.539 33.270 1.00 11.82

ATOM 1411 C LEU B 138 34.609 14.927 34.467 1.00 10.74

ATOM 1412 O LEU B 138 35.711 14.683 33.998 1.00 11.43

ATOM 1414 N GLN B 139 34.444 15.607 35.588 1.00 11.08

ATOM 1415 CA GLN B 139 35.584 16.092 36.338 1.00 11.20

ATOM 1417 CB GLN B 139 35.332 17.499 36.819 1.00 11.73

ATOM 1420 CG GLN B 139 36.558 18.122 37.450 1.00 13.63

ATOM 1423 CD GLN B 139 36.314 19.564 37.853 1.00 13.61

ATOM 1424 OEl GLN B 139 35.185 19.969 38.167 1.00 19.71

ATOM 1425 NE 2 GLN B 139 37.388 20.336 37.886 1.00 21.72

ATOM 1428 C GLN B 139 35.758 15.212 37.550 1.00 10.67

ATOM 1429 O GLN B 139 34.822 15.034 38.314 1.00 11.00

ATOM 1431 N LEU B 140 36.943 14.654 37.703 1.00 10.62

ATOM 1432 CA LEU B 140 37.263 13.805 38.843 1.00 10.82

ATOM 1434 CB LEU B 140 38.605 13.116 38.602 1.00 11.42

ATOM 1437 CG LEU B 140 38.743 12.303 37.316 1.00 12.16

ATOM 1439 CDl LEU B 140 40.116 11.683 37.218 1.00 13.20

ATOM 1443 CD2 LEU B 140 37.619 11.289 37.288 1.00 13.09

ATOM 1447 C LEU B 140 37.379 14.706 40.078 1.00 11.54

ATOM 1448 O LEU B 140 37.780 15.871 39.970 1.00 11.60

ATOM 1450 N SER B 141 37.043 14.170 41.240 1.00 12.53

ATOM 1451 CA SER B 141 37.064 14.972 42.478 1.00 13.86

ATOM 1453 CB SER B 141 36.572 14.131 43.646 1.00 13.63

ATOM 1456 OG SER B 141 35.193 13.895 43.458 1.00 13.43

ATOM 1458 C SER B 141 38.433 15.567 42.784 1.00 16.14

ATOM 1459 O SER B 141 38.527 16.679 43.349 1.00 17.73

ATOM 1461 N ARG B 142 39.465 14.832 42.394 1.00 16.96

ATOM 1462 CA ARG B 142 40.850 15.226 42.524 1.00 18.36

ATOM 1464 CB ARG B 142 41.461 14.545 43.745 1.00 19.78

ATOM 1467 CG ARG B 142 40.905 15.013 45.094 1.00 24.03

ATOM 1470 CD ARG B 142 41.301 16.440 45.391 1.00 30.64

ATOM 1473 NE ARG B 142 42.756 16.608 45.337 1.00 34.64

ATOM 1475 CZ ARG B 142 43.390 17.748 45.059 1.00 35.07

ATOM 1476 NHl ARG B 142 42.716 18.868 44.787 1.00 33.97

ATOM 1479 NH2 ARG B 142 44.717 17.757 45.023 1.00 32.05

ATOM 1482 C ARG B 142 41.629 14.783 41.305 1.00 18.24

ATOM 1483 O ARG B 142 41.335 13.735 40.716 1.00 17.15

ATOM 1485 N PRO B 143 42.666 15.545 40.941 1.00 19.11

ATOM 1486 CA PRO B 143 43.498 15.110 39.826 1 .00 19.49

ATOM 1488 CB PRO B 143 44.514 16.240 39.672 .00 20.83

ATOM 1491 CG PRO B 143 44.549 16.890 40.992 1.00 23.14

ATOM 1494 CD PRO B 143 43.146 16.813 41.516 1.00 18.99 ATOM 1497 C PRO B 143 44.197 13.800 40.130 1.00 19.74

ATOM 1498 O PRO B 143 44.508 13.506 41.294 1.00 20.73

ATOM 1499 N ILE B 144 44.438 13.008 39.102 1.00 20.05

ATOM 1500 CA ILE B 144 45.147 11.748 39.298 1.00 20.75

ATOM 1502 CB ILE B 144 44.398 10.539 38.683 1.00 22.78

ATOM 1504 CGl ILE B 144 44.079 10.741 37.209 1.00 23.97

ATOM 1507 CDl ILE B 144 45.279 10.853 36.272 1.00 26.71

ATOM 1511 CG2 ILE B 144 43.080 10.311 39.436 1.00 24.77

ATOM 1515 C ILE B 144 46.587 11.882 38.794 1.00 21.65

ATOM 1516 O ILE B 144 46.892 12.780 38.009 1.00 23.63

ATOM 1518 N THR B 145 47.474 11.027 39.294 1.00 20.58

ATOM 1519 CA THR B 145 48.850 10.999 38.835 1.00 19.82

ATOM 1521 CB THR B 145 49.802 10.556 39.969 1.00 20.46

ATOM 1523 OGl THR B 145 49.720 11.500 41.037 1.00 24.98

ATOM 1525 CG2 THR B 145 51.232 10.485 39.490 1.00 22.44

ATOM 1529 C THR B 145 48.940 10.007 37.693 1.00 18.43

ATOM 1530 O THR B 145 48.432 8.890 37.795 1.00 19.16

ATOM 1532 N PHE B 146 49.574 10.413 36.605 1.00 17.17

ATOM 1533 CA PHE B 146 49.754 9.526 35.490 1.00 15.91

ATOM 1535 CB PHE B 146 50.187 10.287 34.248 1.00 15.69

ATOM 1538 CG PHE B 146 49.220 11.355 33.792 1.00 14.82

ATOM 1539 CDl PHE B 146 47.843 11.206 33.927 1.00 15.38

ATOM 1541 CEl PHE B 146 46.980 12.188 33.494 1.00 18.07

ATOM 1543 CZ PHE B 146 47.480 13.323 32.906 1.00 16.40

ATOM 1545 CE2 PHE B 146 48.836 13.473 32.763 1.00 16.96

ATOM 1547 CD2 PHE B 146 49.693 12.500 33.194 1.00 16.92

ATOM 1549 C PHE B 146 50.765 8.421 35.804 1.00 16.77

ATOM 1550 O PHE B 146 51.577 8.532 36.730 1.00 17.42

ATOM 1552 N SER B 147 50.687 7.347 35.031 1.00 15.03

ATOM 1553 CA SER B 147 51.576 6.199 35.147 1.00 14.30

ATOM 1555 CB SER B 147 51.072 5.222 36.217 1.00 13.94

ATOM 1558 OG SER B 147 49.884 4.591 35.789 1.00 13.21

ATOM 1560 C SER B 147 51.607 5.497 33.799 1.00 14.58

ATOM 1561 O SER B 147 50.937 5.929 32.867 1.00 13.28

ATOM 1563 N ARG B 148 52.349 4.402 33.713 1.00 16.00

ATOM 1564 CA ARG B 148 52.316 3.543 32.538 1.00 16.09

ATOM 1566 CB ARG B 148 53.164 2.287 32.783 1.00 18.00

ATOM 1569 CG ARG B 148 53.078 1.268 31.703 1.00 19.95

ATOM 1572 CD ARG B 148 54.039 0.086 31.943 1.00 22.76

ATOM 1575 NE ARG B 148 53.843 -0.925 30.899 1.00 31.48

ATOM 1577 CZ ARG B 148 54.444 -2.114 30.846 1.00 37.32

ATOM 1578 NHl ARG B 148 55.319 -2.490 31.781 1.00 40.68

ATOM 1581 NH2 ARG B 148 54.162 -2.939 29.841 1.00 37.41

ATOM 1584 C ARG B 148 50.874 3.133 32.222 1.00 14.93

ATOM 1585 O ARG B 148 50.510 2.914 31.069 1.00 15.11

ATOM 1587 N TYR B 149 50.053 3.030 33.260 1.00 11.46

ATOM 1588 CA TYR B 149 48.709 2.502 33.119 1.00 11.21

ATOM 1590 CB TYR B 149 48.441 1.545 34.268 1.00 11.96

ATOM 1593 CG TYR B 149 49.516 0.501 34.325 1.00 13.50

ATOM 1594 CDl TYR B 149 49.556 -0.514 33.384 1.00 15.09

ATOM 1596 CEl TYR B 149 50.549 -1.465 33.392 1.00 17.49

ATOM 1598 CZ TYR B 149 51.548 -1.379 34.337 1.00 18.79

ATOM 1599 OH TYR B 149 52.537 -2.341 34.334 1.00 21.30

ATOM 1601 CE2 TYR B 149 51.550 -0.352 35.269 1.00 15.82

ATOM 1603 CD2 TYR B 149 50.544 0.586 35.247 1.00 15.57

ATOM 1605 C TYR B 149 47.622 3.554 33.041 1.00 10.41

ATOM 1606 O TYR B 149 46.468 3.215 32.777 1.00 10.68

ATOM 1608 N ILE B 150 47.991 4.811 33.291 1.00 9.40

ATOM 1609 CA ILE B 150 47.024 5.898 33.346 1.00 10.51

ATOM 1611 CB ILE B 150 46.712 6.268 34.783 1.00 10.20

ATOM 1613 CGl ILE B 150 46.207 5.049 35.573 1.00 11.82 ATOM 1616 CDl ILE B 150 45.963 5.322 37.035 1.00 11.20

ATOM 1620 CG2 ILE B 150 45.714 7.443 34.820 1.00 11.11

ATOM 1624 C ILE B 150 47.595 7.120 32.644 1.00 11.63

ATOM 1625 O ILE B 150 48.485 7.780 33.166 1.00 11.75

ATOM 1627 N ARG B 151 47.075 7.413 31.456 1.00 10.15

ATOM 1628 CA ARG B 151 47.581 8.500 30.627 1.00 10.85

ATOM 1630 CB ARG B 151 48.629 7.971 29.655 1.00 11.44

ATOM 1633 CG ARG B 151 49.911 7.536 30.287 1.00 18.68

ATOM 1636 CD ARG B 151 50.760 8.728 30.586 1.00 32.30

ATOM 1639 NE ARG B 151 52.049 8.365 31.147 1.00 36.84

ATOM 1641 CZ ARG B 151 52.932 9.249 31.589 1.00 39.39

ATOM 1642 NHl ARG B 151 52.683 10.555 31.514 1.00 41.55

ATOM 1645 NH2 ARG B 151 54.081 8.828 32.088 1.00 42.34

ATOM 1648 C ARG B 151 46.464 9.026 29.796 1.00 10.59

ATOM 1649 O ARG B 151 45.625 8.270 29.354 1.00 10.23

ATOM 1651 N PRO B 152 46.461 10.323 29.544 1.00 8.50

ATOM 1652 CA PRO B 152 45.390 10.930 28.758 1.00 9.15

ATOM 1654 CB PRO B 152 45.499 12.404 29.117 1.00 10.31

ATOM 1657 CG PRO B 152 46.950 12.606 29.444 1.00 12.16

ATOM 1660 CD PRO B 152 47.444 11.313 30.024 1.00 9.91

ATOM 1663 C PRO B 152 45.537 10.695 27.236 1.00 10.67

ATOM 1664 O PRO B 152 46.645 10.482 26.729 1.00 10.34

ATOM 1665 N ILE B 153 44.415 10.697 26.536 1.00 10.23

ATOM 1666 CA ILE B 153 44.430 10.723 25.080 1.00 9.94

ATOM 1668 CB ILE B 153 43.395 9.743 24.490 1.00 10.33

ATOM 1670 CGl ILE B 153 43.538 9.647 22.958 1.00 7.53

ATOM 1673 CDl ILE B 153 42.764 8.528 22.336 1.00 9.85

ATOM 1677 CG2 ILE B 153 41.988 10.133 24.877 1.00 9.80

ATOM 1681 C ILE B 153 44.207 12.145 24.574 1.00 9.50

ATOM 1682 O ILE B 153 43.450 12.909 25.163 1.00 8.46

ATOM 1684 N SER B 154 44.849 12.462 23.444 1.00 8.64

ATOM 1685 CA SER B 154 44.709 13.749 22.808 1.00 9.73

ATOM 1687 CB SER B 154 45.737 13.901 21.677 1.00 11.28

ATOM 1690 OG SER B 154 47.059 13.893 22.195 1.00 12.24

ATOM 1692 C SER B 154 43.314 13.891 22.234 1.00 9.81

ATOM 1693 O SER B 154 42.779 12.956 21.623 1.00 10.18

ATOM 1695 N LEU B 155 42.721 15.052 22.481 1.00 10.33

ATOM 1696 CA LEU B 155 41.483 15.447 21.831 1.00 10.35

ATOM 1698 CB LEU B 155 40.753 16.482 22.690 1.00 9.86

ATOM 1701 CG LEU B 155 40.200 15.912 23.984 1.00 14.12

ATOM 1703 CDl LEU B 155 39.812 17.033 24.913 1.00 17.05

ATOM 1707 CD2 LEU B 155 39.003 14.996 23.699 1.00 17.88

ATOM 1711 C LEU B 155 41.776 16.056 20.469 1.00 11.00

ATOM 1712 O LEU B 155 42.697 16.883 20.330 1.00 12.01

ATOM 1714 N PRO B 156 40.981 15.693 19.461 1.00 11.05

ATOM 1715 CA PRO B 156 41.172 16.301 18.140 1.00 10.99

ATOM 1717 CB PRO B 156 40.476 15.331 17.207 1.00 11.17

ATOM 1720 CG PRO B 156 39.392 14.711 18.051 1.00 11.29

ATOM 1723 CD PRO B 156 39.854 14.740 19.481 1.00 11.82

ATOM 1726 C PRO B 156 40.556 17.701 18.100 1.00 12.21

ATOM 1727 O PRO B 156 39.452 17.926 18.598 1.00 10.60

ATOM 1728 N ALA B 157 41.295 18.633 17.507 1.00 12.76

ATOM 1729 CA ALA B 157 40.834 20.002 17.322 1.00 12.80

ATOM 1731 CB ALA B 157 41.979 20.878 16.840 1.00 15.24

ATOM 1735 C ALA B 157 39.682 20.023 16.321 1.00 13.06

ATOM 1736 O ALA B 157 39.487 19.083 15.566 1.00 12.46

ATOM 1738 N ALA B 158 38.941 21.121 16.329 1.00 13.87

ATOM 1739 CA ALA B 158 37.727 21.271 15.557 1.00 15.04

ATOM 1741 CB ALA B 158 37.211 22.722 15.701 1.00 16.79

ATOM 1745 C ALA B 158 37.863 20.905 14.077 1.00 16.72

ATOM 1746 O ALA B 158 36.933 20.341 13.488 1.00 19.13 ATOM 1748 N GLN B 159 38.999 21.218 13.469 1.00 15.55

ATOM 1749 CA GLN B 159 39.158 20.971 12.025 1.00 16.82

ATOM 1751 CB GLN B 159 39.954 22.114 11.399 1.00 16.65

ATOM 1754 CG GLN B 159 39.224 23.420 11.429 1.00 17.44

ATOM 1757 CD GLN B 159 39.924 24.476 10.607 1.00 16.16

ATOM 1758 OEl GLN B 159 41.104 24.810 10.864 1.00 19.56

ATOM 1759 NE2 GLN B 159 39.227 24.979 9.574 1.00 15.93

ATOM 1762 C GLN B 159 39.835 19.644 11.689 1.00 17.13

ATOM 1763 O GLN B 159 40.224 19.398 10.537 1.00 16.33

ATOM 1765 N ALA B 160 39.998 18.784 12.679 1.00 16.43

ATOM 1766 CA ALA B 160 40.693 17.518 12.453 1.00 16.99

ATOM 1768 CB ALA B 160 40.912 16.790 13.781 1.00 16.73

ATOM 1772 C ALA B 160 39.900 16.641 11.490 1.00 17.20

ATOM 1773 O ALA B 160 38.690 16.564 11.566 1.00 19.24

ATOM 1775 N SER B 161 40.579 15.988 10.563 1.00 18.19

ATOM 1776 CA SER B 161 39.912 15.031 9.700 1.00 17.70

ATOM 1778 CB SER B 161 39.867 15.526 8.259 1.00 19.58

ATOM 1781 OG SER B 161 41.181 15.729 7.775 1.00 28.06

ATOM 1783 C SER B 161 40.690 13.739 9.795 1.00 17.08

ATOM 1784 O SER B 161 41.926 13.741 9.818 1.00 18.59

ATOM 1786 N PHE B 162 39.964 12.638 9.909 1.00 13.53

ATOM 1787 CA PHE B 162 40.567 11.316 9.933 1.00 12.84

ATOM 1789 CB PHE B 162 40.166 10.571 11.189 1.00 11.57

ATOM 1792 CG PHE B 162 40.651 11.238 12.433 1.00 8.48

ATOM 1793 CDl PHE B 162 41.873 10.902 12.965 1.00 9.43

ATOM 1795 CEl PHE B 162 42.347 11.500 14.083 1.00 11.22

ATOM 1797 CZ PHE B 162 41.588 12.471 14.695 1.00 9.58

ATOM 1799 CE2 PHE B 162 40.345 12.845 14.157 1.00 9.57

ATOM 1801 CD2 PHE B 162 39.892 12.210 13.033 1.00 8.24

ATOM 1803 C PHE B 162 40.058 10.627 8.693 1.00 12.89

ATOM 1804 O PHE B 162 38.848 10.663 8.422 1.00 13.39

ATOM 1806 N PRO B 163 40.974 10.070 7.897 1.00 13.02

