WO2016201566A1 - Systems and methods of selecting compounds with reduced risk of cardiotoxicity using herg models - Google Patents

Systems and methods of selecting compounds with reduced risk of cardiotoxicity using herg models

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WO2016201566A1
WO2016201566A1 PCT/CA2016/050691 CA2016050691W WO2016201566A1 WO 2016201566 A1 WO2016201566 A1 WO 2016201566A1 CA 2016050691 W CA2016050691 W CA 2016050691W WO 2016201566 A1 WO2016201566 A1 WO 2016201566A1
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atom
prob
prod
proa
proc
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PCT/CA2016/050691
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French (fr)
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Sergei NOSKOV
Serdar DURDAGI
Henry DUFF
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Uti Limited Partnership
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    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12QMEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • CCHEMISTRY; METALLURGY
    • C40COMBINATORIAL CHEMISTRY
    • C40BCOMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES, IN SILICO LIBRARIES
    • C40B30/00Methods of screening libraries
    • C40B30/02In silico screening
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/5005Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
    • G01N33/5008Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
    • G01N33/5014Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing toxicity
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6872Intracellular protein regulatory factors and their receptors, e.g. including ion channels
    • GPHYSICS
    • G06COMPUTING; CALCULATING; COUNTING
    • G06FELECTRIC DIGITAL DATA PROCESSING
    • G06F19/00Digital computing or data processing equipment or methods, specially adapted for specific applications
    • G06F19/10Bioinformatics, i.e. methods or systems for genetic or protein-related data processing in computational molecular biology
    • G06F19/16Bioinformatics, i.e. methods or systems for genetic or protein-related data processing in computational molecular biology for molecular structure, e.g. structure alignment, structural or functional relations, protein folding, domain topologies, drug targeting using structure data, involving two-dimensional or three-dimensional structures

Abstract

Provided herein are systems and methods for selecting compounds that have reduced risk of cardiotoxicity or which are not likely to be cardiotoxic. As an example, a system and method can include a computational dynamic model combined with a high throughput screeningin silicothat mimics one of the most important ion channels associated with cardiotoxicity, namely the human Ether-a-go-go Related Gene (hERG) channel. Also provided herein are systems and methods for redesigning compounds that are predicted to be cardiotoxic based on the model and the high throughput screening.

Description

SYSTEMS AND METHODS OF SELECTING COMPOUNDS WITH REDUCED

RISK OF CARDIOTOXICITY USING HERG MODELS

1. CROSS REFERENCE TO RELATED APPLICATIONS

[001] The present application claims the benefit of priority of U.S. Provisional

Application No. 62/181,169, filed June 17, 2015, the content of which is hereby incorporated by reference in its entirety.

2. TECHNICAL FIELD

[002] This application relates generally to compounds and cardiotoxicity and more generally to processor-implemented systems and methods for analyzing compounds with respect to cardiotoxicity using hERG models.

3. BACKGROUND

[003] Cardiotoxicity is a leading cause of attrition in clinical studies and postmarketing withdrawal. The human Ether-a-go-go Related Gene 1 (hERGl) K+ ion channel is implicated in cardiotoxicity, and the U.S. Food and Drug Administration (FDA) requires that candidate drugs be screened for activity against the hERGl channel. Recent investigations suggest that non-hERG cardiac ion channels are also implicated in cardiotoxicity. Therefore, screening of candidate drugs for activity against cardiac ion channels, including hERGl, is recommended.

[004] The hERGl ion channel (also referred to as KCNH2 or Kvl 1.1) is a key element for the rapid component of the delayed rectified potassium currents (/¾) in cardiac myocytes, required for the normal repolarization phase of the cardiac action potential (Curran et al, 1995, "A Molecular Basis for Cardiac -Arrhythmia; HERG Mutations Cause Long Qt Syndrome," Cell, 80, 795-803; Tseng, 2001, "I(Kr): The hERG Channel," J. Mol. Cell. Cardiol, 33, 835-49; Vandenberg et al, 2001, "HERG Kb Channels: Friend and Foe," Trends. Pharm. Sci. 22, 240-246). Loss of function mutations in hERGl cause increased duration of ventricular repolarization, which leads to prolongation of the time interval between Q and T waves of the body surface electrocardiogram (long QT syndrome-LQTS) (Vandenberg et al, 2001; Splawski et al , 2000, "Spectrum of Mutations in Long-QT Syndrome Genes KVLQT1, HERG, SCN5A, KCNE1, and KCNE2," Circulation, 102, 1178- 1185; Witchel et al, 2000, "Familial and Acquired Long QT Syndrome and the Cardiac Rapid Delayed Rectifier Potassium Current, Clin. Exp. Pharmacol. Physiol , 27, 753-766). LQTS leads to serious cardiovascular disorders, such as tachyarrhythmia and sudden cardiac death.

[005] Diverse types of organic compounds used both in common cardiac and noncardiac medications, such as antibiotics, antihistamines, and antibacterial, can reduce the repolarizing current (i.e., with binding to the central cavity of the pore domain of hERGl) and lead to ventricular arrhythmia (Lees-Miller et al., 2000, "Novel Gain-of-Function Mechanism in Kb Channel-Related Long-QT Syndrome: Altered Gating and Selectivity in the HERGl N629D Mutant," Circ. Res., 86, 507-513; Mitcheson et al, 2005, "Structural Determinants for High-affinity Block of hERG Potassium Channels," Novartis Found. Symp. 266, 136-150; Lees-Miller et al, 2000, "Molecular Determinant of High- Affinity Dofetilide Binding to HERGl Expressed in Xenopus Oocytes: Involvement of S6 Sites," Mol.

Pharmacol., 57, 367-374). Therefore, several approved drugs (i.e., terfenadine, cisapride, astemizole, and grepafloxin) have been withdrawn from the market, whereas several drugs, such as thioridazine, haloperidol, sertindole, and pimozide, are restricted in their use because of their effects on QT interval prolongation (Du et al., 2009, "Interactions between hERG Potassium Channel and Blockers," Curr. Top. Med. Chem., 9, 330-338; Sanguinetti et al., 2006, "hERG Potassium Channels and Cardiac Arrhythmia," Nature, 440, 463-469).

[006] The recommended in vitro drug screening process includes traditional patch clamp techniques, radiolabeled drug binding assays, 86RB-flux assays, and high-throughput cell-based fluorescent dyes and stably transfected hERGl ion channels from Chinese hamster ovary (CHO) cells (Stork et al., 2007, "State Dependent Dissociation of HERG Channel Inhibitors," Br. J. Pharmacol., 151, 1368-1376) and HEK 293 cells (also known as 293T cells) (Diaz et al, 2004, "The [3H]Dofetilide Binding Assay is a Predictive Screening Tool for hERG Blockade and Proarrhythmia: Comparison of Intact Cell and Membrane

Preparations and Effects of Altering [K+]o," J Pharmacol. Toxicol. Methods., 50(3), 187- 199). Although elaborate nonclinical tests display a reasonable sensitivity and establish safety standards for novel therapeutics, the screening of all of potential candidates remains very time-consuming and thus increases the final cost of drug design.

[007] Molecular modeling techniques have provided some guidance in screening drug candidates for their blocking ability to cardiac channel proteins. For example, several receptor-based models of hERG-drug interactions based on molecular docking and molecular dynamics (MD) simulation studies have been published (Stansfeld et al., 2007, "Drug Block of the hERG Potassium Channel: Insight from Modeling," Proteins: Struct. Funct. Bioinf. 68, 568-580; Masetti et al, 2007, "Modeling the hERG Potassium Channel in a Phospholipid Bilayer: Molecular Dynamics and Drug Docking Studies, J. Comp. Chem., 29(5), 795-808; Zachariae et al, 2009, "Side Chain Flexibilities in the Human Ether-a-go-go Related Gene Potassium Channel (hERG) Together with Matched-Pair Binding Studies Suggest a New Binding Mode for Channel Blockers," J. Med. Chem., 52, 4266-4276; Boukharta et al, 2011, "Computer Simulations of Structure - Activity Relationships for hERG Channel Blockers," Biochemistry, 50, 6146-6156; Durdagi et al, 2011, "Combined Receptor and Ligand-Based Approach to the Universal Pharmacophore Model Development for Studies of Drug

Blockade to the hERGl Pore Domain," J. Chem. Inf. Model, 51, 463-474). More recently, long timescale MD simulations of hERG-drug interactions have been published (Barakat et al, 2014, "A Human Ether- a-go-go-related (Herg) Ion Channel Atomistic Model Generated by Long Supercomputer Molecular Dynamics Simulations and its Use in Predicting Drug Cardiotoxicity," Toxicol Lett. 230(3), 382-392). However, most of these structural studies are focused on binding to the open-state of the hERGl channel, whereas many of the common blockers exhibit a state-dependent mechanism of action which is dependent on the multi-state conformational dynamics hERGl (see, e.g., Walker et al, 1999, "Inhibition of the Human Ether-a-go-go-related Gene (HERG) Potassium Channel by Cisapride: Affinity for Open and Inactivated States," Br. J. Pharmacol, 128, 444-450). Moreover, recent studies show that drugs with similar hERG potency but different binding kinetics and mode of action are not uniformly proarrhythmic (Di Veroli et al, 2014, "hERG Inhibitors with Similar Potency but Different Binding Kinetics do not Pose the Same Proarrhythmic Risk:

Implications for Drug Safety Assessment," J. Cardiovascular Electrophysiol 25(2), 197- 207). What is therefore needed is an improved atomistic approach to the screening of drug candidates for their ability to block hERGl that addresses the state-dependent mechanism of action of blockers, without adding unnecessary complexity.

4. SUMMARY

[008] Provided herein are computational dynamic models of a membrane-bound ion channel, the human Ether-a-go-go Related Gene 1 (hERGl) K+ ion channel, that provide atomistically detailed sampling of the physiologically relevant conformational states of this channel. In certain embodiments, the model is combined with an atomistically detailed high throughput screening algorithm of test compounds in silico to predict cardiotoxicity or risk of cardiotoxicity and to select for compounds with reduced risk of cardiotoxicity. [009] In certain embodiments, the model and methods disclosed herein can be used to screen a standardized panel of drugs showing that cardiotoxic compounds are blockers of hERGl, whereas proven safe drugs do not block these channels. In certain embodiments, the model and methods disclosed herein can be used to screen thousands of new candidate drugs in silico, which greatly accelerates drug development and renders it safer and cheaper rather than having to test all compounds in biological assays.

[0010] In certain embodiments, the model and methods disclosed herein can be used to predict compounds that are cardiotoxic or are potentially cardiotoxic, or to identify which chemical moieties of the compounds may be implicated in the toxicity, so that drug developers may avoid using the molecule, or may structurally modify the molecule to address the toxicity concerns.

[0011] The hERGl ion channel used in the computational dynamic model is a tetrameric protein, surrounded by a membrane, ions, solvent or physiological fluid molecules, and optionally, other components of an in vivo system, to simulate the realistic environment of the channel. In certain embodiments, the duration of the computational dynamic model is of sufficient length (e.g., greater than 200 ns) to allow sampling of all physiologically relevant conformational states of the hERGl channel, including the open, closed and open- inactivated states.

[0012] In certain embodiments, the atomistic detail afforded by the computational dynamic model and high throughput screening algorithm allows a determination of whether a test compound blocks one or more of the physiologically relevant conformations of the hERGl channel. In certain embodiments, a compound that blocks one or more of the physiologically relevant conformations the hERGl channel is cardiotoxic.

[0013] In one aspect, provided herein, is a system and method for selecting a compound with reduced risk of cardiotoxicity. As an example, the system and method can include a computational dynamic model combined with a high throughput screening in silico that mimics the open, closed, and/or open-inactivated conformational states of hERGl . Also provided herein are processor-implemented systems and methods for redesigning compounds that are predicted to be cardiotoxic based on the model and the high throughput screening.

[0014] As another example, methods include the steps of: a) providing structural information, including, for example, in the form of coordinates, describing one or more conformations of a hERGl channel protein; b) providing structural information describing conformers of one or more compounds; c) using a docking algorithm to dock the conformers of the one or more compounds of step b) to the one or more conformations of step a);

d) identifying a plurality of preferred binding conformations for each of the combinations of protein and compound; e) optimizing the preferred binding conformations using Molecular Dynamics (MD) simulations; and f) determining if the compound blocks the ion channel of the protein in the preferred binding conformations; wherein one or more of the steps a) through f) are not necessarily executed in the recited order.

[0015] In certain embodiments, one or more of the steps a) through f) of the method are performed in the recited order.

[0016] In certain embodiments, the conformation of step a) corresponds to the open state of the hERGl protein. In certain embodiments, the conformation of step a) corresponds to the closed state of the hERGl protein. In certain embodiments, the conformation of step a) corresponds to the open-inactivated state of the hERGl protein.

[0017] In certain embodiments, providing the structural information in step a) comprises using the coordinates of one or more dominant conformations identified from an MD simulation of the hERGl protein. In certain embodiments, the MD simulation incorporates implicit or explicit solvent molecules and ion molecules, and a hydrated lipid bilayer with explicit phospholipid, solvent and ion molecules. In certain embodiments, the duration of the MD simulation is greater than 100 ns. In certain embodiments, the duration of the MD simulation is 100, 150, 200, 250, 300, 350, 400, 450 or 500 ns. In certain embodiments, the coordinates of the one or more dominant conformations identified from the MD simulation correspond to the open state of the hERGl protein. In certain embodiments, the coordinates of the one or more dominant conformations identified from the MD simulation correspond to the closed state of the hERGl protein. In certain embodiments, the coordinates of the one or more dominant conformations identified from the MD simulation correspond to the open-inactivated state of the hERGl protein. In certain embodiments, the coordinates of the one or more dominant conformations identified from the MD simulation, including, for example, the coordinates of Table A, correspond to the open state of the hERGl protein. In certain embodiments, the coordinates of the one or more dominant conformations identified from the MD simulation, including, for example, the coordinates of Table B, correspond to the closed state of the hERGl protein. In certain embodiments, the coordinates of the one or more dominant conformation identified from the MD simulation, including, for example, the coordinates of Table C, correspond to the open-inactivated state of the hERGl protein.

[0018] In certain embodiments, providing the structural information in step a) comprises using coordinates selected from the group consisting of Table A, Table B and Table C. In certain embodiments, the coordinates are selected from Table A. In certain embodiments, the coordinates are selected from Table B. In certain embodiments, the coordinates are selected from Table C.

[0019] In certain embodiments, step b) comprises providing the chemical structure of a compound and determining the conformers of the compound. In certain embodiments, the chemical structure of the compound defines the conformers.

[0020] In certain embodiments, if the compound does not block the ion channel in the preferred binding conformations, the compound is selected for further development or possible use in humans, or to be used as a compound for further drug design.

[0021] In certain embodiments, steps a) through f) of the method are executed on one or more processors.

[0022] In certain embodiments, the compound is selected from the group consisting of an antihistamine, an antiarrhythmic, an antianginal, an antipsychotic, an anticholinergic, an antitussive, an antibiotic, an antispasmodic, a calcium antagonist, an inotrope, an ACE inhibitor, an antihypertensive, a beta-blocker, an antiepileptic, a gastroprokinetic agent, an alphal -blocker, an antidepressant, an aldosterone antagonist, an opiate, an anesthetic, an antiviral, a PDE inhibitor, an antifungal, a serotonin antagonist, an antiestrogen, and a diuretic.

[0023] In certain embodiments, the MD simulation of step e) incorporates implicit or explicit solvent molecules and ion molecules. In certain embodiments, the MD simulation of step e) incorporates a hydrated lipid bilayer with explicit phospholipid, solvent and ion molecules. In certain embodiments, the MD simulation uses an AMBER force field, a CHARMM force field, or a GROMACS force field. In certain embodiments, the duration of the MD simulation of step e) is 50 ns. In certain embodiments, the duration of the MD simulation of step e) is greater than 50 ns.

[0024] In certain embodiments, the docking algorithm of step c) is selected from

DOCK, AutoDock, and Glide-XP. [0025] In certain embodiments, the method further comprises the step of evaluating the potential of mean force for each of the combinations of hERGl protein and compound in the corresponding optimized preferred binding conformations. In certain embodiments, the potential of mean force is evaluated using umbrella sampling.

[0026] In certain embodiments, the method further comprises the step of calculating binding energies for each of the combinations of hERGl protein and compound in the corresponding optimized preferred binding conformations. In certain embodiments, the method further comprises the step of selecting for each of the combinations of hERGl protein and compound the lowest calculated binding energy in the optimized preferred binding conformations, and outputting the selected calculated binding energies as the predicted binding energies for each of the combinations of protein and compound.

[0027] In another aspect, provided herein, is a method for predicting cardiotoxicity or risk of cardiotoxicity of a compound.

[0028] In certain embodiments of the methods disclosed herein, if the compound does not block the hERGl ion channel in the preferred binding conformations, the compound is predicted to have reduced risk of cardiotoxicity. In certain embodiments, if the compound is predicted to have reduced risk of cardiotoxicity, the compound is selected for further development or possible use in humans, or to be used as a compound for further drug design.

[0029] In certain embodiments of the methods disclosed herein, if the compound blocks the hERGl ion channel in the preferred binding conformations, the compound is predicted to be cardiotoxic. In certain embodiments, if the compound is predicted to be cardiotoxic, the compound is not selected for further clinical development or for use in humans.

[0030] In another aspect, provided herein is a method for chemically modifying a compound that is predicted to be cardiotoxic.

[0031] In certain embodiments of the methods disclosed herein, if the compound blocks the ion channel in one of the preferred binding conformations, the method further comprises the step of using a molecular modeling algorithm to chemically modify or redesign the compound such that it does not block the ion channel in any of the preferred binding conformations. In certain embodiments, the method further comprises repeating steps a) through f) for the modified compound. [0032] In another aspect, provided herein are biological methods for testing the cardiotoxicity of the compound or modified compound in an in vitro biological assay or in vivo in a wild type animal or a transgenic animal model.

[0033] In certain embodiments, the method further comprises testing the

cardiotoxicity of the compound or modified compound in an in vitro biological assay. In certain embodiments, the in vitro biological assay comprises high throughput screening of ion channel and transporter activities. In certain embodiments, the in vitro biological assay comprises high throughput screening of potassium ion channel and transporter activities. In certain embodiments, the in vitro biological assay is a hERGl channel inhibition assay. In certain embodiments, the in vitro biological assay is a FluxOR™ potassium ion channel assay. In certain embodiments, the FluxOR™ potassium channel assay is performed on HEK 293 cells stably expressing hERGl or mouse cardiomyocyte cell line HL-1 cells. In certain embodiments, the in vitro biological assay comprises electrophysiology measurements in single cells. In certain embodiments, the electrophysiology measurements in single cells comprise patch clamp measurements. In certain embodiments, the single cells are Chinese hamster ovary cells stably transfected with hERGl . In certain embodiments, the in vitro biological assay is a Cloe Screen IC50 hERGl Safety assay.

[0034] In certain embodiments, the method further comprises testing the

cardiotoxicity of the compound or modified compound in vivo by measuring ECG in a wild type animal, for example a wild type mouse, or a transgenic animal model, for example, a transgenic mouse model expressing human hERGl .

[0035] In another aspect, provided herein is a processor-implemented system is provided for designing a compound in order to reduce risk of cardiotoxicity. The system includes one or more computer-readable mediums, a grid computing system, and a data structure. The one or more computer-readable mediums are for storing protein structural information representative of a hERGl ion channel protein and for storing compound structural information describing conformers of the compound. The grid computing system includes a plurality of processor-implemented compute nodes and a processor-implemented central coordinator, said grid computing system receiving the stored protein structural information and the stored compound structural information from the one or more computer- readable mediums. Said grid computing system uses the received protein structural information to perform molecular dynamics simulations for determining configurations of target protein flexibility over a simulation length of greater than 50 ns. The molecular dynamics simulations involve each of the compute nodes determining forces acting on an atom based upon an empirical force field that approximates intramolecular forces, where numerical integration is performed to update positions and velocities of atoms. The central coordinator forms molecular dynamic trajectories based upon the updated positions and velocities of the atoms as determined by each of the compute nodes. Said grid computing system configured to: cluster the molecular dynamic trajectories into one or more dominant conformations of the protein, execute a docking algorithm that uses the compound's structural information in order to dock the compound's conformers to the one or more dominant conformations of the protein, and identify a plurality of preferred binding conformations for each of the combinations of protein and compound based on information related to the docked compound's conformers. The data structure is stored in memory which includes information about the one or more of the identified plurality of preferred binding conformations blocking the hERGl channel of the protein. Based upon the information about blocking the hERGl channel, the compound is redesigned in order to reduce risk of cardiotoxicity.

[0036] In another aspect, provided herein, is a computer-implemented system for selecting a compound with reduced risk of cardiotoxicity which includes one or more data processors and a computer-readable storage medium encoded with instructions for commanding the one or more data processors to execute certain operations. The operations include: a) providing structural information describing one or more conformations of a hERGl channel protein; b) providing structural information describing conformers of one or more compounds; c) using a docking algorithm to dock the conformers of the one or more compounds of step b) to the one or more conformations of step a); d) identifying a plurality of preferred binding conformations for each of the combinations of protein and compound; e) optimizing the preferred binding conformations using Molecular Dynamics (MD) simulations; and f) determining if the compound blocks the channel of the hERGl protein in the preferred binding conformations. If the compound blocks the channel in the preferred binding conformations, the compound is predicted to be cardiotoxic. If the compound does not block the channel in the preferred binding conformations, the compound is predicted to have reduced risk of cardiotoxicity. Based on a prediction that the compound has reduced risk of cardiotoxicity, the compound is selected.

[0037] In certain embodiments, the structural information of step a) describes a conformation of the hERGl protein. In certain embodiments, step a) uses coordinates selected from the group consisting of Table A, Table B and Table C, describing a conformation of the hERGl protein. In certain embodiments, the coordinates are selected from Table A. In certain embodiments, the coordinates are selected from Table B. In certain embodiments, the coordinates are selected from Table C.

[0038] In certain embodiments, a computer-implemented system for selecting a compound with reduced risk of cardiotoxicity includes: one or more computer memories and one or more data processors. The one or more computer memories are for storing a single computer database having a database schema that contains and interrelates protein-structural- information fields, compound-structural-information fields, and preferred-binding- conformation fields. The protein-structural-information fields are contained within the database schema and configured to store protein structural information representative of a hERGl ion channel protein. The compound-structural-information fields are contained within the database schema and are configured to store compound structural information describing conformers of one or more compounds. The preferred-binding-conformation fields are contained within the database schema and are configured to store information related to one or more preferred binding conformations for each combination of protein and compound determined based at least in part on information in the protein-structural- information fields and the compound-structural-information fields. The one or more data processors are configured to: process a database query that operates over data related to the protein-structural-information fields, the compound-structural-information fields, and the preferred-binding-conformation fields and determine whether the one or more compounds are cardiotoxic by using information in the preferred-binding-conformation fields.

[0039] In certain embodiments, a non-transitory computer-readable storage medium is provided for storing data for access by a compound-selection program which is executed on a data processing system. The storage medium includes a protein-structural-information data structure, a candidate-compound-structural-information data structure, a molecular- dynamics-simulations data structure, a dominant-conformations data structure, and a binding- conformations data structure. The protein-structural-information data structure has access to information stored in a database and includes protein structural information representative of a hERGl ion channel protein. The candidate-compound-structural-information data structure has access to information stored in the database and includes compound structural information describing conformers of one or more compounds. The molecular-dynamics- simulations data structure has access to information stored in the database and includes configuration information of target protein flexibility determined by performing molecular dynamics simulations on the protein structural information. The dominant-conformations data structure has access to information stored in the database and is determined by using a first clustering algorithm based at least in part on the configuration information of target protein flexibility. The binding-conformations data structure has access to information stored in the database and includes information related to one or more combinations of protein and compound determined by using a docking algorithm based at least in part on the compound structural information and the one or more dominant conformations, one or more preferred binding conformations being determined by using a second clustering algorithm based at least in part on the information related to the one or more combinations of protein and compound. A compound is selected if the compound does not block the channel of the hERGl protein in the preferred binding conformations.

5. BRIEF DESCRIPTION OF THE FIGURES

[0040] FIGURES 1A and IB: System block diagrams for selecting a compound that has reduced risk of cardiotoxicity. Processes illustrated in the system block diagrams (1 A) and (IB) are: Target Preparation (includes, e.g., combined de «ονο/homology protein modeling of hERG), Ligand Collection Preparation (includes, e.g., translation of the 2D information of the ligand into a 3D representative structure), Ensemble Generation (includes, e.g., Molecular Dynamics simulations, principal component analysis, and iterative clustering), Docking (includes, e.g., docking and iterative clustering), MP Simulations on Selected Complexes (includes, e.g., Molecular Dynamics simulations and preliminary ranking of docking hits), Rescoring using MM-PBSA (includes, e.g., binding free energy calculation and rescoring of top hits), and Experimental Testing (includes, e.g., hERGl channel inhibition studies in mammalian cells, Fluxor™ potassium channel assays in mammalian cells, and electrocardiograpy to test anti-arrhythmic activity in wild type mice or transgenic mice expressing hERG). The top hits from the Rescoring step can act as positive controls for the next phase screening. The Ensemble Generation. Docking. MP Simulations on Selected Complexes, and Rescoring using MM-PBSA steps may be performed on a supercomputer, for example, the "IBM Blue Gene/Q" supercomputer system at the Health Sciences Center for Computational Innovation, University of Rochester (e.g., as shown in the block diagram (IB)).

[0041] FIGURE 2: (Top) Schematic drawing illustrating the general topology of hERGl. The six transmembrane helices (SI to S6), the pore helix (PH), the pore forming loop, the Per-Arnt-Sim (PAS) domain, the cyclic nucleotide-binding domain (CNBD) are shown. The voltage sensor in S4 is indicated by the positive charges. Mutations studied are displayed with yellow stars. (Bottom) Schematic comparison of hERG isoforms a and b. The boxed numbers indicate the coding exons of the KNCH2 gene. The gray box represent the unique region not present in hERGl a.

[0042] FIGURE 3 : (A) The structural homology models for the transmembrane part

(Pore domain: S5-S6) of open and open-inactivated hERGl with side view and top view. (B) Structure of neutral and cationic dofetilide.

[0043] FIGURE 4: (A) Potential of mean force for the movement of neutral dofetilide. Two energy wells were chosen from each open (black: a, b) and open-inactivated (grey: a', b') hERG l . (B) Average locations of dofetilide in hERG l open and open- inactivated states, nearby interacting residue's names are shown in different grey shading for each monomer. All atoms within 3.9 A of dofetilide are shown with sticks. Water molecules are shown as balls and the hydrogen bonds as sticks.

[0044] FIGURE 5: (A) Potential of mean force for the movement of cationic dofetilide. Two energy wells were chosen from open (black:a, b) and open-inactivated (grey: a',b') hERGl . (B) Average locations of dofetilide in hERGl open and open-inactivated states, nearby interacting residue's names are shown in different grey shading for each monomer. All atoms within 3.9 A of dofetilide are shown with sticks. Water molecules are shown as balls and the hydrogen bonds as sticks.

[0045] FIGURE 6: Molecular dynamic simulations of docking of ivabradine to the inner cavity of hERGl .

[0046] FIGURE 7: Results from Molecular Dynamic Simulation of

ivabradinebinding to the lipid-exposed binding site in the open and closed states of the channel.

[0047] FIGURE 8: Example block diagram depicting an environment wherein users can interact with a grid computing environment.

[0048] FIGURE 9: Example block diagram depicting hardware and software components for the grid computing environment.

[0049] FIGURE 10: Example schematics of data structures utilized by a compound- selection system. [0050] FIGURE 11 : Example block diagram depicting a compound-selection system provided on a stand-alone computer for access by a user.

6. DETAILED DESCRIPTION

6 1 DEFINITIONS

[0051] As used herein, the term "cardiotoxic" or "cardiotoxicity" refers to having a toxic effect on the heart, for example, by a compound having a deleterious effect on the action of the heart, due to poisoning of the cardiac muscle or of its conducting system. In certain embodiments, long Q-T syndrome or "LQTS" is an aspect of cardiotoxicity.

[0052] As used herein, the term "reduced cardiotoxicity" refers to a favorable cardiotoxicity profile with reference to, for example, one or more ion channel proteins disclosed herein. In certain embodiments, a "ligand," "compound" or "drug," as defined herein, has reduced cardiotoxicity if it does not inhibit "hERG" or "hERGl," as defined herein. As used herein, the terns "hERG" and "hERG" are used interchangeably. In certain embodiments, a ligand, compound or drug has reduced cardiotoxicity if it does not block, obstruct, or partially obstruct, the hERGl channel, as defined herein. In certain

embodiments, a ligand, compound or drug has reduced cardiotoxicity if it does not block, obstruct, or partially obstruct, the flow of K+ ions through the hERGl channel, as defined herein. In certain embodiments, a ligand, compound or drug has reduced cardiotoxicity if it is not a "blocker," as defined herein. In certain embodiments, a ligand, compound or drug has reduced cardiotoxicity if it does not block, obstruct, or partially obstruct, the hERGl channel, as defined herein. In certain embodiments, a ligand, compound or drug has reduced cardiotoxicity if it is not a blocker of hERGl, as defined herein.

[0053] As used herein, the terms "reducing risk" or "reduced risk" as it applies to cardiotoxicity (e.g., "reduced risk of cardiotoxicity") refers to observable results which tend to demonstrate an improved cardiotoxicity profile with reference to, for example, the hERGl channel. In certain embodiments, a ligand, compound or drug has a reduced risk of cardiotoxicity if it does not block, obstruct, or partially obstruct, the hERGl channel. In certain embodiments, a ligand, compound or drug has a reduced risk of cardiotoxicity if it does not block, obstruct, or partially obstruct, the flow of K+ ions through the hERGl channel. In certain embodiments, a ligand, compound or drug has a reduced risk of cardiotoxicity if it is not a blocker of hERGl. In certain embodiments, risk is reduced if there is at least about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or 100% decrease (as measured, e.g., by IC50 data from in vitro biological assays) in the ability of the ligand, compound or drug to inhibit the hERGl channel. In certain embodiments, a reduction in the risk of cardiotoxicity by at least about 90% indicates that cardiotoxicity has been eliminated with respect to the hERGl channel. In certain embodiments, a ligand, compound or drug has a reduced risk of cardiotoxicity if its calculated binding energies, as defined herein, to the hERGl channel, disclosed herein, compare to physiologically relevant concentrations of greater than or equal to 100 μΜ. In certain embodiments, a ligand, compound or drug has a reduced risk of cardiotoxicity if its "selectivity index (SI)," as defined herein, is greater than about 100, about 1000 or about 10,000.

[0054] As used herein, the term "LQTS" as used herein refers to long Q-T syndrome, a group of disorders that increase the risk for sudden death due to an abnormal heartbeat. The QT of LQTS refers to an interval between two points (Q and T) on the common

electrocardiogram (ECG, EKG) used to record the electrical activity of the heart. This electrical activity, in turn, is the result of ions such as sodium and potassium passing through ion channels in the membranes surrounding heart cells. A prolonged QT interval indicates an abnormality in electrical activity that leads to irregularities in heart muscle contraction. One of these irregularities is a specific pattern of very rapid contractions (tachycardia) of the lower chambers of the heart called torsade de pointes, a type of ventricular tachycardia. The rapid contractions, which are not effective in pumping blood to the body, result in a decreased flow of oxygen-rich blood to the brain. This can result in a sudden loss of consciousness (syncope) and death.

[0055] As used herein, the term "lipid bilayer" refers to the basic structure of a cell membrane comprising a double layer of phospholipid molecules. Lipid bilayers are particularly impermeable to ions (such as potassium ions, sodium ions, and calcium ions).

[0056] As used herein, the term "hydrated lipid bilayer" refers to a lipid bilayer in the presence of water molecules.

[0057] As used herein, the term "ion channel" or " ion channel protein," refers to a membrane bound protein that acts as a pore (e.g., permeation pore) in a cell membrane and permits the selective passage of ions (such as potassium ions), by means of which electrical current passes in and out of the cell. Such ion channel proteins include, for example, potassium ion channel proteins, such as hERG or hERGl. In certain embodiments, an ion channel or ion channel protein comprises an inner cavity and a selectivity filter through which the ions pass. In certain embodiments, the terms "permeation pore," "pore" and "channel" are used interchangeably.

[0058] As used herein, the term "transporter activity," when used in relation to an

"ion channel" or " ion channel protein," refers to the movement of an ion across a cell membrane.

[0059] As used herein, the term "potassium ion channel" or "potassium ion channel protein," refers to an ion channel that permits the selective passage of potassium ions (K+).

[0060] As used herein, the term "membrane bound protein" refers to any protein that is bound to a cell membrane under physiological pH and salt concentrations. In certain embodiments, binding of the membrane bound protein can be either by direct binding to the phospholipid bilayer or by binding to a protein, glycoprotein, or other intermediary that is bound to the membrane.

[0061] As used herein, the term "voltage-gated channel" or "voltage-gated ion channel" refers to a class of transmembrane ion channels that are activated by changes in electrical potential difference near the channel. In certain embodiments, the voltage-gated ion channel is a voltage-gated potassium channel.

[0062] As used herein, the term "voltage-gated potassium channel," "voltage-gated potassium ion channel" or "voltage-gated potassium ion (K+) channel" is a transmembrane channel specific for potassium and sensitive to voltage changes in the cell's membrane potential.

[0063] As used herein, the term "human ERG," "human ERG1 ," "hERG" or

"hERGl" refers to the human Ether-a-go-go-Related Gene of chromosome 7q36.1that codes for a protein known as Kvl 1.1, the alpha (a) subunit of potassium voltage-gated channel, subfamily H (eag-related), member 2. It will be known to those of ordinary skill in the art that hERG or hERGl can be also called different names, such as ergl, ERG1, KCNH2, Kvl 1.1, LQT2, and SQT1. See, for example, "KCNH2 potassium voltage-gated channel, subfamily H (eag-related), member 2 [ Homo sapiens (human) ]," Gene ID: 3757, updated 3- Nov-2013, http://www.ncbi.nlm.nih.gov/gene/3757. As used herein, the term "hERG" or "hERGl" refers interchangeably to the gene and gene product, Kvl 1.1. It will further be known to those of ordinary skill in the art the functional hERGl channel is comprised of a homo-tetramer of four identical monomer a-subunits (e.g., the hERGl monomer subunits), as disclosed herein. [0064] As used herein, the term "protein structure" refers to the three-dimensional structure of a protein. The structure of a protein is characterized in four ways. The primary structure is the order of the different amino acids in a protein chain, whereas the secondary structure consists of the geometry of chain segments in forms such as helices or sheets. The tertiary structure describes how a protein folds in on itself; the quaternary structure of a protein describes how different protein monomers or monomer subunits fold in relation to each other.

[0065] As used herein, the term "monomer" or "monomer subunit" refers to one of the proteins making up the quaternary structure of a macromolecule.

[0066] As used herein, the term "tetramer" refers to a macromolecule, for example, a protein macromolecule, made up of four monomer subunits. An example of a tetramer is the hERGl tetramer comprised of four hERGl monomer subunits. Tetrameric assembly into a quaternary structure is required for the formation of the functional hERGl channel.

[0067] As used herein, the term "structural information" refers to the three dimensional structural coordinates of the atoms within a macromolecule, for example, a protein macromolecule such as hERGl.

[0068] As used herein, the term "three-dimensional (3D) structure" refers to the

Cartesian coordinates corresponding to an atom's spatial relationship to other atoms in a macromolecule, for example, a protein macromolecule such as hERGl. Structural coordinates may be obtained using NMR techniques, as known in the art, or using x-ray crystallography as is known in the art. Alternatively, structural coordinates can be derived using molecular replacement analysis or homology modeling. Various software programs allow for the graphical representation of a set of structural coordinates to obtain a three dimensional representation of a molecule or molecular complex.

[0069] As used herein, the term "dynamics," when applied to macromolecule and macromolecular structures, refers to the relative motion of one part of the molecular structure with respect to another. Examples include, but are not limited to: vibrations, rotations, stretches, domain motions, hinge motions, sheer motions, torsion, and the like. Dynamics may also include motions such as translations, rotations, collisions with other molecules, and the like.

[0070] As used herein, the term "flexible" or "flexibility," when applied to macromolecule and macromolecular structures defined by structural coordinates, refers to a certain degree of internal motion about these coordinates, e.g., it may allows for bond stretching, rotation, etc.

[0071] As used herein, the term "molecular modeling algorithm" refers to computational approaches for structure prediction of macromolecule. For instance, these may comprise comparative protein modeling methods including homology modeling methods or protein threading modeling methods, and may further comprise ab initio or de novo protein modeling methods, or a combination of any such approaches.

[0072] As used herein, the term "computational dynamic model" refers to a computer-based model of a system that provides dynamics information of the system. In certain embodiments, when the system is a biological system, for example, a macromolecule or macromolecular structure, the computational dynamic model provides information of the vibrations, rotations, stretches, domain motions, hinge motions, sheer motions, torsion, translations, rotations, collisions with other molecules, and the like, exhibited by the system in the relevant time scale examined by the model.

[0073] As used herein, the term "molecular simulation" refers to a computer-based method to predict the functional properties of a system, including, for example,

thermodynamic properties, thermochemical properties, spectroscopic properties, mechanical properties, transport properties, and morphological information. In certain embodiments, the molecular simulation is a molecular dynamics (MD) simulation.

[0074] As used herein, the term "molecular dynamics simulation" (MD or MD simulation) refers to computer-based molecular simulation methods in which the time evolution of a set of interacting atoms, groups of atoms or molecules, including

macromolecules, is followed by integrating their equations of motion. The atoms or molecules are allowed to interact for a period of time, giving a view of the motion of the atoms or molecules. Thus, the MD simulation may be used to sample conformational space over time to predict the lowest energy, most populated, members of a conformational ensemble. Typically, the trajectories of atoms and molecules are determined by numerically solving the Newton's equations of motion for a system of interacting particles, where forces between the particles and potential energy are defined by molecular mechanics force fields. However, MD simulations incorporating principles of quantum mechanics and hybrid classical-quantum mechanics simulations are also available and may be contemplated herein. [0075] As used herein, the term "scalable molecular dynamics" (scalable MD) refers to computational simulation methods which are suitably efficient and practical when applied to large situations (e.g., a large input data set, a large number of outputs or users, or a large number of participating nodes in the case of a distributed system). In certain embodiments, the methods disclosed herein use scalable MD for simulation of the large systems disclosed herein, for example, the hERGl tetramer in a hydrated lipid bilayer with explicit

phospholipid, solvent and ion molecules, free, or bound to ligand.

[0076] As used herein, the term "energy minimization" (EM) refers to computational methods for computing stable states of interacting atoms, groups of atoms or molecules, including macromolecules, corresponding to global and local minima on their potential energy surface. Starting from a non-equilibrium molecular geometry, EM employs the mathematical procedure of optimization to move atoms so as to reduce the net forces (the gradients of potential energy) on the atoms until they become negligible.

[0077] As used herein, the term "umbrella sampling" refers to computational methods used to improve the sampling of a system where an energy barrier separates two or more regions of conformational space. For example, umbrella sampling can be used to flatten the energy barrier between two regions of conformational space, allowing adequate sampling of the system.

[0078] As used herein, the term "potential of mean force" (PMF) is the potential that gives an average force over all the configurations of a given system.

[0079] As used herein, the term "potential of mean force simulation" (PMF or PFM simulation) is a type of simulation which is often used in Monte Carlo or MD simulations to examine how a system's energy changes as a function of some specific reaction coordinate parameter. For example, PMF simulations may be used to examine how the system's energy changes as a function of the distance between two residues, or as a protein is pulled through a lipid bilayer. One of ordinary skill in the art will understand that PMF simulations are used in conjunction with umbrella sampling because the PMF simulation will typically fail to adequately sample the system space as it proceeds.

[0080] As used herein, the term "ligand," "compound" and "drug" are used interchangeably, and refer to any small molecule which is capable of binding to a target receptor, such as an ion channel protein, for example, hERGl. In certain embodiments, the ligand, compound or drug is a "blocker," as defined herein. [0081] As used herein, the term "dock" or "docking" refers to using a model of a ligand and receptor to simulate association of the ligand-receptor at a proximity sufficient for at least one atom of the ligand to be within bonding distance of at least one atom of the receptor. The term is intended to be consistent with its use in the art pertaining to molecular modeling. A model included in the term can be any of a variety of known representations of a molecule including, for example, a graphical representation of its three-dimensional structure, a set of coordinates, set of distance constraints, set of bond angle constraints or set of other physical or chemical properties or combinations thereof. In certain embodiments, the ligand is a compound, for example a small molecule, and the receptor is a protein macromolecule, for example, hERGl.

[0082] As used herein, the term "docking algorithm" refers to computational approaches for predicting the energetically preferred orientation of a ligand to a receptor when bound or docked to each other to form a stable ligand-receptor complex. Knowledge of the preferred orientation in turn may be used to predict the strength of association or binding affinity between ligand and receptor using, for example, scoring functions. In certain embodiments, the ligand is a compound, for example a small molecule, and the receptor is a protein macromolecule, for example, hERGl.

[0083] As used herein, the term "drug design" or "rational drug design" refers to methods of processes of discovering new drugs based on the knowledge of a biological target. In certain embodiments of the methods disclosed herein, the biological target is a protein macromolecule, for example, hERGl. Those of ordinary skill in the art will appreciate that drug design that relies on the knowledge of the three-dimensional structure of the biomolecular target is also known as "structure-based drug design." Those of ordinary skill in the art will also understand that drug design may rely on computer modeling techniques, which type of modeling is often referred to as "computer-aided drug design." As used herein, the term "binding conformations" refers to the orientation of a ligand to a receptor when bound or docked to each other.

[0084] As used herein, the term "dominant conformation" or "dominant

conformations" refers to most highly populated orientation(s) of a ligand to a receptor when bound or docked to each other. In certain embodiments, when applied to the trajectories of the MD simulations disclosed herein, a clustering algorithm is used to determine the

"dominant conformation" or "dominant conformations." [0085] As used herein, the term "clustering algorithm," when applied to a trajectory of the MD simulations disclosed herein, refers to computational approaches for grouping similar conformations in the trajectory into clusters.

[0086] As used herein, the term "preferred binding conformation" refers to the energetically preferred orientation of a ligand to a receptor when bound or docked to each other to form a stable ligand-receptor complex.

[0087] As used herein, the term "optimized preferred binding conformation" refers to the energetically preferred orientation of a ligand to a receptor when bound or docked to each other to form a stable ligand-receptor complex, following optimizing the preferred binding conformations using MD.

[0088] As used herein, the term "binding energies" is understood to mean the "free energy of binding" (AG ) of a ligand to a receptor. Under equilibrium conditions, this binding energy is equal to AG = ΔΗ - TAS = - R T Log (Keq), where the symbols have their customary meanings. In certain embodiments, the methods disclosed herein allow calculation of binding energies for various ligand-receptor complexes, for example, various compounds bound to hERGl.

[0089] As used herein, the terms "IC50" and "IC90" refer to the concentration of a compound that reduces (e.g., inhibits) the enzyme activity of a target by 50% and 90%, respectively. The term "IC50" generally describes the inhibitory concentration of the compound. Typically, measurements of IC50 and IC90 are made in vitro. In certain embodiments, where the target is a secondary biological target, for example, a membrane- bound ion channel implicated in cardiac cytotoxicity (e.g., hERGl), IC50 is the concentration at which 50% inhibition is observed. ICso's and ICgo's can be measured according to any method known to one of ordinary skill in the art.

[0090] As used herein, the terms "EC50" and "EC90" refer to the plasma

concentration/AUC of a compound that reduces (e.g., inhibits) the cellular effect resulting from enzyme activity by 50% and 90%, respectively. The term "EC50" generally describes the effective dose of the compound. In certain embodiments, where the target is a primary biological target, for example, a viral protein (e.g., HCV NS3/4A protease, HCV NS5B polymerase, or HCV NS5a protein), EC50 is the dose of the compound that inhibits viral replication by 50%. ECso's and ECc>o's can be measured according to any method known to one of ordinary skill in the art. [0091] As used herein, the terms "CC50" and "CC90" refer to the concentration of a compound that reduces the number of viable cells (e.g., kills the cells) compared to that for untreated controls, by 50% and 90%, respectively. The term "CC50" generally describes the concentration of the compound that is cytotoxic to cells. In certain embodiments, where the target is a primary biological target, for example, a viral protein (e.g., HCV NS3/4A protease, HCV NS5B polymerase, or HCV NS5a protein), CC50 is the dose of the compound that is cytotoxic to uninfected cells. In certain embodiments, where the target is a secondary biological target, for example, a membrane-bound ion channel implicated in cardiac cytotoxicity (e.g., hERGl), CC50 is the dose of the compound that is cytotoxic to heart cells. In certain embodiments, the methods disclosed herein select for compounds with reduced risk of cardiotoxicity, but which retain strong biological activity to their primary targets. For example, such compounds may have high EC50 values for the secondary biological target (e.g., hERGl ), high CC50 values for uninfected cells, but low EC50 values against the primary biological target (e.g., HCV NS3/4A protease, HCV NS5B polymerase, or HCV NS5a protein). CCso's and CCgo's can be measured according to any method known to one of ordinary skill in the art.

[0092] As used herein, the term "selectivity index" ("SI") refers to the ratio of the

CC50 for cardiotoxicity with reference to a secondary biological target (e.g., hERGl) and to uninfected cells compared to the EC50 for effectiveness with reference to a primary biological target (e.g., HCV NS3/4A protease, HCV NS5B polymerase, or HCV NS5a protein). In certain embodiments, the methods disclosed herein select for compounds that display SI values greater than about 100. In certain embodiments, the methods disclosed herein select for compounds that display SI values greater than about 1000. In certain embodiments, the methods disclosed herein select for compounds that display SI values greater than about 10,000.

[0093] As used herein, the term "blocker" refers to a compound that blocks, obstructs, or partially obstructs, an ion channel, for example, the hERGl ion channel. In certain embodiments, a blocker is a cardiotoxic compound.

[0094] As used herein, the term "non-blocker" refers to a compound that does not block, obstruct, or partially obstruct, an ion channel, for example, the hERGl ion channel.

[0095] As used herein, "high throughput screening" refers to a method that allows a researcher to quickly conduct chemical, genetic or pharmacological tests, the results of which provide starting points for drug design and for understanding the interaction or role of a particular biochemical process in biology. In certain embodiments, the high throughput screening is through virtual in silico screening, for example, using computer-based methods or computer-based models.

[0096] As used herein, the terms "processor" and "central processing unit" or "CPU" are used interchangeably and refer to a device that is able to read a program from a computer memory (e.g., ROM or other computer memory) and perform a set of steps according to the program.

[0097] As used herein, the terms "computer memory" and "computer memory device" refer to any storage media readable by a computer processor. Examples of computer memory include, but are not limited to, RAM, ROM, computer chips, digital video discs (DVD), compact discs (CDs), hard disk drives (HDD), and magnetic tape.

[0098] As used herein, the term "computer readable medium" refers to any device or system for storing and providing information (e.g., data and instructions) to a computer processor. Examples of computer readable media include, but are not limited to, DVDs, CDs, hard disk drives, magnetic tape and servers for streaming media over networks.

6.2 EMBODIMENTS

[0099] Provided herein is a computational dynamic model of the human Ether-a-go- go Related Gene 1 (hERGl) channel, that provides an atomistically detailed sampling of the physiologically relevant conformational states of this channel, including the open, closed, and/or open-inactivated states. In certain embodiments, the model is combined with an atomistically detailed high throughput screening algorithm of test compounds in silico to predict cardiotoxicity and to select for compounds with reduced cardiotoxicities.

[00100] The hERGl channel is expressed in the heart as well as in various brain regions, smooth muscle cells, endocrine cells, and a wide range of tumor cell lines. However, its role in the heart is the one that has been well characterized and extensively studied for two main reasons. First, it is directly involved in long QT syndrome (LQTS), a disorder associated with an increased risk of ventricular arrhythmias and ultimately sudden cardiac death. Secondly, the blockade of hERGl by prescription medications causes drug-induced QT prolongation that shares the same risk of sudden cardiac arrest like LQTS.

[00101] The hERGl channel is formed as a tetramer through the association of four monomer subunits. In the computer-based molecular simulations and molecular models disclosed herein, the tetramer structure is surrounded by a membrane, ions, and water molecules to simulate the realistic environment of the channel. Further, the computer-based molecular simulations disclosed herein are of sufficient length (e.g., greater than 200 ns) to allow sampling of physiologically relevant conformational states of the hERGl channel, including the open, closed, and/or open-inactived states. This robust molecular simulation of the hERGl channel allows an atomistically detailed high throughput screening in silico to test compounds and determine if the compounds block the channel in any or all of the physiologically relevant conformational states, and therefore are likely to exhibit

cardiotoxicity. The atomistic detail of the molecular simulation also allows a chemical modification or redesign of those compounds found to block the channel. The redesigned compound may then be re-tested in an iterative fashion using the methods disclosed herein.

[00102] An overview of the methods disclosed herein, including computer-based molecular simulations and molecular models, is provided in FIGURES 1A and IB. As an example, the methods can include: using structural information describing the structure of a target protein, for example, an ion channel protein; performing a molecular simulation of the protein structure to identify and select the one or more dominant conformations of the protein structure; using a computer algorithm to dock the conformers of the one or more compounds to the one of more dominant conformations of the protein structure; identifying the preferred binding conformations for each of the combinations of protein and compound; and optimizing the preferred binding conformations using molecular simulations to determine if the compound blocks the ion channel in the preferred binding conformations.

[00103] In certain embodiments, if the compound blocks the hERGl channel, the compound is predicted to be cardiotoxic. The compound may block the hERGl channel in one or more of the relevant physiological conformations of this channel, including, for example, the open, closed and/or open-inactivated conformations of this channel. In certain embodiments, if the compound is predicted to be cardiotoxic, the compound is not selected for further clinical development or for use in humans. In certain embodiments, the compound may be structurally modified or redesigned to address cardiotoxicity.

[00104] In certain embodiments, if the compound does not block the hERGl channel in one or more of its relevant physiological conformations, the compound is predicted to have reduced risk of cardiotoxicity. In certain embodiments, if the compound is predicted to have reduced risk of cardiotoxicity, the compound is selected for further development or possible use in humans, or to be used as a compound for further drug design. [00105] Individual elements and steps of the methods disclosed herein are now described.

6.2.1 Human Ether-a-go-go Related Gene 1 (hERGl) Channel

[00106] The hERGl ion channel (also referred to as KCNH2 or Kvl 1.1) is an important element for the rapid component of the delayed rectified potassium currents (/&) in cardiac myocytes, for the normal repolarization phase of the cardiac action potential (Curran et al, 1995, "A Molecular Basis for Cardiac -Arrhythmia; HERG Mutations Cause Long Qt Syndrome," Cell, 80, 795-803; Tseng, 2001, "I(Kr): The hERG Channel," J. Mol. Cell.

Cardiol, 33, 835-49; Vandenberg et al, 2001, "HERG Kb Channels: Friend and Foe," Trends. Pharm. Sci. 22, 240-246). Loss of function mutations in hERGl cause increased duration of ventricular repolarization, which leads to prolongation of the time interval between Q and T waves of the body surface electrocardiogram (long QT syndrome-LQTS) (Vandenberg et al, 2001; Splawski et al , 2000, "Spectrum of Mutations in Long-QT

Syndrome Genes KVLQT1, HERG, SCN5A, KCNE1, and KCNE2," Circulation, 102, 1178- 1185; Witchel et al, 2000, "Familial and Acquired Long QT Syndrome and the Cardiac Rapid Delayed Rectifier Potassium Current, Clin. Exp. Pharmacol. Physiol , 27, 753-766). LQTS leads to serious cardiovascular disorders, such as tachyarrhythmia and sudden cardiac death.

[00107] The DNA and amino acid sequences for hERGl are provided as SEQ ID

NO: 1 and SEQ ID NO: 2, respectively.

[00108] A detailed atomic structure of the hERGl gene product based on X-ray cystallography or NMR spectroscopy is not yet available, so structural details for hERGl are based on analogy with other ion channels, computer homology models, pharmacology, and mutagenesis studies. For example, as described in EXAMPLE 1 below, the structure of hERGl is based on combined de novo and homology protein modeling, as previously described (Durdagi et al, 2012, "Modeling of Open, Closed, and Open-Inactivated States of the HERGl Channel: Structural Mechanisms of the State-Dependent Drug Binding," J. Chem. Inf. Model , 52, 2760-2774).

[00109] In homology models, the hERGl gene product comprises a tetramer, with each monomer subunit containing six transmembrane helices (see FIGURE 2). hERGl is formed by coassembly of four monomer a-subunits, each of which has six transmembrane spanning a-helical segments (S 1-S6). Within each hERGl subunit, the S1-S4 helices form a voltage sensor domain (VSD) that senses transmembrane potential and is coupled to a central K+-selective pore domain. Each pore domain is comprised of an outer helix (S5) and inner helix (S6) that together coordinate the pore helix and selectivity filter. The carboxy end of the pore helix and selectivity filter contain the highly conserved K channel signature sequence, which in hERGlis Thr-Ser-Val-Gly-Phe-Gly. This sequence forms anarrow conduction pathway at the extracellular end of the pore in which K ions are coordinated by the backbone carbonyl oxygen atoms of the signature sequence residues.

[00110] Movements of the voltage-sensor domain enable the pore domain to open and close in response to changes in membrane potential. The drug binding site is contained within the central pore cavity of the pore domain, located below the selectivity filter and flanked by the four S6 helices (see FIGURE 2) of the tetrameric channel.

[00111] Without being limited by any theory, in one aspect of the disclosure, the blocking of the central pore cavity or channel of hERG by a drug is a predictor of the cardiotoxicity of the drug. Undesired drug blockade of K+ ion flux in hERGl can lead to long QT syndrome, eventually inducing fibrillation and arrhythmia. hERGl blockade is a significant problem experienced during the course of many drug discovery programs.

6.2.2 Conformational Dynamics of the hERGl Channel

[00112] One of ordinary skill in the art will understand that hERGl displays a distinct multi-state conformational dynamics depending on the membrane potential. The "closed" state of the channel is stabilized at negative membrane potentials (i.e., -80 mV) while depolarizating voltages (to -60 mV) leads to channel opening ("open" or "open activated" state) enabling outward current during physiological ionic conditions. The channel opening is followed by a very rapid C-type inactivation where the activation gate is still open, but the permeation pathway is shut down ("open-inactivated" state). One of ordinary skill in the art will understand that C-type inactivation can be regulated by a multitude of factors including external cation concentrations and/or the presence of drugs.

[00113] One of ordinary skill in the art will understand that hERGl blockade is not a single entity, for example, many of the common blockers exhibit a state-dependent mechanism of action (Stork et al, 2007, "State Dependent Dissociation of HERG Channel Inhibitors," Br. J. Pharmacol , 151, 1368 - 1376; Lees-Miller et al, 2015, "Ivabradine Prolongs Phase 3 of Cardiac Repolarization and Blocks the hERGl (KCNH2) Current over a Concentration-Range Overlapping with that Required to Block HCN4," J. Mol Cell Cardiology, 85, 71-78). Therefore, understanding drug blockade of the hERGl channel as a predictor of cardiotoxicity requires consideration of hERGl channel gating dynamics and the differential binding affinities of the blocker to distinct hERGl conformational states.

6.2.3 Computational Aspects

[00114] In certain aspects, provided herein are computational methods for selecting a compound that is not likely to be cardiotoxic.

[00115] In certain embodiments, the computational methods comprise a computational dynamic model. In certain embodiments, the computational dynamic model comprises a molecular simulation that samples conformational space over time. In certain embodiments, the molecular simulation is a molecular dynamics (MD) simulation.

[00116] In certain embodiments, the method comprising the steps of: a) providing structural information describing one or more conformations of a hERGl channel protein; b) providing structural information describing conformers of one or more compounds; c) using a docking algorithm to dock the conformers of the one or more compounds of step b) to the one or more conformations of step a); d) identifying a plurality of preferred binding

conformations for each of the combinations of protein and compound; e) optimizing the preferred binding conformations using Molecular Dynamics (MD) simulations; and f) determining if the compound blocks the ion channel of the protein in the preferred binding conformations; wherein one or more of the steps a) through f) are not necessarily executed in the recited order.

[00117] In certain embodiments, one or more of the steps a) through f) of the method are performed in the recited order.

[00118] In certain embodiments, the structural information of step a) describes a conformation of the hERGl protein. In certain embodiments, the conformation of the hERGl protein corresponds to the open state. In certain embodiments, the conformation of the hERGl protein corresponds to the closed state. In certain embodiments, the conformation of the hERGl protein corresponds to the open-inactivated state.

[00119] In certain embodiments, providing the structural information in step a) comprises using the coordinates of one of more dominant conformations identified from an MD simulation of the hERGl protein. In certain embodiments, the coordinates of the one of more dominant conformations identified from the MD simulation correspond to the open state of the hERGl protein. In certain embodiments, the coordinates of the one or more dominant conformation identified from the MD simulation correspond to the closed state of the hERGl protein. In certain embodiments, the coordinates of the one or more dominant conformations identified from the MD simulation correspond to the open-inactivated state of the hERGl protein.

[00120] In certain embodiments, providing the structural information in step a) comprises using coordinates selected from the group consisting of Table A, Table B and Table C. In certain embodiments, the coordinates are selected from Table A. In certain embodiments, the coordinates are selected from Table B. In certain embodiments, the coordinates are selected from Table C.

[00121] In certain embodiments, step b) comprises providing the chemical structure of a compound and determining the conformers of the compound. In certain embodiments, the chemical structure of the compound defines the conformers.

[00122] In certain embodiments, steps b) through f) comprise a high-throughput screening of the compounds to determine if they are "blockers" or "non-blockers."

[00123] In certain embodiments, one or more of the steps a) through f) of the method are performed in the recited order.

[00124] In certain embodiments, steps a) through f) of the method are executed on one or more processors.

6.2.3.1 Structural information of the hERGl ion channel protein

[00125] In certain embodiments, the method comprises the step of using structural information describing the structure of the hERGl ion channel protein. In certain embodiments, the ion channel protein is also referred to as a "receptor" or "target" and the terms "protein," "receptor" and "target" are used interchangeably.

[00126] In certain embodiments, the structural information describing the structure of the hERGl ion channel protein is from a homology model.

[00127] The hERGl homology model may comprise comparative protein modeling methods including homology modeling methods (see, e.g., Marti -Renom et al, 2000, Annu. Rev. Biophys. Biomol. Struct. 29, 291-325) performable without limitation using the

"Modeller" computer program (Fiser and Sali, 2003, Methods Enzymol. 374, 461-91) or the "Swiss-Model" application (Arnold et al, 2006, Bioinformatics 22, 195-201); or protein threading modeling methods (see, e.g., Bowie et al, 1991, Science 253, 164-170; Jones et al, 1992, Nature 358, 86-89) performable without limitation using the "Hhsearch" program (Soding, 2005, Bioinformatics 21, 951-960), the "Phyre" application (Kelley and Sternberg, 2009, Nature Protocols 4, 363-371) or the "Raptor" program (Xu et al, 2003, J. Bioinform. Comput. Biol. 1, 95-117); may further comprise ab initio or de novo protein modeling methods using various algorithms, performable without limitation using the publically distributed "ROSETTA'" platform (Simons et al, 1999, Genetics 37, 171-176; Baker 2000, Nature 405, 39-42; Bradley et al, 2003, Proteins 53, 457-468; Rohl 2004, Methods Enzymol. 383, 66-93), the "I-TASSER" application (Wu et al, 2007, BMC Biol. 5, 17), or using physics-based prediction (see, e.g., Duan and Kollman 1998, Science 282, 740-744; Oldziej et al, 2005, Proc. Natl. Acad. Sci. USA 102, 7547-7552); or a combination of any such approaches. Computational approaches applicable herein for structure prediction of biomolecules are evaluated annually within the Critical Assessment of Techniques for Protein Structure (CASP) experiment as published in the CASP Proceedings

(http://predictioncenter.org/). Advantageously, data holding information about

computationally predicted conformations and structures of many biomolecules such as peptides, polypeptides and proteins are available through respective publically available repositories (see, e.g., Kopp and Schwede, 2004, Nucleic Acids Research 32, D230-D234).

[00128] In certain embodiments, the structural information describing the structure of the hERGl ion channel protein is selected from one or more of the open, closed, and/or open- inactivated models of the hERGl channel published in Durdagi et al, 2012, "Modeling of Open, Closed, and Open-Inactivated States of the HERGl Channel: Structural Mechanisms of the State-Dependent Drug Binding," J. Chem. Inf. Model , 52, 2760-2774.

6.2.3.2 Structural Information of the Compound (Ligand)

[00129] In certain embodiments, the method comprises providing structural information describing conformers of one or more compounds or ligands. As used herein, the terms "compound" and "ligand" are interchangeable.

[00130] One of ordinary skill in the art will understand that a chemical compound can adopt differing three-dimensional (3-D) shapes or "conformers" due to rotation of atoms about a bond. Conformers can thus interconvert by rotation around a single bond without breaking. A particular conformer of a ligand may provide a complimentary geometry to the pore (e.g., permeation pore) of an ion channel protein, and promote binding. [00131] In certain embodiments, the structural information of describing conformers of one or more compounds or ligands is obtained from the chemical structure of a compound or ligand.

[00132] In certain embodiments, the structural information of the compound is based upon a viral compound being studied or developed by universities, pharmaceutical companies, or individual inventors. Typically, the compound will be a small organic molecule having a molecular weight under 900 atomic mass units. Structural information of the compound may be provided in 2D or 3D, using ChemDraw or simple structural depictions, or by entry of the compound's chemical name. Computer-based modeling of the compound may be used to translate the chemical name or 2D information of the compound into a 3D representative structure.

[00133] The software LigPrep from the Schrodinger package (Schrodinger Release

2013-2: LigPrep, version 2.7, Schrodinger, LLC, New York, NY, 2013) may be used to translate the 2D information of the compound (ligand) into a 3D representative structure which provides the structural information. LigPrep may also be used to generate variants of the same compound (ligand) with different tautomeric, stereochemical, and ionization properties. All generated structures may be conformationally relaxed using energy minimization protocols included in LigPrep.

[00134] In certain embodiments, the compound is selected from a list of compounds that have failed in clinical trials, or were halted in clinical trials due to cardiotoxicity.

[00135] In certain embodiments, the compound is selected from TABLE 1, below:

TABLE 1; Cardiac Hazardous Drugs

Figure imgf000032_0001
[00136] In certain embodiments, the compound is an anticancer agent, such as anthracyclines, mitoxantrone, cyclophosphamide, fluorouracil, capecitabine and trastuzumab. In certain embodiments, the compound is an immunomodulating drug, such as interferon- alpha-2, interleukin-2, infliximab and etanercept. In certain embodiments, the compound is an antidiabetic drug, such as rosiglitazone, pioglitazone and troglitazone. In certain embodiments, the compound is an antimigraine drug, such as ergotamine and methysergide. In certain embodiments, the compound is an appetite suppressant, such as fenfulramine, dexfenfluramine and phentermine. In certain embodiments, the compound is a tricyclic antidepressant. In certain embodiments, the compound is an antipsychotic drug, such as clozapine. In certain embodiments, the compound is an antiparkinsonian drug, such as pergolide and cabergoline. In certain embodiments, the compound is a glucocorticoid. In certain embodiments, the compound is an antifungal drugs such as itraconazole and amphotericin B. In certain embodiments, the compound is an NSAID, including selective cyclo-oxygenase (COX)-2 inhibitors.

[00137] In certain embodiments, the compound is selected from the group consisting of an antihistamine, an antiarrhythmic, an antianginal, an antipsychotic, an anticholinergic, an antitussive, an antibiotic, an antispasmodic, a calcium antagonist, an inotrope, an ACE inhibitor, an antihypertensive, a beta-blocker, an antiepileptic, a gastroprokinetic agent, an alphal -blocker, an antidepressant, an aldosterone antagonist, an opiate, an anesthetic, an antiviral, a PDE inhibitor, an antifungal, a serotonin antagonist, an antiestrogen, and a diuretic.

[00138] In certain embodiments, the compound is an active ingredient in a natural product. In certain embodiments, the compound is a toxin or environmental pollutant.

[00139] In certain embodiments, the compound is an antiviral agent.

[00140] In certain embodiments, the compound is selected from the group consisting of a protease inhibitor, an integrase inhibitor, a chemokine inhibitor, a nucleoside or nucleotide reverse transcriptase inhibitor, a non-nucleoside reverse transcriptase inhibitor, and an entry inhibitor.

[00141] In certain embodiments, the compound is capable of inhibiting hepatitis C virus (HCV) infection. [00142] In certain embodiments, the compound is an inhibitor of HCV NS3/4A serine protease.

[00143] In certain embodiments, the compound is an inhibitor of HCV NS5B RNA dependent RNA polymerase.

[00144] In certain embodiments, the compound is an inhibitor of HCV NS5A monomer protein.

[00145] In certain embodiments, the compound is selected from the group consisting of Abacavir, Aciclovir, Acyclovir, Adefovir, Amantadine, Amprenavir, Ampligen, Arbidol, Atazanavir, Balavir, Boceprevirertet, Cidofovir, Darunavir, Delavirdine, Didanosine.

Docosanol, Edoxudine, Efavirenz, Emtricitabine, Enfuvirtide, Entecavir, Famciclovir, Fomivirsen, Fosamprenavir, Foscarnet, Fosfonet, Ganciclovir, Ibacitabine, Imunovir, Idoxuridine, Imiquimod, Indinavir, Inosine, Interferon type III, Interferon type II, Interferon type I, Interferon, Lamivudine, Lopinavir, Loviride, Maraviroc, Moroxydine, Methisazone, Nelfinavir, Nevirapine, Nexavir, Oseltamivir (Tamiflu), Peginterferon alfa-2a, Penciclovir, Peramivir, Pleconaril, Podophyllotoxin, Raltegravir, Ribavirin, Rimantadine, Ritonavir, Pyramidine, Saquinavir, Sofosbuvir, Stavudine, Telaprevir, Tenofovir, Tenofovir disoproxil, Tipranavir, Trifluridine, Trizivir, Tromantadine, Truvada, Valaciclovir (Valtrex),

Valganciclovir, Vicriviroc, Vidarabine, Viramidine, Zalcitabine, Zanamivir (Relenza), and Zidovudine.

[00146] In certain embodiments, the compound is selected from the group consisting of terfenadine, astemizole, grepafloxacin, terodiline, droperidol, lidoflazine, sertindole, levomethadyl and cisapride.

[00147] In certain embodiments, the compound binds or blocks the hERGl channel in a state-dependent manner. In certain embodiments, the compound binds or blocks the hERGl channel in its open, closed, and/or open-inactivated state. In certain embodiments, the compound binds or blocks the hERGl channel in its open state. In certain embodiments, the compound binds or blocks the hERGl channel in its closed state. In certain embodiments, the compound binds or blocks the hERGl channel in its open-inactivated state.

[00148] In certain embodiments, the compound is selected from the group consisting of ivabradine, dofetilide, ibutilide, E4031, MK-499, KN-93, amiodarone, cisapride, haloperidol, droperidol, bepridil, terfenadine, E-4031, propafenone, domperidone, changrolin, and bertosamil. In certain embodiments, the compound is selected from the group consisting of amiodarone, cisapride, droperidol and haloperidol. In certain embodiments, the compound is selected from the group consisting of bepridil, domperidone, E-4031 and terfenadine.

[00149] In certain embodiments, the compound is ivabradine, for which the chemical name is "3-[3-({[(7S)-3,4-dimethoxybicyclo[4.2.0]octa-l,3,5-trien-7- yl]methyl}(methyl)arnino)propyl]-7,8-dimethoxy-2,3,4,5-tetrahydro-lH-3-benzazepin-2-one." The structure of ivabradine is provided below:

Figure imgf000035_0001

[00150] In certain embodiments, the compound is a methanesulfonanilide, for example, dofetilide or ibutilide.

[00151] In certain embodiments, the compound is dofetilide, for which the chemical name is "N-[4-(2-{[2-(4-methane sulfonamidophenoxy)ethyl]

(methyl)arnino}ethyl)phenyl]methanesulfonamide." The structure of dofetilide is provided below:

Figure imgf000035_0002

[00152] In certain embodiments, the compound is cisapride, for which the chemical name is ' ±)-cis-4-arnino-5-chloro-N-(l-[3-(4-fluorophenoxy)propyl]-3-methoxypiperidin-4- yl)-2-methoxybenzamide." The structure of cisapride is provided below:

Figure imgf000036_0001

F

[00153] In certain embodiments, the compound is Daclatasvir (BMS-790052), for which the chemical name is "Methyl [(2S)-1 {(2S)-2-[5-(4'-{2-[(2S)-l {(2S)-2- [(methoxycarbonyl)amino]-3-methylbutanoyl}2-pyrrolidinyl]-lH-imidazol-5-yl}4- biphenyly 1)- 1 H-imidazol-2-yl] - 1 -py rrolidinyl } 3 -methyl- 1 -oxo-2-butany 1] carbamate. " The structure of Daclastavir is provided below:

Figure imgf000036_0002

[00154] In certain embodiments, the compound is BMS-986094, for which the chemical name is "(2R)-neopentyl 2-(((((2R,3R,4R)-5-(2-amino-6-methoxy-9H-purin-9-yl)- 3,4-dihy droxy-4-methyltetrahydrofuran-2-yl)methoxy)(naphthalen- 1 - yloxy)phosphoryl)amino)propanoate." The structure of BMS-986094 is illustrated below:

Figure imgf000037_0001

6.2.3.3 Energy Minimization

[00155] In certain embodiments, the X-ray crystal structure, NMR solution structures, homology models, molecular models, or generated structures disclosed herein are subjected to energy minimization (EM) prior to performing an MD simulation.

[00156] The goal of EM is to find a local energy minimum for a potential energy function. A potential energy function is a mathematical equation that allows the potential energy of a molecular system to be calculated from its three-dimensional structure. Examples of energy minimization algorithms include, but are not limited to, steepest descent, conjugated gradients, Newton-Raphson, and Adopted Basis Newton-Raphson (Molecular Modeling: Principles and Applications, Author A. R. Leach, Pearson Education

Limited/Prentice Hall (Essex, England), 2nd Edition (2001) pages: 253-302). It is possible to use several methods interchangeably.

6.2.3.4 Molecular Simulations

[00157] In certain embodiments, the method comprises the step of performing a molecular simulation of the structure of the ion channel protein.

[00158] Accordingly, provided herein are molecular simulations that sample conformational space of the ion channel protein according to the methods described herein. In certain embodiments, the molecular simulation is a molecular dynamics (MD) simulation.

[00159] Molecular simulations can be used to monitor time-dependent processes of the macromolecules and macromolecular complexes disclosed herein, in order to study their structural, dynamic, and thermodynamic properties by solving the equation of motion according to the laws of physics, e.g., the chemical bonds within proteins may be allowed to flex, rotate, bend, or vibrate as allowed by the laws of chemistry and physics. This equation of motion provides information about the time dependence and magnitude of fluctuations in both positions and velocities of the given molecule. Interactions such as electrostatic forces, hydrophobic forces, van der Waals interactions, interactions with solvent and others may also be modeled in MD simulations. The direct output of a MD simulation is a set of "snapshots" (coordinates and velocities) taken at equal time intervals, or sampling intervals. Depending on the desired level of accuracy, the equation of motion to be solved may be the classical (Newtonian) equation of motion, a stochastic equation of motion, a Brownian equation of motion, or even a combination (Becker et al , eds. Computational Biochemistry and

Biophysics. New York 2001).

[00160] One of ordinary skill in the art will understand that direct output of a MD simulation, that is, the "snapshots" taken at sampling intervals of the MD simulation, will incorporate thermal fluctuations, for example, random deviations of a system from its average state, that occur in a system at equilibrium.

[00161] In certain embodiments, the molecular simulation is conducted using the

CHARMM (Chemistry at Harvard for Macromolecular Modeling) simulation package (Brooks et al, 2009, "CHARMM: The Biomolecular Simulation Program," J. Comput. Chem., 30(10): 1545-614). In certain embodiments, the molecular simulation is conducted using the NAMD (Not (just) Another Molecular Dynamics program) simulation package (Phillips et al, 2005, "Scalable Molecular Dynamics with NAMD," J. Comput. Chem., 26, 1781-1802; Kale et al, 1999, "NAMD2: Greater Scalability for Parallel Molecular

Dynamics," J. Comp. Phys. 151, 283-312). One of skill in the art will understand that multiple packages may be used in combination. Any of the numerous methodologies known in the art to conduct MD simulations may be used in accordance with the methods disclosed herein. The following publications, which are incorporated herein by reference, describe multiple methodologies which may be employed: AMBER (Assisted Model Building with Energy Refinement) (Case et al, 2005, "The Amber Biomolecular Simulation Programs," J. Comput. Chem. 26, 1668-1688; amber.scripps.edu); CHARMM (Brooks et al, 2009, J. Comput. Chem., 30(10): 1545-614; charmm.org); GROMACS (GROningen MAchine for Chemical Simulations) (Van Der Spoel et al, 2005, "GROMACS: Fast, Flexible, and Free," J. Comput. Chem. , 26(16), 1701-18; gromacs.org); GROMOS (GROningen MOlecular Simulation) (Schuler et al, 2001, J. Comput. Chem. , 22(11), 1205-1218;

igc.ethz.ch/GROMOS/index); LAMMPS (Large-scale Atomic/Molecular Massively Parallel Simulator) (Plimpton et al, 1995, "Fast Parallel Algorithms for Short-Range Molecular Dynamics," J. Comput. Chem. , 117, 1-19; lammps.sandia.gov); and NAMD (Phillips et al., 2005, J. Comput. Chem., 26, 1781-1802; Kale et al, 1999, J. Comp. Phys. 151, 283-312).

[00162] Wherein the methods call for a MD simulation, the simulation may be carried out using a simulation package chosen from the group comprising or consisting of AMBER, CHARMM, GROMACS, GROMOS, LAMMPS, and NAMD. In certain embodiments, the simulation package is the CHARMM simulation package. In certain embodiments, the simulation package is the NAMD simulation package.

[00163] Wherein the methods call for a MD simulation, the simulation may be of any duration. In certain embodiments, the duration of the MD simulation is greater than 500 ns. In certain embodiments, the duration of the MD simulation is greater than 400 ns. In certain embodiments, the duration of the MD simulation is greater than 300 ns. In certain embodiments, the duration of the MD simulation is greater than 200 ns. In certain embodiments, the duration of the MD simulation is greater than 150 ns. In certain embodiments, the duration of the MD simulation is greater than 100 ns. In certain embodiments, the duration of the MD simulation is greater than 50 ns. In certain

embodiments, the duration of the MD simulation of step is about 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 250, 300, 350, 400, 450 or 500 ns.

[00164] In certain embodiments, the molecular simulation incorporates solvent molecules. In certain embodiments, the molecular simulation incorporates implicit or explicit solvent molecules. One of ordinary skill in the art will understand that implicit solvation (also known as continuum solvation) is a method of representing solvent as a continuous medium instead of individual "explicit" solvent molecules most often used in MD

simulations and in other applications of molecular mechanics. In certain embodiments, the molecular simulation incorporates water molecules. In certain embodiments, the molecular simulation incorporates implicit or explicit water molecules. In certain embodiments, the molecular simulation incorporates explicit ion molecules. In certain embodiments, the molecular simulation incorporates a lipid bilayer. In certain embodiments, the lipid bilayer incorporates explicit lipid molecules. In certain embodiments, the lipid bilayer incorporates explicit phopholipid molecules. In certain embodiments, the lipid bilayer incorporates a solvated lipid bilayer. In certain embodiments, the lipid bilayer incorporates a hydrated lipid bilayer. In certain embodiments, the hydrated lipid bilayer incorporates explicit phospholipid molecules and explicit water molecules.

6.2.3.5 Principal Component Analysis

[00165] In certain embodiments, the method optionally comprises the step of principal component analysis (PCA) of the MD trajectory. In certain embodiments, PCA is performed prior to identification of dominant conformations of the ion channel protein using clustering algorithms (see below). In certain embodiments, PCA is performed using the software AMBER-ptraj (Case et al, 2012, AMBER 12, University of California, San Francisco; Salomon-Ferrer et al, 2013, "An Overview of the Amber Biomolecular Simulation

Package," WIREs Comput. Mol. Sci. 3, 198-210; Amber Home Page. Assisted Model Building with Energy Refinement. Available at: http://ambermd.org, accessed October 26, 2013). PCA reduces the system dimensionality toward a finite set of independent principal components covering the essential dynamics of the system.

6.2.3.6 Calculation of RMSDs

[00166] In certain embodiments, the method optionally comprises the step of calculating the root mean square deviation (RMSD) of Ca atoms relative to a reference structure of the ion channel protein. In certain embodiments, calculation of RMSD is performed to observe the overall behavior of the MD trajectory, prior to identification of dominant conformations of the ion channel protein using clustering algorithms (see below).

6.2.3.7 Clustering Algorithms

[00167] In certain embodiments, the method comprises the steps of using a clustering algorithm to identify dominant conformations of the ion channel protein from the MD simulation, and selecting the dominant conformations of the protein structure identified from the clustering algorithm.

[00168] Clustering algorithms are well known by one of ordinary skill in the art (see, e.g., Shao et al., 2007, "Clustering Molecular Dynamics Trajectories: 1. Characterizing the Performance of Different Clustering Algorithms," J. Chem. Theory & Computation. 3, 231).

[00169] In certain embodiments, one dominant conformation is selected. In certain embodiments, more than one dominant conformation is selected. In certain embodiments, 2 dominant conformations are selected. In certain embodiments, 3 dominant conformations are selected. In certain embodiments, 4 dominant conformations are selected. In certain embodiments, 5 dominant conformations are selected. In certain embodiments, 5 or more dominant conformations are selected. In certain embodiments, 10 or more dominant conformations are selected. In certain embodiments, 20 or more dominant conformations are selected. In certain embodiments, 50 or more dominant conformations are selected. In certain embodiments, 100 or more dominant conformations are selected. In certain embodiments, 150 or more dominant conformations are selected. In certain embodiments, 200 or more dominant conformations are selected. In certain embodiments, 250 or more dominant conformations are selected. In certain embodiments, 300 or more dominant conformations are selected.

6.2.3.8 Docking Algorithms

[00170] In certain embodiments, the method comprises the step of using a docking algorithm to dock the conformers of the one or more compounds to the dominant conformations of the structure of the ion channel protein determined from the molecular simulations.

[00171] Various docking algorithms are well known to one of ordinary skill in the art. Examples of such algorithms that are readily available include: GLIDE (Friesner et al, 2004 "Glide: A New Approach for Rapid, Accurate Docking and Scoring. 1. Method and

Assessment of Docking Accuracy," J. Med. Chem. 47(7), 1739-49), GOLD (Jones et al, 1995, "Molecular Recognition of Receptor Sites using a Genetic Algorithm with a

Description of Desolvation," J. Mol. Biol, 245, 43), FRED (McGann et al, 2012, "FRED and HYBRID Docking Performance on Standardized Datasets," Comp. Aid. Mol. Design, 26, 897-906), FlexX (Rarey et al, 1996, "A Fast Flexible Docking Method using an Incremental Construction Algorithm," J. Mol. Biol, 261, 470), DOCK (Ewing et al, 1997, "Critical Evaluation of Search Algorithms for Automated Molecular Docking and Database

Screening," J. Comput. Chem. , 18, 1175-1189), AutoDock (Morris et al, 2009, "Autodock4 and AutoDockTools4: Automated Docking with Selective Receptor Flexiblity," J.

Computational Chemistry, 16, 2785-91), IFREDA (Cavasotto et al, 2004, "Protein

Flexibility in Ligand Docking and Virtual Screening to Protein Kinases," J. Mol. Biol,

337(1), 209-225), and ICM (Abagyan et al, 1994, "ICM-A New Method for Protein

Modeling and Design: Application to Docking and Structure Prediction from the Distorted Native Conformation, " J. Comput. Chem., 15, 488-506), among many others. [00172] In certain embodiments, the docking algorithm is DOCK, AutoDock, or

GLIDE-XP.

6.2.3.9 Identification of Preferred Binding Conformations

[00173] In certain embodiments, the method comprises the step of identifying a plurality of preferred binding conformations for each of the combinations compound (ligand) and hERGl ion channel protein (receptor).

[00174] In certain embodiments, a clustering algorithm, as described above, is used to identify the preferred binding conformations for each of the combinations of compound and protein. In certain embodiments, the preferred binding conformations are those which have the largest cluster population and the lowest binding energy. In certain embodiments, the preferred binding conformations are the energetically preferred orientation of the compound (ligand) docked to one or more conformations of the hERGl protein (receptor), for example, conformations that represent the open, closed or open-inactivated states of the hERGl protein, to form a stable complex. In certain embodiments, there is only one preferrend binding conformation for the docked compound.

[00175] In certain embodiments, a compound that blocks the channel in one of its preferred binding conformations is predicted to be cardiotoxic. In certain embodiments, a compound that does not block the channel in any of its preferred binding conformations is predited to not be cardiotoxic.

[00176] In certain embodiments, a compound that blocks the channel in one of its preferred binding conformations is cardiotoxic. In certain embodiments, a compound that does not block the channel in any of its preferred binding conformations has reduced risk of cardiotoxicity.

6.2.3.10 Optimizing Preferred Binding Conformations

[00177] In certain embodiments, the method comprises the step of optimizing the preferred binding conformations using MD, as described above.

[00178] In certain embodiments, the MD is scalable MD.

[00179] In certain embodiments, the MD uses NAMD software. 6.2.3.11 Calculation of Binding Energies. AGr„ir

[00180] In certain embodiments, the method comprises the step of calculating binding energies, AGcaic, for each of the combinations of compound (ligand) and hERGl protein (receptor) in the corresponding optimized preferred binding conformations.

[00181] Calculation of binding energies using a combination of molecular mechanics and solvation models are well known by one of ordinary skill in the art (see, e.g., Kollman et al, 2000, "Calculating Structures and Free Energies of Complex Molecules: Combining Molecular Mechanics and Continuum Models," Acc. Chem. Res. 3B, 889-897).

[00182] In certain embodiments, the method further comprises outputting the selected calculated binding energies, AGcaic, and comparing them to physiologically relevant concentrations for each of the combinations of protein and compound. In this regard, the IC50 (concentration at which 50% inhibition is observed) values measured from, for example, in vitro biological assays can be converted to the observed free energy change of binding, AG0¾ (cal mol"1) using the relation: AGcaic = RTlnKj, where R is the gas constant, R =1.987 cal K^mol"1, is the absolute temperature, and ^ is approximated to be the IC50 measured for a particular compound, Accordingly, AGcaic may be compared to AG0¾ , and physiologically relevant concentrations (IC50) for each of the combinations of protein and compound.

6.2.3.12 Prediction of Cardiotoxicity and Selection of Compound

[00183] In certain embodiments, the method comprises prediction of cardiotoxicity and selection of a compound based on (i) classification of the compound as "blocker" versus "nonblocker"; and/or (ii) calculated binding energies.

(i) Classification of compound as "blocker " versus "nonblocker ":

[00184] In certain embodiments, where the compound does not block the hERGl ion channel in any of its preferred binding conformations, the compound is identified as a "nonblocker." Under such circumstances, the "non-blocking" compound is predicted to have reduced risk of cardiotoxicity, and the compound is selected for further development or possible use in humans, or to be used as a compound for further drug design. In certain embodiments, further clinical development may comprise further testing for cardiotoxicity with other ion channels, for example, sodium or calcium ion channels, using the methods disclosed herein. [00185] In certain embodiments, wherein the compound blocks the hERGl ion channel in one of its preferred binding conformations, the compound is identified as a "blocker." Under such circumstances, the compound is predicted to be cardiotoxic, and the compound is not selected for further clinical development or for use in humans. However, under such circumstances, the method may further comprise the step of using a molecular modeling algorithm to chemically modify or redesign the compound such that it does not block the ion channel in its preferred binding conformations and retains biological activity to its primary biological target, as described in Sections 5.2.3.13 and 5.2.3.14 below, respectively. As a possible alternative to modification/redesign of the compound, a new compound may also be selected from the collections of a chemical or compound library, for example, a library of new drug candidates generated by organic or medicinal chemists as part of a drug discovery program, as described in Section 5.2.3.15 below.

(ii) Calculated binding energies:

[00186] In certain embodiments, where the calculated binding energies, AGcaic, for the preferred binding conformations compare to physiologically relevant compound

concentrations of greater than or equal to 100 μΜ, binding affinity is predicted to be weak. Under such circumstances, the compound is predicted to have reduced risk of cardiotoxicity at therapeutically relevant concentrations. The compound may be selected for further development or possible use in humans, or to be used as a compound for further drug design. In certain embodiments, further clinical development may comprise further testing for cardiotoxicity with other ion channels using the methods disclosed herein.

[00187] In certain embodiments, where the calculated binding energies, AGcaic, for the preferred binding conformations compare to physiologically relevant compound

concentrations of less than or equal to 1 μΜ, binding affinity is predicted to be moderate to strong. The compound is predicted to be cardiotoxic at therapeutically relevant

concentrations, and the compound is not selected for further clinical development or for use in humans. However, under such circumstances, as described above, the method may further comprise the step of using a molecular modeling algorithm to chemically modify or redesign the compound, or as a possible alternative, selecting a new compound from the collections of a chemical or compound library, as described in the sections below. 6.2.3.13 Modification/Redesign of Compounds

[00188] In certain embodiments, the method further comprises the step of using a molecular modeling algorithm to chemically modify or design the compound such that it does not block the ion channel in any of its preferred binding conformations.