ATOM 1807 CA PRO B 163 40.578 9.554 6.600 1.00 13.33

ATOM 1809 CB PRO B 163 41.912 9.141 5.964 1.00 14.46

ATOM 1812 CG PRO B 163 42.849 9.018 7.027 1.00 16.82

ATOM 1815 CD PRO B 163 42.420 9.938 8.131 1.00 13.65

ATOM 1818 C PRO B 163 39.633 8.372 6.686 1.00 13.19

ATOM 1819 O PRO B 163 39.788 7.485 7.548 1.00 12.33

ATOM 1820 N ASN B 164 38.656 8.332 5.778 1.00 13.26

ATOM 1821 CA ASN B 164 37.850 7.137 5.687 1.00 12.47

ATOM 1823 CB ASN B 164 36.853 7.252 4.542 1.00 13.60

ATOM 1826 CG ASN B 164 35.867 8.399 4.742 1.00 14.75

ATOM 1827 ODl ASN B 164 35.518 8.755 5.874 1.00 18.30

ATOM 1828 ND2 ASN B 164 35.450 9.010 3.645 1.00 20.50

ATOM 1831 C ASN B 164 38.751 5.911 5.516 1.00 12.68

ATOM 1832 O ASN B 164 39.754 5.967 4.811 1.00 12.61

ATOM 1834 N GLY B 165 38.380 4.809 6.157 1.00 12.20

ATOM 1835 CA GLY B 165 39.130 3.564 6.071 1.00 11.46

ATOM 1838 C GLY B 165 40.258 3.399 7.085 1.00 10.79

ATOM 1839 O GLY B 165 40.799 2.305 7.214 1.00 11.94

ATOM 1841 N LEU B 166 40.626 4.474 7.786 1.00 9.44

ATOM 1842 CA LEU B 166 41.621 4.375 8.843 1.00 10.45

ATOM 1844 CB LEU B 166 41.810 5.736 9.514 1.00 9.95

ATOM 1847 CG LEU B 166 42.797 5.818 10.681 1.00 9.00

ATOM 1849 CDl LEU B 166 44.188 5.345 10.285 1.00 9.15

ATOM 1853 CD2 LEU B 166 42.853 7.185 11.255 1.00 10.25

ATOM 1857 C LEU B 166 41.156 3.366 9.879 1.00 10.16

ATOM 1858 O LEU B 166 40.031 3.450 10.358 1.00 11.04

ATOM 1860 N HIS B 167 42.040 2.455 10.252 1.00 10.47

ATOM 1861 CA HIS B 167 41.754 1.508 11.289 1.00 10.83

ATOM 1863 CB HIS B 167 42.557 0.247 11.070 1.00 12.49 ATOM 1866 CG HIS B 167 42.104 -0.533 9.882 1.00 16.99

ATOM 1867 NDl HIS B 167 42.343 -1.883 9.746 1.00 21.32

ATOM 1869 CEl HIS B 167 41.838 -2.298 8.595 1.00 25.04

ATOM 1871 NE2 HIS B 167 41.279 -1.268 7.987 1.00 24.02

ATOM 1873 CD2 HIS B 167 41.421 -0.158 8.779 1.00 22.55

ATOM 1875 C HIS B 167 42.051 2.125 12.649 1.00 11.62

ATOM 1876 O HIS B 167 43.215 2.374 13.019 1.00 11.78

ATOM 1878 N CYS B 168 40.966 2.384 13.368 1.00 8.66

ATOM 1879 CA CYS B 168 41.006 2.902 14.711 1.00 9.01

ATOM 1881 CB CYS B 168 40.022 4.059 14.843 1.00 7.36

ATOM 1884 SG CYS B 168 40.397 5.322 13.638 1.00 8.94

ATOM 1886 C CYS B 168 40.655 1.758 15.646 1.00 9.91

ATOM 1887 O CYS B 168 40.294 0.664 15.188 1.00 9.53

ATOM 1889 N THR B 169 40.800 1.973 16.949 1.00 8.83

ATOM 1890 CA THR B 169 40.516 0.916 17.887 1.00 7.59

ATOM 1892 CB THR B 169 41.768 0.429 18.636 1.00 7.30

ATOM 1894 OGl THR B 169 42.759 -0.017 17.695 1.00 9.66

ATOM 1896 CG2 THR B 169 41.448 -0.726 19.533 1.00 7.02

ATOM 1900 C THR B 169 39.469 1.360 18.877 1.00 7.54

ATOM 1901 O THR B 169 39.585 2.430 19.465 1.00 9.35

ATOM 1903 N VAL B 170 38.465 0.531 19.053 1.00 7.00

ATOM 1904 CA VAL B 170 37.488 0.743 20.124 1.00 6.76

ATOM 1906 CB VAL B 170 36.058 0.667 19.564 1.00 6.21

ATOM 1908 CGl VAL B 170 35.734 -0.719 18.960 1.00 8.21

ATOM 1912 CG2 VAL B 170 35.047 1.085 20.629 1.00 7.83

ATOM 1916 C VAL B 170 37.732 -0.236 21.267 1.00 7.32

ATOM 1917 O VAL B 170 38.068 -1.391 21.047 1.00 6.76

ATOM 1919 N THR B 171 37.608 0.244 22.494 1.00 6.62

ATOM 1920 CA THR B 171 37.910 -0.569 23.655 1.00 7.19

ATOM 1922 CB THR B 171 39.242 -0.124 24.268 1.00 7.38

ATOM 1924 OGl THR B 171 39.274 1.301 24.405 1.00 6.74

ATOM 1926 CG2 THR B 171 40.420 -0.515 23.370 1.00 9.75

ATOM 1930 C THR B 171 36.783 -0.480 24.676 1.00 6.93

ATOM 1931 O THR B 171 36.061 0.498 24.734 1.00 7.21

ATOM 1933 N GLY B 172 36.656 -1.507 25.513 1.00 8.36

ATOM 1934 CA GLY B 172 35.711 -1.473 26.599 1.00 7.32

ATOM 1937 C GLY B 172 35.474 -2.827 27.242 1.00 7.42

ATOM 1938 O GLY B 172 36.002 -3.864 26.802 1.00 6.79

ATOM 1940 N TRP B 173 34.684 -2.780 28.308 1.00 7.29

ATOM 1941 CA TRP B 173 34.309 -3.959 29.077 1.00 8.13

ATOM 1943 CB TRP B 173 34.574 -3.684 30.549 1.00 7.40

ATOM 1946 CG TRP B 173 36.001 -3.556 30.913 1.00 8.44

ATOM 1947 CDl TRP B 173 36.868 -4.571 31.147 1.00 9.65

ATOM 1949 NEl TRP B 173 38.090 -4.081 31.491 1.00 8.86

ATOM 1951 CE2 TRP B 173 38.028 -2.709 31.510 1.00 7.44

ATOM 1952 CD2 TRP B 173 36.728 -2.345 31.130 1.00 8.12

ATOM 1953 CE3 TRP B 173 36.394 -0.989 31.073 1.00 7.56

ATOM 1955 CZ3 TRP B 173 37.365 -0.068 31.349 1.00 9.62

ATOM 1957 CH2 TRP B 173 38.650 -0.463 31.704 1.00 8.35

ATOM 1959 CZ2 TRP B 173 39.001 -1.784 31.778 1.00 10.25

ATOM 1961 C TRP B 173 32.842 -4.363 28.894 1.00 8.54

ATOM 1962 O TRP B 173 32.273 -5.105 29.724 1.00 8.20

ATOM 1964 N GLY B 174 32.234 -3.878 27.822 1.00 8.23

ATOM 1965 CA GLY B 174 30.828 -4.125 27.538 1.00 8.13

ATOM 1968 C GLY B 174 30.602 -5.516 26.977 1.00 8.40

ATOM 1969 O GLY B 174 31.518 -6.351 26.955 1.00 8.16

ATOM 1971 N HIS B 175 29.371 -5.746 26.521 1.00 8.77

ATOM 1972 CA HIS B 175 28.936 -7.085 26.127 1.00 9.57

ATOM 1974 CB HIS B 175 27.466 -7.082 25.733 1.00 9.91

ATOM 1977 CG HIS B 175 26.554 -6.764 26.870 1.00 10.13

ATOM 1978 NDl HIS B 175 25.188 -6.654 26.726 1.00 11.24 ATOM 1980 CEl HIS B 175 24.651 -6.372 27.903 1.00 12.01

ATOM 1982 NE2 HIS B 175 25.618 -6.295 28.802 1.00 13.22

ATOM 1984 CD2 HIS B 175 26.821 -6.532 28.179 1.00 13.44

ATOM 1986 C HIS B 175 29.794 -7.661 24.997 1.00 9.98

ATOM 1987 O HIS B 175 30.285 -6.930 24.144 1.00 9.15

ATOM 1989 N VAL B 176 29.917 -8.981 24.987 1.00 9.79

ATOM 1990 CA VAL B 176 30.720 -9.697 24.002 1.00 10.77

ATOM 1992 CB VAL B 176 31.684 -10.710 24.680 1.00 10.50

ATOM 1994 CGl VAL B 176 32.691 -9.989 25.543 1.00 12.00

ATOM 1998 CG2 VAL B 176 30.910 -11.787 25.461 1.00 14.17

ATOM 2002 C VAL B 176 29.821 -10.435 22.973 1.00 12.03

ATOM 2003 O VAL B 176 30.296 -10.964 21.982 1.00 13.32

ATOM 2005 N ALA B 177 28.532 -10.423 23.221 1.00 11.04

ATOM 2006 CA ALA B 177 27.539 -10.931 22.301 1.00 12.53

ATOM 2008 CB ALA B 177 27.516 -12.461 22.340 1.00 14.20

ATOM 2012 C ALA B 177 26.214 -10.329 22.743 1.00 13.90

ATOM 2013 O ALA B 177 26.106 -9.790 23.854 1.00 14.23

ATOM 2015 N PRO B 178 25.195 -10.380 21.892 1.00 14.34

ATOM 2016 CA PRO B 178 23.934 -9.775 22.305 1.00 14.49

ATOM 2018 CB PRO B 178 22.983 -10.122 21.151 1.00 15.28

ATOM 2021 CG PRO B 178 23.851 -10.275 19.995 1.00 12.71

ATOM 2024 CD PRO B 178 25.125 -10.927 20.528 1.00 15.07

ATOM 2027 C PRO B 178 23.422 -10.283 23.645 1.00 15.67

ATOM 2028 O PRO B 178 23.237 -11.497 23.839 1.00 15.76

ATOM 2029 N SER B 179 23.285 -9.346 24.574 1.00 16.35

ATOM 2030 CA SER B 179 22.877 -9.586 25.946 1.00 16.42

ATOM 2032 CB SER B 179 21.440 -10.096 25.995 1.00 18.32

ATOM 2035 OG SER B 179 20.607 -9.356 25.106 1.00 24.76

ATOM 2037 C SER B 179 23.781 -10.543 26.703 1.00 17.36

ATOM 2038 O SER B 179 23.346 -11.123 27.692 1.00 18.95

ATOM 2040 N VAL B 180 25.030 -10.707 26.271 1.00 16.62

ATOM 2041 CA VAL B 180 25.994 -11.531 27.002 1.00 14.94

ATOM 2043 CB VAL B 180 26.572 -12.622 26.115 1.00 14.31

ATOM 2045 CGl VAL B 180 27.610 -13.451 26.849 1.00 17.29

ATOM 2049 CG2 VAL B 180 25.442 -13.500 25.586 1.00 16.90

ATOM 2053 C VAL B 180 27.135 -10.664 27.533 1.00 15.07

ATOM 2054 O VAL B 180 27.856 -10.039 26.753 1.00 13.04

ATOM 2056 N SER B 181 27.301 -10.660 28.853 1.00 14.15

ATOM 2057 CA SER B 181 28.326 -9.827 29.479 1.00 14.29

ATOM 2059 CB SER B 181 27.998 -9.587 30.964 1.00 16.00

ATOM 2062 OG SER B 181 26.850 -8.752 31.081 1.00 20.62

ATOM 2064 C SER B 181 29.698 -10.448 29.337 1.00 13.93

ATOM 2065 O SER B 181 29.844 -11.674 29.276 1.00 11.87

ATOM 2067 N LEU B 182 30.713 -9.588 29.313 1.00 11.41

ATOM 2068 CA LEU B 182 32.082 -10.038 29.461 1.00 13.24

ATOM 2070 CB LEU B 182 33.025 -8.840 29.385 1.00 12.57

ATOM 2073 CG LEU B 182 34.513 -9.074 29.465 1.00 11.00

ATOM 2075 CDl LEU B 182 35.015 -9.761 28.225 1.00 11.77

ATOM 2079 CD2 LEU B 182 35.211 -7.701 29.593 1.00 12.57

ATOM 2083 C LEU B 182 32.212 -10.709 30.814 1.00 13.53

ATOM 2084 O LEU B 182 31.717 -10.197 31.823 1.00 13.62

ATOM 2086 N LEU B 183 32.858 -11.864 30.827 1.00 15.00

ATOM 2087 CA LEU B 183 32.989 -12.650 32.062 1.00 16.37

ATOM 2089 CB LEU B 183 33.220 -14.134 31.741 1.00 17.97

ATOM 2092 CG LEU B 183 31.994 -15.038 31.829 1.00 23.03

ATOM 2094 CDl LEU B 183 30.736 -14.357 31.282 1.00 29.44

ATOM 2098 CD2 LEU B 183 32.282 -16.364 31.124 1.00 21.71

ATOM 2102 C LEU B 183 34.143 -12.171 32.897 1 .00 15.51

ATOM 2103 O LEU B 183 35.168 -11.751 32.380 .00 14.65

ATOM 2105 N THR B 184 33.978 -12.272 34.211 1.00 15.11

ATOM 2106 CA THR B 184 35.078 -12.087 35.119 1.00 16.24 ATOM 2108 CB THR B 184 34.679 -12.497 36.547 1.00 17.65

ATOM 2110 OGl THR B 184 35.759 -12.204 37.431 1.00 18.56

ATOM 2112 CG2 THR B 184 34.342 -13.990 36.607 1.00 20.05

ATOM 2116 C THR B 184 36.270 -12.930 34.626 1.00 15.33

ATOM 2117 O THR B 184 36.090 -14.044 34.128 1.00 16.51

ATOM 2119 N PRO B 185 37.493 -12.406 34.749 1.00 14.91

ATOM 2120 CA PRO B 185 37.890 -11.183 35.418 1.00 14.27

ATOM 2122 CB PRO B 185 39.358 -11.436 35.722 1.00 14.36

ATOM 2125 CG PRO B 185 39.817 -12.237 34.589 1.00 15.35

ATOM 2128 CD PRO B 185 38.662 -13.128 34.226 1.00 16.33

ATOM 2131 C PRO B 185 37.743 -9.905 34.593 1.00 12.64

ATOM 2132 O PRO B 185 38.281 -8.884 34.984 1.00 14.48

ATOM 2133 N LYS B 186 37.001 -9.982 33.481 1.00 12.42

ATOM 2134 CA LYS B 186 36.686 -8.831 32.653 1.00 12.58

ATOM 2136 CB LYS B 186 35.761 -7.865 33.395 1.00 11.61

ATOM 2139 CG LYS B 186 34.357 -8.374 33.488 1.00 14.10

ATOM 2142 CD LYS B 186 33.471 -7.409 34.243 1.00 16.50

ATOM 2145 CE LYS B 186 32.091 -7.955 34.512 1.00 22.42

ATOM 2148 NZ LYS B 186 31.256 -7.989 33.301 1.00 23.69

ATOM 2152 C LYS B 186 37.925 -8.146 32.108 1.00 11.05

ATOM 2153 O LYS B 186 38.213 -6.969 32.431 1.00 9.87

ATOM 2155 N PRO B 187 38.662 -8.868 31.239 1.00 11.12

ATOM 2156 CA PRO B 187 39.786 -8.276 30.556 1.00 10.78

ATOM 2158 CB PRO B 187 40.432 -9.476 29.857 1.00 11.09

ATOM 2161 CG PRO B 187 39.339 -10.370 29.602 1.00 12.28

ATOM 2164 CD PRO B 187 38.428 -10.251 30.794 1.00 12.13

ATOM 2167 C PRO B 187 39.312 -7.221 29.554 1.00 9.44

ATOM 2168 O PRO B 187 38.384 -7.465 28.765 1.00 10.17

ATOM 2169 N LEU B 188 39.952 -6.053 29.574 1.00 9.28

ATOM 2170 CA LEU B 188 39.590 -5.003 28.627 1.00 8.57

ATOM 2172 CB LEU B 188 40.514 -3.807 28.754 1.00 7.38

ATOM 2175 CG LEU B 188 40.204 -2.657 27.813 1.00 8.73

ATOM 2177 CDl LEU B 188 38.838 -2.015 28.113 1.00 9.68

ATOM 2181 CD2 LEU B 188 41.280 -1.622 27.932 1.00 8.55

ATOM 2185 C LEU B 188 39.684 -5.563 27.222 1.00 8.24

ATOM 2186 O LEU B 188 40.682 -6.194 26.855 1.00 8.25

ATOM 2188 N GLN B 189 38.652 -5.326 26.435 1.00 8.76

ATOM 2189 CA GLN B 189 38.619 -5.759 25.040 1.00 8.21

ATOM 2191 CB GLN B 189 37.246 -6.325 24.670 1.00 6.62

ATOM 2194 CG GLN B 189 36.803 -7.544 25.515 1.00 9.30

ATOM 2197 CD GLN B 189 37.696 -8.718 25.288 1.00 9.28

ATOM 2198 OEl GLN B 189 37.715 -9.282 24.185 1.00 9.97

ATOM 2199 NE2 GLN B 189 38.537 -9.037 26.283 1.00 9.21

ATOM 2202 C GLN B 189 38.944 -4.620 24.087 1.00 8.81

ATOM 2203 O GLN B 189 38.664 -3.471 24.364 1.00 7.72

ATOM 2205 N GLN B 190 39.572 -4.973 22.985 1.00 8.79

ATOM 2206 CA GLN B 190 39.959 -4.029 21.949 1.00 9.58

ATOM 2208 CB GLN B 190 41.468 -3.823 21.968 1.00 10.09

ATOM 2211 CG GLN B 190 42.249 -5.045 21.463 1.00 10.42

ATOM 2214 CD GLN B 190 43.718 -5.007 21.763 1.00 14.49

ATOM 2215 OEl GLN B 190 44.292 -3.964 22.052 1.00 15.92

ATOM 2216 NE2 GLN B 190 44.337 -6.184 21.747 1.00 21.33

ATOM 2219 C GLN B 190 39.518 -4.572 20.610 1.00 9.42

ATOM 2220 O GLN B 190 39.494 -5.790 20.385 1.00 9.33

ATOM 2222 N LEU B 191 39.149 -3.665 19.720 1.00 8.23

ATOM 2223 CA LEU B 191 38.736 -4.065 18.386 1.00 9.61

ATOM 2225 CB LEU B 191 37.243 -4.301 18.352 1.00 8.15

ATOM 2228 CG LEU B 191 36.639 -4.504 16.961 1.00 7.94

ATOM 2230 CDl LEU B 191 36.927 -5.865 16.411 1.00 11.76

ATOM 2234 CD2 LEU B 191 35.178 -4.270 16.998 1.00 12.51

ATOM 2238 C LEU B 191 39.116 -2.997 17.391 1.00 9.54 ATOM 2239 O LEU B 191 38.791 -1.816 17.576 1.00 8.53

ATOM 2241 N GLU B 192 39.788 -3.427 16.329 1.00 10.64

ATOM 2242 CA GLU B 192 40.140 -2.565 15.225 1.00 10.70

ATOM 2244 CB GLU B 192 41.318 -3.191 14.476 1.00 12.14

ATOM 2247 CG GLU B 192 41.815 -2.463 13.283 1.00 15.00

ATOM 2250 CD GLU B 192 43.248 -2.866 12.909 1.00 18.99

ATOM 2251 OEl GLU B 192 43.987 -3.373 13.785 1.00 30.10

ATOM 2252 OE2 GLU B 192 43.635 -2.670 11.737 1.00 33.96

ATOM 2253 C GLU B 192 38.940 -2.436 14.313 1.00 10.01

ATOM 2254 O GLU B 192 38.351 -3.442 13.898 1.00 8.08

ATOM 2256 N VAL B 193 38.551 -1.203 14.051 1.00 9.46

ATOM 2257 CA VAL B 193 37.399 -0.897 13.198 1.00 9.75

ATOM 2259 CB VAL B 193 36.153 -0.434 14.033 1.00 10.14

ATOM 2261 CGl VAL B 193 35.578 -1.602 14.798 1.00 8.07

ATOM 2265 CG2 VAL B 193 36.501 0.714 14.996 1.00 11.21

ATOM 2269 C VAL B 193 37.798 0.223 12.227 1.00 9.86

ATOM 2270 O VAL B 193 38.434 1.190 12.622 1.00 10.31

ATOM 2272 N PRO B 194 37.418 0.093 10.953 1.00 9.69

ATOM 2273 CA PRO B 194 37.702 1.165 10.014 1.00 10.06

ATOM 2275 CB PRO B 194 37.628 0.468 8.666 1.00 8.84

ATOM 2278 CG PRO B 194 36.631 -0.621 8.881 1.00 11.55

ATOM 2281 CD PRO B 194 36.768 -1.059 10.299 1.00 10.02

ATOM 2284 C PRO B 194 36.687 2.275 10.087 1.00 9.77

ATOM 2285 O PRO B 194 35.480 2.003 10.245 1.00 9.99

ATOM 2286 N LEU B 195 37.151 3.523 9.961 1.00 8.56

ATOM 2287 CA LEU B 195 36.236 4.649 9.865 1.00 9.33

ATOM 2289 CB LEU B 195 36.966 5.973 9.913 1.00 7.86

ATOM 2292 CG LEU B 195 37.816 6.221 11.143 1.00 9.37

ATOM 2294 CDl LEU B 195 38.418 7.608 11.006 1.00 9.09

ATOM 2298 CD2 LEU B 195 36.976 6.053 12.414 1.00 8.36

ATOM 2302 C LEU B 195 35.465 4.570 8.555 1.00 10.06

ATOM 2303 O LEU B 195 36.050 4.293 7.505 1.00 10.18

ATOM 2305 N ILE B 196 34.166 4.814 8.631 1.00 10.59

ATOM 2306 CA ILE B 196 33.301 4.773 7.440 1.00 11.10

ATOM 2308 CB ILE B 196 32.118 3.818 7.668 1.00 10.04

ATOM 2310 CGl ILE B 196 32.649 2.414 7.918 1.00 10.68

ATOM 2313 CDl ILE B 196 31.618 1.448 8.335 1.00 12.41

ATOM 2317 CG2 ILE B 196 31.120 3.839 6.498 1.00 12.71

ATOM 2321 C ILE B 196 32.850 6.164 7.074 1.00 11.60

ATOM 2322 O ILE B 196 32.623 7.007 7.934 1.00 11.39

ATOM 2324 N SER B 197 32.722 6.406 5.773 1.00 11.35

ATOM 2325 CA SER B 197 32.359 7.719 5.282 1.00 12.32

ATOM 2327 CB SER B 197 32.334 7.717 3.765 1.00 14.00

ATOM 2330 OG SER B 197 31.170 7.088 3.316 1.00 15.49

ATOM 2332 C SER B 197 30.982 8.149 5.800 1.00 13.09

ATOM 2333 O SER B 197 30.110 7.323 6.003 1.00 13.07

ATOM 2335 N ARG B 198 30.793 9.446 6.000 1.00 14.98

ATOM 2336 CA ARG B 198 29.518 9.939 6.494 1.00 16.30

ATOM 2338 CB ARG B 198 29.600 11.422 6.891 1.00 19.06

ATOM 2341 CG ARG B 198 29.857 12.392 5.782 1.00 21.11

ATOM 2344 CD ARG B 198 30.468 13.697 6.342 1.00 22.47

ATOM 2347 NE ARG B 198 30.471 14.740 5.320 1.00 31.08

ATOM 2349 CZ ARG B 198 31.441 14.963 4.430 1.00 37.47

ATOM 2350 NHl ARG B 198 32.560 14.235 4.408 1.00 41.00

ATOM 2353 NH2 ARG B 198 31.288 15.941 3.542 1.00 38.86

ATOM 2356 C ARG B 198 28.399 9.645 5.498 1.00 15.27

ATOM 2357 O ARG B 198 27.281 9.338 5.899 1.00 14.21

ATOM 2359 N GLU B 199 28.714 9.674 4.206 1.00 15.71

ATOM 2360 CA GLU B 199 27.728 9.319 3.168 1.00 15.16

ATOM 2362 CB GLU B 199 28.346 9.515 1.786 1.00 17.32

ATOM 2365 CG GLU B 199 28.726 10.989 1.438 1.00 26.08 ATOM 2368 CD GLU B 199 30.015 11.516 2.092 1.00 34.18

ATOM 2369 OEl GLU B 199 30.830 10.712 2.604 1.00 29.64

ATOM 2370 OE2 GLU B 199 30.200 12.762 2.094 1.00 40.43

ATOM 2371 C GLU B 199 27.239 7.882 3.338 1.00 13.57

ATOM 2372 O GLU B 199 26.028 7.585 3.264 1.00 13.22

ATOM 2374 N THR B 200 28.174 6.980 3.608 1.00 12.05

ATOM 2375 CA THR B 200 27.849 5.576 3.759 1.00 11.49

ATOM 2377 CB THR B 200 29.112 4.737 3.694 1.00 12.08

ATOM 2379 OGl THR B 200 29.687 4.929 2.398 1.00 11.41

ATOM 2381 CG2 THR B 200 28.805 3.305 3.895 1.00 10.04

ATOM 2385 C THR B 200 27.057 5.331 5.046 1.00 11.71

ATOM 2386 O THR B 200 26.063 4.614 5.042 1.00 10.20

ATOM 2388 N CYS B 201 27.503 5.936 6.145 1.00 10.78

ATOM 2389 CA CYS B 201 26.794 5.797 7.411 1.00 11.79

ATOM 2391 CB CYS B 201 27.551 6.536 8.500 1.00 12.78

ATOM 2394 SG CYS B 201 29.196 5.890 8.794 1.00 15.82

ATOM 2396 C CYS B 201 25.376 6.354 7.303 1.00 12.08

ATOM 2397 O CYS B 201 24.453 5.792 7.874 1.00 11.89

ATOM 2399 N ASN B 202 25.214 7.448 6.568 1.00 10.65

ATOM 2400 CA ASN B 202 23.898 8.044 6.333 1.00 12.18

ATOM 2402 CB ASN B 202 24.038 9.310 5.496 1.00 11.38

ATOM 2405 CG ASN B 202 22.706 9.855 5.048 1.00 15.12

ATOM 2406 ODl ASN B 202 22.341 9.753 3.867 1.00 25.47

ATOM 2407 ND2 ASN B 202 21.968 10.433 5.977 1.00 18.92

ATOM 2410 C ASN B 202 22.991 7.036 5.625 1.00 11.80

ATOM 2411 O ASN B 202 21.831 6.829 5.993 1.00 12.04

ATOM 2413 N SER B 203 23.532 6.385 4.604 1.00 11.86

ATOM 2414 CA ASER B 203 22.789 5.343 3.893 0.50 11.78

ATOM 2415 CA BSER B 203 22.767 5.360 3.903 0.50 12.37

ATOM 2418 CB ASER B 203 23.612 4.783 2.725 0.50 12.30

ATOM 2419 CB BSER B 203 23.524 4.835 2.682 0.50 12.99

ATOM 2424 OG ASER B 203 22.932 3.737 2.041 0.50 9.69

ATOM 2425 OG BSER B 203 23.582 5.823 1.667 0.50 16.98

ATOM 2428 C SER B 203 22.394 4.218 4.822 1.00 12.09

ATOM 2429 O SER B 203 21.227 3.840 4.884 1.00 12.95

ATOM 2431 N LEU B 204 23.373 3.684 5.554 1.00 10.27

ATOM 2432 CA LEU B 204 23.149 2.504 6.373 1.00 10.48

ATOM 2434 CB LEU B 204 24.458 2.056 7.012 1.00 10.44

ATOM 2437 CG LEU B 204 25.417 1.391 6.009 1.00 11.18

ATOM 2439 CDl LEU B 204 26.761 1.309 6.637 1.00 11.36

ATOM 2443 CD2 LEU B 204 24.945 0.023 5.564 1.00 13.58

ATOM 2447 C LEU B 204 22.085 2.712 7.445 1.00 10.81

ATOM 2448 O LEU B 204 21.307 1.793 7.739 1.00 12.04

ATOM 2450 N TYR B 205 22.077 3.909 8.024 1.00 10.99

ATOM 2451 CA TYR B 205 21.210 4.198 9.175 1.00 10.89

ATOM 2453 CB TYR B 205 21.993 4.899 10.262 1.00 11.59

ATOM 2456 CG TYR B 205 22.811 3.955 11.081 1.00 9.10

ATOM 2457 CDl TYR B 205 22.196 3.102 11.987 1.00 13.59

ATOM 2459 CEl TYR B 205 22.920 2.232 12.751 1.00 13.22

ATOM 2461 CZ TYR B 205 24.275 2.167 12.617 1.00 11.63

ATOM 2462 OH TYR B 205 24.948 1.260 13.402 1.00 13.15

ATOM 2464 CE2 TYR B 205 24.946 2.982 11.707 1.00 13.34

ATOM 2466 CD2 TYR B 205 24.216 3.876 10.939 1.00 11.67

ATOM 2468 C TYR B 205 19.996 5.042 8.836 1.00 12.58

ATOM 2469 O TYR B 205 18.905 4.765 9.351 1.00 15.96

ATOM 2471 N ASN B 206 20.158 6.070 8.023 1.00 11.33

ATOM 2472 CA ASN B 206 19.042 6.965 7.772 1.00 11.14

ATOM 2474 CB ASN B 206 19.486 8.424 7.626 1.00 10.13

ATOM 2477 CG ASN B 206 20.147 8.956 8.882 1.00 10.67

ATOM 2478 ODl ASN B 206 19.895 8.448 9.995 1.00 10.73

ATOM 2479 ND2 ASN B 206 21.013 9.945 8.711 1.00 12.29 ATOM 2482 C ASN B 206 18.173 6.559 6.600 1.00 12.75

ATOM 2483 O ASN B 206 16.986 6.905 6.571 1.00 14.47

ATOM 2485 N ILE B 207 18.741 5.859 5.629 1.00 11.35

ATOM 2486 CA ILE B 207 17.974 5.481 4.443 1.00 12.12

ATOM 2488 CB ILE B 207 18.778 5.704 3.173 1.00 12.28

ATOM 2490 CGl ILE B 207 19.271 7.153 3.106 1.00 14.43

ATOM 2493 CDl ILE B 207 18.219 8.171 3.320 1.00 19.11

ATOM 2497 CG2 ILE B 207 17.940 5.341 1.933 1.00 13.39

ATOM 2501 C ILE B 207 17.552 4.026 4.491 1.00 11.76

ATOM 2502 O ILE B 207 16.386 3.717 4.256 1.00 13.53

ATOM 2504 N ASP B 208 18.490 3.140 4.802 1.00 12.10

ATOM 2505 CA ASP B 208 18.258 1.700 4.793 1.00 13.21

ATOM 2507 CB ASP B 208 19.486 0.977 4.208 1.00 15.25

ATOM 2510 CG ASP B 208 19.765 1.345 2.776 1.00 17.33

ATOM 2511 ODl ASP B 208 18.914 1.952 2.122 1.00 18.75

ATOM 2512 OD2 ASP B 208 20.862 1.019 2.295 1.00 27.26

ATOM 2513 C ASP B 208 17.950 1.110 6.171 1.00 15.72

ATOM 2514 O ASP B 208 18.345 -0.024 6.485 1.00 19.34

ATOM 2516 N ALA B 209 17.273 1.858 7.024 1.00 14.66

ATOM 2517 CA ALA B 209 16.890 1.347 8.332 1.00 13.53

ATOM 2519 CB ALA B 209 17.810 1.875 9.443 1.00 15.04

ATOM 2523 C ALA B 209 15.464 1.797 8.579 1.00 12.85

ATOM 2524 O ALA B 209 14.992 2.724 7.933 1.00 13.52

ATOM 2526 N LYS B 210 14.783 1.130 9.494 1.00 10.69

ATOM 2527 CA LYS B 210 13.401 1.506 9.808 1.00 11.36

ATOM 2529 CB LYS B 210 12.763 0.468 10.729 1.00 13.90

ATOM 2532 CG LYS B 210 12.712 -0.941 10.174 1.00 20.42

ATOM 2535 CD LYS B 210 11.936 -1.056 8.895 1.00 27.23

ATOM 2538 CE LYS B 210 11.712 -2.536 8.512 1.00 29.16

ATOM 2541 NZ LYS B 210 10.636 -2.675 7.488 1.00 33.48

ATOM 2545 C LYS B 210 13.327 2.868 10.503 1.00 11.24

ATOM 2546 O LYS B 210 14.325 3.325 11.096 1.00 10.14

ATOM 2548 N PRO B 211 12.144 3.517 10.458 1.00 9.84

ATOM 2549 CA PRO B 211 11.977 4.827 11.131 1.00 10.21

ATOM 2551 CB PRO B 211 10.483 5.102 10.996 1.00 11.11

ATOM 2554 CG PRO B 211 10.060 4.337 9.788 1.00 12.33

ATOM 2557 CD PRO B 211 10.926 3.121 9.727 1.00 11.48

ATOM 2560 C PRO B 211 12.382 4.899 12.602 1.00 9.75

ATOM 2561 O PRO B 211 12.803 5.967 13.067 1.00 10.38

ATOM 2562 N GLU B 212 12.271 3.811 13.341 1.00 10.81

ATOM 2563 CA GLU B 212 12.628 3.872 14.752 1.00 13.60

ATOM 2565 CB GLU B 212 11.971 2.745 15.488 1.00 14.72

ATOM 2568 CG GLU B 212 12.574 1.419 15.279 1.00 15.97

ATOM 2571 CD GLU B 212 11.646 0.371 15.818 1.00 21.23

ATOM 2572 OEl GLU B 212 11.838 -0.026 16.994 1.00 31.46

ATOM 2573 OE2 GLU B 212 10.698 0.013 15.071 1.00 37.07

ATOM 2574 C GLU B 212 14.139 3.846 15.001 1.00 12.11

ATOM 2575 O GLU B 212 14.583 4.029 16.118 1.00 11.66

ATOM 2577 N GLU B 213 14.924 3.657 13.949 1.00 10.98

ATOM 2578 CA GLU B 213 16.367 3.684 14.091 1.00 10.52

ATOM 2580 CB GLU B 213 17.021 3.329 12.782 1.00 9.66

ATOM 2583 CG GLU B 213 18.504 3.039 12.888 1.00 9.17

ATOM 2586 CD GLU B 213 18.806 1.718 13.573 1.00 11.26

ATOM 2587 OEl GLU B 213 17.926 0.810 13.602 1.00 13.96

ATOM 2588 OE2 GLU B 213 19.960 1.575 14.037 1.00 10.19

ATOM 2589 C GLU B 213 16.816 5.093 14.506 1.00 9.21

ATOM 2590 O GLU B 213 16.350 6.075 13.940 1.00 9.32

ATOM 2592 N PRO B 214 17.728 5.197 15.489 1.00 9.16

ATOM 2593 CA PRO B 214 18.253 6.529 15.781 1.00 9.21

ATOM 2595 CB PRO B 214 19.336 6.265 16.829 1.00 9.15

ATOM 2598 CG PRO B 214 18.844 5.058 17.525 1.00 9.35 ATOM 2601 CD PRO B 214 18.281 4.200 16.415 1.00 9.71

ATOM 2604 C PRO B 214 18.833 7.230 14.580 1.00 7.92