[00189] In certain embodiments, the method comprises repeating steps e') through i') for the modified or redesigned compound. In certain embodiments, the method comprises repeating steps a) through f) for the modified or redesigned compound.

[00190] For example, if a chemical moiety of a compound identified as a "blocker" is found to be responsible for blocking, obstructing, or partially obstructing the hERGl ion channel, that chemical moiety may be modified in silico using any one of the molecular modeling algorithms disclosed herein or known to one of ordinary skill in the art. The modified compound may then be retested by repeating steps a) through f) of the methods disclosed herein.

[00191] Following re-testing, if the modified compound does not block, obstruct, or partially obstruct the ion channel in any of its preferred binding conformations, the modified compound may now be identified as a "non-blocker." The modified compound may now be characterized as having reduced risk of cardiotoxicity, and selected for further development or possible use in humans, or to be used as a compound for further drug design. By such modification/redesign, potentially cardiotoxic compounds at risk for QT interval prolongation may be salvaged for further clinical development.

[00192] In certain embodiments, the modified or redesigned compound does not block the ion channel in its preferred binding conformations, but retains selective binding to a desired biological target, as described in Section 5.2.3.14 below.

6.2.3.14 Modification/Redesign of Compounds for Selective

Binding to Primary Biological Target

[00193] In certain embodiments, the modified or redesigned compound retains or even increases selective binding to a primary biological target. In certain embodiments, binding of the compound or modified/redesigned compound to the primary biological target blocks hepatitis C virus (HCV) production. In certain embodiments, the primary biological target is HCV NS3/4A serine protease, HCV NS5B RNA dependent RNA polymerase, or HCV NS5A monomer protein. [00194] In certain embodiments, the modified or redesigned compound retains or even increase its potency as an anticancer agent, an immunomodulating drug, an antidiabetic drug, an antimigraine drug, an appetite suppressant, a tricyclic antidepressant, an antipsychotic drug, an antiparkinsonian drug, a glucocorticoid, an antifungal drug, or an NSAID.

[00195] In certain embodiments, the modified or redesigned compound retains or even increase its potency as an antihistamine, an antiarrhythmic, an antianginal, an antipsychotic, an anticholinergic, an antitussive, an antibiotic, an antispasmodic, a calcium antagonist, an inotrope, an ACE inhibitor, an antihypertensive, a beta-blocker, an antiepileptic, a gastroprokinetic agent, an alphal -blocker, an antidepressant, an aldosterone antagonist, an opiate, an anesthetic, an antiviral, a PDE inhibitor, an antifungal, a serotonin antagonist, an antiestrogen, or a diuretic.

[00196] In certain embodiments, the modified or redesigned compound is tested in an in vitro biological assay for selective binding to its biological target.

[00197] In certain embodiments, the modified or redesigned compound is tested for binding to its biological target in silico using any of the computational models or screening algorithms disclosed herein.

[00198] In certain embodiments, the modified or redesigned compound binds with high affinity to its biological target and/or retains biological activity. In certain

embodiments, where the primary biological target is HCV NS3/4A serine protease, HCV NS5B RNA dependent RNA polymerase, or HCV NS5A monomer protein, the modified or redesigned compound retains antiviral activity.

[00199] In certain embodiments, the computational models or screening algorithms disclosed herein for selecting compounds that have reduced risk of cardiotoxicity may be combined with any computational models or screening algorithms known to those of ordinary skill in the art for modeling the binding of the compound or modified/redesigned compound to its primary biological target.

6.2.3.15 Selection of New Compound from a Chemical Library

[00200] As an alternative to modification/redesign of the compound, a new compound may also be selected from the collections of a chemical or compound library, for example, new drug candidates generated by organic or medicinal chemists as part of a drug discovery program. [00201] For example, once the methods disclosed herein identify a chemical moiety of a original tested compound as a "blocker" that is responsible for blocking, obstructing, or partially obstructing the ion channel, a new compound from a chemical library may be selected wherein, for example, the new compound does not comprise the moiety found to be responsible for the blocking, obstructing, or partially obstructing of the ion channel.

[00202] The new compound may then be retested for cardiotoxicity by repeating steps e) through i) of the methods disclosed herein.

[00203] Following re-testing, if the new compound does not block, obstruct, or partially obstruct the ion channel in any of its preferred binding conformations, the new compound may be identified as a "non-blocker." The new compound may be characterized as having reduced risk of cardiotoxicity, and selected for further development or possible use in humans, or to be used as a compound for further drug design. By such selection of a new compound from a chemical library, an entire drug discovery program with potentially cardiotoxic compounds at risk for QT interval prolongation may be salvaged by redirecting the program to safer lead compounds for further clinical development.

[00204] The new compound selected from the chemical library may also be tested for selective binding to a desired biological target, for example, a primary biological target, as described above in Section 5.2.3.14 above, for the modified/redesigned compound.

6.2.4 Biological Aspects

[00205] Optionally, the methods disclosed herein include checking in silico predicted cardiotoxicities with the results of an in vitro biological assay, or in vivo in an animal model. The methods disclosed herein may also include validating or confirming the in silico predicted cardiotoxicities with the results of an in vitro biological assay, or with the results of an in vivo study in an animal model.

[00206] Accordingly, in certain aspects, provided herein are biological methods for testing, checking, validating or confirming predicted cardiotoxicities.

[00207] In certain embodiments, the method comprises testing, checking, validating or confirming the predicted cardiotoxicity of the compound or modified compound using standard assaying techniques which are known to those of ordinary skill in the art. [00208] In certain embodiments, the method comprises testing, checking, validating or confirming the predicted cardiotoxicity of the compound or modified compound in an in vitro biological assay.

[00209] In certain embodiments, the in vitro biological assay comprises high throughput screening of ion channel and transporter activities.

[00210] In certain embodiments, the in vitro biological assay is a hERGl channel inhibition assay, for example, a FluxOR™ potassium ion channel assay, or electrophysiology measurements in single cells, as explained below.

[00211] In certain embodiments, the method comprises testing the cardiotoxicity of the compound or modified compound in vivo in an animal model.

[00212] In certain embodiments, the cardiotoxicity of the compound or modified compound is tested in vivo by measuring ECG in a wild type mouse or a transgenic mouse model expressing human hERG, as explained below.

6.2.4.1 FluxOR™ Potassium Ion Channel Assay

[00213] In certain embodiments, the in vitro biological assay is a FluxOR™ potassium ion channel assay (see, e.g. Beacham et al, 2010, "Cell-Based Potassium Ion Channel Screening Using FluxOR™ Assay," J. Biomol. Screen., 15(4), 441-446), which allows high throughput screening of potassium ion channel and transporter activities.

[00214] The FluxOR™ assay monitors the permeability of potassium channels to thallium (Tl+) ions. When thallium is added to the extracellular solution with a stimulus to open channels, thallium flows down its concentration gradient into the cells, and channel or transporter activity is detected with a proprietary indicator dye that increases in cytosolic fluorescence. Accordingly, the fluorescence reported in the FluxOR™ system is an indicator of any ion channel activity or transport process that allows thallium into cells.

[00215] In certain embodiments, the FluxOR™ potassium channel assay is performed on HEK 293 cells stably expressing hERGlor mouse cardiomyocyte cell line HL-1 cells.

[00216] In certain embodiments, the FluxOR™ potassium channel assay is performed on a human adult cardiomyocyte cell line expressing hERGl 6.2.4.2 Electrophysiology Measurements in Single Cells

[00217] In certain embodiments, the in vitro biological assay comprises

electrophysiology measurements, for example, patch clamp electrophysiology measurements, which use a high throughput single cell planar patch clamp approach (see, e.g., Schroeder et al , 2003, "Ionworks HT: A New High-Throughput Electrophysiology Measurement Platform," J. Biomol. Screen. 8 (1), 50-64).

[00218] In certain embodiments, electrophysiology measurements are in single cells.

In certain embodiments, the single cells are Chinese hamster ovary (CHO) cells stably transfected with hERGl (CHO-hERG). In certain embodiments, the single cells are from a human adult cardiomyocyte cell line expressing hERGl.

[00219] The cells are dispensed into the PatchPlate. Amphotericin is used as a perforating agent to gain electrical access to the cells. The hERG tail current is measured prior to the addition of the test compound by perforated patch clamping. Following addition of the test compound (typically 0.008, 0.04, 0.2, 1, 5, and 25 μΜ, n = 4 cells per

concentration, final DMSO concentration = 0.25%), a second recording of the hERG current is performed.

[00220] Post-compound hERG currents are usually expressed as a percentage of pre- compound hERG currents (% control current) and plotted against concentration for each compound. Where concentration dependent inhibition is observed the Hill equation is used to fit a sigmoidal line to the data and an IC50 (concentration at which 50% inhibition is observed) is determined.

6.2.4.3 Cloe Screen IC^n hERG Safety Assay

[00221] In certain embodiments, the in vitro biological assay is a Cloe Screen IC50 hERG Safety assay, for example, as provided by the company CYPROTEX (see, e.g., http://www.cyprotex.com/toxicology/cardiotoxicity/hergsafety/).

[00222] In certain embodiments, the Cloe Screen IC50 hERG Safety assay is performed using an Ionworks™ HT platform (Molecular Devices using a CHO hERG cell line) which measures whole-cell current from multiple cells simultaneously using an automated patch clamp system.

[00223] Typically, hERG Safety assay uses a high throughput single cell planar patch clamp approach. CHO-hERG cells are dispensed into a PatchPlate. Amphotericin is used as a perforating agent to gain electrical access to the cells. The hERG tail current is measured prior to the addition of the test compound by perforated patch clamping. Following addition of the test compound (typically 0.008, 0.04, 0.2, 1, 5, and 25 μΜ, n = 4 cells per

concentration, final DMSO concentration = 0.25%), a second recording of the hERG current is performed. Post-compound hERG currents are expressed as a percentage of pre-compound hERG currents (% control current) and plotted against concentration for each compound. Where concentration dependent inhibition is observed the Hill equation is used to fit a sigmoidal line to the data and an IC50 (concentration at which 50% inhibition is observed) is determined.

[00224] In certain embodiments, the hERG safety assay using the Ionworks™ HT system generates data comparable with traditional single cell patch clamp measurements.

6.2.4.4 Electrocardiography Studies in Transgenic Mouse Models

[00225] In certain embodiments, the method comprises testing the cardiotoxicity of the compound or modified compound in vivo by measuring ECG in a transgenic mouse model expressing human hERGl .

[00226] Electrocardiograpy to test anti-arrhythmic activity, in particular, QT prolongation, in transgenic mice expressing hERG specifically in the heart may performed using previously published protocols (Royer et al , 2005, "Expression of Human ERG K+ Channels in the Mouse Heart Exerts Anti-Arrhythmic Activity," Cardiovascular Res. 65, 128-137).

[00227] Alternatively, or in addition, electrocardiograpy to test anti-arrhythmic activity, in particular, QT prolongation, in wild type mice may be performed.

[00228] The following examples are included to demonstrate preferred embodiments of the disclosure. It should be appreciated by those of ordinary skill in the art that the techniques disclosed in the examples which follow represent techniques discovered by the inventor to function well in the practice of the disclosure, and thus can be considered to constitute preferred modes for its practice. However, those of ordinary skill in the art should, in light of the present disclosure, appreciate that many changes can be made in the specific embodiments which are disclosed and still obtain a like or similar result without departing from the spirit and scope of the disclosure. 7. EXAMPLES

[00229] FIGURES 1A and IB depict system block diagrams for selecting a compound that has reduced risk of cardiotoxicity. Processes illustrated in the system block diagrams (1 A) and (IB) are: Target Preparation (includes, e.g., combined de «ονο/homology protein modeling of hERG, as exemplified in EXAMPLE 1, below), Ligand Collection Preparation (as exemplified in EXAMPLE 2, below), Ensemble Generation (includes, e.g., Molecular Dynamics simulations, principal component analysis, and iterative clustering, as exemplified in EXAMPLES 3-4, below), Docking (includes, e.g., docking and iterative clustering, as exemplified in EXAMPLE 5, below), MP Simulations on Selected Complexes (includes, e.g., Molecular Dynamics simulations and preliminary ranking of docking hits, as

exemplified in EXAMPLE 6, below), Rescoring using MM-PBSA (includes, e.g., binding free energy calculation and rescoring of top hits, as exemplified in EXAMPLE 7, below), and Experimental Testing (includes, e.g., hERG channel inhibition studies in mammalian cells, Fluxor™ potassium channel assays in mammalian cells, and electrocardiograpy to test antiarrhythmic activity in transgenic mice expressing hERG, as exemplified in EXAMPLES 9-11, below). The top hits from the Rescoring step can act as positive controls for the next phase screening. In certain embodiments, as shown in the block diagram (IB), the Ensemble Generation. Docking. MP Simulations on Selected Complexes, and Rescoring using MM- PBSA steps may be performed on a supercomputer, for example, the "IBM Blue Gene/Q" supercomputer system at the Health Sciences Center for Computational Innovation,

University of Rochester, or the equivalent thereof. The Target Preparation and Ligand Collection Preparation steps may be performed on local machines (e.g., in a Molecular Operating Environment (MOE)).

[00230] In certain embodiments, the systems and methods disclosed herein bypass the

Target Preparation and Ensemble Generation steps, and use the coordinates of hERGl models, disclosed herein, as direct input for the Docking step. In certain embodiments, these hERGl models correspond to the dominant conformations identified by MD simulations, as described herein. In certain embodiments, these coordinates correspond to the open state, the closed state, or the open-inactivated state of the hERGl protein. In certain embodiments, these coordinates are selected from the group consisting of Table A, Table B and Table C, disclosed herein.

[00231] In certain embodiments, the MD simulations disclosed herein comprise simulations of at least 200,000 atoms and their coordinates (protein, membrane, water and ions). In certain embodiments, the equilibration process of at least 200 ns is equivalent to taking 100 billion steps (1011 steps) updating the position coordinates and velocities of each atom in the system in each of these steps. In certain embodiments, the MD simulations using a current state-of-the art supercomputer, for example, the "IBM Blue Gene/Q" supercomputer system, require an equivalent of 10 million CPU hours which scales approximately linearly with the size of the computational hardware available.

7 1 EXAMPLE 1; COMBINED DE NOVO/HOMOLOGY PROTEIN

MODELING

[00232] Combined ROSETTA-membrane de-novo, homology protein modeling of the hERGl channel protein is performed as previously described (Durdagi et al., 2011,

"Combined Receptor and Ligand-Based Approach to the Universal Pharmacophore Model Development for Studies of Drug Blockade to the hERGl Pore Domain," J. Chem. Inf.

Model, 51, 463-74; Durdagi et al., 2012, "Modeling of Open, Closed, and Open-Inactivated States of the HERGl Channel: Structural Mechanisms of the State-Dependent Drug Binding," J. Chem. Inf. Model, 52, 2760-2774).

[00233] The coordinates for hERGl generated from the homology modeling described in EXAMPLE 1, above, is used as input for the MD simulations, described in EXAMPLE 3 below.

7 2 EXAMPLE 2; COMPOUND (LIGAND) PREPARATION

[00234] The software MOE (Molecular Operating Environment) from Chemical

Computing Group (CCG) (http://www.chemcomp.com/press_releases/2010-l l-30.htm) is used to translate the 2D information of a compound (ligand) into a 3D representative structure. MOE also generates variants of the same ligand with different tautomeric, stereochemical, and ionization properties. All generated structures are conformationally relaxed using energy minimization protocols included in MOE.

[00235] Alternatively, or in addition, the software LigPrep from the Schrodinger package (Schrodinger Release 2013-2: LigPrep, version 2.7, Schrodinger, LLC, New York, NY, 2013) may be used to translate the 2D information of a compound (ligand) into a 3D representative structure. LigPrep may also be used to generate variants of the same ligand with different tautomeric, stereochemical, and ionization properties. All generated structures may be conformationally relaxed using energy minimization protocols included in LigPrep. 7.3 EXAMPLE 3; MOLECULAR DYNAMICS SIMULATIONS

[00236] Long supercomputer MD simulations for the selected models of EXAMPLE 1 is carried out as previously described (Barakat et al., 2014, "A Human Ether-a-go-go-related (Herg) Ion Channel Atomistic Model Generated by Long Supercomputer Molecular

Dynamics Simulations and its Use in Predicting Drug Cardiotoxicity," Toxicol. Lett. 230(3), 382-392; Lees-Miller et al, 2015, "Ivabradine Prolongs Phase 3 of Cardiac Repolarization and Blocks the HERGl (KCNH2) Current over a Concentration-Range Overlapping with that Required to Block HCN4," J. Mol. Cell. Cardiol, 85: 71-78).

7 4 EXAMPLE 4; ITERATIVE CLUSTERING

[00237] Iterative clustering of the MD trajectory of EXAMPLE 3 is then performed to extract dominant conformations of hERGl. The clustering procedure has been previously described (Barakat et al, 2010, "Ensemble-Based Virtual Screening Reveals Dual-Inhibitors for the P53 -MDM2/MDMX Interactions," J. Mol. Graph. & Model. 28, 555-568; Barakat et al, 2011, "Relaxed Complex Scheme Suggests Novel Inhibitors for the Lyase Activity Of DNA Polymerase Beta," J. Mol. Graph. & Model. 29, 702-716). An average-linkage algorithm is used to group similar conformations in the 200 ns trajectory into clusters. The optimal number of clusters is estimated by observing the values of the Davies-Bouldin index (DBI) (see, e.g., Davies et al., 1979, "A Cluster Separation Measure," IEEE Trans. Pattern Anal. Intelligence 1, 224) and the percentage of data explained by the data (SSR/SST) (see, e.g., Shao et al, 2007, "Clustering Molecular Dynamics Trajectories: 1. Characterizing the Performance of Different Clustering Algorithms," J. Chem. Theory & Computation. 3, 231) for different cluster counts ranging from 5 to 600. At the optimal number of clusters, a plateau in the SSR/SST is expected to match a local minimum in the DBI (Shao et al, 2007). Using this methodology, distinct conformations for the intracellular hERG channel are identified.

[00238] Alternatively, or in addition, average coordinates for the hERGl molecule may be calculated over the entire length of the MD trajectory, and this set of averaged coordinates used to select a single "snap shot" at one time step in the trajectory that best represents the conformational space explored by the trajectory.

7 5 EXAMPLE 5; DOCKING

[00239] Docking: Docking of the conformers of the compounds of EXAMPLE 2 to the hERGl conformation(s) of EXAMPLE 4 are performed using the software AutoDock, version 4.0 (Morris et al, 2009, "Autodock4 and AutoDockTools4: Automated docking with selective receptor flexiblity," J. Computational Chemistry, 16, 2785-91). The docking method and parameters are similar to ones previously used (Barakat et al, 2009,

"Characterization of an Inhibitory Dynamic Pharmacophore for the ERCC1-XPA Interaction Using a Combined Molecular Dynamics and Virtual Screening Approach," J. Mol. Graph. Model 28, 113-130). Alternatively, or in addition, docking simulations may be performed using the Glide-XP (extra precision) docking program from Schrodinger (Schrodinger LLC, Portland, USA; http://www.schrodinger.com).

[00240] Iterative Clustering: Clustering of the docking results may follow the same adaptive procedure as one previously employed (Barakat et al., 2009) to identify the best- scored binding poses for each of the combinations of hERGl protein and compound.

7 6 EXAMPLE 6; MOLECULAR DYNAMICS ON SELECTED

COMPLEXES

[00241] The lowest energy poses identified in EXAMPLE 5 for each of the combinations of hERGl protein and compound is used as a starting configuration of an MD simulation. The AMBER99SB force field (Hornak et al, 2006, "Comparison of Multiple AMBER Force Fields and Development of Improved Protein Backbone Parameters," Proteins 65, 712-725) is used for protein parameterization, while the generalized AMBER force field (GAFF) provides parameters for compounds (Wang et al., 2004, "Development and Testing of a General AMBER Force Field," J. Comput. Chem. 25, 1157-1174). For each compound, partial charges are calculated with the AMl-BCC method using the Antechamber module of AMBER 10. Protonation states of all ionizable residues are calculated using the program PDB2PQR. All simulations are performed at 300 K and pH 7 using the NAMD program (Kale et al., 1999, "NAMD2: Greater Scalability for Parallel Molecular Dynamics," J. Comp. Phys. 151, 283-312). Following parameterization, the protein-ligand complexes are immersed in the center of a cube of TIP3P water molecules. The cube dimensions are chosen to provide at least a 10 A buffer of water molecules around each system. When required, chloride or sodium counter-ions are added to neutralize the total charge of the complex by replacing water molecules having the highest electrostatic energies on their oxygen atoms. The fully solvated systems are then minimized and subsequently heated to the simulation temperature with heavy restraints placed on all backbone atoms. Following heating, the systems are equilibrated using periodic boundary conditions for 100 ps and energy restraints reduced to zero in successive steps of the MD simulation. The simulations are then continued for 2 ns during which atomic coordinates are saved to the trajectory every 2 ps for subsequent binding energy analysis.

7.7 EXAMPLE 7; BINDING FREE ENERGY CALCULATION AND RESCORING OF TOP HITS

[00242] The molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) technique is used to re-score the preliminary ranked docking hits (Kollman et al, 2000, "Calculating Structures and Free Energies of Complex Molecules: Combining Molecular Mechanics and Continuum Models," Acc. Chem. Res. 3B, 889-897). This technique combines molecular mechanics with continuum solvation models. The total free energy is estimated as the sum of average molecular mechanical gas-phase energies (EMM), solvation free energies (Gsoiv), and entropy contributions (-TSsoiute) of the binding reaction:

G = EMM + Gsolv - TSS0\ute

[00243] The molecular mechanical (EMM) energy of each snapshot is calculated using the SANDER module of AMBERIO with all pair- wise interactions included using a dielectric constant (ε) of 1.0. The solvation free energy (Gsolv) is estimated as the sum of electrostatic solvation free energy, calculated by the finite-difference solution of the Poisson-Boltzmann equation in the Adaptive Poisson-Boltzmann Solver (APBS) and non-polar solvation free energy, calculated from the solvent-accessible surface area (SASA) algorithm. The solute entropy is approximated using the normal mode analysis. Applying the thermodynamic cycle for each protein-ligand complex, the binding free energy is calculated using the following equation:

f^ hERG-ligand . ~< hERG-ligand t k ^ ligand . ~i hERG

U ca/c _ U £os + U∞/v _ lAU∞/v + (j∞Zv / L>

[00244] Here, (

Figure imgf000055_0001
represents the free energy per mole for the non-covalent association of the ligand-protein complex in vacuum (gas phase) at a representative temperature, while ( -AGSOLV) stands for the work required to transfer a molecule from its solution conformation to the same conformation in vacuum (assuming that the binding conformation of the ligand-protein complex is the same in solution and in vacuum).

[00245] The calculated binding energies, AG°ca/c, can be compared directly to the physiologically relevant concentrations. In this regard, the IC50 (concentration at which 50% inhibition is observed) values measured from, for example, in vitro biological assays are converted to the observed free energy change of binding, AGa s (cal mol"1) using the equation:

AG°obs = RT lnK, (3) where R is the gas constant, R =1.987 cal K^mol"1, T is the absolute temperature, and ^ is approximated to be the IC50 measured for a particular test compound, Accordingly, the calculated binding energies in silico, AG°caic, are compared to the observed binding energy in vitro, AGobs (e.g., from inhibition studies), and thus, also to the physiologically relevant concentrations (IC50) for each of the combinations of compound and protein, for example, hERG.

[00246] The calculated binding energy of a tested compound may also compared to that of a known control (a known hERG blocker from a standardized panel of drugs). The following equation is used:

AG. -AG^ RT ln^)

K ' (4) where Kaand Kj2 are the molar concentrations of the tested compound and the control, repectively.

[00247] Alternatively, or in addition, binding energies may be estimated using umbrella sampling simulations (see, e.g., Kaster et al., "Umbrella Sampling," WIREs Comput Mol Sci 2011, 1 : 932-942. doi: 10.1002/wcms.66) to evaluate the potential of mean force for the tested compound unbinding from the hERGl channel.

7 8 EXAMPLE 8; CLASSIFICATION OF CHANNEL BLOCKAGE

[00248] VMD (Visual MD) (Humphrey et al, 1996, "Visual Molecular Dynamics," J. Mol. Graphics, 14 (1), 33-38) is used to visually analyze the results of the MD trajectories of the selected complexes of EXAMPLE 6 for preliminary ranking of the docking hits.

[00249] A channel blocker binds within the cavity so that the passage of the potassium ions through the selection filter is blocked. On the other hand, a compound may bind to the channel in a way that it does not interfere with the potassium passage. By visual inspection of the selected complexes of EXAMPLE 6, compounds may be classified as "blockers," e.g., compound that blocked the hERGl ion channel, or as "non-blockers," e.g., compounds that do not block the hERGl ion channel. 7.9 EXAMPLE 9; HERG1 CHANNEL INHIBITION (IC n DETERMINATION) IN MAMMALIAN CELLS

[00250] Mammalian cells expressing the hERGl potassium channel are dispensed into

384-well planar arrays and hERG tail-currents are measured by whole-cell voltage-clamping. A range of concentrations (TBD) of the test compounds are then added to the cells and a second recording of the hERG current is made. The percent change in hERG current is calculated. IC50 values are derived by fitting a sigmoidal function to concentration-response data, where concentration-dependent inhibition was observed.

[00251] The experiments are performed on an Ion Works™ HT instrument (Molecular

Devices Corporation), which automatically performs electrophysiology measurements in 48 single cells simultaneously in a specialised 384-well plate (PatchPlate™). All cell suspensions, buffers and test compound solutions are at room temperature during the experiment.

[00252] The cells used are Chinese hamster ovary (CHO) cells stably transfected with hERG (cell-line obtained from Cytomyx, UK). A single-cell suspension is prepared in extracellular solution (Dulbecco's phosphate buffered saline with calcium and magnesium pH 7-7.2) and aliquots are added automatically to each well of a PatchPlate™. The cells are then positioned over a small hole at the bottom of each well by applying a vacuum beneath the plate to form an electrical seal. The vacuum is applied through a single compartment common to all wells which are filled with intracellular solution (buffered to pH 7.2 with HEPES). The resistance of each seal is measured via a common ground-electrode in the intracellular compartment and individual electrodes placed into each of the upper wells.

[00253] Electrical access to the cell is then achieved by circulating a perforating agent, amphotericin, underneath the PatchPlate™ and then measuring the pre-compound hERG current. An electrode is positioned in the extracellular compartment and a holding potential of -80 mV for 15 sec is applied. The hERG channels are then activated by applying a depolarising step to +40 mV for 5 sec and then clamped at -50 mV for 4 sec to elicit the hERG tail current, before returning to -80 mV for 0.3 s.

[00254] A test compound is then added automatically to the upper wells of the PatchPlate™ from a 96-well microtitre plate containing a range of concentrations of each compound. Solutions are prepared by diluting DMSO solutions of the test compound into extracellular buffer. The test compound is left in contact with the cells for 300 sec before recording currents using the same voltage-step protocol as in the pre-compound scan.

Quinidine, an established hERG inhibitor, is included as a positive control and buffer containing 0.25% DMSO is included as a negative control. The results for all compounds on the plate are rejected and the experiment repeated if the IC50 value for quinidine or the negative control results are outside quality-control limits.

[00255] Each concentration is tested in 4 replicate wells on the PatchPlate™.

However, only cells with a seal resistance greater than 50 MOhm and a pre-compound current of at least 0.1 nA are used to evaluate hERG blockade.

[00256] Post-compound currents are then expressed as a percentage of pre-compound currents and plotted against concentration for each compound. Where concentration- dependent inhibition is observed, the data are fitted to the following equation and an IC50 value calculated:

Y _ Y max - Y mi■n ^

~ 1 + (X/X50)s + min (5). where Y = (post-compound current/pre-compound current) x 100, x = concentration, X50 = concentration required to inhibit current by 50% (IC50) and s = slope of the graph.

[00257] An IC50 was reported if concentration-dependent inhibition is observed. The standard error (SE) of the IC50 model and the number of data-points used to determine IC50 is also reported.

7 10 EXAMPLE 10; FLUXOR™ POTASSIUM CHANNEL ASSAY IN MAMMALIAN CELLS

[00258] The FluxOR™ potassium channel assay is performed on Human Embryonic

Kidney 293 cells (HEK 293) cells stably expressing hERGl or mouse cardiomyocyte cell line HL-1 cells (a gift from Dr. William Clay comb, Louisiana, USA). Briefly, FluxOR™ loading buffer is made from Hank's Balanced Saline Solution (HBSS) buffered with 20 mM HEPES and pH adjusted with NaOH to 7.4. Powerload™ concentrate and water-soluble probenecid are used as directed by the kit to enhance the dye solubility and retention, respectively.

Media are removed from the cell plates manually, and 20 of loading buffer containing the FluxOR™ dye mix is applied to each well. Once inside the cell, the nonfluorescent AM ester form of the FluxOR™ dye is cleaved by endogenous esterases into a thallium-sensitive indicator. The dye is loaded for 60 min at room temperature and then removed manually. The cell plates are subsequently washed once with dye-free assay buffer, before adding a final volume of 20 assay buffer containing water-soluble probenecid. Cell plates receive 2 per well of the screening compounds, and are then incubated at room temperature (23- 25 °C) for 30 min for HEK 293 cells to allow equilibration of the test compounds in the cultures or at 37 °C for 24 h for HL-1 cells. Prior to injection, stimulation buffer is prepared from the 5X chloride-free buffer, thallium, and potassium sulfate reagents provided in the kit to contain 10 mM free thallium (5 mM T12S04) and 50 mM free potassium (25 mM K2S04). These concentrations result in final added concentrations of 2 mM free Tl+ and 10 mM free K+ after 1:5 dilution upon injection of the stimulus buffer into cells that has been loaded with FluxOR™ dye. To each well 20 stimulation buffer is added and fluorescence measures are done every 1 sec for a total time of 180 sec. Fluorescence measurement are made using a Perkin Elmer EnSpire Multimode Plate Reader (Massachusetts, USA) using excitation and emission wavelengths of 490/525 nm, respectively.

7 11 EXAMPLE 11; ELECTROCARDIOGRAPY TO TEST ANTIARRHYTHMIC ACTIVITY IN TRANSGENIC MICE EXPRESSING HERG

[00259] Electrocardiograpy to test anti-arrhythmic activity in transgenic mice expressing hERGl specifically in the heart may be performed using previously published protocols (Royer et al. , 2005, "Expression of Human ERG K+ Channels in the Mouse Heart Exerts Anti-Arrhythmic Activity," Cardiovascular Res. 65, 128-137).

7 12 EXAMPLE 12; STATE-DEPENDENT BINDING OF A TEST

COMPOUND

[00260] State-dependent binding of a test compound is presented. As an example, computational dynamic models of dofetilide bound to hERGl in its open and open- inactivated states is presented.

[00261] Dofetilide is a class III antiarrhythmic agent, which is marketed in the United

States under the trade name Tikosyn®. Dofetilide is used for the maintenance of sinus rhythm in individuals prone to the occurrence of atrial fibrillation and flutter arrhythmias, and for chemical cardioversion to sinus rhythm from atrial fibrillation and flutter. Torsades de Pointes is the most serious side effect of dofetilide therapy. The atomistic details of this cardiotoxicity are explored in the present example using the methods and systems disclosed herein. [00262] Three-dimensional coordinates describing the hERGl protein in the open and open-inactivated states were obtained by a combination of ROSETTA-membrane de-novo, homology modelling and MD simulations. In brief, ROSETTA-membrane simulations were run to generate refined ensembles for open-inactivated and closed states. ROSETTA output was clusted into 12 to 20 stable clusters and these clusters run on the "IBM Blue Gene/Q" supercomputer system for timescales around 100 ns. The structural difference between open state and open-inactivated states is schematically illustrated in FIGURE 3.

[00263] The structure of dofetilide was downloaded from ZINC database (Irwin et al.

2012, "ZINC: A Free Tool to Discover Chemistry for Biology," J. Chem. Inf. Model. , 52, 1757-1768). Dofetilide was docked in silico to the developed hERGl models representing the open and open-inactivated states of the channel with Glide-XP (extra precision) docking program from Schrodinger (Schrodinger LLC, Portland, USA; http://www.schrodinger.com). The best-scored binding poses for neutral and cationic dofetilide binding to an intra-cavitary site in the open and open-inactivated HERGl were chosen as the initial structure for the next step.

[00264] The HERGl -dofetilide complexes were embedded in a DPPC bilayer. The system was solvated in TIP3P water molecules with 150 mM KC1. All of the systems (4 complexes for charged/neutral dofetilide at open and open-inactivated states) were built and pre-equilibrated with the CHARMM program using CHARMM27 force field (see, e.g., Noskov et al., 2008, "Control of Ion Selectivity In LeuT: Two Na(+) Binding Sites with two Different Mechanisms," J. Mol. Biol., 377, 804-818). The topology and parameters of neutral and cationic dofetilide were generated by CHARMM generalized force fields (CGenFF) (Vanommeslaeghe et al., 2010, "CHARMM General Force Field: a Force Field for Drug- Like Molecules Compatible with the CHARMM All-Atom Additive Biological Force Fields," J. Comput. Chem. 31, 671-690). The systems were equilibrated for 10 ns using NAMD2.9 program package (Phillips et al., 2005, "Scalable Molecular Dynamics with NAMD," J.

Comput. Chem. , 26, 1781-1802). The NPaT ensemble was used for all simulations with pressure set to 1 atm and temperature to 310.15 K. Long-range electrostatic interactions were treated by the particle mesh Ewald (PME) algorithm (Essmann et al, 1995, J. Chem. Phys., 103, 8577-8593). Non-bonded interactions were switched off at 10-12 A. The systems were simulated with periodic orthorhombic boundary conditions applied in all directions with the time step of 2 fs. [00265] Energetics of dofetilide binding was estimated using umbrella sampling simulations to evaluate potential of mean force (PMF) for drug unbinding from the hERGl channel. Simulations were performed with harmonic biasing potentials with a force constant of 10 kcal/(mol A2) along the z-axis. The zero position along the z-axis was the center of mass of the Ca of residues 623-628 in the filter. The flat-bottom cylindrical constraints with radius of 10 A was used to cap lateral displacement of the bound drug. The reaction coordinate for each window was the distance along the z-axis between the center of mass of dofetilide and the zero position. The sampling windows were spaced every 0.5 A from -7.5 A to -49.5 A resulting in 85 windows for open hERG and from -8.5 A to -38.0 A resulting in 60 windows for open-inactivated hERG. The simulation time per window was set to 22 ns. The total simulation time was 1.87 and 1.32 for open and open-inactivated systems, respectively. The binding free energy profiles were rebuilt based on the last 20 ns/window with the use of Weighted Histogram Analysis Method (WHAM) (Kumar et al, 1992, "The Weighted Histogram Analysis Method for Free-Energy Calculations on Biomolecules.

1. The Method," J. Comput. Chem., 13, 1011-1021), and the tolerance for WHAM was set to 10"7 kcal/mol.

[00266] The computed PMFs for dofetilide binding to open and open-inactivated states display well-pronounced state- and charge-dependent properties.

[00267] For the neutral form of dofetilide (shown in FIGURE 4A), the computed

PMFs show two well-separated energy wells for the open state. This suggests that dofetilide has at least two binding sites in the intra-cavitary site of the open state channel. The energy wells for dofetilide binding to the open state are around -12 kcal/mol for the inner binding site and -13 kcal/mol for the outer binding site. In contrast, the computed PMFs for dofetilide binding to open-inactivated state display a flat basin between two binding sites and the energy wells are less than -10 kcal/mol in the cavity of open-inactivated hERGl .

[00268] The topologies of the binding pockets for the neutral form of dofetilide in the open and open-inactivated states are shown in FIGURE 4B. In the first binding site

(FIGURE 4B-a) of open hERGl, dofetilide is stabilized by multiple interactions with the apex of the pore helix (S621-S624) and with a cluster of residues from the distal S6 including S649, Y652 and F656. The second binding site for neutral dofetilide (FIGURE 4B-b) is located at the distal S6, where the ligand is primarily coordinated by the cluster of hydrophobic residues (Y562, A653 and F656) and polar residues (T623, S624 and S649). There are also multiple hydrogen bonds formed between the ethoxy- or methanesulfonamide- oxygens of dofetilide and S649 or water molecules. In the open-inactivated hERGl cavity, the binding site is located between Y652 and the filter. Both head groups are coordinated by S649 and water molecules (FIGURE 4B-a'). The outer binding site is at the gate and close to the hydrophobic residues Y652, F656 and 1655 (FIGURE 4B-b'). One arm of dofetilide points into the solvent.

[00269] The computed and measured pKa of dofetilide is estimated to be between 9.0 and 9.6, which suggests that a substantial fraction of molecules will be ionized at physiological pH. To study effects of ionization in silico, binding profiles for the cationic form of dofetilide to open and open-inactivated states of the channel were computed (FIGURE 5A). The open-inactivated state of the channel displays a high-affinity site for cationic dofetilide, while open channel has only marginal ability to stabilize the drug.

FIGURE 5 shows that open state of the hERGl channel displays only one low-affinity site for the cationic form of the blocker located around at z = -16 A. Dofetilide interacts with the hydrophobic residues A653, Y652, F656 and S660, the polar residues S624, T623, S649 and S660, and water molecules which are coordinated with two methanesulfonamide groups. (FIGURE 5B-b and FIGURE 5B-a).

[00270] The simulations run for open-inactivated state display a remarkable difference in the unbinding PMFs for cationic dofetilide. There is a well-defined high-affinity binding site located at Z = -10 A. As shown in FIGURE 5B-a', the drug binds close to a comer of two monomers. The drug is stabilized by strong hydrophobic and polar interactions with residues F652 from four monomers, S621-S624 from the bottom of the filter of one monomer, and T623, M645, S649, M651 and 1655. One head group is stabilized by a hydrogen bond with G648 and a water molecule, suggesting that the binding of cationic dofetilide may help to stabilize the open-inactivated state of hERGl. Besides the inner binding site, there is one more local minimum of energy profile located at z = -16 A

(FIGURE 5B-b'). Dofetilide is located among four Y652, four F656, one 1656 from the distal S6, and one T623 from the bottom of the filter. There is one hydrogen bond between the nitrogen of methanesulfonamide and Y652. Dofetilide also forms bifurcating hydrogen bonds with water molecules around the head groups.

[00271] The total equilibrium dissociation constant i¾(single) from PMF in presence of a cylindrical constraint was calculated using the following equation: {single) = nR2 (Zmax dz e-w^kBT * (10"9)3L

zmin /A3 * N mol (6) where R is the radius of the cylindrical restraint oriented normal to the z-axis and NA the Avogadro's number. The w(z) was offset to zero for dofetilide in the bulk phase.

[00272] The binding free energy was calculated using the following equation:

AG = RT ln^ (7)

[00273] As shown in TABLE 2, cationic dofetilide binding to the open-inactivated channel is most favored over all the other three systems with the binding free energy of -16.3 kcal/mol.

[00274] TABLE 2; Equilibrium Dissociation Constants and Gibbs Free Energies

Neutral Ligand Cationic Ligand

open open-inactivated open open-inactivated

KD (M) 1.32E-09 6.70E-08 1.32E-03 3.22E-12

AG (kcal/mol) -12.59 -10.18 -4.09 -16.30

[00275] In the present example, molecular simulations of dofetilide binding to models of the hERGl protein in its open and open-inactivated states were examined. Protonated dofetilide (-28.5 % at physiological pH) was found to exhibit strong preference for binding to open-inactivated state, highlighting the importance of this compound's charged ionization state as a blocker. Without being limited by any theory, preferential binding of the cationic dofetilide to the open-inactivated state of hERGl may stabilize this state to such an extent that the channel is trapped in its open-inactivated state, and passage of potassium ions is blocked. The atomistically detailed information provided in the present example may be used to chemically modify or redesign dofetilide such that it does not block the hERGl protein in any of its conformational states, including the open and open-inactivated states.

7 13 EXAMPLE 13; STATE-DEPENDENT BINDING OF A TEST

COMPOUND

[00276] State-dependent binding of a test compound is presented. As an example, computational dynamic models of ivabradine bound to hERGl in its open and closed states is presented. [00277] Ivabradine has recently been approved in Europe to treat patients with angina who have intolerance to beta blockers and/or heart failure. Ivabradine is considered to act specifically on the sinoatrial node by inhibiting the If current (the funny current) to slow automaticity. No episodes of Torsades de Pointes have been reported in randomized clinical studies. However, in vitro studies show that ivabradine prolongs phase 3 repolarization in ventricular tissue. In a recent publication, ivabradine was found to blocks the hERGl current over a range of concentrations overlapping with those required to block HCN4 (Lees-Miller et al, 2015, "Ivabradine Prolongs Phase 3 of Cardiac Repolarization and Blocks the hERGl (KCNH2) Current over a Concentration-Range Overlapping with that Required to Block HCN4," J. Mol. Cell. Cardiology, 85, 71-78). The atomistic details of this blockage are explored in the present example using the methods and systems disclosed herein.

[00278] Three-dimensional coordinates describing the hERGl protein in the open- and closed states were obtained by a combination of ROSETTA-membrane de-novo, homology modelling and MD simulations.

[00279] The Glide-XP (extra precision) docking program with two-tier docking approach was used as previously described (Durdagi et al., 2011, "Combined Receptor and Ligand-Based Approach to the Universal Pharmacophore Model Development for Studies of Drug Blockade to the hERGl Pore Domain," J. Chem. Inf. Model, 51, 463-74; Durdagi et al., 2012, "Modeling of Open, Closed, and Open-Inactivated States of the HERGl Channel: Structural Mechanisms of the State-Dependent Drug Binding," J Chem. Inf. Model, 52, 2760-2774). Clustering of docking poses was done with a docking score imposed by Epik- state penalty protocol (Greenwood et al, 2010, "Towards the Comprehensive, Rapid, and Accurate Prediction of the Favorable Tautomeric States of Drug-Like Molecules in Aqueous Solution," J. Comput. Aid. Mol. Des., 24, 591-604).

[00280] The neutral and cationic forms of ivabradine and corresponding tautomeric states were generated using LigPrep and the OPLS_2005 force field (Beckstein et al, 2014, "Prediction of Hydration Free Energies for the SAMPL4 Diverse Set of Compounds using Molecular Dynamics Simulations with the OPLS-AA Force Field," J. Comput. Aid. Mol. Des., 28, 265-276). All of the tautomers/ionization state were evaluated at pH=7.0.

[00281] The most populated clusters from docking studies were used to run MD simulations for hERG-ivabradine complexes embedded into lipid bilayers. The exact details of protocol were published previously (Durdagi et al, 2011, 2012). An equilibrated complex was subjected for equilibrium MD simulations of 50 ns long for each of the studied systems. The binding enthalpies for the drug were evaluated with MM/PBSA (Durdagi et al, 2014, "Rehabilitating Drug-Induced Long-QT Promoters: In-silico Design of hERG-neutral Cisapride Analogues with Retained Pharmacological Activity ," BMC Pharmacol. Toxicol, 15, 14) method. Briefly, electrostatic and vdW interactions were evaluated with an infinite cutoffs and the scaling factor for computations of vdW contributions to binding energy was set to 0.171 according to Erikkson and Roux work on toxin binding to ion channels (Eriksson et al, 2002, "Modeling the Structure of Agitoxin in Complex with the Shaker K+ Channel: a Computational Approach Based on Experimental Distance Restraints Extracted from

Thermodynamic Mutant Cycles," Biophys J., 83, 2595-609). The solvati on-related part of the binding energetics was estimated by solving Poisson-Boltzmann equation on the

201 x 201 x 201 A3 grid with 0.5 A spacing. A focusing method was used to obtain

electrostatic contributions to the solvation energies and the implicit membrane and protein/drug dielectric constant was set to 2.0. The solvent was represented by a continuum with dielectric constant of 80.

[00282] Umbrella sampling simulations for ivabradine partitioning into DPPC bilayer were performed using the protocol described previously (MacCallum et al, 2007,

"Partitioning of Amino Acid Side Chains into Lipid Bilayers: Results from Computer Simulations and Comparison to Experiment," J Gen. Physiol, 129, 371-7). Harmonic constraints of 5 kcal/(mol- A2) were applied to the reaction coordinate spanning 72 A. 72 windows spaced every 1 A were used to describe ivabradine transport along the channel and 5 seeding conformations per window. Five independent simulations per window were performed to sample better conformational dynamics of the ivabradine. Each window was equilibrated for 2.5 ns in presence of restraining potential and then subjected to a 7.5 ns production run, which was used for weighted histogram analysis (WHAM). The WHAM convergence tolerance was set to 0.0001 kcal/mol. The statistical uncertainties were estimated by separating the data into seven blocks and were found to be within ±1.5 kcal/mol.

[00283] Ivabradine was docked to an in silico hERG models representing open and closed states. The best-scored binding poses for neutral and cationic ivabradine binding to an intra-cavitary site in the open-state of hERGl are shown in FIGURE 6. The identified lipid- exposed binding site found in open and closed state of hERGl are shown in FIGURE 7. Docking scores to an intra-cavitary site in the open state of hERGl are -6.4 kcal/mol and -6.7 kcal/mol for neutral and ionized forms of ivabradine, respectively. The computed binding enthalpy for neutral and charged forms of ivabradine to an intra-cavitary sites were -16±4 kcal/mol and -14±5 kcal/mol, respectively. The key residues involved in the intra-cavity binding site for ivabradine are F656, Y652 and A653. The key residues important for stabilizing the polar groups in the drug are S624, T623 and S642.

[00284] The docking studies also mapped a well-defined binding site on the hERGl surface exposed to lipids. The results of MD simulations support that ivabradine is stable at the lipid-exposed pocket in hERGl (shown in FIGURE 7). The diffusion of the drug center of mass in 50 ns of equilibrium MD simulations is illustrated in FIGURE 7 along with metrics describing conformational dynamics of the bound drug. Using the approach described above, binding enthalpies for neutral ivabradine binding to lipid-facing site were calculated. The calculated binding enthalpy was -13±3 kcal/mol and -14±3 kcal/mol for site found in open and closed states, respectively.

[00285] The lipid exposed binding pocket is formed predominantly by F551, 1663,

M651 and L622 in the open state and by the side-chains of V644, L552 and F551 in the closed state. The binding in the closed state of the channel displays two possible drug orientations in the pocket.

[00286] In the present example, molecular simulations of ivabradine binding to models of the hERGl protein in its open and closed states were examined. The atomistically detailed information provided in the present example may be used to chemically modify or redesign ivabradine such that it does not block the hERGl protein in any of its conformational states, including the open and closed states.

7 14 EXAMPLE 14; COMPUTATIONS FOR COMPOUND SELECTION

[00287] FIGURE 8 depicts a grid computing environment for selecting a compound with reduced risk of cardiotoxicity. As shown in FIGURE 8, user computers 1302 can interact with the grid computing environment 1306 through a number of ways, such as over one or more networks 1304. The grid computing environment 1306 can assist users to select a compound with reduced risk of cardiotoxicity.

[00288] One or more data stores 1308 can store the data to be analyzed by the grid computing environment 1306 as well as any intermediate or final data generated by the grid computing environment. However in certain embodiments, the configuration of the grid computing environment 1306 allows its operations to be performed such that intermediate and final data results can be stored solely in volatile memory (e.g., RAM), without a requirement that intermediate or final data results be stored to non-volatile types of memory (e.g., disk).

[00289] This can be useful in certain situations, such as when the grid computing environment 1306 receives ad hoc queries from a user and when responses, which are generated by processing large amounts of data, need to be generated on-the-fly. In this non- limiting situation, the grid computing environment 1306 is configured to retain the processed information within the grid memory so that responses can be generated for the user at different levels of detail as well as allow a user to interactively query against this information.

[00290] For example, the grid computing environment 1306 receives structural information describing the structure of the ion channel protein, and performs a molecular dynamics simulation of the protein structure. Then, the grid computing environment 1306 uses a clustering algorithm to identify dominant conformations of the protein structure from the molecular dynamics simulation, and select the dominant conformations of the protein structure identified from the clustering algorithm. In addition, the grid computing environment 1306 receives structural information describing conformers of one or more compounds, and uses a docking algorithm to dock the conformers of the one or more compounds to the dominant conformations. The grid computing environment 1306 further identifies a plurality of preferred binding conformations for each of the combinations of protein and compound, and optimizes the preferred binding conformations using molecular dynamics simulations so as to determine whether the compound blocks the ion channel of the protein in the preferred binding conformations.

[00291] Specifically, in response to user inquires about cardiotoxicity of a compound, the grid computing environment 1306, without an OLAP or relational database environment being required, aggregates protein structural information and compound structural information from the data stores 1308. Then the grid computing environment 1306 uses the received protein structural information to perform molecular dynamics simulations for determining configurations of target protein flexibility (e.g., over a simulation length of greater than 50 ns). The molecular dynamics simulations involve the grid computing environment 1306 determining forces acting on an atom based upon an empirical force field that approximates intramolecular forces, where numerical integration is performed to update positions and velocities of atoms. The grid computing environment 1306 clusters molecular dynamic trajectories formed based upon the updated positions and velocities of the atoms into dominant conformations of the protein, and executes a docking algorithm that uses the compound's structural information in order to dock the compound's conformers to the dominant conformations of the protein. Based on information related to the docked compound's conformers, the grid computing environment 1306 identifies a plurality of preferred binding conformations for each of the combinations of protein and compound. If the compound does not block the ion channel of the protein in the preferred binding conformations, the grid computing environment 1306 predicts the compound has reduced risk of cardiotoxicity. Otherwise, the grid computing environment 1306 predicts the compound is cardiotoxic, and redesigns the compound in order to reduce risk of

cadiotoxicity.

[00292] FIGURE 9 illustrates hardware and software components for the grid computing environment 1306. As shown in FIGURE 9, the grid computing environment 1306 includes a central coordinator software component 1406 which operates on a root data processor 1404. The central coordinator 1406 of the grid computing environment 1306 communicates with a user computer 1402 and with node coordinator software components (1412, 1414) which execute on their own separate data processors (1408, 1410) contained within the grid computing environment 1306.

[00293] As an example of an implementation environment, the grid computing environment 1306 can comprise a number of blade servers, and a central coordinator 1406 and the node coordinators (1412, 1414) are associated with their own blade server. In other words, a central coordinator 1406 and the node coordinators (1412, 1414) execute on their own respective blade server. In some embodiments, each blade server contains multiple cores and a thread is associated with and executes on a core belonging to a node processor (e.g., node processor 1408). A network connects each blade server together.

[00294] The central coordinator 1406 comprises a node on the grid. For example, there might be 100 nodes, with only 50 nodes specified to be run as node coordinators. The grid computing environment 1306 will run the central coordinator 1406 as a 51st node, and selects the central coordinator node randomly from within the grid. Accordingly, the central coordinator 1406 has the same hardware configuration as a node coordinator.

[00295] The central coordinator 1406 may receive information and provide information to a user regarding queries that the user has submitted to the grid. The central coordinator 1406 is also responsible for communicating with the 50 node coordinator nodes, such as by sending those instructions on what to do as well as receiving and processing information from the node coordinators. In one implementation, the central coordinator 1406 is the central point of contact for the client with respect to the grid, and a user never directly communicates with any of the node coordinators.

[00296] With respect to data transfers involving the central coordinator 1406, the central coordinator 1406 communicates with the client (or another source) to obtain the input data to be processed. The central coordinator 1406 divides up the input data and sends the correct portion of the input data for routing to the node coordinators. The central coordinator 1406 also may generate random numbers for use by the node coordinators in simulation operations as well as aggregate any processing results from the node coordinators. The central coordinator 1406 manages the node coordinators, and each node coordinator manages the threads which execute on their respective machines.

[00297] A node coordinator allocates memory for the threads with which it is associated. Associated threads are those that are in the same physical blade server as the node coordinator. However, it should be understood that other configurations could be used, such as multiple node coordinators being in the same blade server to manage different threads which operate on the server. Similar to a node coordinator managing and controlling operations within a blade server, the central coordinator 1406 manages and controls operations within a chassis.

[00298] In certain embodiments, a node processor includes shared memory for use for a node coordinator and its threads. The grid computing environment 1306 is structured to conduct its operations (e.g., matrix operations, etc.) such that as many data transfers as possible occur within a blade server (i.e., between threads via shared memory on their node) versus performing data transfers between threads which operate on different blades. Such data transfers via shared memory are more efficient than a data transfer involving a connection with another blade server.

[00299] FIGURE 10 depicts example schematics of data structures utilized by a compound-selection system. Multiple data structures are stored in a data store 1500, including a protein-structural-information data structure 1502, a candidate-compound- structural-information data structure 1504, a binding-conformations data structure 1506, a molecular-dynamics-simulations data structure 1508, a dominant-conformations data structure 1510, a cluster data structure 1512, and a cardiotoxi city-analysis data structure 1514. These interrelated data structures can be part of the central coordinator 1406 by aggregating data from individual nodes. However, portions of these data structures can be distributed as needed, so that the individual nodes can store the process data. The data store 1500 can be different types of storage devices and programming constructs (e.g., RAM, ROM, Flash memory, flat files, databases, programming data structures, programming variables, IF-THEN (or similar type) statement constructs, etc.). For example, the data store 1500 can be a single relational database or can be databases residing on a server in a distributed network.

[00300] Specifically, the protein-structural-information data structure 1502 is configured to store data related to the structure of the hERGl ion channel protein, for example, special relationship data between different atoms. The data related to the structure of the potassium ion channel protein may be obtained from a homology model, an NMR solution structure, an X-ray crystal structure, a molecular model, etc. Molecular dynamics simulations can be performed on data stored in the protein-structural-information data structure 1502. For example, the molecular dynamics simulations involve solving the equation of motion according to the laws of physics, e.g., the chemical bonds within proteins being allowed to flex, rotate, bend, or vibrate. Information about the time dependence and magnitude of fluctuations in both positions and velocities of the given molecule/atoms is obtained from the molecular dynamics simulations. For example, data related to coordinates and velocities of molecules/atoms at equal time intervals or sampling intervals are obtained from the molecular dynamics simulations. Atomistic trajectory data (e.g., at different time slices) are formed based on the positions and velocities of molecules/atoms resulted from the molecular dynamics simulations and stored in the molecular-dynamics-simulations data structure 1508. The molecular dynamics simulations can be of any duration. In certain embodiments, the duration of the molecular dynamics simulation is greater than 50 ns, for example, preferably greater than 200 ns.

[00301] Data stored in the molecular-dynamics-simulations data structure 1508 are processed using a clustering algorithm, and associated cluster population data are stored in the cluster data structure 1512. Dominant conformations of the potassium ion channel protein are identified based at least in part on the data stored in the molecular-dynamics- simulations data structure 1508 and the associated cluster population data stored in the cluster data structure 1512. Atomistic trajectory data (e.g., at different time slices) related to the identified dominant conformations are stored in the dominant-conformations data structure 1510. [00302] Data stored in the candidate-compound-structure-information data structure

1504 are processed together with data related to the dominant conformations of the hERGl ion channel protein stored in the dominant-conformations data structure 1510. The conformers of the one or more compounds are docked to the dominant conformations of the structure of the potassium ion channel protein using a docking algorithm (e.g., DOCK, AutoDock, etc.), so that data related to various combinations of potassium ion channel protein and compound is determined and stored in the binding-conformations data structure 1506. For example, the compound is an antiviral agent (e.g., hepatitis C inhibitor). As an example, the binding-conformations data structure includes data related to binding energies. 2D information of the compound may be translated into a 3D representative structure to be stored in the candidate-compound-structure-information data structure 1504 for docking. Data stored in the binding-conformations data structure 1506 are processed using a clustering algorithm, and associated cluster population data are stored in the cluster data structure 1512. One or more preferred binding conformations are identified based at least in part on the data stored in the binding-conformations data structure 1506 and the associated cluster population data stored in the cluster data structure 1512. For example, the preferred binding

conformations include those with a largest cluster population and a lowest binding energy.

[00303] The identified preferred binding conformations are optimized using a scalable molecular dynamics simulations (e.g., through a NAMD software, etc.). In certain embodiments, binding energies are calculated (e.g., using salvation models, etc.) for each of the combinations of protein and compound (receptor and ligand) in the corresponding optimized preferred binding conformation(s). The calculated binding energies are output as the predicted binding energies for each of the combinations of protein and compound.

[00304] The cardiotoxicity-analysis data structure 1514 includes data related to a blocking degree of one or more compounds, e.g., in the preferred binding conformations. For example, the data stored in the cardiotoxicity-analysis data structure 1514 includes identification of blocking sites and non-blocking sites. The data stored in the cardiotoxicity- analysis data structure 1514 indicates a potential cardiac hazard when (i) a pocket within the hERGl channel is classified as a blocking site and (ii) a ligand fits within the pocket and is within a predetermined binding affinity level. The data stored in the cardiotoxicity-analysis data structure 1514 does not indicate a potential cardiac hazard when a ligand binds to a pocket within the hERGl channel that is classified as a non-blocking site. In some embodiments, if the compound does not block the ion channel (e.g., the blocking degree being lower than a threshold) in the preferred binding conformation(s), the compound is predicted to have reduced risk of cardiotoxicity, and the compound can be selected. In other embodiments, if the compound blocks the ion channel (e.g., the blocking degree being higher than the threshold) in the preferred binding conformation(s), the compound is predicted to be cardiotoxic. A molecular modeling algorithm can be used to chemically modify or redesign the compound so as to reduce the risk of cardiotoxicity (e.g., to reduce the blocking degree).

[00305] A system can be configured such that a compound-selection system 2102 can be provided on a stand-alone computer for access by a user 2104, such as shown at 2100 in FIGURE 11.

[00306] Additionally, the methods and systems described herein may be implemented on many different types of processing devices by program code comprising program instructions that are executable by the device processing subsystem. The software program instructions may include source code, object code, machine code, or any other stored data that is operable to cause a processing system to perform the methods and operations described herein. Other implementations may also be used, however, such as firmware or even appropriately designed hardware configured to carry out the methods and systems described herein.

[00307] The systems' and methods' data (e.g., associations, mappings, data input, data output, intermediate data results, final data results, etc.) may be stored and implemented in one or more different types of computer-implemented data stores, such as different types of storage devices and programming constructs (e.g., RAM, ROM, Flash memory, flat files, databases, programming data structures, programming variables, IF-THEN (or similar type) statement constructs, etc.). It is noted that data structures describe formats for use in organizing and storing data in databases, programs, memory, or other computer-readable media for use by a computer program.

[00308] The systems and methods may be provided on many different types of computer-readable media including computer storage mechanisms (e.g., CD-ROM, diskette, RAM, flash memory, computer's hard drive, etc.) that contain instructions (e.g., software) for use in execution by a processor to perform the methods' operations and implement the systems described herein.

[00309] The computer components, software modules, functions, data stores and data structures described herein may be connected directly or indirectly to each other in order to allow the flow of data needed for their operations. It is also noted that a module or processor includes but is not limited to a unit of code that performs a software operation, and can be implemented for example as a subroutine unit of code, or as a software function unit of code, or as an object (as in an object-oriented paradigm), or as an applet, or in a computer script language, or as another type of computer code. The software components and/or functionality may be located on a single computer or distributed across multiple computers depending upon the situation at hand.

[00310] The computing system can include clients and servers. A client and server are generally remote from each other and typically interact through a communication network. The relationship of client and server arises by virtue of computer programs running on the respective computers and having a client-server relationship to each other.

[00311] While this specification contains many specifics, these should not be construed as limitations on the scope or of what may be claimed, but rather as descriptions of features specific to particular embodiments. Certain features that are described in this specification in the context or separate embodiments can also be implemented in combination in a single embodiment. Conversely, various features that are described in the context of a single embodiment can also be implemented in multiple embodiments separately or in any suitable subcombination. Moreover, although features may be described above as acting in certain combinations and even initially claimed as such, one or more features from a claimed combination can in some cases be excised from the combination, and the claimed combination may be directed to a subcombination or variation of a subcombination.

[00312] Similarly, while operations are depicted in the drawings in a particular order, this should not be understood as requiring that such operations be performed in the particular order shown or in sequential order, or that all illustrated operations be performed, to achieve desirable results. In certain circumstances, multitasking and parallel processing may be advantageous. Moreover, the separation of various system components in the embodiments described above should not be understood as requiring such separation in all embodiments, and it should be understood that the described program components and systems can generally be integrated together in a single software product or packaged into multiple software products. [00313] Thus, particular embodiments have been described. Other embodiments are within the scope of the following claims. For example, the actions recited in the claims can be performed in a different order and still achieve desirable results.

[00314] All publications and patent applications cited in this specification are herein incorporated by reference as if each individual publication or patent application were specifically and individually indicated to be incorporated by reference. Although the foregoing has been described in some detail by way of illustration and example for purposes of clarity of understanding, it will be readily apparent to those of ordinary skill in the art in light of the teachings of the specification that certain changes and modifications may be made thereto without departing from the spirit or scope of the appended claims.

Table A

CRYSTl 0..000 0.000 0.000 90.00 90.00 9C1.00 p :1 1

ATOM 1 N MET X 554 2. .652 15 .587 -9. 600 0 .00 0. .00 PROA

ATOM 2 HT1 MET X 554 3 .683 15 .697 -9. 530 0 .00 0. .00 PROA

ATOM 3 HT2 MET X 554 2 .334 16 .577 -9. 579 0 .00 0. .00 PROA

ATOM 4 HT3 MET X 554 2 .415 15 .198 -10. 535 0 .00 0. .00 PROA

ATOM 5 CA MET X 554 2. .092 14 .680 -8. 545 0 .00 0. .00 PROA

ATOM 6 HA MET X 554 1. .022 14 .620 -8. 672 0 .00 0. .00 PROA

ATOM 7 CB MET X 554 2. .806 13 .292 -8. 581 0 .00 0. .00 PROA

ATOM 8 HB1 MET X 554 2 .699 12 .812 -9. 577 0 .00 0. .00 PROA

ATOM 9 HB2 MET X 554 3 .901 13 .419 -8. 449 0 .00 0. .00 PROA

ATOM 10 CG MET X 554 2. .323 12 .225 -7. 559 0 .00 0. .00 PROA

ATOM 11 HG1 MET X 554 1 .239 12 .047 -7. 726 0 .00 0. .00 PROA

ATOM 12 HG2 MET X 554 2 .771 11 .253 -7. 858 0 .00 0. .00 PROA

ATOM 13 SD MET X 554 2. .866 12 .318 -5. 865 0 .00 0. .00 PROA

ATOM 14 CE MET X 554 4. .492 11 .691 -6. 250 0 .00 0. .00 PROA

ATOM 15 HE1 MET X 554 4 .392 10 .785 -6. 884 0 .00 0. .00 PROA

ATOM 16 HE2 MET X 554 5 .185 12 .473 -6. 627 0 .00 0. .00 PROA

ATOM 17 HE3 MET X 554 4 .866 11 .298 -5. 280 0 .00 0. .00 PROA

ATOM 18 C MET X 554 2. .281 15 .386 -7. 213 0 .00 0. .00 PROA

ATOM 19 O MET X 554 1. .328 15 .847 -6. 563 0 .00 0. .00 PROA

ATOM 20 N CYS X 555 3. .549 15 .566 -6. 749 0 .00 0. .00 PROA

ATOM 21 HN CYS X 555 4. .410 15 .472 -7. 243 0 .00 0. .00 PROA

ATOM 22 CA CYS X 555 3. .706 16 .183 -5. 462 0 .00 0. .00 PROA

ATOM 23 HA CYS X 555 3. .211 15 .576 -4. 719 0 .00 0. .00 PROA

ATOM 24 CB CYS X 555 5. .228 16 .189 -5. 021 0 .00 0. .00 PROA

ATOM 25 HB1 CYS X 555 5 .234 16 .409 -3. 932 0 .00 0. .00 PROA

ATOM 26 HB2 CYS X 555 5 .542 15 .130 -5. 145 0 .00 0. .00 PROA

ATOM 27 SG CYS X 555 6. .331 17 .139 -6. 059 0 .00 0. .00 PROA

ATOM 28 HG1 CYS X 555 6 .780 16 .116 -6. 771 0 .00 0. .00 PROA

ATOM 29 C CYS X 555 3. .154 17 .538 -5. 248 0 .00 0. .00 PROA

ATOM 30 O CYS X 555 2. .515 17 .731 -4. 213 0 .00 0. .00 PROA

ATOM 31 N THR X 556 3. .268 18 .585 -6. 154 0 .00 0. .00 PROA

ATOM 32 HN THR X 556 3. .850 18 .417 -6. 946 0 .00 0. .00 PROA

ATOM 33 CA THR X 556 2. .561 19 .888 -6. 082 0 .00 0. .00 PROA

ATOM 34 HA THR X 556 2. .724 20 .301 -5. 098 0 .00 0. .00 PROA

ATOM 35 CB THR X 556 3. .209 20 .853 -7. 022 0 .00 0. .00 PROA

ATOM 36 HB THR X 556 2. .755 21 .865 -6. 964 0 .00 0. .00 PROA

ATOM 37 OG1 THR X 556 3 .098 20 .469 -8. 430 0 .00 0. .00 PROA

ATOM 38 HG1 THR X 556 3 .155 21 .233 -9. 009 0 .00 0. .00 PROA

ATOM 39 CG2 THR X 556 4 .696 20 .980 -6. 747 0 .00 0. .00 PROA

ATOM 40 HG21 THR X 556 4 .846 21 .202 -5. 669 0 .00 0. .00 PROA

ATOM 41 HG22 THR X 556 5 .223 20 .012 -6. 892 0 .00 0. .00 PROA

ATOM 42 HG23 THR X 556 5 .333 21 .610 -7. 404 0 .00 0. .00 PROA

ATOM 43 C THR X 556 1. .054 19 .838 -6. 081 0 .00 0. .00 PROA

ATOM 44 O THR X 556 0. .441 20 .506 -5. 264 0 .00 0. .00 PROA

ATOM 45 N PHE X 557 0. .395 18 .997 -6. 919 0 .00 0. .00 PROA

ATOM 46 HN PHE X 557 0. .868 18 .379 -7. 542 0 .00 0. .00 PROA

ATOM 47 CA PHE X 557 -1 .076 18 .815 -6. 894 0 .00 0. .00 PROA

ATOM 48 HA PHE X 557 -1 .482 19 .814 -6. 830 0 .00 0. .00 PROA

ATOM 49 CB PHE X 557 -1 .545 17 .987 -8. 114 0 .00 0. .00 PROA

ATOM 50 HB1 PHE X 557 -1 .306 18 .459 -9. 090 0 .00 0. .00 PROA

ATOM 51 HB2 PHE X 557 -1 .194 16 .934 -8. 160 0 .00 0. .00 PROA

ATOM 52 CG PHE X 557 -3 .040 17 .867 -8. 149 0 .00 0. .00 PROA

ATOM 53 CD1 PHE X 557 -3 .613 16 .560 -8. 076 0 .00 0. .00 PROA

ATOM 54 HD1 PHE X 557 -3 .039 15 .662 -7. 903 0 .00 0. .00 PROA

ATOM 55 CE1 PHE X 557 -5 .041 16 .372 -8. 250 0 .00 0. .00 PROA

ATOM 56 HE1 PHE X 557 -5 .304 15 .334 -8. 112 0 .00 0. .00 PROA

ATOM 57 CZ PHE X 557 -5 .891 17 .451 -8. 434 0 .00 0. .00 PROA

ATOM 58 HZ PHE X 557 -6 .967 17 .422 -8. 353 0 .00 0. .00 PROA

ATOM 59 CD2 PHE X 557 -4 .007 18 .888 -8. 382 0 .00 0. .00 PROA

ATOM 60 HD2 PHE X 557 -3 .639 19 .901 -8. 315 0 .00 0. .00 PROA

ATOM 61 CE2 PHE X 557 -5 .365 18 .660 -8. 559 0 .00 0. .00 PROA

ATOM 62 HE2 PHE X 557 -5 .960 19 .528 -8. 803 0 .00 0. .00 PROA

ATOM 63 C PHE X 557 -1 .598 18 .281 -5. 611 0 .00 0. .00 PROA

ATOM 64 O PHE X 557 -2 .619 18 .728 -5. 090 0 .00 0. .00 PROA

ATOM 65 N ALA X 558 -0 .859 17 .281 -5. 019 0 .00 0. .00 PROA ATOM 66 HN ALA X 558 0..024 17.001 -5..386 0..00 0..00 PROA

ATOM 67 CA ALA X 558 -1 .264 16 .563 -3. .812 0. .00 0. .00 PROA

ATOM 68 HA ALA X 558 -2 .287 16 .238 -3. .932 0. .00 0. .00 PROA

ATOM 69 CB ALA X 558 -0 .434 15 .343 -3. .652 0. .00 0. .00 PROA

ATOM 70 HB1 ALA X 558 -0 .770 14 .607 -2. .890 0. .00 0. .00 PROA

ATOM 71 HB2 ALA X 558 -0 .344 14 .752 -4. .589 0. .00 0. .00 PROA

ATOM 72 HB3 ALA X 558 0 .633 15 .598 -3. .478 0. .00 0. .00 PROA

ATOM 73 C ALA X 558 -1 .413 17 .433 -2. .592 0. .00 0. .00 PROA

ATOM 74 O ALA X 558 -2 .440 17 .432 -1. .884 0. .00 0. .00 PROA

ATOM 75 N LEU X 559 -0 .357 18 .236 -2. .287 0. .00 0. .00 PROA

ATOM 76 HN LEU X 559 0. .476 18 .203 -2. .833 0. .00 0. .00 PROA

ATOM 77 CA LEU X 559 -0 .362 19 .221 -1. .204 0. .00 0. .00 PROA

ATOM 78 HA LEU X 559 -0 .240 18 .654 -0. .293 0. .00 0. .00 PROA

ATOM 79 CB LEU X 559 0. .932 20 .083 -1. .248 0. .00 0. .00 PROA

ATOM 80 HB1 LEU X 559 1 .705 19 .288 -1. .317 0. .00 0. .00 PROA

ATOM 81 HB2 LEU X 559 1 .018 20 .580 -2. .239 0. .00 0. .00 PROA

ATOM 82 CG LEU X 559 1. .273 21 .008 -0. .062 0. .00 0. .00 PROA

ATOM 83 HG LEU X 559 0. .369 21 .621 0. .141 0. .00 0. .00 PROA

ATOM 84 CD1 LEU X 559 1 .337 20 .399 1. .361 0. .00 0. .00 PROA

ATOM 85 HD11 LEU X 559 1 .735 20 .996 2. .209 0. .00 0. .00 PROA

ATOM 86 HD12 LEU X 559 0 .320 20 .160 1. .739 0. .00 0. .00 PROA

ATOM 87 HD13 LEU X 559 1 .926 19 .463 1. .254 0. .00 0. .00 PROA

ATOM 88 CD2 LEU X 559 2 .570 21 .844 -0. .357 0. .00 0. .00 PROA

ATOM 89 HD21 LEU X 559 2 .357 22 .547 -1. .190 0. .00 0. .00 PROA

ATOM 90 HD22 LEU X 559 2 .836 22 .425 0. .552 0. .00 0. .00 PROA

ATOM 91 HD23 LEU X 559 3 .481 21 .235 -0. .540 0. .00 0. .00 PROA

ATOM 92 C LEU X 559 -1 .631 20 .141 -1. .088 0. .00 0. .00 PROA

ATOM 93 O LEU X 559 -2 .029 20 .443 -0. .021 0. .00 0. .00 PROA

ATOM 94 N ILE X 560 -2 .232 20 .592 -2. .225 0. .00 0. .00 PROA

ATOM 95 HN ILE X 560 -1 .755 20 .309 -3. .054 0. .00 0. .00 PROA

ATOM 96 CA ILE X 560 -3 .450 21 .411 -2. .207 0. .00 0. .00 PROA

ATOM 97 HA ILE X 560 -3 .364 22 .263 -1. .549 0. .00 0. .00 PROA

ATOM 98 CB ILE X 560 -3 .726 21 .884 -3. .644 0. .00 0. .00 PROA

ATOM 99 HB ILE X 560 -3 .762 20 .967 -4. .271 0. .00 0. .00 PROA

ATOM 100 CG2 ILE X 560 -5 .004 22 .811 -3. .710 0. .00 0. .00 PROA

ATOM 101 HG21 ILE X 560 -5 .225 23 .203 -4. .726 0. .00 0. .00 PROA

ATOM 102 HG22 ILE X 560 -5 .896 22 .228 -3. .396 0. .00 0. .00 PROA

ATOM 103 HG23 ILE X 560 -4 .747 23 .770 -3. .212 0. .00 0. .00 PROA

ATOM 104 CGI ILE X 560 -2 .464 22 .688 -4. .163 0. .00 0. .00 PROA

ATOM 105 HG11 ILE X 560 -2 .320 23 .602 -3. .548 0. .00 0. .00 PROA

ATOM 106 HG12 ILE X 560 -1 .486 22 .182 -4. .018 0. .00 0. .00 PROA

ATOM 107 CD ILE X 560 -2 .675 23 .173 -5. .629 0. .00 0. .00 PROA

ATOM 108 HD1 ILE X 560 -2 .963 22 .251 -6. .177 0. .00 0. .00 PROA

ATOM 109 HD2 ILE X 560 -3 .469 23 .950 -5. .655 0. .00 0. .00 PROA

ATOM 110 HD3 ILE X 560 -1 .722 23 .561 -6. .047 0. .00 0. .00 PROA

ATOM 111 C ILE X 560 -4 .596 20 .683 -1. .732 0. .00 0. .00 PROA

ATOM 112 O ILE X 560 -5 .364 21 .224 -0. .944 0. .00 0. .00 PROA

ATOM 113 N ALA X 561 -4 .793 19 .412 -2. .142 0. .00 0. .00 PROA

ATOM 114 HN ALA X 561 -4 .195 19 .000 -2. .825 0. .00 0. .00 PROA

ATOM 115 CA ALA X 561 -5 .844 18 .574 -1. .590 0. .00 0. .00 PROA

ATOM 116 HA ALA X 561 -6 .760 19 .141 -1. .669 0. .00 0. .00 PROA

ATOM 117 CB ALA X 561 -5 .822 17 .271 -2. .385 0. .00 0. .00 PROA

ATOM 118 HB1 ALA X 561 -4 .793 16 .878 -2. .529 0. .00 0. .00 PROA

ATOM 119 HB2 ALA X 561 -6 .307 16 .467 -1. .791 0. .00 0. .00 PROA

ATOM 120 HB3 ALA X 561 -6 .243 17 .309 -3. .412 0. .00 0. .00 PROA

ATOM 121 C ALA X 561 -5 .625 18 .261 -0. .159 0. .00 0. .00 PROA

ATOM 122 O ALA X 561 -6 .541 18 .360 0. .605 0. .00 0. .00 PROA

ATOM 123 N HSD X 562 -4 .329 17 .950 0. .154 0. .00 0. .00 PROA

ATOM 124 HN HSD X 562 -3 .627 18 .001 -0. .552 0. .00 0. .00 PROA

ATOM 125 CA HSD X 562 -3 .959 17 .606 1. .551 0. .00 0. .00 PROA

ATOM 126 HA HSD X 562 -4 .542 16 .743 1. .838 0. .00 0. .00 PROA

ATOM 127 CB HSD X 562 -2 .495 17 .287 1. .678 0. .00 0. .00 PROA

ATOM 128 HB1 HSD X 562 -1 .955 17 .818 0. .866 0. .00 0. .00 PROA

ATOM 129 HB2 HSD X 562 -2 .140 17 .334 2. .730 0. .00 0. .00 PROA

ATOM 130 ND1 HSD X 562 -2 .064 15 .260 0. .221 0. .00 0. .00 PROA

ATOM 131 HD1 HSD X 562 -2 .276 15 .661 -0. .670 0. .00 0. .00 PROA ATOM 132 CG HSD X 562 -1.999 15.848 1..411 0..00 0..00 PROA

ATOM 133 CE1 HSD X 562 -1 .645 13 .998 0. .401 0. .00 0. .00 PROA

ATOM 134 HE1 HSD X 562 -1 .563 13 .214 -0. .353 0. .00 0. .00 PROA

ATOM 135 NE2 HSD X 562 -1 .235 13 .772 1. .639 0. .00 0. .00 PROA

ATOM 136 CD2 HSD X 562 -1 .538 14 .947 2. .317 0. .00 0. .00 PROA

ATOM 137 HD2 HSD X 562 -1 .203 15 .188 3. .318 0. .00 0. .00 PROA

ATOM 138 C HSD X 562 -4 .423 18 .712 2. .538 0. .00 0. .00 PROA

ATOM 139 O HSD X 562 -4 .879 18 .417 3. .628 0. .00 0. .00 PROA

ATOM 140 N TRP X 563 -4 .232 20 .033 2. .156 0. .00 0. .00 PROA

ATOM 141 HN TRP X 563 -3 .758 20 .334 1. .333 0. .00 0. .00 PROA

ATOM 142 CA TRP X 563 -4 .829 21 .077 3. .006 0. .00 0. .00 PROA

ATOM 143 HA TRP X 563 -4 .501 21 .006 4. .033 0. .00 0. .00 PROA

ATOM 144 CB TRP X 563 -4 .146 22 .421 2. .639 0. .00 0. .00 PROA

ATOM 145 HB1 TRP X 563 -4 .295 22 .449 1. .539 0. .00 0. .00 PROA

ATOM 146 HB2 TRP X 563 -4 .711 23 .319 2. .970 0. .00 0. .00 PROA

ATOM 147 CG TRP X 563 -2 .745 22 .657 2. .956 0. .00 0. .00 PROA

ATOM 148 CD1 TRP X 563 -1 .742 22 .777 2. .040 0. .00 0. .00 PROA

ATOM 149 HD1 TRP X 563 -1 .918 22 .836 0. .977 0. .00 0. .00 PROA

ATOM 150 NE1 TRP X 563 -0 .501 22 .921 2. .748 0. .00 0. .00 PROA

ATOM 151 HE1 TRP X 563 0 .366 22 .978 2. .304 0. .00 0. .00 PROA

ATOM 152 CE2 TRP X 563 -0 .804 22 .789 4. .098 0. .00 0. .00 PROA

ATOM 153 CD2 TRP X 563 -2 .211 22 .702 4. .263 0. .00 0. .00 PROA

ATOM 154 CE3 TRP X 563 -2 .806 22 .462 5. .507 0. .00 0. .00 PROA

ATOM 155 HE3 TRP X 563 -3 .880 22 .380 5. .587 0. .00 0. .00 PROA

ATOM 156 CZ3 TRP X 563 -1 .925 22 .400 6. .616 0. .00 0. .00 PROA

ATOM 157 HZ3 TRP X 563 -2 .478 22 .498 7. .539 0. .00 0. .00 PROA

ATOM 158 CZ2 TRP X 563 0 .029 22 .756 5. .200 0. .00 0. .00 PROA

ATOM 159 HZ2 TRP X 563 1 .102 22 .845 5. .123 0. .00 0. .00 PROA

ATOM 160 CH2 TRP X 563 -0 .529 22 .552 6. .465 0. .00 0. .00 PROA

ATOM 161 HH2 TRP X 563 0 .059 22 .641 7. .366 0. .00 0. .00 PROA

ATOM 162 C TRP X 563 -6 .293 21 .142 3. .152 0. .00 0. .00 PROA

ATOM 163 O TRP X 563 -6 .781 21 .416 4. .222 0. .00 0. .00 PROA

ATOM 164 N LEU X 564 -7 .033 20 .942 1. .990 0. .00 0. .00 PROA

ATOM 165 HN LEU X 564 -6 .694 21 . Ill 1. .067 0. .00 0. .00 PROA

ATOM 166 CA LEU X 564 -8 .473 20 .623 2. .035 0. .00 0. .00 PROA

ATOM 167 HA LEU X 564 -8 .981 21 .537 2. .304 0. .00 0. .00 PROA

ATOM 168 CB LEU X 564 -9 .127 20 .321 0. .599 0. .00 0. .00 PROA

ATOM 169 HB1 LEU X 564 -8 .569 19 .412 0. .287 0. .00 0. .00 PROA

ATOM 170 HB2 LEU X 564 -10 .215 20 .217 0. .797 0. .00 0. .00 PROA

ATOM 171 CG LEU X 564 -8 .936 21 .391 -0. .468 0. .00 0. .00 PROA

ATOM 172 HG LEU X 564 -7 .845 21 .504 -0. .642 0. .00 0. .00 PROA

ATOM 173 CD1 LEU X 564 -9 .436 21 .061 -1. .839 0. .00 0. .00 PROA

ATOM 174 HD11 LEU X 564 -9 .100 20 .069 -2. .211 0. .00 0. .00 PROA

ATOM 175 HD12 LEU X 564 -10 .546 21 .004 -1. .821 0. .00 0. .00 PROA

ATOM 176 HD13 LEU X 564 -9 .095 21 .800 -2. .594 0. .00 0. .00 PROA

ATOM 177 CD2 LEU X 564 -9 .402 22 .794 -0. .046 0. .00 0. .00 PROA

ATOM 178 HD21 LEU X 564 -9 .224 23 .451 -0. .925 0. .00 0. .00 PROA

ATOM 179 HD22 LEU X 564 -10 .476 22 .757 0. .234 0. .00 0. .00 PROA

ATOM 180 HD23 LEU X 564 -8 .931 23 .262 0. .845 0. .00 0. .00 PROA

ATOM 181 C LEU X 564 -8 .791 19 .405 2. .958 0. .00 0. .00 PROA

ATOM 182 O LEU X 564 -9 .845 19 .388 3. .588 0. .00 0. .00 PROA

ATOM 183 N ALA X 565 -8 .001 18 .364 2. .987 0. .00 0. .00 PROA

ATOM 184 HN ALA X 565 -7 .190 18 .475 2. .418 0. .00 0. .00 PROA

ATOM 185 CA ALA X 565 -8 .297 17 .239 3. .869 0. .00 0. .00 PROA

ATOM 186 HA ALA X 565 -9 .335 16 .961 3. .761 0. .00 0. .00 PROA

ATOM 187 CB ALA X 565 -7 .616 15 .926 3. .435 0. .00 0. .00 PROA

ATOM 188 HB1 ALA X 565 -7 .820 15 .691 2. .369 0. .00 0. .00 PROA

ATOM 189 HB2 ALA X 565 -6 .532 16 .032 3. .656 0. .00 0. .00 PROA

ATOM 190 HB3 ALA X 565 -8 .005 15 .077 4. .036 0. .00 0. .00 PROA

ATOM 191 C ALA X 565 -8 .182 17 .508 5. .385 0. .00 0. .00 PROA

ATOM 192 O ALA X 565 -8 .925 16 .981 6. .190 0. .00 0. .00 PROA

ATOM 193 N CYS X 566 -7 .173 18 .306 5. .731 0. .00 0. .00 PROA

ATOM 194 HN CYS X 566 -6 .615 18 .695 5. .002 0. .00 0. .00 PROA

ATOM 195 CA CYS X 566 -6 .758 18 .700 7. .073 0. .00 0. .00 PROA

ATOM 196 HA CYS X 566 -6 .606 17 .762 7. .586 0. .00 0. .00 PROA

ATOM 197 CB CYS X 566 -5 .432 19 .556 7. .063 0. .00 0. .00 PROA ATOM 198 HB1 CYS X 566 -5.620 20.357 6..317 0..00 0..00 PROA

ATOM 199 HB2 CYS X 566 -5 .274 19 .987 8. .075 0. .00 0. .00 PROA

ATOM 200 SG CYS X 566 -3 .963 18 .552 6. .828 0. .00 0. .00 PROA

ATOM 201 HG1 CYS X 566 -4 .522 17 .671 6. .011 0. .00 0. .00 PROA

ATOM 202 C CYS X 566 -7 .804 19 .549 7. .858 0. .00 0. .00 PROA

ATOM 203 O CYS X 566 -7 .862 19 .335 9. .057 0. .00 0. .00 PROA

ATOM 204 N ILE X 567 -8 .653 20 .329 7. .252 0. .00 0. .00 PROA

ATOM 205 HN ILE X 567 -8 .498 20 .465 6. .276 0. .00 0. .00 PROA

ATOM 206 CA ILE X 567 -9 .684 21 .086 7. .847 0. .00 0. .00 PROA

ATOM 207 HA ILE X 567 -9 .354 21 .661 8. .699 0. .00 0. .00 PROA

ATOM 208 CB ILE X 567 -10 .105 22 .141 6. .879 0. .00 0. .00 PROA

ATOM 209 HB ILE X 567 -10 .933 22 .755 7. .294 0. .00 0. .00 PROA

ATOM 210 CG2 ILE X 567 -8 .838 23 .076 6. .632 0. .00 0. .00 PROA

ATOM 211 HG21 ILE X 567 -8 .457 23 .298 7. .652 0. .00 0. .00 PROA

ATOM 212 HG22 ILE X 567 -8 .014 22 .501 6. .160 0. .00 0. .00 PROA

ATOM 213 HG23 ILE X 567 -9 .056 23 .989 6. .039 0. .00 0. .00 PROA

ATOM 214 CGI ILE X 567 -10 .695 21 .485 5. .602 0. .00 0. .00 PROA

ATOM 215 HG11 ILE X 567 -9 .869 20 .887 5. .161 0. .00 0. .00 PROA

ATOM 216 HG12 ILE X 567 -11 .486 20 .735 5. .818 0. .00 0. .00 PROA

ATOM 217 CD ILE X 567 -11 .213 22 .378 4. .439 0. .00 0. .00 PROA

ATOM 218 HD1 ILE X 567 -10 .316 22 .675 3. .854 0. .00 0. .00 PROA

ATOM 219 HD2 ILE X 567 -12 .019 22 .068 3. .739 0. .00 0. .00 PROA

ATOM 220 HD3 ILE X 567 -11 .569 23 .301 4. .943 0. .00 0. .00 PROA

ATOM 221 C ILE X 567 -10 .850 20 .302 8. .474 0. .00 0. .00 PROA

ATOM 222 O ILE X 567 -11 .384 20 .636 9. .532 0. .00 0. .00 PROA

ATOM 223 N TRP X 568 -11 .189 19 .175 7. .891 0. .00 0. .00 PROA

ATOM 224 HN TRP X 568 -10 .853 18 .936 6. .983 0. .00 0. .00 PROA

ATOM 225 CA TRP X 568 -12 .201 18 .292 8. .538 0. .00 0. .00 PROA

ATOM 226 HA TRP X 568 -12 .916 18 .890 9. .082 0. .00 0. .00 PROA

ATOM 227 CB TRP X 568 -12 .920 17 .332 7. .545 0. .00 0. .00 PROA

ATOM 228 HB1 TRP X 568 -12 .159 16 .778 6. .954 0. .00 0. .00 PROA

ATOM 229 HB2 TRP X 568 -13 .508 16 .727 8. .267 0. .00 0. .00 PROA

ATOM 230 CG TRP X 568 -13 .975 17 .916 6. .680 0. .00 0. .00 PROA

ATOM 231 CD1 TRP X 568 -15 .144 18 .441 7. .207 0. .00 0. .00 PROA

ATOM 232 HD1 TRP X 568 -15 .640 18 .181 8. .131 0. .00 0. .00 PROA

ATOM 233 NE1 TRP X 568 -15 .760 19 .162 6. .223 0. .00 0. .00 PROA

ATOM 234 HE1 TRP X 568 -16 .561 19 .719 6. .230 0. .00 0. .00 PROA

ATOM 235 CE2 TRP X 568 -14 .935 19 .328 5. .163 0. .00 0. .00 PROA

ATOM 236 CD2 TRP X 568 -13 .892 18 .394 5. .328 0. .00 0. .00 PROA

ATOM 237 CE3 TRP X 568 -12 .917 18 .198 4. .388 0. .00 0. .00 PROA

ATOM 238 HE3 TRP X 568 -12 .116 17 .480 4. .492 0. .00 0. .00 PROA

ATOM 239 CZ3 TRP X 568 -13 .141 18 .820 3. .185 0. .00 0. .00 PROA

ATOM 240 HZ3 TRP X 568 -12 .400 18 .648 2. .419 0. .00 0. .00 PROA

ATOM 241 CZ2 TRP X 568 -15 .142 20 .003 3. .998 0. .00 0. .00 PROA

ATOM 242 HZ2 TRP X 568 -16 .045 20 .583 3. .878 0. .00 0. .00 PROA

ATOM 243 CH2 TRP X 568 -14 .203 19 .720 2. .953 0. .00 0. .00 PROA

ATOM 244 HH2 TRP X 568 -14 .555 19 .989 1. .968 0. .00 0. .00 PROA

ATOM 245 C TRP X 568 -11 .553 17 .467 9. .621 0. .00 0. .00 PROA

ATOM 246 O TRP X 568 -12 .270 16 .985 10. .509 0. .00 0. .00 PROA

ATOM 247 N TYR X 569 -10 .200 17 .312 9. .654 0. .00 0. .00 PROA

ATOM 248 HN TYR X 569 -9 .681 17 .756 8. .927 0. .00 0. .00 PROA

ATOM 249 CA TYR X 569 -9 .496 16 .609 10. .761 0. .00 0. .00 PROA

ATOM 250 HA TYR X 569 -10 .136 15 .799 11. .080 0. .00 0. .00 PROA

ATOM 251 CB TYR X 569 -8 .199 16 .079 10. .233 0. .00 0. .00 PROA

ATOM 252 HB1 TYR X 569 -7 .703 16 .872 9. .634 0. .00 0. .00 PROA

ATOM 253 HB2 TYR X 569 -7 .500 15 .885 11. .074 0. .00 0. .00 PROA

ATOM 254 CG TYR X 569 -8 .401 14 .798 9. .488 0. .00 0. .00 PROA

ATOM 255 CD1 TYR X 569 -9 .053 13 .733 10. .123 0. .00 0. .00 PROA

ATOM 256 HD1 TYR X 569 -9 .457 13 .812 11. .121 0. .00 0. .00 PROA

ATOM 257 CE1 TYR X 569 -9 .190 12 .505 9. .497 0. .00 0. .00 PROA

ATOM 258 HE1 TYR X 569 -9 .831 11 .770 9. .961 0. .00 0. .00 PROA

ATOM 259 CZ TYR X 569 -8 .562 12 .285 8. .303 0. .00 0. .00 PROA

ATOM 260 OH TYR X 569 -8 .783 11 .107 7. .688 0. .00 0. .00 PROA

ATOM 261 HH TYR X 569 -9 .505 10 .607 8. .076 0. .00 0. .00 PROA

ATOM 262 CD2 TYR X 569 -7 .692 14 .495 8. .260 0. .00 0. .00 PROA

ATOM 263 HD2 TYR X 569 -6 .981 15 .191 7. .839 0. .00 0. .00 PROA ATOM 264 CE2 TYR X 569 -7.812 13.278 7..651 0..00 0..00 PROA

ATOM 265 HE2 TYR X 569 -7 .318 13 .040 6. .721 0. .00 0. .00 PROA

ATOM 266 C TYR X 569 -9 .275 17 .523 11. .897 0. .00 0. .00 PROA

ATOM 267 O TYR X 569 -9 .363 17 .128 13. .043 0. .00 0. .00 PROA

ATOM 268 N ALA X 570 -9 .017 18 .817 11. .650 0. .00 0. .00 PROA

ATOM 269 HN ALA X 570 -8 .810 18 .977 10. .688 0. .00 0. .00 PROA

ATOM 270 CA ALA X 570 -8 .791 19 .825 12. .634 0. .00 0. .00 PROA

ATOM 271 HA ALA X 570 -8 .098 19 .434 13. .365 0. .00 0. .00 PROA

ATOM 272 CB ALA X 570 -8 .162 21 .070 11. .840 0. .00 0. .00 PROA

ATOM 273 HB1 ALA X 570 -7 .162 20 .873 11. .398 0. .00 0. .00 PROA

ATOM 274 HB2 ALA X 570 -8 .873 21 .301 11. .018 0. .00 0. .00 PROA

ATOM 275 HB3 ALA X 570 -8 .055 21 .936 12. .528 0. .00 0. .00 PROA

ATOM 276 C ALA X 570 -10 .162 20 .175 13. .341 0. .00 0. .00 PROA

ATOM 277 O ALA X 570 -10 .281 20 .235 14. .560 0. .00 0. .00 PROA

ATOM 278 N ILE X 571 -11 .298 20 .441 12. .559 0. .00 0. .00 PROA

ATOM 279 HN ILE X 571 -11 .266 20 .258 11. .579 0. .00 0. .00 PROA

ATOM 280 CA ILE X 571 -12 .529 21 .075 13. .085 0. .00 0. .00 PROA

ATOM 281 HA ILE X 571 -12 .215 22 .083 13. .313 0. .00 0. .00 PROA

ATOM 282 CB ILE X 571 -13 .639 21 .289 12. .050 0. .00 0. .00 PROA

ATOM 283 HB ILE X 571 -13 .192 21 .799 11. .171 0. .00 0. .00 PROA

ATOM 284 CG2 ILE X 571 -14 .044 19 .871 11. .502 0. .00 0. .00 PROA

ATOM 285 HG21 ILE X 571 -14 .247 19 .216 12. .376 0. .00 0. .00 PROA

ATOM 286 HG22 ILE X 571 -14 .969 19 .756 10. .897 0. .00 0. .00 PROA

ATOM 287 HG23 ILE X 571 -13 .271 19 .283 10. .962 0. .00 0. .00 PROA

ATOM 288 CGI ILE X 571 -14 .859 22 .177 12. .460 0. .00 0. .00 PROA

ATOM 289 HG11 ILE X 571 -15 .724 21 .936 11. .806 0. .00 0. .00 PROA

ATOM 290 HG12 ILE X 571 -15 .270 21 .934 13. .463 0. .00 0. .00 PROA

ATOM 291 CD ILE X 571 -14 .579 23 .715 12. .440 0. .00 0. .00 PROA

ATOM 292 HD1 ILE X 571 -13 .964 23 .931 13. .339 0. .00 0. .00 PROA

ATOM 293 HD2 ILE X 571 -14 .110 23 .987 11. .470 0. .00 0. .00 PROA

ATOM 294 HD3 ILE X 571 -15 .481 24 .346 12. .589 0. .00 0. .00 PROA

ATOM 295 C ILE X 571 -13 .065 20 .666 14. .471 0. .00 0. .00 PROA

ATOM 296 O ILE X 571 -13 .222 21 .403 15. .427 0. .00 0. .00 PROA

ATOM 297 N GLY X 572 -13 .249 19 .336 14. .663 0. .00 0. .00 PROA

ATOM 298 HN GLY X 572 -12 .858 18 .750 13. .958 0. .00 0. .00 PROA

ATOM 299 CA GLY X 572 -13 .757 18 .655 15. .866 0. .00 0. .00 PROA

ATOM 300 HA1 GLY X 572 -13 .906 17 .605 15. .662 0. .00 0. .00 PROA

ATOM 301 HA2 GLY X 572 -14 .646 19 .197 16. .151 0. .00 0. .00 PROA

ATOM 302 C GLY X 572 -12 .808 18 .614 17. .067 0. .00 0. .00 PROA

ATOM 303 O GLY X 572 -13 .131 18 .126 18. .082 0. .00 0. .00 PROA

ATOM 304 N ASN X 573 -11 .556 19 .062 16. .861 0. .00 0. .00 PROA

ATOM 305 HN ASN X 573 -11 .352 19 .307 15. .917 0. .00 0. .00 PROA

ATOM 306 CA ASN X 573 -10 .512 19 .078 17. .846 0. .00 0. .00 PROA

ATOM 307 HA ASN X 573 -10 .923 18 .767 18. .796 0. .00 0. .00 PROA

ATOM 308 CB ASN X 573 -9 .249 18 .304 17. .410 0. .00 0. .00 PROA

ATOM 309 HB1 ASN X 573 -8 .916 18 .596 16. .392 0. .00 0. .00 PROA

ATOM 310 HB2 ASN X 573 -8 .379 18 .547 18. .057 0. .00 0. .00 PROA

ATOM 311 CG ASN X 573 -9 .525 16 .823 17. .586 0. .00 0. .00 PROA

ATOM 312 OD1 ASN X 573 -9 .370 16 .272 18. .641 0. .00 0. .00 PROA

ATOM 313 ND2 ASN X 573 -9 .997 16 .177 16. .505 0. .00 0. .00 PROA

ATOM 314 HD21 ASN X 573 -10 .236 15 .206 16. .507 0. .00 0. .00 PROA

ATOM 315 HD22 ASN X 573 -9 .745 16 .664 15. .669 0. .00 0. .00 PROA

ATOM 316 C ASN X 573 -10 .070 20 .568 18. .154 0. .00 0. .00 PROA

ATOM 317 O ASN X 573 -9 .213 20 .857 18. .964 0. .00 0. .00 PROA

ATOM 318 N MET X 574 -10 .684 21 .552 17. .440 0. .00 0. .00 PROA

ATOM 319 HN MET X 574 -11 .229 21 .296 16. .646 0. .00 0. .00 PROA

ATOM 320 CA MET X 574 -10 .619 22 .956 17. .669 0. .00 0. .00 PROA

ATOM 321 HA MET X 574 -9 .826 23 .189 18. .364 0. .00 0. .00 PROA

ATOM 322 CB MET X 574 -10 .458 23 .702 16. .306 0. .00 0. .00 PROA

ATOM 323 HB1 MET X 574 -11 .327 23 .601 15. .621 0. .00 0. .00 PROA

ATOM 324 HB2 MET X 574 -10 .368 24 .774 16. .580 0. .00 0. .00 PROA

ATOM 325 CG MET X 574 -9 .178 23 .207 15. .598 0. .00 0. .00 PROA

ATOM 326 HG1 MET X 574 -8 .358 23 .288 16. .342 0. .00 0. .00 PROA

ATOM 327 HG2 MET X 574 -9 .353 22 .126 15. .412 0. .00 0. .00 PROA

ATOM 328 SD MET X 574 -8 .782 24 .166 14. .134 0. .00 0. .00 PROA

ATOM 329 C MET X 574 -11 .864 23 .415 18. .339 0. .00 0. .00 PROA ATOM 330 O MET X 574 -12.062 24.683 18..468 0..00 0..00 PROA

ATOM 331 N GLU X 575 -12 .817 22 .481 18. .579 0. .00 0. .00 PROA

ATOM 332 HN GLU X 575 -12 .466 21 .548 18. .599 0. .00 0. .00 PROA

ATOM 333 CA GLU X 575 -14 .222 22 .664 18. .983 0. .00 0. .00 PROA

ATOM 334 HA GLU X 575 -14 .773 23 .260 18. .271 0. .00 0. .00 PROA

ATOM 335 CB GLU X 575 -14 .957 21 .280 19. .149 0. .00 0. .00 PROA

ATOM 336 HB1 GLU X 575 -14 .940 20 .886 18. .110 0. .00 0. .00 PROA

ATOM 337 HB2 GLU X 575 -14 .401 20 .640 19. .868 0. .00 0. .00 PROA

ATOM 338 CG GLU X 575 -16 .428 21 .360 19. .605 0. .00 0. .00 PROA

ATOM 339 HG1 GLU X 575 -16 .484 21 .629 20. .681 0. .00 0. .00 PROA

ATOM 340 HG2 GLU X 575 -16 .919 21 .996 18. .837 0. .00 0. .00 PROA

ATOM 341 CD GLU X 575 -17 .012 19 .903 19. .580 0. .00 0. .00 PROA

ATOM 342 OE1 GLU X 575 -18 .005 19 .701 18. .789 0. .00 0. .00 PROA

ATOM 343 OE2 GLU X 575 -16 .510 19 .106 20. .369 0. .00 0. .00 PROA

ATOM 344 C GLU X 575 -14 .375 23 .374 20. .360 0. .00 0. .00 PROA

ATOM 345 O GLU X 575 -15 .265 24 .170 20. .578 0. .00 0. .00 PROA

ATOM 346 N GLN X 576 -13 .500 22 .982 21. .353 0. .00 0. .00 PROA

ATOM 347 HN GLN X 576 -12 .825 22 .255 21. .254 0. .00 0. .00 PROA

ATOM 348 CA GLN X 576 -13 .272 23 .602 22. .592 0. .00 0. .00 PROA

ATOM 349 HA GLN X 576 -12 .610 22 .898 23. .073 0. .00 0. .00 PROA

ATOM 350 CB GLN X 576 -12 .439 24 .866 22. .396 0. .00 0. .00 PROA

ATOM 351 HB1 GLN X 576 -13 .063 25 .512 21. .743 0. .00 0. .00 PROA

ATOM 352 HB2 GLN X 576 -12 .219 25 .462 23. .307 0. .00 0. .00 PROA

ATOM 353 CG GLN X 576 -11 .010 24 .621 21. .799 0. .00 0. .00 PROA

ATOM 354 HG1 GLN X 576 -10 .279 24 .065 22. .423 0. .00 0. .00 PROA

ATOM 355 HG2 GLN X 576 -11 .089 24 .059 20. .844 0. .00 0. .00 PROA

ATOM 356 CD GLN X 576 -10 .465 25 .991 21. .467 0. .00 0. .00 PROA

ATOM 357 OE1 GLN X 576 -11 .022 27 .069 21. .636 0. .00 0. .00 PROA

ATOM 358 NE2 GLN X 576 -9 .225 25 .943 20. .811 0. .00 0. .00 PROA

ATOM 359 HE21 GLN X 576 -8 .931 26 .832 20. .460 0. .00 0. .00 PROA

ATOM 360 HE22 GLN X 576 -8 .702 25 .093 20. .739 0. .00 0. .00 PROA

ATOM 361 C GLN X 576 -14 .468 23 .843 23. .456 0. .00 0. .00 PROA

ATOM 362 O GLN X 576 -14 .573 24 .913 24. .023 0. .00 0. .00 PROA

ATOM 363 N PRO X 577 -15 .452 22 .990 23. .664 0. .00 0. .00 PROA

ATOM 364 CD PRO X 577 -15 .342 21 .547 23. .368 0. .00 0. .00 PROA

ATOM 365 HD1 PRO X 577 -14 .752 21 .160 22. .510 0. .00 0. .00 PROA

ATOM 366 HD2 PRO X 577 -14 .951 21 .102 24. .307 0. .00 0. .00 PROA

ATOM 367 CA PRO X 577 -16 .721 23 .340 24. .365 0. .00 0. .00 PROA

ATOM 368 HA PRO X 577 -17 .284 23 .984 23. .705 0. .00 0. .00 PROA

ATOM 369 CB PRO X 577 -17 .451 22 .030 24. .418 0. .00 0. .00 PROA

ATOM 370 HB1 PRO X 577 -18 .525 22 .092 24. .140 0. .00 0. .00 PROA

ATOM 371 HB2 PRO X 577 -17 .194 21 .526 25. .374 0. .00 0. .00 PROA

ATOM 372 CG PRO X 577 -16 .801 21 .174 23. .374 0. .00 0. .00 PROA

ATOM 373 HG1 PRO X 577 -17 .216 21 .402 22. .369 0. .00 0. .00 PROA

ATOM 374 HG2 PRO X 577 -16 .975 20 .104 23. .619 0. .00 0. .00 PROA

ATOM 375 C PRO X 577 -16 .558 24 .005 25. .642 0. .00 0. .00 PROA

ATOM 376 O PRO X 577 -15 .759 23 .445 26. .382 0. .00 0. .00 PROA

ATOM 377 N HSD X 578 -17 .340 25 .029 26. .003 0. .00 0. .00 PROA

ATOM 378 HN HSD X 578 -18 .087 25 .276 25. .390 0. .00 0. .00 PROA

ATOM 379 CA HSD X 578 -17 .152 25 .931 27. .174 0. .00 0. .00 PROA

ATOM 380 HA HSD X 578 -16 .201 25 .617 27. .579 0. .00 0. .00 PROA

ATOM 381 CB HSD X 578 -17 .276 27 .463 26. .864 0. .00 0. .00 PROA

ATOM 382 HB1 HSD X 578 -18 .307 27 .704 26. .527 0. .00 0. .00 PROA

ATOM 383 HB2 HSD X 578 -16 .987 28 .117 27. .714 0. .00 0. .00 PROA

ATOM 384 ND1 HSD X 578 -15 .117 27 .607 25. .641 0. .00 0. .00 PROA

ATOM 385 HD1 HSD X 578 -14 .585 26 .992 26. .224 0. .00 0. .00 PROA

ATOM 386 CG HSD X 578 -16 .431 27 .898 25. .612 0. .00 0. .00 PROA

ATOM 387 CE1 HSD X 578 -14 .557 28 .086 24. .547 0. .00 0. .00 PROA

ATOM 388 HE1 HSD X 578 -13 .628 27 .833 24. .036 0. .00 0. .00 PROA

ATOM 389 NE2 HSD X 578 -15 .413 28 .720 23. .764 0. .00 0. .00 PROA

ATOM 390 CD2 HSD X 578 -16 .622 28 .675 24. .467 0. .00 0. .00 PROA

ATOM 391 HD2 HSD X 578 -17 .512 29 .262 24. .280 0. .00 0. .00 PROA

ATOM 392 C HSD X 578 -18 .208 25 .540 28. .212 0. .00 0. .00 PROA

ATOM 393 O HSD X 578 -18 .408 26 .265 29. .185 0. .00 0. .00 PROA

ATOM 394 N MET X 579 -18 .977 24 .496 27. .942 0. .00 0. .00 PROA

ATOM 395 HN MET X 579 -18 .824 24 .000 27. .091 0. .00 0. .00 PROA ATOM 396 CA MET X 579 -20.187 24.131 28..627 0..00 0..00 PROA

ATOM 397 HA MET X 579 -20 .761 25 .044 28. .686 0. .00 0. .00 PROA

ATOM 398 CB MET X 579 -20 .844 23 .195 27. .581 0. .00 0. .00 PROA

ATOM 399 HB1 MET X 579 -20 .861 23 .730 26. .608 0. .00 0. .00 PROA

ATOM 400 HB2 MET X 579 -20 .174 22 .313 27. .491 0. .00 0. .00 PROA

ATOM 401 CG MET X 579 -22 .340 22 .907 27. .839 0. .00 0. .00 PROA

ATOM 402 HG1 MET X 579 -22 .683 22 .219 27. .037 0. .00 0. .00 PROA

ATOM 403 HG2 MET X 579 -22 .430 22 .235 28. .719 0. .00 0. .00 PROA

ATOM 404 C MET X 579 -19 .998 23 .412 29. .940 0. .00 0. .00 PROA

ATOM 405 O MET X 579 -20 .675 23 .629 30. .953 0. .00 0. .00 PROA

ATOM 406 N ASP X 580 -18 .960 22 .484 29. .944 0. .00 0. .00 PROA

ATOM 407 HN ASP X 580 -18 .331 22 .318 29. .189 0. .00 0. .00 PROA

ATOM 408 CA ASP X 580 -18 .676 21 .620 31. .080 0. .00 0. .00 PROA

ATOM 409 HA ASP X 580 -19 .177 21 .993 31. .961 0. .00 0. .00 PROA

ATOM 410 CB ASP X 580 -19 .180 20 .155 30. .710 0. .00 0. .00 PROA

ATOM 411 HB1 ASP X 580 -20 .097 20 .362 30. .117 0. .00 0. .00 PROA

ATOM 412 HB2 ASP X 580 -18 .386 19 .690 30. .087 0. .00 0. .00 PROA

ATOM 413 CG ASP X 580 -19 .580 19 .245 31. .925 0. .00 0. .00 PROA

ATOM 414 OD1 ASP X 580 -20 .672 18 .664 31. .860 0. .00 0. .00 PROA

ATOM 415 OD2 ASP X 580 -18 .771 19 .112 32. .863 0. .00 0. .00 PROA

ATOM 416 C ASP X 580 -17 .228 21 .754 31. .501 0. .00 0. .00 PROA

ATOM 417 O ASP X 580 -16 .400 22 .427 30. .912 0. .00 0. .00 PROA

ATOM 418 N SER X 581 -16 .872 21 .040 32. .575 0. .00 0. .00 PROA

ATOM 419 HN SER X 581 -17 .448 20 .335 32. .983 0. .00 0. .00 PROA

ATOM 420 CA SER X 581 -15 .595 21 .255 33. .236 0. .00 0. .00 PROA

ATOM 421 HA SER X 581 -15 .185 22 .245 33. .100 0. .00 0. .00 PROA

ATOM 422 CB SER X 581 -15 .678 21 .019 34. .812 0. .00 0. .00 PROA

ATOM 423 HB1 SER X 581 -16 .393 21 .709 35. .309 0. .00 0. .00 PROA

ATOM 424 HB2 SER X 581 -15 .933 19 .942 34. .915 0. .00 0. .00 PROA

ATOM 425 OG SER X 581 -14 .417 21 .290 35. .420 0. .00 0. .00 PROA

ATOM 426 HG1 SER X 581 -14 .517 21 .504 36. .350 0. .00 0. .00 PROA

ATOM 427 C SER X 581 -14 .482 20 .337 32. .700 0. .00 0. .00 PROA

ATOM 428 O SER X 581 -14 .643 19 .141 32. .567 0. .00 0. .00 PROA

ATOM 429 N ARG X 582 -13 .335 20 .928 32. .261 0. .00 0. .00 PROA

ATOM 430 HN ARG X 582 -13 .367 21 .918 32. .153 0. .00 0. .00 PROA

ATOM 431 CA ARG X 582 -12 .118 20 .228 31. .942 0. .00 0. .00 PROA

ATOM 432 HA ARG X 582 -12 .370 19 .416 31. .276 0. .00 0. .00 PROA

ATOM 433 CB ARG X 582 -11 .005 21 .145 31. .290 0. .00 0. .00 PROA

ATOM 434 HB1 ARG X 582 -10 .684 21 .944 31. .992 0. .00 0. .00 PROA

ATOM 435 HB2 ARG X 582 -10 .137 20 .479 31. .096 0. .00 0. .00 PROA

ATOM 436 CG ARG X 582 -11 .535 21 .887 30. .037 0. .00 0. .00 PROA

ATOM 437 HG1 ARG X 582 -12 .060 21 .204 29. .335 0. .00 0. .00 PROA

ATOM 438 HG2 ARG X 582 -12 .280 22 .586 30. .473 0. .00 0. .00 PROA

ATOM 439 CD ARG X 582 -10 .377 22 .594 29. .374 0. .00 0. .00 PROA

ATOM 440 HD1 ARG X 582 -10 .273 23 .642 29. .728 0. .00 0. .00 PROA

ATOM 441 HD2 ARG X 582 -9 .477 21 .963 29. .536 0. .00 0. .00 PROA

ATOM 442 NE ARG X 582 -10 .698 22 .545 27. .913 0. .00 0. .00 PROA

ATOM 443 HE ARG X 582 -11 .659 22 .505 27. .638 0. .00 0. .00 PROA

ATOM 444 CZ ARG X 582 -9 .866 22 .965 26. .936 0. .00 0. .00 PROA

ATOM 445 NH1 ARG X 582 -8 .710 23 .444 27. .161 0. .00 0. .00 PROA

ATOM 446 HH11 ARG X 582 -8 .255 23 .823 26. .355 0. .00 0. .00 PROA

ATOM 447 HH12 ARG X 582 -8 .284 23 .577 28. .056 0. .00 0. .00 PROA

ATOM 448 NH2 ARG X 582 -10 .301 22 .773 25. .715 0. .00 0. .00 PROA

ATOM 449 HH21 ARG X 582 -9 .636 22 .677 24. .975 0. .00 0. .00 PROA

ATOM 450 HH22 ARG X 582 -11 .094 22 .173 25. .614 0. .00 0. .00 PROA

ATOM 451 C ARG X 582 -11 .465 19 .448 33. .136 0. .00 0. .00 PROA

ATOM 452 O ARG X 582 -11 .029 18 .294 32. .995 0. .00 0. .00 PROA

ATOM 453 N ILE X 583 -11 .464 20 .138 34. .298 0. .00 0. .00 PROA

ATOM 454 HN ILE X 583 -11 .727 21 .100 34. .304 0. .00 0. .00 PROA

ATOM 455 CA ILE X 583 -10 .954 19 .567 35. .494 0. .00 0. .00 PROA

ATOM 456 HA ILE X 583 -10 .020 19 .117 35. .192 0. .00 0. .00 PROA

ATOM 457 CB ILE X 583 -10 .575 20 .663 36. .625 0. .00 0. .00 PROA

ATOM 458 HB ILE X 583 -9 .835 21 .362 36. .179 0. .00 0. .00 PROA

ATOM 459 CG2 ILE X 583 -11 .792 21 .484 37. . Ill 0. .00 0. .00 PROA

ATOM 460 HG21 ILE X 583 -12 .190 22 .003 36. .213 0. .00 0. .00 PROA

ATOM 461 HG22 ILE X 583 -12 .534 20 .805 37. .583 0. .00 0. .00 PROA ATOM 462 HG23 ILE X 583 -11.426 22.200 37..878 0..00 0..00 PROA

ATOM 463 CGI ILE X 583 -9 .866 20 .080 37. .874 0. .00 0. .00 PROA

ATOM 464 HG11 ILE X 583 -9 .912 20 .844 38. .679 0. .00 0. .00 PROA

ATOM 465 HG12 ILE X 583 -10 .519 19 .216 38. .121 0. .00 0. .00 PROA

ATOM 466 CD ILE X 583 -8 .419 19 .724 37. .456 0. .00 0. .00 PROA

ATOM 467 HD1 ILE X 583 -7 .902 19 .225 38. .304 0. .00 0. .00 PROA

ATOM 468 HD2 ILE X 583 -8 .251 19 .228 36. .476 0. .00 0. .00 PROA

ATOM 469 HD3 ILE X 583 -7 .897 20 .704 37. .452 0. .00 0. .00 PROA

ATOM 470 C ILE X 583 -11 .860 18 .481 36. .045 0. .00 0. .00 PROA

ATOM 471 O ILE X 583 -11 .444 17 .452 36. .604 0. .00 0. .00 PROA

ATOM 472 N GLY X 584 -13 .204 18 .590 35. .892 0. .00 0. .00 PROA

ATOM 473 HN GLY X 584 -13 .680 19 .449 35. .722 0. .00 0. .00 PROA

ATOM 474 CA GLY X 584 -14 .034 17 .506 36. .207 0. .00 0. .00 PROA

ATOM 475 HA1 GLY X 584 -15 .017 17 .944 36. .295 0. .00 0. .00 PROA

ATOM 476 HA2 GLY X 584 -13 .780 17 .135 37. .189 0. .00 0. .00 PROA

ATOM 477 C GLY X 584 -14 .126 16 .378 35. .244 0. .00 0. .00 PROA

ATOM 478 O GLY X 584 -14 .639 15 .311 35. .566 0. .00 0. .00 PROA

ATOM 479 N TRP X 585 -13 .644 16 .558 33. .995 0. .00 0. .00 PROA

ATOM 480 HN TRP X 585 -13 .250 17 .440 33. .747 0. .00 0. .00 PROA

ATOM 481 CA TRP X 585 -13 .675 15 .474 32. .963 0. .00 0. .00 PROA

ATOM 482 HA TRP X 585 -14 .694 15 .252 32. .683 0. .00 0. .00 PROA

ATOM 483 CB TRP X 585 -12 .885 16 .056 31. .720 0. .00 0. .00 PROA

ATOM 484 HB1 TRP X 585 -13 .465 16 .937 31. .372 0. .00 0. .00 PROA

ATOM 485 HB2 TRP X 585 -11 .933 16 .505 32. .076 0. .00 0. .00 PROA

ATOM 486 CG TRP X 585 -12 .592 15 .098 30. .580 0. .00 0. .00 PROA

ATOM 487 CD1 TRP X 585 -13 .489 14 .210 30. .048 0. .00 0. .00 PROA

ATOM 488 HD1 TRP X 585 -14 .561 14 .332 30. .098 0. .00 0. .00 PROA

ATOM 489 NE1 TRP X 585 -12 .829 13 .629 28. .972 0. .00 0. .00 PROA

ATOM 490 HE1 TRP X 585 -13 .204 13 .151 28. .208 0. .00 0. .00 PROA

ATOM 491 CE2 TRP X 585 -11 .473 13 .925 28. .982 0. .00 0. .00 PROA

ATOM 492 CD2 TRP X 585 -11 .289 14 .784 30. .084 0. .00 0. .00 PROA

ATOM 493 CE3 TRP X 585 -10 .019 15 .327 30. .371 0. .00 0. .00 PROA

ATOM 494 HE3 TRP X 585 -9 .904 16 .003 31. .206 0. .00 0. .00 PROA

ATOM 495 CZ3 TRP X 585 -8 .927 14 .813 29. .644 0. .00 0. .00 PROA

ATOM 496 HZ3 TRP X 585 -7 .902 15 .130 29. .774 0. .00 0. .00 PROA

ATOM 497 CZ2 TRP X 585 -10 .434 13 .492 28. .219 0. .00 0. .00 PROA

ATOM 498 HZ2 TRP X 585 -10 .623 12 .819 27. .396 0. .00 0. .00 PROA

ATOM 499 CH2 TRP X 585 -9 .171 13 .939 28. .554 0. .00 0. .00 PROA

ATOM 500 HH2 TRP X 585 -8 .345 13 .581 27. .957 0. .00 0. .00 PROA

ATOM 501 C TRP X 585 -12 .948 14 .176 33. .491 0. .00 0. .00 PROA

ATOM 502 O TRP X 585 -13 .567 13 .133 33. .354 0. .00 0. .00 PROA

ATOM 503 N LEU X 586 -11 .793 14 .267 34. .189 0. .00 0. .00 PROA

ATOM 504 HN LEU X 586 -11 .267 15 .101 34. .332 0. .00 0. .00 PROA

ATOM 505 CA LEU X 586 -11 .053 13 .169 34. .709 0. .00 0. .00 PROA

ATOM 506 HA LEU X 586 -10 .474 12 .676 33. .942 0. .00 0. .00 PROA

ATOM 507 CB LEU X 586 -9 .946 13 .862 35. .690 0. .00 0. .00 PROA

ATOM 508 HB1 LEU X 586 -10 .492 14 .529 36. .391 0. .00 0. .00 PROA

ATOM 509 HB2 LEU X 586 -9 .512 13 .049 36. .311 0. .00 0. .00 PROA

ATOM 510 CG LEU X 586 -8 .696 14 .531 35. .106 0. .00 0. .00 PROA

ATOM 511 HG LEU X 586 -8 .093 14 .918 35. .956 0. .00 0. .00 PROA

ATOM 512 CD1 LEU X 586 -7 .810 13 .627 34. .254 0. .00 0. .00 PROA

ATOM 513 HD11 LEU X 586 -8 .484 13 .071 33. .568 0. .00 0. .00 PROA

ATOM 514 HD12 LEU X 586 -7 .064 14 .323 33. .813 0. .00 0. .00 PROA

ATOM 515 HD13 LEU X 586 -7 .316 12 .966 34. .998 0. .00 0. .00 PROA

ATOM 516 CD2 LEU X 586 -9 .092 15 .782 34. .241 0. .00 0. .00 PROA

ATOM 517 HD21 LEU X 586 -9 .818 16 .420 34. .789 0. .00 0. .00 PROA

ATOM 518 HD22 LEU X 586 -8 .151 16 .343 34. .060 0. .00 0. .00 PROA

ATOM 519 HD23 LEU X 586 -9 .540 15 .389 33. .303 0. .00 0. .00 PROA

ATOM 520 C LEU X 586 -11 .845 12 .208 35. .610 0. .00 0. .00 PROA

ATOM 521 O LEU X 586 -11 .864 10 .979 35. .396 0. .00 0. .00 PROA

ATOM 522 N HSD X 587 -12 .588 12 .704 36. .553 0. .00 0. .00 PROA

ATOM 523 HN HSD X 587 -12 .539 13 .694 36. .666 0. .00 0. .00 PROA

ATOM 524 CA HSD X 587 -13 .546 11 .990 37. .345 0. .00 0. .00 PROA

ATOM 525 HA HSD X 587 -13 .039 11 .191 37. .865 0. .00 0. .00 PROA

ATOM 526 CB HSD X 587 -14 .066 13 .028 38. .376 0. .00 0. .00 PROA

ATOM 527 HB1 HSD X 587 -14 .756 13 .732 37. .863 0. .00 0. .00 PROA ATOM 528 HB2 HSD X 587 -14.674 12.476 39..124 0..00 0..00 PROA

ATOM 529 ND1 HSD X 587 -13 .172 15 .127 39. .468 0. .00 0. .00 PROA

ATOM 530 HD1 HSD X 587 -13 .989 15 .703 39. .481 0. .00 0. .00 PROA

ATOM 531 CG HSD X 587 -12 .946 13 .809 39. .031 0. .00 0. .00 PROA

ATOM 532 CE1 HSD X 587 -12 .129 15 .402 40. .339 0. .00 0. .00 PROA

ATOM 533 HE1 HSD X 587 -11 .997 16 .371 40. .821 0. .00 0. .00 PROA

ATOM 534 NE2 HSD X 587 -11 .215 14 .460 40. .408 0. .00 0. .00 PROA

ATOM 535 CD2 HSD X 587 -11 .706 13 .466 39. .517 0. .00 0. .00 PROA

ATOM 536 HD2 HSD X 587 -11 .258 12 .481 39. .522 0. .00 0. .00 PROA

ATOM 537 C HSD X 587 -14 .710 11 .328 36. .641 0. .00 0. .00 PROA

ATOM 538 O HSD X 587 -14 .982 10 .123 36. .930 0. .00 0. .00 PROA

ATOM 539 N ASN X 588 -15 .332 12 .015 35. .652 0. .00 0. .00 PROA

ATOM 540 HN ASN X 588 -14 .992 12 .915 35. .389 0. .00 0. .00 PROA

ATOM 541 CA ASN X 588 -16 .488 11 .565 34. .951 0. .00 0. .00 PROA

ATOM 542 HA ASN X 588 -17 .115 10 .991 35. .618 0. .00 0. .00 PROA

ATOM 543 CB ASN X 588 -17 .221 12 .749 34. .270 0. .00 0. .00 PROA

ATOM 544 HB1 ASN X 588 -16 .521 13 .311 33. .616 0. .00 0. .00 PROA

ATOM 545 HB2 ASN X 588 -18 .047 12 .342 33. .648 0. .00 0. .00 PROA

ATOM 546 CG ASN X 588 -17 .809 13 .795 35. .240 0. .00 0. .00 PROA

ATOM 547 OD1 ASN X 588 -17 .798 14 .958 34. .850 0. .00 0. .00 PROA

ATOM 548 ND2 ASN X 588 -18 .395 13 .347 36. .363 0. .00 0. .00 PROA

ATOM 549 HD21 ASN X 588 -18 .151 12 .445 36. .719 0. .00 0. .00 PROA

ATOM 550 HD22 ASN X 588 -19 .086 13 .926 36. .796 0. .00 0. .00 PROA

ATOM 551 C ASN X 588 -16 .046 10 .528 33. .928 0. .00 0. .00 PROA

ATOM 552 O ASN X 588 -16 .848 9 .609 33. .622 0. .00 0. .00 PROA

ATOM 553 N LEU X 589 -14 .886 10 .672 33. .303 0. .00 0. .00 PROA

ATOM 554 HN LEU X 589 -14 .327 11 .477 33. .486 0. .00 0. .00 PROA

ATOM 555 CA LEU X 589 -14 .209 9 .681 32. .443 0. .00 0. .00 PROA

ATOM 556 HA LEU X 589 -14 .855 9 .427 31. .616 0. .00 0. .00 PROA

ATOM 557 CB LEU X 589 -12 .857 10 .261 31. .856 0. .00 0. .00 PROA

ATOM 558 HB1 LEU X 589 -12 .930 11 .154 31. .198 0. .00 0. .00 PROA

ATOM 559 HB2 LEU X 589 -12 .361 10 .546 32. .808 0. .00 0. .00 PROA

ATOM 560 CG LEU X 589 -12 .005 9 .195 31. .095 0. .00 0. .00 PROA

ATOM 561 HG LEU X 589 -11 .877 8 .374 31. .833 0. .00 0. .00 PROA

ATOM 562 CD1 LEU X 589 -12 .768 8 .667 29. .869 0. .00 0. .00 PROA

ATOM 563 HD11 LEU X 589 -11 .957 8 .317 29. .195 0. .00 0. .00 PROA

ATOM 564 HD12 LEU X 589 -13 .472 7 .811 29. .950 0. .00 0. .00 PROA

ATOM 565 HD13 LEU X 589 -13 .336 9 .472 29. .355 0. .00 0. .00 PROA

ATOM 566 CD2 LEU X 589 -10 .601 9 .727 30. .711 0. .00 0. .00 PROA

ATOM 567 HD21 LEU X 589 -10 .041 9 .937 31. .648 0. .00 0. .00 PROA

ATOM 568 HD22 LEU X 589 -9 .995 8 .941 30. .211 0. .00 0. .00 PROA

ATOM 569 HD23 LEU X 589 -10 .448 10 .642 30. .101 0. .00 0. .00 PROA

ATOM 570 C LEU X 589 -13 .996 8 .310 33. .162 0. .00 0. .00 PROA

ATOM 571 O LEU X 589 -14 .391 7 .231 32. .685 0. .00 0. .00 PROA

ATOM 572 N GLY X 590 -13 .375 8 .371 34. .381 0. .00 0. .00 PROA

ATOM 573 HN GLY X 590 -13 .004 9 .252 34. .667 0. .00 0. .00 PROA

ATOM 574 CA GLY X 590 -13 .239 7 .127 35. .214 0. .00 0. .00 PROA

ATOM 575 HA1 GLY X 590 -12 .604 7 .457 36. .023 0. .00 0. .00 PROA

ATOM 576 HA2 GLY X 590 -12 .726 6 .325 34. .705 0. .00 0. .00 PROA

ATOM 577 C GLY X 590 -14 .504 6 .552 35. .788 0. .00 0. .00 PROA

ATOM 578 O GLY X 590 -14 .587 5 .339 35. .979 0. .00 0. .00 PROA

ATOM 579 N ASP X 591 -15 .596 7 .307 35. .935 0. .00 0. .00 PROA

ATOM 580 HN ASP X 591 -15 .420 8 .284 35. .840 0. .00 0. .00 PROA

ATOM 581 CA ASP X 591 -16 .878 6 .690 36. .149 0. .00 0. .00 PROA

ATOM 582 HA ASP X 591 -16 .798 5 .794 36. .747 0. .00 0. .00 PROA

ATOM 583 CB ASP X 591 -17 .810 7 .593 36. .971 0. .00 0. .00 PROA

ATOM 584 HB1 ASP X 591 -17 .613 8 .658 36. .723 0. .00 0. .00 PROA

ATOM 585 HB2 ASP X 591 -18 .897 7 .368 36. .916 0. .00 0. .00 PROA

ATOM 586 CG ASP X 591 -17 .438 7 .711 38. .504 0. .00 0. .00 PROA

ATOM 587 OD1 ASP X 591 -17 .829 8 .711 39. .138 0. .00 0. .00 PROA

ATOM 588 OD2 ASP X 591 -16 .815 6 .738 39. .033 0. .00 0. .00 PROA

ATOM 589 C ASP X 591 -17 .681 6 .355 34. .916 0. .00 0. .00 PROA

ATOM 590 O ASP X 591 -18 .881 6 .003 35. .051 0. .00 0. .00 PROA

ATOM 591 N GLN X 592 -17 .030 6 .446 33. .676 0. .00 0. .00 PROA

ATOM 592 HN GLN X 592 -16 .056 6 .662 33. .694 0. .00 0. .00 PROA

ATOM 593 CA GLN X 592 -17 .648 6 .181 32. .397 0. .00 0. .00 PROA ATOM 594 HA GLN X 592 -16.859 6.364 31..683 0..00 0..00 PROA

ATOM 595 CB GLN X 592 -17 .630 4 .654 32. .102 0. .00 0. .00 PROA

ATOM 596 HB1 GLN X 592 -18 .250 4 .105 32. .843 0. .00 0. .00 PROA

ATOM 597 HB2 GLN X 592 -17 .948 4 .508 31. .047 0. .00 0. .00 PROA

ATOM 598 CG GLN X 592 -16 .274 3 .867 32. .148 0. .00 0. .00 PROA

ATOM 599 HG1 GLN X 592 -15 .488 4 .266 31. .472 0. .00 0. .00 PROA

ATOM 600 HG2 GLN X 592 -15 .819 4 .013 33. .151 0. .00 0. .00 PROA

ATOM 601 CD GLN X 592 -16 .524 2 .429 31. .714 0. .00 0. .00 PROA

ATOM 602 OE1 GLN X 592 -17 .013 2 .121 30. .621 0. .00 0. .00 PROA

ATOM 603 NE2 GLN X 592 -16 .270 1 .494 32. .690 0. .00 0. .00 PROA

ATOM 604 HE21 GLN X 592 -16 .317 0 .529 32. .430 0. .00 0. .00 PROA

ATOM 605 HE22 GLN X 592 -15 .910 1 .798 33. .573 0. .00 0. .00 PROA

ATOM 606 C GLN X 592 -18 .948 6 .882 31. .993 0. .00 0. .00 PROA

ATOM 607 O GLN X 592 -19 .868 6 .253 31. .433 0. .00 0. .00 PROA

ATOM 608 N ILE X 593 -19 .094 8 .250 32. .297 0. .00 0. .00 PROA

ATOM 609 HN ILE X 593 -18 .319 8 .704 32. .731 0. .00 0. .00 PROA

ATOM 610 CA ILE X 593 -20 .286 9 .052 32. .088 0. .00 0. .00 PROA

ATOM 611 HA ILE X 593 -21 .006 8 .497 32. .671 0. .00 0. .00 PROA

ATOM 612 CB ILE X 593 -20 .001 10 .366 32. .688 0. .00 0. .00 PROA

ATOM 613 HB ILE X 593 -18 .946 10 .567 32. .401 0. .00 0. .00 PROA

ATOM 614 CG2 ILE X 593 -20 .919 11 .505 32. .177 0. .00 0. .00 PROA

ATOM 615 HG21 ILE X 593 -21 .987 11 .377 32. .456 0. .00 0. .00 PROA

ATOM 616 HG22 ILE X 593 -20 .493 12 .452 32. .572 0. .00 0. .00 PROA

ATOM 617 HG23 ILE X 593 -20 .876 11 .716 31. .087 0. .00 0. .00 PROA

ATOM 618 CGI ILE X 593 -20 .002 10 .325 34. .272 0. .00 0. .00 PROA

ATOM 619 HG11 ILE X 593 -19 .079 9 .809 34. .614 0. .00 0. .00 PROA

ATOM 620 HG12 ILE X 593 -19 .887 11 .378 34. .610 0. .00 0. .00 PROA

ATOM 621 CD ILE X 593 -21 .313 9 .841 34. .972 0. .00 0. .00 PROA

ATOM 622 HD1 ILE X 593 -21 .279 9 .874 36. .082 0. .00 0. .00 PROA

ATOM 623 HD2 ILE X 593 -22 .067 10 .627 34. .755 0. .00 0. .00 PROA

ATOM 624 HD3 ILE X 593 -21 .664 8 .840 34. .640 0. .00 0. .00 PROA

ATOM 625 C ILE X 593 -20 .810 9 .132 30. .612 0. .00 0. .00 PROA

ATOM 626 O ILE X 593 -20 .024 9 .495 29. .714 0. .00 0. .00 PROA

ATOM 627 N GLY X 594 -22 .096 8 .853 30. .378 0. .00 0. .00 PROA

ATOM 628 HN GLY X 594 -22 .663 8 .462 31. .099 0. .00 0. .00 PROA

ATOM 629 CA GLY X 594 -22 .798 8 .853 29. .061 0. .00 0. .00 PROA

ATOM 630 HA1 GLY X 594 -23 .696 8 .279 29. .239 0. .00 0. .00 PROA

ATOM 631 HA2 GLY X 594 -22 .101 8 .449 28. .342 0. .00 0. .00 PROA

ATOM 632 C GLY X 594 -23 .190 10 .164 28. .531 0. .00 0. .00 PROA

ATOM 633 O GLY X 594 -23 .800 10 .227 27. .464 0. .00 0. .00 PROA

ATOM 634 N LYS X 595 -22 .873 11 .287 29. .249 0. .00 0. .00 PROA

ATOM 635 HN LYS X 595 -22 .485 11 .183 30. .161 0. .00 0. .00 PROA

ATOM 636 CA LYS X 595 -23 .059 12 .642 28. .719 0. .00 0. .00 PROA

ATOM 637 HA LYS X 595 -24 .078 12 .640 28. .361 0. .00 0. .00 PROA

ATOM 638 CB LYS X 595 -22 .909 13 .860 29. .700 0. .00 0. .00 PROA

ATOM 639 HB1 LYS X 595 -21 .912 13 .760 30. .179 0. .00 0. .00 PROA

ATOM 640 HB2 LYS X 595 -22 .957 14 .805 29. .118 0. .00 0. .00 PROA

ATOM 641 CG LYS X 595 -23 .973 13 .882 30. .848 0. .00 0. .00 PROA

ATOM 642 HG1 LYS X 595 -24 .969 13 .974 30. .363 0. .00 0. .00 PROA

ATOM 643 HG2 LYS X 595 -23 .951 12 .920 31. .403 0. .00 0. .00 PROA

ATOM 644 CD LYS X 595 -23 .916 15 .119 31. .716 0. .00 0. .00 PROA

ATOM 645 HD1 LYS X 595 -23 .086 15 .104 32. .455 0. .00 0. .00 PROA

ATOM 646 HD2 LYS X 595 -23 .816 16 .039 31. .100 0. .00 0. .00 PROA

ATOM 647 CE LYS X 595 -25 .181 15 .471 32. .516 0. .00 0. .00 PROA

ATOM 648 HE1 LYS X 595 -25 .930 15 .714 31. .733 0. .00 0. .00 PROA

ATOM 649 HE2 LYS X 595 -25 .479 14 .707 33. .265 0. .00 0. .00 PROA

ATOM 650 NZ LYS X 595 -25 .068 16 .659 33. .260 0. .00 0. .00 PROA

ATOM 651 HZ1 LYS X 595 -24 .760 17 .491 32. .718 0. .00 0. .00 PROA

ATOM 652 HZ2 LYS X 595 -25 .879 16 .983 33. .826 0. .00 0. .00 PROA

ATOM 653 HZ3 LYS X 595 -24 .254 16 .487 33. .884 0. .00 0. .00 PROA

ATOM 654 C LYS X 595 -22 .108 12 .957 27. .524 0. .00 0. .00 PROA

ATOM 655 O LYS X 595 -20 .961 12 .503 27. .658 0. .00 0. .00 PROA

ATOM 656 N PRO X 596 -22 .516 13 .719 26. .443 0. .00 0. .00 PROA

ATOM 657 CD PRO X 596 -23 .876 14 .291 26. .270 0. .00 0. .00 PROA

ATOM 658 HD1 PRO X 596 -24 .665 13 .547 26. .030 0. .00 0. .00 PROA

ATOM 659 HD2 PRO X 596 -24 .030 14 .955 27. .147 0. .00 0. .00 PROA ATOM 660 CA PRO X 596 -21.709 14.087 25..277 0..00 0..00 PROA

ATOM 661 HA PRO X 596 -21 .704 13 .134 24. .768 0. .00 0. .00 PROA

ATOM 662 CB PRO X 596 -22 .430 15 .230 24. .598 0. .00 0. .00 PROA

ATOM 663 HB1 PRO X 596 -22 .254 15 .182 23. .502 0. .00 0. .00 PROA

ATOM 664 HB2 PRO X 596 -22 .084 16 .212 24. .985 0. .00 0. .00 PROA

ATOM 665 CG PRO X 596 -23 .824 14 .953 24. .908 0. .00 0. .00 PROA

ATOM 666 HG1 PRO X 596 -24 .178 14 .160 24. .215 0. .00 0. .00 PROA

ATOM 667 HG2 PRO X 596 -24 .556 15 .787 24. .964 0. .00 0. .00 PROA

ATOM 668 C PRO X 596 -20 .259 14 .461 25. .567 0. .00 0. .00 PROA

ATOM 669 O PRO X 596 -19 .329 13 .758 25. .121 0. .00 0. .00 PROA

ATOM 670 N TYR X 597 -19 .851 15 .477 26. .393 0. .00 0. .00 PROA

ATOM 671 HN TYR X 597 -20 .485 16 .138 26. .786 0. .00 0. .00 PROA

ATOM 672 CA TYR X 597 -18 .481 15 .903 26. .497 0. .00 0. .00 PROA

ATOM 673 HA TYR X 597 -18 .032 15 .883 25. .515 0. .00 0. .00 PROA

ATOM 674 CB TYR X 597 -18 .410 17 .381 26. .771 0. .00 0. .00 PROA

ATOM 675 HB1 TYR X 597 -18 .778 17 .676 27. .777 0. .00 0. .00 PROA

ATOM 676 HB2 TYR X 597 -17 .374 17 .753 26. .623 0. .00 0. .00 PROA

ATOM 677 CG TYR X 597 -19 .248 18 .156 25. .787 0. .00 0. .00 PROA

ATOM 678 CD1 TYR X 597 -20 .025 19 .240 26. .295 0. .00 0. .00 PROA

ATOM 679 HD1 TYR X 597 -19 .899 19 .604 27. .303 0. .00 0. .00 PROA

ATOM 680 CE1 TYR X 597 -20 .915 19 .921 25. .492 0. .00 0. .00 PROA

ATOM 681 HE1 TYR X 597 -21 .572 20 .668 25. .912 0. .00 0. .00 PROA

ATOM 682 CZ TYR X 597 -20 .916 19 .714 24. .102 0. .00 0. .00 PROA

ATOM 683 OH TYR X 597 -21 .542 20 .574 23. .190 0. .00 0. .00 PROA

ATOM 684 HH TYR X 597 -21 .069 20 .438 22. .366 0. .00 0. .00 PROA

ATOM 685 CD2 TYR X 597 -19 .304 17 .842 24. .402 0. .00 0. .00 PROA

ATOM 686 HD2 TYR X 597 -18 .701 17 .131 23. .855 0. .00 0. .00 PROA

ATOM 687 CE2 TYR X 597 -20 .131 18 .650 23. .579 0. .00 0. .00 PROA

ATOM 688 HE2 TYR X 597 -20 .153 18 .496 22. .510 0. .00 0. .00 PROA

ATOM 689 C TYR X 597 -17 .620 15 .109 27. .499 0. .00 0. .00 PROA

ATOM 690 O TYR X 597 -16 .471 15 .442 27. .768 0. .00 0. .00 PROA

ATOM 691 N ASN X 598 -18 .202 13 .979 27. .965 0. .00 0. .00 PROA

ATOM 692 HN ASN X 598 -19 .147 13 .710 27. .798 0. .00 0. .00 PROA

ATOM 693 CA ASN X 598 -17 .468 13 .029 28. .767 0. .00 0. .00 PROA

ATOM 694 HA ASN X 598 -16 .450 13 .353 28. .926 0. .00 0. .00 PROA

ATOM 695 CB ASN X 598 -18 .278 12 .859 30. .041 0. .00 0. .00 PROA

ATOM 696 HB1 ASN X 598 -19 .306 12 .562 29. .743 0. .00 0. .00 PROA

ATOM 697 HB2 ASN X 598 -17 .924 12 .077 30. .746 0. .00 0. .00 PROA

ATOM 698 CG ASN X 598 -18 .381 14 .226 30. .708 0. .00 0. .00 PROA

ATOM 699 OD1 ASN X 598 -19 .460 14 .725 30. .936 0. .00 0. .00 PROA

ATOM 700 ND2 ASN X 598 -17 .140 14 .813 31. .049 0. .00 0. .00 PROA

ATOM 701 HD21 ASN X 598 -17 .103 15 .737 31. .430 0. .00 0. .00 PROA

ATOM 702 HD22 ASN X 598 -16 .271 14 .500 30. .666 0. .00 0. .00 PROA

ATOM 703 C ASN X 598 -17 .421 11 .688 28. .052 0. .00 0. .00 PROA

ATOM 704 O ASN X 598 -16 .889 10 .728 28. .565 0. .00 0. .00 PROA

ATOM 705 N SER X 599 -17 .971 11 .615 26. .836 0. .00 0. .00 PROA

ATOM 706 HN SER X 599 -18 .236 12 .484 26. .427 0. .00 0. .00 PROA

ATOM 707 CA SER X 599 -18 .020 10 .333 26. .078 0. .00 0. .00 PROA

ATOM 708 HA SER X 599 -17 .296 9 .693 26. .560 0. .00 0. .00 PROA

ATOM 709 CB SER X 599 -19 .457 9 .729 26. .202 0. .00 0. .00 PROA

ATOM 710 HB1 SER X 599 -19 .472 8 .747 25. .682 0. .00 0. .00 PROA

ATOM 711 HB2 SER X 599 -19 .530 9 .408 27. .262 0. .00 0. .00 PROA

ATOM 712 OG SER X 599 -20 .529 10 .521 25. .791 0. .00 0. .00 PROA

ATOM 713 HG1 SER X 599 -20 .552 11 .134 26. .529 0. .00 0. .00 PROA

ATOM 714 C SER X 599 -17 .608 10 .358 24. .623 0. .00 0. .00 PROA

ATOM 715 O SER X 599 -17 .214 9 .365 23. .946 0. .00 0. .00 PROA

ATOM 716 N SER X 600 -17 .752 11 .555 24. .017 0. .00 0. .00 PROA

ATOM 717 HN SER X 600 -17 .931 12 .361 24. .575 0. .00 0. .00 PROA

ATOM 718 CA SER X 600 -17 .554 11 .747 22. .599 0. .00 0. .00 PROA

ATOM 719 HA SER X 600 -18 .157 10 .988 22. .122 0. .00 0. .00 PROA

ATOM 720 CB SER X 600 -18 .010 13 .011 21. .984 0. .00 0. .00 PROA

ATOM 721 HB1 SER X 600 -17 .730 13 .022 20. .909 0. .00 0. .00 PROA

ATOM 722 HB2 SER X 600 -19 .114 12 .940 22. .085 0. .00 0. .00 PROA

ATOM 723 OG SER X 600 -17 .429 14 .116 22. .722 0. .00 0. .00 PROA

ATOM 724 HG1 SER X 600 -17 .589 14 .956 22. .286 0. .00 0. .00 PROA

ATOM 725 C SER X 600 -16 .059 11 .458 22. .189 0. .00 0. .00 PROA ATOM 726 O SER X 600 -15.813 10.807 21..149 0..00 0..00 PROA

ATOM 727 N GLY X 601 -15 .100 12 .021 22. .930 0. .00 0. .00 PROA

ATOM 728 HN GLY X 601 -15 .390 12 .676 23. .623 0. .00 0. .00 PROA

ATOM 729 CA GLY X 601 -13 .752 11 .704 22. .667 0. .00 0. .00 PROA

ATOM 730 HA1 GLY X 601 -13 .522 12 .008 21. .657 0. .00 0. .00 PROA

ATOM 731 HA2 GLY X 601 -13 .600 10 .637 22. .740 0. .00 0. .00 PROA

ATOM 732 C GLY X 601 -12 .750 12 .325 23. .605 0. .00 0. .00 PROA

ATOM 733 O GLY X 601 -12 .059 11 .643 24. .349 0. .00 0. .00 PROA

ATOM 734 N LEU X 602 -12 .573 13 .664 23. .611 0. .00 0. .00 PROA

ATOM 735 HN LEU X 602 -13 .142 14 .263 23. .054 0. .00 0. .00 PROA

ATOM 736 CA LEU X 602 -11 .606 14 .229 24. .519 0. .00 0. .00 PROA

ATOM 737 HA LEU X 602 -11 .398 13 .621 25. .387 0. .00 0. .00 PROA

ATOM 738 CB LEU X 602 -10 .312 14 .631 23. .816 0. .00 0. .00 PROA

ATOM 739 HB1 LEU X 602 -10 .501 15 .104 22. .828 0. .00 0. .00 PROA

ATOM 740 HB2 LEU X 602 -9 .778 15 .365 24. .456 0. .00 0. .00 PROA

ATOM 741 CG LEU X 602 -9 .269 13 .547 23. .588 0. .00 0. .00 PROA

ATOM 742 HG LEU X 602 -9 .712 12 .809 22. .887 0. .00 0. .00 PROA

ATOM 743 CD1 LEU X 602 -8 .129 14 .272 22. .810 0. .00 0. .00 PROA

ATOM 744 HD11 LEU X 602 -7 .701 15 .092 23. .426 0. .00 0. .00 PROA

ATOM 745 HD12 LEU X 602 -7 .376 13 .497 22. .551 0. .00 0. .00 PROA

ATOM 746 HD13 LEU X 602 -8 .396 14 .746 21. .841 0. .00 0. .00 PROA

ATOM 747 CD2 LEU X 602 -8 .758 12 .849 24. .851 0. .00 0. .00 PROA

ATOM 748 HD21 LEU X 602 -8 .092 12 .004 24. .574 0. .00 0. .00 PROA

ATOM 749 HD22 LEU X 602 -8 .461 13 .576 25. .637 0. .00 0. .00 PROA

ATOM 750 HD23 LEU X 602 -9 .557 12 .310 25. .403 0. .00 0. .00 PROA

ATOM 751 C LEU X 602 -12 .115 15 .533 25. .039 0. .00 0. .00 PROA

ATOM 752 O LEU X 602 -12 .759 16 .356 24. .311 0. .00 0. .00 PROA

ATOM 753 N GLY X 603 -11 .993 15 .797 26. .330 0. .00 0. .00 PROA

ATOM 754 HN GLY X 603 -11 .543 15 .170 26. .962 0. .00 0. .00 PROA

ATOM 755 CA GLY X 603 -12 .646 16 .930 26. .959 0. .00 0. .00 PROA

ATOM 756 HA1 GLY X 603 -13 .096 16 .536 27. .858 0. .00 0. .00 PROA

ATOM 757 HA2 GLY X 603 -13 .399 17 .325 26. .294 0. .00 0. .00 PROA

ATOM 758 C GLY X 603 -11 .645 17 .976 27. .424 0. .00 0. .00 PROA

ATOM 759 O GLY X 603 -11 .901 19 .196 27. .412 0. .00 0. .00 PROA

ATOM 760 N GLY X 604 -10 .390 17 .413 27. .602 0. .00 0. .00 PROA

ATOM 761 HN GLY X 604 -10 .299 16 .420 27. .586 0. .00 0. .00 PROA

ATOM 762 CA GLY X 604 -9 .260 18 .280 27. .719 0. .00 0. .00 PROA

ATOM 763 HA1 GLY X 604 -8 .645 17 .785 28. .456 0. .00 0. .00 PROA

ATOM 764 HA2 GLY X 604 -9 .623 19 .245 28. .041 0. .00 0. .00 PROA

ATOM 765 C GLY X 604 -8 .522 18 .527 26. .430 0. .00 0. .00 PROA

ATOM 766 O GLY X 604 -9 .002 18 .106 25. .370 0. .00 0. .00 PROA

ATOM 767 N PRO X 605 -7 .380 19 .102 26. .409 0. .00 0. .00 PROA

ATOM 768 CD PRO X 605 -6 .919 19 .849 27. .572 0. .00 0. .00 PROA

ATOM 769 HD1 PRO X 605 -7 .701 20 .499 28. .020 0. .00 0. .00 PROA

ATOM 770 HD2 PRO X 605 -6 .423 19 .179 28. .306 0. .00 0. .00 PROA

ATOM 771 CA PRO X 605 -6 .617 19 .408 25. .157 0. .00 0. .00 PROA

ATOM 772 HA PRO X 605 -7 .196 20 .170 24. .657 0. .00 0. .00 PROA

ATOM 773 CB PRO X 605 -5 .394 20 .001 25. .754 0. .00 0. .00 PROA

ATOM 774 HB1 PRO X 605 -4 .745 20 .530 25. .024 0. .00 0. .00 PROA

ATOM 775 HB2 PRO X 605 -4 .681 19 .243 26. .144 0. .00 0. .00 PROA

ATOM 776 CG PRO X 605 -5 .911 20 .789 26. .947 0. .00 0. .00 PROA

ATOM 777 HG1 PRO X 605 -6 .433 21 .616 26. .421 0. .00 0. .00 PROA

ATOM 778 HG2 PRO X 605 -5 .134 21 .175 27. .641 0. .00 0. .00 PROA

ATOM 779 C PRO X 605 -6 .234 18 .236 24. .272 0. .00 0. .00 PROA

ATOM 780 O PRO X 605 -6 .231 17 .071 24. .629 0. .00 0. .00 PROA

ATOM 781 N SER X 606 -6 .020 18 .525 22. .962 0. .00 0. .00 PROA

ATOM 782 HN SER X 606 -6 .009 19 .480 22. .675 0. .00 0. .00 PROA

ATOM 783 CA SER X 606 -5 .854 17 .482 21. .939 0. .00 0. .00 PROA

ATOM 784 HA SER X 606 -5 .876 16 .535 22. .457 0. .00 0. .00 PROA

ATOM 785 CB SER X 606 -7 .071 17 .549 20. .940 0. .00 0. .00 PROA

ATOM 786 HB1 SER X 606 -7 .886 17 .184 21. .602 0. .00 0. .00 PROA

ATOM 787 HB2 SER X 606 -7 .271 18 .593 20. .616 0. .00 0. .00 PROA

ATOM 788 OG SER X 606 -6 .988 16 .744 19. .804 0. .00 0. .00 PROA

ATOM 789 HG1 SER X 606 -7 .860 16 .672 19. .410 0. .00 0. .00 PROA

ATOM 790 C SER X 606 -4 .493 17 .781 21. .212 0. .00 0. .00 PROA

ATOM 791 O SER X 606 -3 .964 18 .877 21. .337 0. .00 0. .00 PROA ATOM 792 N ILE X 607 -3.944 16.740 20..536 0..00 0..00 PROA

ATOM 793 HN ILE X 607 -4 .336 15 .825 20. .482 0. .00 0. .00 PROA

ATOM 794 CA ILE X 607 -2 .672 16 .838 19. .821 0. .00 0. .00 PROA

ATOM 795 HA ILE X 607 -2 .110 17 .534 20. .427 0. .00 0. .00 PROA

ATOM 796 CB ILE X 607 -1 .963 15 .452 19. .665 0. .00 0. .00 PROA

ATOM 797 HB ILE X 607 -1 .147 15 .503 18. .912 0. .00 0. .00 PROA

ATOM 798 CG2 ILE X 607 -1 .382 15 .213 21. .130 0. .00 0. .00 PROA

ATOM 799 HG21 ILE X 607 -0 .882 16 .116 21. .541 0. .00 0. .00 PROA

ATOM 800 HG22 ILE X 607 -2 .145 14 .894 21. .872 0. .00 0. .00 PROA

ATOM 801 HG23 ILE X 607 -0 .588 14 .438 21. .071 0. .00 0. .00 PROA

ATOM 802 CGI ILE X 607 -2 .912 14 .284 19. .053 0. .00 0. .00 PROA

ATOM 803 HG11 ILE X 607 -3 .638 13 .969 19. .832 0. .00 0. .00 PROA

ATOM 804 HG12 ILE X 607 -3 .529 14 .628 18. .195 0. .00 0. .00 PROA

ATOM 805 CD ILE X 607 -2 .173 12 .945 18. .725 0. .00 0. .00 PROA

ATOM 806 HD1 ILE X 607 -2 .772 12 .180 18. .186 0. .00 0. .00 PROA

ATOM 807 HD2 ILE X 607 -1 .336 13 .205 18. .041 0. .00 0. .00 PROA

ATOM 808 HD3 ILE X 607 -1 .837 12 .474 19. .673 0. .00 0. .00 PROA

ATOM 809 C ILE X 607 -2 .929 17 .239 18. .367 0. .00 0. .00 PROA

ATOM 810 O ILE X 607 -2 .035 17 .555 17. .596 0. .00 0. .00 PROA

ATOM 811 N LYS X 608 -4 .203 17 .138 17. .997 0. .00 0. .00 PROA

ATOM 812 HN LYS X 608 -4 .906 16 .879 18. .654 0. .00 0. .00 PROA

ATOM 813 CA LYS X 608 -4 .682 17 .061 16. .626 0. .00 0. .00 PROA

ATOM 814 HA LYS X 608 -3 .861 16 .547 16. .149 0. .00 0. .00 PROA

ATOM 815 CB LYS X 608 -5 .841 15 .985 16. .597 0. .00 0. .00 PROA

ATOM 816 HB1 LYS X 608 -5 .430 15 .041 17. .014 0. .00 0. .00 PROA

ATOM 817 HB2 LYS X 608 -6 .660 16 .329 17. .265 0. .00 0. .00 PROA

ATOM 818 CG LYS X 608 -6 .306 15 .905 15. .156 0. .00 0. .00 PROA

ATOM 819 HG1 LYS X 608 -7 .127 15 .156 15. .165 0. .00 0. .00 PROA

ATOM 820 HG2 LYS X 608 -6 .856 16 .800 14. .798 0. .00 0. .00 PROA

ATOM 821 CD LYS X 608 -5 .204 15 .437 14. .203 0. .00 0. .00 PROA

ATOM 822 HD1 LYS X 608 -4 .601 16 .254 13. .753 0. .00 0. .00 PROA

ATOM 823 HD2 LYS X 608 -4 .523 14 .759 14. .760 0. .00 0. .00 PROA

ATOM 824 CE LYS X 608 -5 .712 14 .646 12. .986 0. .00 0. .00 PROA

ATOM 825 HE1 LYS X 608 -6 .355 15 .365 12. .435 0. .00 0. .00 PROA

ATOM 826 HE2 LYS X 608 -4 .855 14 .398 12. .324 0. .00 0. .00 PROA

ATOM 827 NZ LYS X 608 -6 .452 13 .439 13. .288 0. .00 0. .00 PROA

ATOM 828 HZ1 LYS X 608 -7 .465 13 .669 13. .251 0. .00 0. .00 PROA

ATOM 829 HZ2 LYS X 608 -6 .177 12 .791 12. .522 0. .00 0. .00 PROA

ATOM 830 HZ3 LYS X 608 -6 .199 13 .108 14. .241 0. .00 0. .00 PROA

ATOM 831 C LYS X 608 -4 .991 18 .405 16. .091 0. .00 0. .00 PROA

ATOM 832 O LYS X 608 -4 .986 18 .570 14. .855 0. .00 0. .00 PROA

ATOM 833 N ASP X 609 -5 .228 19 .429 16. .848 0. .00 0. .00 PROA

ATOM 834 HN ASP X 609 -5 .362 19 .410 17. .836 0. .00 0. .00 PROA

ATOM 835 CA ASP X 609 -5 .283 20 .786 16. .353 0. .00 0. .00 PROA

ATOM 836 HA ASP X 609 -5 .977 20 .856 15. .528 0. .00 0. .00 PROA

ATOM 837 CB ASP X 609 -5 .999 21 .669 17. .363 0. .00 0. .00 PROA

ATOM 838 HB1 ASP X 609 -6 .101 22 .713 16. .997 0. .00 0. .00 PROA

ATOM 839 HB2 ASP X 609 -6 .992 21 .205 17. .546 0. .00 0. .00 PROA

ATOM 840 CG ASP X 609 -5 .261 21 .740 18. .738 0. .00 0. .00 PROA

ATOM 841 OD1 ASP X 609 -5 .702 22 .582 19. .498 0. .00 0. .00 PROA

ATOM 842 OD2 ASP X 609 -4 .322 20 .975 19. .096 0. .00 0. .00 PROA

ATOM 843 C ASP X 609 -3 .985 21 .548 15. .948 0. .00 0. .00 PROA

ATOM 844 O ASP X 609 -4 .142 22 .653 15. .405 0. .00 0. .00 PROA

ATOM 845 N LYS X 610 -2 .833 20 .945 16. .304 0. .00 0. .00 PROA

ATOM 846 HN LYS X 610 -2 .927 20 .112 16. .843 0. .00 0. .00 PROA

ATOM 847 CA LYS X 610 -1 .514 21 .353 15. .684 0. .00 0. .00 PROA

ATOM 848 HA LYS X 610 -1 .480 22 .432 15. .729 0. .00 0. .00 PROA

ATOM 849 CB LYS X 610 -0 .388 20 .654 16. .434 0. .00 0. .00 PROA

ATOM 850 HB1 LYS X 610 -0 .366 19 .545 16. .372 0. .00 0. .00 PROA

ATOM 851 HB2 LYS X 610 0 .534 21 .046 15. .953 0. .00 0. .00 PROA

ATOM 852 CG LYS X 610 -0 .362 21 .155 17. .908 0. .00 0. .00 PROA

ATOM 853 HG1 LYS X 610 -0 .335 22 .259 18. .029 0. .00 0. .00 PROA

ATOM 854 HG2 LYS X 610 -1 .308 20 .913 18. .437 0. .00 0. .00 PROA

ATOM 855 CD LYS X 610 0. .748 20 .480 18. .738 0. .00 0. .00 PROA

ATOM 856 HD1 LYS X 610 0 .511 19 .399 18. .843 0. .00 0. .00 PROA

ATOM 857 HD2 LYS X 610 1 .651 20 .610 18. .105 0. .00 0. .00 PROA ATOM 858 CE LYS X 610 1..062 21.208 20..041 0..00 0..00 PROA

ATOM 859 HE1 LYS X 610 2 .041 20 .865 20. .440 0. .00 0. .00 PROA

ATOM 860 HE2 LYS X 610 1 .030 22 .298 19. .827 0. .00 0. .00 PROA

ATOM 861 NZ LYS X 610 0. .104 20 .964 21. .086 0. .00 0. .00 PROA

ATOM 862 HZ1 LYS X 610 -0 .728 21 .585 21. .034 0. .00 0. .00 PROA

ATOM 863 HZ2 LYS X 610 -0 .247 19 .988 21. .005 0. .00 0. .00 PROA

ATOM 864 HZ3 LYS X 610 0 .555 20 .964 22. .023 0. .00 0. .00 PROA

ATOM 865 C LYS X 610 -1 .452 20 .993 14. .245 0. .00 0. .00 PROA

ATOM 866 O LYS X 610 -1 .767 19 .855 13. .847 0. .00 0. .00 PROA

ATOM 867 N TYR X 611 -1 .072 21 .932 13. .351 0. .00 0. .00 PROA

ATOM 868 HN TYR X 611 -0 .755 22 .827 13. .655 0. .00 0. .00 PROA

ATOM 869 CA TYR X 611 -1 .126 21 .700 11. .929 0. .00 0. .00 PROA

ATOM 870 HA TYR X 611 -2 .143 21 .486 11. .634 0. .00 0. .00 PROA

ATOM 871 CB TYR X 611 -0 .780 23 .099 11. .227 0. .00 0. .00 PROA

ATOM 872 HB1 TYR X 611 0 .269 23 .294 11. .536 0. .00 0. .00 PROA

ATOM 873 HB2 TYR X 611 -0 .944 23 .064 10. .129 0. .00 0. .00 PROA

ATOM 874 CG TYR X 611 -1 .663 24 .190 11. .838 0. .00 0. .00 PROA

ATOM 875 CD1 TYR X 611 -1 .109 25 .321 12. .339 0. .00 0. .00 PROA

ATOM 876 HD1 TYR X 611 -0 .039 25 .460 12. .366 0. .00 0. .00 PROA

ATOM 877 CE1 TYR X 611 -1 .951 26 .300 12. .917 0. .00 0. .00 PROA

ATOM 878 HE1 TYR X 611 -1 .484 27 .208 13. .268 0. .00 0. .00 PROA

ATOM 879 CZ TYR X 611 -3 .358 26 .247 12. .774 0. .00 0. .00 PROA

ATOM 880 OH TYR X 611 -4 .194 27 .247 13. .217 0. .00 0. .00 PROA

ATOM 881 HH TYR X 611 -3 .634 28 .026 13. .232 0. .00 0. .00 PROA

ATOM 882 CD2 TYR X 611 -3 .074 24 .078 11. .803 0. .00 0. .00 PROA

ATOM 883 HD2 TYR X 611 -3 .492 23 .181 11. .371 0. .00 0. .00 PROA

ATOM 884 CE2 TYR X 611 -3 .933 25 .057 12. .284 0. .00 0. .00 PROA

ATOM 885 HE2 TYR X 611 -5 .002 24 .974 12. .155 0. .00 0. .00 PROA

ATOM 886 C TYR X 611 -0 .262 20 .544 11. .394 0. .00 0. .00 PROA

ATOM 887 O TYR X 611 -0 .599 19 .667 10. .616 0. .00 0. .00 PROA

ATOM 888 N VAL X 612 0. .942 20 .420 12. .003 0. .00 0. .00 PROA

ATOM 889 HN VAL X 612 1. .194 20 .981 12. .787 0. .00 0. .00 PROA

ATOM 890 CA VAL X 612 1. .863 19 .291 11. .757 0. .00 0. .00 PROA

ATOM 891 HA VAL X 612 2. .016 19 .348 10. .690 0. .00 0. .00 PROA

ATOM 892 CB VAL X 612 3. .181 19 .462 12. .523 0. .00 0. .00 PROA

ATOM 893 HB VAL X 612 3. .096 19 .617 13. .620 0. .00 0. .00 PROA

ATOM 894 CGI VAL X 612 4 .278 18 .371 12. .181 0. .00 0. .00 PROA

ATOM 895 HG11 VAL X 612 5 .206 18 .761 12. .651 0. .00 0. .00 PROA

ATOM 896 HG12 VAL X 612 4 .080 17 .369 12. .618 0. .00 0. .00 PROA

ATOM 897 HG13 VAL X 612 4 .423 18 .402 11. .079 0. .00 0. .00 PROA

ATOM 898 CG2 VAL X 612 3 .703 20 .834 12. .120 0. .00 0. .00 PROA

ATOM 899 HG21 VAL X 612 4 .676 21 .172 12. .535 0. .00 0. .00 PROA

ATOM 900 HG22 VAL X 612 3 .692 20 .878 11. .010 0. .00 0. .00 PROA

ATOM 901 HG23 VAL X 612 2 .975 21 .640 12. .355 0. .00 0. .00 PROA

ATOM 902 C VAL X 612 1. .247 17 .978 12. .052 0. .00 0. .00 PROA

ATOM 903 O VAL X 612 1. .406 17 .002 11. .269 0. .00 0. .00 PROA

ATOM 904 N THR X 613 0. .494 17 .800 13. .184 0. .00 0. .00 PROA

ATOM 905 HN THR X 613 0. .340 18 .527 13. .848 0. .00 0. .00 PROA

ATOM 906 CA THR X 613 -0 .350 16 .602 13. .437 0. .00 0. .00 PROA

ATOM 907 HA THR X 613 0. .286 15 .742 13. .583 0. .00 0. .00 PROA

ATOM 908 CB THR X 613 -0 .991 16 .703 14. .828 0. .00 0. .00 PROA

ATOM 909 HB THR X 613 -1 .821 17 .436 14. .918 0. .00 0. .00 PROA

ATOM 910 OG1 THR X 613 -0 .096 17 .105 15. .861 0. .00 0. .00 PROA

ATOM 911 HG1 THR X 613 -0 .718 17 .432 16. .516 0. .00 0. .00 PROA

ATOM 912 CG2 THR X 613 -1 .313 15 .310 15. .458 0. .00 0. .00 PROA

ATOM 913 HG21 THR X 613 -1 .806 15 .272 16. .453 0. .00 0. .00 PROA

ATOM 914 HG22 THR X 613 -1 .995 14 .832 14. .723 0. .00 0. .00 PROA

ATOM 915 HG23 THR X 613 -0 .397 14 .681 15. .494 0. .00 0. .00 PROA

ATOM 916 C THR X 613 -1 .462 16 .255 12. .406 0. .00 0. .00 PROA

ATOM 917 O THR X 613 -1 .532 15 .137 11. .961 0. .00 0. .00 PROA

ATOM 918 N ALA X 614 -2 .120 17 .332 11. .933 0. .00 0. .00 PROA

ATOM 919 HN ALA X 614 -1 .879 18 .224 12. .309 0. .00 0. .00 PROA

ATOM 920 CA ALA X 614 -3 .150 17 .213 10. .898 0. .00 0. .00 PROA

ATOM 921 HA ALA X 614 -3 .927 16 .519 11. .184 0. .00 0. .00 PROA

ATOM 922 CB ALA X 614 -3 .722 18 .642 10. .715 0. .00 0. .00 PROA

ATOM 923 HB1 ALA X 614 -4 .590 18 .551 10. .029 0. .00 0. .00 PROA ATOM 924 HB2 ALA X 614 -4.061 18.973 11..720 0..00 0..00 PROA

ATOM 925 HB3 ALA X 614 -3 .037 19 .454 10. .391 0. .00 0. .00 PROA

ATOM 926 C ALA X 614 -2 .519 16 .684 9. .602 0. .00 0. .00 PROA

ATOM 927 O ALA X 614 -2 .952 15 .747 8. .960 0. .00 0. .00 PROA

ATOM 928 N LEU X 615 -1 .358 17 .260 9. .239 0. .00 0. .00 PROA

ATOM 929 HN LEU X 615 -1 .061 18 .043 9. .780 0. .00 0. .00 PROA

ATOM 930 CA LEU X 615 -0 .700 16 .942 7. .965 0. .00 0. .00 PROA

ATOM 931 HA LEU X 615 -1 .451 16 .867 7. .192 0. .00 0. .00 PROA

ATOM 932 CB LEU X 615 0. .414 17 .944 7. .543 0. .00 0. .00 PROA

ATOM 933 HB1 LEU X 615 0 .023 18 .983 7. .514 0. .00 0. .00 PROA

ATOM 934 HB2 LEU X 615 1 .273 18 .200 8. .199 0. .00 0. .00 PROA

ATOM 935 CG LEU X 615 0. .986 17 .649 6. .134 0. .00 0. .00 PROA

ATOM 936 HG LEU X 615 1. .505 16 .667 6. .123 0. .00 0. .00 PROA

ATOM 937 CD1 LEU X 615 -0 .095 17 .635 4. .981 0. .00 0. .00 PROA

ATOM 938 HD11 LEU X 615 -0 .355 18 .696 4. .781 0. .00 0. .00 PROA

ATOM 939 HD12 LEU X 615 0 .421 17 .168 4. .115 0. .00 0. .00 PROA

ATOM 940 HD13 LEU X 615 -0 .979 17 .042 5. .299 0. .00 0. .00 PROA

ATOM 941 CD2 LEU X 615 2 .074 18 .688 5. .905 0. .00 0. .00 PROA

ATOM 942 HD21 LEU X 615 2 .594 18 .420 4. .960 0. .00 0. .00 PROA

ATOM 943 HD22 LEU X 615 1 .684 19 .724 6. .004 0. .00 0. .00 PROA

ATOM 944 HD23 LEU X 615 2 .780 18 .637 6. .761 0. .00 0. .00 PROA

ATOM 945 C LEU X 615 -0 .099 15 .506 8. .041 0. .00 0. .00 PROA

ATOM 946 O LEU X 615 -0 .363 14 .701 7. .136 0. .00 0. .00 PROA

ATOM 947 N TYR X 616 0. .631 15 .087 9. .028 0. .00 0. .00 PROA

ATOM 948 HN TYR X 616 0. .802 15 .666 9. .821 0. .00 0. .00 PROA

ATOM 949 CA TYR X 616 1. .334 13 .792 9. .003 0. .00 0. .00 PROA

ATOM 950 HA TYR X 616 1. .828 13 .611 8. .059 0. .00 0. .00 PROA

ATOM 951 CB TYR X 616 2. .340 13 .586 10. .176 0. .00 0. .00 PROA

ATOM 952 HB1 TYR X 616 2 .949 14 .514 10. .209 0. .00 0. .00 PROA

ATOM 953 HB2 TYR X 616 1 .864 13 .384 11. .160 0. .00 0. .00 PROA

ATOM 954 CG TYR X 616 3. .387 12 .557 9. .872 0. .00 0. .00 PROA

ATOM 955 CD1 TYR X 616 4 .497 12 .921 9. .054 0. .00 0. .00 PROA

ATOM 956 HD1 TYR X 616 4 .485 13 .916 8. .633 0. .00 0. .00 PROA

ATOM 957 CE1 TYR X 616 5 .532 12 .039 8. .952 0. .00 0. .00 PROA

ATOM 958 HE1 TYR X 616 6 .421 12 .405 8. .461 0. .00 0. .00 PROA

ATOM 959 CZ TYR X 616 5. .516 10 .759 9. .530 0. .00 0. .00 PROA

ATOM 960 OH TYR X 616 6. .687 9 .863 9. .479 0. .00 0. .00 PROA

ATOM 961 HH TYR X 616 7. .305 10 .453 9. .041 0. .00 0. .00 PROA

ATOM 962 CD2 TYR X 616 3 .345 11 .285 10. .561 0. .00 0. .00 PROA

ATOM 963 HD2 TYR X 616 2 .584 11 .057 11. .292 0. .00 0. .00 PROA

ATOM 964 CE2 TYR X 616 4 .363 10 .365 10. .311 0. .00 0. .00 PROA

ATOM 965 HE2 TYR X 616 4 .350 9 .385 10. .766 0. .00 0. .00 PROA

ATOM 966 C TYR X 616 0. .350 12 .641 9. .058 0. .00 0. .00 PROA

ATOM 967 O TYR X 616 0. .510 11 .518 8. .505 0. .00 0. .00 PROA

ATOM 968 N PHE X 617 -0 .715 12 .797 9. .844 0. .00 0. .00 PROA

ATOM 969 HN PHE X 617 -0 .725 13 .557 10. .489 0. .00 0. .00 PROA

ATOM 970 CA PHE X 617 -1 .678 11 .741 10. .025 0. .00 0. .00 PROA

ATOM 971 HA PHE X 617 -1 .137 10 .830 10. .237 0. .00 0. .00 PROA

ATOM 972 CB PHE X 617 -2 .651 12 .046 11. .227 0. .00 0. .00 PROA

ATOM 973 HB1 PHE X 617 -3 .140 13 .033 11. .075 0. .00 0. .00 PROA

ATOM 974 HB2 PHE X 617 -3 .469 11 .295 11. .222 0. .00 0. .00 PROA

ATOM 975 CG PHE X 617 -1 .995 12 .039 12. .564 0. .00 0. .00 PROA

ATOM 976 CD1 PHE X 617 -2 .854 12 .266 13. .659 0. .00 0. .00 PROA

ATOM 977 HD1 PHE X 617 -3 .916 12 .389 13. .505 0. .00 0. .00 PROA

ATOM 978 CE1 PHE X 617 -2 .314 12 .279 14. .896 0. .00 0. .00 PROA

ATOM 979 HE1 PHE X 617 -3 .039 12 .475 15. .672 0. .00 0. .00 PROA

ATOM 980 CZ PHE X 617 -0 .949 12 .229 15. .087 0. .00 0. .00 PROA

ATOM 981 HZ PHE X 617 -0 .545 12 .285 16. .086 0. .00 0. .00 PROA

ATOM 982 CD2 PHE X 617 -0 .588 11 .909 12. .773 0. .00 0. .00 PROA

ATOM 983 HD2 PHE X 617 0 .079 11 .673 11. .957 0. .00 0. .00 PROA

ATOM 984 CE2 PHE X 617 -0 .047 11 .921 14. .024 0. .00 0. .00 PROA

ATOM 985 HE2 PHE X 617 1 .008 11 .825 14. .236 0. .00 0. .00 PROA

ATOM 986 C PHE X 617 -2 .561 11 .511 8. .793 0. .00 0. .00 PROA

ATOM 987 O PHE X 617 -2 .853 10 .377 8. .380 0. .00 0. .00 PROA

ATOM 988 N THR X 618 -2 .802 12 .598 8. .090 0. .00 0. .00 PROA

ATOM 989 HN THR X 618 -2 .342 13 .459 8. .294 0. .00 0. .00 PROA ATOM 990 CA THR X 618 -3.432 12.768 6..676 0..00 0..00 PROA