ATOM 2605 O PRO B 214 19.300 6.590 13.636 1.00 10.63

ATOM 2606 N HIS B 215 18.777 8.547 14.616 1.00 9.28

ATOM 2607 CA HIS B 215 19.161 9.352 13.494 1.00 9.27

ATOM 2609 CB HIS B 215 18.470 10.696 13.523 1.00 10.70

ATOM 2612 CG HIS B 215 18.700 11.476 12.281 1.00 11.85

ATOM 2613 NDl HIS B 215 19.323 12.702 12.266 1.00 20.21

ATOM 2615 CEl HIS B 215 19.399 13.135 11.019 1.00 11.04

ATOM 2617 NE2 HIS B 215 18.858 12.229 10.231 1.00 18.51

ATOM 2619 CD2 HIS B 215 18.411 11.186 10.999 1.00 10.92

ATOM 2621 C HIS B 215 20.655 9.580 13.484 1.00 9.89

ATOM 2622 O HIS B 215 21.224 10.025 14.484 1.00 10.21

ATOM 2624 N PHE B 216 21.281 9.311 12.341 1.00 8.20

ATOM 2625 CA PHE B 216 22.714 9.515 12.183 1.00 9.75

ATOM 2627 CB PHE B 216 23.324 8.478 11.222 1.00 9.69

ATOM 2630 CG PHE B 216 24.786 8.685 10.983 1.00 7.80

ATOM 2631 CDl PHE B 216 25.739 8.154 11.863 1.00 8.67

ATOM 2633 CEl PHE B 216 27.087 8.374 11.654 1.00 9.05

ATOM 2635 CZ PHE B 216 27.503 9.111 10.573 1.00 11.67

ATOM 2637 CE2 PHE B 216 26.579 9.637 9.693 1.00 10.95

ATOM 2639 CD2 PHE B 216 25.224 9.427 9.903 1.00 10.94

ATOM 2641 C PHE B 216 22.906 10.941 11.688 1.00 9.55

ATOM 2642 O PHE B 216 22.335 11.347 10.666 1.00 10.84

ATOM 2644 N VAL B 217 23.670 11.722 12.439 1.00 10.23

ATOM 2645 CA VAL B 217 23.899 13.116 12.137 1.00 11.87

ATOM 2647 CB VAL B 217 23.737 13.995 13.381 1.00 12.02

ATOM 2649 CGl VAL B 217 24.074 15.417 13.067 1.00 13.11

ATOM 2653 CG2 VAL B 217 22.320 13.887 13.937 1.00 15.38

ATOM 2657 C VAL B 217 25.319 13.219 11.604 1.00 12.15

ATOM 2658 O VAL B 217 26.281 13.088 12.373 1.00 11.76

ATOM 2660 N GLN B 218 25.441 13.470 10.300 1.00 12.68

ATOM 2661 CA GLN B 218 26.737 13.388 9.598 1.00 14.79

ATOM 2663 CB GLN B 218 26.555 13.579 8.077 1.00 15.34

ATOM 2666 CG GLN B 218 25.656 12.533 7.410 1.00 17.98

ATOM 2669 CD GLN B 218 25.323 12.861 5.968 1.00 21.72

ATOM 2670 OEl GLN B 218 24.164 13.127 5.627 1.00 32.15

ATOM 2671 NE2 GLN B 218 26.336 12.862 5.123 1.00 22.78

ATOM 2674 C GLN B 218 27.795 14.368 10.135 1.00 14.76

ATOM 2675 O GLN B 218 28.999 14.103 10.069 1.00 16.50

ATOM 2677 N GLU B 219 27.335 15.479 10.697 1.00 13.49

ATOM 2678 CA GLU B 219 28.227 16.531 11.126 1.00 14.91

ATOM 2680 CB GLU B 219 27.454 17.831 11.307 1.00 15.30

ATOM 2683 CG GLU B 219 26.782 18.374 10.009 1.00 22.98

ATOM 2686 CD GLU B 219 25.800 17.391 9.306 1.00 30.08

ATOM 2687 OEl GLU B 219 24.912 16.783 9.972 1.00 21.65

ATOM 2688 OE2 GLU B 219 25.915 17.251 8.056 1.00 38.54

ATOM 2689 C GLU B 219 28.906 16.189 12.437 1.00 14.02

ATOM 2690 O GLU B 219 30.019 16.670 12.692 1.00 15.23

ATOM 2692 N ASP B 220 28.258 15.364 13.260 1.00 12.26

ATOM 2693 CA AASP B 220 28.626 15.169 14.662 0.50 12.02

ATOM 2694 CA BASP B 220 28.794 15.148 14.610 0.50 11.82

ATOM 2697 CB AASP B 220 27.550 15.822 15.531 0.50 12.63

ATOM 2698 CB BASP B 220 28.151 16.119 15.614 0.50 12.64

ATOM 2703 CG AASP B 220 27.320 17.282 15.175 0.50 14.92

ATOM 2704 CG BASP B 220 26.646 15.965 15.720 0.50 12.08

ATOM 2705 ODlAASP B 220 28.285 17.960 14.769 0.50 19.05

ATOM 2706 ODlBASP B 220 26.142 14.850 15.551 0.50 13.75

ATOM 2707 OD2AASP B 220 26.170 17.747 15.303 0.50 17.84

ATOM 2708 OD2BASP B 220 25.962 16.980 15.998 0.50 17.77

ATOM 2709 C ASP B 220 28.771 13.708 15.096 1.00 11.10 ATOM 2710 O ASP B 220 28.948 13.426 16.287 1.00 9.60

ATOM 2712 N MET B 221 28.637 12.792 14.154 1.00 9.83

ATOM 2713 CA MET B 221 28.786 11.378 14.430 1.00 10.05

ATOM 2715 CB MET B 221 27.412 10.699 14.434 1.00 9.47

ATOM 2718 CG MET B 221 26.502 11.234 15.514 1.00 11.02

ATOM 2721 SD MET B 221 24.847 10.546 15.392 1.00 9.01

ATOM 2722 CE MET B 221 23.944 11.682 16.448 1.00 12.63

ATOM 2726 C MET B 221 29.666 10.734 13.383 1.00 9.80

ATOM 2727 O MET B 221 29.838 11.260 12.267 1.00 9.83

ATOM 2729 N VAL B 222 30.276 9.628 13.760 1.00 9.33

ATOM 2730 CA VAL B 222 30.993 8.795 12.797 1.00 9.80

ATOM 2732 CB VAL B 222 32.526 8.993 12.905 1.00 11.39

ATOM 2734 CGl VAL B 222 33.046 8.728 14.352 1.00 9.78

ATOM 2738 CG2 VAL B 222 33.248 8.106 11.883 1.00 12.07

ATOM 2742 C VAL B 222 30.614 7.362 13.044 1.00 11.18

ATOM 2743 O VAL B 222 30.466 6.950 14.186 1.00 9.57

ATOM 2745 N CYS B 223 30.415 6.600 11.980 1.00 10.19

ATOM 2746 CA CYS B 223 30.248 5.166 12.144 1.00 10.86

ATOM 2748 CB CYS B 223 28.934 4.623 11.513 1.00 12.96

ATOM 2751 SG CYS B 223 28.932 4.146 9.789 1.00 14.96

ATOM 2753 C CYS B 223 31.524 4.483 11.717 1.00 11.17

ATOM 2754 O CYS B 223 32.290 4.986 10.905 1.00 10.26

ATOM 2756 N ALA B 224 31.792 3.359 12.355 1.00 10.19

ATOM 2757 CA ALA B 224 33.046 2.696 12.219 1.00 10.87

ATOM 2759 CB ALA B 224 34.056 3.296 13.143 1.00 11.58

ATOM 2763 C ALA B 224 32.802 1.263 12.559 1.00 9.90

ATOM 2764 O ALA B 224 32.106 0.958 13.521 1.00 10.90

ATOM 2766 N GLY B 225 33.358 0.378 11.750 1.00 11.16

ATOM 2767 CA GLY B 225 33.136 -1.033 11.933 1.00 11.64

ATOM 2770 C GLY B 225 32.858 -1.724 10.627 1.00 12.16

ATOM 2771 O GLY B 225 33.484 -1.430 9.586 1.00 11.69

ATOM 2773 N TYR B 226 31.898 -2.631 10.679 1.00 13.09

ATOM 2774 CA TYR B 226 31.746 -3.647 9.647 1.00 14.53

ATOM 2776 CB TYR B 226 32.382 -4.948 10.126 1.00 15.03

ATOM 2779 CG TYR B 226 33.848 -4.799 10.412 1.00 15.36

ATOM 2780 CDl TYR B 226 34.782 -4.859 9.387 1.00 20.72

ATOM 2782 CEl TYR B 226 36.127 -4.688 9.650 1.00 17.30

ATOM 2784 CZ TYR B 226 36.525 -4.459 10.937 1.00 12.42

ATOM 2785 OH TYR B 226 37.856 -4.267 11.211 1.00 17.80

ATOM 2787 CE 2 TYR B 226 35.619 -4.372 11.951 1.00 15.90

ATOM 2789 CD2 TYR B 226 34.299 -4.524 11.695 1.00 14.07

ATOM 2791 C TYR B 226 30.271 -3.835 9.385 1.00 15.82

ATOM 2792 O TYR B 226 29.442 -3.625 10.284 1.00 17.00

ATOM 2794 N VAL B 227 29.915 -4.155 8.147 1.00 12.95

ATOM 2795 CA VAL B 227 28.544 -4.560 7.889 1.00 14.30

ATOM 2797 CB VAL B 227 28.088 -4.155 6.481 1.00 14.07

ATOM 2799 CGl VAL B 227 28.261 -2.643 6.279 1.00 13.30

ATOM 2803 CG2 VAL B 227 28.809 -4.957 5.443 1.00 16.94

ATOM 2807 C VAL B 227 28.360 -6.072 8.114 1.00 13.93

ATOM 2808 O VAL B 227 27.239 -6.535 8.308 1.00 15.60

ATOM 2810 N GLU B 228 29.464 -6.812 8.105 1.00 13.79

ATOM 2811 CA GLU B 228 29.474 -8.299 8.198 1.00 17.25

ATOM 2813 CB GLU B 228 30.867 -8.881 7.988 1.00 18.80

ATOM 2816 CG GLU B 228 31.465 -8.657 6.654 1.00 24.72

ATOM 2819 CD GLU B 228 32.464 -7.546 6.685 1.00 26.77

ATOM 2820 OEl GLU B 228 32.104 -6.461 7.179 1.00 20.08

ATOM 2821 OE 2 GLU B 228 33.590 -7.749 6.172 1.00 32.03

ATOM 2822 C GLU B 228 28.996 -8.908 9.490 1.00 18.74

ATOM 2823 O GLU B 228 28.743 -10.119 9.539 1.00 22.23

ATOM 2825 N GLY B 229 28.931 -8.136 10.557 1.00 17.91

ATOM 2826 CA GLY B 229 28.496 -8.719 11.807 1.00 16.67 ATOM 2829 C GLY B 229 29.592 -9.264 12.696 1.00 16.60

ATOM 2830 O GLY B 229 30.651 -9.708 12.234 1.00 14.72

ATOM 2832 N GLY B 230 29.327 -9.194 13.994 1.00 14.01

ATOM 2833 CA GLY B 230 30.179 -9.822 14.987 1.00 13.10

ATOM 2836 C GLY B 230 31.377 -9.006 15.423 1.00 12.59

ATOM 2837 O GLY B 230 32.159 -9.484 16.222 1.00 12.32

ATOM 2839 N LYS B 231 31.526 -7.783 14.923 1.00 10.75

ATOM 2840 CA LYS B 231 32.648 -6.937 15.296 1.00 11.37

ATOM 2842 CB LYS B 231 33.717 -6.937 14.205 1.00 12.81

ATOM 2845 CG LYS B 231 34.449 -8.263 14.058 1.00 13.33

ATOM 2848 CD LYS B 231 35.547 -8.188 13.007 1.00 14.38

ATOM 2851 CE LYS B 231 36.396 -9.464 13.001 1.00 17.82

ATOM 2854 NZ LYS B 231 37.511 -9.457 11.998 1.00 17.77

ATOM 2858 C LYS B 231 32.150 -5.501 15.572 1.00 11.36

ATOM 2859 O LYS B 231 31.914 -4.737 14.655 1.00 10.08

ATOM 2861 N ASP B 232 32.000 -5.153 16.838 1.00 10.59

ATOM 2862 CA ASP B 232 31.400 -3.858 17.183 1.00 10.47

ATOM 2864 CB ASP B 232 29.894 -3.957 16.893 1.00 12.56

ATOM 2867 CG ASP B 232 29.184 -2.602 16.742 1.00 11.70

ATOM 2868 ODl ASP B 232 29.773 -1.495 16.851 1.00 11.32

ATOM 2869 OD2 ASP B 232 27.975 -2.673 16.500 1.00 19.04

ATOM 2870 C ASP B 232 31.610 -3.595 18.673 1.00 10.87

ATOM 2871 O ASP B 232 31.934 -4.517 19.443 1.00 9.40

ATOM 2873 N ALA B 233 31.342 -2.358 19.077 1.00 9.33

ATOM 2874 CA ALA B 233 31.094 -2.052 20.474 1.00 9.37

ATOM 2876 CB ALA B 233 31.238 -0.561 20.730 1.00 9.32

ATOM 2880 C ALA B 233 29.677 -2.506 20.804 1.00 9.65

ATOM 2881 O ALA B 233 28.841 -2.687 19.910 1.00 8.33

ATOM 2883 N CYS B 234 29.390 -2.651 22.091 1.00 8.80

ATOM 2884 CA CYS B 234 28.096 -3.107 22.537 1.00 9.04

ATOM 2886 CB CYS B 234 28.166 -4.607 22.801 1.00 9.35

ATOM 2889 SG CYS B 234 28.772 -5.463 21.333 1.00 13.12

ATOM 2891 C CYS B 234 27.653 -2.365 23.799 1.00 8.41

ATOM 2892 O CYS B 234 28.342 -1.442 24.286 1.00 7.89

ATOM 2894 N GLN B 235 26.513 -2.785 24.341 1.00 9.91

ATOM 2895 CA GLN B 235 26.083 -2.238 25.614 1.00 10.56

ATOM 2897 CB GLN B 235 24.836 -2.922 26.147 1.00 11.23

ATOM 2900 CG GLN B 235 23.565 -2.443 25.490 1.00 17.12

ATOM 2903 CD GLN B 235 23.238 -1.009 25.829 1.00 22.92

ATOM 2904 OEl GLN B 235 23.731 -0.460 26.831 1.00 27.54

ATOM 2905 NE2 GLN B 235 22.419 -0.384 24.998 1.00 24.90

ATOM 2908 C GLN B 235 27.197 -2.346 26.639 1.00 8.89

ATOM 2909 O GLN B 235 27.894 -3.335 26.695 1.00 10.22

ATOM 2911 N GLY B 236 27.377 -1.298 27.439 1.00 8.28

ATOM 2912 CA GLY B 236 28.459 -1.247 28.394 1.00 7.77

ATOM 2915 C GLY B 236 29.748 -0.641 27.889 1.00 8.25

ATOM 2916 O GLY B 236 30.646 -0.330 28.675 1.00 8.53

ATOM 2918 N ASP B 237 29.834 -0.423 26.585 1.00 7.21

ATOM 2919 CA ASP B 237 30.990 0.242 25.991 1.00 6.71

ATOM 2921 CB ASP B 237 31.350 -0.427 24.668 1.00 6.01

ATOM 2924 CG ASP B 237 31.863 -1.835 24.841 1.00 7.46

ATOM 2925 ODl ASP B 237 32.605 -2.094 25.797 1.00 6.98

ATOM 2926 OD2 ASP B 237 31.509 -2.697 24.017 1.00 8.87

ATOM 2927 C ASP B 237 30.862 1.745 25.775 1.00 5.25

ATOM 2928 O ASP B 237 31.848 2.401 25.518 1.00 6.39

ATOM 2930 N SER B 238 29.652 2.269 25.865 1.00 6.34

ATOM 2931 CA SER B 238 29.394 3.688 25.617 1.00 6.25

ATOM 2933 CB SER B 238 28.009 4.072 26.055 1.00 6.51

ATOM 2936 OG SER B 238 27.036 3.403 25.252 1.00 9.78

ATOM 2938 C SER B 238 30.334 4.538 26.382 1.00 6.03

ATOM 2939 O SER B 238 30.687 4.226 27.519 1.00 7.65 ATOM 2941 N GLY B 239 30.708 5.651 25.786 1.00 6.68

ATOM 2942 CA GLY B 239 31.582 6.591 26.443 1.00 7.19

ATOM 2945 C GLY B 239 33.040 6.221 26.319 1.00 5.65

ATOM 2946 O GLY B 239 33.910 7.044 26.569 1.00 9.60

ATOM 2948 N GLY B 240 33.334 4.985 25.927 1.00 5.84

ATOM 2949 CA GLY B 240 34.680 4.571 25.678 1.00 7.25

ATOM 2952 C GLY B 240 35.229 5.127 24.367 1.00 7.46

ATOM 2953 O GLY B 240 34.466 5.630 23.506 1.00 6.69

ATOM 2955 N PRO B 241 36.555 5.072 24.223 1.00 7.08

ATOM 2956 CA PRO B 241 37.223 5.665 23.072 1.00 7.22

ATOM 2958 CB PRO B 241 38.680 5.737 23.525 1.00 7.26

ATOM 2961 CG PRO B 241 38.859 4.553 24.418 1.00 6.54

ATOM 2964 CD PRO B 241 37.531 4.512 25.182 1.00 7.47

ATOM 2967 C PRO B 241 37.181 4.874 21.781 1.00 8.16

ATOM 2968 O PRO B 241 37.300 3.657 21.779 1.00 8.29

ATOM 2969 N LEU B 242 37.009 5.627 20.703 1.00 8.03