ATOM 991 HA THR X 618 -4 .440 12 .382 6. .630 0. .00 0. .00 PROA

ATOM 992 CB THR X 618 -3 .622 14 .180 6. .124 0. .00 0. .00 PROA

ATOM 993 HB THR X 618 -2 .665 14 .726 5. .980 0. .00 0. .00 PROA

ATOM 994 OG1 THR X 618 -4 .527 14 .981 6. .872 0. .00 0. .00 PROA

ATOM 995 HG1 THR X 618 -4 .108 15 .201 7. .707 0. .00 0. .00 PROA

ATOM 996 CG2 THR X 618 -4 .329 14 .276 4. .723 0. .00 0. .00 PROA

ATOM 997 HG21 THR X 618 -4 .363 15 .297 4. .288 0. .00 0. .00 PROA

ATOM 998 HG22 THR X 618 -3 .821 13 .648 3. .961 0. .00 0. .00 PROA

ATOM 999 HG23 THR X 618 -5 .347 13 .876 4. .922 0. .00 0. .00 PROA

ATOM 1000 C THR X 618 -2 .551 12 .069 5. .632 0. .00 0. .00 PROA

ATOM 1001 O THR X 618 -3 .090 11 .331 4. .865 0. .00 0. .00 PROA

ATOM 1002 N PHE X 619 -1 .215 12 .216 5. .675 0. .00 0. .00 PROA

ATOM 1003 HN PHE X 619 -0 .931 13 .050 6. .142 0. .00 0. .00 PROA

ATOM 1004 CA PHE X 619 -0 .343 11 .418 4. .871 0. .00 0. .00 PROA

ATOM 1005 HA PHE X 619 -0 .629 11 .651 3. .856 0. .00 0. .00 PROA

ATOM 1006 CB PHE X 619 1. .161 11 .884 4. .967 0. .00 0. .00 PROA

ATOM 1007 HB1 PHE X 619 1 .211 12 .988 4. .861 0. .00 0. .00 PROA

ATOM 1008 HB2 PHE X 619 1 .543 11 .524 5. .946 0. .00 0. .00 PROA

ATOM 1009 CG PHE X 619 1. .991 11 .427 3. .847 0. .00 0. .00 PROA

ATOM 1010 CD1 PHE X 619 1 .748 11 .728 2. .494 0. .00 0. .00 PROA

ATOM 1011 HD1 PHE X 619 0 .877 12 .332 2. .289 0. .00 0. .00 PROA

ATOM 1012 CE1 PHE X 619 2 .562 11 .240 1. .471 0. .00 0. .00 PROA

ATOM 1013 HE1 PHE X 619 2 .214 11 .405 0. .462 0. .00 0. .00 PROA

ATOM 1014 CZ PHE X 619 3. .617 10 .426 1. .749 0. .00 0. .00 PROA

ATOM 1015 HZ PHE X 619 4. .168 9 .883 0. .995 0. .00 0. .00 PROA

ATOM 1016 CD2 PHE X 619 3 .119 10 .627 4. .106 0. .00 0. .00 PROA

ATOM 1017 HD2 PHE X 619 3 .304 10 .320 5. .125 0. .00 0. .00 PROA

ATOM 1018 CE2 PHE X 619 3 .926 10 .100 3. .100 0. .00 0. .00 PROA

ATOM 1019 HE2 PHE X 619 4 .724 9 .434 3. .393 0. .00 0. .00 PROA

ATOM 1020 C PHE X 619 -0 .497 9 .921 5. .026 0. .00 0. .00 PROA

ATOM 1021 O PHE X 619 -0 .661 9 .133 4. .101 0. .00 0. .00 PROA

ATOM 1022 N SER X 620 -0 .488 9 .534 6. .347 0. .00 0. .00 PROA

ATOM 1023 HN SER X 620 -0 .327 10 .144 7. .119 0. .00 0. .00 PROA

ATOM 1024 CA SER X 620 -0 .543 8 .154 6. .869 0. .00 0. .00 PROA

ATOM 1025 HA SER X 620 0. .205 7 .555 6. .370 0. .00 0. .00 PROA

ATOM 1026 CB SER X 620 -0 .355 8 .054 8. .408 0. .00 0. .00 PROA

ATOM 1027 HB1 SER X 620 0 .455 8 .805 8. .529 0. .00 0. .00 PROA

ATOM 1028 HB2 SER X 620 -1 .188 8 .247 9. .117 0. .00 0. .00 PROA

ATOM 1029 OG SER X 620 0. .252 6 .812 8. .645 0. .00 0. .00 PROA

ATOM 1030 HG1 SER X 620 0 .190 6 .523 9. .558 0. .00 0. .00 PROA

ATOM 1031 C SER X 620 -1 .848 7 .454 6. .489 0. .00 0. .00 PROA

ATOM 1032 O SER X 620 -1 .901 6 .332 6. .066 0. .00 0. .00 PROA

ATOM 1033 N SER X 621 -2 .997 8 .154 6. .663 0. .00 0. .00 PROA

ATOM 1034 HN SER X 621 -2 .994 9 .046 7. .108 0. .00 0. .00 PROA

ATOM 1035 CA SER X 621 -4 .295 7 .619 6. .337 0. .00 0. .00 PROA

ATOM 1036 HA SER X 621 -4 .462 6 .610 6. .682 0. .00 0. .00 PROA

ATOM 1037 CB SER X 621 -5 .275 8 .534 6. .980 0. .00 0. .00 PROA

ATOM 1038 HB1 SER X 621 -5 .138 9 .592 6. .668 0. .00 0. .00 PROA

ATOM 1039 HB2 SER X 621 -6 .329 8 .254 6. .767 0. .00 0. .00 PROA

ATOM 1040 OG SER X 621 -5 .064 8 .578 8. .411 0. .00 0. .00 PROA

ATOM 1041 HG1 SER X 621 -4 .521 9 .308 8. .717 0. .00 0. .00 PROA

ATOM 1042 C SER X 621 -4 .574 7 .684 4. .798 0. .00 0. .00 PROA

ATOM 1043 O SER X 621 -4 .972 6 .649 4. .334 0. .00 0. .00 PROA

ATOM 1044 N LEU X 622 -4 .390 8 .833 4. .124 0. .00 0. .00 PROA

ATOM 1045 HN LEU X 622 -4 .106 9 .640 4. .636 0. .00 0. .00 PROA

ATOM 1046 CA LEU X 622 -4 .626 9 .011 2. .730 0. .00 0. .00 PROA

ATOM 1047 HA LEU X 622 -5 .676 8 .757 2. .734 0. .00 0. .00 PROA

ATOM 1048 CB LEU X 622 -4 .471 10 .526 2. .262 0. .00 0. .00 PROA

ATOM 1049 HB1 LEU X 622 -5 .003 11 .096 3. .054 0. .00 0. .00 PROA

ATOM 1050 HB2 LEU X 622 -3 .385 10 .752 2. .308 0. .00 0. .00 PROA

ATOM 1051 CG LEU X 622 -4 .904 10 .935 0. .844 0. .00 0. .00 PROA

ATOM 1052 HG LEU X 622 -5 .932 10 .572 0. .629 0. .00 0. .00 PROA

ATOM 1053 CD1 LEU X 622 -4 .881 12 .460 0. .762 0. .00 0. .00 PROA

ATOM 1054 HD11 LEU X 622 -3 .995 12 .936 1. .235 0. .00 0. .00 PROA

ATOM 1055 HD12 LEU X 622 -5 .147 12 .886 -0. .229 0. .00 0. .00 PROA ATOM 1056 HD13 LEU X 622 -5.757 12.763 1..376 0..00 0..00 PROA

ATOM 1057 CD2 LEU X 622 -4 .183 10 .459 -0. .433 0. .00 0. .00 PROA

ATOM 1058 HD21 LEU X 622 -3 .196 10 .930 -0. .632 0. .00 0. .00 PROA

ATOM 1059 HD22 LEU X 622 -3 .928 9 .378 -0. .449 0. .00 0. .00 PROA

ATOM 1060 HD23 LEU X 622 -4 .753 10 .694 -1. .357 0. .00 0. .00 PROA

ATOM 1061 C LEU X 622 -3 .902 8 .028 1. .842 0. .00 0. .00 PROA

ATOM 1062 O LEU X 622 -4 .460 7 .551 0. .880 0. .00 0. .00 PROA

ATOM 1063 N THR X 623 -2 .602 7 .774 2. .215 0. .00 0. .00 PROA

ATOM 1064 HN THR X 623 -2 .199 8 .287 2. .968 0. .00 0. .00 PROA

ATOM 1065 CA THR X 623 -1 .711 6 .856 1. .476 0. .00 0. .00 PROA

ATOM 1066 HA THR X 623 -2 .207 6 .604 0. .550 0. .00 0. .00 PROA

ATOM 1067 CB THR X 623 -0 .370 7 .403 1. .143 0. .00 0. .00 PROA

ATOM 1068 HB THR X 623 0. .176 6 .754 0. .426 0. .00 0. .00 PROA

ATOM 1069 OG1 THR X 623 0 .476 7 .403 2. .240 0. .00 0. .00 PROA

ATOM 1070 HG1 THR X 623 0 .061 7 .968 2. .896 0. .00 0. .00 PROA

ATOM 1071 CG2 THR X 623 -0 .475 8 .802 0. .580 0. .00 0. .00 PROA

ATOM 1072 HG21 THR X 623 -0 .806 9 .519 1. .362 0. .00 0. .00 PROA

ATOM 1073 HG22 THR X 623 0 .524 9 .229 0. .349 0. .00 0. .00 PROA

ATOM 1074 HG23 THR X 623 -1 .050 8 .913 -0. .364 0. .00 0. .00 PROA

ATOM 1075 C THR X 623 -1 .528 5 .436 2. .088 0. .00 0. .00 PROA

ATOM 1076 O THR X 623 -0 .931 4 .556 1. .498 0. .00 0. .00 PROA

ATOM 1077 N SER X 624 -2 .179 5 .176 3. .276 0. .00 0. .00 PROA

ATOM 1078 HN SER X 624 -2 .614 5 .976 3. .681 0. .00 0. .00 PROA

ATOM 1079 CA SER X 624 -2 .158 3 .879 4. .127 0. .00 0. .00 PROA

ATOM 1080 HA SER X 624 -2 .739 4 .098 5. .011 0. .00 0. .00 PROA

ATOM 1081 CB SER X 624 -3 .028 2 .700 3. .474 0. .00 0. .00 PROA

ATOM 1082 HB1 SER X 624 -4 .067 3 .054 3. .300 0. .00 0. .00 PROA

ATOM 1083 HB2 SER X 624 -2 .602 2 .417 2. .487 0. .00 0. .00 PROA

ATOM 1084 OG SER X 624 -3 .171 1 .511 4. .259 0. .00 0. .00 PROA

ATOM 1085 HG1 SER X 624 -3 .138 0 .741 3. .686 0. .00 0. .00 PROA

ATOM 1086 C SER X 624 -0 .807 3 .376 4. .641 0. .00 0. .00 PROA

ATOM 1087 O SER X 624 -0 .353 2 .225 4. .515 0. .00 0. .00 PROA

ATOM 1088 N VAL X 625 -0 .033 4 .289 5. .290 0. .00 0. .00 PROA

ATOM 1089 HN VAL X 625 -0 .230 5 .258 5. .157 0. .00 0. .00 PROA

ATOM 1090 CA VAL X 625 1. .122 3 .910 6. .069 0. .00 0. .00 PROA

ATOM 1091 HA VAL X 625 1. .594 3 .034 5. .649 0. .00 0. .00 PROA

ATOM 1092 CB VAL X 625 2. .142 5 .002 6. .330 0. .00 0. .00 PROA

ATOM 1093 HB VAL X 625 1. .590 5 .809 6. .856 0. .00 0. .00 PROA

ATOM 1094 CGI VAL X 625 3 .339 4 .477 7. .115 0. .00 0. .00 PROA

ATOM 1095 HG11 VAL X 625 3 .872 3 .581 6. .732 0. .00 0. .00 PROA

ATOM 1096 HG12 VAL X 625 4 .082 5 .302 7. .137 0. .00 0. .00 PROA

ATOM 1097 HG13 VAL X 625 3 .013 4 .285 8. .159 0. .00 0. .00 PROA

ATOM 1098 CG2 VAL X 625 2 .576 5 .580 4. .945 0. .00 0. .00 PROA

ATOM 1099 HG21 VAL X 625 3 .329 6 .282 5. .363 0. .00 0. .00 PROA

ATOM 1100 HG22 VAL X 625 3 .213 4 .883 4. .360 0. .00 0. .00 PROA

ATOM 1101 HG23 VAL X 625 1 .790 6 .127 4. .383 0. .00 0. .00 PROA

ATOM 1102 C VAL X 625 0. .518 3 .399 7. .404 0. .00 0. .00 PROA

ATOM 1103 O VAL X 625 0. .930 2 .402 7. .970 0. .00 0. .00 PROA

ATOM 1104 N GLY X 626 -0 .561 4 .000 7. .817 0. .00 0. .00 PROA

ATOM 1105 HN GLY X 626 -0 .926 4 .751 7. .273 0. .00 0. .00 PROA

ATOM 1106 CA GLY X 626 -1 .328 3 .546 9. .023 0. .00 0. .00 PROA

ATOM 1107 HA1 GLY X 626 -1 .634 2 .516 8. .919 0. .00 0. .00 PROA

ATOM 1108 HA2 GLY X 626 -2 .234 4 .132 9. .073 0. .00 0. .00 PROA

ATOM 1109 C GLY X 626 -0 .638 3 .782 10. .346 0. .00 0. .00 PROA

ATOM 1110 O GLY X 626 -0 .539 4 .900 10. .832 0. .00 0. .00 PROA

ATOM 1111 N PHE X 627 -0 .122 2 .750 11. .027 0. .00 0. .00 PROA

ATOM 1112 HN PHE X 627 -0 .159 1 .816 10. .681 0. .00 0. .00 PROA

ATOM 1113 CA PHE X 627 0. .728 2 .762 12. .246 0. .00 0. .00 PROA

ATOM 1114 HA PHE X 627 0. .966 1 .708 12. .265 0. .00 0. .00 PROA

ATOM 1115 CB PHE X 627 2. .195 3 .275 12. .073 0. .00 0. .00 PROA

ATOM 1116 HB1 PHE X 627 2 .915 2 .582 12. .558 0. .00 0. .00 PROA

ATOM 1117 HB2 PHE X 627 2 .374 3 .324 10. .978 0. .00 0. .00 PROA

ATOM 1118 CG PHE X 627 2. .437 4 .666 12. .676 0. .00 0. .00 PROA

ATOM 1119 CD1 PHE X 627 2 .602 4 .919 14. .040 0. .00 0. .00 PROA

ATOM 1120 HD1 PHE X 627 2 .536 4 .056 14. .686 0. .00 0. .00 PROA

ATOM 1121 CE1 PHE X 627 2 .874 6 .194 14. .471 0. .00 0. .00 PROA ATOM 1122 HE1 PHE X 627 3.058 6.425 15..510 0..00 0..00 PROA

ATOM 1123 CZ PHE X 627 3. .091 7 .234 13. .518 0. .00 0. .00 PROA

ATOM 1124 HZ PHE X 627 3. .264 8 .246 13. .853 0. .00 0. .00 PROA

ATOM 1125 CD2 PHE X 627 2 .504 5 .650 11. .745 0. .00 0. .00 PROA

ATOM 1126 HD2 PHE X 627 2 .448 5 .574 10. .669 0. .00 0. .00 PROA

ATOM 1127 CE2 PHE X 627 2 .956 6 .919 12. .141 0. .00 0. .00 PROA

ATOM 1128 HE2 PHE X 627 3 .114 7 .597 11. .315 0. .00 0. .00 PROA

ATOM 1129 C PHE X 627 0. .048 2 .977 13. .599 0. .00 0. .00 PROA

ATOM 1130 O PHE X 627 0. .591 2 .481 14. .594 0. .00 0. .00 PROA

ATOM 1131 N GLY X 628 -1 .193 3 .673 13. .705 0. .00 0. .00 PROA

ATOM 1132 HN GLY X 628 -1 .508 4 .285 12. .983 0. .00 0. .00 PROA

ATOM 1133 CA GLY X 628 -2 .013 3 .461 14. .926 0. .00 0. .00 PROA

ATOM 1134 HA1 GLY X 628 -1 .925 2 .388 15. .012 0. .00 0. .00 PROA

ATOM 1135 HA2 GLY X 628 -3 .009 3 .797 14. .677 0. .00 0. .00 PROA

ATOM 1136 C GLY X 628 -1 .722 4 .396 16. .035 0. .00 0. .00 PROA

ATOM 1137 O GLY X 628 -2 .290 4 .329 17. .123 0. .00 0. .00 PROA

ATOM 1138 N ASN X 629 -0 .821 5 .396 15. .876 0. .00 0. .00 PROA

ATOM 1139 HN ASN X 629 -0 .307 5 .587 15. .043 0. .00 0. .00 PROA

ATOM 1140 CA ASN X 629 -0 .878 6 .561 16. .776 0. .00 0. .00 PROA

ATOM 1141 HA ASN X 629 -1 .588 6 .395 17. .572 0. .00 0. .00 PROA

ATOM 1142 CB ASN X 629 0. .462 6 .954 17. .314 0. .00 0. .00 PROA

ATOM 1143 HB1 ASN X 629 1 .163 7 .282 16. .517 0. .00 0. .00 PROA

ATOM 1144 HB2 ASN X 629 0 .305 7 .745 18. .078 0. .00 0. .00 PROA

ATOM 1145 CG ASN X 629 1. .293 5 .932 18. .107 0. .00 0. .00 PROA

ATOM 1146 OD1 ASN X 629 2 .456 5 .750 17. .820 0. .00 0. .00 PROA

ATOM 1147 ND2 ASN X 629 0 .772 5 .454 19. .262 0. .00 0. .00 PROA

ATOM 1148 HD21 ASN X 629 1 .450 5 .251 19. .969 0. .00 0. .00 PROA

ATOM 1149 HD22 ASN X 629 -0 .194 5 .446 19. .521 0. .00 0. .00 PROA

ATOM 1150 C ASN X 629 -1 .363 7 .752 15. .986 0. .00 0. .00 PROA

ATOM 1151 O ASN X 629 -1 .297 8 .874 16. .466 0. .00 0. .00 PROA

ATOM 1152 N VAL X 630 -1 .788 7 .588 14. .710 0. .00 0. .00 PROA

ATOM 1153 HN VAL X 630 -1 .817 6 .661 14. .344 0. .00 0. .00 PROA

ATOM 1154 CA VAL X 630 -2 .227 8 .641 13. .883 0. .00 0. .00 PROA

ATOM 1155 HA VAL X 630 -1 .746 9 .565 14. .167 0. .00 0. .00 PROA

ATOM 1156 CB VAL X 630 -1 .824 8 .353 12. .444 0. .00 0. .00 PROA

ATOM 1157 HB VAL X 630 -2 .049 9 .209 11. .772 0. .00 0. .00 PROA

ATOM 1158 CGI VAL X 630 -0 .304 8 .175 12. .345 0. .00 0. .00 PROA

ATOM 1159 HG11 VAL X 630 -0 .117 8 .137 11. .250 0. .00 0. .00 PROA

ATOM 1160 HG12 VAL X 630 0 .276 9 .001 12. .809 0. .00 0. .00 PROA

ATOM 1161 HG13 VAL X 630 0 .007 7 .196 12. .768 0. .00 0. .00 PROA

ATOM 1162 CG2 VAL X 630 -2 .595 7 .067 11. .912 0. .00 0. .00 PROA

ATOM 1163 HG21 VAL X 630 -2 .156 6 .099 12. .237 0. .00 0. .00 PROA

ATOM 1164 HG22 VAL X 630 -3 .693 7 .127 12. .069 0. .00 0. .00 PROA

ATOM 1165 HG23 VAL X 630 -2 .324 6 .982 10. .838 0. .00 0. .00 PROA

ATOM 1166 C VAL X 630 -3 .722 8 .885 13. .906 0. .00 0. .00 PROA

ATOM 1167 O VAL X 630 -4 .354 9 .539 13. .100 0. .00 0. .00 PROA

ATOM 1168 N SER X 631 -4 .446 8 .127 14. .710 0. .00 0. .00 PROA

ATOM 1169 HN SER X 631 -3 .983 7 .679 15. .471 0. .00 0. .00 PROA

ATOM 1170 CA SER X 631 -5 .841 7 .908 14. .750 0. .00 0. .00 PROA

ATOM 1171 HA SER X 631 -6 .064 7 .601 13. .739 0. .00 0. .00 PROA

ATOM 1172 CB SER X 631 -6 .337 6 .654 15. .652 0. .00 0. .00 PROA

ATOM 1173 HB1 SER X 631 -6 .129 6 .817 16. .732 0. .00 0. .00 PROA

ATOM 1174 HB2 SER X 631 -7 .415 6 .517 15. .421 0. .00 0. .00 PROA

ATOM 1175 OG SER X 631 -5 .518 5 .613 15. .142 0. .00 0. .00 PROA

ATOM 1176 HG1 SER X 631 -5 .324 5 .006 15. .860 0. .00 0. .00 PROA

ATOM 1177 C SER X 631 -6 .742 9 .032 15. .115 0. .00 0. .00 PROA

ATOM 1178 O SER X 631 -6 .385 9 .865 15. .929 0. .00 0. .00 PROA

ATOM 1179 N PRO X 632 -7 .985 9 .167 14. .521 0. .00 0. .00 PROA

ATOM 1180 CD PRO X 632 -8 .393 8 .515 13. .223 0. .00 0. .00 PROA

ATOM 1181 HD1 PRO X 632 -7 .645 8 .459 12. .404 0. .00 0. .00 PROA

ATOM 1182 HD2 PRO X 632 -8 .674 7 .476 13. .497 0. .00 0. .00 PROA

ATOM 1183 CA PRO X 632 -8 .958 10 .088 15. .070 0. .00 0. .00 PROA

ATOM 1184 HA PRO X 632 -8 .610 11 .101 14. .935 0. .00 0. .00 PROA

ATOM 1185 CB PRO X 632 -10 .226 9 .827 14. .167 0. .00 0. .00 PROA

ATOM 1186 HB1 PRO X 632 -10 .850 10 .744 14. .093 0. .00 0. .00 PROA

ATOM 1187 HB2 PRO X 632 -10 .751 8 .975 14. .650 0. .00 0. .00 PROA ATOM 1188 CG PRO X 632 -9.676 9.226 12..850 0..00 0..00 PROA

ATOM 1189 HG1 PRO X 632 -9 .288 10 .178 12. .429 0. .00 0. .00 PROA

ATOM 1190 HG2 PRO X 632 -10 .344 8 .651 12. .173 0. .00 0. .00 PROA

ATOM 1191 C PRO X 632 -9 .238 10 .187 16. .567 0. .00 0. .00 PROA

ATOM 1192 O PRO X 632 -9 .402 9 .134 17. .158 0. .00 0. .00 PROA

ATOM 1193 N ASN X 633 -9 .459 11 .410 17. .096 0. .00 0. .00 PROA

ATOM 1194 HN ASN X 633 -9 .668 12 .153 16. .466 0. .00 0. .00 PROA

ATOM 1195 CA ASN X 633 -9 .546 11 .601 18. .607 0. .00 0. .00 PROA

ATOM 1196 HA ASN X 633 -9 .223 10 .708 19. .122 0. .00 0. .00 PROA

ATOM 1197 CB ASN X 633 -8 .712 12 .784 19. .054 0. .00 0. .00 PROA

ATOM 1198 HB1 ASN X 633 -8 .861 13 .629 18. .348 0. .00 0. .00 PROA

ATOM 1199 HB2 ASN X 633 -8 .996 13 .167 20. .058 0. .00 0. .00 PROA

ATOM 1200 CG ASN X 633 -7 .269 12 .361 19. .082 0. .00 0. .00 PROA

ATOM 1201 OD1 ASN X 633 -6 .521 13 .178 18. .537 0. .00 0. .00 PROA

ATOM 1202 ND2 ASN X 633 -6 .816 11 .305 19. .823 0. .00 0. .00 PROA

ATOM 1203 HD21 ASN X 633 -5 .827 11 .302 19. .970 0. .00 0. .00 PROA

ATOM 1204 HD22 ASN X 633 -7 .492 10 .799 20. .359 0. .00 0. .00 PROA

ATOM 1205 C ASN X 633 -10 .991 11 .946 19. .083 0. .00 0. .00 PROA

ATOM 1206 O ASN X 633 -11 .246 12 .091 20. .287 0. .00 0. .00 PROA

ATOM 1207 N THR X 634 -11 .975 12 .051 18. .179 0. .00 0. .00 PROA

ATOM 1208 HN THR X 634 -11 .750 11 .934 17. .214 0. .00 0. .00 PROA

ATOM 1209 CA THR X 634 -13 .329 12 .292 18. .623 0. .00 0. .00 PROA

ATOM 1210 HA THR X 634 -13 .411 11 .708 19. .527 0. .00 0. .00 PROA

ATOM 1211 CB THR X 634 -13 .620 13 .677 18. .952 0. .00 0. .00 PROA

ATOM 1212 HB THR X 634 -12 .818 14 .088 19. .602 0. .00 0. .00 PROA

ATOM 1213 OG1 THR X 634 -14 .779 13 .663 19. .817 0. .00 0. .00 PROA

ATOM 1214 HG1 THR X 634 -14 .485 14 .192 20. .562 0. .00 0. .00 PROA

ATOM 1215 CG2 THR X 634 -13 .858 14 .563 17. .676 0. .00 0. .00 PROA

ATOM 1216 HG21 THR X 634 -14 .639 14 .174 16. .988 0. .00 0. .00 PROA

ATOM 1217 HG22 THR X 634 -14 .150 15 .594 17. .971 0. .00 0. .00 PROA

ATOM 1218 HG23 THR X 634 -12 .911 14 .566 17. .094 0. .00 0. .00 PROA

ATOM 1219 C THR X 634 -14 .309 11 .739 17. .517 0. .00 0. .00 PROA

ATOM 1220 O THR X 634 -13 .896 11 .556 16. .392 0. .00 0. .00 PROA

ATOM 1221 N ASN X 635 -15 .608 11 .451 17. .848 0. .00 0. .00 PROA

ATOM 1222 HN ASN X 635 -15 .835 11 .542 18. .815 0. .00 0. .00 PROA

ATOM 1223 CA ASN X 635 -16 .610 10 .861 16. .988 0. .00 0. .00 PROA

ATOM 1224 HA ASN X 635 -16 .189 9 .951 16. .587 0. .00 0. .00 PROA

ATOM 1225 CB ASN X 635 -17 .853 10 .584 17. .842 0. .00 0. .00 PROA

ATOM 1226 HB1 ASN X 635 -17 .456 9 .979 18. .685 0. .00 0. .00 PROA

ATOM 1227 HB2 ASN X 635 -18 .337 11 .487 18. .273 0. .00 0. .00 PROA

ATOM 1228 CG ASN X 635 -18 .904 9 .750 17. .209 0. .00 0. .00 PROA

ATOM 1229 OD1 ASN X 635 -18 .685 8 .759 16. .511 0. .00 0. .00 PROA

ATOM 1230 ND2 ASN X 635 -20 .165 10 .206 17. .318 0. .00 0. .00 PROA

ATOM 1231 HD21 ASN X 635 -20 .927 9 .611 17. .064 0. .00 0. .00 PROA

ATOM 1232 HD22 ASN X 635 -20 .312 11 .032 17. .863 0. .00 0. .00 PROA

ATOM 1233 C ASN X 635 -16 .985 11 .674 15. .693 0. .00 0. .00 PROA

ATOM 1234 O ASN X 635 -16 .950 11 .081 14. .660 0. .00 0. .00 PROA

ATOM 1235 N SER X 636 -17 .208 12 .987 15. .743 0. .00 0. .00 PROA

ATOM 1236 HN SER X 636 -17 .219 13 .378 16. .660 0. .00 0. .00 PROA

ATOM 1237 CA SER X 636 -17 .393 13 .868 14. .599 0. .00 0. .00 PROA

ATOM 1238 HA SER X 636 -18 .247 13 .517 14. .040 0. .00 0. .00 PROA

ATOM 1239 CB SER X 636 -17 .560 15 .314 14. .982 0. .00 0. .00 PROA

ATOM 1240 HB1 SER X 636 -17 .502 15 .935 14. .062 0. .00 0. .00 PROA

ATOM 1241 HB2 SER X 636 -18 .560 15 .557 15. .399 0. .00 0. .00 PROA

ATOM 1242 OG SER X 636 -16 .538 15 .840 15. .847 0. .00 0. .00 PROA

ATOM 1243 HG1 SER X 636 -16 .775 16 .726 16. .130 0. .00 0. .00 PROA

ATOM 1244 C SER X 636 -16 .236 13 .653 13. .593 0. .00 0. .00 PROA

ATOM 1245 O SER X 636 -16 .499 13 .321 12. .437 0. .00 0. .00 PROA

ATOM 1246 N GLU X 637 -14 .935 13 .783 14. .042 0. .00 0. .00 PROA

ATOM 1247 HN GLU X 637 -14 .614 14 .258 14. .857 0. .00 0. .00 PROA

ATOM 1248 CA GLU X 637 -13 .778 13 .355 13. .290 0. .00 0. .00 PROA

ATOM 1249 HA GLU X 637 -13 .688 14 .056 12. .473 0. .00 0. .00 PROA

ATOM 1250 CB GLU X 637 -12 .571 13 .656 14. .106 0. .00 0. .00 PROA

ATOM 1251 HB1 GLU X 637 -12 .698 14 .680 14. .520 0. .00 0. .00 PROA

ATOM 1252 HB2 GLU X 637 -12 .444 12 .929 14. .936 0. .00 0. .00 PROA

ATOM 1253 CG GLU X 637 -11 .264 13 .581 13. .267 0. .00 0. .00 PROA ATOM 1254 HG1 GLU X 637 -11.093 12.698 12..616 0..00 0..00 PROA

ATOM 1255 HG2 GLU X 637 -11 .309 14 .528 12. .688 0. .00 0. .00 PROA

ATOM 1256 CD GLU X 637 -10 .113 13 .733 14. .161 0. .00 0. .00 PROA

ATOM 1257 OE1 GLU X 637 -10 .123 13 .602 15. .375 0. .00 0. .00 PROA

ATOM 1258 OE2 GLU X 637 -9 .051 14 .067 13. .519 0. .00 0. .00 PROA

ATOM 1259 C GLU X 637 -13 .728 11 .905 12. .745 0. .00 0. .00 PROA

ATOM 1260 O GLU X 637 -13 .332 11 .721 11. .621 0. .00 0. .00 PROA

ATOM 1261 N LYS X 638 -14 .200 10 .907 13. .603 0. .00 0. .00 PROA

ATOM 1262 HN LYS X 638 -14 .481 11 .079 14. .544 0. .00 0. .00 PROA

ATOM 1263 CA LYS X 638 -14 .362 9 .527 13. .164 0. .00 0. .00 PROA

ATOM 1264 HA LYS X 638 -13 .413 9 .163 12. .801 0. .00 0. .00 PROA

ATOM 1265 CB LYS X 638 -14 .781 8 .604 14. .264 0. .00 0. .00 PROA

ATOM 1266 HB1 LYS X 638 -13 .938 8 .694 14. .983 0. .00 0. .00 PROA

ATOM 1267 HB2 LYS X 638 -15 .711 9 .039 14. .688 0. .00 0. .00 PROA

ATOM 1268 CG LYS X 638 -14 .928 7 .140 13. .871 0. .00 0. .00 PROA

ATOM 1269 HG1 LYS X 638 -15 .674 7 .053 13. .052 0. .00 0. .00 PROA

ATOM 1270 HG2 LYS X 638 -13 .964 6 .720 13. .514 0. .00 0. .00 PROA

ATOM 1271 CD LYS X 638 -15 .372 6 .087 14. .978 0. .00 0. .00 PROA

ATOM 1272 HD1 LYS X 638 -15 .252 5 .054 14. .588 0. .00 0. .00 PROA

ATOM 1273 HD2 LYS X 638 -14 .617 6 .125 15. .791 0. .00 0. .00 PROA

ATOM 1274 CE LYS X 638 -16 .723 6 .377 15. .561 0. .00 0. .00 PROA

ATOM 1275 HE1 LYS X 638 -16 .707 7 .237 16. .264 0. .00 0. .00 PROA

ATOM 1276 HE2 LYS X 638 -17 .456 6 .706 14. .793 0. .00 0. .00 PROA

ATOM 1277 NZ LYS X 638 -17 .335 5 .216 16. .237 0. .00 0. .00 PROA

ATOM 1278 HZ1 LYS X 638 -18 .054 5 .512 16. .927 0. .00 0. .00 PROA

ATOM 1279 HZ2 LYS X 638 -17 .806 4 .666 15. .490 0. .00 0. .00 PROA

ATOM 1280 HZ3 LYS X 638 -16 .650 4 .599 16. .719 0. .00 0. .00 PROA

ATOM 1281 C LYS X 638 -15 .296 9 .431 11. .989 0. .00 0. .00 PROA

ATOM 1282 O LYS X 638 -14 .998 8 .820 10. .978 0. .00 0. .00 PROA

ATOM 1283 N ILE X 639 -16 .476 10 .064 12. .103 0. .00 0. .00 PROA

ATOM 1284 HN ILE X 639 -16 .629 10 .640 12. .902 0. .00 0. .00 PROA

ATOM 1285 CA ILE X 639 -17 .571 10 .051 11. .075 0. .00 0. .00 PROA

ATOM 1286 HA ILE X 639 -17 .740 9 .033 10. .754 0. .00 0. .00 PROA

ATOM 1287 CB ILE X 639 -18 .892 10 .565 11. .616 0. .00 0. .00 PROA

ATOM 1288 HB ILE X 639 -18 .743 11 .637 11. .869 0. .00 0. .00 PROA

ATOM 1289 CG2 ILE X 639 -19 .899 10 .544 10. .385 0. .00 0. .00 PROA

ATOM 1290 HG21 ILE X 639 -20 .832 11 .010 10. .769 0. .00 0. .00 PROA

ATOM 1291 HG22 ILE X 639 -19 .614 11 .333 9. .657 0. .00 0. .00 PROA

ATOM 1292 HG23 ILE X 639 -20 .003 9 .484 10. .069 0. .00 0. .00 PROA

ATOM 1293 CGI ILE X 639 -19 .430 9 .655 12. .806 0. .00 0. .00 PROA

ATOM 1294 HG11 ILE X 639 -19 .982 8 .820 12. .324 0. .00 0. .00 PROA

ATOM 1295 HG12 ILE X 639 -18 .594 9 .346 13. .470 0. .00 0. .00 PROA

ATOM 1296 CD ILE X 639 -20 .457 10 .475 13. .565 0. .00 0. .00 PROA

ATOM 1297 HD1 ILE X 639 -20 .809 9 .983 14. .497 0. .00 0. .00 PROA

ATOM 1298 HD2 ILE X 639 -19 .942 11 .437 13. .770 0. .00 0. .00 PROA

ATOM 1299 HD3 ILE X 639 -21 .349 10 .677 12. .933 0. .00 0. .00 PROA

ATOM 1300 C ILE X 639 -17 .088 10 .739 9. .800 0. .00 0. .00 PROA

ATOM 1301 O ILE X 639 -17 .184 10 .246 8. .645 0. .00 0. .00 PROA

ATOM 1302 N PHE X 640 -16 .490 11 .937 9. .891 0. .00 0. .00 PROA

ATOM 1303 HN PHE X 640 -16 .267 12 .367 10. .762 0. .00 0. .00 PROA

ATOM 1304 CA PHE X 640 -16 .071 12 .692 8. .734 0. .00 0. .00 PROA

ATOM 1305 HA PHE X 640 -16 .957 12 .801 8. .127 0. .00 0. .00 PROA

ATOM 1306 CB PHE X 640 -15 .557 14 .123 9. .092 0. .00 0. .00 PROA

ATOM 1307 HB1 PHE X 640 -14 .602 14 .023 9. .652 0. .00 0. .00 PROA

ATOM 1308 HB2 PHE X 640 -15 .354 14 .718 8. .176 0. .00 0. .00 PROA

ATOM 1309 CG PHE X 640 -16 .611 15 .025 9. .752 0. .00 0. .00 PROA

ATOM 1310 CD1 PHE X 640 -16 .135 16 .108 10. .504 0. .00 0. .00 PROA

ATOM 1311 HD1 PHE X 640 -15 .088 16 .363 10. .576 0. .00 0. .00 PROA

ATOM 1312 CE1 PHE X 640 -17 .000 16 .972 11. .254 0. .00 0. .00 PROA

ATOM 1313 HE1 PHE X 640 -16 .649 17 .871 11. .738 0. .00 0. .00 PROA

ATOM 1314 CZ PHE X 640 -18 .389 16 .606 11. .328 0. .00 0. .00 PROA

ATOM 1315 HZ PHE X 640 -19 .121 17 .207 11. .846 0. .00 0. .00 PROA

ATOM 1316 CD2 PHE X 640 -18 .000 14 .790 9. .812 0. .00 0. .00 PROA

ATOM 1317 HD2 PHE X 640 -18 .416 13 .902 9. .358 0. .00 0. .00 PROA

ATOM 1318 CE2 PHE X 640 -18 .895 15 .577 10. .569 0. .00 0. .00 PROA

ATOM 1319 HE2 PHE X 640 -19 .917 15 .229 10. .554 0. .00 0. .00 PROA ATOM 1320 C PHE X 640 -14.774 11.964 8..044 0..00 0..00 PROA

ATOM 1321 O PHE X 640 -14 .523 12 .002 6. .879 0. .00 0. .00 PROA

ATOM 1322 N SER X 641 -13 .956 11 .201 8. .746 0. .00 0. .00 PROA

ATOM 1323 HN SER X 641 -13 .986 11 .031 9. .728 0. .00 0. .00 PROA

ATOM 1324 CA SER X 641 -12 .716 10 .556 8. .232 0. .00 0. .00 PROA

ATOM 1325 HA SER X 641 -12 .003 11 .288 7. .882 0. .00 0. .00 PROA

ATOM 1326 CB SER X 641 -11 .981 9 .743 9. .280 0. .00 0. .00 PROA

ATOM 1327 HB1 SER X 641 -11 .665 10 .369 10. .142 0. .00 0. .00 PROA

ATOM 1328 HB2 SER X 641 -12 .638 8 .914 9. .620 0. .00 0. .00 PROA

ATOM 1329 OG SER X 641 -10 .715 9 .242 8. .822 0. .00 0. .00 PROA

ATOM 1330 HG1 SER X 641 -10 .757 8 .365 9. .210 0. .00 0. .00 PROA

ATOM 1331 C SER X 641 -12 .998 9 .651 7. .050 0. .00 0. .00 PROA

ATOM 1332 O SER X 641 -12 .213 9 .604 6. .077 0. .00 0. .00 PROA

ATOM 1333 N ILE X 642 -14 .115 8 .944 7. .131 0. .00 0. .00 PROA

ATOM 1334 HN ILE X 642 -14 .739 9 .081 7. .896 0. .00 0. .00 PROA

ATOM 1335 CA ILE X 642 -14 .608 8 .057 6. .188 0. .00 0. .00 PROA

ATOM 1336 HA ILE X 642 -13 .908 7 .235 6. .148 0. .00 0. .00 PROA

ATOM 1337 CB ILE X 642 -15 .996 7 .433 6. .621 0. .00 0. .00 PROA

ATOM 1338 HB ILE X 642 -16 .660 8 .271 6. .921 0. .00 0. .00 PROA

ATOM 1339 CG2 ILE X 642 -16 .776 6 .654 5. .463 0. .00 0. .00 PROA

ATOM 1340 HG21 ILE X 642 -17 .625 6 .043 5. .836 0. .00 0. .00 PROA

ATOM 1341 HG22 ILE X 642 -16 .964 7 .462 4. .724 0. .00 0. .00 PROA

ATOM 1342 HG23 ILE X 642 -15 .963 5 .997 5. .086 0. .00 0. .00 PROA

ATOM 1343 CGI ILE X 642 -15 .790 6 .466 7. .831 0. .00 0. .00 PROA

ATOM 1344 HG11 ILE X 642 -15 .359 5 .492 7. .514 0. .00 0. .00 PROA

ATOM 1345 HG12 ILE X 642 -14 .942 6 .850 8. .437 0. .00 0. .00 PROA

ATOM 1346 CD ILE X 642 -16 .942 6 .202 8. .810 0. .00 0. .00 PROA

ATOM 1347 HD1 ILE X 642 -16 .735 6 .415 9. .880 0. .00 0. .00 PROA

ATOM 1348 HD2 ILE X 642 -17 .785 6 .890 8. .585 0. .00 0. .00 PROA

ATOM 1349 HD3 ILE X 642 -17 .265 5 .178 8. .526 0. .00 0. .00 PROA

ATOM 1350 C ILE X 642 -14 .750 8 .658 4. .756 0. .00 0. .00 PROA

ATOM 1351 O ILE X 642 -14 .174 8 .131 3. .789 0. .00 0. .00 PROA

ATOM 1352 N CYS X 643 -15 .434 9 .798 4. .685 0. .00 0. .00 PROA

ATOM 1353 HN CYS X 643 -15 .791 10 .284 5. .479 0. .00 0. .00 PROA

ATOM 1354 CA CYS X 643 -15 .676 10 .462 3. .425 0. .00 0. .00 PROA

ATOM 1355 HA CYS X 643 -15 .919 9 .622 2. .791 0. .00 0. .00 PROA

ATOM 1356 CB CYS X 643 -16 .893 11 .389 3. .481 0. .00 0. .00 PROA

ATOM 1357 HB1 CYS X 643 -16 .682 12 .282 4. .107 0. .00 0. .00 PROA

ATOM 1358 HB2 CYS X 643 -16 .999 11 .705 2. .421 0. .00 0. .00 PROA

ATOM 1359 C CYS X 643 -14 .455 11 .071 2. .781 0. .00 0. .00 PROA

ATOM 1360 O CYS X 643 -14 .192 10 .861 1. .631 0. .00 0. .00 PROA

ATOM 1361 N VAL X 644 -13 .649 11 .848 3. .628 0. .00 0. .00 PROA

ATOM 1362 HN VAL X 644 -13 .792 12 .126 4. .574 0. .00 0. .00 PROA

ATOM 1363 CA VAL X 644 -12 .433 12 .405 3. .159 0. .00 0. .00 PROA

ATOM 1364 HA VAL X 644 -12 .549 12 .977 2. .251 0. .00 0. .00 PROA

ATOM 1365 CB VAL X 644 -11 .777 13 .369 4. .229 0. .00 0. .00 PROA

ATOM 1366 HB VAL X 644 -10 .761 13 .635 3. .867 0. .00 0. .00 PROA

ATOM 1367 CGI VAL X 644 -12 .553 14 .633 4. .404 0. .00 0. .00 PROA

ATOM 1368 HG11 VAL X 644 -12 .648 15 .113 3. .406 0. .00 0. .00 PROA

ATOM 1369 HG12 VAL X 644 -13 .610 14 .387 4. .642 0. .00 0. .00 PROA

ATOM 1370 HG13 VAL X 644 -12 .131 15 .319 5. .169 0. .00 0. .00 PROA

ATOM 1371 CG2 VAL X 644 -11 .425 12 .850 5. .647 0. .00 0. .00 PROA

ATOM 1372 HG21 VAL X 644 -10 .605 13 .425 6. .128 0. .00 0. .00 PROA

ATOM 1373 HG22 VAL X 644 -12 .332 12 .858 6. .288 0. .00 0. .00 PROA

ATOM 1374 HG23 VAL X 644 -10 .970 11 .837 5. .687 0. .00 0. .00 PROA

ATOM 1375 C VAL X 644 -11 .432 11 .301 2. .749 0. .00 0. .00 PROA

ATOM 1376 O VAL X 644 -10 .763 11 .438 1. .726 0. .00 0. .00 PROA

ATOM 1377 N MET X 645 -11 .286 10 .149 3. .435 0. .00 0. .00 PROA

ATOM 1378 HN MET X 645 -11 .977 10 .049 4. .147 0. .00 0. .00 PROA

ATOM 1379 CA MET X 645 -10 .299 9 .066 3. .207 0. .00 0. .00 PROA

ATOM 1380 HA MET X 645 -9 .362 9 .524 2. .928 0. .00 0. .00 PROA

ATOM 1381 CB MET X 645 -10 .118 8 .002 4. .371 0. .00 0. .00 PROA

ATOM 1382 HB1 MET X 645 -9 .667 8 .594 5. .195 0. .00 0. .00 PROA

ATOM 1383 HB2 MET X 645 -11 .084 7 .553 4. .686 0. .00 0. .00 PROA

ATOM 1384 CG MET X 645 -9 .068 6 .925 4. .059 0. .00 0. .00 PROA

ATOM 1385 HG1 MET X 645 -9 .074 6 .707 2. .970 0. .00 0. .00 PROA ATOM 1386 HG2 MET X 645 -8.125 7.506 4..148 0..00 0..00 PROA

ATOM 1387 C MET X 645 -10 .697 8 .376 1. .865 0. .00 0. .00 PROA

ATOM 1388 O MET X 645 -9 .880 8 .222 0. .953 0. .00 0. .00 PROA

ATOM 1389 N LEU X 646 -11 .996 7 .919 1. .695 0. .00 0. .00 PROA

ATOM 1390 HN LEU X 646 -12 .603 7 .956 2. .485 0. .00 0. .00 PROA

ATOM 1391 CA LEU X 646 -12 .476 7 .299 0. .475 0. .00 0. .00 PROA

ATOM 1392 HA LEU X 646 -11 .888 6 .422 0. .249 0. .00 0. .00 PROA

ATOM 1393 CB LEU X 646 -13 .891 6 .629 0. .708 0. .00 0. .00 PROA

ATOM 1394 HB1 LEU X 646 -14 .583 7 .475 0. .909 0. .00 0. .00 PROA

ATOM 1395 HB2 LEU X 646 -14 .154 6 .157 -0. .262 0. .00 0. .00 PROA

ATOM 1396 CG LEU X 646 -13 .860 5 .681 1. .972 0. .00 0. .00 PROA

ATOM 1397 HG LEU X 646 -13 .402 6 .197 2. .843 0. .00 0. .00 PROA

ATOM 1398 CD1 LEU X 646 -15 .261 5 .248 2. .369 0. .00 0. .00 PROA

ATOM 1399 HD11 LEU X 646 -15 .822 6 .142 2. .718 0. .00 0. .00 PROA

ATOM 1400 HD12 LEU X 646 -15 .812 4 .660 1. .605 0. .00 0. .00 PROA

ATOM 1401 HD13 LEU X 646 -15 .224 4 .555 3. .237 0. .00 0. .00 PROA

ATOM 1402 CD2 LEU X 646 -12 .963 4 .524 1. .695 0. .00 0. .00 PROA

ATOM 1403 HD21 LEU X 646 -11 .933 4 .624 2. .099 0. .00 0. .00 PROA

ATOM 1404 HD22 LEU X 646 -13 .307 3 .642 2. .278 0. .00 0. .00 PROA

ATOM 1405 HD23 LEU X 646 -12 .842 4 .176 0. .647 0. .00 0. .00 PROA

ATOM 1406 C LEU X 646 -12 .350 8 .192 -0. .767 0. .00 0. .00 PROA

ATOM 1407 O LEU X 646 -12 .088 7 .778 -1. .921 0. .00 0. .00 PROA

ATOM 1408 N ILE X 647 -12 .506 9 .518 -0. .622 0. .00 0. .00 PROA

ATOM 1409 HN ILE X 647 -12 .716 9 .829 0. .302 0. .00 0. .00 PROA

ATOM 1410 CA ILE X 647 -12 .331 10 .538 -1. .675 0. .00 0. .00 PROA

ATOM 1411 HA ILE X 647 -12 .700 9 .984 -2. .525 0. .00 0. .00 PROA

ATOM 1412 CB ILE X 647 -13 .140 11 .799 -1. .640 0. .00 0. .00 PROA

ATOM 1413 HB ILE X 647 -13 .948 11 .563 -0. .915 0. .00 0. .00 PROA

ATOM 1414 CG2 ILE X 647 -12 .394 12 .945 -0. .872 0. .00 0. .00 PROA

ATOM 1415 HG21 ILE X 647 -11 .396 13 .250 -1. .252 0. .00 0. .00 PROA

ATOM 1416 HG22 ILE X 647 -13 .180 13 .729 -0. .828 0. .00 0. .00 PROA

ATOM 1417 HG23 ILE X 647 -12 .287 12 .591 0. .175 0. .00 0. .00 PROA

ATOM 1418 CGI ILE X 647 -13 .735 12 .333 -2. .914 0. .00 0. .00 PROA

ATOM 1419 HG11 ILE X 647 -12 .991 12 .850 -3. .556 0. .00 0. .00 PROA

ATOM 1420 HG12 ILE X 647 -14 .060 11 .454 -3. .511 0. .00 0. .00 PROA

ATOM 1421 CD ILE X 647 -14 .924 13 .373 -2. .821 0. .00 0. .00 PROA

ATOM 1422 HD1 ILE X 647 -15 .253 13 .621 -3. .853 0. .00 0. .00 PROA

ATOM 1423 HD2 ILE X 647 -15 .838 13 .011 -2. .304 0. .00 0. .00 PROA

ATOM 1424 HD3 ILE X 647 -14 .482 14 .283 -2. .361 0. .00 0. .00 PROA

ATOM 1425 C ILE X 647 -10 .879 10 .877 -1. .970 0. .00 0. .00 PROA

ATOM 1426 O ILE X 647 -10 .472 11 .024 -3. .166 0. .00 0. .00 PROA

ATOM 1427 N GLY X 648 -9 .958 10 .778 -1. .026 0. .00 0. .00 PROA

ATOM 1428 HN GLY X 648 -10 .359 10 .468 -0. .167 0. .00 0. .00 PROA

ATOM 1429 CA GLY X 648 -8 .496 10 .832 -1. .177 0. .00 0. .00 PROA

ATOM 1430 HA1 GLY X 648 -8 .180 10 .875 -0. .145 0. .00 0. .00 PROA

ATOM 1431 HA2 GLY X 648 -8 .174 11 .708 -1. .721 0. .00 0. .00 PROA

ATOM 1432 C GLY X 648 -7 .809 9 .657 -1. .923 0. .00 0. .00 PROA

ATOM 1433 O GLY X 648 -6 .843 9 .744 -2. .719 0. .00 0. .00 PROA

ATOM 1434 N SER X 649 -8 .472 8 .585 -1. .752 0. .00 0. .00 PROA

ATOM 1435 HN SER X 649 -9 .257 8 .578 -1. .137 0. .00 0. .00 PROA

ATOM 1436 CA SER X 649 -8 .049 7 .276 -2. .202 0. .00 0. .00 PROA

ATOM 1437 HA SER X 649 -7 .030 7 .131 -1. .873 0. .00 0. .00 PROA

ATOM 1438 CB SER X 649 -8 .943 6 .201 -1. .601 0. .00 0. .00 PROA

ATOM 1439 HB1 SER X 649 -9 .109 6 .419 -0. .524 0. .00 0. .00 PROA

ATOM 1440 HB2 SER X 649 -9 .964 6 .313 -2. .024 0. .00 0. .00 PROA

ATOM 1441 OG SER X 649 -8 .372 4 .882 -1. .708 0. .00 0. .00 PROA

ATOM 1442 HG1 SER X 649 -9 .055 4 .303 -1. .361 0. .00 0. .00 PROA

ATOM 1443 C SER X 649 -8 .092 7 .194 -3. .716 0. .00 0. .00 PROA

ATOM 1444 O SER X 649 -7 .117 6 .888 -4. .407 0. .00 0. .00 PROA

ATOM 1445 N LEU X 650 -9 .246 7 .595 -4. .290 0. .00 0. .00 PROA

ATOM 1446 HN LEU X 650 -10 .013 7 .828 -3. .697 0. .00 0. .00 PROA

ATOM 1447 CA LEU X 650 -9 .361 7 .578 -5. .710 0. .00 0. .00 PROA

ATOM 1448 HA LEU X 650 -9 .019 6 .653 -6. .148 0. .00 0. .00 PROA

ATOM 1449 CB LEU X 650 -10 .874 7 .594 -6. .205 0. .00 0. .00 PROA

ATOM 1450 HB1 LEU X 650 -10 .818 7 .472 -7. .308 0. .00 0. .00 PROA

ATOM 1451 HB2 LEU X 650 -11 .274 6 .710 -5. .664 0. .00 0. .00 PROA ATOM 1452 CG LEU X 650 -11.857 8.712 -5..786 0..00 0..00 PROA

ATOM 1453 HG LEU X 650 -11 .507 8 .884 -4. .746 0. .00 0. .00 PROA

ATOM 1454 CD1 LEU X 650 -11 .561 10 .015 -6. .480 0. .00 0. .00 PROA

ATOM 1455 HD11 LEU X 650 -12 .511 10 .539 -6. .719 0. .00 0. .00 PROA

ATOM 1456 HD12 LEU X 650 -10 .826 10 .672 -5. .967 0. .00 0. .00 PROA

ATOM 1457 HD13 LEU X 650 -11 .139 9 .772 -7. .479 0. .00 0. .00 PROA

ATOM 1458 CD2 LEU X 650 -13 .364 8 .483 -5. .709 0. .00 0. .00 PROA

ATOM 1459 HD21 LEU X 650 -13 .790 9 .388 -5. .228 0. .00 0. .00 PROA

ATOM 1460 HD22 LEU X 650 -13 .842 8 .358 -6. .704 0. .00 0. .00 PROA

ATOM 1461 HD23 LEU X 650 -13 .662 7 .665 -5. .019 0. .00 0. .00 PROA

ATOM 1462 C LEU X 650 -8 .505 8 .622 -6. .443 0. .00 0. .00 PROA

ATOM 1463 O LEU X 650 -7 .991 8 .399 -7. .506 0. .00 0. .00 PROA

ATOM 1464 N MET X 651 -8 .238 9 .758 -5. .797 0. .00 0. .00 PROA

ATOM 1465 HN MET X 651 -8 .579 9 .781 -4. .860 0. .00 0. .00 PROA

ATOM 1466 CA MET X 651 -7 .307 10 .761 -6. .237 0. .00 0. .00 PROA

ATOM 1467 HA MET X 651 -7 .529 10 .959 -7. .275 0. .00 0. .00 PROA

ATOM 1468 CB MET X 651 -7 .518 12 .054 -5. .385 0. .00 0. .00 PROA

ATOM 1469 HB1 MET X 651 -8 .599 12 .302 -5. .331 0. .00 0. .00 PROA

ATOM 1470 HB2 MET X 651 -7 .133 11 .902 -4. .354 0. .00 0. .00 PROA

ATOM 1471 CG MET X 651 -6 .779 13 .199 -6. .056 0. .00 0. .00 PROA

ATOM 1472 HG1 MET X 651 -5 .885 12 .853 -6. .617 0. .00 0. .00 PROA

ATOM 1473 HG2 MET X 651 -7 .529 13 .572 -6. .785 0. .00 0. .00 PROA

ATOM 1474 C MET X 651 -5 .892 10 .299 -6. .224 0. .00 0. .00 PROA

ATOM 1475 O MET X 651 -5 .277 10 .497 -7. .221 0. .00 0. .00 PROA

ATOM 1476 N TYR X 652 -5 .386 9 .682 -5. .132 0. .00 0. .00 PROA

ATOM 1477 HN TYR X 652 -5 .833 9 .614 -4. .243 0. .00 0. .00 PROA

ATOM 1478 CA TYR X 652 -4 .052 9 .124 -5. .093 0. .00 0. .00 PROA

ATOM 1479 HA TYR X 652 -3 .312 9 .806 -5. .485 0. .00 0. .00 PROA

ATOM 1480 CB TYR X 652 -3 .558 8 .577 -3. .705 0. .00 0. .00 PROA

ATOM 1481 HB1 TYR X 652 -4 .140 9 .133 -2. .939 0. .00 0. .00 PROA

ATOM 1482 HB2 TYR X 652 -3 .592 7 .470 -3. .624 0. .00 0. .00 PROA

ATOM 1483 CG TYR X 652 -2 .129 8 .871 -3. .548 0. .00 0. .00 PROA

ATOM 1484 CD1 TYR X 652 -1 .230 7 .846 -3. .827 0. .00 0. .00 PROA

ATOM 1485 HD1 TYR X 652 -1 .595 6 .914 -4. .234 0. .00 0. .00 PROA

ATOM 1486 CE1 TYR X 652 0 .123 7 .976 -3. .488 0. .00 0. .00 PROA

ATOM 1487 HE1 TYR X 652 0 .771 7 .123 -3. .625 0. .00 0. .00 PROA

ATOM 1488 CZ TYR X 652 0. .576 9 .216 -3. .065 0. .00 0. .00 PROA

ATOM 1489 OH TYR X 652 1. .914 9 .489 -2. .775 0. .00 0. .00 PROA

ATOM 1490 HH TYR X 652 2. .408 8 .670 -2. .866 0. .00 0. .00 PROA

ATOM 1491 CD2 TYR X 652 -1 .711 10 .134 -3. .122 0. .00 0. .00 PROA

ATOM 1492 HD2 TYR X 652 -2 .446 10 .901 -2. .925 0. .00 0. .00 PROA

ATOM 1493 CE2 TYR X 652 -0 .330 10 .244 -2. .822 0. .00 0. .00 PROA

ATOM 1494 HE2 TYR X 652 0 .098 11 .189 -2. .522 0. .00 0. .00 PROA

ATOM 1495 C TYR X 652 -3 .840 8 .068 -6. .130 0. .00 0. .00 PROA

ATOM 1496 O TYR X 652 -2 .872 8 .147 -6. .846 0. .00 0. .00 PROA

ATOM 1497 N ALA X 653 -4 .750 7 .105 -6. .278 0. .00 0. .00 PROA

ATOM 1498 HN ALA X 653 -5 .464 6 .976 -5. .594 0. .00 0. .00 PROA

ATOM 1499 CA ALA X 653 -4 .693 6 .065 -7. .283 0. .00 0. .00 PROA

ATOM 1500 HA ALA X 653 -3 .822 5 .451 -7. .108 0. .00 0. .00 PROA

ATOM 1501 CB ALA X 653 -5 .904 5 .206 -7. .122 0. .00 0. .00 PROA

ATOM 1502 HB1 ALA X 653 -5 .790 4 .497 -6. .274 0. .00 0. .00 PROA

ATOM 1503 HB2 ALA X 653 -6 .833 5 .805 -7. .014 0. .00 0. .00 PROA

ATOM 1504 HB3 ALA X 653 -6 .014 4 .598 -8. .045 0. .00 0. .00 PROA

ATOM 1505 C ALA X 653 -4 .595 6 .606 -8. .699 0. .00 0. .00 PROA

ATOM 1506 O ALA X 653 -3 .801 6 .231 -9. .549 0. .00 0. .00 PROA

ATOM 1507 N SER X 654 -5 .432 7 .580 -9. .043 0. .00 0. .00 PROA

ATOM 1508 HN SER X 654 -6 .183 7 .893 -8. .468 0. .00 0. .00 PROA

ATOM 1509 CA SER X 654 -5 .391 8 .208 -10. .380 0. .00 0. .00 PROA

ATOM 1510 HA SER X 654 -5 .480 7 .416 -11. .110 0. .00 0. .00 PROA

ATOM 1511 CB SER X 654 -6 .432 9 .213 -10. .608 0. .00 0. .00 PROA

ATOM 1512 HB1 SER X 654 -6 .347 9 .672 -11. .616 0. .00 0. .00 PROA

ATOM 1513 HB2 SER X 654 -7 .388 8 .698 -10. .840 0. .00 0. .00 PROA

ATOM 1514 OG SER X 654 -6 .631 10 .309 -9. .706 0. .00 0. .00 PROA

ATOM 1515 HG1 SER X 654 -6 .623 9 .960 -8. .811 0. .00 0. .00 PROA

ATOM 1516 C SER X 654 -4 .097 8 .919 -10. .761 0. .00 0. .00 PROA

ATOM 1517 O SER X 654 -3 .583 8 .837 -11. .872 0. .00 0. .00 PROA ATOM 1518 N ILE X 655 -3.614 9.802 -9..874 0..00 0..00 PROA

ATOM 1519 HN ILE X 655 -4 .197 10 .171 -9. .154 0. .00 0. .00 PROA

ATOM 1520 CA ILE X 655 -2 .326 10 .508 -10. .098 0. .00 0. .00 PROA

ATOM 1521 HA ILE X 655 -2 .551 11 .025 -11. .019 0. .00 0. .00 PROA

ATOM 1522 CB ILE X 655 -1 .999 11 .655 -9. .099 0. .00 0. .00 PROA

ATOM 1523 HB ILE X 655 -1 .112 12 .183 -9. .511 0. .00 0. .00 PROA

ATOM 1524 CG2 ILE X 655 -3 .061 12 .653 -9. .109 0. .00 0. .00 PROA

ATOM 1525 HG21 ILE X 655 -3 .899 12 .587 -8. .381 0. .00 0. .00 PROA

ATOM 1526 HG22 ILE X 655 -2 .596 13 .640 -8. .902 0. .00 0. .00 PROA

ATOM 1527 HG23 ILE X 655 -3 .576 12 .748 -10. .089 0. .00 0. .00 PROA

ATOM 1528 CGI ILE X 655 -1 .664 11 .175 -7. .696 0. .00 0. .00 PROA

ATOM 1529 HG11 ILE X 655 -2 .539 10 .682 -7. .223 0. .00 0. .00 PROA

ATOM 1530 HG12 ILE X 655 -0 .824 10 .452 -7. .621 0. .00 0. .00 PROA

ATOM 1531 CD ILE X 655 -1 .300 12 .321 -6. .783 0. .00 0. .00 PROA

ATOM 1532 HD1 ILE X 655 -1 .868 13 .260 -6. .955 0. .00 0. .00 PROA

ATOM 1533 HD2 ILE X 655 -1 .123 12 .131 -5. .702 0. .00 0. .00 PROA

ATOM 1534 HD3 ILE X 655 -0 .367 12 .818 -7. .125 0. .00 0. .00 PROA

ATOM 1535 C ILE X 655 -1 .171 9 .529 -10. .242 0. .00 0. .00 PROA

ATOM 1536 O ILE X 655 -0 .322 9 .649 -11. .156 0. .00 0. .00 PROA

ATOM 1537 N PHE X 656 -1 .069 8 .577 -9. .285 0. .00 0. .00 PROA

ATOM 1538 HN PHE X 656 -1 .757 8 .600 -8. .565 0. .00 0. .00 PROA

ATOM 1539 CA PHE X 656 0. .010 7 .584 -9. .262 0. .00 0. .00 PROA

ATOM 1540 HA PHE X 656 0. .959 8 .095 -9. .327 0. .00 0. .00 PROA

ATOM 1541 CB PHE X 656 -0 .009 6 .758 -7. .861 0. .00 0. .00 PROA

ATOM 1542 HB1 PHE X 656 -0 .375 7 .473 -7. .094 0. .00 0. .00 PROA

ATOM 1543 HB2 PHE X 656 -0 .553 5 .791 -7. .917 0. .00 0. .00 PROA

ATOM 1544 CG PHE X 656 1. .394 6 .431 -7. .553 0. .00 0. .00 PROA

ATOM 1545 CD1 PHE X 656 1 .840 5 .113 -7. .819 0. .00 0. .00 PROA

ATOM 1546 HD1 PHE X 656 1 .202 4 .453 -8. .388 0. .00 0. .00 PROA

ATOM 1547 CE1 PHE X 656 3 .145 4 .697 -7. .433 0. .00 0. .00 PROA

ATOM 1548 HE1 PHE X 656 3 .507 3 .680 -7. .440 0. .00 0. .00 PROA

ATOM 1549 CZ PHE X 656 3. .924 5 .621 -6. .675 0. .00 0. .00 PROA

ATOM 1550 HZ PHE X 656 4. .862 5 .320 -6. .234 0. .00 0. .00 PROA

ATOM 1551 CD2 PHE X 656 2 .310 7 .377 -6. .940 0. .00 0. .00 PROA

ATOM 1552 HD2 PHE X 656 1 .872 8 .295 -6. .575 0. .00 0. .00 PROA

ATOM 1553 CE2 PHE X 656 3 .583 6 .951 -6. .506 0. .00 0. .00 PROA

ATOM 1554 HE2 PHE X 656 4 .161 7 .720 -6. .014 0. .00 0. .00 PROA

ATOM 1555 C PHE X 656 0. .070 6 .664 -10. .491 0. .00 0. .00 PROA

ATOM 1556 O PHE X 656 1. .089 6 .248 -11. .023 0. .00 0. .00 PROA

ATOM 1557 N GLY X 657 -1 .085 6 .502 -11. .139 0. .00 0. .00 PROA

ATOM 1558 HN GLY X 657 -1 .865 6 .969 -10. .731 0. .00 0. .00 PROA

ATOM 1559 CA GLY X 657 -1 .249 5 .659 -12. .308 0. .00 0. .00 PROA

ATOM 1560 HA1 GLY X 657 -2 .277 5 .345 -12. .412 0. .00 0. .00 PROA

ATOM 1561 HA2 GLY X 657 -0 .698 4 .738 -12. .184 0. .00 0. .00 PROA

ATOM 1562 C GLY X 657 -0 .829 6 .417 -13. .578 0. .00 0. .00 PROA

ATOM 1563 O GLY X 657 -0 .253 5 .812 -14. .488 0. .00 0. .00 PROA

ATOM 1564 N ASN X 658 -0 .947 7 .716 -13. .658 0. .00 0. .00 PROA

ATOM 1565 HN ASN X 658 -1 .399 8 .205 -12. .915 0. .00 0. .00 PROA

ATOM 1566 CA ASN X 658 -0 .474 8 .557 -14. .741 0. .00 0. .00 PROA

ATOM 1567 HA ASN X 658 -0 .729 8 .206 -15. .730 0. .00 0. .00 PROA

ATOM 1568 CB ASN X 658 -1 .116 10 .009 -14. .571 0. .00 0. .00 PROA

ATOM 1569 HB1 ASN X 658 -1 .132 10 .386 -13. .526 0. .00 0. .00 PROA

ATOM 1570 HB2 ASN X 658 -0 .433 10 .713 -15. .093 0. .00 0. .00 PROA

ATOM 1571 CG ASN X 658 -2 .500 10 .102 -15. .163 0. .00 0. .00 PROA

ATOM 1572 OD1 ASN X 658 -2 .830 9 .242 -16. .004 0. .00 0. .00 PROA

ATOM 1573 ND2 ASN X 658 -3 .290 11 .058 -14. .732 0. .00 0. .00 PROA

ATOM 1574 HD21 ASN X 658 -4 .181 11 .095 -15. .185 0. .00 0. .00 PROA

ATOM 1575 HD22 ASN X 658 -2 .902 11 .803 -14. .188 0. .00 0. .00 PROA

ATOM 1576 C ASN X 658 1. .054 8 .591 -14. .675 0. .00 0. .00 PROA

ATOM 1577 O ASN X 658 1. .682 8 .488 -15. .764 0. .00 0. .00 PROA

ATOM 1578 N VAL X 659 1. .600 8 .761 -13. .416 0. .00 0. .00 PROA

ATOM 1579 HN VAL X 659 0. .933 8 .889 -12. .686 0. .00 0. .00 PROA

ATOM 1580 CA VAL X 659 3. .035 8 .561 -13. .069 0. .00 0. .00 PROA

ATOM 1581 HA VAL X 659 3. .552 9 .280 -13. .687 0. .00 0. .00 PROA

ATOM 1582 CB VAL X 659 3. .201 8 .980 -11. .596 0. .00 0. .00 PROA

ATOM 1583 HB VAL X 659 2. .363 8 .547 -11. .009 0. .00 0. .00 PROA ATOM 1584 CGI VAL X 659 4.639 8.553 -11..078 0..00 0..00 PROA

ATOM 1585 HG11 VAL X 659 4 .750 8 .686 -9. .980 0. .00 0. .00 PROA

ATOM 1586 HG12 VAL X 659 4 .936 7 .499 -11. .265 0. .00 0. .00 PROA

ATOM 1587 HG13 VAL X 659 5 .322 9 .227 -11. .639 0. .00 0. .00 PROA

ATOM 1588 CG2 VAL X 659 3 .075 10 .455 -11. .359 0. .00 0. .00 PROA

ATOM 1589 HG21 VAL X 659 3 .904 10 .925 -11. .931 0. .00 0. .00 PROA

ATOM 1590 HG22 VAL X 659 2 .122 10 .818 -11. .800 0. .00 0. .00 PROA

ATOM 1591 HG23 VAL X 659 3 .176 10 .649 -10. .270 0. .00 0. .00 PROA

ATOM 1592 C VAL X 659 3. .619 7 .192 -13. .539 0. .00 0. .00 PROA

ATOM 1593 O VAL X 659 4. .537 7 .109 -14. .319 0. .00 0. .00 PROA

ATOM 1594 N SER X 660 2. .985 6 .046 -13. .269 0. .00 0. .00 PROA

ATOM 1595 HN SER X 660 2. .246 6 .313 -12. .655 0. .00 0. .00 PROA

ATOM 1596 CA SER X 660 3. .409 4 .701 -13. .643 0. .00 0. .00 PROA

ATOM 1597 HA SER X 660 4. .389 4 .683 -13. .190 0. .00 0. .00 PROA

ATOM 1598 CB SER X 660 2. .560 3 .651 -12. .892 0. .00 0. .00 PROA

ATOM 1599 HB1 SER X 660 1 .499 3 .771 -13. .198 0. .00 0. .00 PROA

ATOM 1600 HB2 SER X 660 3 .015 2 .731 -13. .318 0. .00 0. .00 PROA

ATOM 1601 OG SER X 660 2. .642 3 .634 -11. .501 0. .00 0. .00 PROA

ATOM 1602 HG1 SER X 660 2 .295 4 .505 -11. .296 0. .00 0. .00 PROA

ATOM 1603 C SER X 660 3. .445 4 .455 -15. .124 0. .00 0. .00 PROA

ATOM 1604 O SER X 660 4. .297 3 .625 -15. .593 0. .00 0. .00 PROA

ATOM 1605 N ALA X 661 2. .545 5 .152 -15. .940 0. .00 0. .00 PROA

ATOM 1606 HN ALA X 661 1. .843 5 .731 -15. .533 0. .00 0. .00 PROA

ATOM 1607 CA ALA X 661 2. .608 5 .091 -17. .355 0. .00 0. .00 PROA

ATOM 1608 HA ALA X 661 2. .573 4 .044 -17. .620 0. .00 0. .00 PROA

ATOM 1609 CB ALA X 661 1. .334 5 .795 -17. .855 0. .00 0. .00 PROA

ATOM 1610 HB1 ALA X 661 1 .294 6 .866 -17. .560 0. .00 0. .00 PROA

ATOM 1611 HB2 ALA X 661 1 .235 5 .688 -18. .956 0. .00 0. .00 PROA

ATOM 1612 HB3 ALA X 661 0 .469 5 .312 -17. .351 0. .00 0. .00 PROA

ATOM 1613 C ALA X 661 3. .819 5 .740 -17. .929 0. .00 0. .00 PROA

ATOM 1614 O ALA X 661 4. .359 5 .296 -18. .936 0. .00 0. .00 PROA

ATOM 1615 N ILE X 662 4. .275 6 .853 -17. .365 0. .00 0. .00 PROA

ATOM 1616 HN ILE X 662 3. .813 7 .310 -16. .609 0. .00 0. .00 PROA

ATOM 1617 CA ILE X 662 5. .528 7 .523 -17. .762 0. .00 0. .00 PROA

ATOM 1618 HA ILE X 662 5. .504 7 .730 -18. .821 0. .00 0. .00 PROA

ATOM 1619 CB ILE X 662 5. .737 8 .826 -17. .032 0. .00 0. .00 PROA

ATOM 1620 HB ILE X 662 5. .871 8 .705 -15. .935 0. .00 0. .00 PROA

ATOM 1621 CG2 ILE X 662 7 .027 9 .507 -17. .510 0. .00 0. .00 PROA

ATOM 1622 HG21 ILE X 662 7 .879 8 .969 -17. .044 0. .00 0. .00 PROA

ATOM 1623 HG22 ILE X 662 7 .062 9 .605 -18. .616 0. .00 0. .00 PROA

ATOM 1624 HG23 ILE X 662 6 .947 10 .549 -17. .131 0. .00 0. .00 PROA

ATOM 1625 CGI ILE X 662 4 .442 9 .712 -17. .123 0. .00 0. .00 PROA

ATOM 1626 HG11 ILE X 662 3 .664 9 .210 -16. .508 0. .00 0. .00 PROA

ATOM 1627 HG12 ILE X 662 4 .778 10 .569 -16. .501 0. .00 0. .00 PROA

ATOM 1628 CD ILE X 662 3. .898 10 .017 -18. .516 0. .00 0. .00 PROA

ATOM 1629 HD1 ILE X 662 4 .779 10 .278 -19. .140 0. .00 0. .00 PROA

ATOM 1630 HD2 ILE X 662 3 .197 9 .227 -18. .859 0. .00 0. .00 PROA

ATOM 1631 HD3 ILE X 662 3 .308 10 .953 -18. .409 0. .00 0. .00 PROA

ATOM 1632 C ILE X 662 6. .753 6 .634 -17. .584 0. .00 0. .00 PROA

ATOM 1633 O ILE X 662 7. .622 6 .524 -18. .418 0. .00 0. .00 PROA

ATOM 1634 N ILE X 663 6. .886 5 .983 -16. .375 0. .00 0. .00 PROA

ATOM 1635 HN ILE X 663 6. .184 6 .070 -15. .672 0. .00 0. .00 PROA

ATOM 1636 CA ILE X 663 8. .106 5 .252 -15. .936 0. .00 0. .00 PROA

ATOM 1637 HA ILE X 663 8. .830 6 .048 -16. .033 0. .00 0. .00 PROA

ATOM 1638 CB ILE X 663 8. .066 4 .667 -14. .488 0. .00 0. .00 PROA

ATOM 1639 HB ILE X 663 7. .133 4 .083 -14. .340 0. .00 0. .00 PROA

ATOM 1640 CG2 ILE X 663 9 .295 3 .862 -14. .040 0. .00 0. .00 PROA

ATOM 1641 HG21 ILE X 663 9 .223 3 .543 -12. .978 0. .00 0. .00 PROA

ATOM 1642 HG22 ILE X 663 9 .541 3 .023 -14. .726 0. .00 0. .00 PROA

ATOM 1643 HG23 ILE X 663 10 .245 4 .428 -14. .142 0. .00 0. .00 PROA

ATOM 1644 CGI ILE X 663 7 .797 5 .925 -13. .621 0. .00 0. .00 PROA

ATOM 1645 HG11 ILE X 663 8 .768 6 .459 -13. .556 0. .00 0. .00 PROA

ATOM 1646 HG12 ILE X 663 7 .065 6 .591 -14. .126 0. .00 0. .00 PROA

ATOM 1647 CD ILE X 663 7. .266 5 .664 -12. .267 0. .00 0. .00 PROA

ATOM 1648 HD1 ILE X 663 8 .059 5 .085 -11. .747 0. .00 0. .00 PROA

ATOM 1649 HD2 ILE X 663 7 .128 6 .639 -11. .753 0. .00 0. .00 PROA ATOM 1650 HD3 ILE X 663 6.320 5.086 -12..327 0..00 0..00 PROA

ATOM 1651 C ILE X 663 8. .415 4 .134 -16. .896 0. .00 0. .00 PROA

ATOM 1652 O ILE X 663 9. .634 3 .945 -17. .098 0. .00 0. .00 PROA

ATOM 1653 N GLN X 664 7. .379 3 .492 -17. .512 0. .00 0. .00 PROA

ATOM 1654 HN GLN X 664 6. .480 3 .918 -17. .454 0. .00 0. .00 PROA

ATOM 1655 CA GLN X 664 7. .535 2 .329 -18. .397 0. .00 0. .00 PROA

ATOM 1656 HA GLN X 664 8. .376 1 .769 -18. .013 0. .00 0. .00 PROA

ATOM 1657 CB GLN X 664 6. .301 1 .407 -18. .371 0. .00 0. .00 PROA

ATOM 1658 HB1 GLN X 664 6 .500 0 .469 -18. .933 0. .00 0. .00 PROA

ATOM 1659 HB2 GLN X 664 6 .164 1 .143 -17. .300 0. .00 0. .00 PROA

ATOM 1660 CG GLN X 664 4. .986 2 .119 -18. .900 0. .00 0. .00 PROA

ATOM 1661 HG1 GLN X 664 4 .835 3 .040 -18. .298 0. .00 0. .00 PROA

ATOM 1662 HG2 GLN X 664 5 .013 2 .462 -19. .956 0. .00 0. .00 PROA

ATOM 1663 CD GLN X 664 3. .756 1 .205 -18. .834 0. .00 0. .00 PROA

ATOM 1664 OE1 GLN X 664 3 .344 0 .583 -19. .817 0. .00 0. .00 PROA

ATOM 1665 NE2 GLN X 664 3 .141 1 .122 -17. .636 0. .00 0. .00 PROA

ATOM 1666 HE21 GLN X 664 2 .257 0 .663 -17. .548 0. .00 0. .00 PROA

ATOM 1667 HE22 GLN X 664 3 .475 1 .591 -16. .818 0. .00 0. .00 PROA

ATOM 1668 C GLN X 664 7. .842 2 .545 -19. .828 0. .00 0. .00 PROA

ATOM 1669 O GLN X 664 8. .208 1 .627 -20. .590 0. .00 0. .00 PROA

ATOM 1670 N ARG X 665 7. .683 3 .795 -20. .311 0. .00 0. .00 PROA

ATOM 1671 HN ARG X 665 7. .233 4 .409 -19. .668 0. .00 0. .00 PROA

ATOM 1672 CA ARG X 665 8. .191 4 .272 -21. .572 0. .00 0. .00 PROA

ATOM 1673 HA ARG X 665 7. .989 3 .489 -22. .288 0. .00 0. .00 PROA

ATOM 1674 CB ARG X 665 7. .486 5 .510 -22. .066 0. .00 0. .00 PROA

ATOM 1675 HB1 ARG X 665 7 .791 6 .364 -21. .424 0. .00 0. .00 PROA

ATOM 1676 HB2 ARG X 665 7 .776 5 .831 -23. .089 0. .00 0. .00 PROA

ATOM 1677 CG ARG X 665 5. .922 5 .371 -22. .036 0. .00 0. .00 PROA

ATOM 1678 HG1 ARG X 665 5 .599 4 .450 -22. .566 0. .00 0. .00 PROA

ATOM 1679 HG2 ARG X 665 5 .712 5 .071 -20. .987 0. .00 0. .00 PROA

ATOM 1680 CD ARG X 665 5. .171 6 .595 -22. .482 0. .00 0. .00 PROA

ATOM 1681 HD1 ARG X 665 5 .449 7 .463 -21. .846 0. .00 0. .00 PROA

ATOM 1682 HD2 ARG X 665 5 .346 6 .811 -23. .558 0. .00 0. .00 PROA

ATOM 1683 NE ARG X 665 3. .679 6 .254 -22. .225 0. .00 0. .00 PROA

ATOM 1684 HE ARG X 665 3. .547 5 .293 -21. .981 0. .00 0. .00 PROA

ATOM 1685 CZ ARG X 665 2. .633 6 .982 -21. .889 0. .00 0. .00 PROA

ATOM 1686 NH1 ARG X 665 1 .447 6 .453 -21. .605 0. .00 0. .00 PROA

ATOM 1687 HH11 ARG X 665 0 .638 7 .004 -21. .401 0. .00 0. .00 PROA

ATOM 1688 HH12 ARG X 665 1 .419 5 .462 -21. .474 0. .00 0. .00 PROA

ATOM 1689 NH2 ARG X 665 2 .783 8 .313 -21. .865 0. .00 0. .00 PROA

ATOM 1690 HH21 ARG X 665 1 .982 8 .908 -21. .799 0. .00 0. .00 PROA

ATOM 1691 HH22 ARG X 665 3 .623 8 .742 -22. .198 0. .00 0. .00 PROA

ATOM 1692 C ARG X 665 9. .694 4 .612 -21. .529 0. .00 0. .00 PROA

ATOM 1693 O ARG X 665 10 .260 4 .772 -22. .647 0. .00 0. .00 PROA

ATOM 1694 N LEU X 666 10 .322 4 .800 -20. .352 0. .00 0. .00 PROA

ATOM 1695 HN LEU X 666 9. .880 4 .694 -19. .464 0. .00 0. .00 PROA

ATOM 1696 CA LEU X 666 11 .797 5 .236 -20. .300 0. .00 0. .00 PROA

ATOM 1697 HA LEU X 666 12 .061 5 .934 -21. .080 0. .00 0. .00 PROA

ATOM 1698 CB LEU X 666 12 .040 5 .987 -18. .928 0. .00 0. .00 PROA

ATOM 1699 HB1 LEU X 666 11 .958 5 .187 -18. .162 0. .00 0. .00 PROA

ATOM 1700 HB2 LEU X 666 13 .028 6 .496 -18. .929 0. .00 0. .00 PROA

ATOM 1701 CG LEU X 666 10 .887 6 .990 -18. .704 0. .00 0. .00 PROA

ATOM 1702 HG LEU X 666 9. .929 6 .443 -18. .842 0. .00 0. .00 PROA

ATOM 1703 CD1 LEU X 666 10 .898 7 .656 -17. .330 0. .00 0. .00 PROA

ATOM 1704 HD11 LEU X 666 11 .860 8 .201 -17. .223 0. .00 0. .00 PROA

ATOM 1705 HD12 LEU X 666 10 .075 8 .396 -17. .235 0. .00 0. .00 PROA

ATOM 1706 HD13 LEU X 666 10 .883 6 .767 -16. .663 0. .00 0. .00 PROA

ATOM 1707 CD2 LEU X 666 10 .890 8 .136 -19. .669 0. .00 0. .00 PROA

ATOM 1708 HD21 LEU X 666 11 .892 8 .612 -19. .720 0. .00 0. .00 PROA

ATOM 1709 HD22 LEU X 666 10 .624 7 .908 -20. .724 0. .00 0. .00 PROA

ATOM 1710 HD23 LEU X 666 10 .047 8 .782 -19. .345 0. .00 0. .00 PROA

ATOM 1711 C LEU X 666 12 .718 4 .067 -20. .403 0. .00 0. .00 PROA

ATOM 1712 OT1 LEU X 666 13 .460 4 .103 -21. .409 0. .00 0. .00 PROA

ATOM 1713 OT2 LEU X 666 12 .618 3 .123 -19. .577 0. .00 0. .00 PROA

ATOM 1714 N MET X 554 17 .715 -5 .606 -7. .612 0. .00 0. .00 PROB

ATOM 1715 HT1 MET X 554 18 .368 -6 .212 -7. .076 0. .00 0. .00 PROB ATOM 1716 HT2 MET X 554 18.393 -4.934 -8..025 0..00 0..00 PROB

ATOM 1717 HT3 MET X 554 17 .234 -6 .215 -8. .305 0. .00 0. .00 PROB

ATOM 1718 CA MET X 554 16 .696 -4 .710 -6. .849 0. .00 0. .00 PROB

ATOM 1719 HA MET X 554 16 .534 -3 .742 -7. .299 0. .00 0. .00 PROB

ATOM 1720 CB MET X 554 15 .329 -5 .468 -6. .751 0. .00 0. .00 PROB

ATOM 1721 HB1 MET X 554 14 .951 -5 .821 -7. .734 0. .00 0. .00 PROB

ATOM 1722 HB2 MET X 554 15 .500 -6 .391 -6. .156 0. .00 0. .00 PROB

ATOM 1723 CG MET X 554 14 .202 -4 .545 -6. .175 0. .00 0. .00 PROB

ATOM 1724 HG1 MET X 554 14 .645 -4 .153 -5. .235 0. .00 0. .00 PROB

ATOM 1725 HG2 MET X 554 14 .070 -3 .845 -7. .027 0. .00 0. .00 PROB

ATOM 1726 C MET X 554 17 .209 -4 .271 -5. .490 0. .00 0. .00 PROB

ATOM 1727 O MET X 554 17 .340 -3 .086 -5. .193 0. .00 0. .00 PROB

ATOM 1728 N CYS X 555 17 .643 -5 .206 -4. .611 0. .00 0. .00 PROB

ATOM 1729 HN CYS X 555 17 .755 -6 .158 -4. .885 0. .00 0. .00 PROB

ATOM 1730 CA CYS X 555 17 .976 -4 .763 -3. .267 0. .00 0. .00 PROB

ATOM 1731 HA CYS X 555 17 .244 -4 .085 -2. .853 0. .00 0. .00 PROB

ATOM 1732 CB CYS X 555 17 .779 -6 .084 -2. .384 0. .00 0. .00 PROB

ATOM 1733 HB1 CYS X 555 16 .953 -6 .714 -2. .779 0. .00 0. .00 PROB

ATOM 1734 HB2 CYS X 555 18 .786 -6 .552 -2. .419 0. .00 0. .00 PROB

ATOM 1735 C CYS X 555 19 .320 -4 .155 -3. .072 0. .00 0. .00 PROB

ATOM 1736 O CYS X 555 19 .452 -3 .534 -2. .031 0. .00 0. .00 PROB

ATOM 1737 N THR X 556 20 .261 -4 .367 -3. .997 0. .00 0. .00 PROB

ATOM 1738 HN THR X 556 20 .157 -4 .979 -4. .777 0. .00 0. .00 PROB

ATOM 1739 CA THR X 556 21 .538 -3 .662 -3. .956 0. .00 0. .00 PROB

ATOM 1740 HA THR X 556 21 .856 -3 .536 -2. .931 0. .00 0. .00 PROB

ATOM 1741 CB THR X 556 22 .670 -4 .301 -4. .803 0. .00 0. .00 PROB

ATOM 1742 HB THR X 556 23 .662 -3 .946 -4. .449 0. .00 0. .00 PROB

ATOM 1743 OG1 THR X 556 22 .383 -4 .133 -6. .213 0. .00 0. .00 PROB

ATOM 1744 HG1 THR X 556 23 .186 -4 .064 -6. .733 0. .00 0. .00 PROB

ATOM 1745 CG2 THR X 556 22 .681 -5 .750 -4. .451 0. .00 0. .00 PROB

ATOM 1746 HG21 THR X 556 22 .654 -5 .800 -3. .341 0. .00 0. .00 PROB

ATOM 1747 HG22 THR X 556 21 .768 -6 .244 -4. .847 0. .00 0. .00 PROB

ATOM 1748 HG23 THR X 556 23 .556 -6 .389 -4. .696 0. .00 0. .00 PROB

ATOM 1749 C THR X 556 21 .430 -2 .167 -4. .420 0. .00 0. .00 PROB

ATOM 1750 O THR X 556 22 .225 -1 .256 -4. .113 0. .00 0. .00 PROB

ATOM 1751 N PHE X 557 20 .406 -1 .886 -5. .265 0. .00 0. .00 PROB

ATOM 1752 HN PHE X 557 19 .897 -2 .691 -5. .562 0. .00 0. .00 PROB

ATOM 1753 CA PHE X 557 20 .039 -0 .513 -5. .679 0. .00 0. .00 PROB

ATOM 1754 HA PHE X 557 20 .925 -0 .017 -6. .046 0. .00 0. .00 PROB

ATOM 1755 CB PHE X 557 19 .089 -0 .542 -6. .911 0. .00 0. .00 PROB

ATOM 1756 HB1 PHE X 557 19 .532 -1 .272 -7. .621 0. .00 0. .00 PROB

ATOM 1757 HB2 PHE X 557 18 .106 -0 .986 -6. .644 0. .00 0. .00 PROB

ATOM 1758 CG PHE X 557 18 .854 0 .802 -7. .627 0. .00 0. .00 PROB

ATOM 1759 CD1 PHE X 557 17 .785 1 .691 -7. .281 0. .00 0. .00 PROB

ATOM 1760 HD1 PHE X 557 17 .141 1 .417 -6. .458 0. .00 0. .00 PROB

ATOM 1761 CE1 PHE X 557 17 .541 2 .901 -7. .968 0. .00 0. .00 PROB

ATOM 1762 HE1 PHE X 557 16 .859 3 .653 -7. .599 0. .00 0. .00 PROB

ATOM 1763 CZ PHE X 557 18 .371 3 .125 -9. .062 0. .00 0. .00 PROB

ATOM 1764 HZ PHE X 557 18 .351 4 .046 -9. .628 0. .00 0. .00 PROB

ATOM 1765 CD2 PHE X 557 19 .695 1 .134 -8. .664 0. .00 0. .00 PROB

ATOM 1766 HD2 PHE X 557 20 .473 0 .466 -9. .002 0. .00 0. .00 PROB

ATOM 1767 CE2 PHE X 557 19 .333 2 .205 -9. .454 0. .00 0. .00 PROB

ATOM 1768 HE2 PHE X 557 19 .862 2 .427 -10. .369 0. .00 0. .00 PROB

ATOM 1769 C PHE X 557 19 .362 0 .214 -4. .541 0. .00 0. .00 PROB

ATOM 1770 O PHE X 557 19 .624 1 .286 -4. .135 0. .00 0. .00 PROB

ATOM 1771 N ALA X 558 18 .418 -0 .521 -3. .950 0. .00 0. .00 PROB

ATOM 1772 HN ALA X 558 18 .010 -1 .281 -4. .451 0. .00 0. .00 PROB

ATOM 1773 CA ALA X 558 17 .597 -0 .021 -2. .893 0. .00 0. .00 PROB

ATOM 1774 HA ALA X 558 17 .083 0 .868 -3. .227 0. .00 0. .00 PROB

ATOM 1775 CB ALA X 558 16 .550 -1 .101 -2. .433 0. .00 0. .00 PROB

ATOM 1776 HB1 ALA X 558 15 .769 -1 .271 -3. .204 0. .00 0. .00 PROB

ATOM 1777 HB2 ALA X 558 16 .981 -2 .036 -2. .016 0. .00 0. .00 PROB

ATOM 1778 HB3 ALA X 558 15 .957 -0 .704 -1. .581 0. .00 0. .00 PROB

ATOM 1779 C ALA X 558 18 .451 0 .348 -1. .641 0. .00 0. .00 PROB

ATOM 1780 O ALA X 558 18 .163 1 .401 -1. .057 0. .00 0. .00 PROB

ATOM 1781 N LEU X 559 19 .495 -0 .381 -1. .314 0. .00 0. .00 PROB ATOM 1782 HN LEU X 559 19.543 -1.324 -1..633 0..00 0..00 PROB

ATOM 1783 CA LEU X 559 20 .366 -0 .211 -0. .155 0. .00 0. .00 PROB

ATOM 1784 HA LEU X 559 19 .780 -0 .208 0. .752 0. .00 0. .00 PROB

ATOM 1785 CB LEU X 559 21 .456 -1 .388 -0. .070 0. .00 0. .00 PROB

ATOM 1786 HB1 LEU X 559 20 .885 -2 .336 -0. .173 0. .00 0. .00 PROB

ATOM 1787 HB2 LEU X 559 22 .103 -1 .249 -0. .962 0. .00 0. .00 PROB

ATOM 1788 CG LEU X 559 22 .328 -1 .489 1. .152 0. .00 0. .00 PROB

ATOM 1789 HG LEU X 559 22 .749 -2 .516 1. .213 0. .00 0. .00 PROB

ATOM 1790 CD1 LEU X 559 21 .643 -1 .246 2. .502 0. .00 0. .00 PROB

ATOM 1791 HD11 LEU X 559 20 .820 -1 .984 2. .618 0. .00 0. .00 PROB

ATOM 1792 HD12 LEU X 559 22 .372 -1 .421 3. .322 0. .00 0. .00 PROB

ATOM 1793 HD13 LEU X 559 21 .360 -0 .175 2. .584 0. .00 0. .00 PROB

ATOM 1794 CD2 LEU X 559 23 .613 -0 .620 0. .956 0. .00 0. .00 PROB

ATOM 1795 HD21 LEU X 559 24 .054 -0 .993 0. .006 0. .00 0. .00 PROB

ATOM 1796 HD22 LEU X 559 23 .327 0 .453 0. .962 0. .00 0. .00 PROB

ATOM 1797 HD23 LEU X 559 24 .373 -0 .845 1. .735 0. .00 0. .00 PROB

ATOM 1798 C LEU X 559 21 .160 1 .161 -0. .226 0. .00 0. .00 PROB

ATOM 1799 O LEU X 559 21 .176 1 .822 0. .788 0. .00 0. .00 PROB

ATOM 1800 N ILE X 560 21 .644 1 .612 -1. .443 0. .00 0. .00 PROB

ATOM 1801 HN ILE X 560 21 .536 1 .009 -2. .229 0. .00 0. .00 PROB

ATOM 1802 CA ILE X 560 22 .212 2 .964 -1. .497 0. .00 0. .00 PROB

ATOM 1803 HA ILE X 560 22 .987 2 .894 -0. .748 0. .00 0. .00 PROB

ATOM 1804 CB ILE X 560 22 .836 3 .115 -2. .897 0. .00 0. .00 PROB

ATOM 1805 HB ILE X 560 21 .952 3 .085 -3. .570 0. .00 0. .00 PROB

ATOM 1806 CG2 ILE X 560 23 .646 4 .423 -2. .983 0. .00 0. .00 PROB

ATOM 1807 HG21 ILE X 560 24 .509 4 .212 -2. .316 0. .00 0. .00 PROB

ATOM 1808 HG22 ILE X 560 23 .828 4 .703 -4. .043 0. .00 0. .00 PROB

ATOM 1809 HG23 ILE X 560 23 .183 5 .308 -2. .497 0. .00 0. .00 PROB

ATOM 1810 CGI ILE X 560 23 .798 1 .948 -3. .337 0. .00 0. .00 PROB

ATOM 1811 HG11 ILE X 560 24 .491 1 .648 -2. .522 0. .00 0. .00 PROB

ATOM 1812 HG12 ILE X 560 23 .120 1 .078 -3. .470 0. .00 0. .00 PROB

ATOM 1813 CD ILE X 560 24 .530 2 .089 -4. .604 0. .00 0. .00 PROB

ATOM 1814 HD1 ILE X 560 24 .595 1 .038 -4. .958 0. .00 0. .00 PROB

ATOM 1815 HD2 ILE X 560 23 .908 2 .647 -5. .337 0. .00 0. .00 PROB

ATOM 1816 HD3 ILE X 560 25 .561 2 .504 -4. .596 0. .00 0. .00 PROB

ATOM 1817 C ILE X 560 21 .229 4 .127 -1. .208 0. .00 0. .00 PROB

ATOM 1818 O ILE X 560 21 .581 5 .070 -0. .490 0. .00 0. .00 PROB

ATOM 1819 N ALA X 561 19 .958 3 .970 -1. .618 0. .00 0. .00 PROB

ATOM 1820 HN ALA X 561 19 .687 3 .183 -2. .166 0. .00 0. .00 PROB

ATOM 1821 CA ALA X 561 18 .935 4 .961 -1. .410 0. .00 0. .00 PROB

ATOM 1822 HA ALA X 561 19 .330 5 .947 -1. .603 0. .00 0. .00 PROB

ATOM 1823 CB ALA X 561 17 .700 4 .693 -2. .153 0. .00 0. .00 PROB

ATOM 1824 HB1 ALA X 561 16 .860 5 .396 -1. .968 0. .00 0. .00 PROB

ATOM 1825 HB2 ALA X 561 17 .925 4 .779 -3. .237 0. .00 0. .00 PROB

ATOM 1826 HB3 ALA X 561 17 .284 3 .691 -1. .914 0. .00 0. .00 PROB

ATOM 1827 C ALA X 561 18 .457 5 .003 0. .090 0. .00 0. .00 PROB

ATOM 1828 O ALA X 561 18 .015 5 .996 0. .571 0. .00 0. .00 PROB

ATOM 1829 N HSD X 562 18 .436 3 .832 0. .733 0. .00 0. .00 PROB

ATOM 1830 HN HSD X 562 18 .737 2 .997 0. .279 0. .00 0. .00 PROB

ATOM 1831 CA HSD X 562 18 .212 3 .610 2. .170 0. .00 0. .00 PROB

ATOM 1832 HA HSD X 562 17 .355 4 .213 2. .432 0. .00 0. .00 PROB

ATOM 1833 CB HSD X 562 18 .049 2 .126 2. .527 0. .00 0. .00 PROB

ATOM 1834 HB1 HSD X 562 18 .870 1 .608 1. .987 0. .00 0. .00 PROB

ATOM 1835 HB2 HSD X 562 18 .131 2 .081 3. .634 0. .00 0. .00 PROB

ATOM 1836 ND1 HSD X 562 16 .240 1 .217 0. .922 0. .00 0. .00 PROB

ATOM 1837 HD1 HSD X 562 16 .589 1 .635 0. .083 0. .00 0. .00 PROB

ATOM 1838 CG HSD X 562 16 .773 1 .368 2. .166 0. .00 0. .00 PROB

ATOM 1839 CE1 HSD X 562 15 .119 0 .437 1. .008 0. .00 0. .00 PROB

ATOM 1840 HE1 HSD X 562 14 .737 0 .180 0. .019 0. .00 0. .00 PROB

ATOM 1841 NE2 HSD X 562 14 .862 0 .080 2. .207 0. .00 0. .00 PROB

ATOM 1842 CD2 HSD X 562 15 .898 0 .635 2. .986 0. .00 0. .00 PROB

ATOM 1843 HD2 HSD X 562 15 .977 0 .284 4. .007 0. .00 0. .00 PROB

ATOM 1844 C HSD X 562 19 .333 4 .289 2. .895 0. .00 0. .00 PROB

ATOM 1845 O HSD X 562 18 .970 5 .024 3. .859 0. .00 0. .00 PROB

ATOM 1846 N TRP X 563 20 .628 4 .264 2. .493 0. .00 0. .00 PROB

ATOM 1847 HN TRP X 563 20 .884 3 .634 1. .764 0. .00 0. .00 PROB ATOM 1848 CA TRP X 563 21.713 5.069 2..973 0..00 0..00 PROB

ATOM 1849 HA TRP X 563 22 .597 4 .987 2. .358 0. .00 0. .00 PROB

ATOM 1850 CB TRP X 563 22 .081 4 .647 4. .354 0. .00 0. .00 PROB

ATOM 1851 HB1 TRP X 563 22 .863 5 .253 4. .860 0. .00 0. .00 PROB

ATOM 1852 HB2 TRP X 563 21 .176 4 .635 4. .999 0. .00 0. .00 PROB

ATOM 1853 CG TRP X 563 22 .458 3 .155 4. .615 0. .00 0. .00 PROB

ATOM 1854 CD1 TRP X 563 23 .159 2 .236 3. .826 0. .00 0. .00 PROB

ATOM 1855 HD1 TRP X 563 23 .091 2 .344 2. .754 0. .00 0. .00 PROB

ATOM 1856 NE1 TRP X 563 23 .413 1 .054 4. .573 0. .00 0. .00 PROB

ATOM 1857 HE1 TRP X 563 24 .023 0 .300 4. .464 0. .00 0. .00 PROB

ATOM 1858 CE2 TRP X 563 22 .979 1 .201 5. .855 0. .00 0. .00 PROB

ATOM 1859 CD2 TRP X 563 22 .417 2 .540 5. .944 0. .00 0. .00 PROB

ATOM 1860 CE3 TRP X 563 21 .985 2 .961 7. .149 0. .00 0. .00 PROB

ATOM 1861 HE3 TRP X 563 21 .524 3 .925 7. .308 0. .00 0. .00 PROB

ATOM 1862 CZ3 TRP X 563 21 .970 2 .156 8. .278 0. .00 0. .00 PROB

ATOM 1863 HZ3 TRP X 563 21 .800 2 .645 9. .226 0. .00 0. .00 PROB

ATOM 1864 CZ2 TRP X 563 23 .056 0 .388 6. .963 0. .00 0. .00 PROB

ATOM 1865 HZ2 TRP X 563 23 .456 -0 .612 6. .883 0. .00 0. .00 PROB

ATOM 1866 CH2 TRP X 563 22 .641 0 .897 8. .256 0. .00 0. .00 PROB

ATOM 1867 HH2 TRP X 563 22 .553 0 .338 9. .176 0. .00 0. .00 PROB

ATOM 1868 C TRP X 563 21 .386 6 .629 3. .080 0. .00 0. .00 PROB

ATOM 1869 O TRP X 563 21 .741 7 .373 4. .005 0. .00 0. .00 PROB

ATOM 1870 N LEU X 564 20 .672 7 .123 2. .035 0. .00 0. .00 PROB

ATOM 1871 HN LEU X 564 20 .499 6 .511 1. .267 0. .00 0. .00 PROB

ATOM 1872 CA LEU X 564 20 .329 8 .567 1. .816 0. .00 0. .00 PROB

ATOM 1873 HA LEU X 564 21 .227 9 .012 2. .218 0. .00 0. .00 PROB

ATOM 1874 CB LEU X 564 20 .262 8 .832 0. .357 0. .00 0. .00 PROB

ATOM 1875 HB1 LEU X 564 21 .139 8 .492 -0. .234 0. .00 0. .00 PROB

ATOM 1876 HB2 LEU X 564 19 .414 8 .277 -0. .097 0. .00 0. .00 PROB

ATOM 1877 CG LEU X 564 20 .083 10 .310 0. .054 0. .00 0. .00 PROB

ATOM 1878 HG LEU X 564 19 .192 10 .625 0. .638 0. .00 0. .00 PROB

ATOM 1879 CD1 LEU X 564 21 .360 11 .074 0. .474 0. .00 0. .00 PROB

ATOM 1880 HD11 LEU X 564 21 .482 11 .200 1. .571 0. .00 0. .00 PROB

ATOM 1881 HD12 LEU X 564 22 .329 10 .798 0. .005 0. .00 0. .00 PROB

ATOM 1882 HD13 LEU X 564 21 .221 12 .049 -0. .040 0. .00 0. .00 PROB

ATOM 1883 CD2 LEU X 564 19 .752 10 .561 -1. .453 0. .00 0. .00 PROB

ATOM 1884 HD21 LEU X 564 18 .823 10 .059 -1. .798 0. .00 0. .00 PROB

ATOM 1885 HD22 LEU X 564 19 .773 11 .648 -1. .684 0. .00 0. .00 PROB

ATOM 1886 HD23 LEU X 564 20 .540 10 .084 -2. .074 0. .00 0. .00 PROB

ATOM 1887 C LEU X 564 19 .069 9 .066 2. .643 0. .00 0. .00 PROB

ATOM 1888 O LEU X 564 18 .931 10 .222 3. .118 0. .00 0. .00 PROB

ATOM 1889 N ALA X 565 18 .126 8 .118 2. .812 0. .00 0. .00 PROB

ATOM 1890 HN ALA X 565 18 .155 7 .277 2. .278 0. .00 0. .00 PROB

ATOM 1891 CA ALA X 565 16 .942 8 .438 3. .583 0. .00 0. .00 PROB

ATOM 1892 HA ALA X 565 16 .721 9 .485 3. .437 0. .00 0. .00 PROB

ATOM 1893 CB ALA X 565 15 .712 7 .481 3. .100 0. .00 0. .00 PROB

ATOM 1894 HB1 ALA X 565 15 .786 7 .670 2. .008 0. .00 0. .00 PROB

ATOM 1895 HB2 ALA X 565 15 .937 6 .405 3. .262 0. .00 0. .00 PROB

ATOM 1896 HB3 ALA X 565 14 .772 7 .881 3. .536 0. .00 0. .00 PROB

ATOM 1897 C ALA X 565 17 .161 8 .320 5. .081 0. .00 0. .00 PROB

ATOM 1898 O ALA X 565 16 .722 9 .157 5. .823 0. .00 0. .00 PROB

ATOM 1899 N CYS X 566 18 .059 7 .335 5. .470 0. .00 0. .00 PROB

ATOM 1900 HN CYS X 566 18 .302 6 .642 4. .797 0. .00 0. .00 PROB

ATOM 1901 CA CYS X 566 18 .296 6 .986 6. .861 0. .00 0. .00 PROB

ATOM 1902 HA CYS X 566 17 .431 6 .638 7. .406 0. .00 0. .00 PROB

ATOM 1903 CB CYS X 566 19 .261 5 .795 6. .837 0. .00 0. .00 PROB

ATOM 1904 HB1 CYS X 566 18 .802 5 .081 6. .120 0. .00 0. .00 PROB

ATOM 1905 HB2 CYS X 566 20 .300 6 .071 6. .556 0. .00 0. .00 PROB

ATOM 1906 C CYS X 566 18 .882 8 .135 7. .668 0. .00 0. .00 PROB

ATOM 1907 O CYS X 566 18 .409 8 .459 8. .755 0. .00 0. .00 PROB

ATOM 1908 N ILE X 567 19 .842 8 .876 7. .162 0. .00 0. .00 PROB

ATOM 1909 HN ILE X 567 20 .223 8 .684 6. .261 0. .00 0. .00 PROB

ATOM 1910 CA ILE X 567 20 .391 10 .013 7. .823 0. .00 0. .00 PROB

ATOM 1911 HA ILE X 567 20 .795 9 .774 8. .796 0. .00 0. .00 PROB

ATOM 1912 CB ILE X 567 21 .593 10 .569 7. .035 0. .00 0. .00 PROB

ATOM 1913 HB ILE X 567 22 .320 9 .747 7. .211 0. .00 0. .00 PROB ATOM 1914 CG2 ILE X 567 21.451 10.641 5..539 0..00 0..00 PROB

ATOM 1915 HG21 ILE X 567 22 .208 11 .228 4. .976 0. .00 0. .00 PROB

ATOM 1916 HG22 ILE X 567 21 .471 9 .633 5. .071 0. .00 0. .00 PROB

ATOM 1917 HG23 ILE X 567 20 .457 11 .041 5. .247 0. .00 0. .00 PROB

ATOM 1918 CGI ILE X 567 22 .245 11 .865 7. .622 0. .00 0. .00 PROB

ATOM 1919 HG11 ILE X 567 23 .120 12 .085 6. .975 0. .00 0. .00 PROB

ATOM 1920 HG12 ILE X 567 21 .673 12 .772 7. .331 0. .00 0. .00 PROB

ATOM 1921 CD ILE X 567 22 .761 11 .797 9. .100 0. .00 0. .00 PROB

ATOM 1922 HD1 ILE X 567 23 .711 12 .372 9. .119 0. .00 0. .00 PROB

ATOM 1923 HD2 ILE X 567 22 .092 12 .369 9. .778 0. .00 0. .00 PROB

ATOM 1924 HD3 ILE X 567 23 .002 10 .828 9. .587 0. .00 0. .00 PROB

ATOM 1925 C ILE X 567 19 .380 11 .086 8. .196 0. .00 0. .00 PROB

ATOM 1926 O ILE X 567 19 .466 11 .763 9. .200 0. .00 0. .00 PROB

ATOM 1927 N TRP X 568 18 .409 11 .457 7. .257 0. .00 0. .00 PROB

ATOM 1928 HN TRP X 568 18 .320 10 .906 6. .430 0. .00 0. .00 PROB

ATOM 1929 CA TRP X 568 17 .303 12 .405 7. .478 0. .00 0. .00 PROB

ATOM 1930 HA TRP X 568 17 .739 13 .342 7. .792 0. .00 0. .00 PROB

ATOM 1931 CB TRP X 568 16 .406 12 .672 6. .180 0. .00 0. .00 PROB

ATOM 1932 HB1 TRP X 568 16 .155 11 .763 5. .591 0. .00 0. .00 PROB

ATOM 1933 HB2 TRP X 568 15 .501 13 .234 6. .496 0. .00 0. .00 PROB

ATOM 1934 CG TRP X 568 16 .977 13 .606 5. .076 0. .00 0. .00 PROB

ATOM 1935 CD1 TRP X 568 17 .482 13 .274 3. .876 0. .00 0. .00 PROB

ATOM 1936 HD1 TRP X 568 17 .736 12 .246 3. .665 0. .00 0. .00 PROB

ATOM 1937 NE1 TRP X 568 18 .118 14 .360 3. .256 0. .00 0. .00 PROB

ATOM 1938 HE1 TRP X 568 18 .633 14 .356 2. .427 0. .00 0. .00 PROB

ATOM 1939 CE2 TRP X 568 17 .767 15 .453 4. .078 0. .00 0. .00 PROB

ATOM 1940 CD2 TRP X 568 17 .013 14 .962 5. .218 0. .00 0. .00 PROB

ATOM 1941 CE3 TRP X 568 16 .570 15 .878 6. .216 0. .00 0. .00 PROB

ATOM 1942 HE3 TRP X 568 16 .068 15 .421 7. .056 0. .00 0. .00 PROB

ATOM 1943 CZ3 TRP X 568 16 .682 17 .246 6. .089 0. .00 0. .00 PROB

ATOM 1944 HZ3 TRP X 568 16 .343 17 .963 6. .822 0. .00 0. .00 PROB

ATOM 1945 CZ2 TRP X 568 17 .958 16 .811 3. .973 0. .00 0. .00 PROB

ATOM 1946 HZ2 TRP X 568 18 .457 17 .258 3. .125 0. .00 0. .00 PROB

ATOM 1947 CH2 TRP X 568 17 .359 17 .693 4. .879 0. .00 0. .00 PROB

ATOM 1948 HH2 TRP X 568 17 .614 18 .743 4. .849 0. .00 0. .00 PROB

ATOM 1949 C TRP X 568 16 .359 12 .083 8. .644 0. .00 0. .00 PROB

ATOM 1950 O TRP X 568 15 .881 13 .003 9. .320 0. .00 0. .00 PROB

ATOM 1951 N TYR X 569 16 .090 10 .759 8. .849 0. .00 0. .00 PROB

ATOM 1952 HN TYR X 569 16 .528 10 .134 8. .207 0. .00 0. .00 PROB

ATOM 1953 CA TYR X 569 15 .331 10 .200 10. .007 0. .00 0. .00 PROB

ATOM 1954 HA TYR X 569 14 .364 10 .649 10. .181 0. .00 0. .00 PROB

ATOM 1955 CB TYR X 569 15 .078 8 .685 9. .816 0. .00 0. .00 PROB

ATOM 1956 HB1 TYR X 569 16 .107 8 .271 9. .750 0. .00 0. .00 PROB

ATOM 1957 HB2 TYR X 569 14 .691 8 .342 10. .799 0. .00 0. .00 PROB

ATOM 1958 CG TYR X 569 14 .051 8 .304 8. .743 0. .00 0. .00 PROB

ATOM 1959 CD1 TYR X 569 12 .718 8 .903 8. .765 0. .00 0. .00 PROB

ATOM 1960 HD1 TYR X 569 12 .376 9 .530 9. .575 0. .00 0. .00 PROB

ATOM 1961 CE1 TYR X 569 11 .805 8 .501 7. .796 0. .00 0. .00 PROB

ATOM 1962 HE1 TYR X 569 10 .780 8 .836 7. .854 0. .00 0. .00 PROB

ATOM 1963 CZ TYR X 569 12 .081 7 .588 6. .804 0. .00 0. .00 PROB

ATOM 1964 OH TYR X 569 11 .031 7 .302 5. .864 0. .00 0. .00 PROB

ATOM 1965 HH TYR X 569 11 .449 6 .676 5. .269 0. .00 0. .00 PROB

ATOM 1966 CD2 TYR X 569 14 .377 7 .508 7. .670 0. .00 0. .00 PROB

ATOM 1967 HD2 TYR X 569 15 .392 7 .181 7. .505 0. .00 0. .00 PROB

ATOM 1968 CE2 TYR X 569 13 .397 7 .070 6. .781 0. .00 0. .00 PROB

ATOM 1969 HE2 TYR X 569 13 .759 6 .481 5. .952 0. .00 0. .00 PROB

ATOM 1970 C TYR X 569 16 .162 10 .392 11. .293 0. .00 0. .00 PROB

ATOM 1971 O TYR X 569 15 .717 10 .932 12. .247 0. .00 0. .00 PROB

ATOM 1972 N ALA X 570 17 .505 10 .025 11. .196 0. .00 0. .00 PROB

ATOM 1973 HN ALA X 570 17 .848 9 .544 10. .393 0. .00 0. .00 PROB

ATOM 1974 CA ALA X 570 18 .461 10 .016 12. .277 0. .00 0. .00 PROB

ATOM 1975 HA ALA X 570 18 .017 9 .697 13. .209 0. .00 0. .00 PROB

ATOM 1976 CB ALA X 570 19 .680 9 .113 12. .047 0. .00 0. .00 PROB

ATOM 1977 HB1 ALA X 570 19 .306 8 .067 12. .042 0. .00 0. .00 PROB

ATOM 1978 HB2 ALA X 570 20 .203 9 .263 11. .078 0. .00 0. .00 PROB

ATOM 1979 HB3 ALA X 570 20 .437 9 .303 12. .838 0. .00 0. .00 PROB ATOM 1980 C ALA X 570 18.871 11.412 12..749 0..00 0..00 PROB

ATOM 1981 O ALA X 570 19 .005 11 .630 13. .923 0. .00 0. .00 PROB

ATOM 1982 N ILE X 571 18 .932 12 .466 11. .883 0. .00 0. .00 PROB

ATOM 1983 HN ILE X 571 18 .758 12 .260 10. .923 0. .00 0. .00 PROB

ATOM 1984 CA ILE X 571 19 .479 13 .807 12. .184 0. .00 0. .00 PROB

ATOM 1985 HA ILE X 571 20 .488 13 .526 12. .449 0. .00 0. .00 PROB

ATOM 1986 CB ILE X 571 19 .521 14 .659 10. .968 0. .00 0. .00 PROB

ATOM 1987 HB ILE X 571 19 .927 13 .957 10. .209 0. .00 0. .00 PROB

ATOM 1988 CG2 ILE X 571 18 .206 15 .233 10. .415 0. .00 0. .00 PROB

ATOM 1989 HG21 ILE X 571 17 .697 16 .020 11. .011 0. .00 0. .00 PROB

ATOM 1990 HG22 ILE X 571 18 .239 15 .512 9. .340 0. .00 0. .00 PROB

ATOM 1991 HG23 ILE X 571 17 .495 14 .380 10. .444 0. .00 0. .00 PROB

ATOM 1992 CGI ILE X 571 20 .626 15 .648 11. .140 0. .00 0. .00 PROB

ATOM 1993 HG11 ILE X 571 20 .213 16 .577 11. .589 0. .00 0. .00 PROB

ATOM 1994 HG12 ILE X 571 21 .340 15 .229 11. .880 0. .00 0. .00 PROB

ATOM 1995 CD ILE X 571 21 .351 15 .866 9. .882 0. .00 0. .00 PROB

ATOM 1996 HD1 ILE X 571 20 .588 16 .146 9. .124 0. .00 0. .00 PROB

ATOM 1997 HD2 ILE X 571 22 .135 16 .635 10. .047 0. .00 0. .00 PROB

ATOM 1998 HD3 ILE X 571 21 .943 14 .963 9. .617 0. .00 0. .00 PROB

ATOM 1999 C ILE X 571 18 .903 14 .684 13. .301 0. .00 0. .00 PROB

ATOM 2000 O ILE X 571 19 .592 15 .397 14. .013 0. .00 0. .00 PROB

ATOM 2001 N GLY X 572 17 .535 14 .644 13. .501 0. .00 0. .00 PROB

ATOM 2002 HN GLY X 572 16 .942 14 .104 12. .908 0. .00 0. .00 PROB

ATOM 2003 CA GLY X 572 16 .996 15 .512 14. .569 0. .00 0. .00 PROB

ATOM 2004 HA1 GLY X 572 15 .922 15 .531 14. .455 0. .00 0. .00 PROB

ATOM 2005 HA2 GLY X 572 17 .455 16 .485 14. .666 0. .00 0. .00 PROB

ATOM 2006 C GLY X 572 17 .243 14 .925 15. .914 0. .00 0. .00 PROB

ATOM 2007 O GLY X 572 16 .967 15 .439 17. .005 0. .00 0. .00 PROB

ATOM 2008 N ASN X 573 17 .643 13 .646 15. .941 0. .00 0. .00 PROB

ATOM 2009 HN ASN X 573 17 .837 13 .190 15. .076 0. .00 0. .00 PROB

ATOM 2010 CA ASN X 573 17 .910 12 .864 17. .109 0. .00 0. .00 PROB

ATOM 2011 HA ASN X 573 17 .430 13 .296 17. .975 0. .00 0. .00 PROB

ATOM 2012 CB ASN X 573 17 .435 11 .445 16. .867 0. .00 0. .00 PROB

ATOM 2013 HB1 ASN X 573 17 .924 10 .900 16. .031 0. .00 0. .00 PROB

ATOM 2014 HB2 ASN X 573 17 .594 10 .805 17. .761 0. .00 0. .00 PROB

ATOM 2015 CG ASN X 573 15 .908 11 .407 16. .572 0. .00 0. .00 PROB

ATOM 2016 OD1 ASN X 573 15 . Ill 11 .408 17. .503 0. .00 0. .00 PROB

ATOM 2017 ND2 ASN X 573 15 .482 11 .476 15. .265 0. .00 0. .00 PROB

ATOM 2018 HD21 ASN X 573 14 .493 11 .569 15. .152 0. .00 0. .00 PROB

ATOM 2019 HD22 ASN X 573 16 .085 11 .365 14. .475 0. .00 0. .00 PROB

ATOM 2020 C ASN X 573 19 .410 12 .896 17. .473 0. .00 0. .00 PROB

ATOM 2021 O ASN X 573 19 .739 12 .488 18. .530 0. .00 0. .00 PROB

ATOM 2022 N MET X 574 20 .244 13 .307 16. .558 0. .00 0. .00 PROB

ATOM 2023 HN MET X 574 20 .068 13 .226 15. .580 0. .00 0. .00 PROB

ATOM 2024 CA MET X 574 21 .629 13 .601 16. .842 0. .00 0. .00 PROB

ATOM 2025 HA MET X 574 22 .056 12 .868 17. .510 0. .00 0. .00 PROB

ATOM 2026 CB MET X 574 22 .481 13 .373 15. .518 0. .00 0. .00 PROB

ATOM 2027 HB1 MET X 574 22 .074 14 .118 14. .801 0. .00 0. .00 PROB

ATOM 2028 HB2 MET X 574 23 .560 13 .624 15. .589 0. .00 0. .00 PROB

ATOM 2029 CG MET X 574 22 .310 11 .990 14. .872 0. .00 0. .00 PROB

ATOM 2030 HG1 MET X 574 21 .270 11 .643 14. .691 0. .00 0. .00 PROB

ATOM 2031 HG2 MET X 574 22 .641 12 .126 13. .820 0. .00 0. .00 PROB

ATOM 2032 SD MET X 574 23 .246 10 .730 15. .703 0. .00 0. .00 PROB

ATOM 2033 CE MET X 574 23 .314 9 .666 14. .320 0. .00 0. .00 PROB

ATOM 2034 HE1 MET X 574 22 .315 9 .308 13. .990 0. .00 0. .00 PROB

ATOM 2035 HE2 MET X 574 23 .840 10 .149 13. .469 0. .00 0. .00 PROB

ATOM 2036 HE3 MET X 574 23 .978 8 .794 14. .501 0. .00 0. .00 PROB

ATOM 2037 C MET X 574 21 .864 14 .993 17. .362 0. .00 0. .00 PROB

ATOM 2038 O MET X 574 22 .965 15 .343 17. .740 0. .00 0. .00 PROB

ATOM 2039 N GLU X 575 20 .791 15 .814 17. .454 0. .00 0. .00 PROB

ATOM 2040 HN GLU X 575 19 .904 15 .485 17. .140 0. .00 0. .00 PROB

ATOM 2041 CA GLU X 575 20 .901 17 .265 17. .812 0. .00 0. .00 PROB

ATOM 2042 HA GLU X 575 21 .493 17 .734 17. .040 0. .00 0. .00 PROB

ATOM 2043 CB GLU X 575 19 .444 17 .706 17. .852 0. .00 0. .00 PROB

ATOM 2044 HB1 GLU X 575 18 .858 17 .156 17. .085 0. .00 0. .00 PROB

ATOM 2045 HB2 GLU X 575 18 .940 17 .367 18. .782 0. .00 0. .00 PROB ATOM 2046 CG GLU X 575 19.029 19.175 17..640 0..00 0..00 PROB

ATOM 2047 HG1 GLU X 575 19 .341 19 .795 18. .508 0. .00 0. .00 PROB

ATOM 2048 HG2 GLU X 575 19 .326 19 .595 16. .655 0. .00 0. .00 PROB

ATOM 2049 CD GLU X 575 17 .510 19 .265 17. .733 0. .00 0. .00 PROB

ATOM 2050 OE1 GLU X 575 16 .848 19 .792 16. .789 0. .00 0. .00 PROB

ATOM 2051 OE2 GLU X 575 16 .931 18 .871 18. .827 0. .00 0. .00 PROB

ATOM 2052 C GLU X 575 21 .509 17 .646 19. .150 0. .00 0. .00 PROB

ATOM 2053 O GLU X 575 22 .305 18 .537 19. .251 0. .00 0. .00 PROB

ATOM 2054 N GLN X 576 21 .185 16 .892 20. .183 0. .00 0. .00 PROB

ATOM 2055 HN GLN X 576 20 .592 16 .106 20. .025 0. .00 0. .00 PROB

ATOM 2056 CA GLN X 576 21 .267 17 .236 21. .652 0. .00 0. .00 PROB

ATOM 2057 HA GLN X 576 20 .348 16 .852 22. .068 0. .00 0. .00 PROB

ATOM 2058 CB GLN X 576 22 .470 16 .461 22. .289 0. .00 0. .00 PROB

ATOM 2059 HB1 GLN X 576 23 .472 16 .818 21. .967 0. .00 0. .00 PROB

ATOM 2060 HB2 GLN X 576 22 .440 16 .856 23. .327 0. .00 0. .00 PROB

ATOM 2061 CG GLN X 576 22 .328 14 .912 22. .089 0. .00 0. .00 PROB

ATOM 2062 HG1 GLN X 576 21 .315 14 .482 22. .242 0. .00 0. .00 PROB

ATOM 2063 HG2 GLN X 576 22 .690 14 .681 21. .064 0. .00 0. .00 PROB

ATOM 2064 CD GLN X 576 23 .314 14 .128 22. .968 0. .00 0. .00 PROB

ATOM 2065 OE1 GLN X 576 22 .884 13 .400 23. .849 0. .00 0. .00 PROB

ATOM 2066 NE2 GLN X 576 24 .628 14 .073 22. .576 0. .00 0. .00 PROB

ATOM 2067 HE21 GLN X 576 25 .209 13 .639 23. .265 0. .00 0. .00 PROB

ATOM 2068 HE22 GLN X 576 25 .005 14 .447 21. .728 0. .00 0. .00 PROB

ATOM 2069 C GLN X 576 21 .409 18 .633 22. .151 0. .00 0. .00 PROB

ATOM 2070 O GLN X 576 22 .535 19 .118 22. .303 0. .00 0. .00 PROB

ATOM 2071 N PRO X 577 20 .398 19 .580 22. .276 0. .00 0. .00 PROB

ATOM 2072 CD PRO X 577 19 .012 19 .271 21. .801 0. .00 0. .00 PROB

ATOM 2073 HD1 PRO X 577 19 .063 18 .973 20. .732 0. .00 0. .00 PROB

ATOM 2074 HD2 PRO X 577 18 .619 18 .483 22. .479 0. .00 0. .00 PROB

ATOM 2075 CA PRO X 577 20 .451 20 .998 22. .727 0. .00 0. .00 PROB

ATOM 2076 HA PRO X 577 20 .954 21 .514 21. .923 0. .00 0. .00 PROB

ATOM 2077 CB PRO X 577 19 .003 21 .344 23. .075 0. .00 0. .00 PROB

ATOM 2078 HB1 PRO X 577 18 .892 22 .449 23. .089 0. .00 0. .00 PROB

ATOM 2079 HB2 PRO X 577 18 .733 21 .004 24. .098 0. .00 0. .00 PROB

ATOM 2080 CG PRO X 577 18 .206 20 .493 21. .984 0. .00 0. .00 PROB

ATOM 2081 HG1 PRO X 577 18 .130 21 .060 21. .032 0. .00 0. .00 PROB

ATOM 2082 HG2 PRO X 577 17 .182 20 .178 22. .279 0. .00 0. .00 PROB

ATOM 2083 C PRO X 577 21 .353 21 .192 23. .933 0. .00 0. .00 PROB

ATOM 2084 O PRO X 577 21 .156 20 .497 24. .969 0. .00 0. .00 PROB

ATOM 2085 N HSD X 578 22 .320 22 .093 23. .888 0. .00 0. .00 PROB

ATOM 2086 HN HSD X 578 22 .356 22 .639 23. .055 0. .00 0. .00 PROB

ATOM 2087 CA HSD X 578 23 .297 22 .383 24. .912 0. .00 0. .00 PROB

ATOM 2088 HA HSD X 578 23 .940 21 .525 25. .039 0. .00 0. .00 PROB

ATOM 2089 CB HSD X 578 24 .215 23 .478 24. .326 0. .00 0. .00 PROB

ATOM 2090 HB1 HSD X 578 23 .623 24 .385 24. .075 0. .00 0. .00 PROB

ATOM 2091 HB2 HSD X 578 25 .018 23 .827 25. .010 0. .00 0. .00 PROB

ATOM 2092 ND1 HSD X 578 25 .860 23 .921 22. .446 0. .00 0. .00 PROB

ATOM 2093 HD1 HSD X 578 25 .963 24 .856 22. .785 0. .00 0. .00 PROB

ATOM 2094 CG HSD X 578 24 .898 23 .128 22. .990 0. .00 0. .00 PROB

ATOM 2095 CE1 HSD X 578 26 .371 23 .338 21. .337 0. .00 0. .00 PROB

ATOM 2096 HE1 HSD X 578 27 .088 23 .776 20. .642 0. .00 0. .00 PROB

ATOM 2097 NE2 HSD X 578 25 .924 22 .124 21. .233 0. .00 0. .00 PROB

ATOM 2098 CD2 HSD X 578 24 .950 21 .970 22. .262 0. .00 0. .00 PROB

ATOM 2099 HD2 HSD X 578 24 .488 21 .010 22. .458 0. .00 0. .00 PROB

ATOM 2100 C HSD X 578 22 .806 22 .861 26. .307 0. .00 0. .00 PROB

ATOM 2101 O HSD X 578 23 .296 22 .449 27. .370 0. .00 0. .00 PROB

ATOM 2102 N MET X 579 21 .812 23 .785 26. .351 0. .00 0. .00 PROB

ATOM 2103 HN MET X 579 21 .443 24 .127 25. .490 0. .00 0. .00 PROB

ATOM 2104 CA MET X 579 21 .234 24 .303 27. .586 0. .00 0. .00 PROB

ATOM 2105 HA MET X 579 21 .427 23 .518 28. .303 0. .00 0. .00 PROB

ATOM 2106 CB MET X 579 21 .766 25 .726 27. .984 0. .00 0. .00 PROB

ATOM 2107 HB1 MET X 579 21 .655 26 .502 27. .196 0. .00 0. .00 PROB

ATOM 2108 HB2 MET X 579 21 .216 26 .097 28. .875 0. .00 0. .00 PROB

ATOM 2109 CG MET X 579 23 .228 25 .631 28. .393 0. .00 0. .00 PROB

ATOM 2110 HG1 MET X 579 23 .238 25 .087 29. .361 0. .00 0. .00 PROB

ATOM 2111 HG2 MET X 579 23 .866 24 .953 27. .786 0. .00 0. .00 PROB ATOM 2112 C MET X 579 19.696 24.402 27..347 0..00 0..00 PROB

ATOM 2113 O MET X 579 19 .291 24 .893 26. .266 0. .00 0. .00 PROB

ATOM 2114 N ASP X 580 18 .799 23 .906 28. .193 0. .00 0. .00 PROB

ATOM 2115 HN ASP X 580 17 .848 23 .962 27. .899 0. .00 0. .00 PROB

ATOM 2116 CA ASP X 580 18 .959 23 .420 29. .585 0. .00 0. .00 PROB

ATOM 2117 HA ASP X 580 19 .820 23 .933 29. .988 0. .00 0. .00 PROB

ATOM 2118 CB ASP X 580 17 .698 23 .748 30. .428 0. .00 0. .00 PROB

ATOM 2119 HB1 ASP X 580 16 .773 23 .271 30. .039 0. .00 0. .00 PROB

ATOM 2120 HB2 ASP X 580 17 .850 23 .508 31. .502 0. .00 0. .00 PROB

ATOM 2121 CG ASP X 580 17 .190 25 .214 30. .293 0. .00 0. .00 PROB

ATOM 2122 OD1 ASP X 580 16 .043 25 .476 29. .951 0. .00 0. .00 PROB

ATOM 2123 OD2 ASP X 580 18 .054 26 .093 30. .512 0. .00 0. .00 PROB

ATOM 2124 C ASP X 580 19 .292 21 .951 29. .801 0. .00 0. .00 PROB

ATOM 2125 O ASP X 580 19 .324 21 .108 28. .892 0. .00 0. .00 PROB

ATOM 2126 N SER X 581 19 .575 21 .638 31. .055 0. .00 0. .00 PROB

ATOM 2127 HN SER X 581 19 .736 22 .357 31. .726 0. .00 0. .00 PROB

ATOM 2128 CA SER X 581 19 .873 20 .333 31. .516 0. .00 0. .00 PROB

ATOM 2129 HA SER X 581 20 .817 20 .133 31. .031 0. .00 0. .00 PROB

ATOM 2130 CB SER X 581 20 .089 20 .305 33. .041 0. .00 0. .00 PROB

ATOM 2131 HB1 SER X 581 20 .692 21 .156 33. .426 0. .00 0. .00 PROB

ATOM 2132 HB2 SER X 581 19 .134 20 .470 33. .584 0. .00 0. .00 PROB

ATOM 2133 OG SER X 581 20 .830 19 .131 33. .471 0. .00 0. .00 PROB

ATOM 2134 HG1 SER X 581 21 .617 19 .339 33. .980 0. .00 0. .00 PROB

ATOM 2135 C SER X 581 18 .809 19 .258 31. .231 0. .00 0. .00 PROB

ATOM 2136 O SER X 581 17 .594 19 .460 31. .399 0. .00 0. .00 PROB

ATOM 2137 N ARG X 582 19 .305 17 .993 30. .908 0. .00 0. .00 PROB

ATOM 2138 HN ARG X 582 20 .263 17 .883 30. .654 0. .00 0. .00 PROB

ATOM 2139 CA ARG X 582 18 .460 16 .836 30. .779 0. .00 0. .00 PROB

ATOM 2140 HA ARG X 582 17 .651 17 .150 30. .136 0. .00 0. .00 PROB

ATOM 2141 CB ARG X 582 19 .200 15 .722 29. .944 0. .00 0. .00 PROB

ATOM 2142 HB1 ARG X 582 20 .259 15 .673 30. .276 0. .00 0. .00 PROB

ATOM 2143 HB2 ARG X 582 18 .640 14 .779 30. .119 0. .00 0. .00 PROB

ATOM 2144 CG ARG X 582 19 .161 15 .995 28. .433 0. .00 0. .00 PROB

ATOM 2145 HG1 ARG X 582 18 .125 15 .965 28. .033 0. .00 0. .00 PROB

ATOM 2146 HG2 ARG X 582 19 .571 16 .998 28. .186 0. .00 0. .00 PROB

ATOM 2147 CD ARG X 582 20 .011 15 .039 27. .616 0. .00 0. .00 PROB

ATOM 2148 HD1 ARG X 582 21 .031 15 .150 28. .043 0. .00 0. .00 PROB

ATOM 2149 HD2 ARG X 582 19 .468 14 .086 27. .795 0. .00 0. .00 PROB

ATOM 2150 NE ARG X 582 19 .957 15 .435 26. .176 0. .00 0. .00 PROB

ATOM 2151 HE ARG X 582 19 .750 16 .361 25. .859 0. .00 0. .00 PROB

ATOM 2152 CZ ARG X 582 20 .037 14 .567 25. .143 0. .00 0. .00 PROB

ATOM 2153 NH1 ARG X 582 20 .472 13 .342 25. .330 0. .00 0. .00 PROB

ATOM 2154 HH11 ARG X 582 21 .030 12 .993 24. .577 0. .00 0. .00 PROB

ATOM 2155 HH12 ARG X 582 20 .932 13 .171 26. .201 0. .00 0. .00 PROB

ATOM 2156 NH2 ARG X 582 19 .507 14 .870 23. .937 0. .00 0. .00 PROB

ATOM 2157 HH21 ARG X 582 19 .621 14 .208 23. .196 0. .00 0. .00 PROB

ATOM 2158 HH22 ARG X 582 18 .784 15 .560 23. .900 0. .00 0. .00 PROB

ATOM 2159 C ARG X 582 17 .684 16 .391 32. .024 0. .00 0. .00 PROB

ATOM 2160 O ARG X 582 16 .513 16 .087 31. .904 0. .00 0. .00 PROB

ATOM 2161 N ILE X 583 18 .202 16 .607 33. .320 0. .00 0. .00 PROB

ATOM 2162 HN ILE X 583 19 .145 16 .927 33. .375 0. .00 0. .00 PROB

ATOM 2163 CA ILE X 583 17 .566 16 .340 34. .573 0. .00 0. .00 PROB

ATOM 2164 HA ILE X 583 17 .199 15 .327 34. .507 0. .00 0. .00 PROB

ATOM 2165 CB ILE X 583 18 .603 16 .788 35. .709 0. .00 0. .00 PROB

ATOM 2166 HB ILE X 583 18 .712 17 .888 35. .600 0. .00 0. .00 PROB

ATOM 2167 CG2 ILE X 583 18 .064 16 .445 37. .129 0. .00 0. .00 PROB

ATOM 2168 HG21 ILE X 583 17 .644 15 .431 37. .302 0. .00 0. .00 PROB

ATOM 2169 HG22 ILE X 583 18 .840 16 .569 37. .914 0. .00 0. .00 PROB

ATOM 2170 HG23 ILE X 583 17 .307 17 .231 37. .337 0. .00 0. .00 PROB

ATOM 2171 CGI ILE X 583 19 .978 15 .992 35. .524 0. .00 0. .00 PROB

ATOM 2172 HG11 ILE X 583 20 .424 16 .243 34. .537 0. .00 0. .00 PROB

ATOM 2173 HG12 ILE X 583 20 .612 16 .370 36. .354 0. .00 0. .00 PROB

ATOM 2174 CD ILE X 583 19 .870 14 .521 35. .791 0. .00 0. .00 PROB

ATOM 2175 HD1 ILE X 583 19 .168 14 .073 35. .056 0. .00 0. .00 PROB

ATOM 2176 HD2 ILE X 583 20 .804 13 .925 35. .716 0. .00 0. .00 PROB

ATOM 2177 HD3 ILE X 583 19 .384 14 .382 36. .781 0. .00 0. .00 PROB ATOM 2178 C ILE X 583 16.238 17.054 34..817 0..00 0..00 PROB

ATOM 2179 O ILE X 583 15 .305 16 .542 35. .363 0. .00 0. .00 PROB

ATOM 2180 N GLY X 584 16 .121 18 .327 34. .326 0. .00 0. .00 PROB

ATOM 2181 HN GLY X 584 16 .773 18 .613 33. .628 0. .00 0. .00 PROB

ATOM 2182 CA GLY X 584 14 .996 19 .163 34. .441 0. .00 0. .00 PROB

ATOM 2183 HA1 GLY X 584 15 .196 20 .164 34. .090 0. .00 0. .00 PROB

ATOM 2184 HA2 GLY X 584 14 .543 19 .014 35. .410 0. .00 0. .00 PROB

ATOM 2185 C GLY X 584 13 .889 18 .781 33. .464 0. .00 0. .00 PROB

ATOM 2186 O GLY X 584 12 .754 19 .281 33. .600 0. .00 0. .00 PROB

ATOM 2187 N TRP X 585 14 .178 17 .916 32. .527 0. .00 0. .00 PROB

ATOM 2188 HN TRP X 585 15 .132 17 .686 32. .354 0. .00 0. .00 PROB

ATOM 2189 CA TRP X 585 13 .172 17 .564 31. .510 0. .00 0. .00 PROB

ATOM 2190 HA TRP X 585 12 .711 18 .503 31. .240 0. .00 0. .00 PROB

ATOM 2191 CB TRP X 585 13 .875 16 .805 30. .317 0. .00 0. .00 PROB

ATOM 2192 HB1 TRP X 585 14 .756 17 .444 30. .094 0. .00 0. .00 PROB

ATOM 2193 HB2 TRP X 585 14 .127 15 .772 30. .642 0. .00 0. .00 PROB

ATOM 2194 CG TRP X 585 12 .950 16 .800 29. .112 0. .00 0. .00 PROB

ATOM 2195 CD1 TRP X 585 12 .467 17 .705 28. .335 0. .00 0. .00 PROB

ATOM 2196 HD1 TRP X 585 12 .966 18 .660 28. .274 0. .00 0. .00 PROB

ATOM 2197 NE1 TRP X 585 11 .579 17 .210 27. .417 0. .00 0. .00 PROB

ATOM 2198 HE1 TRP X 585 11 .165 17 .682 26. .670 0. .00 0. .00 PROB

ATOM 2199 CE2 TRP X 585 11 .561 15 .812 27. .586 0. .00 0. .00 PROB

ATOM 2200 CD2 TRP X 585 12 .503 15 .533 28. .550 0. .00 0. .00 PROB

ATOM 2201 CE3 TRP X 585 12 .671 14 .180 29. .013 0. .00 0. .00 PROB

ATOM 2202 HE3 TRP X 585 13 .364 13 .848 29. .772 0. .00 0. .00 PROB

ATOM 2203 CZ3 TRP X 585 12 .211 13 .229 28. .140 0. .00 0. .00 PROB

ATOM 2204 HZ3 TRP X 585 12 .400 12 .226 28. .491 0. .00 0. .00 PROB

ATOM 2205 CZ2 TRP X 585 10 .837 14 .862 26. .889 0. .00 0. .00 PROB

ATOM 2206 HZ2 TRP X 585 10 .071 15 .034 26. .148 0. .00 0. .00 PROB

ATOM 2207 CH2 TRP X 585 11 .187 13 .526 27. .206 0. .00 0. .00 PROB

ATOM 2208 HH2 TRP X 585 10 .637 12 .751 26. .693 0. .00 0. .00 PROB

ATOM 2209 C TRP X 585 11 .881 16 .897 32. .028 0. .00 0. .00 PROB

ATOM 2210 O TRP X 585 10 .787 17 .193 31. .606 0. .00 0. .00 PROB

ATOM 2211 N LEU X 586 11 .977 15 .978 32. .949 0. .00 0. .00 PROB

ATOM 2212 HN LEU X 586 12 .881 15 .695 33. .260 0. .00 0. .00 PROB

ATOM 2213 CA LEU X 586 10 .680 15 .220 33. .141 0. .00 0. .00 PROB

ATOM 2214 HA LEU X 586 10 .257 15 .170 32. .148 0. .00 0. .00 PROB

ATOM 2215 CB LEU X 586 10 .936 13 .741 33. .750 0. .00 0. .00 PROB

ATOM 2216 HB1 LEU X 586 11 .592 13 .868 34. .637 0. .00 0. .00 PROB

ATOM 2217 HB2 LEU X 586 9 .960 13 .400 34. .157 0. .00 0. .00 PROB

ATOM 2218 CG LEU X 586 11 .512 12 .662 32. .825 0. .00 0. .00 PROB

ATOM 2219 HG LEU X 586 12 .521 12 .930 32. .444 0. .00 0. .00 PROB

ATOM 2220 CD1 LEU X 586 11 .562 11 .356 33. .581 0. .00 0. .00 PROB

ATOM 2221 HD11 LEU X 586 12 .156 11 .544 34. .501 0. .00 0. .00 PROB

ATOM 2222 HD12 LEU X 586 10 .561 10 .944 33. .829 0. .00 0. .00 PROB

ATOM 2223 HD13 LEU X 586 12 .152 10 .566 33. .070 0. .00 0. .00 PROB

ATOM 2224 CD2 LEU X 586 10 .616 12 .507 31. .551 0. .00 0. .00 PROB

ATOM 2225 HD21 LEU X 586 9 .636 12 .151 31. .934 0. .00 0. .00 PROB

ATOM 2226 HD22 LEU X 586 10 .391 13 .451 31. .011 0. .00 0. .00 PROB

ATOM 2227 HD23 LEU X 586 11 .106 11 .787 30. .861 0. .00 0. .00 PROB

ATOM 2228 C LEU X 586 9. .656 15 .933 34. .092 0. .00 0. .00 PROB

ATOM 2229 O LEU X 586 8. .454 15 .781 33. .913 0. .00 0. .00 PROB

ATOM 2230 N HSD X 587 10 .107 16 .743 35. .005 0. .00 0. .00 PROB

ATOM 2231 HN HSD X 587 11 .089 16 .591 35. .091 0. .00 0. .00 PROB

ATOM 2232 CA HSD X 587 9. .322 17 .621 35. .792 0. .00 0. .00 PROB

ATOM 2233 HA HSD X 587 8. .607 17 .030 36. .345 0. .00 0. .00 PROB

ATOM 2234 CB HSD X 587 10 .110 18 .259 36. .908 0. .00 0. .00 PROB

ATOM 2235 HB1 HSD X 587 10 .418 17 .455 37. .611 0. .00 0. .00 PROB

ATOM 2236 HB2 HSD X 587 10 .975 18 .765 36. .428 0. .00 0. .00 PROB

ATOM 2237 ND1 HSD X 587 8 .487 19 .041 38. .574 0. .00 0. .00 PROB

ATOM 2238 HD1 HSD X 587 8 .287 18 .078 38. .751 0. .00 0. .00 PROB

ATOM 2239 CG HSD X 587 9. .375 19 .340 37. .544 0. .00 0. .00 PROB

ATOM 2240 CE1 HSD X 587 8 .171 20 .165 39. .162 0. .00 0. .00 PROB

ATOM 2241 HE1 HSD X 587 7 .433 20 .319 39. .950 0. .00 0. .00 PROB

ATOM 2242 NE2 HSD X 587 8 .787 21 .178 38. .569 0. .00 0. .00 PROB

ATOM 2243 CD2 HSD X 587 9 .531 20 .640 37. .502 0. .00 0. .00 PROB ATOM 2244 HD2 HSD X 587 10.071 21.208 36..754 0..00 0..00 PROB

ATOM 2245 C HSD X 587 8. .554 18 .611 34. .981 0. .00 0. .00 PROB

ATOM 2246 O HSD X 587 7. .354 18 .771 35. .141 0. .00 0. .00 PROB

ATOM 2247 N ASN X 588 9. .169 19 .175 33. .874 0. .00 0. .00 PROB

ATOM 2248 HN ASN X 588 10 .166 19 .166 33. .840 0. .00 0. .00 PROB

ATOM 2249 CA ASN X 588 8. .692 20 .015 32. .812 0. .00 0. .00 PROB

ATOM 2250 HA ASN X 588 8. .247 20 .914 33. .213 0. .00 0. .00 PROB

ATOM 2251 CB ASN X 588 9. .965 20 .603 32. .147 0. .00 0. .00 PROB

ATOM 2252 HB1 ASN X 588 10 .680 19 .756 32. .074 0. .00 0. .00 PROB

ATOM 2253 HB2 ASN X 588 9 .709 20 .955 31. .124 0. .00 0. .00 PROB

ATOM 2254 CG ASN X 588 10 .581 21 .789 32. .806 0. .00 0. .00 PROB

ATOM 2255 OD1 ASN X 588 10 .101 22 .262 33. .846 0. .00 0. .00 PROB

ATOM 2256 ND2 ASN X 588 11 .654 22 .417 32. .212 0. .00 0. .00 PROB

ATOM 2257 HD21 ASN X 588 11 .677 23 .407 32. .346 0. .00 0. .00 PROB

ATOM 2258 HD22 ASN X 588 12 .053 21 .955 31. .419 0. .00 0. .00 PROB

ATOM 2259 C ASN X 588 7. .672 19 .369 31. .930 0. .00 0. .00 PROB

ATOM 2260 O ASN X 588 6. .601 19 .923 31. .778 0. .00 0. .00 PROB

ATOM 2261 N LEU X 589 7. .987 18 .143 31. .475 0. .00 0. .00 PROB

ATOM 2262 HN LEU X 589 8. .880 17 .744 31. .669 0. .00 0. .00 PROB

ATOM 2263 CA LEU X 589 7. .099 17 .414 30. .640 0. .00 0. .00 PROB

ATOM 2264 HA LEU X 589 6. .797 18 .076 29. .842 0. .00 0. .00 PROB

ATOM 2265 CB LEU X 589 7. .785 16 .158 30. .059 0. .00 0. .00 PROB

ATOM 2266 HB1 LEU X 589 8 .621 16 .369 29. .358 0. .00 0. .00 PROB

ATOM 2267 HB2 LEU X 589 8 .209 15 .508 30. .854 0. .00 0. .00 PROB

ATOM 2268 CG LEU X 589 6. .853 15 .207 29. .258 0. .00 0. .00 PROB

ATOM 2269 HG LEU X 589 5. .997 14 .826 29. .856 0. .00 0. .00 PROB

ATOM 2270 CD1 LEU X 589 6 .461 15 .881 27. .926 0. .00 0. .00 PROB

ATOM 2271 HD11 LEU X 589 5 .804 15 .204 27. .338 0. .00 0. .00 PROB

ATOM 2272 HD12 LEU X 589 5 .993 16 .841 28. .232 0. .00 0. .00 PROB

ATOM 2273 HD13 LEU X 589 7 .394 16 .092 27. .362 0. .00 0. .00 PROB

ATOM 2274 CD2 LEU X 589 7 .677 14 .058 28. .864 0. .00 0. .00 PROB

ATOM 2275 HD21 LEU X 589 8 .764 14 .240 28. .722 0. .00 0. .00 PROB

ATOM 2276 HD22 LEU X 589 7 .553 13 .234 29. .599 0. .00 0. .00 PROB

ATOM 2277 HD23 LEU X 589 7 .331 13 .682 27. .877 0. .00 0. .00 PROB

ATOM 2278 C LEU X 589 5. .833 16 .885 31. .396 0. .00 0. .00 PROB

ATOM 2279 O LEU X 589 4. .709 16 .899 30. .934 0. .00 0. .00 PROB

ATOM 2280 N GLY X 590 6. .006 16 .533 32. .696 0. .00 0. .00 PROB

ATOM 2281 HN GLY X 590 6. .958 16 .518 32. .993 0. .00 0. .00 PROB

ATOM 2282 CA GLY X 590 4. .957 16 .268 33. .676 0. .00 0. .00 PROB

ATOM 2283 HA1 GLY X 590 5 .386 15 .918 34. .604 0. .00 0. .00 PROB

ATOM 2284 HA2 GLY X 590 4 .327 15 .500 33. .252 0. .00 0. .00 PROB

ATOM 2285 C GLY X 590 4. .001 17 .478 33. .891 0. .00 0. .00 PROB

ATOM 2286 O GLY X 590 2. .845 17 .271 34. .217 0. .00 0. .00 PROB

ATOM 2287 N ASP X 591 4. .541 18 .718 33. .659 0. .00 0. .00 PROB

ATOM 2288 HN ASP X 591 5. .504 18 .925 33. .504 0. .00 0. .00 PROB

ATOM 2289 CA ASP X 591 3. .695 19 .923 33. .662 0. .00 0. .00 PROB

ATOM 2290 HA ASP X 591 2. .691 19 .740 34. .014 0. .00 0. .00 PROB

ATOM 2291 CB ASP X 591 4. .253 21 .015 34. .576 0. .00 0. .00 PROB

ATOM 2292 HB1 ASP X 591 5 .358 20 .940 34. .491 0. .00 0. .00 PROB

ATOM 2293 HB2 ASP X 591 3 .994 22 .056 34. .290 0. .00 0. .00 PROB

ATOM 2294 CG ASP X 591 3. .876 20 .744 36. .100 0. .00 0. .00 PROB

ATOM 2295 OD1 ASP X 591 4 .722 20 .539 36. .956 0. .00 0. .00 PROB

ATOM 2296 OD2 ASP X 591 2 .644 20 .638 36. .355 0. .00 0. .00 PROB

ATOM 2297 C ASP X 591 3. .500 20 .567 32. .274 0. .00 0. .00 PROB

ATOM 2298 O ASP X 591 3. .024 21 .689 32. .150 0. .00 0. .00 PROB

ATOM 2299 N GLN X 592 3. .774 19 .829 31. .145 0. .00 0. .00 PROB

ATOM 2300 HN GLN X 592 4. .121 18 .897 31. .214 0. .00 0. .00 PROB

ATOM 2301 CA GLN X 592 3. .419 20 .321 29. .836 0. .00 0. .00 PROB

ATOM 2302 HA GLN X 592 3. .974 19 .651 29. .196 0. .00 0. .00 PROB

ATOM 2303 CB GLN X 592 1. .893 20 .261 29. .532 0. .00 0. .00 PROB

ATOM 2304 HB1 GLN X 592 1 .365 20 .773 30. .365 0. .00 0. .00 PROB

ATOM 2305 HB2 GLN X 592 1 .678 20 .806 28. .587 0. .00 0. .00 PROB

ATOM 2306 CG GLN X 592 1. .383 18 .806 29. .195 0. .00 0. .00 PROB

ATOM 2307 HG1 GLN X 592 1 .605 18 .196 30. .096 0. .00 0. .00 PROB

ATOM 2308 HG2 GLN X 592 0 .311 18 .803 28. .901 0. .00 0. .00 PROB

ATOM 2309 CD GLN X 592 2. .166 18 .106 27. .976 0. .00 0. .00 PROB ATOM 2310 OE1 GLN X 592 2.657 17.038 28..246 0..00 0..00 PROB

ATOM 2311 NE2 GLN X 592 2 .247 18 .769 26. .834 0. .00 0. .00 PROB

ATOM 2312 HE21 GLN X 592 1 .752 19 .634 26. .753 0. .00 0. .00 PROB

ATOM 2313 HE22 GLN X 592 2 .891 18 .513 26. .113 0. .00 0. .00 PROB

ATOM 2314 C GLN X 592 4. .169 21 .646 29. .414 0. .00 0. .00 PROB

ATOM 2315 O GLN X 592 3. .468 22 .514 28. .910 0. .00 0. .00 PROB

ATOM 2316 N ILE X 593 5. .452 21 .884 29. .745 0. .00 0. .00 PROB

ATOM 2317 HN ILE X 593 5. .954 21 .131 30. .162 0. .00 0. .00 PROB

ATOM 2318 CA ILE X 593 6. .047 23 .260 29. .574 0. .00 0. .00 PROB

ATOM 2319 HA ILE X 593 5. .389 24 .011 29. .985 0. .00 0. .00 PROB

ATOM 2320 CB ILE X 593 7. .377 23 .354 30. .376 0. .00 0. .00 PROB

ATOM 2321 HB ILE X 593 8. .068 22 .515 30. .146 0. .00 0. .00 PROB

ATOM 2322 CG2 ILE X 593 8 .201 24 .641 30. .099 0. .00 0. .00 PROB

ATOM 2323 HG21 ILE X 593 8 .830 24 .530 29. .190 0. .00 0. .00 PROB

ATOM 2324 HG22 ILE X 593 7 .575 25 .558 30. .147 0. .00 0. .00 PROB

ATOM 2325 HG23 ILE X 593 8 .946 24 .791 30. .910 0. .00 0. .00 PROB

ATOM 2326 CGI ILE X 593 7 .078 23 .332 31. .860 0. .00 0. .00 PROB

ATOM 2327 HG11 ILE X 593 6 .530 22 .411 32. .152 0. .00 0. .00 PROB

ATOM 2328 HG12 ILE X 593 8 .041 23 .384 32. .412 0. .00 0. .00 PROB

ATOM 2329 CD ILE X 593 6. .139 24 .427 32. .351 0. .00 0. .00 PROB

ATOM 2330 HD1 ILE X 593 6 .207 24 .561 33. .452 0. .00 0. .00 PROB

ATOM 2331 HD2 ILE X 593 6 .269 25 .414 31. .857 0. .00 0. .00 PROB

ATOM 2332 HD3 ILE X 593 5 .081 24 .239 32. .067 0. .00 0. .00 PROB

ATOM 2333 C ILE X 593 6. .067 23 .678 28. .090 0. .00 0. .00 PROB

ATOM 2334 O ILE X 593 6. .510 22 .939 27. .228 0. .00 0. .00 PROB

ATOM 2335 N GLY X 594 5. .704 24 .922 27. .733 0. .00 0. .00 PROB

ATOM 2336 HN GLY X 594 5. .432 25 .593 28. .418 0. .00 0. .00 PROB

ATOM 2337 CA GLY X 594 5. .442 25 .270 26. .368 0. .00 0. .00 PROB

ATOM 2338 HA1 GLY X 594 4 .952 26 .228 26. .463 0. .00 0. .00 PROB

ATOM 2339 HA2 GLY X 594 4 .811 24 .514 25. .925 0. .00 0. .00 PROB

ATOM 2340 C GLY X 594 6. .668 25 .545 25. .600 0. .00 0. .00 PROB

ATOM 2341 O GLY X 594 6. .642 25 .483 24. .374 0. .00 0. .00 PROB

ATOM 2342 N LYS X 595 7. .841 25 .845 26. .287 0. .00 0. .00 PROB

ATOM 2343 HN LYS X 595 7. .741 25 .877 27. .279 0. .00 0. .00 PROB

ATOM 2344 CA LYS X 595 9. .212 26 .160 25. .931 0. .00 0. .00 PROB

ATOM 2345 HA LYS X 595 9. .142 27 .097 25. .400 0. .00 0. .00 PROB

ATOM 2346 CB LYS X 595 10 .148 26 .422 27. .117 0. .00 0. .00 PROB

ATOM 2347 HB1 LYS X 595 10 .139 25 .499 27. .735 0. .00 0. .00 PROB

ATOM 2348 HB2 LYS X 595 11 .177 26 .626 26. .751 0. .00 0. .00 PROB

ATOM 2349 CG LYS X 595 9. .562 27 .452 28. .143 0. .00 0. .00 PROB

ATOM 2350 HG1 LYS X 595 9 .575 28 .436 27. .626 0. .00 0. .00 PROB

ATOM 2351 HG2 LYS X 595 8 .502 27 .229 28. .391 0. .00 0. .00 PROB

ATOM 2352 CD LYS X 595 10 .415 27 .377 29. .438 0. .00 0. .00 PROB

ATOM 2353 HD1 LYS X 595 10 .381 26 .326 29. .796 0. .00 0. .00 PROB

ATOM 2354 HD2 LYS X 595 11 .443 27 .669 29. .134 0. .00 0. .00 PROB

ATOM 2355 CE LYS X 595 10 .044 28 .434 30. .475 0. .00 0. .00 PROB

ATOM 2356 HE1 LYS X 595 8 .965 28 .610 30. .672 0. .00 0. .00 PROB

ATOM 2357 HE2 LYS X 595 10 .488 28 .168 31. .458 0. .00 0. .00 PROB

ATOM 2358 NZ LYS X 595 10 .496 29 .829 30. .062 0. .00 0. .00 PROB

ATOM 2359 HZ1 LYS X 595 9 .830 30 .255 29. .386 0. .00 0. .00 PROB

ATOM 2360 HZ2 LYS X 595 10 .708 30 .475 30. .849 0. .00 0. .00 PROB

ATOM 2361 HZ3 LYS X 595 11 .319 29 .756 29. .431 0. .00 0. .00 PROB

ATOM 2362 C LYS X 595 9. .807 25 .064 24. .981 0. .00 0. .00 PROB

ATOM 2363 O LYS X 595 9. .408 23 .907 25. .034 0. .00 0. .00 PROB

ATOM 2364 N PRO X 596 10 .680 25 .298 24. .013 0. .00 0. .00 PROB

ATOM 2365 CD PRO X 596 11 .192 26 .578 23. .608 0. .00 0. .00 PROB

ATOM 2366 HD1 PRO X 596 10 .287 27 .217 23. .692 0. .00 0. .00 PROB

ATOM 2367 HD2 PRO X 596 11 .944 26 .899 24. .360 0. .00 0. .00 PROB

ATOM 2368 CA PRO X 596 10 .955 24 .312 22. .892 0. .00 0. .00 PROB

ATOM 2369 HA PRO X 596 10 .043 24 .214 22. .321 0. .00 0. .00 PROB

ATOM 2370 CB PRO X 596 12 .024 24 .897 22. .031 0. .00 0. .00 PROB

ATOM 2371 HB1 PRO X 596 12 .023 24 .493 20. .996 0. .00 0. .00 PROB

ATOM 2372 HB2 PRO X 596 13 .033 24 .710 22. .457 0. .00 0. .00 PROB

ATOM 2373 CG PRO X 596 11 .643 26 .423 22. .175 0. .00 0. .00 PROB

ATOM 2374 HG1 PRO X 596 10 .815 26 .708 21. .492 0. .00 0. .00 PROB

ATOM 2375 HG2 PRO X 596 12 .478 27 .069 21. .829 0. .00 0. .00 PROB ATOM 2376 C PRO X 596 11.444 22.957 23..315 0..00 0..00 PROB

ATOM 2377 O PRO X 596 10 .832 21 .976 22. .842 0. .00 0. .00 PROB

ATOM 2378 N TYR X 597 12 .473 22 .800 24. .126 0. .00 0. .00 PROB

ATOM 2379 HN TYR X 597 12 .954 23 .590 24. .498 0. .00 0. .00 PROB

ATOM 2380 CA TYR X 597 13 .225 21 .524 24. .288 0. .00 0. .00 PROB

ATOM 2381 HA TYR X 597 13 .147 21 .010 23. .341 0. .00 0. .00 PROB

ATOM 2382 CB TYR X 597 14 .738 21 .745 24. .741 0. .00 0. .00 PROB

ATOM 2383 HB1 TYR X 597 14 .842 22 .054 25. .803 0. .00 0. .00 PROB

ATOM 2384 HB2 TYR X 597 15 .198 20 .735 24. .698 0. .00 0. .00 PROB

ATOM 2385 CG TYR X 597 15 .470 22 .707 23. .918 0. .00 0. .00 PROB

ATOM 2386 CD1 TYR X 597 15 .346 22 .755 22. .540 0. .00 0. .00 PROB

ATOM 2387 HD1 TYR X 597 14 .711 22 .075 21. .992 0. .00 0. .00 PROB

ATOM 2388 CE1 TYR X 597 15 .827 23 .851 21. .813 0. .00 0. .00 PROB

ATOM 2389 HE1 TYR X 597 15 .743 23 .951 20. .741 0. .00 0. .00 PROB

ATOM 2390 CZ TYR X 597 16 .528 24 .863 22. .478 0. .00 0. .00 PROB

ATOM 2391 OH TYR X 597 17 .054 25 .998 21. .793 0. .00 0. .00 PROB

ATOM 2392 HH TYR X 597 17 .014 25 .726 20. .873 0. .00 0. .00 PROB

ATOM 2393 CD2 TYR X 597 16 .197 23 .728 24. .620 0. .00 0. .00 PROB

ATOM 2394 HD2 TYR X 597 16 .272 23 .645 25. .695 0. .00 0. .00 PROB

ATOM 2395 CE2 TYR X 597 16 .793 24 .756 23. .873 0. .00 0. .00 PROB

ATOM 2396 HE2 TYR X 597 17 .260 25 .496 24. .505 0. .00 0. .00 PROB

ATOM 2397 C TYR X 597 12 .581 20 .688 25. .411 0. .00 0. .00 PROB

ATOM 2398 O TYR X 597 12 .894 19 .536 25. .716 0. .00 0. .00 PROB

ATOM 2399 N ASN X 598 11 .454 21 .290 25. .941 0. .00 0. .00 PROB

ATOM 2400 HN ASN X 598 11 .380 22 .240 25. .649 0. .00 0. .00 PROB

ATOM 2401 CA ASN X 598 10 .521 20 .587 26. .747 0. .00 0. .00 PROB

ATOM 2402 HA ASN X 598 10 .982 19 .720 27. .197 0. .00 0. .00 PROB

ATOM 2403 CB ASN X 598 10 .000 21 .515 27. .962 0. .00 0. .00 PROB

ATOM 2404 HB1 ASN X 598 9 .211 22 .256 27. .712 0. .00 0. .00 PROB

ATOM 2405 HB2 ASN X 598 9 .604 20 .874 28. .779 0. .00 0. .00 PROB

ATOM 2406 CG ASN X 598 11 .171 22 .110 28. .686 0. .00 0. .00 PROB

ATOM 2407 OD1 ASN X 598 11 .856 21 .331 29. .312 0. .00 0. .00 PROB

ATOM 2408 ND2 ASN X 598 11 .405 23 .450 28. .741 0. .00 0. .00 PROB

ATOM 2409 HD21 ASN X 598 12 .073 23 .802 29. .397 0. .00 0. .00 PROB

ATOM 2410 HD22 ASN X 598 11 .175 24 .032 27. .961 0. .00 0. .00 PROB

ATOM 2411 C ASN X 598 9. .280 20 .097 25. .977 0. .00 0. .00 PROB

ATOM 2412 O ASN X 598 8. .375 19 .544 26. .580 0. .00 0. .00 PROB

ATOM 2413 N SER X 599 9. .173 20 .375 24. .658 0. .00 0. .00 PROB

ATOM 2414 HN SER X 599 9. .905 20 .812 24. .141 0. .00 0. .00 PROB

ATOM 2415 CA SER X 599 7. .986 20 .263 23. .900 0. .00 0. .00 PROB

ATOM 2416 HA SER X 599 7. .500 19 .352 24. .218 0. .00 0. .00 PROB

ATOM 2417 CB SER X 599 6. .955 21 .423 24. .060 0. .00 0. .00 PROB

ATOM 2418 HB1 SER X 599 5 .902 21 .102 23. .907 0. .00 0. .00 PROB

ATOM 2419 HB2 SER X 599 6 .943 21 .656 25. .146 0. .00 0. .00 PROB

ATOM 2420 OG SER X 599 7. .383 22 .627 23. .364 0. .00 0. .00 PROB

ATOM 2421 HG1 SER X 599 7 .759 23 .158 24. .070 0. .00 0. .00 PROB

ATOM 2422 C SER X 599 8. .205 19 .958 22. .410 0. .00 0. .00 PROB

ATOM 2423 O SER X 599 7. .282 20 .031 21. .592 0. .00 0. .00 PROB

ATOM 2424 N SER X 600 9. .427 19 .481 22. .018 0. .00 0. .00 PROB

ATOM 2425 HN SER X 600 10 .160 19 .387 22. .688 0. .00 0. .00 PROB

ATOM 2426 CA SER X 600 9. .648 19 .270 20. .605 0. .00 0. .00 PROB

ATOM 2427 HA SER X 600 8. .925 19 .750 19. .962 0. .00 0. .00 PROB

ATOM 2428 CB SER X 600 11 .032 19 .783 20. .122 0. .00 0. .00 PROB

ATOM 2429 HB1 SER X 600 11 .790 19 .377 20. .826 0. .00 0. .00 PROB

ATOM 2430 HB2 SER X 600 11 .234 19 .447 19. .082 0. .00 0. .00 PROB

ATOM 2431 OG SER X 600 11 .051 21 .218 20. .184 0. .00 0. .00 PROB

ATOM 2432 HG1 SER X 600 11 .235 21 .461 21. .094 0. .00 0. .00 PROB

ATOM 2433 C SER X 600 9. .736 17 .795 20. .251 0. .00 0. .00 PROB

ATOM 2434 O SER X 600 9. .462 17 .396 19. .156 0. .00 0. .00 PROB

ATOM 2435 N GLY X 601 10 .051 16 .979 21. .277 0. .00 0. .00 PROB

ATOM 2436 HN GLY X 601 10 .356 17 .239 22. .190 0. .00 0. .00 PROB

ATOM 2437 CA GLY X 601 9. .996 15 .535 21. .121 0. .00 0. .00 PROB

ATOM 2438 HA1 GLY X 601 10 .638 15 .289 20. .288 0. .00 0. .00 PROB

ATOM 2439 HA2 GLY X 601 8 .969 15 .204 21. .170 0. .00 0. .00 PROB

ATOM 2440 C GLY X 601 10 .506 14 .863 22. .331 0. .00 0. .00 PROB

ATOM 2441 O GLY X 601 9. .863 14 .855 23. .362 0. .00 0. .00 PROB ATOM 2442 N LEU X 602 11.827 14.520 22..293 0..00 0..00 PROB

ATOM 2443 HN LEU X 602 12 .384 14 .540 21. .467 0. .00 0. .00 PROB

ATOM 2444 CA LEU X 602 12 .437 14 .004 23. .505 0. .00 0. .00 PROB

ATOM 2445 HA LEU X 602 11 .753 13 .890 24. .334 0. .00 0. .00 PROB

ATOM 2446 CB LEU X 602 12 .964 12 .535 23. .254 0. .00 0. .00 PROB

ATOM 2447 HB1 LEU X 602 13 .722 12 .796 22. .484 0. .00 0. .00 PROB

ATOM 2448 HB2 LEU X 602 13 .505 12 .097 24. .120 0. .00 0. .00 PROB

ATOM 2449 CG LEU X 602 11 .905 11 .561 22. .748 0. .00 0. .00 PROB

ATOM 2450 HG LEU X 602 11 .503 12 .069 21. .845 0. .00 0. .00 PROB

ATOM 2451 CD1 LEU X 602 12 .558 10 .212 22. .368 0. .00 0. .00 PROB

ATOM 2452 HD11 LEU X 602 13 .347 10 .400 21. .608 0. .00 0. .00 PROB

ATOM 2453 HD12 LEU X 602 13 .065 9 .733 23. .233 0. .00 0. .00 PROB

ATOM 2454 HD13 LEU X 602 11 .700 9 .551 22. .120 0. .00 0. .00 PROB

ATOM 2455 CD2 LEU X 602 10 .706 11 .324 23. .682 0. .00 0. .00 PROB

ATOM 2456 HD21 LEU X 602 10 .224 12 .324 23. .722 0. .00 0. .00 PROB

ATOM 2457 HD22 LEU X 602 9 .979 10 .638 23. .197 0. .00 0. .00 PROB

ATOM 2458 HD23 LEU X 602 11 .020 10 .796 24. .608 0. .00 0. .00 PROB

ATOM 2459 C LEU X 602 13 .708 14 .852 23. .879 0. .00 0. .00 PROB

ATOM 2460 O LEU X 602 14 .641 15 .138 23. .144 0. .00 0. .00 PROB

ATOM 2461 N GLY X 603 13 .633 15 .346 25. .128 0. .00 0. .00 PROB

ATOM 2462 HN GLY X 603 12 .787 15 .190 25. .632 0. .00 0. .00 PROB

ATOM 2463 CA GLY X 603 14 .781 15 .902 25. .809 0. .00 0. .00 PROB

ATOM 2464 HA1 GLY X 603 14 .365 16 .356 26. .697 0. .00 0. .00 PROB

ATOM 2465 HA2 GLY X 603 15 .214 16 .636 25. .146 0. .00 0. .00 PROB

ATOM 2466 C GLY X 603 15 .884 14 .962 26. .224 0. .00 0. .00 PROB

ATOM 2467 O GLY X 603 17 .068 15 .219 26. .087 0. .00 0. .00 PROB

ATOM 2468 N GLY X 604 15 .568 13 .853 26. .836 0. .00 0. .00 PROB

ATOM 2469 HN GLY X 604 14 .602 13 .672 27. .006 0. .00 0. .00 PROB

ATOM 2470 CA GLY X 604 16 .547 12 .763 27. .064 0. .00 0. .00 PROB

ATOM 2471 HA1 GLY X 604 16 .120 12 .215 27. .892 0. .00 0. .00 PROB

ATOM 2472 HA2 GLY X 604 17 .518 13 .175 27. .296 0. .00 0. .00 PROB

ATOM 2473 C GLY X 604 16 .823 11 .921 25. .923 0. .00 0. .00 PROB

ATOM 2474 O GLY X 604 16 .233 12 .250 24. .882 0. .00 0. .00 PROB

ATOM 2475 N PRO X 605 17 .635 10 .902 26. .035 0. .00 0. .00 PROB

ATOM 2476 CD PRO X 605 18 .435 10 .548 27. .273 0. .00 0. .00 PROB

ATOM 2477 HD1 PRO X 605 19 .078 11 .296 27. .786 0. .00 0. .00 PROB

ATOM 2478 HD2 PRO X 605 17 .800 10 .099 28. .067 0. .00 0. .00 PROB

ATOM 2479 CA PRO X 605 18 .016 10 .090 24. .942 0. .00 0. .00 PROB

ATOM 2480 HA PRO X 605 18 .576 10 .626 24. .190 0. .00 0. .00 PROB

ATOM 2481 CB PRO X 605 18 .813 8 .901 25. .600 0. .00 0. .00 PROB

ATOM 2482 HB1 PRO X 605 19 .690 8 .686 24. .952 0. .00 0. .00 PROB

ATOM 2483 HB2 PRO X 605 18 .241 8 .024 25. .971 0. .00 0. .00 PROB

ATOM 2484 CG PRO X 605 19 .502 9 .506 26. .823 0. .00 0. .00 PROB

ATOM 2485 HG1 PRO X 605 20 .376 10 .118 26. .515 0. .00 0. .00 PROB

ATOM 2486 HG2 PRO X 605 19 .797 8 .822 27. .648 0. .00 0. .00 PROB

ATOM 2487 C PRO X 605 16 .929 9 .545 24. .032 0. .00 0. .00 PROB

ATOM 2488 O PRO X 605 15 .843 9 .193 24. .526 0. .00 0. .00 PROB

ATOM 2489 N SER X 606 17 .197 9 .401 22. .715 0. .00 0. .00 PROB

ATOM 2490 HN SER X 606 18 .104 9 .644 22. .378 0. .00 0. .00 PROB

ATOM 2491 CA SER X 606 16 .344 8 .922 21. .703 0. .00 0. .00 PROB

ATOM 2492 HA SER X 606 15 .358 8 .785 22. .121 0. .00 0. .00 PROB

ATOM 2493 CB SER X 606 16 .205 9 .729 20. .376 0. .00 0. .00 PROB

ATOM 2494 HB1 SER X 606 15 .875 10 .734 20. .715 0. .00 0. .00 PROB

ATOM 2495 HB2 SER X 606 17 .220 9 .952 19. .984 0. .00 0. .00 PROB

ATOM 2496 OG SER X 606 15 .252 9 .223 19. .473 0. .00 0. .00 PROB

ATOM 2497 HG1 SER X 606 15 .291 9 .888 18. .782 0. .00 0. .00 PROB

ATOM 2498 C SER X 606 16 .858 7 .462 21. .487 0. .00 0. .00 PROB

ATOM 2499 O SER X 606 17 .719 6 .988 22. .219 0. .00 0. .00 PROB

ATOM 2500 N ILE X 607 16 .219 6 .746 20. .540 0. .00 0. .00 PROB

ATOM 2501 HN ILE X 607 15 .468 7 .289 20. .173 0. .00 0. .00 PROB

ATOM 2502 CA ILE X 607 16 .264 5 .301 20. .248 0. .00 0. .00 PROB

ATOM 2503 HA ILE X 607 17 .052 4 .829 20. .816 0. .00 0. .00 PROB

ATOM 2504 CB ILE X 607 14 .911 4 .695 20. .460 0. .00 0. .00 PROB

ATOM 2505 HB ILE X 607 14 .502 5 .118 21. .402 0. .00 0. .00 PROB

ATOM 2506 CG2 ILE X 607 13 .843 5 .146 19. .479 0. .00 0. .00 PROB

ATOM 2507 HG21 ILE X 607 13 .875 4 .672 18. .475 0. .00 0. .00 PROB ATOM 2508 HG22 ILE X 607 12.841 4.945 19..914 0..00 0..00 PROB