ATOM 2970 CA LEU B 242 37.417 5.227 19.395 1.00 7.93

ATOM 2972 CB LEU B 242 36.392 5.690 18.383 1.00 9.33

ATOM 2975 CG LEU B 242 36.766 5.338 16.952 1.00 7.83

ATOM 2977 CDl LEU B 242 36.890 3.835 16.749 1.00 9.94

ATOM 2981 CD2 LEU B 242 35.728 5.911 15.993 1.00 8.69

ATOM 2985 C LEU B 242 38.740 5.956 19.214 1.00 8.00

ATOM 2986 O LEU B 242 38.774 7.173 18.968 1.00 6.98

ATOM 2988 N SER B 243 39.837 5.223 19.386 1.00 7.59

ATOM 2989 CA SER B 243 41.174 5.793 19.385 1.00 7.68

ATOM 2991 CB SER B 243 42.040 5.055 20.394 1.00 8.80

ATOM 2994 OG SER B 243 41.452 5.037 21.684 1.00 8.45

ATOM 2996 C SER B 243 41.756 5.615 17.994 1.00 7.99

ATOM 2997 O SER B 243 41.864 4.476 17.534 1.00 8.02

ATOM 2999 N CYS B 244 42.072 6.715 17.322 1.00 7.20

ATOM 3000 CA CYS B 244 42.626 6.651 15.955 1.00 8.20

ATOM 3002 CB CYS B 244 41.857 7.559 15.003 1.00 8.81

ATOM 3005 SG CYS B 244 40.176 7.078 14.657 1.00 9.71

ATOM 3007 C CYS B 244 44.073 7.113 15.951 1.00 8.83

ATOM 3008 O CYS B 244 44.399 8.129 16.537 1.00 8.60

ATOM 3010 N PRO B 245 44.936 6.374 15.253 1.00 8.97

ATOM 3011 CA PRO B 245 46.339 6.712 15.145 1.00 8.16

ATOM 3013 CB PRO B 245 46.982 5.361 14.943 1.00 7.84

ATOM 3016 CG PRO B 245 45.994 4.594 14.190 1.00 7.21

ATOM 3019 CD PRO B 245 44.644 5.097 14.579 1.00 8.78

ATOM 3022 C PRO B 245 46.627 7.598 13.938 1.00 9.87

ATOM 3023 O PRO B 245 46.207 7.300 12.831 1.00 10.73

ATOM 3024 N VAL B 246 47.371 8.667 14.174 1.00 8.95

ATOM 3025 CA VAL B 246 47.887 9.509 13.105 1.00 9.69

ATOM 3027 CB VAL B 246 47.056 10.807 12.942 1.00 10.43

ATOM 3029 CGl VAL B 246 47.679 11.697 11.902 1.00 11.30

ATOM 3033 CG2 VAL B 246 45.585 10.466 12.581 1.00 10.95

ATOM 3037 C VAL B 246 49.334 9.828 13.437 1.00 10.25

ATOM 3038 O VAL B 246 49.619 10.433 14.471 1.00 9.44

ATOM 3040 N GLU B 247 50.249 9.413 12.557 1.00 11.38

ATOM 3041 CA GLU B 247 51.668 9.689 12.735 1.00 11.30

ATOM 3043 CB GLU B 247 52.006 11.160 12.470 1.00 12.35

ATOM 3046 CG GLU B 247 51.745 11.591 11.048 1.00 12.09

ATOM 3049 CD GLU B 247 52.363 12.937 10.724 1.00 15.31

ATOM 3050 OEl GLU B 247 52.886 13.609 11.655 1.00 24.15

ATOM 3051 OE 2 GLU B 247 52.278 13.313 9.552 1.00 26.18

ATOM 3052 C GLU B 247 52.123 9.260 14.131 1.00 11.97

ATOM 3053 O GLU B 247 52.862 9.960 14.796 1.00 12.53

ATOM 3055 N GLY B 248 51.645 8.106 14.578 1.00 9.83

ATOM 3056 CA GLY B 248 52.111 7.551 15.819 1.00 10.74

ATOM 3059 C GLY B 248 51.468 8.068 17.095 1.00 10.59 ATOM 3060 O GLY B 248 51.786 7.582 18.179 1.00 12.66

ATOM 3062 N LEU B 249 50.590 9.049 16.969 1.00 9.34

ATOM 3063 CA LEU B 249 49.849 9.596 18.101 1.00 9.74

ATOM 3065 CB LEU B 249 49.896 11.122 18.108 1.00 9.42

ATOM 3068 CG LEU B 249 51.258 11.783 18.343 1.00 12.99

ATOM 3070 CDl LEU B 249 51.057 13.280 18.529 1.00 18.22

ATOM 3074 CD2 LEU B 249 52.050 11.175 19.535 1.00 15.14

ATOM 3078 C LEU B 249 48.415 9.138 18.007 1.00 9.01

ATOM 3079 O LEU B 249 47.867 9.040 16.925 1.00 10.08

ATOM 3081 N TRP B 250 47.788 8.957 19.168 1.00 9.86

ATOM 3082 CA TRP B 250 46.401 8.482 19.269 1.00 10.02

ATOM 3084 CB TRP B 250 46.270 7.376 20.301 1.00 9.50

ATOM 3087 CG TRP B 250 47.005 6.173 19.899 1.00 10.88

ATOM 3088 CDl TRP B 250 48.314 5.900 20.142 1.00 11.70

ATOM 3090 NEl TRP B 250 48.660 4.698 19.578 1.00 12.07

ATOM 3092 CE2 TRP B 250 47.569 4.181 18.938 1.00 9.91

ATOM 3093 CD2 TRP B 250 46.505 5.100 19.114 1.00 9.96

ATOM 3094 CE3 TRP B 250 45.265 4.805 18.555 1.00 9.01

ATOM 3096 CZ3 TRP B 250 45.127 3.623 17.861 1.00 10.10

ATOM 3098 CH2 TRP B 250 46.203 2.738 17.709 1.00 10.76

ATOM 3100 CZ2 TRP B 250 47.419 3.003 18.243 1.00 10.45

ATOM 3102 C TRP B 250 45.516 9.663 19.603 1.00 9.61

ATOM 3103 O TRP B 250 45.848 10.466 20.477 1.00 9.27

ATOM 3105 N TYR B 251 44.399 9.759 18.884 1.00 8.47

ATOM 3106 CA TYR B 251 43.409 10.818 19.067 1.00 8.78

ATOM 3108 CB TYR B 251 43.276 11.675 17.818 1.00 10.59

ATOM 3111 CG TYR B 251 44.558 12.392 17.492 1.00 9.10

ATOM 3112 CDl TYR B 251 44.829 13.645 18.013 1.00 14.68

ATOM 3114 CEl TYR B 251 46.023 14.278 17.755 1.00 11.47

ATOM 3116 CZ TYR B 251 46.965 13.672 16.969 1.00 14.51

ATOM 3117 OH TYR B 251 48.148 14.313 16.695 1.00 13.62

ATOM 3119 CE2 TYR B 251 46.718 12.427 16.433 1.00 9.74

ATOM 3121 CD2 TYR B 251 45.531 11.787 16.718 1.00 12.00

ATOM 3123 C TYR B 251 42.066 10.192 19.384 1.00 7.79

ATOM 3124 O TYR B 251 41.712 9.139 18.855 1.00 6.71

ATOM 3126 N LEU B 252 41.338 10.855 20.255 1.00 7.26

ATOM 3127 CA LEU B 252 39.982 10.476 20.570 1.00 7.66

ATOM 3129 CB LEU B 252 39.569 11.122 21.873 1.00 8.63

ATOM 3132 CG LEU B 252 38.252 10.639 22.481 1.00 7.56

ATOM 3134 CDl LEU B 252 38.277 9.145 22.684 1.00 10.74

ATOM 3138 CD2 LEU B 252 38.026 11.384 23.794 1.00 10.95

ATOM 3142 C LEU B 252 39.073 10.952 19.456 1.00 8.62

ATOM 3143 O LEU B 252 38.409 11.972 19.577 1.00 8.84

ATOM 3145 N THR B 253 39.018 10.176 18.389 1.00 7.99

ATOM 3146 CA THR B 253 38.217 10.535 17.253 1.00 7.46

ATOM 3148 CB THR B 253 38.552 9.623 16.098 1.00 8.21

ATOM 3150 OGl THR B 253 39.940 9.831 15.786 1.00 8.30

ATOM 3152 CG2 THR B 253 37.701 9.952 14.905 1.00 9.45

ATOM 3156 C THR B 253 36.740 10.464 17.598 1.00 7.79

ATOM 3157 O THR B 253 35.956 11.292 17.160 1.00 7.91

ATOM 3159 N GLY B 254 36.373 9.481 18.400 1.00 8.07

ATOM 3160 CA GLY B 254 34.967 9.270 18.725 1.00 7.68

ATOM 3163 C GLY B 254 34.809 8.655 20.088 1.00 7.39

ATOM 3164 O GLY B 254 35.769 8.199 20.704 1.00 7.61

ATOM 3166 N ILE B 255 33.564 8.687 20.527 1.00 8.26

ATOM 3167 CA ILE B 255 33.104 8.195 21.805 1.00 8.90

ATOM 3169 CB ILE B 255 32.557 9.375 22.641 1.00 9.86

ATOM 3171 CGl ILE B 255 33.693 10.387 22.863 1.00 13.52

ATOM 3174 CDl ILE B 255 33.247 11.640 23.530 1.00 13.14

ATOM 3178 CG2 ILE B 255 31.964 8.897 23.916 1.00 12.86

ATOM 3182 C ILE B 255 31.973 7.239 21.454 1.00 7.55 ATOM 3183 O ILE B 255 31.025 7.624 20.756 1.00 6.31

ATOM 3185 N VAL B 256 32.037 6.020 21.979 1.00 6.73

ATOM 3186 CA VAL B 256 31.017 5.009 21.715 1.00 7.20

ATOM 3188 CB VAL B 256 31.264 3.737 22.517 1.00 6.82

ATOM 3190 CGl VAL B 256 30.094 2.743 22.353 1.00 8.07

ATOM 3194 CG2 VAL B 256 32.622 3.096 22.144 1.00 6.86

ATOM 3198 C VAL B 256 29.655 5.558 22.106 1.00 6.83

ATOM 3199 O VAL B 256 29.450 5.967 23.260 1.00 7.73

ATOM 3201 N SER B 257 28.706 5.569 21.179 1.00 6.20

ATOM 3202 CA SER B 257 27.391 6.125 21.487 1.00 7.48

ATOM 3204 CB SER B 257 27.170 7.386 20.679 1.00 7.88

ATOM 3207 OG SER B 257 25.901 7.933 20.910 1.00 8.49

ATOM 3209 C SER B 257 26.243 5.144 21.287 1.00 8.25

ATOM 3210 O SER B 257 25.469 4.895 22.216 1.00 7.57

ATOM 3212 N TRP B 258 26.123 4.559 20.094 1.00 7.20

ATOM 3213 CA TRP B 258 24.969 3.713 19.797 1.00 7.63

ATOM 3215 CB TRP B 258 23.682 4.534 19.595 1.00 8.81

ATOM 3218 CG TRP B 258 23.660 5.489 18.464 1.00 8.83

ATOM 3219 CDl TRP B 258 24.129 6.771 18.472 1.00 9.62

ATOM 3221 NEl TRP B 258 23.889 7.377 17.289 1.00 9.19

ATOM 3223 CE 2 TRP B 258 23.268 6.486 16.454 1.00 6.85

ATOM 3224 CD2 TRP B 258 23.089 5.288 17.169 1.00 9.17

ATOM 3225 CE 3 TRP B 258 22.456 4.203 16.543 1.00 10.80

ATOM 3227 CZ3 TRP B 258 22.026 4.349 15.249 1.00 8.88

ATOM 3229 CH2 TRP B 258 22.217 5.562 14.560 1.00 6.87

ATOM 3231 CZ2 TRP B 258 22.834 6.642 15.138 1.00 9.36

ATOM 3233 C TRP B 258 25.197 2.808 18.598 1.00 7.57

ATOM 3234 O TRP B 258 26.188 2.934 17.891 1.00 7.23

ATOM 3236 N GLY B 259 24.280 1.873 18.413 1.00 7.94

ATOM 3237 CA GLY B 259 24.280 0.999 17.261 1.00 8.30

ATOM 3240 C GLY B 259 23.078 0.116 17.426 1.00 9.50

ATOM 3241 O GLY B 259 22.144 0.469 18.163 1.00 9.25

ATOM 3243 N ASP B 260 23.084 -1.045 16.811 1.00 10.67

ATOM 3244 CA ASP B 260 21.982 -1.966 17.049 1.00 11.84

ATOM 3246 CB ASP B 260 21.503 -2.540 15.712 1.00 11.71

ATOM 3249 CG ASP B 260 20.726 -1.546 14.920 1.00 15.67

ATOM 3250 ODl ASP B 260 20.660 -0.369 15.324 1.00 13.30

ATOM 3251 OD2 ASP B 260 20.117 -1.955 13.918 1.00 19.15

ATOM 3252 C ASP B 260 22.396 -3.020 18.078 1.00 12.66

ATOM 3253 O ASP B 260 23.195 -2.729 18.988 1.00 12.59

ATOM 3255 N ALA B 261 21.872 -4.233 17.988 1.00 12.97

ATOM 3256 CA ALA B 261 22.319 -5.274 18.882 1.00 13.53

ATOM 3258 CB ALA B 261 21.537 -6.564 18.655 1.00 15.01

ATOM 3262 C ALA B 261 23.807 -5.512 18.710 1.00 14.71

ATOM 3263 O ALA B 261 24.394 -5.191 17.673 1.00 15.29

ATOM 3265 N CYS B 262 24.422 -6.029 19.761 1.00 14.10

ATOM 3266 CA CYS B 262 25.852 -6.249 19.800 1.00 14.30

ATOM 3268 CB CYS B 262 26.189 -6.981 21.114 1.00 14.15

ATOM 3271 SG CYS B 262 27.866 -7.309 21.460 1.00 14.94

ATOM 3273 C CYS B 262 26.292 -7.060 18.589 1.00 15.38

ATOM 3274 O CYS B 262 25.994 -8.250 18.501 1.00 16.88

ATOM 3276 N GLY B 263 26.977 -6.394 17.663 1.00 16.89

ATOM 3277 CA GLY B 263 27.560 -7.031 16.493 1.00 17.06

ATOM 3280 C GLY B 263 26.579 -7.259 15.357 1.00 18.62

ATOM 3281 O GLY B 263 26.842 -8.084 14.466 1.00 18.33

ATOM 3283 N ALA B 264 25.448 -6.541 15.385 1.00 18.16

ATOM 3284 CA ALA B 264 24.419 -6.679 14.357 1.00 17.24

ATOM 3286 CB ALA B 264 23.263 -5.669 14.595 1.00 17.38

ATOM 3290 C ALA B 264 25.011 -6.459 12.975 1.00 16.85

ATOM 3291 O ALA B 264 25.960 -5.684 12.781 1.00 18.24

ATOM 3293 N ARG B 265 24.408 -7.124 12.007 1.00 16.78 ATOM 3294 CA ARG B 265 24.773 -6.958 10.622 1.00 17.09

ATOM 3296 CB ARG B 265 24.229 -8.142 9.826 1.00 16.94

ATOM 3299 CG ARG B 265 24.859 -9.424 10.290 1.00 19.59

ATOM 3302 CD ARG B 265 24.602 -10.574 9.384 1.00 21.77

ATOM 3305 NE ARG B 265 25.011 -10.347 7.992 1.00 24.34

ATOM 3307 CZ ARG B 265 25.145 -11.329 7.106 1.00 24.26

ATOM 3308 NHl ARG B 265 25.477 -11.060 5.855 1.00 20.98

ATOM 3311 NH2 ARG B 265 24.941 -12.591 7.467 1.00 26.33

ATOM 3314 C ARG B 265 24.279 -5.619 10.048 1.00 15.56

ATOM 3315 O ARG B 265 23.263 -5.046 10.488 1.00 15.10

ATOM 3317 N ASN B 266 25.071 -5.082 9.123 1.00 16.08

ATOM 3318 CA ASN B 266 24.715 -3.901 8.353 1.00 16.56

ATOM 3320 CB ASN B 266 23.436 -4.155 7.553 1.00 17.98

ATOM 3323 CG ASN B 266 23.502 -5.443 6.759 1.00 21.90

ATOM 3324 ODl ASN B 266 24.428 -5.640 5.991 1.00 26.50

ATOM 3325 ND2 ASN B 266 22.515 -6.312 6.940 1.00 25.69

ATOM 3328 C ASN B 266 24.570 -2.647 9.181 1.00 15.83

ATOM 3329 O ASN B 266 24.013 -1.658 8.723 1.00 17.17

ATOM 3331 N ARG B 267 25.115 -2.658 10.389 1.00 13.95

ATOM 3332 CA ARG B 267 24.942 -1.522 11.280 1.00 14.44

ATOM 3334 CB ARG B 267 23.778 -1.784 12.234 1.00 15.27

ATOM 3337 CG ARG B 267 22.438 -1.981 11.543 1.00 16.64

ATOM 3340 CD ARG B 267 21.803 -0.665 11.086 1.00 15.87

ATOM 3343 NE ARG B 267 20.803 -0.885 10.038 1.00 18.43

ATOM 3345 CZ ARG B 267 19.560 -1.292 10.244 1.00 15.80

ATOM 3346 NHl ARG B 267 19.092 -1.494 11.457 1.00 18.97

ATOM 3349 NH2 ARG B 267 18.747 -1.456 9.203 1.00 18.16

ATOM 3352 C ARG B 267 26.237 -1.308 12.040 1.00 12.81

ATOM 3353 O ARG B 267 26.339 -1.666 13.241 1.00 12.28

ATOM 3355 N PRO B 268 27.217 -0.674 11.377 1.00 11.57

ATOM 3356 CA PRO B 268 28.502 -0.445 12.058 1.00 11.14