ATOM 2509 HG23 ILE X 607 13 .775 6 .244 19. .324 0. .00 0. .00 PROB

ATOM 2510 CGI ILE X 607 15 .003 3 .204 20. .714 0. .00 0. .00 PROB

ATOM 2511 HG11 ILE X 607 13 .933 2 .905 20. .720 0. .00 0. .00 PROB

ATOM 2512 HG12 ILE X 607 15 .488 2 .599 19. .918 0. .00 0. .00 PROB

ATOM 2513 CD ILE X 607 15 .717 2 .883 22. .085 0. .00 0. .00 PROB

ATOM 2514 HD1 ILE X 607 15 .265 3 .564 22. .837 0. .00 0. .00 PROB

ATOM 2515 HD2 ILE X 607 15 .633 1 .795 22. .293 0. .00 0. .00 PROB

ATOM 2516 HD3 ILE X 607 16 .754 3 .234 21. .897 0. .00 0. .00 PROB

ATOM 2517 C ILE X 607 16 .624 5 .211 18. .755 0. .00 0. .00 PROB

ATOM 2518 O ILE X 607 16 .784 4 .118 18. .127 0. .00 0. .00 PROB

ATOM 2519 N LYS X 608 16 .647 6 .394 18. .105 0. .00 0. .00 PROB

ATOM 2520 HN LYS X 608 16 .589 7 .155 18. .746 0. .00 0. .00 PROB

ATOM 2521 CA LYS X 608 16 .660 6 .538 16. .694 0. .00 0. .00 PROB

ATOM 2522 HA LYS X 608 16 .462 5 .574 16. .248 0. .00 0. .00 PROB

ATOM 2523 CB LYS X 608 15 .664 7 .697 16. .435 0. .00 0. .00 PROB

ATOM 2524 HB1 LYS X 608 14 .674 7 .521 16. .907 0. .00 0. .00 PROB

ATOM 2525 HB2 LYS X 608 16 .037 8 .627 16. .916 0. .00 0. .00 PROB

ATOM 2526 CG LYS X 608 15 .515 8 .085 14. .965 0. .00 0. .00 PROB

ATOM 2527 HG1 LYS X 608 14 .850 8 .966 14. .832 0. .00 0. .00 PROB

ATOM 2528 HG2 LYS X 608 16 .487 8 .276 14. .463 0. .00 0. .00 PROB

ATOM 2529 CD LYS X 608 14 .737 7 .099 14. .175 0. .00 0. .00 PROB

ATOM 2530 HD1 LYS X 608 14 .689 7 .553 13. .162 0. .00 0. .00 PROB

ATOM 2531 HD2 LYS X 608 15 .231 6 .105 14. .142 0. .00 0. .00 PROB

ATOM 2532 CE LYS X 608 13 .333 6 .694 14. .673 0. .00 0. .00 PROB

ATOM 2533 HE1 LYS X 608 12 .784 5 .902 14. .120 0. .00 0. .00 PROB

ATOM 2534 HE2 LYS X 608 13 .410 6 .205 15. .667 0. .00 0. .00 PROB

ATOM 2535 NZ LYS X 608 12 .498 7 .850 14. .933 0. .00 0. .00 PROB

ATOM 2536 HZ1 LYS X 608 12 .560 8 .522 14. .142 0. .00 0. .00 PROB

ATOM 2537 HZ2 LYS X 608 11 .494 7 .617 15. .071 0. .00 0. .00 PROB

ATOM 2538 HZ3 LYS X 608 12 .912 8 .314 15. .766 0. .00 0. .00 PROB

ATOM 2539 C LYS X 608 17 .972 6 .989 16. .169 0. .00 0. .00 PROB

ATOM 2540 O LYS X 608 18 .277 6 .835 15. .002 0. .00 0. .00 PROB

ATOM 2541 N ASP X 609 18 .979 7 .306 17. .072 0. .00 0. .00 PROB

ATOM 2542 HN ASP X 609 18 .764 7 .187 18. .038 0. .00 0. .00 PROB

ATOM 2543 CA ASP X 609 20 .386 7 .501 16. .782 0. .00 0. .00 PROB

ATOM 2544 HA ASP X 609 20 .371 7 .927 15. .789 0. .00 0. .00 PROB

ATOM 2545 CB ASP X 609 20 .935 8 .603 17. .677 0. .00 0. .00 PROB

ATOM 2546 HB1 ASP X 609 21 .967 8 .955 17. .467 0. .00 0. .00 PROB

ATOM 2547 HB2 ASP X 609 20 .212 9 .447 17. .675 0. .00 0. .00 PROB

ATOM 2548 CG ASP X 609 20 .830 8 .100 19. .110 0. .00 0. .00 PROB

ATOM 2549 OD1 ASP X 609 19 .751 8 .049 19. .759 0. .00 0. .00 PROB

ATOM 2550 OD2 ASP X 609 21 .951 7 .808 19. .678 0. .00 0. .00 PROB

ATOM 2551 C ASP X 609 21 .251 6 .258 16. .709 0. .00 0. .00 PROB

ATOM 2552 O ASP X 609 22 .429 6 .423 16. .294 0. .00 0. .00 PROB

ATOM 2553 N LYS X 610 20 .723 5 .030 17. .035 0. .00 0. .00 PROB

ATOM 2554 HN LYS X 610 19 .789 4 .964 17. .378 0. .00 0. .00 PROB

ATOM 2555 CA LYS X 610 21 .367 3 .794 16. .574 0. .00 0. .00 PROB

ATOM 2556 HA LYS X 610 22 .408 4 .050 16. .445 0. .00 0. .00 PROB

ATOM 2557 CB LYS X 610 21 .365 2 .595 17. .631 0. .00 0. .00 PROB

ATOM 2558 HB1 LYS X 610 22 .031 1 .740 17. .387 0. .00 0. .00 PROB

ATOM 2559 HB2 LYS X 610 21 .902 3 .084 18. .471 0. .00 0. .00 PROB

ATOM 2560 CG LYS X 610 20 .014 2 .101 18. .064 0. .00 0. .00 PROB

ATOM 2561 HG1 LYS X 610 19 .542 2 .932 18. .631 0. .00 0. .00 PROB

ATOM 2562 HG2 LYS X 610 19 .436 1 .907 17. .135 0. .00 0. .00 PROB

ATOM 2563 CD LYS X 610 20 .194 0 .817 18. .818 0. .00 0. .00 PROB

ATOM 2564 HD1 LYS X 610 20 .361 0 .013 18. .068 0. .00 0. .00 PROB

ATOM 2565 HD2 LYS X 610 21 .028 0 .937 19. .542 0. .00 0. .00 PROB

ATOM 2566 CE LYS X 610 18 .966 0 .651 19. .667 0. .00 0. .00 PROB

ATOM 2567 HE1 LYS X 610 18 .645 1 .486 20. .326 0. .00 0. .00 PROB

ATOM 2568 HE2 LYS X 610 18 .127 0 .547 18. .946 0. .00 0. .00 PROB

ATOM 2569 NZ LYS X 610 18 .974 -0 .585 20. .449 0. .00 0. .00 PROB

ATOM 2570 HZ1 LYS X 610 19 .473 -1 .295 19. .875 0. .00 0. .00 PROB

ATOM 2571 HZ2 LYS X 610 19 .558 -0 .466 21. .301 0. .00 0. .00 PROB

ATOM 2572 HZ3 LYS X 610 18 .040 -1 .005 20. .626 0. .00 0. .00 PROB

ATOM 2573 C LYS X 610 20 .939 3 .386 15. .235 0. .00 0. .00 PROB ATOM 2574 O LYS X 610 19.809 3.476 14..860 0..00 0..00 PROB

ATOM 2575 N TYR X 611 21 .834 2 .891 14. .342 0. .00 0. .00 PROB

ATOM 2576 HN TYR X 611 22 .727 2 .687 14. .735 0. .00 0. .00 PROB

ATOM 2577 CA TYR X 611 21 .536 2 .976 12. .900 0. .00 0. .00 PROB

ATOM 2578 HA TYR X 611 20 .816 3 .759 12. .713 0. .00 0. .00 PROB

ATOM 2579 CB TYR X 611 22 .816 3 .192 12. .083 0. .00 0. .00 PROB

ATOM 2580 HB1 TYR X 611 23 .589 2 .571 12. .583 0. .00 0. .00 PROB

ATOM 2581 HB2 TYR X 611 22 .705 2 .836 11. .036 0. .00 0. .00 PROB

ATOM 2582 CG TYR X 611 23 .261 4 .583 11. .987 0. .00 0. .00 PROB

ATOM 2583 CD1 TYR X 611 22 .503 5 .549 11. .309 0. .00 0. .00 PROB

ATOM 2584 HD1 TYR X 611 21 .624 5 .196 10. .790 0. .00 0. .00 PROB

ATOM 2585 CE1 TYR X 611 22 .943 6 .899 11. .229 0. .00 0. .00 PROB

ATOM 2586 HE1 TYR X 611 22 .400 7 .685 10. .725 0. .00 0. .00 PROB

ATOM 2587 CZ TYR X 611 24 .184 7 .196 11. .859 0. .00 0. .00 PROB

ATOM 2588 OH TYR X 611 24 .620 8 .509 11. .720 0. .00 0. .00 PROB

ATOM 2589 HH TYR X 611 25 .341 8 .680 12. .331 0. .00 0. .00 PROB

ATOM 2590 CD2 TYR X 611 24 .472 4 .904 12. .644 0. .00 0. .00 PROB

ATOM 2591 HD2 TYR X 611 25 .043 4 .219 13. .254 0. .00 0. .00 PROB

ATOM 2592 CE2 TYR X 611 24 .952 6 .245 12. .502 0. .00 0. .00 PROB

ATOM 2593 HE2 TYR X 611 25 .880 6 .549 12. .964 0. .00 0. .00 PROB

ATOM 2594 C TYR X 611 20 .830 1 .695 12. .375 0. .00 0. .00 PROB

ATOM 2595 O TYR X 611 20 .288 1 .660 11. .239 0. .00 0. .00 PROB

ATOM 2596 N VAL X 612 20 .685 0 .677 13. .292 0. .00 0. .00 PROB

ATOM 2597 HN VAL X 612 21 .138 0 .596 14. .176 0. .00 0. .00 PROB

ATOM 2598 CA VAL X 612 19 .782 -0 .456 13. .105 0. .00 0. .00 PROB

ATOM 2599 HA VAL X 612 19 .871 -0 .836 12. .098 0. .00 0. .00 PROB

ATOM 2600 CB VAL X 612 20 .180 -1 .405 14. .245 0. .00 0. .00 PROB

ATOM 2601 HB VAL X 612 21 .263 -1 .613 14. .112 0. .00 0. .00 PROB

ATOM 2602 CGI VAL X 612 19 .903 -0 .969 15. .743 0. .00 0. .00 PROB

ATOM 2603 HG11 VAL X 612 20 .337 0 .048 15. .856 0. .00 0. .00 PROB

ATOM 2604 HG12 VAL X 612 18 .851 -1 .069 16. .088 0. .00 0. .00 PROB

ATOM 2605 HG13 VAL X 612 20 .574 -1 .618 16. .344 0. .00 0. .00 PROB

ATOM 2606 CG2 VAL X 612 19 .657 -2 .852 13. .913 0. .00 0. .00 PROB

ATOM 2607 HG21 VAL X 612 20 .036 -3 .022 12. .882 0. .00 0. .00 PROB

ATOM 2608 HG22 VAL X 612 20 .147 -3 .582 14. .592 0. .00 0. .00 PROB

ATOM 2609 HG23 VAL X 612 18 .546 -2 .876 13. .894 0. .00 0. .00 PROB

ATOM 2610 C VAL X 612 18 .324 -0 .020 13. .319 0. .00 0. .00 PROB

ATOM 2611 O VAL X 612 17 .412 -0 .539 12. .683 0. .00 0. .00 PROB

ATOM 2612 N THR X 613 18 .049 0 .959 14. .182 0. .00 0. .00 PROB

ATOM 2613 HN THR X 613 18 .787 1 .406 14. .682 0. .00 0. .00 PROB

ATOM 2614 CA THR X 613 16 .653 1 .458 14. .332 0. .00 0. .00 PROB

ATOM 2615 HA THR X 613 16 .034 0 .576 14. .256 0. .00 0. .00 PROB

ATOM 2616 CB THR X 613 16 .171 2 .074 15. .710 0. .00 0. .00 PROB

ATOM 2617 HB THR X 613 16 .554 3 .099 15. .900 0. .00 0. .00 PROB

ATOM 2618 OG1 THR X 613 16 .825 1 .344 16. .704 0. .00 0. .00 PROB

ATOM 2619 HG1 THR X 613 16 .983 1 .947 17. .434 0. .00 0. .00 PROB

ATOM 2620 CG2 THR X 613 14 .643 1 .920 15. .833 0. .00 0. .00 PROB

ATOM 2621 HG21 THR X 613 14 .150 2 .239 14. .889 0. .00 0. .00 PROB

ATOM 2622 HG22 THR X 613 14 .304 0 .862 15. .860 0. .00 0. .00 PROB

ATOM 2623 HG23 THR X 613 14 .113 2 .371 16. .699 0. .00 0. .00 PROB

ATOM 2624 C THR X 613 16 .168 2 .263 13. .203 0. .00 0. .00 PROB

ATOM 2625 O THR X 613 15 .032 2 .130 12. .691 0. .00 0. .00 PROB

ATOM 2626 N ALA X 614 17 .107 3 .196 12. .802 0. .00 0. .00 PROB

ATOM 2627 HN ALA X 614 17 .982 3 .283 13. .273 0. .00 0. .00 PROB

ATOM 2628 CA ALA X 614 16 .949 4 .085 11. .698 0. .00 0. .00 PROB

ATOM 2629 HA ALA X 614 16 .063 4 .702 11. .701 0. .00 0. .00 PROB

ATOM 2630 CB ALA X 614 18 .300 4 .993 11. .522 0. .00 0. .00 PROB

ATOM 2631 HB1 ALA X 614 18 .053 5 .664 10. .672 0. .00 0. .00 PROB

ATOM 2632 HB2 ALA X 614 18 .516 5 .592 12. .432 0. .00 0. .00 PROB

ATOM 2633 HB3 ALA X 614 19 .218 4 .386 11. .371 0. .00 0. .00 PROB

ATOM 2634 C ALA X 614 16 .762 3 .262 10. .417 0. .00 0. .00 PROB

ATOM 2635 O ALA X 614 15 .827 3 .481 9. .694 0. .00 0. .00 PROB

ATOM 2636 N LEU X 615 17 .677 2 .230 10. .159 0. .00 0. .00 PROB

ATOM 2637 HN LEU X 615 18 .566 2 .151 10. .604 0. .00 0. .00 PROB

ATOM 2638 CA LEU X 615 17 .439 1 .293 9. .102 0. .00 0. .00 PROB

ATOM 2639 HA LEU X 615 17 .429 1 .932 8. .231 0. .00 0. .00 PROB ATOM 2640 CB LEU X 615 18.648 0.343 8..907 0..00 0..00 PROB

ATOM 2641 HB1 LEU X 615 19 .590 0 .902 8. .725 0. .00 0. .00 PROB

ATOM 2642 HB2 LEU X 615 18 .708 -0 .276 9. .828 0. .00 0. .00 PROB

ATOM 2643 CG LEU X 615 18 .374 -0 .701 7. .765 0. .00 0. .00 PROB

ATOM 2644 HG LEU X 615 17 .486 -1 .248 8. .150 0. .00 0. .00 PROB

ATOM 2645 CD1 LEU X 615 18 .127 -0 .057 6. .411 0. .00 0. .00 PROB

ATOM 2646 HD11 LEU X 615 18 .000 -0 .818 5. .612 0. .00 0. .00 PROB

ATOM 2647 HD12 LEU X 615 18 .954 0 .616 6. .099 0. .00 0. .00 PROB

ATOM 2648 HD13 LEU X 615 17 .144 0 .445 6. .538 0. .00 0. .00 PROB

ATOM 2649 CD2 LEU X 615 19 .662 -1 .484 7. .541 0. .00 0. .00 PROB

ATOM 2650 HD21 LEU X 615 19 .627 -2 .279 6. .766 0. .00 0. .00 PROB

ATOM 2651 HD22 LEU X 615 20 .553 -0 .874 7. .282 0. .00 0. .00 PROB

ATOM 2652 HD23 LEU X 615 19 .810 -2 .086 8. .463 0. .00 0. .00 PROB

ATOM 2653 C LEU X 615 16 .093 0 .590 9. .204 0. .00 0. .00 PROB

ATOM 2654 O LEU X 615 15 .342 0 .523 8. .216 0. .00 0. .00 PROB

ATOM 2655 N TYR X 616 15 .734 -0 .026 10. .325 0. .00 0. .00 PROB

ATOM 2656 HN TYR X 616 16 .336 0 .014 11. .119 0. .00 0. .00 PROB

ATOM 2657 CA TYR X 616 14 .495 -0 .659 10. .614 0. .00 0. .00 PROB

ATOM 2658 HA TYR X 616 14 .443 -1 .543 9. .996 0. .00 0. .00 PROB

ATOM 2659 CB TYR X 616 14 .440 -1 .131 12. .101 0. .00 0. .00 PROB

ATOM 2660 HB1 TYR X 616 15 .314 -1 .717 12. .457 0. .00 0. .00 PROB

ATOM 2661 HB2 TYR X 616 14 .200 -0 .226 12. .699 0. .00 0. .00 PROB

ATOM 2662 CG TYR X 616 13 .385 -2 .205 12. .305 0. .00 0. .00 PROB

ATOM 2663 CD1 TYR X 616 13 .526 -3 .506 11. .790 0. .00 0. .00 PROB

ATOM 2664 HD1 TYR X 616 14 .472 -3 .696 11. .307 0. .00 0. .00 PROB

ATOM 2665 CE1 TYR X 616 12 .652 -4 .564 11. .999 0. .00 0. .00 PROB

ATOM 2666 HE1 TYR X 616 13 .023 -5 .553 11. .773 0. .00 0. .00 PROB

ATOM 2667 CZ TYR X 616 11 .429 -4 .282 12. .622 0. .00 0. .00 PROB

ATOM 2668 OH TYR X 616 10 .484 -5 .307 12. .934 0. .00 0. .00 PROB

ATOM 2669 HH TYR X 616 9. .881 -4 .995 13. .614 0. .00 0. .00 PROB

ATOM 2670 CD2 TYR X 616 12 .141 -1 .988 12. .979 0. .00 0. .00 PROB

ATOM 2671 HD2 TYR X 616 11 .856 -0 .964 13. .170 0. .00 0. .00 PROB

ATOM 2672 CE2 TYR X 616 11 .170 -2 .964 13. .114 0. .00 0. .00 PROB

ATOM 2673 HE2 TYR X 616 10 .216 -2 .729 13. .562 0. .00 0. .00 PROB

ATOM 2674 C TYR X 616 13 .296 0 .175 10. .281 0. .00 0. .00 PROB

ATOM 2675 O TYR X 616 12 .370 -0 .275 9. .603 0. .00 0. .00 PROB

ATOM 2676 N PHE X 617 13 .281 1 .436 10. .718 0. .00 0. .00 PROB

ATOM 2677 HN PHE X 617 14 .031 1 .680 11. .328 0. .00 0. .00 PROB

ATOM 2678 CA PHE X 617 12 .238 2 .429 10. .395 0. .00 0. .00 PROB

ATOM 2679 HA PHE X 617 11 .305 2 .002 10. .733 0. .00 0. .00 PROB

ATOM 2680 CB PHE X 617 12 .515 3 .664 11. .271 0. .00 0. .00 PROB

ATOM 2681 HB1 PHE X 617 12 .519 3 .380 12. .345 0. .00 0. .00 PROB

ATOM 2682 HB2 PHE X 617 13 .546 3 .996 11. .025 0. .00 0. .00 PROB

ATOM 2683 CG PHE X 617 11 .501 4 .722 11. .137 0. .00 0. .00 PROB

ATOM 2684 CD1 PHE X 617 10 .119 4 .576 10. .771 0. .00 0. .00 PROB

ATOM 2685 HD1 PHE X 617 9 .625 3 .643 10. .543 0. .00 0. .00 PROB

ATOM 2686 CE1 PHE X 617 9 .344 5 .694 10. .640 0. .00 0. .00 PROB

ATOM 2687 HE1 PHE X 617 8 .306 5 .491 10. .423 0. .00 0. .00 PROB

ATOM 2688 CZ PHE X 617 9. .844 6 .975 10. .874 0. .00 0. .00 PROB

ATOM 2689 HZ PHE X 617 9. .289 7 .889 10. .725 0. .00 0. .00 PROB

ATOM 2690 CD2 PHE X 617 12 .028 5 .983 11. .304 0. .00 0. .00 PROB

ATOM 2691 HD2 PHE X 617 13 .101 6 .010 11. .419 0. .00 0. .00 PROB

ATOM 2692 CE2 PHE X 617 11 .239 7 .134 11. .284 0. .00 0. .00 PROB

ATOM 2693 HE2 PHE X 617 11 .652 8 .116 11. .465 0. .00 0. .00 PROB

ATOM 2694 C PHE X 617 12 .138 2 .629 8. .879 0. .00 0. .00 PROB

ATOM 2695 O PHE X 617 11 .063 2 .629 8. .307 0. .00 0. .00 PROB

ATOM 2696 N THR X 618 13 .271 2 .832 8. .252 0. .00 0. .00 PROB

ATOM 2697 HN THR X 618 14 .110 2 .754 8. .784 0. .00 0. .00 PROB

ATOM 2698 CA THR X 618 13 .430 3 .256 6. .867 0. .00 0. .00 PROB

ATOM 2699 HA THR X 618 12 .775 4 .100 6. .710 0. .00 0. .00 PROB

ATOM 2700 CB THR X 618 14 .924 3 .567 6. .511 0. .00 0. .00 PROB

ATOM 2701 HB THR X 618 15 .534 2 .659 6. .704 0. .00 0. .00 PROB

ATOM 2702 OG1 THR X 618 15 .435 4 .546 7. .353 0. .00 0. .00 PROB

ATOM 2703 HG1 THR X 618 15 .632 4 .188 8. .221 0. .00 0. .00 PROB

ATOM 2704 CG2 THR X 618 15 .096 4 .041 4. .979 0. .00 0. .00 PROB

ATOM 2705 HG21 THR X 618 14 .952 3 .160 4. .317 0. .00 0. .00 PROB ATOM 2706 HG22 THR X 618 14.293 4.795 4..836 0..00 0..00 PROB

ATOM 2707 HG23 THR X 618 16 .116 4 .472 4. .888 0. .00 0. .00 PROB

ATOM 2708 C THR X 618 12 .834 2 .206 5. .929 0. .00 0. .00 PROB

ATOM 2709 O THR X 618 12 .056 2 .432 4. .964 0. .00 0. .00 PROB

ATOM 2710 N PHE X 619 13 .131 0 .941 6. .138 0. .00 0. .00 PROB

ATOM 2711 HN PHE X 619 13 .893 0 .780 6. .761 0. .00 0. .00 PROB

ATOM 2712 CA PHE X 619 12 .522 -0 .160 5. .457 0. .00 0. .00 PROB

ATOM 2713 HA PHE X 619 12 .632 0 .019 4. .398 0. .00 0. .00 PROB

ATOM 2714 CB PHE X 619 13 .252 -1 .486 5. .903 0. .00 0. .00 PROB

ATOM 2715 HB1 PHE X 619 14 .282 -1 .409 5. .495 0. .00 0. .00 PROB

ATOM 2716 HB2 PHE X 619 13 .353 -1 .577 7. .006 0. .00 0. .00 PROB

ATOM 2717 CG PHE X 619 12 .708 -2 .693 5. .164 0. .00 0. .00 PROB

ATOM 2718 CD1 PHE X 619 12 .743 -2 .814 3. .780 0. .00 0. .00 PROB

ATOM 2719 HD1 PHE X 619 13 .146 -2 .014 3. .175 0. .00 0. .00 PROB

ATOM 2720 CE1 PHE X 619 12 .117 -3 .889 3. .101 0. .00 0. .00 PROB

ATOM 2721 HE1 PHE X 619 11 .931 -3 .797 2. .041 0. .00 0. .00 PROB

ATOM 2722 CZ PHE X 619 11 .486 -4 .845 3. .899 0. .00 0. .00 PROB

ATOM 2723 HZ PHE X 619 11 .079 -5 .744 3. .459 0. .00 0. .00 PROB

ATOM 2724 CD2 PHE X 619 12 .105 -3 .712 5. .937 0. .00 0. .00 PROB

ATOM 2725 HD2 PHE X 619 12 .224 -3 .590 7. .003 0. .00 0. .00 PROB

ATOM 2726 CE2 PHE X 619 11 .438 -4 .731 5. .289 0. .00 0. .00 PROB

ATOM 2727 HE2 PHE X 619 10 .939 -5 .505 5. .854 0. .00 0. .00 PROB

ATOM 2728 C PHE X 619 11 .051 -0 .234 5. .750 0. .00 0. .00 PROB

ATOM 2729 O PHE X 619 10 .287 -0 .393 4. .830 0. .00 0. .00 PROB

ATOM 2730 N SER X 620 10 .593 -0 .096 7. .021 0. .00 0. .00 PROB

ATOM 2731 HN SER X 620 11 .190 0 .221 7. .754 0. .00 0. .00 PROB

ATOM 2732 CA SER X 620 9. .215 -0 .174 7. .419 0. .00 0. .00 PROB

ATOM 2733 HA SER X 620 8. .961 -1 .148 7. .027 0. .00 0. .00 PROB

ATOM 2734 CB SER X 620 9. .139 -0 .327 9. .005 0. .00 0. .00 PROB

ATOM 2735 HB1 SER X 620 8 .158 -0 .742 9. .323 0. .00 0. .00 PROB

ATOM 2736 HB2 SER X 620 9 .868 -1 .120 9. .277 0. .00 0. .00 PROB

ATOM 2737 OG SER X 620 9. .247 0 .850 9. .824 0. .00 0. .00 PROB

ATOM 2738 HG1 SER X 620 10 .115 1 .261 9. .827 0. .00 0. .00 PROB

ATOM 2739 C SER X 620 8. .278 0 .939 6. .924 0. .00 0. .00 PROB

ATOM 2740 O SER X 620 7. .100 0 .684 6. .646 0. .00 0. .00 PROB

ATOM 2741 N SER X 621 8. .742 2 .220 6. .828 0. .00 0. .00 PROB

ATOM 2742 HN SER X 621 9. .633 2 .411 7. .232 0. .00 0. .00 PROB

ATOM 2743 CA SER X 621 8. .048 3 .329 6. .272 0. .00 0. .00 PROB

ATOM 2744 HA SER X 621 7. .053 3 .289 6. .689 0. .00 0. .00 PROB

ATOM 2745 CB SER X 621 8. .699 4 .626 6. .669 0. .00 0. .00 PROB

ATOM 2746 HB1 SER X 621 8 .261 5 .390 5. .992 0. .00 0. .00 PROB

ATOM 2747 HB2 SER X 621 8 .310 4 .856 7. .684 0. .00 0. .00 PROB

ATOM 2748 OG SER X 621 10 .176 4 .688 6. .704 0. .00 0. .00 PROB

ATOM 2749 HG1 SER X 621 10 .515 5 .489 7. .109 0. .00 0. .00 PROB

ATOM 2750 C SER X 621 8. .027 3 .242 4. .767 0. .00 0. .00 PROB

ATOM 2751 O SER X 621 7. .083 3 .708 4. .132 0. .00 0. .00 PROB

ATOM 2752 N LEU X 622 9. .125 2 .710 4. .157 0. .00 0. .00 PROB

ATOM 2753 HN LEU X 622 9. .850 2 .426 4. .780 0. .00 0. .00 PROB

ATOM 2754 CA LEU X 622 9. .287 2 .619 2. .715 0. .00 0. .00 PROB

ATOM 2755 HA LEU X 622 9. .173 3 .611 2. .305 0. .00 0. .00 PROB

ATOM 2756 CB LEU X 622 10 .549 1 .814 2. .296 0. .00 0. .00 PROB

ATOM 2757 HB1 LEU X 622 11 .475 2 .201 2. .773 0. .00 0. .00 PROB

ATOM 2758 HB2 LEU X 622 10 .458 0 .736 2. .546 0. .00 0. .00 PROB

ATOM 2759 CG LEU X 622 10 .707 1 .942 0. .707 0. .00 0. .00 PROB

ATOM 2760 HG LEU X 622 9. .853 1 .440 0. .204 0. .00 0. .00 PROB

ATOM 2761 CD1 LEU X 622 11 .092 3 .224 0. .129 0. .00 0. .00 PROB

ATOM 2762 HD11 LEU X 622 11 .636 3 .004 -0. .815 0. .00 0. .00 PROB

ATOM 2763 HD12 LEU X 622 10 .150 3 .777 -0. .076 0. .00 0. .00 PROB

ATOM 2764 HD13 LEU X 622 11 .848 3 .745 0. .755 0. .00 0. .00 PROB

ATOM 2765 CD2 LEU X 622 11 .924 0 .935 0. .417 0. .00 0. .00 PROB

ATOM 2766 HD21 LEU X 622 12 .890 1 .445 0. .215 0. .00 0. .00 PROB

ATOM 2767 HD22 LEU X 622 12 .030 0 .321 1. .337 0. .00 0. .00 PROB

ATOM 2768 HD23 LEU X 622 11 .807 0 .248 -0. .449 0. .00 0. .00 PROB

ATOM 2769 C LEU X 622 8. .174 1 .833 2. .095 0. .00 0. .00 PROB

ATOM 2770 O LEU X 622 7. .442 2 .264 1. .203 0. .00 0. .00 PROB

ATOM 2771 N THR X 623 7. .942 0 .577 2. .591 0. .00 0. .00 PROB ATOM 2772 HN THR X 623 8..531 0.229 3..316 0..00 0..00 PROB

ATOM 2773 CA THR X 623 6. .901 -0 .370 2. .094 0. .00 0. .00 PROB

ATOM 2774 HA THR X 623 6. .556 0 .067 1. .168 0. .00 0. .00 PROB

ATOM 2775 CB THR X 623 7. .435 -1 .765 1. .888 0. .00 0. .00 PROB

ATOM 2776 HB THR X 623 8. .207 -1 .631 1. .100 0. .00 0. .00 PROB

ATOM 2777 OG1 THR X 623 6 .448 -2 .694 1. .442 0. .00 0. .00 PROB

ATOM 2778 HG1 THR X 623 5 .809 -2 .791 2. .152 0. .00 0. .00 PROB

ATOM 2779 CG2 THR X 623 8 .004 -2 .404 3. .201 0. .00 0. .00 PROB

ATOM 2780 HG21 THR X 623 8 .805 -1 .720 3. .558 0. .00 0. .00 PROB

ATOM 2781 HG22 THR X 623 7 .231 -2 .465 3. .997 0. .00 0. .00 PROB

ATOM 2782 HG23 THR X 623 8 .417 -3 .434 3. .165 0. .00 0. .00 PROB

ATOM 2783 C THR X 623 5. .725 -0 .407 3. .097 0. .00 0. .00 PROB

ATOM 2784 O THR X 623 4. .966 -1 .336 3. .228 0. .00 0. .00 PROB

ATOM 2785 N SER X 624 5. .537 0 .722 3. .780 0. .00 0. .00 PROB

ATOM 2786 HN SER X 624 6. .273 1 .389 3. .695 0. .00 0. .00 PROB

ATOM 2787 CA SER X 624 4. .401 1 .042 4. .578 0. .00 0. .00 PROB

ATOM 2788 HA SER X 624 4. .703 1 .891 5. .173 0. .00 0. .00 PROB

ATOM 2789 CB SER X 624 3. .208 1 .494 3. .666 0. .00 0. .00 PROB

ATOM 2790 HB1 SER X 624 2 .931 0 .610 3. .053 0. .00 0. .00 PROB

ATOM 2791 HB2 SER X 624 2 .340 1 .866 4. .253 0. .00 0. .00 PROB

ATOM 2792 OG SER X 624 3. .709 2 .615 2. .918 0. .00 0. .00 PROB

ATOM 2793 HG1 SER X 624 2 .977 3 . Ill 2. .545 0. .00 0. .00 PROB

ATOM 2794 C SER X 624 3. .824 0 .041 5. .610 0. .00 0. .00 PROB

ATOM 2795 O SER X 624 2. .605 -0 .090 5. .705 0. .00 0. .00 PROB

ATOM 2796 N VAL X 625 4. .688 -0 .786 6. .262 0. .00 0. .00 PROB

ATOM 2797 HN VAL X 625 5. .651 -0 .759 6. .007 0. .00 0. .00 PROB

ATOM 2798 CA VAL X 625 4. .367 -1 .830 7. .264 0. .00 0. .00 PROB

ATOM 2799 HA VAL X 625 3. .844 -2 .636 6. .771 0. .00 0. .00 PROB

ATOM 2800 CB VAL X 625 5. .613 -2 .572 7. .827 0. .00 0. .00 PROB

ATOM 2801 HB VAL X 625 6. .313 -1 .852 8. .301 0. .00 0. .00 PROB

ATOM 2802 CGI VAL X 625 5 .300 -3 .680 8. .748 0. .00 0. .00 PROB

ATOM 2803 HG11 VAL X 625 4 .646 -3 .402 9. .602 0. .00 0. .00 PROB

ATOM 2804 HG12 VAL X 625 4 .708 -4 .432 8. .183 0. .00 0. .00 PROB

ATOM 2805 HG13 VAL X 625 6 .201 -4 .187 9. .156 0. .00 0. .00 PROB

ATOM 2806 CG2 VAL X 625 6 .425 -3 .078 6. .608 0. .00 0. .00 PROB

ATOM 2807 HG21 VAL X 625 5 .689 -3 .559 5. .929 0. .00 0. .00 PROB

ATOM 2808 HG22 VAL X 625 6 .802 -2 .190 6. .057 0. .00 0. .00 PROB

ATOM 2809 HG23 VAL X 625 7 .220 -3 .772 6. .954 0. .00 0. .00 PROB

ATOM 2810 C VAL X 625 3. .576 -1 .299 8. .436 0. .00 0. .00 PROB

ATOM 2811 O VAL X 625 2. .512 -1 .888 8. .778 0. .00 0. .00 PROB

ATOM 2812 N GLY X 626 4. .002 -0 .157 9. .108 0. .00 0. .00 PROB

ATOM 2813 HN GLY X 626 4. .877 0 .274 8. .902 0. .00 0. .00 PROB

ATOM 2814 CA GLY X 626 3. .158 0 .548 10. .108 0. .00 0. .00 PROB

ATOM 2815 HA1 GLY X 626 2 .106 0 .624 9. .875 0. .00 0. .00 PROB

ATOM 2816 HA2 GLY X 626 3 .485 1 .562 10. .285 0. .00 0. .00 PROB

ATOM 2817 C GLY X 626 3. .192 -0 .161 11. .460 0. .00 0. .00 PROB

ATOM 2818 O GLY X 626 2. .182 -0 .375 12. .116 0. .00 0. .00 PROB

ATOM 2819 N PHE X 627 4. .405 -0 .502 11. .956 0. .00 0. .00 PROB

ATOM 2820 HN PHE X 627 5. .142 -0 .453 11. .287 0. .00 0. .00 PROB

ATOM 2821 CA PHE X 627 4. .661 -1 .143 13. .218 0. .00 0. .00 PROB

ATOM 2822 HA PHE X 627 3. .846 -1 .844 13. .317 0. .00 0. .00 PROB

ATOM 2823 CB PHE X 627 5. .970 -1 .889 13. .394 0. .00 0. .00 PROB

ATOM 2824 HB1 PHE X 627 6 .843 -1 .265 13. .105 0. .00 0. .00 PROB

ATOM 2825 HB2 PHE X 627 6 .284 -2 .191 14. .416 0. .00 0. .00 PROB

ATOM 2826 CG PHE X 627 5. .919 -3 .239 12. .647 0. .00 0. .00 PROB

ATOM 2827 CD1 PHE X 627 7 .158 -3 .722 12. .124 0. .00 0. .00 PROB

ATOM 2828 HD1 PHE X 627 7 .953 -2 .998 12. .231 0. .00 0. .00 PROB

ATOM 2829 CE1 PHE X 627 7 .335 -5 .001 11. .632 0. .00 0. .00 PROB

ATOM 2830 HE1 PHE X 627 8 .353 -5 .248 11. .370 0. .00 0. .00 PROB

ATOM 2831 CZ PHE X 627 6. .205 -5 .837 11. .537 0. .00 0. .00 PROB

ATOM 2832 HZ PHE X 627 6. .378 -6 .829 11. .147 0. .00 0. .00 PROB

ATOM 2833 CD2 PHE X 627 4 .803 -4 .126 12. .518 0. .00 0. .00 PROB

ATOM 2834 HD2 PHE X 627 3 .813 -3 .835 12. .837 0. .00 0. .00 PROB

ATOM 2835 CE2 PHE X 627 4 .968 -5 .342 11. .817 0. .00 0. .00 PROB

ATOM 2836 HE2 PHE X 627 4 .077 -5 .932 11. .662 0. .00 0. .00 PROB

ATOM 2837 C PHE X 627 4. .509 -0 .202 14. .306 0. .00 0. .00 PROB ATOM 2838 O PHE X 627 4..120 -0.685 15..376 0..00 0..00 PROB

ATOM 2839 N GLY X 628 4. .831 1 .075 14. .201 0. .00 0. .00 PROB

ATOM 2840 HN GLY X 628 5. .237 1 .553 13. .426 0. .00 0. .00 PROB

ATOM 2841 CA GLY X 628 4. .456 2 .119 15. .057 0. .00 0. .00 PROB

ATOM 2842 HA1 GLY X 628 3 .442 1 .969 15. .395 0. .00 0. .00 PROB

ATOM 2843 HA2 GLY X 628 4 .615 3 .077 14. .585 0. .00 0. .00 PROB

ATOM 2844 C GLY X 628 5. .228 2 .294 16. .349 0. .00 0. .00 PROB

ATOM 2845 O GLY X 628 5. .304 3 .355 16. .886 0. .00 0. .00 PROB

ATOM 2846 N ASN X 629 5. .863 1 .190 16. .849 0. .00 0. .00 PROB

ATOM 2847 HN ASN X 629 5. .566 0 .288 16. .544 0. .00 0. .00 PROB

ATOM 2848 CA ASN X 629 6. .921 1 .256 17. .821 0. .00 0. .00 PROB

ATOM 2849 HA ASN X 629 6. .436 1 .791 18. .625 0. .00 0. .00 PROB

ATOM 2850 CB ASN X 629 7. .304 -0 .116 18. .371 0. .00 0. .00 PROB

ATOM 2851 HB1 ASN X 629 7 .944 -0 .630 17. .623 0. .00 0. .00 PROB

ATOM 2852 HB2 ASN X 629 7 .865 -0 .028 19. .326 0. .00 0. .00 PROB

ATOM 2853 CG ASN X 629 6. .076 -0 .964 18. .728 0. .00 0. .00 PROB

ATOM 2854 OD1 ASN X 629 4 .928 -0 .623 19. .080 0. .00 0. .00 PROB

ATOM 2855 ND2 ASN X 629 6 .287 -2 .332 18. .461 0. .00 0. .00 PROB

ATOM 2856 HD21 ASN X 629 5 .578 -2 .978 18. .743 0. .00 0. .00 PROB

ATOM 2857 HD22 ASN X 629 7 .182 -2 .691 18. .195 0. .00 0. .00 PROB

ATOM 2858 C ASN X 629 8. .165 2 .119 17. .230 0. .00 0. .00 PROB

ATOM 2859 O ASN X 629 8. .443 3 .144 17. .819 0. .00 0. .00 PROB

ATOM 2860 N VAL X 630 8. .752 1 .854 16. .078 0. .00 0. .00 PROB

ATOM 2861 HN VAL X 630 8. .375 1 .121 15. .517 0. .00 0. .00 PROB

ATOM 2862 CA VAL X 630 9. .569 2 .755 15. .306 0. .00 0. .00 PROB

ATOM 2863 HA VAL X 630 10 .129 3 .376 15. .990 0. .00 0. .00 PROB

ATOM 2864 CB VAL X 630 10 .498 2 .134 14. .315 0. .00 0. .00 PROB

ATOM 2865 HB VAL X 630 11 .097 2 .897 13. .774 0. .00 0. .00 PROB

ATOM 2866 CGI VAL X 630 11 .459 1 .327 15. .104 0. .00 0. .00 PROB

ATOM 2867 HG11 VAL X 630 10 .951 0 .441 15. .542 0. .00 0. .00 PROB

ATOM 2868 HG12 VAL X 630 12 .257 0 .930 14. .441 0. .00 0. .00 PROB

ATOM 2869 HG13 VAL X 630 11 .886 1 .807 16. .011 0. .00 0. .00 PROB

ATOM 2870 CG2 VAL X 630 9 .768 1 .227 13. .317 0. .00 0. .00 PROB

ATOM 2871 HG21 VAL X 630 10 .436 0 .744 12. .572 0. .00 0. .00 PROB

ATOM 2872 HG22 VAL X 630 9 .266 0 .372 13. .819 0. .00 0. .00 PROB

ATOM 2873 HG23 VAL X 630 8 .965 1 .736 12. .742 0. .00 0. .00 PROB

ATOM 2874 C VAL X 630 8. .685 3 .747 14. .565 0. .00 0. .00 PROB

ATOM 2875 O VAL X 630 7. .697 3 .419 13. .970 0. .00 0. .00 PROB

ATOM 2876 N SER X 631 8. .951 4 .987 14. .850 0. .00 0. .00 PROB

ATOM 2877 HN SER X 631 9. .627 5 .384 15. .466 0. .00 0. .00 PROB

ATOM 2878 CA SER X 631 8. .050 6 .045 14. .424 0. .00 0. .00 PROB

ATOM 2879 HA SER X 631 7. .720 6 .001 13. .397 0. .00 0. .00 PROB

ATOM 2880 CB SER X 631 6. .747 6 .016 15. .370 0. .00 0. .00 PROB

ATOM 2881 HB1 SER X 631 6 .166 5 .101 15. .127 0. .00 0. .00 PROB

ATOM 2882 HB2 SER X 631 6 .992 5 .922 16. .449 0. .00 0. .00 PROB

ATOM 2883 OG SER X 631 5. .888 7 .193 15. .184 0. .00 0. .00 PROB

ATOM 2884 HG1 SER X 631 5 .334 7 .296 15. .962 0. .00 0. .00 PROB

ATOM 2885 C SER X 631 8. .816 7 .356 14. .639 0. .00 0. .00 PROB

ATOM 2886 O SER X 631 9. .869 7 .201 15. .298 0. .00 0. .00 PROB

ATOM 2887 N PRO X 632 8. .486 8 .610 14. .132 0. .00 0. .00 PROB

ATOM 2888 CD PRO X 632 7. .456 8 .811 13. .042 0. .00 0. .00 PROB

ATOM 2889 HD1 PRO X 632 7 .427 7 .889 12. .424 0. .00 0. .00 PROB

ATOM 2890 HD2 PRO X 632 6 .436 9 .101 13. .374 0. .00 0. .00 PROB

ATOM 2891 CA PRO X 632 9. .215 9 .904 14. .420 0. .00 0. .00 PROB

ATOM 2892 HA PRO X 632 10 .269 9 .785 14. .220 0. .00 0. .00 PROB

ATOM 2893 CB PRO X 632 8. .544 10 .869 13. .442 0. .00 0. .00 PROB

ATOM 2894 HB1 PRO X 632 9 .222 11 .657 13. .050 0. .00 0. .00 PROB

ATOM 2895 HB2 PRO X 632 7 .762 11 .456 13. .969 0. .00 0. .00 PROB

ATOM 2896 CG PRO X 632 7. .928 9 .995 12. .352 0. .00 0. .00 PROB

ATOM 2897 HG1 PRO X 632 8 .626 9 .699 11. .540 0. .00 0. .00 PROB

ATOM 2898 HG2 PRO X 632 7 .128 10 .513 11. .781 0. .00 0. .00 PROB

ATOM 2899 C PRO X 632 9. .264 10 .231 15. .878 0. .00 0. .00 PROB

ATOM 2900 O PRO X 632 8. .223 10 .232 16. .606 0. .00 0. .00 PROB

ATOM 2901 N ASN X 633 10 .461 10 .644 16. .488 0. .00 0. .00 PROB

ATOM 2902 HN ASN X 633 11 .306 10 .684 15. .961 0. .00 0. .00 PROB

ATOM 2903 CA ASN X 633 10 .474 11 .053 17. .939 0. .00 0. .00 PROB ATOM 2904 HA ASN X 633 9..632 10.766 18..551 0..00 0..00 PROB

ATOM 2905 CB ASN X 633 11 .833 10 .485 18. .536 0. .00 0. .00 PROB

ATOM 2906 HB1 ASN X 633 12 .670 10 .877 17. .919 0. .00 0. .00 PROB

ATOM 2907 HB2 ASN X 633 11 .898 10 .777 19. .606 0. .00 0. .00 PROB

ATOM 2908 CG ASN X 633 11 .781 8 .995 18. .477 0. .00 0. .00 PROB

ATOM 2909 OD1 ASN X 633 12 .231 8 .394 17. .500 0. .00 0. .00 PROB

ATOM 2910 ND2 ASN X 633 11 .211 8 .331 19. .447 0. .00 0. .00 PROB

ATOM 2911 HD21 ASN X 633 11 .015 7 .354 19. .364 0. .00 0. .00 PROB

ATOM 2912 HD22 ASN X 633 10 .874 8 .855 20. .229 0. .00 0. .00 PROB

ATOM 2913 C ASN X 633 10 .531 12 .541 18. .117 0. .00 0. .00 PROB

ATOM 2914 O ASN X 633 10 .747 12 .906 19. .264 0. .00 0. .00 PROB

ATOM 2915 N THR X 634 10 .510 13 .374 17. .096 0. .00 0. .00 PROB

ATOM 2916 HN THR X 634 10 .168 13 .011 16. .233 0. .00 0. .00 PROB

ATOM 2917 CA THR X 634 10 .804 14 .803 17. .198 0. .00 0. .00 PROB

ATOM 2918 HA THR X 634 10 .355 15 .120 18. .128 0. .00 0. .00 PROB

ATOM 2919 CB THR X 634 12 .243 15 .064 17. .258 0. .00 0. .00 PROB

ATOM 2920 HB THR X 634 12 .623 14 .664 18. .223 0. .00 0. .00 PROB

ATOM 2921 OG1 THR X 634 12 .490 16 .514 17. .303 0. .00 0. .00 PROB

ATOM 2922 HG1 THR X 634 13 .439 16 .639 17. .384 0. .00 0. .00 PROB

ATOM 2923 CG2 THR X 634 13 .033 14 .611 16. .031 0. .00 0. .00 PROB

ATOM 2924 HG21 THR X 634 13 .285 13 .532 15. .946 0. .00 0. .00 PROB

ATOM 2925 HG22 THR X 634 12 .542 14 .951 15. .094 0. .00 0. .00 PROB

ATOM 2926 HG23 THR X 634 13 .997 15 .164 16. .029 0. .00 0. .00 PROB

ATOM 2927 C THR X 634 10 .127 15 .486 16. .046 0. .00 0. .00 PROB

ATOM 2928 O THR X 634 9. .864 14 .889 14. .982 0. .00 0. .00 PROB

ATOM 2929 N ASN X 635 9. .706 16 .758 16. .228 0. .00 0. .00 PROB

ATOM 2930 HN ASN X 635 9. .801 17 .157 17. .137 0. .00 0. .00 PROB

ATOM 2931 CA ASN X 635 9. .038 17 .548 15. .183 0. .00 0. .00 PROB

ATOM 2932 HA ASN X 635 8. .067 17 .176 14. .894 0. .00 0. .00 PROB

ATOM 2933 CB ASN X 635 8. .839 18 .965 15. .767 0. .00 0. .00 PROB

ATOM 2934 HB1 ASN X 635 9 .704 19 .136 16. .444 0. .00 0. .00 PROB

ATOM 2935 HB2 ASN X 635 8 .860 19 .774 15. .006 0. .00 0. .00 PROB

ATOM 2936 CG ASN X 635 7. .522 19 .008 16. .574 0. .00 0. .00 PROB

ATOM 2937 OD1 ASN X 635 6 .698 18 .121 16. .500 0. .00 0. .00 PROB

ATOM 2938 ND2 ASN X 635 7 .372 20 .060 17. .387 0. .00 0. .00 PROB

ATOM 2939 HD21 ASN X 635 6 .528 20 .119 17. .919 0. .00 0. .00 PROB

ATOM 2940 HD22 ASN X 635 8 .092 20 .752 17. .438 0. .00 0. .00 PROB

ATOM 2941 C ASN X 635 9. .779 17 .717 13. .920 0. .00 0. .00 PROB

ATOM 2942 O ASN X 635 9. .180 17 .579 12. .880 0. .00 0. .00 PROB

ATOM 2943 N SER X 636 11 .113 17 .961 13. .948 0. .00 0. .00 PROB

ATOM 2944 HN SER X 636 11 .636 17 .927 14. .796 0. .00 0. .00 PROB

ATOM 2945 CA SER X 636 11 .843 18 .086 12. .690 0. .00 0. .00 PROB

ATOM 2946 HA SER X 636 11 .382 18 .816 12. .040 0. .00 0. .00 PROB

ATOM 2947 CB SER X 636 13 .250 18 .663 12. .835 0. .00 0. .00 PROB

ATOM 2948 HB1 SER X 636 13 .737 18 .709 11. .837 0. .00 0. .00 PROB

ATOM 2949 HB2 SER X 636 13 .190 19 .701 13. .227 0. .00 0. .00 PROB

ATOM 2950 OG SER X 636 13 .968 17 .950 13. .794 0. .00 0. .00 PROB

ATOM 2951 HG1 SER X 636 14 .846 18 .319 13. .917 0. .00 0. .00 PROB

ATOM 2952 C SER X 636 11 .923 16 .833 11. .830 0. .00 0. .00 PROB

ATOM 2953 O SER X 636 11 .708 16 .934 10. .673 0. .00 0. .00 PROB

ATOM 2954 N GLU X 637 12 .091 15 .655 12. .351 0. .00 0. .00 PROB

ATOM 2955 HN GLU X 637 12 .460 15 .857 13. .255 0. .00 0. .00 PROB

ATOM 2956 CA GLU X 637 11 .944 14 .308 11. .765 0. .00 0. .00 PROB

ATOM 2957 HA GLU X 637 12 .636 14 .136 10. .954 0. .00 0. .00 PROB

ATOM 2958 CB GLU X 637 12 .253 13 .257 12. .826 0. .00 0. .00 PROB

ATOM 2959 HB1 GLU X 637 13 .257 13 .455 13. .257 0. .00 0. .00 PROB

ATOM 2960 HB2 GLU X 637 11 .461 13 .438 13. .584 0. .00 0. .00 PROB

ATOM 2961 CG GLU X 637 12 .134 11 .823 12. .212 0. .00 0. .00 PROB

ATOM 2962 HG1 GLU X 637 11 .079 11 .634 11. .917 0. .00 0. .00 PROB

ATOM 2963 HG2 GLU X 637 12 .839 11 .569 11. .392 0. .00 0. .00 PROB

ATOM 2964 CD GLU X 637 12 .557 10 .780 13. .249 0. .00 0. .00 PROB

ATOM 2965 OE1 GLU X 637 12 .330 11 .099 14. .490 0. .00 0. .00 PROB

ATOM 2966 OE2 GLU X 637 12 .880 9 .545 12. .984 0. .00 0. .00 PROB

ATOM 2967 C GLU X 637 10 .535 14 .083 11. .175 0. .00 0. .00 PROB

ATOM 2968 O GLU X 637 10 .402 13 .688 10. .022 0. .00 0. .00 PROB

ATOM 2969 N LYS X 638 9. .472 14 .525 11. .893 0. .00 0. .00 PROB ATOM 2970 HN LYS X 638 9..692 14.802 12..826 0..00 0..00 PROB

ATOM 2971 CA LYS X 638 8. .050 14 .425 11. .587 0. .00 0. .00 PROB

ATOM 2972 HA LYS X 638 7. .851 13 .398 11. .318 0. .00 0. .00 PROB

ATOM 2973 CB LYS X 638 7. .249 14 .844 12. .863 0. .00 0. .00 PROB

ATOM 2974 HB1 LYS X 638 7 .849 14 .482 13. .725 0. .00 0. .00 PROB

ATOM 2975 HB2 LYS X 638 7 .161 15 .949 12. .796 0. .00 0. .00 PROB

ATOM 2976 CG LYS X 638 5. .916 14 .182 12. .923 0. .00 0. .00 PROB

ATOM 2977 HG1 LYS X 638 5 .340 14 .666 12. .106 0. .00 0. .00 PROB

ATOM 2978 HG2 LYS X 638 5 .859 13 .107 12. .649 0. .00 0. .00 PROB

ATOM 2979 CD LYS X 638 5. .139 14 .437 14. .229 0. .00 0. .00 PROB

ATOM 2980 HD1 LYS X 638 5 .301 15 .525 14. .383 0. .00 0. .00 PROB

ATOM 2981 HD2 LYS X 638 4 .070 14 .319 13. .951 0. .00 0. .00 PROB

ATOM 2982 CE LYS X 638 5. .622 13 .609 15. .477 0. .00 0. .00 PROB

ATOM 2983 HE1 LYS X 638 5 .643 12 .571 15. .082 0. .00 0. .00 PROB

ATOM 2984 HE2 LYS X 638 6 .620 13 .829 15. .913 0. .00 0. .00 PROB

ATOM 2985 NZ LYS X 638 4. .697 13 .664 16. .625 0. .00 0. .00 PROB

ATOM 2986 HZ1 LYS X 638 3 .878 13 .036 16. .497 0. .00 0. .00 PROB

ATOM 2987 HZ2 LYS X 638 5 .139 13 .250 17. .471 0. .00 0. .00 PROB

ATOM 2988 HZ3 LYS X 638 4 .446 14 .618 16. .955 0. .00 0. .00 PROB

ATOM 2989 C LYS X 638 7. .622 15 .247 10. .372 0. .00 0. .00 PROB

ATOM 2990 O LYS X 638 6. .872 14 .866 9. .514 0. .00 0. .00 PROB

ATOM 2991 N ILE X 639 8. .215 16 .467 10. .279 0. .00 0. .00 PROB

ATOM 2992 HN ILE X 639 8. .734 16 .666 11. .107 0. .00 0. .00 PROB

ATOM 2993 CA ILE X 639 8. .158 17 .350 9. .097 0. .00 0. .00 PROB

ATOM 2994 HA ILE X 639 7. .131 17 .269 8. .774 0. .00 0. .00 PROB

ATOM 2995 CB ILE X 639 8. .736 18 .678 9. .497 0. .00 0. .00 PROB

ATOM 2996 HB ILE X 639 9. .639 18 .650 10. .144 0. .00 0. .00 PROB

ATOM 2997 CG2 ILE X 639 8 .952 19 .575 8. .229 0. .00 0. .00 PROB

ATOM 2998 HG21 ILE X 639 9 .859 19 .263 7. .667 0. .00 0. .00 PROB

ATOM 2999 HG22 ILE X 639 8 .079 19 .748 7. .565 0. .00 0. .00 PROB

ATOM 3000 HG23 ILE X 639 9 .136 20 .637 8. .495 0. .00 0. .00 PROB

ATOM 3001 CGI ILE X 639 7 .619 19 .333 10. .355 0. .00 0. .00 PROB

ATOM 3002 HG11 ILE X 639 6 .747 19 .385 9. .669 0. .00 0. .00 PROB

ATOM 3003 HG12 ILE X 639 7 .324 18 .653 11. .182 0. .00 0. .00 PROB

ATOM 3004 CD ILE X 639 8. .057 20 .630 11. .053 0. .00 0. .00 PROB

ATOM 3005 HD1 ILE X 639 8 .941 20 .326 11. .653 0. .00 0. .00 PROB

ATOM 3006 HD2 ILE X 639 8 .294 21 .436 10. .326 0. .00 0. .00 PROB

ATOM 3007 HD3 ILE X 639 7 .277 21 .008 11. .748 0. .00 0. .00 PROB

ATOM 3008 C ILE X 639 8. .985 16 .688 7. .941 0. .00 0. .00 PROB

ATOM 3009 O ILE X 639 8. .374 16 .542 6. .886 0. .00 0. .00 PROB

ATOM 3010 N PHE X 640 10 .325 16 .407 8. .129 0. .00 0. .00 PROB

ATOM 3011 HN PHE X 640 10 .714 16 .424 9. .047 0. .00 0. .00 PROB

ATOM 3012 CA PHE X 640 11 .365 16 .061 7. .168 0. .00 0. .00 PROB

ATOM 3013 HA PHE X 640 11 .312 16 .732 6. .324 0. .00 0. .00 PROB

ATOM 3014 CB PHE X 640 12 .841 15 .921 7. .715 0. .00 0. .00 PROB

ATOM 3015 HB1 PHE X 640 12 .892 15 .230 8. .584 0. .00 0. .00 PROB

ATOM 3016 HB2 PHE X 640 13 .540 15 .534 6. .944 0. .00 0. .00 PROB

ATOM 3017 CG PHE X 640 13 .483 17 .200 8. .181 0. .00 0. .00 PROB

ATOM 3018 CD1 PHE X 640 14 .793 17 .055 8. .814 0. .00 0. .00 PROB

ATOM 3019 HD1 PHE X 640 15 .317 16 . Ill 8. .820 0. .00 0. .00 PROB

ATOM 3020 CE1 PHE X 640 15 .544 18 .156 9. .178 0. .00 0. .00 PROB

ATOM 3021 HE1 PHE X 640 16 .545 17 .979 9. .542 0. .00 0. .00 PROB

ATOM 3022 CZ PHE X 640 15 .050 19 .423 9. .031 0. .00 0. .00 PROB

ATOM 3023 HZ PHE X 640 15 .580 20 .270 9. .442 0. .00 0. .00 PROB

ATOM 3024 CD2 PHE X 640 12 .958 18 .496 8. .078 0. .00 0. .00 PROB

ATOM 3025 HD2 PHE X 640 11 .937 18 .622 7. .750 0. .00 0. .00 PROB

ATOM 3026 CE2 PHE X 640 13 .697 19 .585 8. .503 0. .00 0. .00 PROB

ATOM 3027 HE2 PHE X 640 13 .130 20 .504 8. .470 0. .00 0. .00 PROB

ATOM 3028 C PHE X 640 10 .995 14 .734 6. .469 0. .00 0. .00 PROB

ATOM 3029 O PHE X 640 11 .258 14 .556 5. .315 0. .00 0. .00 PROB

ATOM 3030 N SER X 641 10 .436 13 .743 7. .285 0. .00 0. .00 PROB

ATOM 3031 HN SER X 641 10 .286 13 .892 8. .259 0. .00 0. .00 PROB

ATOM 3032 CA SER X 641 10 .149 12 .401 6. .770 0. .00 0. .00 PROB

ATOM 3033 HA SER X 641 11 .030 12 .010 6. .282 0. .00 0. .00 PROB

ATOM 3034 CB SER X 641 9. .798 11 .370 7. .895 0. .00 0. .00 PROB

ATOM 3035 HB1 SER X 641 9 .372 10 .435 7. .472 0. .00 0. .00 PROB ATOM 3036 HB2 SER X 641 10.662 11.315 8..591 0..00 0..00 PROB

ATOM 3037 OG SER X 641 8. .749 11 .809 8. .736 0. .00 0. .00 PROB

ATOM 3038 HG1 SER X 641 9 .146 12 .524 9. .240 0. .00 0. .00 PROB

ATOM 3039 C SER X 641 8. .992 12 .396 5. .779 0. .00 0. .00 PROB

ATOM 3040 O SER X 641 8. .897 11 .409 4. .980 0. .00 0. .00 PROB

ATOM 3041 N ILE X 642 8. .057 13 .389 5. .694 0. .00 0. .00 PROB

ATOM 3042 HN ILE X 642 7. .973 14 .149 6. .334 0. .00 0. .00 PROB

ATOM 3043 CA ILE X 642 6. .999 13 .481 4. .683 0. .00 0. .00 PROB

ATOM 3044 HA ILE X 642 6. .355 12 .614 4. .694 0. .00 0. .00 PROB

ATOM 3045 CB ILE X 642 6. .046 14 .710 4. .867 0. .00 0. .00 PROB

ATOM 3046 HB ILE X 642 6. .562 15 .694 4. .836 0. .00 0. .00 PROB

ATOM 3047 CG2 ILE X 642 5 .016 14 .654 3. .775 0. .00 0. .00 PROB

ATOM 3048 HG21 ILE X 642 4 .103 15 .267 3. .935 0. .00 0. .00 PROB

ATOM 3049 HG22 ILE X 642 5 .463 15 .007 2. .821 0. .00 0. .00 PROB

ATOM 3050 HG23 ILE X 642 4 .691 13 .606 3. .604 0. .00 0. .00 PROB

ATOM 3051 CGI ILE X 642 5 .375 14 .621 6. .249 0. .00 0. .00 PROB

ATOM 3052 HG11 ILE X 642 4 .558 13 .883 6. .099 0. .00 0. .00 PROB

ATOM 3053 HG12 ILE X 642 6 .059 14 .241 7. .037 0. .00 0. .00 PROB

ATOM 3054 CD ILE X 642 4. .821 16 .011 6. .616 0. .00 0. .00 PROB

ATOM 3055 HD1 ILE X 642 4 .051 16 .326 5. .879 0. .00 0. .00 PROB

ATOM 3056 HD2 ILE X 642 4 .457 16 .105 7. .662 0. .00 0. .00 PROB

ATOM 3057 HD3 ILE X 642 5 .688 16 .704 6. .574 0. .00 0. .00 PROB

ATOM 3058 C ILE X 642 7. .613 13 .411 3. .226 0. .00 0. .00 PROB

ATOM 3059 O ILE X 642 7. .289 12 .499 2. .461 0. .00 0. .00 PROB

ATOM 3060 N CYS X 643 8. .611 14 .272 2. .874 0. .00 0. .00 PROB

ATOM 3061 HN CYS X 643 8. .885 15 .068 3. .408 0. .00 0. .00 PROB

ATOM 3062 CA CYS X 643 9. .329 14 .141 1. .588 0. .00 0. .00 PROB

ATOM 3063 HA CYS X 643 8. .584 14 .133 0. .806 0. .00 0. .00 PROB

ATOM 3064 CB CYS X 643 10 .327 15 .388 1. .407 0. .00 0. .00 PROB

ATOM 3065 HB1 CYS X 643 9 .756 16 .278 1. .746 0. .00 0. .00 PROB

ATOM 3066 HB2 CYS X 643 11 .264 15 .179 1. .965 0. .00 0. .00 PROB

ATOM 3067 C CYS X 643 10 .135 12 .890 1. .322 0. .00 0. .00 PROB

ATOM 3068 O CYS X 643 10 .268 12 .334 0. .216 0. .00 0. .00 PROB

ATOM 3069 N VAL X 644 10 .687 12 .364 2. .415 0. .00 0. .00 PROB

ATOM 3070 HN VAL X 644 10 .620 12 .835 3. .291 0. .00 0. .00 PROB

ATOM 3071 CA VAL X 644 11 .472 11 .132 2. .368 0. .00 0. .00 PROB

ATOM 3072 HA VAL X 644 12 .247 11 .173 1. .616 0. .00 0. .00 PROB

ATOM 3073 CB VAL X 644 12 .044 10 .906 3. .775 0. .00 0. .00 PROB

ATOM 3074 HB VAL X 644 11 .238 10 .920 4. .540 0. .00 0. .00 PROB

ATOM 3075 CGI VAL X 644 12 .811 9 .579 3. .851 0. .00 0. .00 PROB

ATOM 3076 HG11 VAL X 644 12 .135 8 .697 3. .842 0. .00 0. .00 PROB

ATOM 3077 HG12 VAL X 644 13 .559 9 .544 3. .030 0. .00 0. .00 PROB

ATOM 3078 HG13 VAL X 644 13 .435 9 .465 4. .764 0. .00 0. .00 PROB

ATOM 3079 CG2 VAL X 644 13 .054 12 .007 4. .079 0. .00 0. .00 PROB

ATOM 3080 HG21 VAL X 644 14 .026 11 .866 3. .560 0. .00 0. .00 PROB

ATOM 3081 HG22 VAL X 644 12 .665 12 .966 3. .675 0. .00 0. .00 PROB

ATOM 3082 HG23 VAL X 644 13 .110 11 .961 5. .187 0. .00 0. .00 PROB

ATOM 3083 C VAL X 644 10 .657 9 .949 1. .918 0. .00 0. .00 PROB

ATOM 3084 O VAL X 644 11 .030 9 .212 0. .984 0. .00 0. .00 PROB

ATOM 3085 N MET X 645 9. .477 9 .690 2. .532 0. .00 0. .00 PROB

ATOM 3086 HN MET X 645 9. .198 10 .260 3. .300 0. .00 0. .00 PROB

ATOM 3087 CA MET X 645 8. .529 8 .654 2. .144 0. .00 0. .00 PROB

ATOM 3088 HA MET X 645 8. .946 7 .657 2. .154 0. .00 0. .00 PROB

ATOM 3089 CB MET X 645 7. .343 8 .690 3. .174 0. .00 0. .00 PROB

ATOM 3090 HB1 MET X 645 6 .917 9 .706 3. .310 0. .00 0. .00 PROB

ATOM 3091 HB2 MET X 645 6 .447 8 .138 2. .818 0. .00 0. .00 PROB

ATOM 3092 CG MET X 645 7. .762 8 .023 4. .496 0. .00 0. .00 PROB

ATOM 3093 HG1 MET X 645 8 .306 7 .072 4. .314 0. .00 0. .00 PROB

ATOM 3094 HG2 MET X 645 8 .478 8 .701 5. .006 0. .00 0. .00 PROB

ATOM 3095 SD MET X 645 6. .386 7 .862 5. .616 0. .00 0. .00 PROB

ATOM 3096 C MET X 645 7. .948 8 .859 0. .828 0. .00 0. .00 PROB

ATOM 3097 O MET X 645 7. .682 7 .943 0. .101 0. .00 0. .00 PROB

ATOM 3098 N LEU X 646 7. .655 10 .131 0. .444 0. .00 0. .00 PROB

ATOM 3099 HN LEU X 646 7. .788 10 .829 1. .144 0. .00 0. .00 PROB

ATOM 3100 CA LEU X 646 7. .058 10 .357 -0. .887 0. .00 0. .00 PROB

ATOM 3101 HA LEU X 646 6. .128 9 .807 -0. .882 0. .00 0. .00 PROB ATOM 3102 CB LEU X 646 6..685 11.893 -0..993 0..00 0..00 PROB

ATOM 3103 HB1 LEU X 646 5 .930 12 .054 -0. .194 0. .00 0. .00 PROB

ATOM 3104 HB2 LEU X 646 7 .545 12 .556 -0. .755 0. .00 0. .00 PROB

ATOM 3105 CG LEU X 646 6. .048 12 .378 -2. .293 0. .00 0. .00 PROB

ATOM 3106 HG LEU X 646 6. .636 11 .892 -3. .099 0. .00 0. .00 PROB

ATOM 3107 CD1 LEU X 646 4 .619 12 .142 -2. .468 0. .00 0. .00 PROB

ATOM 3108 HD11 LEU X 646 4 .092 12 .575 -1. .591 0. .00 0. .00 PROB

ATOM 3109 HD12 LEU X 646 4 .331 12 .654 -3. .411 0. .00 0. .00 PROB

ATOM 3110 HD13 LEU X 646 4 .505 11 .040 -2. .548 0. .00 0. .00 PROB

ATOM 3111 CD2 LEU X 646 6 .518 13 .853 -2. .514 0. .00 0. .00 PROB

ATOM 3112 HD21 LEU X 646 6 .775 14 .357 -1. .558 0. .00 0. .00 PROB

ATOM 3113 HD22 LEU X 646 7 .435 13 .977 -3. .128 0. .00 0. .00 PROB

ATOM 3114 HD23 LEU X 646 5 .643 14 .408 -2. .916 0. .00 0. .00 PROB

ATOM 3115 C LEU X 646 7. .960 9 .967 -2. .098 0. .00 0. .00 PROB

ATOM 3116 O LEU X 646 7. .579 9 .259 -3. .006 0. .00 0. .00 PROB

ATOM 3117 N ILE X 647 9. .228 10 .539 -2. .089 0. .00 0. .00 PROB

ATOM 3118 HN ILE X 647 9. .606 11 .189 -1. .435 0. .00 0. .00 PROB

ATOM 3119 CA ILE X 647 10 .281 10 .129 -2. .982 0. .00 0. .00 PROB

ATOM 3120 HA ILE X 647 9. .882 10 .303 -3. .971 0. .00 0. .00 PROB

ATOM 3121 CB ILE X 647 11 .479 11 .129 -2. .800 0. .00 0. .00 PROB

ATOM 3122 HB ILE X 647 11 .982 10 .892 -1. .838 0. .00 0. .00 PROB

ATOM 3123 CG2 ILE X 647 12 .444 10 .835 -3. .942 0. .00 0. .00 PROB

ATOM 3124 HG21 ILE X 647 13 .042 11 .765 -4. .051 0. .00 0. .00 PROB

ATOM 3125 HG22 ILE X 647 13 .041 9 .942 -3. .659 0. .00 0. .00 PROB

ATOM 3126 HG23 ILE X 647 11 .876 10 .654 -4. .879 0. .00 0. .00 PROB

ATOM 3127 CGI ILE X 647 10 .909 12 .662 -2. .869 0. .00 0. .00 PROB

ATOM 3128 HG11 ILE X 647 10 .232 12 .810 -2. .000 0. .00 0. .00 PROB

ATOM 3129 HG12 ILE X 647 11 .717 13 .412 -2. .729 0. .00 0. .00 PROB

ATOM 3130 CD ILE X 647 10 .276 13 .066 -4. .174 0. .00 0. .00 PROB

ATOM 3131 HD1 ILE X 647 9 .440 12 .412 -4. .501 0. .00 0. .00 PROB

ATOM 3132 HD2 ILE X 647 9 .970 14 .134 -4. .147 0. .00 0. .00 PROB

ATOM 3133 HD3 ILE X 647 10 .966 12 .994 -5. .041 0. .00 0. .00 PROB

ATOM 3134 C ILE X 647 10 .728 8 .654 -2. .925 0. .00 0. .00 PROB

ATOM 3135 O ILE X 647 10 .777 7 .986 -3. .984 0. .00 0. .00 PROB

ATOM 3136 N GLY X 648 10 .884 8 .030 -1. .715 0. .00 0. .00 PROB

ATOM 3137 HN GLY X 648 10 .877 8 .575 -0. .880 0. .00 0. .00 PROB

ATOM 3138 CA GLY X 648 11 .025 6 .579 -1. .490 0. .00 0. .00 PROB

ATOM 3139 HA1 GLY X 648 10 .907 6 .367 -0. .438 0. .00 0. .00 PROB

ATOM 3140 HA2 GLY X 648 11 .989 6 .346 -1. .917 0. .00 0. .00 PROB

ATOM 3141 C GLY X 648 9. .943 5 .759 -2. .282 0. .00 0. .00 PROB

ATOM 3142 O GLY X 648 10 .182 4 .720 -2. .878 0. .00 0. .00 PROB

ATOM 3143 N SER X 649 8. .701 6 .198 -2. .118 0. .00 0. .00 PROB

ATOM 3144 HN SER X 649 8. .432 7 .043 -1. .662 0. .00 0. .00 PROB

ATOM 3145 CA SER X 649 7. .559 5 .438 -2. .693 0. .00 0. .00 PROB

ATOM 3146 HA SER X 649 7. .730 4 .398 -2. .458 0. .00 0. .00 PROB

ATOM 3147 CB SER X 649 6. .155 5 .903 -2. .243 0. .00 0. .00 PROB

ATOM 3148 HB1 SER X 649 6 .239 5 .963 -1. .136 0. .00 0. .00 PROB

ATOM 3149 HB2 SER X 649 5 .887 6 .904 -2. .642 0. .00 0. .00 PROB

ATOM 3150 OG SER X 649 5. .082 5 .020 -2. .554 0. .00 0. .00 PROB

ATOM 3151 HG1 SER X 649 5 .278 4 .180 -2. .132 0. .00 0. .00 PROB

ATOM 3152 C SER X 649 7. .534 5 .311 -4. .240 0. .00 0. .00 PROB

ATOM 3153 O SER X 649 7. .234 4 .292 -4. .888 0. .00 0. .00 PROB

ATOM 3154 N LEU X 650 7. .855 6 .402 -4. .982 0. .00 0. .00 PROB

ATOM 3155 HN LEU X 650 7. .998 7 .270 -4. .512 0. .00 0. .00 PROB

ATOM 3156 CA LEU X 650 7. .991 6 .461 -6. .444 0. .00 0. .00 PROB

ATOM 3157 HA LEU X 650 7. .123 6 .081 -6. .961 0. .00 0. .00 PROB

ATOM 3158 CB LEU X 650 8. .244 7 .908 -6. .948 0. .00 0. .00 PROB

ATOM 3159 HB1 LEU X 650 7 .234 8 .364 -6. .874 0. .00 0. .00 PROB

ATOM 3160 HB2 LEU X 650 8 .992 8 .483 -6. .360 0. .00 0. .00 PROB

ATOM 3161 CG LEU X 650 8. .587 8 .133 -8. .571 0. .00 0. .00 PROB

ATOM 3162 HG LEU X 650 9. .460 7 .529 -8. .900 0. .00 0. .00 PROB

ATOM 3163 CD1 LEU X 650 7 .447 7 .530 -9. .386 0. .00 0. .00 PROB

ATOM 3164 HD11 LEU X 650 6 .525 7 .918 -8. .904 0. .00 0. .00 PROB

ATOM 3165 HD12 LEU X 650 7 .469 7 .828 -10. .456 0. .00 0. .00 PROB

ATOM 3166 HD13 LEU X 650 7 .489 6 .420 -9. .370 0. .00 0. .00 PROB

ATOM 3167 CD2 LEU X 650 8 .740 9 .664 -8. .861 0. .00 0. .00 PROB ATOM 3168 HD21 LEU X 650 9.057 9.758 -9..922 0..00 0..00 PROB

ATOM 3169 HD22 LEU X 650 7 .815 10 .242 -8. .650 0. .00 0. .00 PROB

ATOM 3170 HD23 LEU X 650 9 .499 10 .106 -8. .181 0. .00 0. .00 PROB

ATOM 3171 C LEU X 650 9. .251 5 .539 -6. .862 0. .00 0. .00 PROB

ATOM 3172 O LEU X 650 9. .159 4 .787 -7. .885 0. .00 0. .00 PROB

ATOM 3173 N MET X 651 10 .390 5 .608 -6. .119 0. .00 0. .00 PROB

ATOM 3174 HN MET X 651 10 .421 6 .357 -5. .461 0. .00 0. .00 PROB

ATOM 3175 CA MET X 651 11 .547 4 .816 -6. .379 0. .00 0. .00 PROB

ATOM 3176 HA MET X 651 12 .039 5 .065 -7. .308 0. .00 0. .00 PROB

ATOM 3177 CB MET X 651 12 .701 5 .166 -5. .370 0. .00 0. .00 PROB

ATOM 3178 HB1 MET X 651 13 .120 6 .161 -5. .634 0. .00 0. .00 PROB

ATOM 3179 HB2 MET X 651 12 .355 5 .076 -4. .319 0. .00 0. .00 PROB

ATOM 3180 CG MET X 651 13 .956 4 .258 -5. .485 0. .00 0. .00 PROB

ATOM 3181 HG1 MET X 651 13 .872 3 .623 -6. .393 0. .00 0. .00 PROB

ATOM 3182 HG2 MET X 651 14 .847 4 .892 -5. .681 0. .00 0. .00 PROB

ATOM 3183 C MET X 651 11 .182 3 .307 -6. .316 0. .00 0. .00 PROB

ATOM 3184 O MET X 651 11 .506 2 .424 -7. .104 0. .00 0. .00 PROB

ATOM 3185 N TYR X 652 10 .465 2 .966 -5. .294 0. .00 0. .00 PROB

ATOM 3186 HN TYR X 652 10 .311 3 .711 -4. .649 0. .00 0. .00 PROB

ATOM 3187 CA TYR X 652 10 .002 1 .565 -5. .018 0. .00 0. .00 PROB

ATOM 3188 HA TYR X 652 10 .817 0 .890 -5. .232 0. .00 0. .00 PROB

ATOM 3189 CB TYR X 652 9. .551 1 .414 -3. .510 0. .00 0. .00 PROB

ATOM 3190 HB1 TYR X 652 10 .226 1 .874 -2. .757 0. .00 0. .00 PROB

ATOM 3191 HB2 TYR X 652 8 .484 1 .710 -3. .413 0. .00 0. .00 PROB

ATOM 3192 CG TYR X 652 9. .478 -0 .016 -3. .129 0. .00 0. .00 PROB

ATOM 3193 CD1 TYR X 652 8 .312 -0 .596 -2. .587 0. .00 0. .00 PROB

ATOM 3194 HD1 TYR X 652 7 .473 0 .042 -2. .352 0. .00 0. .00 PROB

ATOM 3195 CE1 TYR X 652 8 .387 -1 .911 -2. .106 0. .00 0. .00 PROB

ATOM 3196 HE1 TYR X 652 7 .418 -2 .287 -1. .813 0. .00 0. .00 PROB

ATOM 3197 CZ TYR X 652 9. .498 -2 .719 -2. .290 0. .00 0. .00 PROB

ATOM 3198 OH TYR X 652 9. .559 -4 .035 -1. .780 0. .00 0. .00 PROB

ATOM 3199 HH TYR X 652 8. .738 -4 .441 -2. .067 0. .00 0. .00 PROB

ATOM 3200 CD2 TYR X 652 10 .671 -0 .690 -3. .094 0. .00 0. .00 PROB

ATOM 3201 HD2 TYR X 652 11 .616 -0 .188 -3. .242 0. .00 0. .00 PROB

ATOM 3202 CE2 TYR X 652 10 .669 -2 .094 -2. .747 0. .00 0. .00 PROB

ATOM 3203 HE2 TYR X 652 11 .646 -2 .554 -2. .719 0. .00 0. .00 PROB

ATOM 3204 C TYR X 652 9. .028 1 .056 -6. .062 0. .00 0. .00 PROB

ATOM 3205 O TYR X 652 9. .255 0 .032 -6. .647 0. .00 0. .00 PROB

ATOM 3206 N ALA X 653 8. .097 1 .957 -6. .509 0. .00 0. .00 PROB

ATOM 3207 HN ALA X 653 7. .951 2 .805 -6. .005 0. .00 0. .00 PROB

ATOM 3208 CA ALA X 653 7. .120 1 .637 -7. .600 0. .00 0. .00 PROB

ATOM 3209 HA ALA X 653 6. .519 0 .792 -7. .301 0. .00 0. .00 PROB

ATOM 3210 CB ALA X 653 6. .150 2 .817 -7. .842 0. .00 0. .00 PROB

ATOM 3211 HB1 ALA X 653 5 .488 2 .505 -8. .677 0. .00 0. .00 PROB

ATOM 3212 HB2 ALA X 653 5 .434 2 .904 -6. .997 0. .00 0. .00 PROB

ATOM 3213 HB3 ALA X 653 6 .665 3 .794 -7. .967 0. .00 0. .00 PROB

ATOM 3214 C ALA X 653 7. .947 1 .352 -8. .936 0. .00 0. .00 PROB

ATOM 3215 O ALA X 653 7. .681 0 .402 -9. .626 0. .00 0. .00 PROB

ATOM 3216 N SER X 654 8. .931 2 .178 -9. .269 0. .00 0. .00 PROB

ATOM 3217 HN SER X 654 9. .142 2 .944 -8. .668 0. .00 0. .00 PROB

ATOM 3218 CA SER X 654 9. .798 2 .080 -10. .333 0. .00 0. .00 PROB

ATOM 3219 HA SER X 654 9. .145 2 .120 -11. .192 0. .00 0. .00 PROB

ATOM 3220 CB SER X 654 10 .754 3 .269 -10. .402 0. .00 0. .00 PROB

ATOM 3221 HB1 SER X 654 10 .133 4 .189 -10. .351 0. .00 0. .00 PROB

ATOM 3222 HB2 SER X 654 11 .345 3 .284 -9. .462 0. .00 0. .00 PROB

ATOM 3223 OG SER X 654 11 .600 3 .354 -11. .538 0. .00 0. .00 PROB

ATOM 3224 HG1 SER X 654 12 .463 3 .361 -11. .118 0. .00 0. .00 PROB

ATOM 3225 C SER X 654 10 .619 0 .751 -10. .496 0. .00 0. .00 PROB

ATOM 3226 O SER X 654 10 .473 0 .017 -11. .459 0. .00 0. .00 PROB

ATOM 3227 N ILE X 655 11 .347 0 .347 -9. .412 0. .00 0. .00 PROB

ATOM 3228 HN ILE X 655 11 .511 1 .041 -8. .715 0. .00 0. .00 PROB

ATOM 3229 CA ILE X 655 12 .027 -0 .894 -9. .266 0. .00 0. .00 PROB

ATOM 3230 HA ILE X 655 12 .498 -1 .097 -10. .217 0. .00 0. .00 PROB

ATOM 3231 CB ILE X 655 13 .178 -0 .814 -8. .244 0. .00 0. .00 PROB

ATOM 3232 HB ILE X 655 13 .804 -1 .728 -8. .319 0. .00 0. .00 PROB

ATOM 3233 CG2 ILE X 655 14 .038 0 .367 -8. .747 0. .00 0. .00 PROB ATOM 3234 HG21 ILE X 655 14.338 0.279 -9..813 0..00 0..00 PROB

ATOM 3235 HG22 ILE X 655 13 .590 1 .381 -8. .673 0. .00 0. .00 PROB

ATOM 3236 HG23 ILE X 655 14 .920 0 .521 -8. .088 0. .00 0. .00 PROB

ATOM 3237 CGI ILE X 655 12 .679 -0 .766 -6. .769 0. .00 0. .00 PROB

ATOM 3238 HG11 ILE X 655 11 .894 0 .004 -6. .610 0. .00 0. .00 PROB

ATOM 3239 HG12 ILE X 655 12 .233 -1 .776 -6. .648 0. .00 0. .00 PROB

ATOM 3240 CD ILE X 655 13 .778 -0 .710 -5. .797 0. .00 0. .00 PROB

ATOM 3241 HD1 ILE X 655 13 .588 -0 .888 -4. .717 0. .00 0. .00 PROB

ATOM 3242 HD2 ILE X 655 14 .560 -1 .447 -6. .083 0. .00 0. .00 PROB

ATOM 3243 HD3 ILE X 655 14 .258 0 .288 -5. .717 0. .00 0. .00 PROB

ATOM 3244 C ILE X 655 11 .108 -2 .144 -9. .155 0. .00 0. .00 PROB

ATOM 3245 O ILE X 655 11 .432 -3 .152 -9. .776 0. .00 0. .00 PROB

ATOM 3246 N PHE X 656 10 .005 -2 .099 -8. .441 0. .00 0. .00 PROB

ATOM 3247 HN PHE X 656 9. .914 -1 .218 -7. .983 0. .00 0. .00 PROB

ATOM 3248 CA PHE X 656 8. .958 -3 .038 -8. .367 0. .00 0. .00 PROB

ATOM 3249 HA PHE X 656 9. .442 -3 .941 -8. .027 0. .00 0. .00 PROB

ATOM 3250 CB PHE X 656 7. .895 -2 .628 -7. .305 0. .00 0. .00 PROB

ATOM 3251 HB1 PHE X 656 8 .323 -2 .694 -6. .281 0. .00 0. .00 PROB

ATOM 3252 HB2 PHE X 656 7 .797 -1 .531 -7. .450 0. .00 0. .00 PROB

ATOM 3253 CG PHE X 656 6. .621 -3 .407 -7. .356 0. .00 0. .00 PROB

ATOM 3254 CD1 PHE X 656 5 .404 -2 .711 -7. .380 0. .00 0. .00 PROB

ATOM 3255 HD1 PHE X 656 5 .440 -1 .633 -7. .326 0. .00 0. .00 PROB

ATOM 3256 CE1 PHE X 656 4 .161 -3 .390 -7. .408 0. .00 0. .00 PROB

ATOM 3257 HE1 PHE X 656 3 .220 -2 .868 -7. .497 0. .00 0. .00 PROB

ATOM 3258 CZ PHE X 656 4. .208 -4 .749 -7. .492 0. .00 0. .00 PROB

ATOM 3259 HZ PHE X 656 3. .251 -5 .250 -7. .493 0. .00 0. .00 PROB

ATOM 3260 CD2 PHE X 656 6 .618 -4 .820 -7. .366 0. .00 0. .00 PROB

ATOM 3261 HD2 PHE X 656 7 .495 -5 .438 -7. .241 0. .00 0. .00 PROB

ATOM 3262 CE2 PHE X 656 5 .388 -5 .519 -7. .297 0. .00 0. .00 PROB

ATOM 3263 HE2 PHE X 656 5 .369 -6 .597 -7. .222 0. .00 0. .00 PROB

ATOM 3264 C PHE X 656 8. .404 -3 .310 -9. .780 0. .00 0. .00 PROB

ATOM 3265 O PHE X 656 8. .006 -4 .414 -10. .129 0. .00 0. .00 PROB

ATOM 3266 N GLY X 657 8. .352 -2 .249 -10. .567 0. .00 0. .00 PROB

ATOM 3267 HN GLY X 657 8. .448 -1 .343 -10. .161 0. .00 0. .00 PROB

ATOM 3268 CA GLY X 657 7. .900 -2 .211 -12. .001 0. .00 0. .00 PROB

ATOM 3269 HA1 GLY X 657 7 .750 -1 .210 -12. .377 0. .00 0. .00 PROB

ATOM 3270 HA2 GLY X 657 6 .909 -2 .640 -12. .008 0. .00 0. .00 PROB

ATOM 3271 C GLY X 657 8. .698 -2 .953 -12. .921 0. .00 0. .00 PROB

ATOM 3272 O GLY X 657 8. .203 -3 .683 -13. .748 0. .00 0. .00 PROB

ATOM 3273 N ASN X 658 10 .005 -2 .917 -12. .664 0. .00 0. .00 PROB

ATOM 3274 HN ASN X 658 10 .381 -2 .394 -11. .903 0. .00 0. .00 PROB

ATOM 3275 CA ASN X 658 11 .012 -3 .605 -13. .479 0. .00 0. .00 PROB

ATOM 3276 HA ASN X 658 10 .723 -3 .517 -14. .515 0. .00 0. .00 PROB

ATOM 3277 CB ASN X 658 12 .450 -3 .130 -13. .150 0. .00 0. .00 PROB

ATOM 3278 HB1 ASN X 658 12 .429 -2 .095 -12. .746 0. .00 0. .00 PROB

ATOM 3279 HB2 ASN X 658 12 .779 -3 .761 -12. .297 0. .00 0. .00 PROB

ATOM 3280 CG ASN X 658 13 .424 -3 .315 -14. .297 0. .00 0. .00 PROB

ATOM 3281 OD1 ASN X 658 13 .967 -4 .429 -14. .383 0. .00 0. .00 PROB

ATOM 3282 ND2 ASN X 658 13 .687 -2 .291 -15. .141 0. .00 0. .00 PROB

ATOM 3283 HD21 ASN X 658 14 .463 -2 .224 -15. .769 0. .00 0. .00 PROB

ATOM 3284 HD22 ASN X 658 13 .256 -1 .400 -14. .996 0. .00 0. .00 PROB

ATOM 3285 C ASN X 658 11 .011 -5 .159 -13. .169 0. .00 0. .00 PROB

ATOM 3286 O ASN X 658 10 .975 -5 .992 -14. .079 0. .00 0. .00 PROB

ATOM 3287 N VAL X 659 10 .956 -5 .622 -11. .908 0. .00 0. .00 PROB

ATOM 3288 HN VAL X 659 11 .130 -5 .063 -11. .101 0. .00 0. .00 PROB

ATOM 3289 CA VAL X 659 10 .809 -7 .034 -11. .640 0. .00 0. .00 PROB

ATOM 3290 HA VAL X 659 11 .548 -7 .520 -12. .259 0. .00 0. .00 PROB

ATOM 3291 CB VAL X 659 11 .252 -7 .334 -10. .213 0. .00 0. .00 PROB

ATOM 3292 HB VAL X 659 11 .315 -8 .440 -10. .127 0. .00 0. .00 PROB

ATOM 3293 CGI VAL X 659 12 .718 -6 .760 -9. .994 0. .00 0. .00 PROB

ATOM 3294 HG11 VAL X 659 13 .284 -7 .104 -10. .886 0. .00 0. .00 PROB

ATOM 3295 HG12 VAL X 659 12 .825 -5 .654 -10. .001 0. .00 0. .00 PROB

ATOM 3296 HG13 VAL X 659 13 .160 -7 .193 -9. .071 0. .00 0. .00 PROB

ATOM 3297 CG2 VAL X 659 10 .409 -6 .685 -9. .109 0. .00 0. .00 PROB

ATOM 3298 HG21 VAL X 659 10 .515 -5 .585 -9. .216 0. .00 0. .00 PROB

ATOM 3299 HG22 VAL X 659 9 .327 -6 .921 -9. .192 0. .00 0. .00 PROB ATOM 3300 HG23 VAL X 659 10.695 -7.067 -8..106 0..00 0..00 PROB

ATOM 3301 C VAL X 659 9. .414 -7 .655 -11. .822 0. .00 0. .00 PROB

ATOM 3302 O VAL X 659 9. .262 -8 .904 -11. .879 0. .00 0. .00 PROB

ATOM 3303 N SER X 660 8. .387 -6 .831 -11. .783 0. .00 0. .00 PROB

ATOM 3304 HN SER X 660 8. .553 -5 .854 -11. .679 0. .00 0. .00 PROB

ATOM 3305 CA SER X 660 6. .971 -7 .303 -12. .183 0. .00 0. .00 PROB

ATOM 3306 HA SER X 660 6. .778 -8 .200 -11. .614 0. .00 0. .00 PROB

ATOM 3307 CB SER X 660 5. .827 -6 .311 -11. .960 0. .00 0. .00 PROB

ATOM 3308 HB1 SER X 660 6 .024 -5 .260 -12. .259 0. .00 0. .00 PROB

ATOM 3309 HB2 SER X 660 4 .871 -6 .608 -12. .441 0. .00 0. .00 PROB

ATOM 3310 OG SER X 660 5. .660 -6 .186 -10. .601 0. .00 0. .00 PROB

ATOM 3311 HG1 SER X 660 6 .425 -5 .768 -10. .199 0. .00 0. .00 PROB

ATOM 3312 C SER X 660 6. .970 -7 .762 -13. .634 0. .00 0. .00 PROB

ATOM 3313 O SER X 660 6. .292 -8 .717 -14. .019 0. .00 0. .00 PROB

ATOM 3314 N ALA X 661 7. .819 -7 .154 -14. .484 0. .00 0. .00 PROB

ATOM 3315 HN ALA X 661 8. .345 -6 .387 -14. .128 0. .00 0. .00 PROB

ATOM 3316 CA ALA X 661 7. .881 -7 .528 -15. .859 0. .00 0. .00 PROB

ATOM 3317 HA ALA X 661 6. .932 -7 .637 -16. .363 0. .00 0. .00 PROB

ATOM 3318 CB ALA X 661 8. .600 -6 .352 -16. .602 0. .00 0. .00 PROB

ATOM 3319 HB1 ALA X 661 8 .270 -5 .366 -16. .210 0. .00 0. .00 PROB

ATOM 3320 HB2 ALA X 661 9 .701 -6 .426 -16. .478 0. .00 0. .00 PROB

ATOM 3321 HB3 ALA X 661 8 .242 -6 .448 -17. .650 0. .00 0. .00 PROB

ATOM 3322 C ALA X 661 8. .588 -8 .910 -16. .164 0. .00 0. .00 PROB

ATOM 3323 O ALA X 661 7. .981 -9 .729 -16. .785 0. .00 0. .00 PROB

ATOM 3324 N ILE X 662 9. .790 -9 .142 -15. .545 0. .00 0. .00 PROB

ATOM 3325 HN ILE X 662 10 .342 -8 .391 -15. .191 0. .00 0. .00 PROB

ATOM 3326 CA ILE X 662 10 .579 -10 .390 -15. .582 0. .00 0. .00 PROB

ATOM 3327 HA ILE X 662 10 .774 -10 .589 -16. .626 0. .00 0. .00 PROB

ATOM 3328 CB ILE X 662 11 .966 -10 .361 -14. .865 0. .00 0. .00 PROB

ATOM 3329 HB ILE X 662 11 .713 -10 .125 -13. .809 0. .00 0. .00 PROB

ATOM 3330 CG2 ILE X 662 12 .831 -11 .685 -14. .945 0. .00 0. .00 PROB

ATOM 3331 HG21 ILE X 662 13 .852 -11 .646 -14. .508 0. .00 0. .00 PROB

ATOM 3332 HG22 ILE X 662 12 .253 -12 .521 -14. .496 0. .00 0. .00 PROB

ATOM 3333 HG23 ILE X 662 12 .957 -11 .892 -16. .029 0. .00 0. .00 PROB

ATOM 3334 CGI ILE X 662 12 .770 -9 .138 -15. .467 0. .00 0. .00 PROB

ATOM 3335 HG11 ILE X 662 13 .311 -9 .455 -16. .384 0. .00 0. .00 PROB

ATOM 3336 HG12 ILE X 662 12 .149 -8 .276 -15. .792 0. .00 0. .00 PROB

ATOM 3337 CD ILE X 662 13 .759 -8 .780 -14. .422 0. .00 0. .00 PROB

ATOM 3338 HD1 ILE X 662 13 .424 -8 .659 -13. .370 0. .00 0. .00 PROB

ATOM 3339 HD2 ILE X 662 14 .496 -9 .610 -14. .372 0. .00 0. .00 PROB

ATOM 3340 HD3 ILE X 662 14 .268 -7 .853 -14. .762 0. .00 0. .00 PROB

ATOM 3341 C ILE X 662 9. .704 -11 .590 -15. .019 0. .00 0. .00 PROB

ATOM 3342 O ILE X 662 9. .686 -12 .639 -15. .651 0. .00 0. .00 PROB

ATOM 3343 N ILE X 663 8. .951 -11 .399 -14. .007 0. .00 0. .00 PROB

ATOM 3344 HN ILE X 663 8. .869 -10 .455 -13. .697 0. .00 0. .00 PROB

ATOM 3345 CA ILE X 663 8. .139 -12 .438 -13. .456 0. .00 0. .00 PROB

ATOM 3346 HA ILE X 663 8. .799 -13 .265 -13. .236 0. .00 0. .00 PROB

ATOM 3347 CB ILE X 663 7. .583 -12 .197 -11. .984 0. .00 0. .00 PROB

ATOM 3348 HB ILE X 663 8. .466 -11 .761 -11. .470 0. .00 0. .00 PROB

ATOM 3349 CG2 ILE X 663 6 .345 -11 .200 -11. .928 0. .00 0. .00 PROB

ATOM 3350 HG21 ILE X 663 6 .008 -11 .276 -10. .872 0. .00 0. .00 PROB

ATOM 3351 HG22 ILE X 663 6 .477 -10 .132 -12. .204 0. .00 0. .00 PROB

ATOM 3352 HG23 ILE X 663 5 .573 -11 .662 -12. .580 0. .00 0. .00 PROB

ATOM 3353 CGI ILE X 663 7 .287 -13 .598 -11. .383 0. .00 0. .00 PROB

ATOM 3354 HG11 ILE X 663 6 .264 -13 .912 -11. .679 0. .00 0. .00 PROB

ATOM 3355 HG12 ILE X 663 8 .058 -14 .288 -11. .789 0. .00 0. .00 PROB

ATOM 3356 CD ILE X 663 7. .211 -13 .539 -9. .830 0. .00 0. .00 PROB

ATOM 3357 HD1 ILE X 663 6 .859 -14 .522 -9. .451 0. .00 0. .00 PROB

ATOM 3358 HD2 ILE X 663 8 .201 -13 .418 -9. .339 0. .00 0. .00 PROB

ATOM 3359 HD3 ILE X 663 6 .513 -12 .712 -9. .578 0. .00 0. .00 PROB

ATOM 3360 C ILE X 663 7. .052 -13 .048 -14. .362 0. .00 0. .00 PROB

ATOM 3361 O ILE X 663 6. .775 -14 .263 -14. .432 0. .00 0. .00 PROB

ATOM 3362 N GLN X 664 6. .435 -12 .214 -15. .201 0. .00 0. .00 PROB

ATOM 3363 HN GLN X 664 6. .695 -11 .254 -15. .263 0. .00 0. .00 PROB

ATOM 3364 CA GLN X 664 5. .384 -12 .585 -16. .073 0. .00 0. .00 PROB

ATOM 3365 HA GLN X 664 4. .799 -13 .430 -15. .741 0. .00 0. .00 PROB ATOM 3366 CB GLN X 664 4..338 -11.464 -16..330 0..00 0..00 PROB

ATOM 3367 HB1 GLN X 664 3 .607 -12 .021 -16. .954 0. .00 0. .00 PROB

ATOM 3368 HB2 GLN X 664 3 .939 -11 .292 -15. .307 0. .00 0. .00 PROB

ATOM 3369 CG GLN X 664 4. .878 -10 .156 -16. .960 0. .00 0. .00 PROB

ATOM 3370 HG1 GLN X 664 5 .486 -9 .504 -16. .297 0. .00 0. .00 PROB

ATOM 3371 HG2 GLN X 664 5 .623 -10 .319 -17. .767 0. .00 0. .00 PROB

ATOM 3372 CD GLN X 664 3. .660 -9 .474 -17. .611 0. .00 0. .00 PROB

ATOM 3373 OE1 GLN X 664 2 .874 -8 .714 -17. .056 0. .00 0. .00 PROB

ATOM 3374 NE2 GLN X 664 3 .472 -9 .840 -18. .898 0. .00 0. .00 PROB

ATOM 3375 HE21 GLN X 664 2 .727 -9 .423 -19. .418 0. .00 0. .00 PROB

ATOM 3376 HE22 GLN X 664 4 .216 -10 .262 -19. .416 0. .00 0. .00 PROB

ATOM 3377 C GLN X 664 5. .998 -12 .840 -17. .489 0. .00 0. .00 PROB

ATOM 3378 O GLN X 664 5. .310 -13 .012 -18. .491 0. .00 0. .00 PROB

ATOM 3379 N ARG X 665 7. .334 -12 .811 -17. .637 0. .00 0. .00 PROB

ATOM 3380 HN ARG X 665 7. .939 -12 .608 -16. .870 0. .00 0. .00 PROB

ATOM 3381 CA ARG X 665 7. .984 -13 .263 -18. .795 0. .00 0. .00 PROB

ATOM 3382 HA ARG X 665 7. .400 -13 .213 -19. .702 0. .00 0. .00 PROB

ATOM 3383 CB ARG X 665 9. .240 -12 .335 -18. .766 0. .00 0. .00 PROB

ATOM 3384 HB1 ARG X 665 8 .709 -11 .366 -18. .646 0. .00 0. .00 PROB

ATOM 3385 HB2 ARG X 665 9 .849 -12 .668 -17. .899 0. .00 0. .00 PROB

ATOM 3386 CG ARG X 665 10 .069 -12 .245 -20. .050 0. .00 0. .00 PROB

ATOM 3387 HG1 ARG X 665 10 .463 -13 .237 -20. .356 0. .00 0. .00 PROB

ATOM 3388 HG2 ARG X 665 9 .467 -11 .879 -20. .909 0. .00 0. .00 PROB

ATOM 3389 CD ARG X 665 11 .382 -11 .420 -19. .870 0. .00 0. .00 PROB

ATOM 3390 HD1 ARG X 665 11 .987 -11 .864 -19. .050 0. .00 0. .00 PROB

ATOM 3391 HD2 ARG X 665 11 .922 -11 .310 -20. .834 0. .00 0. .00 PROB

ATOM 3392 NE ARG X 665 11 .019 -10 .032 -19. .573 0. .00 0. .00 PROB

ATOM 3393 HE ARG X 665 10 .088 -9 .685 -19. .457 0. .00 0. .00 PROB

ATOM 3394 CZ ARG X 665 11 .904 -9 .125 -19. .153 0. .00 0. .00 PROB

ATOM 3395 NH1 ARG X 665 13 .227 -9 .330 -19. .184 0. .00 0. .00 PROB

ATOM 3396 HH11 ARG X 665 13 .743 -8 .545 -18. .842 0. .00 0. .00 PROB

ATOM 3397 HH12 ARG X 665 13 .643 -10 .184 -19. .497 0. .00 0. .00 PROB

ATOM 3398 NH2 ARG X 665 11 .432 -7 .934 -18. .866 0. .00 0. .00 PROB

ATOM 3399 HH21 ARG X 665 12 .075 -7 .169 -18. .892 0. .00 0. .00 PROB

ATOM 3400 HH22 ARG X 665 10 .551 -7 .621 -19. .220 0. .00 0. .00 PROB

ATOM 3401 C ARG X 665 8. .481 -14 .662 -18. .705 0. .00 0. .00 PROB

ATOM 3402 O ARG X 665 8. .838 -15 .166 -19. .773 0. .00 0. .00 PROB

ATOM 3403 N LEU X 666 8. .457 -15 .250 -17. .491 0. .00 0. .00 PROB

ATOM 3404 HN LEU X 666 8. .036 -14 .914 -16. .651 0. .00 0. .00 PROB

ATOM 3405 CA LEU X 666 8. .903 -16 .590 -17. .297 0. .00 0. .00 PROB

ATOM 3406 HA LEU X 666 9. .908 -16 .731 -17. .668 0. .00 0. .00 PROB

ATOM 3407 CB LEU X 666 9. .060 -16 .857 -15. .759 0. .00 0. .00 PROB

ATOM 3408 HB1 LEU X 666 8 .181 -16 .359 -15. .296 0. .00 0. .00 PROB

ATOM 3409 HB2 LEU X 666 9 .120 -17 .936 -15. .500 0. .00 0. .00 PROB

ATOM 3410 CG LEU X 666 10 .360 -16 .329 -15. .194 0. .00 0. .00 PROB

ATOM 3411 HG LEU X 666 10 .546 -15 .281 -15. .514 0. .00 0. .00 PROB

ATOM 3412 CD1 LEU X 666 10 .317 -16 .391 -13. .647 0. .00 0. .00 PROB

ATOM 3413 HD11 LEU X 666 10 .665 -17 .387 -13. .297 0. .00 0. .00 PROB

ATOM 3414 HD12 LEU X 666 11 .121 -15 .667 -13. .396 0. .00 0. .00 PROB

ATOM 3415 HD13 LEU X 666 9 .366 -16 .014 -13. .214 0. .00 0. .00 PROB

ATOM 3416 CD2 LEU X 666 11 .669 -17 .036 -15. .602 0. .00 0. .00 PROB

ATOM 3417 HD21 LEU X 666 11 .749 -17 .151 -16. .705 0. .00 0. .00 PROB

ATOM 3418 HD22 LEU X 666 12 .552 -16 .454 -15. .260 0. .00 0. .00 PROB

ATOM 3419 HD23 LEU X 666 11 .666 -18 .046 -15. .139 0. .00 0. .00 PROB

ATOM 3420 C LEU X 666 7. .929 -17 .640 -17. .859 0. .00 0. .00 PROB

ATOM 3421 OT1 LEU X 666 6 .682 -17 .606 -17. .569 0. .00 0. .00 PROB

ATOM 3422 OT2 LEU X 666 8 .455 -18 .441 -18. .625 0. .00 0. .00 PROB

ATOM 3423 N MET X 554 -6 .116 -17 .284 -4. .436 0. .00 0. .00 PROC

ATOM 3424 HT1 MET X 554 -5 .976 -18 .312 -4. .359 0. .00 0. .00 PROC

ATOM 3425 HT2 MET X 554 -5 .980 -16 .993 -5. .425 0. .00 0. .00 PROC

ATOM 3426 HT3 MET X 554 -7 .138 -17 .147 -4. .301 0. .00 0. .00 PROC

ATOM 3427 CA MET X 554 -5 .412 -16 .299 -3. .566 0. .00 0. .00 PROC

ATOM 3428 HA MET X 554 -4 .499 -16 .049 -4. .085 0. .00 0. .00 PROC

ATOM 3429 CB MET X 554 -6 .252 -15 .125 -3. .128 0. .00 0. .00 PROC

ATOM 3430 HB1 MET X 554 -6 .573 -14 .657 -4. .083 0. .00 0. .00 PROC

ATOM 3431 HB2 MET X 554 -7 .210 -15 .448 -2. .669 0. .00 0. .00 PROC ATOM 3432 CG MET X 554 -5.463 -14.114 -2..389 0..00 0..00 PROC

ATOM 3433 HG1 MET X 554 -5 .422 -14 .486 -1. .343 0. .00 0. .00 PROC

ATOM 3434 HG2 MET X 554 -4 .374 -14 .105 -2. .612 0. .00 0. .00 PROC

ATOM 3435 C MET X 554 -4 .890 -16 .944 -2. .362 0. .00 0. .00 PROC

ATOM 3436 O MET X 554 -3 .706 -17 .232 -2. .256 0. .00 0. .00 PROC

ATOM 3437 N CYS X 555 -5 .883 -17 .374 -1. .482 0. .00 0. .00 PROC

ATOM 3438 HN CYS X 555 -6 .824 -17 .419 -1. .808 0. .00 0. .00 PROC

ATOM 3439 CA CYS X 555 -5 .697 -17 .747 -0. .116 0. .00 0. .00 PROC

ATOM 3440 HA CYS X 555 -5 .158 -16 .929 0. .338 0. .00 0. .00 PROC

ATOM 3441 CB CYS X 555 -7 .149 -17 .931 0. .494 0. .00 0. .00 PROC

ATOM 3442 HB1 CYS X 555 -7 .726 -18 .751 0. .015 0. .00 0. .00 PROC

ATOM 3443 HB2 CYS X 555 -7 .027 -18 .307 1. .532 0. .00 0. .00 PROC

ATOM 3444 C CYS X 555 -4 .899 -19 .011 0. .066 0. .00 0. .00 PROC

ATOM 3445 O CYS X 555 -4 .080 -19 .038 0. .924 0. .00 0. .00 PROC

ATOM 3446 N THR X 556 -5 .114 -20 .082 -0. .777 0. .00 0. .00 PROC

ATOM 3447 HN THR X 556 -5 .725 -19 .950 -1. .554 0. .00 0. .00 PROC

ATOM 3448 CA THR X 556 -4 .528 -21 .452 -0. .596 0. .00 0. .00 PROC

ATOM 3449 HA THR X 556 -4 .549 -21 .622 0. .470 0. .00 0. .00 PROC

ATOM 3450 CB THR X 556 -5 .346 -22 .595 -1. .252 0. .00 0. .00 PROC

ATOM 3451 HB THR X 556 -4 .905 -23 .607 -1. .125 0. .00 0. .00 PROC

ATOM 3452 OG1 THR X 556 -5 .535 -22 .313 -2. .618 0. .00 0. .00 PROC

ATOM 3453 HG1 THR X 556 -5 .638 -23 .151 -3. .075 0. .00 0. .00 PROC

ATOM 3454 CG2 THR X 556 -6 .741 -22 .696 -0. .659 0. .00 0. .00 PROC

ATOM 3455 HG21 THR X 556 -7 .405 -23 .382 -1. .227 0. .00 0. .00 PROC

ATOM 3456 HG22 THR X 556 -6 .610 -23 .080 0. .375 0. .00 0. .00 PROC

ATOM 3457 HG23 THR X 556 -7 .175 -21 .674 -0. .692 0. .00 0. .00 PROC

ATOM 3458 C THR X 556 -3 .055 -21 .471 -1. .169 0. .00 0. .00 PROC

ATOM 3459 O THR X 556 -2 .296 -22 .298 -0. .755 0. .00 0. .00 PROC

ATOM 3460 N PHE X 557 -2 .726 -20 .586 -2. .093 0. .00 0. .00 PROC

ATOM 3461 HN PHE X 557 -3 .415 -19 .931 -2. .392 0. .00 0. .00 PROC

ATOM 3462 CA PHE X 557 -1 .360 -20 .384 -2. .533 0. .00 0. .00 PROC

ATOM 3463 HA PHE X 557 -0 .915 -21 .356 -2. .691 0. .00 0. .00 PROC

ATOM 3464 CB PHE X 557 -1 .327 -19 .566 -3. .903 0. .00 0. .00 PROC

ATOM 3465 HB1 PHE X 557 -2 .103 -20 .039 -4. .541 0. .00 0. .00 PROC

ATOM 3466 HB2 PHE X 557 -1 .654 -18 .512 -3. .767 0. .00 0. .00 PROC

ATOM 3467 CG PHE X 557 -0 .083 -19 .428 -4. .779 0. .00 0. .00 PROC

ATOM 3468 CD1 PHE X 557 0 .964 -18 .563 -4. .389 0. .00 0. .00 PROC

ATOM 3469 HD1 PHE X 557 0 .960 -17 .960 -3. .493 0. .00 0. .00 PROC

ATOM 3470 CE1 PHE X 557 2 .136 -18 .465 -5. .220 0. .00 0. .00 PROC

ATOM 3471 HE1 PHE X 557 2 .921 -17 .755 -5. .008 0. .00 0. .00 PROC

ATOM 3472 CZ PHE X 557 2. .265 -19 .283 -6. .365 0. .00 0. .00 PROC

ATOM 3473 HZ PHE X 557 3. .170 -19 .225 -6. .952 0. .00 0. .00 PROC

ATOM 3474 CD2 PHE X 557 0 .002 -20 .148 -5. .959 0. .00 0. .00 PROC

ATOM 3475 HD2 PHE X 557 -0 .915 -20 .623 -6. .275 0. .00 0. .00 PROC

ATOM 3476 CE2 PHE X 557 1 .220 -20 .071 -6. .685 0. .00 0. .00 PROC

ATOM 3477 HE2 PHE X 557 1 .307 -20 .600 -7. .622 0. .00 0. .00 PROC

ATOM 3478 C PHE X 557 -0 .539 -19 .671 -1. .506 0. .00 0. .00 PROC

ATOM 3479 O PHE X 557 0. .640 -19 .981 -1. .357 0. .00 0. .00 PROC

ATOM 3480 N ALA X 558 -1 .032 -18 .647 -0. .878 0. .00 0. .00 PROC

ATOM 3481 HN ALA X 558 -1 .961 -18 .337 -1. .068 0. .00 0. .00 PROC

ATOM 3482 CA ALA X 558 -0 .257 -17 .830 -0. .038 0. .00 0. .00 PROC

ATOM 3483 HA ALA X 558 0. .701 -17 .513 -0. .421 0. .00 0. .00 PROC

ATOM 3484 CB ALA X 558 -1 .073 -16 .569 0. .333 0. .00 0. .00 PROC

ATOM 3485 HB1 ALA X 558 -1 .723 -16 .789 1. .208 0. .00 0. .00 PROC

ATOM 3486 HB2 ALA X 558 -0 .403 -15 .761 0. .697 0. .00 0. .00 PROC

ATOM 3487 HB3 ALA X 558 -1 .671 -16 .267 -0. .553 0. .00 0. .00 PROC

ATOM 3488 C ALA X 558 0. .103 -18 .447 1. .343 0. .00 0. .00 PROC

ATOM 3489 O ALA X 558 1. .104 -18 .120 1. .870 0. .00 0. .00 PROC

ATOM 3490 N LEU X 559 -0 .768 -19 .350 1. .859 0. .00 0. .00 PROC

ATOM 3491 HN LEU X 559 -1 .561 -19 .500 1. .274 0. .00 0. .00 PROC

ATOM 3492 CA LEU X 559 -0 .844 -20 .123 3. .097 0. .00 0. .00 PROC

ATOM 3493 HA LEU X 559 -0 .639 -19 .375 3. .848 0. .00 0. .00 PROC

ATOM 3494 CB LEU X 559 -2 .189 -20 .855 3. .142 0. .00 0. .00 PROC

ATOM 3495 HB1 LEU X 559 -3 .002 -20 .143 2. .885 0. .00 0. .00 PROC

ATOM 3496 HB2 LEU X 559 -2 .182 -21 .716 2. .441 0. .00 0. .00 PROC

ATOM 3497 CG LEU X 559 -2 .515 -21 .287 4. .639 0. .00 0. .00 PROC ATOM 3498 HG LEU X 559 -1.554 -21.722 4..987 0..00 0..00 PROC

ATOM 3499 CD1 LEU X 559 -2 .743 -20 .137 5. .612 0. .00 0. .00 PROC

ATOM 3500 HD11 LEU X 559 -3 .583 -19 .427 5. .453 0. .00 0. .00 PROC

ATOM 3501 HD12 LEU X 559 -2 .879 -20 .565 6. .628 0. .00 0. .00 PROC

ATOM 3502 HD13 LEU X 559 -1 .777 -19 .595 5. .698 0. .00 0. .00 PROC

ATOM 3503 CD2 LEU X 559 -3 .625 -22 .277 4. .595 0. .00 0. .00 PROC

ATOM 3504 HD21 LEU X 559 -4 .596 -21 .889 4. .219 0. .00 0. .00 PROC

ATOM 3505 HD22 LEU X 559 -3 .293 -23 .181 4. .042 0. .00 0. .00 PROC

ATOM 3506 HD23 LEU X 559 -3 .876 -22 .685 5. .598 0. .00 0. .00 PROC

ATOM 3507 C LEU X 559 0. .363 -21 .018 3. .141 0. .00 0. .00 PROC

ATOM 3508 O LEU X 559 0. .955 -21 .130 4. .201 0. .00 0. .00 PROC

ATOM 3509 N ILE X 560 0. .791 -21 .579 1. .986 0. .00 0. .00 PROC

ATOM 3510 HN ILE X 560 0. .291 -21 .628 1. .125 0. .00 0. .00 PROC

ATOM 3511 CA ILE X 560 2. .115 -22 .300 1. .917 0. .00 0. .00 PROC

ATOM 3512 HA ILE X 560 2. .118 -22 .961 2. .771 0. .00 0. .00 PROC

ATOM 3513 CB ILE X 560 2. .189 -23 .008 0. .518 0. .00 0. .00 PROC

ATOM 3514 HB ILE X 560 2. .145 -22 .274 -0. .316 0. .00 0. .00 PROC

ATOM 3515 CG2 ILE X 560 3 .492 -23 .859 0. .521 0. .00 0. .00 PROC

ATOM 3516 HG21 ILE X 560 3 .777 -24 .347 1. .477 0. .00 0. .00 PROC

ATOM 3517 HG22 ILE X 560 3 .433 -24 .592 -0. .312 0. .00 0. .00 PROC

ATOM 3518 HG23 ILE X 560 4 .356 -23 .249 0. .180 0. .00 0. .00 PROC

ATOM 3519 CGI ILE X 560 0 .962 -23 .987 0. .318 0. .00 0. .00 PROC

ATOM 3520 HG11 ILE X 560 1 .034 -24 .853 1. .010 0. .00 0. .00 PROC

ATOM 3521 HG12 ILE X 560 0 .019 -23 .477 0. .610 0. .00 0. .00 PROC

ATOM 3522 CD ILE X 560 0. .746 -24 .396 -1. .148 0. .00 0. .00 PROC

ATOM 3523 HD1 ILE X 560 0 .600 -23 .562 -1. .867 0. .00 0. .00 PROC

ATOM 3524 HD2 ILE X 560 1 .595 -25 .030 -1. .483 0. .00 0. .00 PROC

ATOM 3525 HD3 ILE X 560 -0 .219 -24 .946 -1. .135 0. .00 0. .00 PROC

ATOM 3526 C ILE X 560 3. .333 -21 .335 2. . Ill 0. .00 0. .00 PROC

ATOM 3527 O ILE X 560 4. .274 -21 .592 2. .906 0. .00 0. .00 PROC

ATOM 3528 N ALA X 561 3. .338 -20 .160 1. .429 0. .00 0. .00 PROC

ATOM 3529 HN ALA X 561 2. .584 -19 .834 0. .864 0. .00 0. .00 PROC

ATOM 3530 CA ALA X 561 4. .385 -19 .197 1. .703 0. .00 0. .00 PROC

ATOM 3531 HA ALA X 561 5. .324 -19 .695 1. .512 0. .00 0. .00 PROC

ATOM 3532 CB ALA X 561 4. .145 -17 .990 0. .851 0. .00 0. .00 PROC

ATOM 3533 HB1 ALA X 561 3 .873 -18 .322 -0. .174 0. .00 0. .00 PROC

ATOM 3534 HB2 ALA X 561 3 .318 -17 .386 1. .280 0. .00 0. .00 PROC

ATOM 3535 HB3 ALA X 561 5 .060 -17 .360 0. .851 0. .00 0. .00 PROC

ATOM 3536 C ALA X 561 4. .469 -18 .708 3. .146 0. .00 0. .00 PROC

ATOM 3537 O ALA X 561 5. .599 -18 .589 3. .606 0. .00 0. .00 PROC

ATOM 3538 N HSD X 562 3. .288 -18 .553 3. .805 0. .00 0. .00 PROC

ATOM 3539 HN HSD X 562 2. .481 -18 .598 3. .221 0. .00 0. .00 PROC

ATOM 3540 CA HSD X 562 3. .252 -18 .248 5. .233 0. .00 0. .00 PROC

ATOM 3541 HA HSD X 562 3. .655 -17 .288 5. .520 0. .00 0. .00 PROC

ATOM 3542 CB HSD X 562 1. .761 -18 .052 5. .758 0. .00 0. .00 PROC

ATOM 3543 HB1 HSD X 562 1 .097 -18 .867 5. .398 0. .00 0. .00 PROC

ATOM 3544 HB2 HSD X 562 1 .879 -18 .049 6. .863 0. .00 0. .00 PROC

ATOM 3545 ND1 HSD X 562 0 .268 -16 .203 6. .451 0. .00 0. .00 PROC

ATOM 3546 HD1 HSD X 562 -0 .082 -16 .657 7. .270 0. .00 0. .00 PROC

ATOM 3547 CG HSD X 562 1. .151 -16 .718 5. .494 0. .00 0. .00 PROC

ATOM 3548 CE1 HSD X 562 -0 .026 -14 .943 6. .014 0. .00 0. .00 PROC

ATOM 3549 HE1 HSD X 562 -0 .832 -14 .384 6. .489 0. .00 0. .00 PROC

ATOM 3550 NE2 HSD X 562 0 .595 -14 .576 4. .910 0. .00 0. .00 PROC

ATOM 3551 CD2 HSD X 562 1 .301 -15 .727 4. .552 0. .00 0. .00 PROC

ATOM 3552 HD2 HSD X 562 2 .021 -15 .578 3. .757 0. .00 0. .00 PROC

ATOM 3553 C HSD X 562 3. .946 -19 .261 6. .051 0. .00 0. .00 PROC

ATOM 3554 O HSD X 562 4. .726 -18 .807 6. .922 0. .00 0. .00 PROC

ATOM 3555 N TRP X 563 3. .771 -20 .568 5. .858 0. .00 0. .00 PROC

ATOM 3556 HN TRP X 563 3. .418 -20 .958 5. .011 0. .00 0. .00 PROC

ATOM 3557 CA TRP X 563 4. .364 -21 .633 6. .657 0. .00 0. .00 PROC

ATOM 3558 HA TRP X 563 4. .113 -21 .521 7. .702 0. .00 0. .00 PROC

ATOM 3559 CB TRP X 563 3. .859 -23 .029 6. .255 0. .00 0. .00 PROC

ATOM 3560 HB1 TRP X 563 4 .014 -23 .307 5. .191 0. .00 0. .00 PROC

ATOM 3561 HB2 TRP X 563 4 .373 -23 .888 6. .737 0. .00 0. .00 PROC

ATOM 3562 CG TRP X 563 2. .364 -23 .207 6. .511 0. .00 0. .00 PROC

ATOM 3563 CD1 TRP X 563 1 .633 -22 .713 7. .603 0. .00 0. .00 PROC ATOM 3564 HD1 TRP X 563 1.962 -21.905 8..240 0..00 0..00 PROC

ATOM 3565 NE1 TRP X 563 0 .383 -23 .300 7. .643 0. .00 0. .00 PROC

ATOM 3566 HE1 TRP X 563 -0 .187 -23 .383 8. .431 0. .00 0. .00 PROC

ATOM 3567 CE2 TRP X 563 0 .209 -24 .010 6. .525 0. .00 0. .00 PROC

ATOM 3568 CD2 TRP X 563 1 .389 -24 .043 5. .788 0. .00 0. .00 PROC

ATOM 3569 CE3 TRP X 563 1 .449 -24 .619 4. .560 0. .00 0. .00 PROC

ATOM 3570 HE3 TRP X 563 2 .441 -24 .723 4. .146 0. .00 0. .00 PROC

ATOM 3571 CZ3 TRP X 563 0 .363 -25 .367 4. .070 0. .00 0. .00 PROC

ATOM 3572 HZ3 TRP X 563 0 .415 -25 .759 3. .065 0. .00 0. .00 PROC

ATOM 3573 CZ2 TRP X 563 -0 .927 -24 .760 6. .095 0. .00 0. .00 PROC

ATOM 3574 HZ2 TRP X 563 -1 .799 -24 .822 6. .728 0. .00 0. .00 PROC

ATOM 3575 CH2 TRP X 563 -0 .829 -25 .392 4. .820 0. .00 0. .00 PROC

ATOM 3576 HH2 TRP X 563 -1 .566 -26 .126 4. .530 0. .00 0. .00 PROC

ATOM 3577 C TRP X 563 5. .908 -21 .614 6. .515 0. .00 0. .00 PROC

ATOM 3578 O TRP X 563 6. .678 -21 .824 7. .468 0. .00 0. .00 PROC

ATOM 3579 N LEU X 564 6. .362 -21 .243 5. .299 0. .00 0. .00 PROC

ATOM 3580 HN LEU X 564 5. .781 -21 .199 4. .489 0. .00 0. .00 PROC

ATOM 3581 CA LEU X 564 7. .750 -20 .910 4. .961 0. .00 0. .00 PROC

ATOM 3582 HA LEU X 564 8. .291 -21 .823 5. .160 0. .00 0. .00 PROC

ATOM 3583 CB LEU X 564 7. .976 -20 .641 3. .412 0. .00 0. .00 PROC

ATOM 3584 HB1 LEU X 564 7 .456 -21 .466 2. .880 0. .00 0. .00 PROC

ATOM 3585 HB2 LEU X 564 7 .462 -19 .728 3. .042 0. .00 0. .00 PROC

ATOM 3586 CG LEU X 564 9. .425 -20 .596 3. .017 0. .00 0. .00 PROC

ATOM 3587 HG LEU X 564 9. .945 -19 .811 3. .606 0. .00 0. .00 PROC

ATOM 3588 CD1 LEU X 564 10 .100 -21 .954 3. .394 0. .00 0. .00 PROC

ATOM 3589 HD11 LEU X 564 11 .134 -22 .043 2. .998 0. .00 0. .00 PROC

ATOM 3590 HD12 LEU X 564 10 .232 -22 .068 4. .491 0. .00 0. .00 PROC

ATOM 3591 HD13 LEU X 564 9 .491 -22 .800 3. .010 0. .00 0. .00 PROC

ATOM 3592 CD2 LEU X 564 9 .719 -20 .243 1. .557 0. .00 0. .00 PROC

ATOM 3593 HD21 LEU X 564 9 .415 -21 .169 1. .023 0. .00 0. .00 PROC

ATOM 3594 HD22 LEU X 564 9 .014 -19 .419 1. .319 0. .00 0. .00 PROC

ATOM 3595 HD23 LEU X 564 10 .782 -20 .038 1. .305 0. .00 0. .00 PROC

ATOM 3596 C LEU X 564 8. .383 -19 .737 5. .699 0. .00 0. .00 PROC

ATOM 3597 O LEU X 564 9. .500 -19 .759 6. .204 0. .00 0. .00 PROC

ATOM 3598 N ALA X 565 7. .636 -18 .687 5. .825 0. .00 0. .00 PROC

ATOM 3599 HN ALA X 565 6. .790 -18 .623 5. .302 0. .00 0. .00 PROC

ATOM 3600 CA ALA X 565 7. .843 -17 .526 6. .656 0. .00 0. .00 PROC

ATOM 3601 HA ALA X 565 8. .871 -17 .270 6. .450 0. .00 0. .00 PROC

ATOM 3602 CB ALA X 565 6. .900 -16 .385 6. .243 0. .00 0. .00 PROC

ATOM 3603 HB1 ALA X 565 7 .294 -15 .491 6. .772 0. .00 0. .00 PROC

ATOM 3604 HB2 ALA X 565 6 .907 -16 .215 5. .145 0. .00 0. .00 PROC

ATOM 3605 HB3 ALA X 565 5 .806 -16 .421 6. .433 0. .00 0. .00 PROC

ATOM 3606 C ALA X 565 7. .820 -17 .733 8. .180 0. .00 0. .00 PROC

ATOM 3607 O ALA X 565 8. .648 -17 .210 8. .954 0. .00 0. .00 PROC

ATOM 3608 N CYS X 566 6. .875 -18 .554 8. .679 0. .00 0. .00 PROC

ATOM 3609 HN CYS X 566 6. .279 -18 .876 7. .947 0. .00 0. .00 PROC

ATOM 3610 CA CYS X 566 6. .598 -18 .922 10. .054 0. .00 0. .00 PROC

ATOM 3611 HA CYS X 566 6. .478 -18 .068 10. .703 0. .00 0. .00 PROC

ATOM 3612 CB CYS X 566 5. .360 -19 .809 10. .130 0. .00 0. .00 PROC

ATOM 3613 HB1 CYS X 566 5 .488 -20 .759 9. .569 0. .00 0. .00 PROC

ATOM 3614 HB2 CYS X 566 5 .253 -20 .183 11. .171 0. .00 0. .00 PROC

ATOM 3615 C CYS X 566 7. .776 -19 .604 10. .730 0. .00 0. .00 PROC

ATOM 3616 O CYS X 566 8. .175 -19 .191 11. .863 0. .00 0. .00 PROC

ATOM 3617 N ILE X 567 8. .463 -20 .608 10. .115 0. .00 0. .00 PROC

ATOM 3618 HN ILE X 567 8. .120 -21 .005 9. .268 0. .00 0. .00 PROC

ATOM 3619 CA ILE X 567 9. .698 -21 .175 10. .745 0. .00 0. .00 PROC

ATOM 3620 HA ILE X 567 9. .364 -21 .544 11. .704 0. .00 0. .00 PROC

ATOM 3621 CB ILE X 567 10 .171 -22 .546 10. .078 0. .00 0. .00 PROC

ATOM 3622 HB ILE X 567 9. .214 -23 .108 10. .018 0. .00 0. .00 PROC

ATOM 3623 CG2 ILE X 567 10 .605 -22 .333 8. .561 0. .00 0. .00 PROC

ATOM 3624 HG21 ILE X 567 11 .086 -23 .285 8. .249 0. .00 0. .00 PROC

ATOM 3625 HG22 ILE X 567 9 .797 -21 .951 7. .900 0. .00 0. .00 PROC

ATOM 3626 HG23 ILE X 567 11 .398 -21 .557 8. .616 0. .00 0. .00 PROC

ATOM 3627 CGI ILE X 567 11 .132 -23 .470 10. .830 0. .00 0. .00 PROC

ATOM 3628 HG11 ILE X 567 11 .144 -24 .409 10. .237 0. .00 0. .00 PROC

ATOM 3629 HG12 ILE X 567 12 .130 -22 .985 10. .764 0. .00 0. .00 PROC ATOM 3630 CD ILE X 567 10.606 -23.753 12..267 0..00 0..00 PROC

ATOM 3631 HD1 ILE X 567 9 .507 -23 .894 12. .346 0. .00 0. .00 PROC

ATOM 3632 HD2 ILE X 567 11 .137 -24 .647 12. .658 0. .00 0. .00 PROC

ATOM 3633 HD3 ILE X 567 10 .991 -22 .967 12. .952 0. .00 0. .00 PROC

ATOM 3634 C ILE X 567 10 .868 -20 .245 11. .029 0. .00 0. .00 PROC

ATOM 3635 O ILE X 567 11 .427 -20 .176 12. .099 0. .00 0. .00 PROC

ATOM 3636 N TRP X 568 11 .114 -19 .405 10. .017 0. .00 0. .00 PROC

ATOM 3637 HN TRP X 568 10 .551 -19 .376 9. .195 0. .00 0. .00 PROC

ATOM 3638 CA TRP X 568 12 .179 -18 .440 9. .917 0. .00 0. .00 PROC

ATOM 3639 HA TRP X 568 13 .079 -18 .949 10. .227 0. .00 0. .00 PROC

ATOM 3640 CB TRP X 568 12 .153 -17 .725 8. .586 0. .00 0. .00 PROC

ATOM 3641 HB1 TRP X 568 12 .201 -18 .453 7. .748 0. .00 0. .00 PROC

ATOM 3642 HB2 TRP X 568 11 .214 -17 .141 8. .472 0. .00 0. .00 PROC

ATOM 3643 CG TRP X 568 13 .393 -17 .037 8. .124 0. .00 0. .00 PROC

ATOM 3644 CD1 TRP X 568 14 .449 -16 .411 8. .732 0. .00 0. .00 PROC

ATOM 3645 HD1 TRP X 568 14 .703 -16 .348 9. .780 0. .00 0. .00 PROC

ATOM 3646 NE1 TRP X 568 15 .147 -15 .642 7. .869 0. .00 0. .00 PROC

ATOM 3647 HE1 TRP X 568 15 .662 -14 .846 8. .101 0. .00 0. .00 PROC

ATOM 3648 CE2 TRP X 568 14 .474 -15 .773 6. .600 0. .00 0. .00 PROC

ATOM 3649 CD2 TRP X 568 13 .409 -16 .552 6. .787 0. .00 0. .00 PROC

ATOM 3650 CE3 TRP X 568 12 .563 -16 .793 5. .659 0. .00 0. .00 PROC

ATOM 3651 HE3 TRP X 568 11 .616 -17 .296 5. .790 0. .00 0. .00 PROC

ATOM 3652 CZ3 TRP X 568 12 .922 -16 .243 4. .443 0. .00 0. .00 PROC

ATOM 3653 HZ3 TRP X 568 12 .351 -16 .582 3. .591 0. .00 0. .00 PROC

ATOM 3654 CZ2 TRP X 568 14 .797 -15 .154 5. .409 0. .00 0. .00 PROC

ATOM 3655 HZ2 TRP X 568 15 .705 -14 .572 5. .363 0. .00 0. .00 PROC

ATOM 3656 CH2 TRP X 568 14 .041 -15 .470 4. .253 0. .00 0. .00 PROC

ATOM 3657 HH2 TRP X 568 14 .257 -14 .935 3. .340 0. .00 0. .00 PROC

ATOM 3658 C TRP X 568 12 . Ill -17 .360 11. .007 0. .00 0. .00 PROC

ATOM 3659 O TRP X 568 13 .059 -16 .887 11. .621 0. .00 0. .00 PROC

ATOM 3660 N TYR X 569 10 .922 -16 .842 11. .238 0. .00 0. .00 PROC

ATOM 3661 HN TYR X 569 10 .166 -17 .131 10. .657 0. .00 0. .00 PROC

ATOM 3662 CA TYR X 569 10 .515 -15 .929 12. .300 0. .00 0. .00 PROC

ATOM 3663 HA TYR X 569 11 .205 -15 .098 12. .309 0. .00 0. .00 PROC

ATOM 3664 CB TYR X 569 9. .033 -15 .459 12. .107 0. .00 0. .00 PROC

ATOM 3665 HB1 TYR X 569 8 .268 -16 .261 12. .037 0. .00 0. .00 PROC

ATOM 3666 HB2 TYR X 569 8 .749 -14 .883 13. .014 0. .00 0. .00 PROC

ATOM 3667 CG TYR X 569 8. .819 -14 .498 11. .014 0. .00 0. .00 PROC

ATOM 3668 CD1 TYR X 569 7 .613 -14 .464 10. .311 0. .00 0. .00 PROC

ATOM 3669 HD1 TYR X 569 6 .970 -15 .323 10. .435 0. .00 0. .00 PROC

ATOM 3670 CE1 TYR X 569 7 .277 -13 .489 9. .433 0. .00 0. .00 PROC

ATOM 3671 HE1 TYR X 569 6 .330 -13 .387 8. .924 0. .00 0. .00 PROC

ATOM 3672 CZ TYR X 569 8. .140 -12 .438 9. .259 0. .00 0. .00 PROC

ATOM 3673 OH TYR X 569 7. .858 -11 .351 8. .424 0. .00 0. .00 PROC

ATOM 3674 HH TYR X 569 6. .909 -11 .207 8. .450 0. .00 0. .00 PROC

ATOM 3675 CD2 TYR X 569 9 .725 -13 .490 10. .729 0. .00 0. .00 PROC

ATOM 3676 HD2 TYR X 569 10 .697 -13 .409 11. .191 0. .00 0. .00 PROC

ATOM 3677 CE2 TYR X 569 9 .383 -12 .451 9. .856 0. .00 0. .00 PROC

ATOM 3678 HE2 TYR X 569 10 .001 -11 .575 9. .730 0. .00 0. .00 PROC

ATOM 3679 C TYR X 569 10 .524 -16 .561 13. .719 0. .00 0. .00 PROC

ATOM 3680 O TYR X 569 10 .950 -15 .961 14. .712 0. .00 0. .00 PROC

ATOM 3681 N ALA X 570 9. .960 -17 .748 13. .893 0. .00 0. .00 PROC

ATOM 3682 HN ALA X 570 9. .461 -18 .173 13. .142 0. .00 0. .00 PROC

ATOM 3683 CA ALA X 570 9. .939 -18 .501 15. .182 0. .00 0. .00 PROC

ATOM 3684 HA ALA X 570 9. .796 -17 .872 16. .048 0. .00 0. .00 PROC

ATOM 3685 CB ALA X 570 8. .840 -19 .524 15. .072 0. .00 0. .00 PROC

ATOM 3686 HB1 ALA X 570 8 .670 -19 .976 16. .073 0. .00 0. .00 PROC

ATOM 3687 HB2 ALA X 570 7 .918 -19 .019 14. .712 0. .00 0. .00 PROC

ATOM 3688 HB3 ALA X 570 9 .150 -20 .326 14. .368 0. .00 0. .00 PROC

ATOM 3689 C ALA X 570 11 .330 -18 .963 15. .584 0. .00 0. .00 PROC

ATOM 3690 O ALA X 570 11 .648 -19 .000 16. .717 0. .00 0. .00 PROC

ATOM 3691 N ILE X 571 12 .241 -19 .386 14. .701 0. .00 0. .00 PROC

ATOM 3692 HN ILE X 571 12 .031 -19 .243 13. .737 0. .00 0. .00 PROC

ATOM 3693 CA ILE X 571 13 .307 -20 .296 15. .084 0. .00 0. .00 PROC

ATOM 3694 HA ILE X 571 12 .735 -21 .092 15. .537 0. .00 0. .00 PROC

ATOM 3695 CB ILE X 571 14 .075 -20 .874 13. .853 0. .00 0. .00 PROC ATOM 3696 HB ILE X 571 13.373 -21.341 13..129 0..00 0..00 PROC

ATOM 3697 CG2 ILE X 571 14 .809 -19 .780 13. .096 0. .00 0. .00 PROC

ATOM 3698 HG21 ILE X 571 14 .826 -20 .150 12. .048 0. .00 0. .00 PROC

ATOM 3699 HG22 ILE X 571 14 .251 -18 .820 13. .069 0. .00 0. .00 PROC

ATOM 3700 HG23 ILE X 571 15 .889 -19 .694 13. .343 0. .00 0. .00 PROC

ATOM 3701 CGI ILE X 571 15 .016 -21 .946 14. .220 0. .00 0. .00 PROC

ATOM 3702 HG11 ILE X 571 15 .722 -22 .107 13. .377 0. .00 0. .00 PROC

ATOM 3703 HG12 ILE X 571 15 .686 -21 .711 15. .074 0. .00 0. .00 PROC

ATOM 3704 CD ILE X 571 14 .254 -23 .178 14. .602 0. .00 0. .00 PROC

ATOM 3705 HD1 ILE X 571 13 .402 -22 .988 15. .290 0. .00 0. .00 PROC

ATOM 3706 HD2 ILE X 571 13 .816 -23 .619 13. .682 0. .00 0. .00 PROC

ATOM 3707 HD3 ILE X 571 14 .951 -23 .999 14. .872 0. .00 0. .00 PROC

ATOM 3708 C ILE X 571 14 .292 -19 .768 16. . Ill 0. .00 0. .00 PROC

ATOM 3709 O ILE X 571 14 .782 -20 .466 16. .976 0. .00 0. .00 PROC

ATOM 3710 N GLY X 572 14 .562 -18 .431 16. .090 0. .00 0. .00 PROC

ATOM 3711 HN GLY X 572 14 .108 -17 .828 15. .439 0. .00 0. .00 PROC

ATOM 3712 CA GLY X 572 15 .423 -17 .892 17. .055 0. .00 0. .00 PROC

ATOM 3713 HA1 GLY X 572 15 .693 -16 .902 16. .719 0. .00 0. .00 PROC

ATOM 3714 HA2 GLY X 572 16 .299 -18 .478 17. .289 0. .00 0. .00 PROC

ATOM 3715 C GLY X 572 14 .789 -17 .824 18. .499 0. .00 0. .00 PROC

ATOM 3716 O GLY X 572 15 .473 -17 .851 19. .510 0. .00 0. .00 PROC

ATOM 3717 N ASN X 573 13 .400 -17 .912 18. .594 0. .00 0. .00 PROC

ATOM 3718 HN ASN X 573 12 .873 -17 .885 17. .748 0. .00 0. .00 PROC

ATOM 3719 CA ASN X 573 12 .706 -18 .118 19. .871 0. .00 0. .00 PROC

ATOM 3720 HA ASN X 573 13 .168 -17 .513 20. .637 0. .00 0. .00 PROC

ATOM 3721 CB ASN X 573 11 .283 -17 .543 19. .831 0. .00 0. .00 PROC

ATOM 3722 HB1 ASN X 573 10 .779 -18 .081 19. .000 0. .00 0. .00 PROC

ATOM 3723 HB2 ASN X 573 10 .820 -17 .781 20. .813 0. .00 0. .00 PROC

ATOM 3724 CG ASN X 573 11 .395 -16 .044 19. .698 0. .00 0. .00 PROC

ATOM 3725 OD1 ASN X 573 11 .314 -15 .354 20. .757 0. .00 0. .00 PROC

ATOM 3726 ND2 ASN X 573 11 .487 -15 .462 18. .441 0. .00 0. .00 PROC

ATOM 3727 HD21 ASN X 573 11 .421 -14 .488 18. .227 0. .00 0. .00 PROC

ATOM 3728 HD22 ASN X 573 11 .504 -16 .115 17. .684 0. .00 0. .00 PROC

ATOM 3729 C ASN X 573 12 .769 -19 .512 20. .285 0. .00 0. .00 PROC

ATOM 3730 O ASN X 573 12 .461 -19 .782 21. .405 0. .00 0. .00 PROC

ATOM 3731 N MET X 574 13 .118 -20 .495 19. .416 0. .00 0. .00 PROC

ATOM 3732 HN MET X 574 13 .224 -20 .229 18. .461 0. .00 0. .00 PROC

ATOM 3733 CA MET X 574 13 .157 -21 .927 19. .785 0. .00 0. .00 PROC

ATOM 3734 HA MET X 574 12 .610 -22 .172 20. .684 0. .00 0. .00 PROC

ATOM 3735 CB MET X 574 12 .476 -22 .661 18. .587 0. .00 0. .00 PROC

ATOM 3736 HB1 MET X 574 13 .040 -22 .376 17. .674 0. .00 0. .00 PROC

ATOM 3737 HB2 MET X 574 12 .506 -23 .764 18. .718 0. .00 0. .00 PROC

ATOM 3738 CG MET X 574 10 .994 -22 .300 18. .248 0. .00 0. .00 PROC

ATOM 3739 HG1 MET X 574 10 .498 -22 .633 19. .185 0. .00 0. .00 PROC

ATOM 3740 HG2 MET X 574 10 .778 -21 .210 18. .262 0. .00 0. .00 PROC

ATOM 3741 C MET X 574 14 .564 -22 .522 19. .987 0. .00 0. .00 PROC

ATOM 3742 O MET X 574 14 .721 -23 .736 20. .304 0. .00 0. .00 PROC

ATOM 3743 N GLU X 575 15 .613 -21 .679 19. .724 0. .00 0. .00 PROC

ATOM 3744 HN GLU X 575 15 .454 -20 .785 19. .312 0. .00 0. .00 PROC

ATOM 3745 CA GLU X 575 16 .931 -22 .065 19. .991 0. .00 0. .00 PROC

ATOM 3746 HA GLU X 575 17 .182 -23 .006 19. .524 0. .00 0. .00 PROC

ATOM 3747 CB GLU X 575 17 .825 -20 .908 19. .363 0. .00 0. .00 PROC

ATOM 3748 HB1 GLU X 575 17 .750 -20 .916 18. .254 0. .00 0. .00 PROC

ATOM 3749 HB2 GLU X 575 17 .523 -19 .928 19. .788 0. .00 0. .00 PROC

ATOM 3750 CG GLU X 575 19 .388 -20 .989 19. .654 0. .00 0. .00 PROC

ATOM 3751 HG1 GLU X 575 19 .647 -21 .244 20. .704 0. .00 0. .00 PROC

ATOM 3752 HG2 GLU X 575 19 .695 -21 .750 18. .905 0. .00 0. .00 PROC

ATOM 3753 CD GLU X 575 20 .230 -19 .781 19. .159 0. .00 0. .00 PROC

ATOM 3754 OE1 GLU X 575 19 .881 -19 .208 18. .134 0. .00 0. .00 PROC

ATOM 3755 OE2 GLU X 575 21 .161 -19 .423 19. .898 0. .00 0. .00 PROC

ATOM 3756 C GLU X 575 17 .193 -22 .267 21. .486 0. .00 0. .00 PROC

ATOM 3757 O GLU X 575 17 .869 -23 .202 21. .866 0. .00 0. .00 PROC

ATOM 3758 N GLN X 576 16 .610 -21 .295 22. .270 0. .00 0. .00 PROC

ATOM 3759 HN GLN X 576 16 .340 -20 .458 21. .800 0. .00 0. .00 PROC

ATOM 3760 CA GLN X 576 16 .689 -21 .375 23. .737 0. .00 0. .00 PROC

ATOM 3761 HA GLN X 576 16 .415 -20 .440 24. .201 0. .00 0. .00 PROC ATOM 3762 CB GLN X 576 15.519 -22.286 24..284 0..00 0..00 PROC

ATOM 3763 HB1 GLN X 576 15 .752 -23 .334 23. .998 0. .00 0. .00 PROC

ATOM 3764 HB2 GLN X 576 15 .369 -22 .144 25. .376 0. .00 0. .00 PROC

ATOM 3765 CG GLN X 576 14 .131 -21 .906 23. .755 0. .00 0. .00 PROC

ATOM 3766 HG1 GLN X 576 13 .601 -21 .142 24. .364 0. .00 0. .00 PROC

ATOM 3767 HG2 GLN X 576 14 .231 -21 .505 22. .724 0. .00 0. .00 PROC

ATOM 3768 CD GLN X 576 13 .204 -23 .180 23. .800 0. .00 0. .00 PROC

ATOM 3769 OE1 GLN X 576 12 .305 -23 .274 24. .637 0. .00 0. .00 PROC

ATOM 3770 NE2 GLN X 576 13 .445 -24 .151 22. .929 0. .00 0. .00 PROC

ATOM 3771 HE21 GLN X 576 12 .962 -25 .027 22. .943 0. .00 0. .00 PROC

ATOM 3772 HE22 GLN X 576 14 .258 -24 .145 22. .347 0. .00 0. .00 PROC

ATOM 3773 C GLN X 576 18 .083 -21 .816 24. .377 0. .00 0. .00 PROC

ATOM 3774 O GLN X 576 18 .197 -22 .904 25. .023 0. .00 0. .00 PROC

ATOM 3775 N PRO X 577 19 .239 -21 .041 24. .101 0. .00 0. .00 PROC

ATOM 3776 CD PRO X 577 19 .194 -19 .701 23. .500 0. .00 0. .00 PROC

ATOM 3777 HD1 PRO X 577 18 .630 -19 .717 22. .543 0. .00 0. .00 PROC

ATOM 3778 HD2 PRO X 577 18 .869 -18 .888 24. .184 0. .00 0. .00 PROC

ATOM 3779 CA PRO X 577 20 .577 -21 .275 24. .755 0. .00 0. .00 PROC

ATOM 3780 HA PRO X 577 20 .965 -22 .152 24. .258 0. .00 0. .00 PROC

ATOM 3781 CB PRO X 577 21 .297 -19 .955 24. .519 0. .00 0. .00 PROC

ATOM 3782 HB1 PRO X 577 22 .403 -19 .880 24. .444 0. .00 0. .00 PROC

ATOM 3783 HB2 PRO X 577 21 .039 -19 .282 25. .364 0. .00 0. .00 PROC

ATOM 3784 CG PRO X 577 20 .638 -19 .434 23. .211 0. .00 0. .00 PROC

ATOM 3785 HG1 PRO X 577 20 .931 -20 .082 22. .357 0. .00 0. .00 PROC

ATOM 3786 HG2 PRO X 577 20 .959 -18 .412 22. .917 0. .00 0. .00 PROC

ATOM 3787 C PRO X 577 20 .579 -21 .845 26. .184 0. .00 0. .00 PROC

ATOM 3788 O PRO X 577 19 .980 -21 .280 27. .095 0. .00 0. .00 PROC

ATOM 3789 N HSD X 578 21 .282 -22 .980 26. .483 0. .00 0. .00 PROC

ATOM 3790 HN HSD X 578 21 .767 -23 .411 25. .726 0. .00 0. .00 PROC

ATOM 3791 CA HSD X 578 21 .326 -23 .668 27. .762 0. .00 0. .00 PROC

ATOM 3792 HA HSD X 578 20 .428 -23 .297 28. .233 0. .00 0. .00 PROC

ATOM 3793 CB HSD X 578 21 .173 -25 .233 27. .639 0. .00 0. .00 PROC

ATOM 3794 HB1 HSD X 578 20 .437 -25 .389 26. .821 0. .00 0. .00 PROC

ATOM 3795 HB2 HSD X 578 22 .081 -25 .688 27. .188 0. .00 0. .00 PROC

ATOM 3796 ND1 HSD X 578 19 .512 -25 .699 29. .608 0. .00 0. .00 PROC

ATOM 3797 HD1 HSD X 578 18 .757 -25 .099 29. .344 0. .00 0. .00 PROC

ATOM 3798 CG HSD X 578 20 .644 -26 .007 28. .924 0. .00 0. .00 PROC

ATOM 3799 CE1 HSD X 578 19 .403 -26 .597 30. .624 0. .00 0. .00 PROC

ATOM 3800 HE1 HSD X 578 18 .420 -26 .813 31. .043 0. .00 0. .00 PROC

ATOM 3801 NE2 HSD X 578 20 .430 -27 .482 30. .693 0. .00 0. .00 PROC

ATOM 3802 CD2 HSD X 578 21 .160 -27 .164 29. .547 0. .00 0. .00 PROC

ATOM 3803 HD2 HSD X 578 21 .985 -27 .761 29. .180 0. .00 0. .00 PROC

ATOM 3804 C HSD X 578 22 .574 -23 .230 28. .548 0. .00 0. .00 PROC

ATOM 3805 O HSD X 578 22 .880 -23 .945 29. .529 0. .00 0. .00 PROC

ATOM 3806 N MET X 579 23 .296 -22 .208 28. .154 0. .00 0. .00 PROC

ATOM 3807 HN MET X 579 23 .045 -21 .762 27. .298 0. .00 0. .00 PROC

ATOM 3808 CA MET X 579 24 .655 -21 .885 28. .594 0. .00 0. .00 PROC

ATOM 3809 HA MET X 579 25 .005 -22 .802 29. .044 0. .00 0. .00 PROC

ATOM 3810 CB MET X 579 25 .398 -21 .433 27. .341 0. .00 0. .00 PROC

ATOM 3811 HB1 MET X 579 26 .391 -21 .034 27. .638 0. .00 0. .00 PROC

ATOM 3812 HB2 MET X 579 25 .334 -22 .281 26. .626 0. .00 0. .00 PROC

ATOM 3813 CG MET X 579 24 .733 -20 .276 26. .561 0. .00 0. .00 PROC

ATOM 3814 HG1 MET X 579 25 .066 -20 .324 25. .502 0. .00 0. .00 PROC

ATOM 3815 HG2 MET X 579 23 .627 -20 .380 26. .594 0. .00 0. .00 PROC

ATOM 3816 C MET X 579 24 .762 -20 .860 29. .648 0. .00 0. .00 PROC

ATOM 3817 O MET X 579 25 .885 -20 .619 30. .141 0. .00 0. .00 PROC

ATOM 3818 N ASP X 580 23 .661 -20 .320 30. .106 0. .00 0. .00 PROC

ATOM 3819 HN ASP X 580 22 .783 -20 .584 29. .714 0. .00 0. .00 PROC

ATOM 3820 CA ASP X 580 23 .525 -19 .362 31. .117 0. .00 0. .00 PROC

ATOM 3821 HA ASP X 580 24 .161 -19 .677 31. .932 0. .00 0. .00 PROC

ATOM 3822 CB ASP X 580 23 .901 -17 .985 30. .502 0. .00 0. .00 PROC

ATOM 3823 HB1 ASP X 580 24 .904 -18 .076 30. .033 0. .00 0. .00 PROC

ATOM 3824 HB2 ASP X 580 23 .157 -17 .768 29. .706 0. .00 0. .00 PROC

ATOM 3825 CG ASP X 580 24 .012 -16 .878 31. .531 0. .00 0. .00 PROC

ATOM 3826 OD1 ASP X 580 24 .819 -17 .008 32. .512 0. .00 0. .00 PROC

ATOM 3827 OD2 ASP X 580 23 .348 -15 .811 31. .371 0. .00 0. .00 PROC ATOM 3828 C ASP X 580 22.140 -19.413 31..702 0..00 0..00 PROC

ATOM 3829 O ASP X 580 21 .208 -19 .867 31. .093 0. .00 0. .00 PROC

ATOM 3830 N SER X 581 22 .029 -19 .040 33. .022 0. .00 0. .00 PROC

ATOM 3831 HN SER X 581 22 .856 -18 .696 33. .459 0. .00 0. .00 PROC

ATOM 3832 CA SER X 581 20 .774 -19 .024 33. .786 0. .00 0. .00 PROC

ATOM 3833 HA SER X 581 20 .499 -20 .058 33. .934 0. .00 0. .00 PROC

ATOM 3834 CB SER X 581 21 .160 -18 .626 35. .270 0. .00 0. .00 PROC

ATOM 3835 HB1 SER X 581 21 .943 -19 .356 35. .569 0. .00 0. .00 PROC

ATOM 3836 HB2 SER X 581 21 .623 -17 .617 35. .276 0. .00 0. .00 PROC

ATOM 3837 OG SER X 581 20 .040 -18 .778 36. .167 0. .00 0. .00 PROC

ATOM 3838 HG1 SER X 581 20 .359 -19 .065 37. .026 0. .00 0. .00 PROC

ATOM 3839 C SER X 581 19 .595 -18 .191 33. .110 0. .00 0. .00 PROC

ATOM 3840 O SER X 581 19 .797 -17 .088 32. .620 0. .00 0. .00 PROC

ATOM 3841 N ARG X 582 18 .421 -18 .809 33. .114 0. .00 0. .00 PROC

ATOM 3842 HN ARG X 582 18 .343 -19 .749 33. .437 0. .00 0. .00 PROC

ATOM 3843 CA ARG X 582 17 .219 -18 .015 33. .058 0. .00 0. .00 PROC

ATOM 3844 HA ARG X 582 17 .250 -17 .211 32. .338 0. .00 0. .00 PROC

ATOM 3845 CB ARG X 582 16 .057 -18 .961 32. .747 0. .00 0. .00 PROC

ATOM 3846 HB1 ARG X 582 15 .971 -19 .716 33. .558 0. .00 0. .00 PROC

ATOM 3847 HB2 ARG X 582 15 .076 -18 .441 32. .719 0. .00 0. .00 PROC

ATOM 3848 CG ARG X 582 16 .265 -19 .824 31. .449 0. .00 0. .00 PROC

ATOM 3849 HG1 ARG X 582 16 .444 -19 .263 30. .507 0. .00 0. .00 PROC

ATOM 3850 HG2 ARG X 582 17 .171 -20 .453 31. .580 0. .00 0. .00 PROC

ATOM 3851 CD ARG X 582 15 .067 -20 .764 31. .216 0. .00 0. .00 PROC

ATOM 3852 HD1 ARG X 582 15 .009 -21 .629 31. .910 0. .00 0. .00 PROC

ATOM 3853 HD2 ARG X 582 14 .148 -20 .181 31. .440 0. .00 0. .00 PROC

ATOM 3854 NE ARG X 582 15 .126 -21 .220 29. .851 0. .00 0. .00 PROC

ATOM 3855 HE ARG X 582 15 .891 -21 .005 29. .242 0. .00 0. .00 PROC

ATOM 3856 CZ ARG X 582 14 .123 -21 .935 29. .233 0. .00 0. .00 PROC

ATOM 3857 NH1 ARG X 582 12 .897 -22 .095 29. .657 0. .00 0. .00 PROC

ATOM 3858 HH11 ARG X 582 12 .210 -22 .577 29. .114 0. .00 0. .00 PROC

ATOM 3859 HH12 ARG X 582 12 .695 -21 .692 30. .549 0. .00 0. .00 PROC

ATOM 3860 NH2 ARG X 582 14 .455 -22 .401 28. .033 0. .00 0. .00 PROC

ATOM 3861 HH21 ARG X 582 13 .753 -22 .888 27. .514 0. .00 0. .00 PROC

ATOM 3862 HH22 ARG X 582 15 .370 -22 .096 27. .770 0. .00 0. .00 PROC

ATOM 3863 C ARG X 582 16 .943 -17 .385 34. .431 0. .00 0. .00 PROC

ATOM 3864 O ARG X 582 16 .423 -16 .304 34. .458 0. .00 0. .00 PROC

ATOM 3865 N ILE X 583 17 .188 -18 .060 35. .597 0. .00 0. .00 PROC

ATOM 3866 HN ILE X 583 17 .562 -18 .979 35. .694 0. .00 0. .00 PROC

ATOM 3867 CA ILE X 583 16 .894 -17 .584 36. .949 0. .00 0. .00 PROC

ATOM 3868 HA ILE X 583 15 .861 -17 .308 37. .100 0. .00 0. .00 PROC

ATOM 3869 CB ILE X 583 17 .267 -18 .621 38. .094 0. .00 0. .00 PROC

ATOM 3870 HB ILE X 583 18 .361 -18 .480 38. .231 0. .00 0. .00 PROC

ATOM 3871 CG2 ILE X 583 16 .554 -18 .110 39. .395 0. .00 0. .00 PROC

ATOM 3872 HG21 ILE X 583 15 .748 -17 .394 39. .128 0. .00 0. .00 PROC

ATOM 3873 HG22 ILE X 583 16 .206 -18 .956 40. .025 0. .00 0. .00 PROC

ATOM 3874 HG23 ILE X 583 17 .270 -17 .464 39. .949 0. .00 0. .00 PROC

ATOM 3875 CGI ILE X 583 16 .933 -20 .089 37. .723 0. .00 0. .00 PROC

ATOM 3876 HG11 ILE X 583 17 .316 -20 .222 36. .689 0. .00 0. .00 PROC

ATOM 3877 HG12 ILE X 583 17 .529 -20 .711 38. .425 0. .00 0. .00 PROC

ATOM 3878 CD ILE X 583 15 .451 -20 .393 37. .858 0. .00 0. .00 PROC

ATOM 3879 HD1 ILE X 583 15 .009 -20 .393 38. .877 0. .00 0. .00 PROC

ATOM 3880 HD2 ILE X 583 14 .787 -19 .777 37. .215 0. .00 0. .00 PROC

ATOM 3881 HD3 ILE X 583 15 .364 -21 .452 37. .533 0. .00 0. .00 PROC

ATOM 3882 C ILE X 583 17 .606 -16 .307 37. .303 0. .00 0. .00 PROC

ATOM 3883 O ILE X 583 16 .974 -15 .421 37. .872 0. .00 0. .00 PROC

ATOM 3884 N GLY X 584 18 .910 -16 .209 36. .923 0. .00 0. .00 PROC

ATOM 3885 HN GLY X 584 19 .264 -16 .882 36. .278 0. .00 0. .00 PROC

ATOM 3886 CA GLY X 584 19 .769 -15 .095 37. .154 0. .00 0. .00 PROC

ATOM 3887 HA1 GLY X 584 20 .797 -15 .420 37. .099 0. .00 0. .00 PROC

ATOM 3888 HA2 GLY X 584 19 .566 -14 .657 38. .120 0. .00 0. .00 PROC

ATOM 3889 C GLY X 584 19 .538 -13 .990 36. .173 0. .00 0. .00 PROC

ATOM 3890 O GLY X 584 20 .156 -12 .928 36. .227 0. .00 0. .00 PROC

ATOM 3891 N TRP X 585 18 .784 -14 .220 35. .076 0. .00 0. .00 PROC

ATOM 3892 HN TRP X 585 18 .220 -15 .040 35. .027 0. .00 0. .00 PROC

ATOM 3893 CA TRP X 585 18 .615 -13 .241 34. .029 0. .00 0. .00 PROC ATOM 3894 HA TRP X 585 19.550 -12.975 33..560 0..00 0..00 PROC

ATOM 3895 CB TRP X 585 17 .777 -13 .968 32. .987 0. .00 0. .00 PROC

ATOM 3896 HB1 TRP X 585 17 .857 -15 .076 33. .011 0. .00 0. .00 PROC

ATOM 3897 HB2 TRP X 585 16 .726 -13 .709 33. .234 0. .00 0. .00 PROC

ATOM 3898 CG TRP X 585 18 .158 -13 .617 31. .637 0. .00 0. .00 PROC

ATOM 3899 CD1 TRP X 585 19 .220 -14 .018 30. .870 0. .00 0. .00 PROC

ATOM 3900 HD1 TRP X 585 19 .954 -14 .714 31. .248 0. .00 0. .00 PROC

ATOM 3901 NE1 TRP X 585 19 .294 -13 .255 29. .741 0. .00 0. .00 PROC

ATOM 3902 HE1 TRP X 585 19 .740 -13 .486 28. .904 0. .00 0. .00 PROC

ATOM 3903 CE2 TRP X 585 18 .293 -12 .415 29. .703 0. .00 0. .00 PROC

ATOM 3904 CD2 TRP X 585 17 .543 -12 .587 30. .871 0. .00 0. .00 PROC

ATOM 3905 CE3 TRP X 585 16 .385 -11 .914 31. .081 0. .00 0. .00 PROC

ATOM 3906 HE3 TRP X 585 15 .644 -12 .160 31. .827 0. .00 0. .00 PROC

ATOM 3907 CZ3 TRP X 585 15 .935 -10 .969 30. .151 0. .00 0. .00 PROC

ATOM 3908 HZ3 TRP X 585 14 .936 -10 .569 30. .240 0. .00 0. .00 PROC

ATOM 3909 CZ2 TRP X 585 17 .862 -11 .474 28. .780 0. .00 0. .00 PROC

ATOM 3910 HZ2 TRP X 585 18 .488 -11 .202 27. .943 0. .00 0. .00 PROC

ATOM 3911 CH2 TRP X 585 16 .706 -10 .714 29. .008 0. .00 0. .00 PROC

ATOM 3912 HH2 TRP X 585 16 .486 -9 .957 28. .269 0. .00 0. .00 PROC

ATOM 3913 C TRP X 585 17 .962 -11 .949 34. .338 0. .00 0. .00 PROC

ATOM 3914 O TRP X 585 18 .205 -10 .875 33. .659 0. .00 0. .00 PROC

ATOM 3915 N LEU X 586 17 .042 -11 .939 35. .340 0. .00 0. .00 PROC

ATOM 3916 HN LEU X 586 16 .944 -12 .727 35. .943 0. .00 0. .00 PROC

ATOM 3917 CA LEU X 586 16 .312 -10 .750 35. .729 0. .00 0. .00 PROC

ATOM 3918 HA LEU X 586 15 .866 -10 .274 34. .868 0. .00 0. .00 PROC

ATOM 3919 CB LEU X 586 15 .045 -10 .999 36. .571 0. .00 0. .00 PROC

ATOM 3920 HB1 LEU X 586 15 .363 -11 .229 37. .610 0. .00 0. .00 PROC

ATOM 3921 HB2 LEU X 586 14 .484 -10 .040 36. .574 0. .00 0. .00 PROC

ATOM 3922 CG LEU X 586 14 .125 -12 .086 35. .946 0. .00 0. .00 PROC

ATOM 3923 HG LEU X 586 14 .601 -13 .080 35. .807 0. .00 0. .00 PROC

ATOM 3924 CD1 LEU X 586 12 .924 -12 .462 36. .806 0. .00 0. .00 PROC

ATOM 3925 HD11 LEU X 586 12 .110 -12 .980 36. .255 0. .00 0. .00 PROC

ATOM 3926 HD12 LEU X 586 13 .370 -12 .974 37. .685 0. .00 0. .00 PROC

ATOM 3927 HD13 LEU X 586 12 .528 -11 .464 37. .092 0. .00 0. .00 PROC

ATOM 3928 CD2 LEU X 586 13 .662 -11 .756 34. .431 0. .00 0. .00 PROC

ATOM 3929 HD21 LEU X 586 13 .325 -10 .698 34. .391 0. .00 0. .00 PROC

ATOM 3930 HD22 LEU X 586 14 .569 -11 .999 33. .837 0. .00 0. .00 PROC

ATOM 3931 HD23 LEU X 586 12 .798 -12 .414 34. .198 0. .00 0. .00 PROC

ATOM 3932 C LEU X 586 17 .249 -9 .761 36. .465 0. .00 0. .00 PROC

ATOM 3933 O LEU X 586 17 .186 -8 .530 36. .348 0. .00 0. .00 PROC

ATOM 3934 N HSD X 587 18 .183 -10 .263 37. .309 0. .00 0. .00 PROC

ATOM 3935 HN HSD X 587 18 .250 -11 .238 37. .502 0. .00 0. .00 PROC

ATOM 3936 CA HSD X 587 19 .255 -9 .417 37. .836 0. .00 0. .00 PROC

ATOM 3937 HA HSD X 587 18 .771 -8 .562 38. .284 0. .00 0. .00 PROC

ATOM 3938 CB HSD X 587 20 .135 -10 .008 38. .960 0. .00 0. .00 PROC

ATOM 3939 HB1 HSD X 587 20 .558 -11 .007 38. .720 0. .00 0. .00 PROC

ATOM 3940 HB2 HSD X 587 20 .940 -9 .258 39. .110 0. .00 0. .00 PROC

ATOM 3941 ND1 HSD X 587 20 .341 -10 .095 41. .423 0. .00 0. .00 PROC

ATOM 3942 HD1 HSD X 587 21 .330 -10 .186 41. .538 0. .00 0. .00 PROC

ATOM 3943 CG HSD X 587 19 .479 -10 .005 40. .354 0. .00 0. .00 PROC

ATOM 3944 CE1 HSD X 587 19 .543 -10 .005 42. .548 0. .00 0. .00 PROC

ATOM 3945 HE1 HSD X 587 19 .939 -9 .828 43. .548 0. .00 0. .00 PROC

ATOM 3946 NE2 HSD X 587 18 .255 -9 .793 42. .247 0. .00 0. .00 PROC

ATOM 3947 CD2 HSD X 587 18 .219 -9 .939 40. .852 0. .00 0. .00 PROC

ATOM 3948 HD2 HSD X 587 17 .293 -9 .786 40. .310 0. .00 0. .00 PROC

ATOM 3949 C HSD X 587 20 .150 -8 .909 36. .804 0. .00 0. .00 PROC

ATOM 3950 O HSD X 587 20 .502 -7 .759 36. .722 0. .00 0. .00 PROC

ATOM 3951 N ASN X 588 20 .466 -9 .740 35. .800 0. .00 0. .00 PROC

ATOM 3952 HN ASN X 588 20 .431 -10 .733 35. .875 0. .00 0. .00 PROC

ATOM 3953 CA ASN X 588 21 .284 -9 .335 34. .615 0. .00 0. .00 PROC

ATOM 3954 HA ASN X 588 22 .165 -8 .825 34. .976 0. .00 0. .00 PROC

ATOM 3955 CB ASN X 588 21 .832 -10 .527 33. .876 0. .00 0. .00 PROC

ATOM 3956 HB1 ASN X 588 21 .089 -11 .261 33. .499 0. .00 0. .00 PROC

ATOM 3957 HB2 ASN X 588 22 .376 -10 .167 32. .976 0. .00 0. .00 PROC

ATOM 3958 CG ASN X 588 22 .935 -11 .272 34. .729 0. .00 0. .00 PROC

ATOM 3959 OD1 ASN X 588 23 .331 -10 .908 35. .817 0. .00 0. .00 PROC ATOM 3960 ND2 ASN X 588 23.517 -12.304 34..082 0..00 0..00 PROC