ATOM 3358 CB PRO B 268 29.361 0.222 10.985 1.00 11.08

ATOM 3361 CG PRO B 268 28.660 -0.019 9.698 1.00 14.78

ATOM 3364 CD PRO B 268 27.211 -0.102 10.021 1.00 12.24

ATOM 3367 C PRO B 268 28.308 0.504 13.229 1.00 10.60

ATOM 3368 O PRO B 268 27.506 1.419 13.144 1.00 12.68

ATOM 3369 N GLY B 269 29.042 0.321 14.315 1.00 10.62

ATOM 3370 CA GLY B 269 28.794 1.147 15.488 1.00 9.01

ATOM 3373 C GLY B 269 28.850 2.634 15.215 1.00 9.33

ATOM 3374 O GLY B 269 29.637 3.118 14.369 1.00 9.43

ATOM 3376 N VAL B 270 28.048 3.383 15.965 1.00 9.10

ATOM 3377 CA VAL B 270 28.017 4.823 15.854 1.00 7.47

ATOM 3379 CB VAL B 270 26.615 5.382 15.647 1.00 8.79

ATOM 3381 CGl VAL B 270 26.662 6.904 15.397 1.00 8.14

ATOM 3385 CG2 VAL B 270 25.931 4.681 14.482 1.00 8.84

ATOM 3389 C VAL B 270 28.669 5.466 17.090 1.00 8.51

ATOM 3390 O VAL B 270 28.466 5.016 18.241 1.00 6.24

ATOM 3392 N TYR B 271 29.446 6.500 16.794 1.00 6.89

ATOM 3393 CA TYR B 271 30.292 7.212 17.767 1.00 7.40

ATOM 3395 CB TYR B 271 31.775 6.947 17.452 1.00 8.53

ATOM 3398 CG TYR B 271 32.144 5.495 17.502 1.00 5.52

ATOM 3399 CDl TYR B 271 32.839 4.979 18.601 1.00 7.20

ATOM 3401 CEl TYR B 271 33.200 3.674 18.666 1.00 8.75

ATOM 3403 CZ TYR B 271 32.837 2.809 17.633 1.00 9.28

ATOM 3404 OH TYR B 271 33.140 1.440 17.706 1.00 10.29

ATOM 3406 CE2 TYR B 271 32.138 3.301 16.535 1.00 8.03

ATOM 3408 CD2 TYR B 271 31.806 4.622 16.474 1.00 5.89

ATOM 3410 C TYR B 271 30.051 8.697 17.684 1.00 8.22

ATOM 3411 O TYR B 271 29.853 9.211 16.606 1.00 7.44

ATOM 3413 N THR B 272 30.070 9.394 18.813 1.00 7.77

ATOM 3414 CA THR B 272 30.065 10.842 18.789 1.00 8.13 ATOM 3416 CB THR B 272 29.852 11.389 20.167 1.00 8.95

ATOM 3418 OGl THR B 272 28.658 10.796 20.696 1.00 8.25

ATOM 3420 CG2 THR B 272 29.760 12.880 20.153 1.00 12.45

ATOM 3424 C THR B 272 31.403 11.311 18.252 1.00 8.12

ATOM 3425 O THR B 272 32.458 10.852 18.717 1.00 9.44

ATOM 3427 N LEU B 273 31.363 12.203 17.276 1.00 8.26

ATOM 3428 CA LEU B 273 32.577 12.692 16.630 1.00 8.19

ATOM 3430 CB LEU B 273 32.266 13.245 15.245 1.00 7.90

ATOM 3433 CG LEU B 273 33.488 13.597 14.419 1.00 8.60

ATOM 3435 CDl LEU B 273 34.327 12.357 14.089 1.00 10.12

ATOM 3439 CD2 LEU B 273 33.057 14.295 13.129 1.00 12.87

ATOM 3443 C LEU B 273 33.184 13.769 17.472 1.00 8.73

ATOM 3444 O LEU B 273 32.690 14.894 17.486 1.00 9.38

ATOM 3446 N ALA B 274 34.270 13.457 18.153 1.00 8.53

ATOM 3447 CA ALA B 274 34.849 14.407 19.119 1.00 8.93

ATOM 3449 CB ALA B 274 36.013 13.756 19.842 1.00 8.81

ATOM 3453 C ALA B 274 35.274 15.762 18.537 1.00 9.60

ATOM 3454 O ALA B 274 35.127 16.800 19.209 1.00 9.55

ATOM 3456 N SER B 275 35.802 15.776 17.318 1.00 8.97

ATOM 3457 CA SER B 275 36.198 17.051 16.711 1.00 8.79

ATOM 3459 CB SER B 275 36.754 16.859 15.314 1.00 8.21

ATOM 3462 OG SER B 275 35.810 16.273 14.432 1.00 12.14

ATOM 3464 C SER B 275 35.039 18.036 16.681 1.00 8.83

ATOM 3465 O SER B 275 35.251 19.241 16.867 1.00 11.07

ATOM 3467 N SER B 276 33.816 17.544 16.469 1.00 10.33

ATOM 3468 CA SER B 276 32.643 18.420 16.397 1.00 11.32

ATOM 3470 CB SER B 276 31.418 17.646 15.947 1.00 12.43

ATOM 3473 OG SER B 276 31.668 17.078 14.683 1.00 16.30

ATOM 3475 C SER B 276 32.307 19.103 17.717 1.00 11.51

ATOM 3476 O SER B 276 31.521 20.074 17.746 1.00 12.20

ATOM 3478 N TYR B 277 32.863 18.588 18.806 1.00 10.77

ATOM 3479 CA TYR B 277 32.629 19.124 20.137 1.00 9.72

ATOM 3481 CB TYR B 277 32.107 18.018 21.063 1.00 9.67

ATOM 3484 CG TYR B 277 30.752 17.571 20.615 1.00 6.11

ATOM 3485 CDl TYR B 277 29.614 18.221 21.060 1.00 8.86

ATOM 3487 CEl TYR B 277 28.368 17.869 20.607 1.00 10.94

ATOM 3489 CZ TYR B 277 28.237 16.859 19.680 1.00 11.04

ATOM 3490 OH TYR B 277 26.970 16.496 19.248 1.00 12.13

ATOM 3492 CE 2 TYR B 277 29.359 16.194 19.212 1.00 9.30

ATOM 3494 CD2 TYR B 277 30.608 16.561 19.675 1.00 6.76

ATOM 3496 C TYR B 277 33.866 19.775 20.738 1.00 8.60

ATOM 3497 O TYR B 277 33.863 20.223 21.888 1.00 8.77

ATOM 3499 N ALA B 278 34.948 19.826 19.966 1.00 10.02

ATOM 3500 CA ALA B 278 36.193 20.377 20.478 1.00 10.71

ATOM 3502 CB ALA B 278 37.248 20.363 19.419 1.00 11.08

ATOM 3506 C ALA B 278 36.022 21.795 20.984 1.00 11.60

ATOM 3507 O ALA B 278 36.542 22.131 22.050 1.00 11.79

ATOM 3509 N SER B 279 35.331 22.644 20.222 1.00 11.75

ATOM 3510 CA SER B 279 35.160 24.044 20.645 1.00 13.81

ATOM 3512 CB SER B 279 34.516 24.897 19.540 1.00 14.55

ATOM 3515 OG SER B 279 33.155 24.577 19.416 1.00 23.33

ATOM 3517 C SER B 279 34.351 24.119 21.929 1.00 13.41

ATOM 3518 O SER B 279 34.694 24.893 22.845 1.00 12.62

ATOM 3520 N TRP B 280 33.325 23.278 22.023 1.00 13.19

ATOM 3521 CA TRP B 280 32.526 23.191 23.233 1.00 13.35

ATOM 3523 CB TRP B 280 31.343 22.237 23.047 1.00 14.42

ATOM 3526 CG TRP B 280 30.573 22.046 24.302 1.00 13.18

ATOM 3527 CDl TRP B 280 29.755 22.953 24.900 1.00 19.13

ATOM 3529 NEl TRP B 280 29.217 22.416 26.047 1.00 19.05

ATOM 3531 CE 2 TRP B 280 29.691 21.144 26.209 1.00 15.84

ATOM 3532 CD2 TRP B 280 30.550 20.877 25.122 1.00 15.57 ATOM 3533 CE3 TRP B 280 31.164 19.619 25.037 1.00 14.66

ATOM 3535 CZ3 TRP B 280 30.911 18.694 26.027 1.00 15.91

ATOM 3537 CH2 TRP B 280 30.039 18.990 27.082 1.00 16.57

ATOM 3539 CZ2 TRP B 280 29.429 20.205 27.193 1.00 18.87

ATOM 3541 C TRP B 280 33.373 22.735 24.411 1.00 12.13

ATOM 3542 O TRP B 280 33.332 23.339 25.491 1.00 12.11

ATOM 3544 N ILE B 281 34.164 21.684 24.205 1.00 11.84

ATOM 3545 CA ILE B 281 34.953 21.124 25.288 1.00 12.71

ATOM 3547 CB ILE B 281 35.714 19.899 24.846 1.00 11.79

ATOM 3549 CGl ILE B 281 34.745 18.756 24.545 1.00 12.35

ATOM 3552 CDl ILE B 281 35.377 17.614 23.801 1.00 12.73

ATOM 3556 CG2 ILE B 281 36.730 19.483 25.927 1.00 11.51

ATOM 3560 C ILE B 281 35.932 22.177 25.815 1.00 13.16

ATOM 3561 O ILE B 281 35.990 22.450 27.008 1.00 13.02

ATOM 3563 N GLN B 282 36.682 22.791 24.910 1.00 13.64

ATOM 3564 CA GLN B 282 37.660 23.789 25.312 1.00 15.46

ATOM 3566 CB GLN B 282 38.518 24.169 24.118 1.00 15.51

ATOM 3569 CG GLN B 282 39.657 25.078 24.484 1.00 16.46

ATOM 3572 CD GLN B 282 40.673 25.138 23.391 1.00 17.98

ATOM 3573 OEl GLN B 282 40.386 24.758 22.218 1.00 15.21

ATOM 3574 NE2 GLN B 282 41.869 25.608 23.740 1.00 18.77

ATOM 3577 C GLN B 282 37.012 25.025 25.934 1.00 17.16

ATOM 3578 O GLN B 282 37.604 25.642 26.839 1.00 17.63

ATOM 3580 N SER B 283 35.822 25.395 25.466 1.00 17.65

ATOM 3581 CA SER B 283 35.097 26.525 26.045 1.00 19.81

ATOM 3583 CB SER B 283 33.862 26.884 25.224 1.00 21.63

ATOM 3586 OG SER B 283 32.853 25.894 25.336 1.00 29.41

ATOM 3588 C SER B 283 34.701 26.232 27.489 1.00 21.07

ATOM 3589 O SER B 283 34.819 27.101 28.353 1.00 20.32

ATOM 3591 N LYS B 284 34.271 24.999 27.761 1.00 19.26

ATOM 3592 CA LYS B 284 33.835 24.614 29.122 1.00 20.16

ATOM 3594 CB LYS B 284 33.016 23.307 29.120 1.00 19.03

ATOM 3597 CG LYS B 284 31.762 23.320 28.267 1.00 24.73

ATOM 3600 CD LYS B 284 30.773 24.394 28.679 1.00 26.60

ATOM 3603 CE LYS B 284 30.245 24.185 30.065 1.00 27.49

ATOM 3606 NZ LYS B 284 29.063 25.072 30.248 1.00 32.11

ATOM 3610 C LYS B 284 34.997 24.407 30.065 1.00 18.56

ATOM 3611 O LYS B 284 34.895 24.695 31.258 1.00 19.28

ATOM 3613 N VAL B 285 36.078 23.849 29.541 1.00 18.93

ATOM 3614 CA VAL B 285 37.204 23.432 30.343 1.00 20.31

ATOM 3616 CB VAL B 285 37.310 21.885 30.471 1.00 19.35

ATOM 3618 CGl VAL B 285 38.390 21.512 31.451 1.00 18.99

ATOM 3622 CG2 VAL B 285 35.977 21.263 30.920 1.00 20.68

ATOM 3626 C VAL B 285 38.472 24.002 29.713 1.00 20.72

ATOM 3627 O VAL B 285 39.007 23.463 28.765 1.00 18.59

ATOM 3629 N THR B 286 38.942 25.106 30.272 1.00 23.67

ATOM 3630 CA THR B 286 40.113 25.798 29.735 1.00 24.56

ATOM 3632 CB THR B 286 40.352 27.109 30.505 1.00 25.28

ATOM 3634 OGl THR B 286 40.182 26.887 31.922 1.00 30.93

ATOM 3636 CG2 THR B 286 39.355 28.123 30.042 1.00 20.56

ATOM 3640 C THR B 286 41.372 24.917 29.707 1.00 25.62

ATOM 3641 O THR B 286 42.154 25.019 28.760 1.00 27.26

ATOM 3643 N GLU B 287 41.516 24.040 30.706 1.00 25.37

ATOM 3644 CA GLU B 287 42.610 23.037 30.822 1.00 25.08

ATOM 3646 CB GLU B 287 42.471 22.282 32.179 1.00 26.08

ATOM 3649 CG GLU B 287 43.050 20.797 32.325 1.00 27.75

ATOM 3652 CD GLU B 287 42.558 20.054 33.617 1.00 29.31

ATOM 3653 OEl GLU B 287 41.906 20.709 34.472 1.00 42.03

ATOM 3654 OE2 GLU B 287 42.817 18.826 33.814 1.00 27.08

ATOM 3655 C GLU B 287 42.681 22.037 29.654 1.00 24.53

ATOM 3656 O GLU B 287 43.726 21.422 29.414 1.00 24.92 ATOM 3658 N LEU B 288 41.566 21.848 28.952 1.00 21.88

ATOM 3659 CA LEU B 288 41.503 20.895 27.860 1.00 21.03

ATOM 3661 CB LEU B 288 40.134 20.217 27.808 1.00 19.84

ATOM 3664 CG LEU B 288 39.888 19.320 29.019 1.00 19.18

ATOM 3666 CDl LEU B 288 38.528 18.650 28.939 1.00 16.50

ATOM 3670 CD2 LEU B 288 40.992 18.285 29.161 1.00 20.43

ATOM 3674 C LEU B 288 41.799 21.620 26.563 1.00 20.10

ATOM 3675 O LEU B 288 41.044 22.489 26.153 1.00 21.86

ATOM 3677 N GLN B 289 42.911 21.251 25.941 1.00 19.25

ATOM 3678 CA GLN B 289 43.375 21.874 24.715 1.00 19.69

ATOM 3680 CB GLN B 289 44.758 22.484 24.913 1.00 19.62

ATOM 3683 CG GLN B 289 44.702 23.792 25.708 1.00 22.41

ATOM 3686 CD GLN B 289 46.018 24.561 25.708 1.00 21.76

ATOM 3687 OEl GLN B 289 46.866 24.390 24.830 1.00 31.99

ATOM 3688 NE 2 GLN B 289 46.174 25.432 26.680 1.00 28.73

ATOM 3691 C GLN B 289 43.427 20.822 23.626 1.00 18.12

ATOM 3692 O GLN B 289 44.339 20.005 23.597 1.00 19.27

ATOM 3694 N PRO B 290 42.411 20.803 22.760 1.00 18.32

ATOM 3695 CA PRO B 290 42.440 19.902 21.625 1.00 18.01

ATOM 3697 CB PRO B 290 41.162 20.257 20.866 1.00 18.20

ATOM 3700 CG PRO B 290 40.256 20.811 21.894 1.00 18.45

ATOM 3703 CD PRO B 290 41.160 21.568 22.816 1.00 17.57

ATOM 3706 C PRO B 290 43.673 20.127 20.757 1.00 19.21

ATOM 3707 O PRO B 290 44.170 21.253 20.669 1.00 18.91

ATOM 3708 N ARG B 291 44.176 19.058 20.163 1.00 17.91

ATOM 3709 CA ARG B 291 45.406 19.108 19.409 1.00 18.64

ATOM 3711 CB ARG B 291 46.302 17.936 19.780 1.00 20.55

ATOM 3714 CG ARG B 291 46.556 17.797 21.274 1.00 26.33

ATOM 3717 CD ARG B 291 47.275 19.016 21.831 1.00 36.16

ATOM 3720 NE ARG B 291 47.289 19.039 23.293 1.00 37.96

ATOM 3722 CZ ARG B 291 47.719 20.062 24.028 1.00 42.27

ATOM 3723 NHl ARG B 291 48.182 21.171 23.448 1.00 45.77

ATOM 3726 NH2 ARG B 291 47.689 19.977 25.355 1.00 44.51

ATOM 3729 C ARG B 291 45.098 19.076 17.933 1.00 18.56

ATOM 3730 O ARG B 291 44.181 18.390 17.489 1.00 17.58

ATOM 3732 N VAL B 292 45.862 19.836 17.170 1.00 18.20

ATOM 3733 CA VAL B 292 45.701 19.836 15.731 1.00 18.70

ATOM 3735 CB VAL B 292 46.460 20.991 15.078 1.00 20.18

ATOM 3737 CGl VAL B 292 46.436 20.828 13.575 1.00 21.86

ATOM 3741 CG2 VAL B 292 45.790 22.313 15.477 1.00 20.58

ATOM 3745 C VAL B 292 46.206 18.499 15.212 1.00 18.65

ATOM 3746 O VAL B 292 47.276 18.035 15.601 1.00 20.39

ATOM 3748 N VAL B 293 45.411 17.872 14.360 1.00 18.41

ATOM 3749 CA VAL B 293 45.735 16.561 13.838 1.00 18.99

ATOM 3751 CB VAL B 293 44.461 15.746 13.642 1.00 16.99

ATOM 3753 CGl VAL B 293 44.780 14.440 12.933 1.00 19.46

ATOM 3757 CG2 VAL B 293 43.789 15.522 14.968 1.00 19.42

ATOM 3761 C VAL B 293 46.374 16.752 12.472 1.00 20.05

ATOM 3762 O VAL B 293 45.763 17.396 11.596 1.00 19.03

ATOM 3764 N PRO B 294 47.579 16.189 12.270 1.00 22.24

ATOM 3765 CA PRO B 294 48.266 16.356 10.994 1.00 24.80

ATOM 3767 CB PRO B 294 49.457 15.394 11.099 1.00 25.34

ATOM 3770 CG PRO B 294 49.688 15.200 12.531 1.00 23.89

ATOM 3773 CD PRO B 294 48.367 15.390 13.226 1.00 22.33

ATOM 3776 C PRO B 294 47.392 15.990 9. 795 1.00 26.87

ATOM 3777 O PRO B 294 46.602 15.038 9. 1.00 27.14

ATOM 3778 N GLN B 295 47.527 16.767 8.715 1.00 30.76

ATOM 3779 CA GLN B 295 46.846 16.541 7.419 1.00 32.87

ATOM 3781 CB GLN B 295 47.816 16.789 6.253 1.00 34.09

ATOM 3784 CG GLN B 295 48.314 18.221 6.063 1.00 38.55

ATOM 3787 CD GLN B 295 49.316 18.319 4.916 1.00 37.41 ATOM 3788 OEl GLN B 295 49.373 17.435 4.056 1.00 44.86

ATOM 3789 NE2 GLN B 295 50.122 19.387 4.907 1.00 45.39

ATOM 3792 C GLN B 295 46.269 15.138 7.248 1.00 34.48

ATOM 3793 O GLN B 295 46.914 14.255 6.657 1.00 37.03

ATOM 3795 N PHE I 1 20.655 -0.013 20.455 1.00 11.14

ATOM 3796 CA PHE I 1 20.279 1.325 20.966 1.00 10.35

ATOM 3798 CB PHE I 1 19.819 2.202 19.838 1.00 11.18

ATOM 3801 CG PHE I 1 18.665 1.647 19.067 1.00 13.20

ATOM 3802 CDl PHE I 1 18.857 1.068 17.823 1.00 13.90

ATOM 3804 CEl PHE I 1 17.775 0.570 17.092 1.00 14.04

ATOM 3806 CZ PHE I 1 16.512 0.615 17.638 1.00 16.00

ATOM 3808 CE2 PHE I 1 16.311 1.162 18.881 1.00 17.34

ATOM 3810 CD2 PHE I 1 17.387 1.677 19.601 1.00 17.33

ATOM 3812 C PHE I 1 21.495 2.006 21.573 1.00 10.63

ATOM 3813 O PHE I 1 22.615 1.792 21.134 1.00 9.20

ATOM 3817 N PHE I 21.254 2.860 22.549 1.00 9.84

ATOM 3818 CA PHE I 22.326 3.641 23.155 1.00 9.56

ATOM 3820 CB PHE I 21.742 4.904 23.777 1.00 10.61

ATOM 3823 CG PHE I 21.233 5.826 22.729 1.00 11.00

ATOM 3824 CDl PHE I 22.091 6.701 22.110 1.00 15.32

ATOM 3826 CEl PHE I 21.661 7.496 21.088 1.00 20.99

ATOM 3828 CZ PHE I 20.373 7.385 20.619 1.00 15.77

ATOM 3830 CE2 PHE I 19.513 6.512 21.200 1.00 15.77

ATOM 3832 CD2 PHE I 19.945 5.707 22.253 1.00 15.79

ATOM 3834 C PHE I 23.126 2.800 24.109 1.00 10.12

ATOM 3835 O PHE I 22.574 2.188 25.013 1.00 12.17

ATOM 3837 N ARM I 3 24.436 2.840 23.950 1.00 9.15

ATOM 3838 CA ARM I 3 25.327 1.855 24.573 1.00 9.03

ATOM 3840 CB ARM I 3 26.368 1.532 23.509 1.00 9.35

ATOM 3843 CG ARM I 3 25.738 0.562 22.514 1.00 9.48

ATOM 3846 CD ARM I 3 26.607 0.417 21.280 1.00 9.57

ATOM 3849 NE ARM I 3 26.103 -0.617 20.394 1.00 10.29

ATOM 3851 CZ ARM I 3 26.587 -0.872 19.180 1.00 12.36

ATOM 3852 NH2 ARM I 3 26.022 -1.877 18.519 1.00 11.37

ATOM 3855 NHl ARM I 3 27.531 -0.203 18.650 1.00 8.18

ATOM 3857 C ARM I 3 25.868 2.199 25.948 1.00 10.23

ATOM 3858 O ARM I 3 26.742 1.508 26.492 1.00 9.27

ATOM 3859 CM ARM I 3 25.173 3.230 26.799 1.00 10.14

ATOM 3864 03 GOL G 1 49.795 9.871 21.026 1.00 30.74

ATOM 3866 C3 GOL G 1 49.221 8.963 21.888 1.00 12.88

ATOM 3869 C2 GOL G 1 49.197 9.627 23.248 1.00 21.97

ATOM 3871 02 GOL G 1 49.492 8.610 24.180 1.00 32.85

ATOM 3873 Cl GOL G 1 47.815 10.160 23.562 1.00 19.02

ATOM 3876 Ol GOL G 1 47.314 10.994 22.558 1.00 13.88

ATOM 3878 03 GOL G 2 17.889 2.035 35.657 1.00 62.85

ATOM 3880 C3 GOL G 2 16.789 2.675 36.274 1.00 60.26

ATOM 3883 C2 GOL G 2 17.034 4.173 36.399 1.00 57.61

ATOM 3885 02 GOL G 17.677 4.432 37.621 1.00 57.83

ATOM 3887 Cl GOL G 17.858 4.701 35.226 1.00 56.15

ATOM 3890 Ol GOL G 2 17.658 6.092 35.097 1.00 53.68

ATOM 3892 03 GOL G 3 49.776 3.628 23.813 1.00 45.33

ATOM 3894 C3 GOL G 3 48.804 3.177 22.880 1.00 43.20

ATOM 3897 C2 GOL G 3 49.136 1.781 22.343 1.00 39.85

ATOM 3899 02 GOL G 3 49.470 0.897 23.392 1.00 39.89

ATOM 3901 Cl GOL G 3 47.961 1.201 21.572 1.00 34.98

ATOM 3904 Ol GOL G 3 48.348 -0.023 20.967 1.00 32.78

ATOM 3906 S SO4 S 1 23.683 -5.627 23.443 1.00 12.85

ATOM 3907 Ol SO4 S 1 24.259 -6.740 24.226 1.00 12.93

ATOM 3908 02 SO4 S 1 23.106 -6.191 22.215 1.00 13.99

ATOM 3909 03 SO4 S 1 22.614 -4.989 24.191 1.00 12.25

ATOM 3910 04 SO4 S 1 24.741 -4.656 23.103 1.00 12.07 ATOM 3911 S SO4 S 2 33.380 24.826 15.496 1.00 40.66

ATOM 3912 Ol SO4 S 2 33.459 23.461 16.010 1.00 42.94

ATOM 3913 02 SO4 S 34.537 25.066 14.625 1.00 38.04

ATOM 3914 03 SO4 S 32.157 24.925 14.694 1.00 42.83

ATOM 3915 04 SO4 S 2 33.303 25.795 16.584 1.00 38.74

ATOM 3916 OH2 HOH W 1 40.429 2.683 22.075 1.00 8.70

ATOM 3919 OH2 HOH W 2 33.471 -0.110 28.787 1.00 7.42

ATOM 3922 OH2 HOH W 3 30.071 -6.792 29.754 1.00 12.19

ATOM 3925 OH2 HOH W 4 34.086 -5.943 26.084 1.00 7.43

ATOM 3928 OH2 HOH W 5 14.619 2.539 2.560 1.00 12.84

ATOM 3931 OH2 HOH W 6 24.170 -2.589 21.354 1.00 11.35

ATOM 3934 OH2 HOH W 7 36.950 13.527 15.987 1.00 9.04

ATOM 3937 OH2 HOH W 8 30.658 -2.674 13.482 1.00 13.48

ATOM 3940 OH2 HOH W 9 29.744 3.633 41.636 1.00 10.51

ATOM 3943 OH2 HOH W 10 20.255 -5.644 15.978 1.00 17.64

ATOM 3946 OH2 HOH W 11 31. Ill 10.582 42.353 1.00 12.07

ATOM 3949 OH2 HOH W 12 35.816 -8.963 22.132 1.00 12.38

ATOM 3952 OH2 HOH W 13 34.310 1.513 26.674 1.00 7.88

ATOM 3955 OH2 HOH W 14 37.254 14.470 13.092 1.00 13.01

ATOM 3958 OH2 HOH W 15 40.651 1.208 34.309 1.00 17.17

ATOM 3961 OH2 HOH W 16 43.143 4.211 32.778 1.00 11.56

ATOM 3964 OH2 HOH W 17 40.941 -3.147 39.576 1.00 12.64

ATOM 3967 OH2 HOH W 18 32.219 -0.261 16.034 1.00 11.08

ATOM 3970 OH2 HOH W 19 22.016 -1.428 22.526 1.00 14.75

ATOM 3973 OH2 HOH W 20 49.188 8.464 9.992 1.00 16.72

ATOM 3976 OH2 HOH W 21 34.997 -0.016 37.489 1.00 18.07

ATOM 3979 OH2 HOH W 22 43.874 1.321 15.460 1.00 12.64

ATOM 3982 OH2 HOH W 23 29.320 2.295 18.884 1.00 10.10

ATOM 3985 OH2 HOH W 24 49.867 13.111 15.074 1.00 12.82

ATOM 3988 OH2 HOH W 25 40.737 -6.239 16.293 1.00 14.96

ATOM 3991 OH2 HOH W 26 37.589 17.205 20.676 1.00 14.47

ATOM 3994 OH2 HOH W 27 43.681 15.408 26.036 1.00 18.83

ATOM 3997 OH2 HOH W 28 25.048 9.775 19.131 1.00 16.14

ATOM 4000 OH2 HOH W 29 36.927 13.018 10.809 1.00 15.78

ATOM 4003 OH2 HOH W 30 35.662 8.788 25.484 1.00 16.83

ATOM 4006 OH2 HOH W 31 32.219 3.919 2.722 1.00 19.51

ATOM 4009 OH2 HOH W 32 51.533 7.519 20.876 1.00 15.04

ATOM 4012 OH2 HOH W 33 26.355 12.023 19.580 1.00 13.13

ATOM 4015 OH2 HOH W 34 45.635 2.261 11.636 1.00 14.44

ATOM 4018 OH2 HOH W 35 16.637 9.113 10.509 1.00 14.21

ATOM 4021 OH2 HOH W 36 21.713 -0.787 7.302 1.00 16.96

ATOM 4024 OH2 HOH W 37 39.449 23.082 18.254 1.00 21.68

ATOM 4027 OH2 HOH W 38 10.334 1.631 12.918 1.00 15.28

ATOM 4030 OH2 HOH W 39 34.338 21.820 17.605 1.00 15.08

ATOM 4033 OH2 HOH W 40 48.880 3.553 37.949 1.00 16.79

ATOM 4036 OH2 HOH W 41 28.158 -3.885 14.003 1.00 21.02

ATOM 4039 OH2 HOH W 42 44.753 2.054 8.955 1.00 12.60

ATOM 4042 OH2 HOH W 43 19.882 13.475 22.195 1.00 20.92

ATOM 4045 OH2 HOH W 44 46.521 8.188 10.075 1.00 13.11

ATOM 4048 OH2 HOH W 45 32.028 22.414 19.582 1.00 14.04

ATOM 4051 OH2 HOH W 46 30.760 8.620 9.415 1.00 16.52

ATOM 4054 OH2 HOH W 47 54.979 9.815 16.844 1.00 15.66

ATOM 4057 OH2 HOH W 48 17.017 8.094 18.906 1.00 17.97

ATOM 4060 OH2 HOH W 49 25.089 -2.272 15.499 1.00 21.68

ATOM 4063 OH2 HOH W 50 13.771 3.669 18.670 1.00 20.19

ATOM 4066 OH2 HOH W 51 24.084 -1.295 42.931 1.00 17.90

ATOM 4069 OH2 HOH W 52 18.516 2.572 23.645 1.00 24.03

ATOM 4072 OH2 HOH W 53 38.340 -11.979 23.925 1.00 23.13

ATOM 4075 OH2 HOH W 54 19.660 -4.455 13.535 1.00 17.16

ATOM 4078 OH2 HOH W 55 33.880 -1.775 6.981 1.00 14.82

ATOM 4081 OH2 HOH W 56 26.414 14.108 18.077 1.00 19.50 ATOM 4084 OH2 HOH W 57 44.144 17.127 23.890 1.00 14.23

ATOM 4087 OH2 HOH W 58 18.899 -2.022 19.473 1.00 17.55

ATOM 4090 OH2 HOH W 59 33.035 11.341 3.678 1.00 31.44

ATOM 4093 OH2 HOH W 60 17.741 6.630 11.196 1.00 17.74

ATOM 4096 OH2 HOH W 61 32.448 -1.306 41.804 1.00 20.33

ATOM 4099 OH2 HOH W 62 17.314 -1.793 14.717 1.00 23.41

ATOM 4102 OH2 HOH W 63 35.826 2.704 5.379 1.00 18.07

ATOM 4105 OH2 HOH W 64 15.233 6.483 11.472 1.00 18.83

ATOM 4108 OH2 HOH W 65 23.830 11.367 35.848 1.00 21.97

ATOM 4111 OH2 HOH W 66 25.909 1.055 28.903 1.00 18.03

ATOM 4114 OH2 HOH W 67 50.873 13.073 36.691 1.00 20.54

ATOM 4117 OH2 HOH W 68 30.965 -14.003 28.100 1.00 33.26

ATOM 4120 OH2 HOH W 70 23.930 8.534 1.780 1.00 23.25

ATOM 4123 OH2 HOH W 71 44.812 -1.772 17.877 1.00 21.69

ATOM 4126 OH2 HOH W 72 20.394 8.625 24.041 1.00 21.71

ATOM 4129 OH2 HOH W 73 43.055 -5.084 36.754 1.00 22.08

ATOM 4132 OH2 HOH W 74 31.392 -4.914 32.341 1.00 19.97

ATOM 4135 OH2 HOH W 75 42.472 -0.043 43.630 1.00 29.16

ATOM 4138 OH2 HOH W 76 28.310 -6.343 32.049 1.00 37.28

ATOM 4141 OH2 HOH W 77 34.196 0.391 5.082 1.00 18.05

ATOM 4144 OH2 HOH W 78 20.526 3.352 45.656 1.00 22.41

ATOM 4147 OH2 HOH W 79 24.932 -5.887 31.342 1.00 29.19

ATOM 4150 OH2 HOH W 80 48.842 -3.689 46.618 1.00 22.67

ATOM 4153 OH2 HOH W 81 32.798 1.305 41.731 1.00 24.45

ATOM 4156 OH2 HOH W 82 25.679 -12.283 30.502 1.00 25.36

ATOM 4159 OH2 HOH W 83 34.168 17.898 13.136 1.00 22.54

ATOM 4162 OH2 HOH W 84 42.368 0.928 31.609 1.00 21.97

ATOM 4165 OH2 HOH W 85 30.036 -6.047 13.044 1.00 20.97

ATOM 4168 OH2 HOH W 86 39.106 -8.653 15.862 1.00 20.71

ATOM 4171 OH2 HOH W 87 38.117 10.497 44.844 1.00 34.92

ATOM 4174 OH2 HOH W 89 24.415 5.577 34.955 1.00 20.65

ATOM 4177 OH2 HOH W 90 15.886 -2.109 10.278 1.00 34.16

ATOM 4180 OH2 HOH W 91 21.881 -6.185 26.501 1.00 22.56

ATOM 4183 OH2 HOH W 92 46.086 -1.633 32.263 1.00 27.58

ATOM 4186 OH2 HOH W 93 28.435 -4.071 30.794 1.00 25.14

ATOM 4189 OH2 HOH W 94 23.314 14.343 34.051 1.00 39.12

ATOM 4192 OH2 HOH W 95 40.893 23.442 14.767 1.00 28.02

ATOM 4195 OH2 HOH W 96 24.925 18.300 19.070 1.00 29.56

ATOM 4198 OH2 HOH W 97 28.107 23.315 21.470 1.00 32.69

ATOM 4201 OH2 HOH W 98 39.459 -7.784 13.446 1.00 31.67

ATOM 4204 OH2 HOH W 99 42.721 -6.952 28.832 1.00 20.74

ATOM 4207 OH2 HOH W 100 45.693 0.909 31.701 1.00 20.90

ATOM 4210 OH2 HOH W 101 28.318 20.337 17.569 1.00 35.65

ATOM 4213 OH2 HOH W 102 44.870 -6.798 37.684 1.00 35.75

ATOM 4216 OH2 HOH W 103 36.631 24.105 9.200 1.00 27.95

ATOM 4219 OH2 HOH W 104 38.594 10.468 3.779 1.00 29.62

ATOM 4222 OH2 HOH W 105 48.692 -5.365 41.462 1.00 20.52

ATOM 4225 OH2 HOH W 106 46.803 9.686 42.202 1.00 32.68

ATOM 4228 OH2 HOH W 107 37.356 26.629 32.061 1.00 26.42

ATOM 4231 OH2 HOH W 108 41.585 -9.630 42.606 1.00 24.05

ATOM 4234 OH2 HOH W 109 48.620 -7.911 30.300 1.00 30.16

ATOM 4237 OH2 HOH W 110 21.202 -8.436 15.346 1.00 38.22

ATOM 4240 OH2 HOH W 111 31.311 -12.756 35.171 1.00 29.21

ATOM 4243 OH2 HOH W 112 20.841 -7.544 22.388 1.00 22.99

ATOM 4246 OH2 HOH W 113 21.827 17.765 28.116 1.00 24.50

ATOM 4249 OH2 HOH W 114 34.131 4.778 3.926 1.00 27.22

ATOM 4252 OH2 HOH W 115 30.983 8.008 45.609 1.00 27.92

ATOM 4255 OH2 HOH W 116 41.063 -12.762 31.331 1.00 30.65

ATOM 4258 OH2 HOH W 117 25.579 -13.288 4.560 1.00 23.77

ATOM 4261 OH2 HOH W 118 36.980 -12.282 19.061 1.00 26.96

ATOM 4264 OH2 HOH W 119 8.693 6.920 7.742 1.00 23.25 ATOM 4267 OH2 HOH W 120 51.503 4.811 21.172 1.00 25.64

ATOM 4270 OH2 HOH W 121 9.702 -0.981 18.710 1.00 28.87

ATOM 4273 OH2 HOH W 122 33.912 15.657 44.910 1.00 28.39

ATOM 4276 OH2 HOH W 123 30.958 11.709 10.094 1.00 31.92

ATOM 4279 OH2 HOH W 124 25.888 -2.726 30.636 1.00 40.39

ATOM 4282 OH2 HOH W 125 42.225 4.617 44.313 1.00 27.07

ATOM 4285 OH2 HOH W 126 14.501 5.318 8.423 1.00 35.09

ATOM 4288 OH2 HOH W 127 27.588 18.209 37.875 1.00 29.55

ATOM 4291 OH2 HOH W 128 42.469 26.708 26.523 1.00 26.56

ATOM 4294 OH2 HOH W 130 46.474 -2.421 34.585 1.00 31.20

ATOM 4297 OH2 HOH W 132 37.155 11.962 6.651 1.00 30.89

ATOM 4300 OH2 HOH W 133 43.886 26.075 22.007 1.00 26.99

ATOM 4303 OH2 HOH W 134 45.530 10.524 8.974 1.00 24.22

ATOM 4306 OH2 HOH W 135 21.364 15.279 30.157 1.00 28.09

ATOM 4309 OH2 HOH W 136 52.668 7.123 38.901 1.00 34.79

ATOM 4312 OH2 HOH W 137 43.272 19.443 13.436 1.00 36.67

ATOM 4315 OH2 HOH W 138 37.297 -15.593 32.245 1.00 36.19

ATOM 4318 OH2 HOH W 139 23.898 O .626 38.613 1.00 30.34

ATOM 4321 OH2 HOH W 140 35.600 -6.182 5.810 1.00 25.84

ATOM 4324 OH2 HOH W 141 43.430 16.492 10.228 1.00 26.98

ATOM 4327 OH2 HOH W 142 23.587 -13.662 22.306 1.00 28.96

ATOM 4330 OH2 HOH W 143 15.798 8.988 7.894 1.00 29.16

ATOM 4333 OH2 HOH W 144 20.874 -5.677 11.626 1.00 24.63

ATOM 4336 OH2 HOH W 146 12.785 1.065 19.048 1.00 25.71

ATOM 4339 OH2 HOH W 147 48.173 21.190 18.689 1.00 27.98

ATOM 4342 OH2 HOH W 149 22.147 -8.790 12.743 1.00 27.98

ATOM 4345 OH2 HOH W 150 21.392 1.835 -0.204 1.00 30.34

ATOM 4348 OH2 HOH W 151 33.140 -11.955 20.985 1.00 35.26

ATOM 4351 OH2 HOH W 152 23.216 13.325 30.483 1.00 26.09

ATOM 4354 OH2 HOH W 153 23.019 13.675 8.814 1.00 31.26

ATOM 4357 OH2 HOH W 154 29.903 -11.002 33.711 1.00 29.50

ATOM 4360 OH2 HOH W 155 48.657 -3.446 35.875 1.00 34.78

ATOM 4363 OH2 HOH W 156 34.272 20.557 13.875 1.00 39.13

ATOM 4366 OH2 HOH W 157 35.610 27.346 22.236 1.00 32.38

ATOM 4369 OH2 HOH W 158 44.436 12.873 9.547 1.00 26.33

ATOM 4372 OH2 HOH W 159 19.510 6.375 26.223 1.00 34.99

ATOM 4375 OH2 HOH W 160 28.671 -16.182 29.382 1.00 33.07

ATOM 4378 OH2 HOH W 161 42.907 11.323 45.296 1.00 94.32

ATOM 4381 OH2 HOH W 162 50.943 12.053 29.029 1.00 42.12

ATOM 4384 OH2 HOH W 163 45.673 -0.608 46.421 1.00 35.90

ATOM 4387 OH2 HOH W 164 18.597 12.343 31.250 1.00 36.62

ATOM 4390 OH2 HOH W 165 52.715 13.715 14.875 1.00 27.96

ATOM 4393 OH2 HOH W 166 44.921 19.407 27.113 1.00 34.63

ATOM 4396 OH2 HOH W 167 17.185 12.317 16.599 1.00 35.44

ATOM 4399 OH2 HOH W 168 45.095 -9.080 41.561 1.00 35.67

ATOM 4402 OH2 HOH W 169 8.307 -0.285 15.228 1.00 33.94

ATOM 4405 OH2 HOH W 170 42.444 5.590 4.733 1.00 32.08

ATOM 4408 OH2 HOH W 171 23.494 14.575 41.051 1.00 28.20

ATOM 4411 OH2 HOH W 172 20.465 -3.740 23.271 1.00 24.71

ATOM 4414 OH2 HOH W 173 40.097 -14.145 27.725 1.00 35.09

ATOM 4417 OH2 HOH W 174 19.548 -8.864 20.620 1.00 34.58

ATOM 4420 OH2 HOH W 175 18.208 -2.725 17.019 1.00 27.06

ATOM 4423 OH2 HOH W 176 30.433 -4.149 37.702 1.00 29.21

ATOM 4426 OH2 HOH W 177 46.993 -6.378 22.279 1.00 39.77

ATOM 4429 OH2 HOH W 178 27.724 -12.337 8.931 1.00 52.43

ATOM 4432 OH2 HOH W 179 34.819 8.698 8.660 1.00 37.08

ATOM 4435 OH2 HOH W 180 35.053 -4.356 39.736 1.00 44.29

ATOM 4438 OH2 HOH W 181 21.147 15.729 10.288 1.00 36.37

ATOM 4441 OH2 HOH W 182 28.710 -8.578 34.412 1.00 41.32

ATOM 4444 OH2 HOH W 183 41.665 24.133 19.804 1.00 27.04

ATOM 4447 OH2 HOH W 184 21.237 -0.651 0.292 1.00 29.88 ATOM 4450 OH2 HOH W 185 15.319 12.631 35.088 1.00 40.82

ATOM 4453 OH2 HOH W 186 17.568 -6.667 20.090 1.00 46.76

ATOM 4456 OH2 HOH W 187 21.510 16.031 32.785 1.00 30.30

ATOM 4459 OH2 HOH W 188 37.891 -12.650 21.487 1.00 38.20

ATOM 4462 OH2 HOH W 189 28.443 -10.580 18.183 1.00 33.07

ATOM 4465 OH2 HOH W 190 25.615 -2.319 33.501 1.00 33.45

ATOM 4468 OH2 HOH W 191 44.793 19.567 10.584 1.00 41.68

ATOM 4471 OH2 HOH W 192 19.440 13.913 15.925 1.00 49.68

ATOM 4474 OH2 HOH W 193 39.679 -0.357 5.804 1.00 43.67

ATOM 4477 OH2 HOH W 194 35.494 -12.230 25.437 1.00 32.24

ATOM 4480 OH2 HOH W 195 51.056 2.331 38.823 1.00 30.10

ATOM 4483 OH2 HOH W 196 23.911 -9.355 30.117 1.00 47.56

ATOM 4486 OH2 HOH W 197 37.238 25.444 13.165 1.00 36.20

ATOM 4489 OH2 HOH W 199 40.947 17.855 48.948 1.00 36.08

ATOM 4492 OH2 HOH W 200 49.428 9.790 26.722 1.00 34.67

ATOM 4495 OH2 HOH W 201 8.178 -0.105 7.840 1.00 46.40

ATOM 4498 OH2 HOH W 202 28.872 22.561 36.006 1.00 66.03

ATOM 4501 OH2 HOH W 203 32.872 29.774 27.679 1.00 47.71

ATOM 4504 OH2 HOH W 204 20.245 -5.283 8.777 1.00 36.89

ATOM 4507 OH2 HOH W 205 25.001 20.665 30.456 1.00 26.78

ATOM 4510 OH2 HOH W 207 18.981 6.379 40.516 1.00 44.49

ATOM 4513 OH2 HOH W 208 18.135 -5.417 17.243 1.00 31.79

ATOM 4516 OH2 HOH W 209 20.375 -2.587 5.981 1.00 41.07

ATOM 4519 OH2 HOH W 210 32.416 -5.946 37.424 1.00 38.09

ATOM 4522 OH2 HOH W 211 31.032 21.871 15.661 1.00 30.27

ATOM 4525 OH2 HOH W 213 48.383 14.254 40.587 1.00 48.37

ATOM 4528 OH2 HOH W 214 27.589 23.396 33.454 1.00 42.67

ATOM 4531 OH2 HOH W 215 36.735 18.290 11.455 1.00 33.50

ATOM 4534 OH2 HOH W 216 45.328 17.450 28.588 1.00 32.63

ATOM 4537 OH2 HOH W 217 28.589 5.848 0.331 1.00 30.88

ATOM 4540 OH2 HOH W 218 45.036 7.204 3.933 1.00 44.32

ATOM 4543 OH2 HOH W 219 36.198 15.391 9.570 1.00 40.50

ATOM 4546 OH2 HOH W 220 51.473 2.532 28.741 1.00 33.07

ATOM 4549 OH2 HOH W 221 16.773 11.375 41.364 1.00 40.40

ATOM 4552 OH2 HOH W 222 18.084 6.955 46.182 1.00 46.26

ATOM 4555 OH2 HOH W 223 22.390 -0.677 40.898 1.00 31.29

ATOM 4558 OH2 HOH W 225 53.950 5.803 29.838 1.00 43.53

ATOM 4561 OH2 HOH W 226 45.166 -0.070 43.645 1.00 35.50

ATOM 4564 OH2 HOH W 227 39.005 -3.963 7.418 1.00 45.59

ATOM 4567 OH2 HOH W 228 36.810 22.964 39.380 1.00 38.67

ATOM 4570 OH2 HOH W 230 31.222 17.540 44.140 1.00 43.16

ATOM 4573 OH2 HOH W 231 46.056 -9.966 27.003 1.00 37.60

ATOM 4576 OH2 HOH W 232 47.040 15.108 26.216 1.00 31.07

ATOM 4579 OH2 HOH W 233 39.996 19.542 42.453 1.00 40.16

ATOM 4582 OH2 HOH W 234 14.945 14.841 32.915 1.00 52.31

ATOM 4585 OH2 HOH W 235 29.815 16.087 45.664 1.00 42.63

ATOM 4588 OH2 HOH W 236 42.550 -12.008 28.799 1.00 36.44

ATOM 4591 OH2 HOH W 237 53.418 13.214 31.220 1.00 53.16

ATOM 4594 OH2 HOH W 238 42.505 -7.172 18.060 1.00 45.33

ATOM 4597 OH2 HOH W 239 27.692 8.818 -1.470 1.00 36.21

ATOM 4600 OH2 HOH W 240 47.095 16.188 29.949 1.00 35.50

ATOM 4603 OH2 HOH W 241 33.024 -2.871 38.053 1.00 36.93

ATOM 4606 OH2 HOH W 242 23.529 3.676 30.017 1.00 30.79

ATOM 4609 OH2 HOH W 243 46.769 21.726 28.201 1.00 40.20

ATOM 4612 OH2 HOH W 245 25.267 16.974 37.153 1.00 50.89

ATOM 4615 OH2 HOH W 246 32.167 -10.939 40.270 1.00 52.37

ATOM 4618 OH2 HOH W 248 16.375 4.307 22.549 1.00 40.20

ATOM 4621 OH2 HOH W 249 36.270 10.573 9.646 1.00 41.27

ATOM 4624 OH2 HOH W 250 21.460 2.455 41.834 1.00 38.85

ATOM 4627 OH2 HOH W 251 52.329 -3.463 41.873 1.00 46.75

ATOM 4630 OH2 HOH W 252 25.502 -3.198 4.280 1.00 27.04 ATOM 4633 OH 2 HOH W 253 17.878 13.800 19.727 1.00 36.40

ATOM 4636 OH 2 HOH W 257 17.028 -4.713 13.089 1.00 45.26

ATOM 4639 OH 2 HOH W 261 31.732 7.477 O .668 1.00 49.60

ATOM 4642 OH 2 HOH W 262 40.671 -12.328 38.892 1.00 49.86

ATOM 4645 OH 2 HOH W 265 14.635 13.902 22.559 1.00 41.46

ATOM 4648 OH 2 HOH W 266 22.873 4.243 33.141 1.00 48.32

ATOM 4651 OH 2 HOH W 267 44.728 25.864 28.836 1.00 42.76

ATOM 4654 OH 2 HOH W 270 43.589 -8.613 30.481 1.00 36.17

ATOM 4657 OH 2 HOH W 272 16.443 14.420 37.349 1.00 43.99

ATOM 4660 OH 2 HOH W 273 49.283 16.801 17.329 1.00 40.11

ATOM 4663 OH 2 HOH W 274 19.543 -4.316 20.151 1.00 42.35

ATOM 4666 OH 2 HOH W 275 30.267 27.516 30.458 1.00 41.78

ATOM 4669 OH 2 HOH W 277 23.015 -4.799 39.381 1.00 48.64

ATOM 4672 OH 2 HOH W 281 56.542 O .326 33.909 1.00 58.04

ATOM 4675 OH 2 HOH W 282 27.842 19.105 40.231 1.00 46.37

ATOM 4678 OH 2 HOH W 283 26.158 22.853 30.042 1.00 48.09

ATOM 4681 OH 2 HOH W 284 40.855 11.861 3.284 1.00 41.76

ATOM 4684 OH 2 HOH W 285 34.296 23.929 34.984 1.00 46.88

ATOM 4687 OH 2 HOH W 290 33.870 21.842 37.051 1.00 37.55

[0069] The amino acid residues that are of particular interest to the invention for designing compounds that modulate prostasin activity are detailed in Table 2, infra.

Table 2

Residue Name Residues Number Pocket Assignmen

VaI 69 Pl' VaI 70 Pl' GIy 71 Pl' His 85 Catalytic His Cys 86 Pl' Tyr 126 P2 Leu 127 P2 GIn 128 P2 GIu 129 P2 GIy 130 P2 Asp 134 Catalytic Asp GIy 174 P4 His 175 P4 VaI 176 P4 Ala 177 P4 Pro 178 P4 Ser 179 P4

VaI 180 P4

Ala 209 P3

Lys 210 P3

Pro 211 P3

GIu 212 P3

GIu 213 P3

Pro 214 P3

His 215 P3

Phe 216 P3

Ala 233 Pl

Cys 234 Pl

GIn 235 Pl

GIy 236 Pl

Asp 237 Pl

Ser 238 Catalytic Ser

VaI 256 Pl

Ser 257 Pl

Trp 258 P2

GIy 259 P2

Asp 260 Pl

Ala 261 Pl

Cys 262 Pl

GIy 269 Pl

VaI 270 Pl

Claims

We Claim:

1. A composition comprising a polypeptide in crystalline form, wherein the polypeptide is a prostasin polypeptide.

2. The composition according to claim 1 , wherein the prostasin polypeptide is the expression product of a polynucleotide encoded by the amino acid residues of SEQ. ID 1.

3. The composition according to claim 1, further comprising a binding partner suitable for co- crystallization with the prostasin polypeptide.

4. The composition according to claim 1, wherein the prostasin crystal diffracts to 1.5 Angstroms.

5. The composition according to claim 4, wherein the crystal space group is ¥2{l{l_\.

6. The composition according to claim 5, wherein the unit cell of the crystal comprises ! crystallographically independent prostasin molecules.

7. The composition according to claim 6, wherein the prostasin crystal has unit cell dimensions of a=53.74A b=54.58A, c=83.694A and alpha=beta=gamma=90.0 degrees.

8. The composition according to claim 1, wherein the polypeptide is characterized by the structure coordinates according to Table 1 , or a substantial part thereof.

9. A method for crystallizing a prostasin polypeptide, comprising: (A) mixing a solution comprising a prostasin polypeptide and an optional binding partner with a crystallization buffer; and (B) crystallizing the mixture of step (A) by drop vapor diffusion to form a crystalline precipitate.

10. The method of claim 9, wherein said crystallization buffer comprises 20% w/v PEG 4000 buffered with 0.1M MES, pH.< 7.0

11. The method of claim 9, wherein crystallization occurs at a temperature ranging from 4 to 20 degrees Celsius.

12. The method of claim 9, wherein the prostasin polypeptide is at a final concentration of about 20g/mL.

13. A method of identifying a compound that associates with prostasin, comprising (A) designing a compound that associates with at least one of the residues of Table 2, (B) synthesizing said compound, and (C) determining in vitro whether said compound modulates the activity of prostasin.