ATOM 3961 HD21 ASN X 588 24 .180 -12 .807 34. .636 0. .00 0. .00 PROC

ATOM 3962 HD22 ASN X 588 23 .099 -12 .522 33. .200 0. .00 0. .00 PROC

ATOM 3963 C ASN X 588 20 .683 -8 .248 33. .785 0. .00 0. .00 PROC

ATOM 3964 O ASN X 588 21 .337 -7 .281 33. .412 0. .00 0. .00 PROC

ATOM 3965 N LEU X 589 19 .383 -8 .409 33. .417 0. .00 0. .00 PROC

ATOM 3966 HN LEU X 589 18 .920 -9 .283 33. .540 0. .00 0. .00 PROC

ATOM 3967 CA LEU X 589 18 .655 -7 .428 32. .639 0. .00 0. .00 PROC

ATOM 3968 HA LEU X 589 19 .080 -7 .234 31. .665 0. .00 0. .00 PROC

ATOM 3969 CB LEU X 589 17 .173 -7 .891 32. .572 0. .00 0. .00 PROC

ATOM 3970 HB1 LEU X 589 17 .128 -8 .855 32. .022 0. .00 0. .00 PROC

ATOM 3971 HB2 LEU X 589 16 .721 -7 .969 33. .584 0. .00 0. .00 PROC

ATOM 3972 CG LEU X 589 16 .213 -6 .933 31. .852 0. .00 0. .00 PROC

ATOM 3973 HG LEU X 589 16 .179 -5 .971 32. .407 0. .00 0. .00 PROC

ATOM 3974 CD1 LEU X 589 16 .569 -6 .715 30. .358 0. .00 0. .00 PROC

ATOM 3975 HD11 LEU X 589 17 .619 -6 .352 30. .323 0. .00 0. .00 PROC

ATOM 3976 HD12 LEU X 589 16 .488 -7 .674 29. .803 0. .00 0. .00 PROC

ATOM 3977 HD13 LEU X 589 15 .976 -5 .875 29. .937 0. .00 0. .00 PROC

ATOM 3978 CD2 LEU X 589 14 .852 -7 .531 31. .855 0. .00 0. .00 PROC

ATOM 3979 HD21 LEU X 589 14 .163 -6 .867 31. .289 0. .00 0. .00 PROC

ATOM 3980 HD22 LEU X 589 14 .734 -8 .531 31. .387 0. .00 0. .00 PROC

ATOM 3981 HD23 LEU X 589 14 .414 -7 .545 32. .876 0. .00 0. .00 PROC

ATOM 3982 C LEU X 589 18 .507 -6 .093 33. .338 0. .00 0. .00 PROC

ATOM 3983 O LEU X 589 18 .740 -4 .964 32. .728 0. .00 0. .00 PROC

ATOM 3984 N GLY X 590 18 .199 -5 .996 34. .659 0. .00 0. .00 PROC

ATOM 3985 HN GLY X 590 17 .980 -6 .703 35. .327 0. .00 0. .00 PROC

ATOM 3986 CA GLY X 590 18 .148 -4 .639 35. .318 0. .00 0. .00 PROC

ATOM 3987 HA1 GLY X 590 17 .566 -4 .682 36. .227 0. .00 0. .00 PROC

ATOM 3988 HA2 GLY X 590 17 .552 -4 .061 34. .627 0. .00 0. .00 PROC

ATOM 3989 C GLY X 590 19 .436 -3 .855 35. .571 0. .00 0. .00 PROC

ATOM 3990 O GLY X 590 19 .362 -2 .636 35. .773 0. .00 0. .00 PROC

ATOM 3991 N ASP X 591 20 .629 -4 .506 35. .583 0. .00 0. .00 PROC

ATOM 3992 HN ASP X 591 20 .637 -5 .503 35. .584 0. .00 0. .00 PROC

ATOM 3993 CA ASP X 591 21 .928 -3 .810 35. .479 0. .00 0. .00 PROC

ATOM 3994 HA ASP X 591 21 .851 -2 .791 35. .831 0. .00 0. .00 PROC

ATOM 3995 CB ASP X 591 22 .977 -4 .501 36. .420 0. .00 0. .00 PROC

ATOM 3996 HB1 ASP X 591 22 .736 -5 .585 36. .478 0. .00 0. .00 PROC

ATOM 3997 HB2 ASP X 591 24 .015 -4 .270 36. .099 0. .00 0. .00 PROC

ATOM 3998 CG ASP X 591 22 .836 -3 .939 37. .831 0. .00 0. .00 PROC

ATOM 3999 OD1 ASP X 591 23 .051 -2 .724 37. .923 0. .00 0. .00 PROC

ATOM 4000 OD2 ASP X 591 22 .657 -4 .719 38. .777 0. .00 0. .00 PROC

ATOM 4001 C ASP X 591 22 .478 -3 .785 34. .027 0. .00 0. .00 PROC

ATOM 4002 O ASP X 591 23 .573 -3 .254 33. .838 0. .00 0. .00 PROC

ATOM 4003 N GLN X 592 21 .697 -4 .263 33. .022 0. .00 0. .00 PROC

ATOM 4004 HN GLN X 592 20 .848 -4 .730 33. .256 0. .00 0. .00 PROC

ATOM 4005 CA GLN X 592 22 .008 -4 .093 31. .576 0. .00 0. .00 PROC

ATOM 4006 HA GLN X 592 21 .409 -4 .830 31. .063 0. .00 0. .00 PROC

ATOM 4007 CB GLN X 592 21 .835 -2 .701 30. .959 0. .00 0. .00 PROC

ATOM 4008 HB1 GLN X 592 22 .586 -2 .039 31. .441 0. .00 0. .00 PROC

ATOM 4009 HB2 GLN X 592 21 .990 -2 .793 29. .863 0. .00 0. .00 PROC

ATOM 4010 CG GLN X 592 20 .384 -2 .156 31. .203 0. .00 0. .00 PROC

ATOM 4011 HG1 GLN X 592 19 .734 -2 .929 30. .741 0. .00 0. .00 PROC

ATOM 4012 HG2 GLN X 592 20 .080 -1 .982 32. .258 0. .00 0. .00 PROC

ATOM 4013 CD GLN X 592 20 .207 -0 .819 30. .496 0. .00 0. .00 PROC

ATOM 4014 OE1 GLN X 592 21 .156 -0 .120 30. .150 0. .00 0. .00 PROC

ATOM 4015 NE2 GLN X 592 18 .927 -0 .539 30. .184 0. .00 0. .00 PROC

ATOM 4016 HE21 GLN X 592 18 .675 0 .253 29. .628 0. .00 0. .00 PROC

ATOM 4017 HE22 GLN X 592 18 .142 -1 .020 30. .576 0. .00 0. .00 PROC

ATOM 4018 C GLN X 592 23 .298 -4 .652 31. .127 0. .00 0. .00 PROC

ATOM 4019 O GLN X 592 24 .148 -3 .991 30. .628 0. .00 0. .00 PROC

ATOM 4020 N ILE X 593 23 .457 -5 .950 31. .442 0. .00 0. .00 PROC

ATOM 4021 HN ILE X 593 22 .802 -6 .400 32. .044 0. .00 0. .00 PROC

ATOM 4022 CA ILE X 593 24 .673 -6 .631 31. .118 0. .00 0. .00 PROC

ATOM 4023 HA ILE X 593 25 .418 -5 .897 31. .390 0. .00 0. .00 PROC

ATOM 4024 CB ILE X 593 24 .837 -7 .893 31. .953 0. .00 0. .00 PROC

ATOM 4025 HB ILE X 593 23 .894 -8 .451 31. .773 0. .00 0. .00 PROC ATOM 4026 CG2 ILE X 593 25.890 -8.884 31..479 0..00 0..00 PROC

ATOM 4027 HG21 ILE X 593 25 .863 -9 .821 32. .075 0. .00 0. .00 PROC

ATOM 4028 HG22 ILE X 593 25 .621 -9 .118 30. .426 0. .00 0. .00 PROC

ATOM 4029 HG23 ILE X 593 26 .899 -8 .439 31. .609 0. .00 0. .00 PROC

ATOM 4030 CGI ILE X 593 25 .077 -7 .482 33. .400 0. .00 0. .00 PROC

ATOM 4031 HG11 ILE X 593 25 .960 -6 .814 33. .493 0. .00 0. .00 PROC

ATOM 4032 HG12 ILE X 593 24 .266 -6 .802 33. .736 0. .00 0. .00 PROC

ATOM 4033 CD ILE X 593 25 .326 -8 .602 34. .427 0. .00 0. .00 PROC

ATOM 4034 HD1 ILE X 593 25 .367 -8 .261 35. .484 0. .00 0. .00 PROC

ATOM 4035 HD2 ILE X 593 24 .510 -9 .356 34. .395 0. .00 0. .00 PROC

ATOM 4036 HD3 ILE X 593 26 .201 -9 .254 34. .218 0. .00 0. .00 PROC

ATOM 4037 C ILE X 593 24 .788 -6 .813 29. .603 0. .00 0. .00 PROC

ATOM 4038 O ILE X 593 23 .845 -7 .157 28. .934 0. .00 0. .00 PROC

ATOM 4039 N GLY X 594 25 .999 -6 .572 29. .043 0. .00 0. .00 PROC

ATOM 4040 HN GLY X 594 26 .824 -6 .321 29. .543 0. .00 0. .00 PROC

ATOM 4041 CA GLY X 594 26 .157 -6 .404 27. .625 0. .00 0. .00 PROC

ATOM 4042 HA1 GLY X 594 27 .039 -5 .787 27. .534 0. .00 0. .00 PROC

ATOM 4043 HA2 GLY X 594 25 .270 -5 .905 27. .261 0. .00 0. .00 PROC

ATOM 4044 C GLY X 594 26 .396 -7 .715 26. .900 0. .00 0. .00 PROC

ATOM 4045 O GLY X 594 26 .452 -7 .716 25. .688 0. .00 0. .00 PROC

ATOM 4046 N LYS X 595 26 .662 -8 .823 27. .644 0. .00 0. .00 PROC

ATOM 4047 HN LYS X 595 26 .839 -8 .751 28. .622 0. .00 0. .00 PROC

ATOM 4048 CA LYS X 595 26 .805 -10 .200 27. .151 0. .00 0. .00 PROC

ATOM 4049 HA LYS X 595 27 .750 -10 .309 26. .640 0. .00 0. .00 PROC

ATOM 4050 CB LYS X 595 26 .823 -11 .185 28. .281 0. .00 0. .00 PROC

ATOM 4051 HB1 LYS X 595 26 .033 -10 .951 29. .026 0. .00 0. .00 PROC

ATOM 4052 HB2 LYS X 595 26 .610 -12 .253 28. .060 0. .00 0. .00 PROC

ATOM 4053 CG LYS X 595 28 .184 -11 .049 29. .025 0. .00 0. .00 PROC

ATOM 4054 HG1 LYS X 595 29 .049 -11 .019 28. .328 0. .00 0. .00 PROC

ATOM 4055 HG2 LYS X 595 28 .242 -10 .158 29. .687 0. .00 0. .00 PROC

ATOM 4056 CD LYS X 595 28 .571 -12 .324 29. .801 0. .00 0. .00 PROC

ATOM 4057 HD1 LYS X 595 27 .941 -12 .389 30. .714 0. .00 0. .00 PROC

ATOM 4058 HD2 LYS X 595 28 .565 -13 .216 29. .139 0. .00 0. .00 PROC

ATOM 4059 CE LYS X 595 30 .011 -12 .169 30. .302 0. .00 0. .00 PROC

ATOM 4060 HE1 LYS X 595 30 .815 -12 .163 29. .535 0. .00 0. .00 PROC

ATOM 4061 HE2 LYS X 595 30 .122 -11 .258 30. .928 0. .00 0. .00 PROC

ATOM 4062 NZ LYS X 595 30 .307 -13 .254 31. .219 0. .00 0. .00 PROC

ATOM 4063 HZ1 LYS X 595 30 .716 -14 .053 30. .694 0. .00 0. .00 PROC

ATOM 4064 HZ2 LYS X 595 31 .024 -12 .964 31. .914 0. .00 0. .00 PROC

ATOM 4065 HZ3 LYS X 595 29 .444 -13 .583 31. .698 0. .00 0. .00 PROC

ATOM 4066 C LYS X 595 25 .587 -10 .647 26. .151 0. .00 0. .00 PROC

ATOM 4067 O LYS X 595 24 .462 -10 .236 26. .251 0. .00 0. .00 PROC

ATOM 4068 N PRO X 596 25 .776 -11 .576 25. .154 0. .00 0. .00 PROC

ATOM 4069 CD PRO X 596 27 .140 -12 .002 24. .785 0. .00 0. .00 PROC

ATOM 4070 HD1 PRO X 596 27 .866 -11 .162 24. .761 0. .00 0. .00 PROC

ATOM 4071 HD2 PRO X 596 27 .407 -12 .774 25. .538 0. .00 0. .00 PROC

ATOM 4072 CA PRO X 596 24 .828 -11 .829 24. .100 0. .00 0. .00 PROC

ATOM 4073 HA PRO X 596 24 .642 -10 .898 23. .585 0. .00 0. .00 PROC

ATOM 4074 CB PRO X 596 25 .596 -12 .875 23. .240 0. .00 0. .00 PROC

ATOM 4075 HB1 PRO X 596 25 .114 -12 .853 22. .239 0. .00 0. .00 PROC

ATOM 4076 HB2 PRO X 596 25 .486 -13 .916 23. .612 0. .00 0. .00 PROC

ATOM 4077 CG PRO X 596 27 .036 -12 .506 23. .337 0. .00 0. .00 PROC

ATOM 4078 HG1 PRO X 596 27 .119 -11 .691 22. .587 0. .00 0. .00 PROC

ATOM 4079 HG2 PRO X 596 27 .805 -13 .260 23. .064 0. .00 0. .00 PROC

ATOM 4080 C PRO X 596 23 .528 -12 .376 24. .665 0. .00 0. .00 PROC

ATOM 4081 O PRO X 596 22 .564 -11 .657 24. .532 0. .00 0. .00 PROC

ATOM 4082 N TYR X 597 23 .548 -13 .455 25. .519 0. .00 0. .00 PROC

ATOM 4083 HN TYR X 597 24 .456 -13 .821 25. .709 0. .00 0. .00 PROC

ATOM 4084 CA TYR X 597 22 .410 -14 .023 26. .175 0. .00 0. .00 PROC

ATOM 4085 HA TYR X 597 21 .596 -14 .145 25. .476 0. .00 0. .00 PROC

ATOM 4086 CB TYR X 597 22 .791 -15 .317 26. .999 0. .00 0. .00 PROC

ATOM 4087 HB1 TYR X 597 23 .373 -15 .943 26. .290 0. .00 0. .00 PROC

ATOM 4088 HB2 TYR X 597 23 .447 -15 .106 27. .871 0. .00 0. .00 PROC

ATOM 4089 CG TYR X 597 21 .664 -16 .126 27. .426 0. .00 0. .00 PROC

ATOM 4090 CD1 TYR X 597 21 .252 -16 .263 28. .723 0. .00 0. .00 PROC

ATOM 4091 HD1 TYR X 597 21 .821 -15 .728 29. .470 0. .00 0. .00 PROC ATOM 4092 CE1 TYR X 597 20.099 -16.968 29..087 0..00 0..00 PROC

ATOM 4093 HE1 TYR X 597 19 .753 -16 .879 30. .106 0. .00 0. .00 PROC

ATOM 4094 CZ TYR X 597 19 .388 -17 .684 28. .089 0. .00 0. .00 PROC

ATOM 4095 OH TYR X 597 18 .189 -18 .386 28. .484 0. .00 0. .00 PROC

ATOM 4096 HH TYR X 597 17 .865 -17 .936 29. .268 0. .00 0. .00 PROC

ATOM 4097 CD2 TYR X 597 20 .809 -16 .662 26. .392 0. .00 0. .00 PROC

ATOM 4098 HD2 TYR X 597 21 .118 -16 .472 25. .375 0. .00 0. .00 PROC

ATOM 4099 CE2 TYR X 597 19 .798 -17 .486 26. .758 0. .00 0. .00 PROC

ATOM 4100 HE2 TYR X 597 19 .167 -17 .898 25. .984 0. .00 0. .00 PROC

ATOM 4101 C TYR X 597 21 .704 -13 .065 27. .110 0. .00 0. .00 PROC

ATOM 4102 O TYR X 597 20 .478 -13 .298 27. .384 0. .00 0. .00 PROC

ATOM 4103 N ASN X 598 22 .387 -11 .954 27. .518 0. .00 0. .00 PROC

ATOM 4104 HN ASN X 598 23 .287 -11 .788 27. .123 0. .00 0. .00 PROC

ATOM 4105 CA ASN X 598 21 .771 -11 .083 28. .515 0. .00 0. .00 PROC

ATOM 4106 HA ASN X 598 20 .876 -11 .465 28. .983 0. .00 0. .00 PROC

ATOM 4107 CB ASN X 598 22 .757 -10 .851 29. .669 0. .00 0. .00 PROC

ATOM 4108 HB1 ASN X 598 23 .691 -10 .483 29. .194 0. .00 0. .00 PROC

ATOM 4109 HB2 ASN X 598 22 .439 -10 .132 30. .453 0. .00 0. .00 PROC

ATOM 4110 CG ASN X 598 23 .297 -12 .124 30. .411 0. .00 0. .00 PROC

ATOM 4111 OD1 ASN X 598 24 .423 -12 .463 30. .193 0. .00 0. .00 PROC

ATOM 4112 ND2 ASN X 598 22 .418 -12 .793 31. .224 0. .00 0. .00 PROC

ATOM 4113 HD21 ASN X 598 22 .643 -13 .696 31. .591 0. .00 0. .00 PROC

ATOM 4114 HD22 ASN X 598 21 .441 -12 .592 31. .290 0. .00 0. .00 PROC

ATOM 4115 C ASN X 598 21 .308 -9 .745 27. .851 0. .00 0. .00 PROC

ATOM 4116 O ASN X 598 20 .657 -8 .998 28. .500 0. .00 0. .00 PROC

ATOM 4117 N SER X 599 21 .449 -9 .615 26. .520 0. .00 0. .00 PROC

ATOM 4118 HN SER X 599 21 .863 -10 .394 26. .055 0. .00 0. .00 PROC

ATOM 4119 CA SER X 599 21 .025 -8 .421 25. .847 0. .00 0. .00 PROC

ATOM 4120 HA SER X 599 20 .309 -7 .820 26. .387 0. .00 0. .00 PROC

ATOM 4121 CB SER X 599 22 .215 -7 .403 25. .775 0. .00 0. .00 PROC

ATOM 4122 HB1 SER X 599 21 .868 -6 .580 25. .116 0. .00 0. .00 PROC

ATOM 4123 HB2 SER X 599 22 .427 -6 .995 26. .787 0. .00 0. .00 PROC

ATOM 4124 OG SER X 599 23 .406 -7 .953 25. .155 0. .00 0. .00 PROC

ATOM 4125 HG1 SER X 599 23 .928 -8 .460 25. .782 0. .00 0. .00 PROC

ATOM 4126 C SER X 599 20 .398 -8 .621 24. .521 0. .00 0. .00 PROC

ATOM 4127 O SER X 599 19 .896 -7 .660 23. .926 0. .00 0. .00 PROC

ATOM 4128 N SER X 600 20 .529 -9 .767 23. .871 0. .00 0. .00 PROC

ATOM 4129 HN SER X 600 20 .993 -10 .588 24. .193 0. .00 0. .00 PROC

ATOM 4130 CA SER X 600 20 .029 -9 .958 22. .555 0. .00 0. .00 PROC

ATOM 4131 HA SER X 600 20 .508 -9 .174 21. .987 0. .00 0. .00 PROC

ATOM 4132 CB SER X 600 20 .410 -11 .342 22. .020 0. .00 0. .00 PROC

ATOM 4133 HB1 SER X 600 20 .395 -12 .139 22. .793 0. .00 0. .00 PROC

ATOM 4134 HB2 SER X 600 19 .931 -11 .651 21. .067 0. .00 0. .00 PROC

ATOM 4135 OG SER X 600 21 .742 -11 .270 21. .592 0. .00 0. .00 PROC

ATOM 4136 HG1 SER X 600 22 .093 -12 .163 21. .606 0. .00 0. .00 PROC

ATOM 4137 C SER X 600 18 .547 -9 .894 22. .428 0. .00 0. .00 PROC

ATOM 4138 O SER X 600 18 .030 -9 .170 21. .611 0. .00 0. .00 PROC

ATOM 4139 N GLY X 601 17 .707 -10 .682 23. .254 0. .00 0. .00 PROC

ATOM 4140 HN GLY X 601 18 .134 -11 .269 23. .937 0. .00 0. .00 PROC

ATOM 4141 CA GLY X 601 16 .210 -10 .568 23. .240 0. .00 0. .00 PROC

ATOM 4142 HA1 GLY X 601 15 .673 -11 .186 22. .536 0. .00 0. .00 PROC

ATOM 4143 HA2 GLY X 601 16 .077 -9 .516 23. .034 0. .00 0. .00 PROC

ATOM 4144 C GLY X 601 15 .638 -10 .890 24. .634 0. .00 0. .00 PROC

ATOM 4145 O GLY X 601 15 .896 -10 .175 25. .608 0. .00 0. .00 PROC

ATOM 4146 N LEU X 602 15 .079 -12 .079 24. .741 0. .00 0. .00 PROC

ATOM 4147 HN LEU X 602 14 .907 -12 .636 23. .932 0. .00 0. .00 PROC

ATOM 4148 CA LEU X 602 14 .521 -12 .729 25. .908 0. .00 0. .00 PROC

ATOM 4149 HA LEU X 602 14 .511 -11 .967 26. .672 0. .00 0. .00 PROC

ATOM 4150 CB LEU X 602 13 .041 -13 .247 25. .644 0. .00 0. .00 PROC

ATOM 4151 HB1 LEU X 602 13 .068 -14 .024 24. .850 0. .00 0. .00 PROC

ATOM 4152 HB2 LEU X 602 12 .635 -13 .775 26. .533 0. .00 0. .00 PROC

ATOM 4153 CG LEU X 602 11 .898 -12 .192 25. .477 0. .00 0. .00 PROC

ATOM 4154 HG LEU X 602 12 .108 -11 .877 24. .433 0. .00 0. .00 PROC

ATOM 4155 CD1 LEU X 602 10 .482 -12 .835 25. .460 0. .00 0. .00 PROC

ATOM 4156 HD11 LEU X 602 10 .345 -13 .765 24. .869 0. .00 0. .00 PROC

ATOM 4157 HD12 LEU X 602 10 .277 -13 .183 26. .495 0. .00 0. .00 PROC ATOM 4158 HD13 LEU X 602 9.741 -12.053 25..189 0..00 0..00 PROC

ATOM 4159 CD2 LEU X 602 11 .952 -10 .966 26. .403 0. .00 0. .00 PROC

ATOM 4160 HD21 LEU X 602 12 .977 -10 .539 26. .385 0. .00 0. .00 PROC

ATOM 4161 HD22 LEU X 602 11 .184 -10 .196 26. .177 0. .00 0. .00 PROC

ATOM 4162 HD23 LEU X 602 11 .623 -11 .291 27. .413 0. .00 0. .00 PROC

ATOM 4163 C LEU X 602 15 .392 -13 .786 26. .375 0. .00 0. .00 PROC

ATOM 4164 O LEU X 602 15 .968 -14 .616 25. .618 0. .00 0. .00 PROC

ATOM 4165 N GLY X 603 15 .573 -13 .906 27. .693 0. .00 0. .00 PROC

ATOM 4166 HN GLY X 603 15 .120 -13 .326 28. .365 0. .00 0. .00 PROC

ATOM 4167 CA GLY X 603 16 .301 -15 .056 28. .240 0. .00 0. .00 PROC

ATOM 4168 HA1 GLY X 603 17 .005 -14 .694 28. .975 0. .00 0. .00 PROC

ATOM 4169 HA2 GLY X 603 16 .968 -15 .550 27. .550 0. .00 0. .00 PROC

ATOM 4170 C GLY X 603 15 .486 -16 .096 28. .912 0. .00 0. .00 PROC

ATOM 4171 O GLY X 603 15 .826 -17 .227 28. .866 0. .00 0. .00 PROC

ATOM 4172 N GLY X 604 14 .321 -15 .671 29. .482 0. .00 0. .00 PROC

ATOM 4173 HN GLY X 604 14 .065 -14 .708 29. .462 0. .00 0. .00 PROC

ATOM 4174 CA GLY X 604 13 .217 -16 .551 29. .861 0. .00 0. .00 PROC

ATOM 4175 HA1 GLY X 604 12 .512 -15 .978 30. .444 0. .00 0. .00 PROC

ATOM 4176 HA2 GLY X 604 13 .625 -17 .408 30. .375 0. .00 0. .00 PROC

ATOM 4177 C GLY X 604 12 .401 -16 .931 28. .679 0. .00 0. .00 PROC

ATOM 4178 O GLY X 604 12 .741 -16 .540 27. .555 0. .00 0. .00 PROC

ATOM 4179 N PRO X 605 11 .290 -17 .664 28. .845 0. .00 0. .00 PROC

ATOM 4180 CD PRO X 605 11 .106 -18 .545 30. .050 0. .00 0. .00 PROC

ATOM 4181 HD1 PRO X 605 12 .055 -19 .024 30. .371 0. .00 0. .00 PROC

ATOM 4182 HD2 PRO X 605 10 .719 -18 .002 30. .939 0. .00 0. .00 PROC

ATOM 4183 CA PRO X 605 10 .389 -18 .074 27. .704 0. .00 0. .00 PROC

ATOM 4184 HA PRO X 605 10 .904 -18 .670 26. .965 0. .00 0. .00 PROC

ATOM 4185 CB PRO X 605 9. .461 -18 .973 28. .505 0. .00 0. .00 PROC

ATOM 4186 HB1 PRO X 605 8 .971 -19 .755 27. .887 0. .00 0. .00 PROC

ATOM 4187 HB2 PRO X 605 8 .599 -18 .438 28. .959 0. .00 0. .00 PROC

ATOM 4188 CG PRO X 605 10 .204 -19 .689 29. .625 0. .00 0. .00 PROC

ATOM 4189 HG1 PRO X 605 10 .706 -20 .563 29. .157 0. .00 0. .00 PROC

ATOM 4190 HG2 PRO X 605 9 .536 -19 .904 30. .486 0. .00 0. .00 PROC

ATOM 4191 C PRO X 605 9. .678 -16 .955 26. .937 0. .00 0. .00 PROC

ATOM 4192 O PRO X 605 9. .658 -15 .809 27. .358 0. .00 0. .00 PROC

ATOM 4193 N SER X 606 9. .237 -17 .305 25. .741 0. .00 0. .00 PROC

ATOM 4194 HN SER X 606 9. .212 -18 .273 25. .503 0. .00 0. .00 PROC

ATOM 4195 CA SER X 606 8. .848 -16 .357 24. .719 0. .00 0. .00 PROC

ATOM 4196 HA SER X 606 8. .530 -15 .476 25. .257 0. .00 0. .00 PROC

ATOM 4197 CB SER X 606 9. .896 -16 .179 23. .564 0. .00 0. .00 PROC

ATOM 4198 HB1 SER X 606 10 .940 -16 .067 23. .925 0. .00 0. .00 PROC

ATOM 4199 HB2 SER X 606 9 .985 -17 .150 23. .033 0. .00 0. .00 PROC

ATOM 4200 OG SER X 606 9. .573 -15 .129 22. .672 0. .00 0. .00 PROC

ATOM 4201 HG1 SER X 606 10 .329 -15 .099 22. .081 0. .00 0. .00 PROC

ATOM 4202 C SER X 606 7. .516 -16 .862 24. .127 0. .00 0. .00 PROC

ATOM 4203 O SER X 606 7. .291 -18 .025 24. .155 0. .00 0. .00 PROC

ATOM 4204 N ILE X 607 6. .747 -16 .013 23. .526 0. .00 0. .00 PROC

ATOM 4205 HN ILE X 607 7. .075 -15 .072 23. .565 0. .00 0. .00 PROC

ATOM 4206 CA ILE X 607 5. .398 -16 .336 23. .016 0. .00 0. .00 PROC

ATOM 4207 HA ILE X 607 4. .904 -17 .097 23. .602 0. .00 0. .00 PROC

ATOM 4208 CB ILE X 607 4. .475 -15 .092 23. .156 0. .00 0. .00 PROC

ATOM 4209 HB ILE X 607 4. .592 -14 .773 24. .214 0. .00 0. .00 PROC

ATOM 4210 CG2 ILE X 607 4 .895 -13 .977 22. .251 0. .00 0. .00 PROC

ATOM 4211 HG21 ILE X 607 5 .882 -13 .545 22. .521 0. .00 0. .00 PROC

ATOM 4212 HG22 ILE X 607 4 .762 -14 .179 21. .167 0. .00 0. .00 PROC

ATOM 4213 HG23 ILE X 607 4 .187 -13 .133 22. .397 0. .00 0. .00 PROC

ATOM 4214 CGI ILE X 607 3 .006 -15 .418 22. .957 0. .00 0. .00 PROC

ATOM 4215 HG11 ILE X 607 2 .798 -15 .600 21. .881 0. .00 0. .00 PROC

ATOM 4216 HG12 ILE X 607 2 .808 -16 .387 23. .463 0. .00 0. .00 PROC

ATOM 4217 CD ILE X 607 2. .166 -14 .330 23. .554 0. .00 0. .00 PROC

ATOM 4218 HD1 ILE X 607 2 .220 -13 .352 23. .030 0. .00 0. .00 PROC

ATOM 4219 HD2 ILE X 607 1 .118 -14 .540 23. .250 0. .00 0. .00 PROC

ATOM 4220 HD3 ILE X 607 2 .204 -14 .211 24. .658 0. .00 0. .00 PROC

ATOM 4221 C ILE X 607 5. .473 -16 .816 21. .588 0. .00 0. .00 PROC

ATOM 4222 O ILE X 607 4. .538 -17 .387 20. .999 0. .00 0. .00 PROC

ATOM 4223 N LYS X 608 6. .592 -16 .551 20. .926 0. .00 0. .00 PROC ATOM 4224 HN LYS X 608 7..452 -16.230 21..316 0..00 0..00 PROC

ATOM 4225 CA LYS X 608 6. .714 -16 .658 19. .471 0. .00 0. .00 PROC

ATOM 4226 HA LYS X 608 5. .750 -16 .450 19. .032 0. .00 0. .00 PROC

ATOM 4227 CB LYS X 608 7. .897 -15 .761 19. .098 0. .00 0. .00 PROC

ATOM 4228 HB1 LYS X 608 7 .852 -14 .824 19. .693 0. .00 0. .00 PROC

ATOM 4229 HB2 LYS X 608 8 .765 -16 .344 19. .474 0. .00 0. .00 PROC

ATOM 4230 CG LYS X 608 8. .008 -15 .401 17. .613 0. .00 0. .00 PROC

ATOM 4231 HG1 LYS X 608 8 .961 -14 .857 17. .443 0. .00 0. .00 PROC

ATOM 4232 HG2 LYS X 608 8 .226 -16 .326 17. .037 0. .00 0. .00 PROC

ATOM 4233 CD LYS X 608 6. .790 -14 .566 16. .957 0. .00 0. .00 PROC

ATOM 4234 HD1 LYS X 608 6 .968 -14 .598 15. .861 0. .00 0. .00 PROC

ATOM 4235 HD2 LYS X 608 5 .864 -15 .080 17. .293 0. .00 0. .00 PROC

ATOM 4236 CE LYS X 608 6. .604 -13 .204 17. .538 0. .00 0. .00 PROC

ATOM 4237 HE1 LYS X 608 6 .129 -12 .558 16. .768 0. .00 0. .00 PROC

ATOM 4238 HE2 LYS X 608 6 .083 -13 .182 18. .519 0. .00 0. .00 PROC

ATOM 4239 NZ LYS X 608 7. .933 -12 .537 17. .756 0. .00 0. .00 PROC

ATOM 4240 HZ1 LYS X 608 8 .212 -12 .696 18. .745 0. .00 0. .00 PROC

ATOM 4241 HZ2 LYS X 608 8 .562 -13 .008 17. .075 0. .00 0. .00 PROC

ATOM 4242 HZ3 LYS X 608 8 .046 -11 .507 17. .660 0. .00 0. .00 PROC

ATOM 4243 C LYS X 608 6. .998 -18 .076 19. .032 0. .00 0. .00 PROC

ATOM 4244 O LYS X 608 6. .996 -18 .349 17. .830 0. .00 0. .00 PROC

ATOM 4245 N ASP X 609 7. .384 -18 .990 19. .942 0. .00 0. .00 PROC

ATOM 4246 HN ASP X 609 7. .579 -18 .746 20. .889 0. .00 0. .00 PROC

ATOM 4247 CA ASP X 609 7. .618 -20 .363 19. .771 0. .00 0. .00 PROC

ATOM 4248 HA ASP X 609 8. .079 -20 .480 18. .802 0. .00 0. .00 PROC

ATOM 4249 CB ASP X 609 8. .591 -20 .983 20. .833 0. .00 0. .00 PROC

ATOM 4250 HB1 ASP X 609 9 .161 -21 .892 20. .546 0. .00 0. .00 PROC

ATOM 4251 HB2 ASP X 609 9 .357 -20 .185 20. .936 0. .00 0. .00 PROC

ATOM 4252 CG ASP X 609 8. .061 -21 .247 22. .217 0. .00 0. .00 PROC

ATOM 4253 OD1 ASP X 609 6 .834 -20 .925 22. .503 0. .00 0. .00 PROC

ATOM 4254 OD2 ASP X 609 8 .789 -21 .839 23. .080 0. .00 0. .00 PROC

ATOM 4255 C ASP X 609 6. .318 -21 . Ill 19. .640 0. .00 0. .00 PROC

ATOM 4256 O ASP X 609 6. .181 -22 .206 19. .105 0. .00 0. .00 PROC

ATOM 4257 N LYS X 610 5. .149 -20 .468 19. .912 0. .00 0. .00 PROC

ATOM 4258 HN LYS X 610 5. .164 -19 .575 20. .354 0. .00 0. .00 PROC

ATOM 4259 CA LYS X 610 3. .921 -20 .943 19. .443 0. .00 0. .00 PROC

ATOM 4260 HA LYS X 610 3. .957 -22 .010 19. .608 0. .00 0. .00 PROC

ATOM 4261 CB LYS X 610 2. .727 -20 .349 20. .287 0. .00 0. .00 PROC

ATOM 4262 HB1 LYS X 610 2 .682 -19 .243 20. .188 0. .00 0. .00 PROC

ATOM 4263 HB2 LYS X 610 1 .809 -20 .838 19. .896 0. .00 0. .00 PROC

ATOM 4264 CG LYS X 610 2. .706 -20 .828 21. .736 0. .00 0. .00 PROC

ATOM 4265 HG1 LYS X 610 1 .669 -21 .121 22. .008 0. .00 0. .00 PROC

ATOM 4266 HG2 LYS X 610 3 .314 -21 .758 21. .725 0. .00 0. .00 PROC

ATOM 4267 CD LYS X 610 3. .415 -19 .943 22. .820 0. .00 0. .00 PROC

ATOM 4268 HD1 LYS X 610 4 .376 -19 .506 22. .474 0. .00 0. .00 PROC

ATOM 4269 HD2 LYS X 610 2 .746 -19 .079 23. .022 0. .00 0. .00 PROC

ATOM 4270 CE LYS X 610 3. .592 -20 .620 24. .115 0. .00 0. .00 PROC

ATOM 4271 HE1 LYS X 610 3 .696 -19 .812 24. .871 0. .00 0. .00 PROC

ATOM 4272 HE2 LYS X 610 2 .716 -21 .239 24. .406 0. .00 0. .00 PROC

ATOM 4273 NZ LYS X 610 4. .794 -21 .417 24. .121 0. .00 0. .00 PROC

ATOM 4274 HZ1 LYS X 610 5 .514 -21 .106 23. .437 0. .00 0. .00 PROC

ATOM 4275 HZ2 LYS X 610 5 .149 -21 .431 25. .099 0. .00 0. .00 PROC

ATOM 4276 HZ3 LYS X 610 4 .636 -22 .385 23. .776 0. .00 0. .00 PROC

ATOM 4277 C LYS X 610 3. .489 -20 .632 18. .018 0. .00 0. .00 PROC

ATOM 4278 O LYS X 610 3. .546 -19 .487 17. .535 0. .00 0. .00 PROC

ATOM 4279 N TYR X 611 2. .945 -21 .673 17. .360 0. .00 0. .00 PROC

ATOM 4280 HN TYR X 611 2. .770 -22 .577 17. .742 0. .00 0. .00 PROC

ATOM 4281 CA TYR X 611 2. .649 -21 .541 15. .947 0. .00 0. .00 PROC

ATOM 4282 HA TYR X 611 3. .549 -21 .126 15. .519 0. .00 0. .00 PROC

ATOM 4283 CB TYR X 611 2. .350 -22 .950 15. .278 0. .00 0. .00 PROC

ATOM 4284 HB1 TYR X 611 3 .327 -23 .454 15. .115 0. .00 0. .00 PROC

ATOM 4285 HB2 TYR X 611 1 .710 -23 .484 16. .013 0. .00 0. .00 PROC

ATOM 4286 CG TYR X 611 1. .498 -22 .979 14. .053 0. .00 0. .00 PROC

ATOM 4287 CD1 TYR X 611 0 .219 -23 .422 14. .087 0. .00 0. .00 PROC

ATOM 4288 HD1 TYR X 611 -0 .009 -23 .959 14. .996 0. .00 0. .00 PROC

ATOM 4289 CE1 TYR X 611 -0 .557 -23 .625 12. .910 0. .00 0. .00 PROC ATOM 4290 HE1 TYR X 611 -1.492 -24.132 13..097 0..00 0..00 PROC

ATOM 4291 CZ TYR X 611 -0 .072 -23 .166 11. .684 0. .00 0. .00 PROC

ATOM 4292 OH TYR X 611 -0 .851 -23 .474 10. .561 0. .00 0. .00 PROC

ATOM 4293 HH TYR X 611 -1 .765 -23 .561 10. .842 0. .00 0. .00 PROC

ATOM 4294 CD2 TYR X 611 1 .985 -22 .599 12. .802 0. .00 0. .00 PROC

ATOM 4295 HD2 TYR X 611 2 .987 -22 .223 12. .656 0. .00 0. .00 PROC

ATOM 4296 CE2 TYR X 611 1 .264 -22 .781 11. .628 0. .00 0. .00 PROC

ATOM 4297 HE2 TYR X 611 1 .828 -22 .611 10. .722 0. .00 0. .00 PROC

ATOM 4298 C TYR X 611 1. .541 -20 .492 15. .611 0. .00 0. .00 PROC

ATOM 4299 O TYR X 611 1. .711 -19 .800 14. .601 0. .00 0. .00 PROC

ATOM 4300 N VAL X 612 0. .515 -20 .377 16. .335 0. .00 0. .00 PROC

ATOM 4301 HN VAL X 612 0. .418 -21 .178 16. .921 0. .00 0. .00 PROC

ATOM 4302 CA VAL X 612 -0 .530 -19 .449 16. .229 0. .00 0. .00 PROC

ATOM 4303 HA VAL X 612 -0 .958 -19 .541 15. .242 0. .00 0. .00 PROC

ATOM 4304 CB VAL X 612 -1 .702 -19 .688 17. .103 0. .00 0. .00 PROC

ATOM 4305 HB VAL X 612 -2 .354 -18 .792 17. .028 0. .00 0. .00 PROC

ATOM 4306 CGI VAL X 612 -2 .493 -20 .931 16. .783 0. .00 0. .00 PROC

ATOM 4307 HG11 VAL X 612 -1 .963 -21 .885 16. .993 0. .00 0. .00 PROC

ATOM 4308 HG12 VAL X 612 -3 .280 -20 .944 17. .567 0. .00 0. .00 PROC

ATOM 4309 HG13 VAL X 612 -2 .986 -20 .918 15. .788 0. .00 0. .00 PROC

ATOM 4310 CG2 VAL X 612 -1 .205 -19 .631 18. .591 0. .00 0. .00 PROC

ATOM 4311 HG21 VAL X 612 -1 .015 -18 .583 18. .908 0. .00 0. .00 PROC

ATOM 4312 HG22 VAL X 612 -1 .915 -20 .033 19. .344 0. .00 0. .00 PROC

ATOM 4313 HG23 VAL X 612 -0 .220 -20 .117 18. .758 0. .00 0. .00 PROC

ATOM 4314 C VAL X 612 -0 .033 -17 .991 16. .417 0. .00 0. .00 PROC

ATOM 4315 O VAL X 612 -0 .469 -17 .123 15. .684 0. .00 0. .00 PROC

ATOM 4316 N THR X 613 0. .942 -17 .742 17. .309 0. .00 0. .00 PROC

ATOM 4317 HN THR X 613 1. .253 -18 .471 17. .914 0. .00 0. .00 PROC

ATOM 4318 CA THR X 613 1. .592 -16 .456 17. .425 0. .00 0. .00 PROC

ATOM 4319 HA THR X 613 0. .856 -15 .671 17. .336 0. .00 0. .00 PROC

ATOM 4320 CB THR X 613 2. .495 -16 .274 18. .620 0. .00 0. .00 PROC

ATOM 4321 HB THR X 613 3. .408 -16 .903 18. .555 0. .00 0. .00 PROC

ATOM 4322 OG1 THR X 613 1 .897 -16 .761 19. .824 0. .00 0. .00 PROC

ATOM 4323 HG1 THR X 613 2 .710 -16 .917 20. .310 0. .00 0. .00 PROC

ATOM 4324 CG2 THR X 613 2 .744 -14 .789 18. .869 0. .00 0. .00 PROC

ATOM 4325 HG21 THR X 613 3 .342 -14 .404 18. .016 0. .00 0. .00 PROC

ATOM 4326 HG22 THR X 613 1 .815 -14 .184 18. .935 0. .00 0. .00 PROC

ATOM 4327 HG23 THR X 613 3 .371 -14 .604 19. .767 0. .00 0. .00 PROC

ATOM 4328 C THR X 613 2. .494 -16 .186 16. .253 0. .00 0. .00 PROC

ATOM 4329 O THR X 613 2. .510 -15 .094 15. .743 0. .00 0. .00 PROC

ATOM 4330 N ALA X 614 3. .279 -17 .210 15. .767 0. .00 0. .00 PROC

ATOM 4331 HN ALA X 614 3. .276 -18 .095 16. .227 0. .00 0. .00 PROC

ATOM 4332 CA ALA X 614 4. .123 -17 .144 14. .543 0. .00 0. .00 PROC

ATOM 4333 HA ALA X 614 4. .779 -16 .286 14. .564 0. .00 0. .00 PROC

ATOM 4334 CB ALA X 614 5. .148 -18 .329 14. .414 0. .00 0. .00 PROC

ATOM 4335 HB1 ALA X 614 5 .679 -18 .612 15. .348 0. .00 0. .00 PROC

ATOM 4336 HB2 ALA X 614 4 .547 -19 .221 14. .135 0. .00 0. .00 PROC

ATOM 4337 HB3 ALA X 614 5 .991 -18 .183 13. .705 0. .00 0. .00 PROC

ATOM 4338 C ALA X 614 3. .249 -16 .897 13. .311 0. .00 0. .00 PROC

ATOM 4339 O ALA X 614 3. .557 -16 .046 12. .448 0. .00 0. .00 PROC

ATOM 4340 N LEU X 615 2. .107 -17 .612 13. .042 0. .00 0. .00 PROC

ATOM 4341 HN LEU X 615 1. .998 -18 .422 13. .612 0. .00 0. .00 PROC

ATOM 4342 CA LEU X 615 1. .117 -17 .224 12. .092 0. .00 0. .00 PROC

ATOM 4343 HA LEU X 615 1. .548 -17 .303 11. .104 0. .00 0. .00 PROC

ATOM 4344 CB LEU X 615 -0 .108 -18 .151 12. .219 0. .00 0. .00 PROC

ATOM 4345 HB1 LEU X 615 0 .257 -19 .200 12. .190 0. .00 0. .00 PROC

ATOM 4346 HB2 LEU X 615 -0 .667 -17 .964 13. .160 0. .00 0. .00 PROC

ATOM 4347 CG LEU X 615 -1 .069 -18 .174 11. .008 0. .00 0. .00 PROC

ATOM 4348 HG LEU X 615 -1 .337 -17 .171 10. .614 0. .00 0. .00 PROC

ATOM 4349 CD1 LEU X 615 -0 .388 -19 .000 9. .894 0. .00 0. .00 PROC

ATOM 4350 HD11 LEU X 615 0 .011 -19 .980 10. .233 0. .00 0. .00 PROC

ATOM 4351 HD12 LEU X 615 -0 .901 -19 .226 8. .935 0. .00 0. .00 PROC

ATOM 4352 HD13 LEU X 615 0 .464 -18 .353 9. .593 0. .00 0. .00 PROC

ATOM 4353 CD2 LEU X 615 -2 .352 -18 .838 11. .344 0. .00 0. .00 PROC

ATOM 4354 HD21 LEU X 615 -2 .959 -18 .003 11. .756 0. .00 0. .00 PROC

ATOM 4355 HD22 LEU X 615 -2 .834 -19 .131 10. .387 0. .00 0. .00 PROC ATOM 4356 HD23 LEU X 615 -2.319 -19.773 11..943 0..00 0..00 PROC

ATOM 4357 C LEU X 615 0. .510 -15 .825 12. .226 0. .00 0. .00 PROC

ATOM 4358 O LEU X 615 0. .255 -15 .208 11. .192 0. .00 0. .00 PROC

ATOM 4359 N TYR X 616 0. .174 -15 .410 13. .449 0. .00 0. .00 PROC

ATOM 4360 HN TYR X 616 0. .118 -15 .995 14. .254 0. .00 0. .00 PROC

ATOM 4361 CA TYR X 616 -0 .434 -14 . Ill 13. .674 0. .00 0. .00 PROC

ATOM 4362 HA TYR X 616 -1 .244 -14 .095 12. .960 0. .00 0. .00 PROC

ATOM 4363 CB TYR X 616 -0 .939 -13 .987 15. .119 0. .00 0. .00 PROC

ATOM 4364 HB1 TYR X 616 -1 .384 -14 .952 15. .445 0. .00 0. .00 PROC

ATOM 4365 HB2 TYR X 616 -0 .045 -13 .891 15. .772 0. .00 0. .00 PROC

ATOM 4366 CG TYR X 616 -1 .970 -13 .075 15. .432 0. .00 0. .00 PROC

ATOM 4367 CD1 TYR X 616 -3 .232 -13 .148 14. .787 0. .00 0. .00 PROC

ATOM 4368 HD1 TYR X 616 -3 .267 -13 .837 13. .956 0. .00 0. .00 PROC

ATOM 4369 CE1 TYR X 616 -4 .264 -12 .325 15. .210 0. .00 0. .00 PROC

ATOM 4370 HE1 TYR X 616 -5 .226 -12 .178 14. .741 0. .00 0. .00 PROC

ATOM 4371 CZ TYR X 616 -4 .065 -11 .464 16. .278 0. .00 0. .00 PROC

ATOM 4372 OH TYR X 616 -5 .025 -10 .528 16. .545 0. .00 0. .00 PROC

ATOM 4373 HH TYR X 616 -4 .942 -10 .323 17. .480 0. .00 0. .00 PROC

ATOM 4374 CD2 TYR X 616 -1 .836 -12 .149 16. .469 0. .00 0. .00 PROC

ATOM 4375 HD2 TYR X 616 -0 .898 -12 .093 17. .002 0. .00 0. .00 PROC

ATOM 4376 CE2 TYR X 616 -2 .782 -11 .246 16. .782 0. .00 0. .00 PROC

ATOM 4377 HE2 TYR X 616 -2 .586 -10 .416 17. .444 0. .00 0. .00 PROC

ATOM 4378 C TYR X 616 0. .514 -12 .959 13. .307 0. .00 0. .00 PROC

ATOM 4379 O TYR X 616 0. .156 -12 .009 12. .557 0. .00 0. .00 PROC

ATOM 4380 N PHE X 617 1. .764 -13 .095 13. .753 0. .00 0. .00 PROC

ATOM 4381 HN PHE X 617 2. .164 -13 .832 14. .293 0. .00 0. .00 PROC

ATOM 4382 CA PHE X 617 2. .821 -12 .198 13. .324 0. .00 0. .00 PROC

ATOM 4383 HA PHE X 617 2. .447 -11 .207 13. .533 0. .00 0. .00 PROC

ATOM 4384 CB PHE X 617 4. .082 -12 .396 14. .225 0. .00 0. .00 PROC

ATOM 4385 HB1 PHE X 617 3 .809 -12 .066 15. .250 0. .00 0. .00 PROC

ATOM 4386 HB2 PHE X 617 4 .301 -13 .483 14. .298 0. .00 0. .00 PROC

ATOM 4387 CG PHE X 617 5. .295 -11 .570 13. .882 0. .00 0. .00 PROC

ATOM 4388 CD1 PHE X 617 5 .256 -10 .163 13. .865 0. .00 0. .00 PROC

ATOM 4389 HD1 PHE X 617 4 .368 -9 .638 14. .185 0. .00 0. .00 PROC

ATOM 4390 CE1 PHE X 617 6 .474 -9 .462 13. .549 0. .00 0. .00 PROC

ATOM 4391 HE1 PHE X 617 6 .369 -8 .387 13. .535 0. .00 0. .00 PROC

ATOM 4392 CZ PHE X 617 7. .674 -10 .163 13. .232 0. .00 0. .00 PROC

ATOM 4393 HZ PHE X 617 8. .572 -9 .649 12. .924 0. .00 0. .00 PROC

ATOM 4394 CD2 PHE X 617 6 .457 -12 .239 13. .587 0. .00 0. .00 PROC

ATOM 4395 HD2 PHE X 617 6 .293 -13 .299 13. .713 0. .00 0. .00 PROC

ATOM 4396 CE2 PHE X 617 7 .629 -11 .551 13. .183 0. .00 0. .00 PROC

ATOM 4397 HE2 PHE X 617 8 .499 -12 .135 12. .920 0. .00 0. .00 PROC

ATOM 4398 C PHE X 617 3. .140 -12 .224 11. .775 0. .00 0. .00 PROC

ATOM 4399 O PHE X 617 3. .281 -11 .095 11. .182 0. .00 0. .00 PROC

ATOM 4400 N THR X 618 3. .162 -13 .413 11. .112 0. .00 0. .00 PROC

ATOM 4401 HN THR X 618 3. .109 -14 .294 11. .575 0. .00 0. .00 PROC

ATOM 4402 CA THR X 618 3. .181 -13 .521 9. .682 0. .00 0. .00 PROC

ATOM 4403 HA THR X 618 4. .133 -13 .114 9. .376 0. .00 0. .00 PROC

ATOM 4404 CB THR X 618 3. .132 -14 .966 9. .262 0. .00 0. .00 PROC

ATOM 4405 HB THR X 618 2. .137 -15 .398 9. .503 0. .00 0. .00 PROC

ATOM 4406 OG1 THR X 618 4 .164 -15 .676 9. .839 0. .00 0. .00 PROC

ATOM 4407 HG1 THR X 618 3 .875 -15 .823 10. .742 0. .00 0. .00 PROC

ATOM 4408 CG2 THR X 618 3 .363 -15 .145 7. .697 0. .00 0. .00 PROC

ATOM 4409 HG21 THR X 618 3 .254 -16 .187 7. .324 0. .00 0. .00 PROC

ATOM 4410 HG22 THR X 618 2 .663 -14 .519 7. .104 0. .00 0. .00 PROC

ATOM 4411 HG23 THR X 618 4 .376 -14 .736 7. .495 0. .00 0. .00 PROC

ATOM 4412 C THR X 618 2. .090 -12 .796 8. .874 0. .00 0. .00 PROC

ATOM 4413 O THR X 618 2. .385 -11 .983 8. .027 0. .00 0. .00 PROC

ATOM 4414 N PHE X 619 0. .761 -12 .985 9. .244 0. .00 0. .00 PROC

ATOM 4415 HN PHE X 619 0. .560 -13 .608 9. .996 0. .00 0. .00 PROC

ATOM 4416 CA PHE X 619 -0 .322 -12 .266 8. .734 0. .00 0. .00 PROC

ATOM 4417 HA PHE X 619 -0 .275 -12 .281 7. .655 0. .00 0. .00 PROC

ATOM 4418 CB PHE X 619 -1 .732 -12 .699 9. .205 0. .00 0. .00 PROC

ATOM 4419 HB1 PHE X 619 -1 .533 -12 .982 10. .261 0. .00 0. .00 PROC

ATOM 4420 HB2 PHE X 619 -2 .542 -11 .941 9. .153 0. .00 0. .00 PROC

ATOM 4421 CG PHE X 619 -2 .218 -13 .841 8. .353 0. .00 0. .00 PROC ATOM 4422 CD1 PHE X 619 -2.103 -15.212 8..754 0..00 0..00 PROC

ATOM 4423 HD1 PHE X 619 -1 .519 -15 .406 9. .642 0. .00 0. .00 PROC

ATOM 4424 CE1 PHE X 619 -2 .595 -16 .184 7. .891 0. .00 0. .00 PROC

ATOM 4425 HE1 PHE X 619 -2 .227 -17 .199 7. .916 0. .00 0. .00 PROC

ATOM 4426 CZ PHE X 619 -3 .166 -15 .885 6. .668 0. .00 0. .00 PROC

ATOM 4427 HZ PHE X 619 -3 .568 -16 .595 5. .961 0. .00 0. .00 PROC

ATOM 4428 CD2 PHE X 619 -2 .857 -13 .537 7. .106 0. .00 0. .00 PROC

ATOM 4429 HD2 PHE X 619 -2 .836 -12 .520 6. .744 0. .00 0. .00 PROC

ATOM 4430 CE2 PHE X 619 -3 .359 -14 .507 6. .270 0. .00 0. .00 PROC

ATOM 4431 HE2 PHE X 619 -3 .785 -14 .181 5. .332 0. .00 0. .00 PROC

ATOM 4432 C PHE X 619 -0 .365 -10 .797 9. .029 0. .00 0. .00 PROC

ATOM 4433 O PHE X 619 -0 .696 -10 .010 8. .184 0. .00 0. .00 PROC

ATOM 4434 N SER X 620 0. .077 -10 .300 10. .254 0. .00 0. .00 PROC

ATOM 4435 HN SER X 620 0. .206 -10 .967 10. .985 0. .00 0. .00 PROC

ATOM 4436 CA SER X 620 0. .352 -8 .884 10. .621 0. .00 0. .00 PROC

ATOM 4437 HA SER X 620 -0 .602 -8 .382 10. .543 0. .00 0. .00 PROC

ATOM 4438 CB SER X 620 0. .827 -8 .766 12. .125 0. .00 0. .00 PROC

ATOM 4439 HB1 SER X 620 0 .033 -9 .228 12. .749 0. .00 0. .00 PROC

ATOM 4440 HB2 SER X 620 1 .794 -9 .269 12. .339 0. .00 0. .00 PROC

ATOM 4441 OG SER X 620 0. .814 -7 .385 12. .380 0. .00 0. .00 PROC

ATOM 4442 HG1 SER X 620 -0 .024 -7 .129 12. .773 0. .00 0. .00 PROC

ATOM 4443 C SER X 620 1. .446 -8 .212 9. .735 0. .00 0. .00 PROC

ATOM 4444 O SER X 620 1. .304 -7 .083 9. .266 0. .00 0. .00 PROC

ATOM 4445 N SER X 621 2. .574 -8 .967 9. .587 0. .00 0. .00 PROC

ATOM 4446 HN SER X 621 2. .547 -9 .898 9. .943 0. .00 0. .00 PROC

ATOM 4447 CA SER X 621 3. .734 -8 .547 8. .825 0. .00 0. .00 PROC

ATOM 4448 HA SER X 621 3. .680 -7 .490 9. .038 0. .00 0. .00 PROC

ATOM 4449 CB SER X 621 5. .042 -9 .063 9. .320 0. .00 0. .00 PROC

ATOM 4450 HB1 SER X 621 5 .948 -8 .519 8. .978 0. .00 0. .00 PROC

ATOM 4451 HB2 SER X 621 5 .022 -8 .896 10. .418 0. .00 0. .00 PROC

ATOM 4452 OG SER X 621 5. .162 -10 .476 9. .088 0. .00 0. .00 PROC

ATOM 4453 HG1 SER X 621 4 .622 -10 .841 9. .793 0. .00 0. .00 PROC

ATOM 4454 C SER X 621 3. .645 -8 .588 7. .275 0. .00 0. .00 PROC

ATOM 4455 O SER X 621 3. .944 -7 .604 6. .684 0. .00 0. .00 PROC

ATOM 4456 N LEU X 622 3. .197 -9 .675 6. .670 0. .00 0. .00 PROC

ATOM 4457 HN LEU X 622 2. .900 -10 .505 7. .135 0. .00 0. .00 PROC

ATOM 4458 CA LEU X 622 2. .971 -9 .828 5. .290 0. .00 0. .00 PROC

ATOM 4459 HA LEU X 622 3. .656 -9 .149 4. .804 0. .00 0. .00 PROC

ATOM 4460 CB LEU X 622 3. .301 -11 .258 4. .730 0. .00 0. .00 PROC

ATOM 4461 HB1 LEU X 622 2 .404 -11 .852 5. .008 0. .00 0. .00 PROC

ATOM 4462 HB2 LEU X 622 3 .417 -11 .147 3. .631 0. .00 0. .00 PROC

ATOM 4463 CG LEU X 622 4. .565 -11 .902 5. .150 0. .00 0. .00 PROC

ATOM 4464 HG LEU X 622 4. .442 -12 .038 6. .245 0. .00 0. .00 PROC

ATOM 4465 CD1 LEU X 622 4 .695 -13 .349 4. .540 0. .00 0. .00 PROC

ATOM 4466 HD11 LEU X 622 4 .471 -13 .342 3. .452 0. .00 0. .00 PROC

ATOM 4467 HD12 LEU X 622 5 .624 -13 .823 4. .922 0. .00 0. .00 PROC

ATOM 4468 HD13 LEU X 622 3 .885 -13 .965 4. .987 0. .00 0. .00 PROC

ATOM 4469 CD2 LEU X 622 5 .794 -10 .984 4. .749 0. .00 0. .00 PROC

ATOM 4470 HD21 LEU X 622 6 .694 -11 .596 4. .972 0. .00 0. .00 PROC

ATOM 4471 HD22 LEU X 622 5 .823 -10 .568 3. .720 0. .00 0. .00 PROC

ATOM 4472 HD23 LEU X 622 5 .626 -10 .056 5. .336 0. .00 0. .00 PROC

ATOM 4473 C LEU X 622 1. .615 -9 .256 4. .909 0. .00 0. .00 PROC

ATOM 4474 O LEU X 622 0. .587 -9 .690 5. .368 0. .00 0. .00 PROC

ATOM 4475 N THR X 623 1. .635 -8 .285 3. .973 0. .00 0. .00 PROC

ATOM 4476 HN THR X 623 2. .517 -8 .156 3. .527 0. .00 0. .00 PROC

ATOM 4477 CA THR X 623 0. .613 -7 .351 3. .479 0. .00 0. .00 PROC

ATOM 4478 HA THR X 623 0. .903 -7 .086 2. .473 0. .00 0. .00 PROC

ATOM 4479 CB THR X 623 -0 .766 -8 .038 3. .337 0. .00 0. .00 PROC

ATOM 4480 HB THR X 623 -1 .241 -7 .960 4. .338 0. .00 0. .00 PROC

ATOM 4481 OG1 THR X 623 -0 .765 -9 .358 2. .881 0. .00 0. .00 PROC

ATOM 4482 HG1 THR X 623 -0 .451 -9 .869 3. .631 0. .00 0. .00 PROC

ATOM 4483 CG2 THR X 623 -1 .585 -7 .299 2. .291 0. .00 0. .00 PROC

ATOM 4484 HG21 THR X 623 -2 .488 -7 .901 2. .052 0. .00 0. .00 PROC

ATOM 4485 HG22 THR X 623 -1 .879 -6 .267 2. .577 0. .00 0. .00 PROC

ATOM 4486 HG23 THR X 623 -0 .989 -7 .036 1. .391 0. .00 0. .00 PROC

ATOM 4487 C THR X 623 0. .489 -6 .055 4. .299 0. .00 0. .00 PROC ATOM 4488 O THR X 623 -0.309 -5.163 4..075 0..00 0..00 PROC

ATOM 4489 N SER X 624 1. .502 -5 .842 5. .170 0. .00 0. .00 PROC

ATOM 4490 HN SER X 624 2. .107 -6 .631 5. .252 0. .00 0. .00 PROC

ATOM 4491 CA SER X 624 1. .798 -4 .635 5. .847 0. .00 0. .00 PROC

ATOM 4492 HA SER X 624 2. .533 -4 .941 6. .575 0. .00 0. .00 PROC

ATOM 4493 CB SER X 624 2. .374 -3 .602 4. .891 0. .00 0. .00 PROC

ATOM 4494 HB1 SER X 624 1 .761 -3 .421 3. .983 0. .00 0. .00 PROC

ATOM 4495 HB2 SER X 624 2 .274 -2 .593 5. .345 0. .00 0. .00 PROC

ATOM 4496 OG SER X 624 3. .714 -3 .847 4. .472 0. .00 0. .00 PROC

ATOM 4497 HG1 SER X 624 4 .042 -3 .040 4. .068 0. .00 0. .00 PROC

ATOM 4498 C SER X 624 0. .687 -4 .124 6. .765 0. .00 0. .00 PROC

ATOM 4499 O SER X 624 0. .195 -3 .015 6. .711 0. .00 0. .00 PROC

ATOM 4500 N VAL X 625 0. .191 -5 .036 7. .561 0. .00 0. .00 PROC

ATOM 4501 HN VAL X 625 0. .661 -5 .901 7. .721 0. .00 0. .00 PROC

ATOM 4502 CA VAL X 625 -0 .953 -4 .756 8. .377 0. .00 0. .00 PROC

ATOM 4503 HA VAL X 625 -1 .543 -4 .008 7. .867 0. .00 0. .00 PROC

ATOM 4504 CB VAL X 625 -1 .946 -5 .894 8. .559 0. .00 0. .00 PROC

ATOM 4505 HB VAL X 625 -1 .385 -6 .619 9. .188 0. .00 0. .00 PROC

ATOM 4506 CGI VAL X 625 -3 .264 -5 .465 9. .132 0. .00 0. .00 PROC

ATOM 4507 HG11 VAL X 625 -3 .876 -4 .828 8. .458 0. .00 0. .00 PROC

ATOM 4508 HG12 VAL X 625 -3 .796 -6 .354 9. .534 0. .00 0. .00 PROC

ATOM 4509 HG13 VAL X 625 -3 .123 -5 .042 10. .149 0. .00 0. .00 PROC

ATOM 4510 CG2 VAL X 625 -2 .147 -6 .744 7. .268 0. .00 0. .00 PROC

ATOM 4511 HG21 VAL X 625 -2 .458 -6 .109 6. .411 0. .00 0. .00 PROC

ATOM 4512 HG22 VAL X 625 -1 .129 -7 .147 7. .078 0. .00 0. .00 PROC

ATOM 4513 HG23 VAL X 625 -2 .869 -7 .571 7. .434 0. .00 0. .00 PROC

ATOM 4514 C VAL X 625 -0 .533 -4 .105 9. .645 0. .00 0. .00 PROC

ATOM 4515 O VAL X 625 -1 .014 -3 .016 9. .954 0. .00 0. .00 PROC

ATOM 4516 N GLY X 626 0. .414 -4 .748 10. .328 0. .00 0. .00 PROC

ATOM 4517 HN GLY X 626 0. .727 -5 .568 9. .855 0. .00 0. .00 PROC

ATOM 4518 CA GLY X 626 1. .076 -4 .329 11. .603 0. .00 0. .00 PROC

ATOM 4519 HA1 GLY X 626 1 .745 -3 .498 11. .435 0. .00 0. .00 PROC

ATOM 4520 HA2 GLY X 626 1 .582 -5 .261 11. .808 0. .00 0. .00 PROC

ATOM 4521 C GLY X 626 0. .185 -4 .243 12. .795 0. .00 0. .00 PROC

ATOM 4522 O GLY X 626 -0 .826 -3 .620 12. .735 0. .00 0. .00 PROC

ATOM 4523 N PHE X 627 0. .653 -4 .864 13. .960 0. .00 0. .00 PROC

ATOM 4524 HN PHE X 627 1. .465 -5 .436 13. .871 0. .00 0. .00 PROC

ATOM 4525 CA PHE X 627 -0 .145 -4 .795 15. .148 0. .00 0. .00 PROC

ATOM 4526 HA PHE X 627 -0 .905 -4 .029 15. .135 0. .00 0. .00 PROC

ATOM 4527 CB PHE X 627 -0 .863 -6 .129 15. .545 0. .00 0. .00 PROC

ATOM 4528 HB1 PHE X 627 -0 .101 -6 .914 15. .737 0. .00 0. .00 PROC

ATOM 4529 HB2 PHE X 627 -1 .403 -5 .979 16. .504 0. .00 0. .00 PROC

ATOM 4530 CG PHE X 627 -1 .820 -6 .623 14. .495 0. .00 0. .00 PROC

ATOM 4531 CD1 PHE X 627 -1 .886 -8 .022 14. .196 0. .00 0. .00 PROC

ATOM 4532 HD1 PHE X 627 -1 .113 -8 .608 14. .672 0. .00 0. .00 PROC

ATOM 4533 CE1 PHE X 627 -2 .885 -8 .444 13. .363 0. .00 0. .00 PROC

ATOM 4534 HE1 PHE X 627 -2 .987 -9 .489 13. .113 0. .00 0. .00 PROC

ATOM 4535 CZ PHE X 627 -3 .892 -7 .529 12. .894 0. .00 0. .00 PROC

ATOM 4536 HZ PHE X 627 -4 .789 -7 .876 12. .404 0. .00 0. .00 PROC

ATOM 4537 CD2 PHE X 627 -2 .792 -5 .802 14. .037 0. .00 0. .00 PROC

ATOM 4538 HD2 PHE X 627 -2 .753 -4 .745 14. .259 0. .00 0. .00 PROC

ATOM 4539 CE2 PHE X 627 -3 .814 -6 .172 13. .171 0. .00 0. .00 PROC

ATOM 4540 HE2 PHE X 627 -4 .563 -5 .564 12. .686 0. .00 0. .00 PROC

ATOM 4541 C PHE X 627 0. .637 -4 .292 16. .394 0. .00 0. .00 PROC

ATOM 4542 O PHE X 627 -0 .032 -3 .864 17. .305 0. .00 0. .00 PROC

ATOM 4543 N GLY X 628 1. .969 -4 .481 16. .490 0. .00 0. .00 PROC

ATOM 4544 HN GLY X 628 2. .510 -4 .914 15. .773 0. .00 0. .00 PROC

ATOM 4545 CA GLY X 628 2. .797 -3 .769 17. .454 0. .00 0. .00 PROC

ATOM 4546 HA1 GLY X 628 2 .274 -2 .856 17. .700 0. .00 0. .00 PROC

ATOM 4547 HA2 GLY X 628 3 .813 -3 .562 17. .155 0. .00 0. .00 PROC

ATOM 4548 C GLY X 628 2. .932 -4 .489 18. .713 0. .00 0. .00 PROC

ATOM 4549 O GLY X 628 4. .024 -4 .640 19. .263 0. .00 0. .00 PROC

ATOM 4550 N ASN X 629 1. .881 -5 .196 19. .169 0. .00 0. .00 PROC

ATOM 4551 HN ASN X 629 0. .984 -5 .128 18. .740 0. .00 0. .00 PROC

ATOM 4552 CA ASN X 629 1. .801 -6 .177 20. .309 0. .00 0. .00 PROC

ATOM 4553 HA ASN X 629 2. .501 -5 .757 21. .017 0. .00 0. .00 PROC ATOM 4554 CB ASN X 629 0..305 -6.375 20..736 0..00 0..00 PROC

ATOM 4555 HB1 ASN X 629 0 .331 -7 .208 21. .471 0. .00 0. .00 PROC

ATOM 4556 HB2 ASN X 629 0 .129 -5 .550 21. .460 0. .00 0. .00 PROC

ATOM 4557 CG ASN X 629 -0 .704 -6 .629 19. .642 0. .00 0. .00 PROC

ATOM 4558 OD1 ASN X 629 -0 .733 -7 .697 18. .952 0. .00 0. .00 PROC

ATOM 4559 ND2 ASN X 629 -1 .698 -5 .680 19. .529 0. .00 0. .00 PROC

ATOM 4560 HD21 ASN X 629 -2 .350 -5 .815 18. .783 0. .00 0. .00 PROC

ATOM 4561 HD22 ASN X 629 -1 .677 -4 .797 19. .998 0. .00 0. .00 PROC

ATOM 4562 C ASN X 629 2. .378 -7 .563 19. .893 0. .00 0. .00 PROC

ATOM 4563 O ASN X 629 2. .975 -8 .197 20. .753 0. .00 0. .00 PROC

ATOM 4564 N VAL X 630 2. .359 -7 .901 18. .584 0. .00 0. .00 PROC

ATOM 4565 HN VAL X 630 1. .818 -7 .349 17. .954 0. .00 0. .00 PROC

ATOM 4566 CA VAL X 630 3. .152 -8 .997 18. .101 0. .00 0. .00 PROC

ATOM 4567 HA VAL X 630 3. .744 -9 .519 18. .838 0. .00 0. .00 PROC

ATOM 4568 CB VAL X 630 2. .449 -10 .019 17. .293 0. .00 0. .00 PROC

ATOM 4569 HB VAL X 630 3. .173 -10 .429 16. .557 0. .00 0. .00 PROC

ATOM 4570 CGI VAL X 630 1 .872 -11 .047 18. .262 0. .00 0. .00 PROC

ATOM 4571 HG11 VAL X 630 1 .081 -10 .664 18. .942 0. .00 0. .00 PROC

ATOM 4572 HG12 VAL X 630 1 .430 -11 .854 17. .639 0. .00 0. .00 PROC

ATOM 4573 HG13 VAL X 630 2 .726 -11 .349 18. .906 0. .00 0. .00 PROC

ATOM 4574 CG2 VAL X 630 1 .269 -9 .347 16. .473 0. .00 0. .00 PROC

ATOM 4575 HG21 VAL X 630 0 .597 -8 .775 17. .148 0. .00 0. .00 PROC

ATOM 4576 HG22 VAL X 630 1 .732 -8 .693 15. .703 0. .00 0. .00 PROC

ATOM 4577 HG23 VAL X 630 0 .750 -10 .154 15. .913 0. .00 0. .00 PROC

ATOM 4578 C VAL X 630 4. .265 -8 .309 17. .198 0. .00 0. .00 PROC

ATOM 4579 O VAL X 630 3. .938 -7 .425 16. .396 0. .00 0. .00 PROC

ATOM 4580 N SER X 631 5. .538 -8 .643 17. .432 0. .00 0. .00 PROC

ATOM 4581 HN SER X 631 5. .733 -9 .421 18. .024 0. .00 0. .00 PROC

ATOM 4582 CA SER X 631 6. .691 -7 .995 16. .785 0. .00 0. .00 PROC

ATOM 4583 HA SER X 631 6. .536 -7 .789 15. .736 0. .00 0. .00 PROC

ATOM 4584 CB SER X 631 7. .049 -6 .653 17. .600 0. .00 0. .00 PROC

ATOM 4585 HB1 SER X 631 6 .068 -6 .210 17. .872 0. .00 0. .00 PROC

ATOM 4586 HB2 SER X 631 7 .502 -6 .615 18. .614 0. .00 0. .00 PROC

ATOM 4587 OG SER X 631 7. .703 -5 .644 16. .872 0. .00 0. .00 PROC

ATOM 4588 HG1 SER X 631 7 .883 -4 .977 17. .539 0. .00 0. .00 PROC

ATOM 4589 C SER X 631 7. .881 -8 .947 16. .954 0. .00 0. .00 PROC

ATOM 4590 O SER X 631 7. .688 -9 .930 17. .646 0. .00 0. .00 PROC

ATOM 4591 N PRO X 632 9. .059 -8 .804 16. .471 0. .00 0. .00 PROC

ATOM 4592 CD PRO X 632 9. .434 -7 .927 15. .334 0. .00 0. .00 PROC

ATOM 4593 HD1 PRO X 632 8 .620 -7 .933 14. .578 0. .00 0. .00 PROC

ATOM 4594 HD2 PRO X 632 9 .597 -6 .868 15. .627 0. .00 0. .00 PROC

ATOM 4595 CA PRO X 632 10 .248 -9 .573 16. .862 0. .00 0. .00 PROC

ATOM 4596 HA PRO X 632 10 .054 -10 .619 16. .674 0. .00 0. .00 PROC

ATOM 4597 CB PRO X 632 11 .417 -8 .948 16. .133 0. .00 0. .00 PROC

ATOM 4598 HB1 PRO X 632 12 .220 -9 .702 15. .987 0. .00 0. .00 PROC

ATOM 4599 HB2 PRO X 632 11 .735 -8 .025 16. .664 0. .00 0. .00 PROC

ATOM 4600 CG PRO X 632 10 .736 -8 .489 14. .832 0. .00 0. .00 PROC

ATOM 4601 HG1 PRO X 632 10 .417 -9 .345 14. .201 0. .00 0. .00 PROC

ATOM 4602 HG2 PRO X 632 11 .438 -7 .895 14. .208 0. .00 0. .00 PROC

ATOM 4603 C PRO X 632 10 .422 -9 .589 18. .383 0. .00 0. .00 PROC

ATOM 4604 O PRO X 632 10 .210 -8 .574 19. .047 0. .00 0. .00 PROC

ATOM 4605 N ASN X 633 10 .939 -10 .686 18. .934 0. .00 0. .00 PROC

ATOM 4606 HN ASN X 633 11 .187 -11 .425 18. .313 0. .00 0. .00 PROC

ATOM 4607 CA ASN X 633 11 .468 -10 .685 20. .246 0. .00 0. .00 PROC

ATOM 4608 HA ASN X 633 11 .312 -9 .813 20. .864 0. .00 0. .00 PROC

ATOM 4609 CB ASN X 633 10 .860 -11 .978 20. .870 0. .00 0. .00 PROC

ATOM 4610 HB1 ASN X 633 10 .967 -12 .823 20. .157 0. .00 0. .00 PROC

ATOM 4611 HB2 ASN X 633 11 .314 -12 .346 21. .815 0. .00 0. .00 PROC

ATOM 4612 CG ASN X 633 9. .360 -11 .762 21. .092 0. .00 0. .00 PROC

ATOM 4613 OD1 ASN X 633 8 .565 -12 .461 20. .459 0. .00 0. .00 PROC

ATOM 4614 ND2 ASN X 633 8 .939 -10 .897 21. .988 0. .00 0. .00 PROC

ATOM 4615 HD21 ASN X 633 7 .954 -10 .730 22. .039 0. .00 0. .00 PROC

ATOM 4616 HD22 ASN X 633 9 .459 -10 .427 22. .702 0. .00 0. .00 PROC

ATOM 4617 C ASN X 633 12 .957 -10 .838 20. .290 0. .00 0. .00 PROC

ATOM 4618 O ASN X 633 13 .425 -10 .779 21. .433 0. .00 0. .00 PROC

ATOM 4619 N THR X 634 13 .686 -11 .179 19. .173 0. .00 0. .00 PROC ATOM 4620 HN THR X 634 13.159 -11.283 18..333 0..00 0..00 PROC

ATOM 4621 CA THR X 634 15 .098 -11 .324 19. .238 0. .00 0. .00 PROC

ATOM 4622 HA THR X 634 15 .452 -10 .791 20. .108 0. .00 0. .00 PROC

ATOM 4623 CB THR X 634 15 .550 -12 .818 19. .558 0. .00 0. .00 PROC

ATOM 4624 HB THR X 634 15 .105 -13 .050 20. .550 0. .00 0. .00 PROC

ATOM 4625 OG1 THR X 634 16 .914 -12 .961 19. .931 0. .00 0. .00 PROC

ATOM 4626 HG1 THR X 634 17 .083 -13 .899 20. .051 0. .00 0. .00 PROC

ATOM 4627 CG2 THR X 634 15 .218 -13 .900 18. .475 0. .00 0. .00 PROC

ATOM 4628 HG21 THR X 634 15 .255 -14 .967 18. .783 0. .00 0. .00 PROC

ATOM 4629 HG22 THR X 634 14 .183 -13 .735 18. .107 0. .00 0. .00 PROC

ATOM 4630 HG23 THR X 634 15 .949 -13 .670 17. .671 0. .00 0. .00 PROC

ATOM 4631 C THR X 634 15 .882 -10 .725 18. .054 0. .00 0. .00 PROC

ATOM 4632 O THR X 634 15 .289 -10 .198 17. .117 0. .00 0. .00 PROC

ATOM 4633 N ASN X 635 17 .198 -10 .728 18. .181 0. .00 0. .00 PROC

ATOM 4634 HN ASN X 635 17 .622 -11 .157 18. .975 0. .00 0. .00 PROC

ATOM 4635 CA ASN X 635 18 .067 -9 .965 17. .341 0. .00 0. .00 PROC

ATOM 4636 HA ASN X 635 17 .674 -8 .995 17. .077 0. .00 0. .00 PROC

ATOM 4637 CB ASN X 635 19 .558 -9 .893 17. .982 0. .00 0. .00 PROC

ATOM 4638 HB1 ASN X 635 20 .028 -8 .999 17. .520 0. .00 0. .00 PROC

ATOM 4639 HB2 ASN X 635 19 .355 -9 .716 19. .060 0. .00 0. .00 PROC

ATOM 4640 CG ASN X 635 20 .368 -11 .139 17. .767 0. .00 0. .00 PROC

ATOM 4641 OD1 ASN X 635 20 .071 -12 .213 18. .284 0. .00 0. .00 PROC

ATOM 4642 ND2 ASN X 635 21 .489 -10 .968 17. .030 0. .00 0. .00 PROC

ATOM 4643 HD21 ASN X 635 21 .931 -11 .835 16. .799 0. .00 0. .00 PROC

ATOM 4644 HD22 ASN X 635 21 .533 -10 .073 16. .587 0. .00 0. .00 PROC

ATOM 4645 C ASN X 635 18 .096 -10 .623 15. .975 0. .00 0. .00 PROC

ATOM 4646 O ASN X 635 18 .133 -9 .916 14. .982 0. .00 0. .00 PROC

ATOM 4647 N SER X 636 18 .066 -11 .987 15. .985 0. .00 0. .00 PROC

ATOM 4648 HN SER X 636 17 .781 -12 .443 16. .824 0. .00 0. .00 PROC

ATOM 4649 CA SER X 636 18 .188 -12 .794 14. .773 0. .00 0. .00 PROC

ATOM 4650 HA SER X 636 18 .870 -12 .286 14. .106 0. .00 0. .00 PROC

ATOM 4651 CB SER X 636 18 .619 -14 .285 15. .068 0. .00 0. .00 PROC

ATOM 4652 HB1 SER X 636 18 .573 -14 .925 14. .161 0. .00 0. .00 PROC

ATOM 4653 HB2 SER X 636 19 .672 -14 .335 15. .417 0. .00 0. .00 PROC

ATOM 4654 OG SER X 636 17 .770 -14 .849 16. .105 0. .00 0. .00 PROC

ATOM 4655 HG1 SER X 636 18 .156 -15 .719 16. .227 0. .00 0. .00 PROC

ATOM 4656 C SER X 636 16 .953 -12 .690 13. .966 0. .00 0. .00 PROC

ATOM 4657 O SER X 636 16 .921 -12 .302 12. .768 0. .00 0. .00 PROC

ATOM 4658 N GLU X 637 15 .800 -12 .748 14. .671 0. .00 0. .00 PROC

ATOM 4659 HN GLU X 637 15 .877 -13 .124 15. .591 0. .00 0. .00 PROC

ATOM 4660 CA GLU X 637 14 .458 -12 .422 14. .168 0. .00 0. .00 PROC

ATOM 4661 HA GLU X 637 14 .085 -13 .182 13. .497 0. .00 0. .00 PROC

ATOM 4662 CB GLU X 637 13 .498 -12 .534 15. .374 0. .00 0. .00 PROC

ATOM 4663 HB1 GLU X 637 13 .562 -13 .483 15. .949 0. .00 0. .00 PROC

ATOM 4664 HB2 GLU X 637 13 .692 -11 .666 16. .039 0. .00 0. .00 PROC

ATOM 4665 CG GLU X 637 12 .016 -12 .558 15. .055 0. .00 0. .00 PROC

ATOM 4666 HG1 GLU X 637 11 .640 -11 .584 14. .673 0. .00 0. .00 PROC

ATOM 4667 HG2 GLU X 637 11 .808 -13 .299 14. .254 0. .00 0. .00 PROC

ATOM 4668 CD GLU X 637 11 .041 -12 .876 16. .213 0. .00 0. .00 PROC

ATOM 4669 OE1 GLU X 637 11 .545 -12 .870 17. .421 0. .00 0. .00 PROC

ATOM 4670 OE2 GLU X 637 9 .865 -13 .123 15. .992 0. .00 0. .00 PROC

ATOM 4671 C GLU X 637 14 .307 -11 .054 13. .581 0. .00 0. .00 PROC

ATOM 4672 O GLU X 637 13 .628 -10 .912 12. .547 0. .00 0. .00 PROC

ATOM 4673 N LYS X 638 14 .881 -9 .953 14. .228 0. .00 0. .00 PROC

ATOM 4674 HN LYS X 638 15 .279 -10 .104 15. .130 0. .00 0. .00 PROC

ATOM 4675 CA LYS X 638 14 .781 -8 .622 13. .568 0. .00 0. .00 PROC

ATOM 4676 HA LYS X 638 13 .744 -8 .329 13. .503 0. .00 0. .00 PROC

ATOM 4677 CB LYS X 638 15 .508 -7 .646 14. .527 0. .00 0. .00 PROC

ATOM 4678 HB1 LYS X 638 14 .881 -7 .707 15. .442 0. .00 0. .00 PROC

ATOM 4679 HB2 LYS X 638 16 .421 -8 .174 14. .875 0. .00 0. .00 PROC

ATOM 4680 CG LYS X 638 15 .646 -6 .146 14. .107 0. .00 0. .00 PROC

ATOM 4681 HG1 LYS X 638 15 .975 -5 .973 13. .060 0. .00 0. .00 PROC

ATOM 4682 HG2 LYS X 638 14 .634 -5 .687 14. .129 0. .00 0. .00 PROC

ATOM 4683 CD LYS X 638 16 .649 -5 .341 14. .960 0. .00 0. .00 PROC

ATOM 4684 HD1 LYS X 638 17 .558 -5 .974 15. .048 0. .00 0. .00 PROC

ATOM 4685 HD2 LYS X 638 16 .887 -4 .446 14. .346 0. .00 0. .00 PROC ATOM 4686 CE LYS X 638 16.003 -4.850 16..228 0..00 0..00 PROC

ATOM 4687 HE1 LYS X 638 15 .121 -4 .216 15. .997 0. .00 0. .00 PROC

ATOM 4688 HE2 LYS X 638 15 .680 -5 .611 16. .970 0. .00 0. .00 PROC

ATOM 4689 NZ LYS X 638 16 .859 -3 .901 17. .082 0. .00 0. .00 PROC

ATOM 4690 HZ1 LYS X 638 16 .467 -4 .081 18. .028 0. .00 0. .00 PROC

ATOM 4691 HZ2 LYS X 638 17 .856 -4 .196 17. .068 0. .00 0. .00 PROC

ATOM 4692 HZ3 LYS X 638 16 .717 -2 .925 16. .749 0. .00 0. .00 PROC

ATOM 4693 C LYS X 638 15 .511 -8 .559 12. .232 0. .00 0. .00 PROC

ATOM 4694 O LYS X 638 14 .929 -8 .120 11. .233 0. .00 0. .00 PROC

ATOM 4695 N ILE X 639 16 .743 -9 .018 12. .118 0. .00 0. .00 PROC

ATOM 4696 HN ILE X 639 17 .287 -9 .173 12. .939 0. .00 0. .00 PROC

ATOM 4697 CA ILE X 639 17 .505 -8 .925 10. .818 0. .00 0. .00 PROC

ATOM 4698 HA ILE X 639 17 .251 -7 .895 10. .619 0. .00 0. .00 PROC

ATOM 4699 CB ILE X 639 19 .039 -8 .958 11. .017 0. .00 0. .00 PROC

ATOM 4700 HB ILE X 639 19 .503 -8 .560 10. .090 0. .00 0. .00 PROC

ATOM 4701 CG2 ILE X 639 19 .410 -7 .983 12. .112 0. .00 0. .00 PROC

ATOM 4702 HG21 ILE X 639 19 .051 -8 .254 13. .128 0. .00 0. .00 PROC

ATOM 4703 HG22 ILE X 639 20 .506 -7 .912 12. .280 0. .00 0. .00 PROC

ATOM 4704 HG23 ILE X 639 19 .093 -6 .955 11. .835 0. .00 0. .00 PROC

ATOM 4705 CGI ILE X 639 19 .686 -10 .390 11. .078 0. .00 0. .00 PROC

ATOM 4706 HG11 ILE X 639 19 .188 -10 .924 11. .915 0. .00 0. .00 PROC

ATOM 4707 HG12 ILE X 639 19 .411 -10 .938 10. .151 0. .00 0. .00 PROC

ATOM 4708 CD ILE X 639 21 .181 -10 .480 11. .140 0. .00 0. .00 PROC

ATOM 4709 HD1 ILE X 639 21 .584 -9 .740 10. .417 0. .00 0. .00 PROC

ATOM 4710 HD2 ILE X 639 21 .596 -10 .137 12. .112 0. .00 0. .00 PROC

ATOM 4711 HD3 ILE X 639 21 .567 -11 .499 10. .925 0. .00 0. .00 PROC

ATOM 4712 C ILE X 639 17 .030 -9 .863 9. .760 0. .00 0. .00 PROC

ATOM 4713 O ILE X 639 17 .043 -9 .550 8. .594 0. .00 0. .00 PROC

ATOM 4714 N PHE X 640 16 .577 -11 .028 10. .095 0. .00 0. .00 PROC

ATOM 4715 HN PHE X 640 16 .582 -11 .325 11. .047 0. .00 0. .00 PROC

ATOM 4716 CA PHE X 640 15 .837 -11 .930 9. .233 0. .00 0. .00 PROC

ATOM 4717 HA PHE X 640 16 .450 -12 .298 8. .423 0. .00 0. .00 PROC

ATOM 4718 CB PHE X 640 15 .516 -13 .147 10. .186 0. .00 0. .00 PROC

ATOM 4719 HB1 PHE X 640 15 .145 -12 .909 11. .206 0. .00 0. .00 PROC

ATOM 4720 HB2 PHE X 640 14 .793 -13 .732 9. .580 0. .00 0. .00 PROC

ATOM 4721 CG PHE X 640 16 .609 -14 .113 10. .436 0. .00 0. .00 PROC

ATOM 4722 CD1 PHE X 640 16 .269 -15 .172 11. .337 0. .00 0. .00 PROC

ATOM 4723 HD1 PHE X 640 15 .281 -15 .107 11. .768 0. .00 0. .00 PROC

ATOM 4724 CE1 PHE X 640 17 .282 -16 .017 11. .825 0. .00 0. .00 PROC

ATOM 4725 HE1 PHE X 640 17 .034 -16 .750 12. .578 0. .00 0. .00 PROC

ATOM 4726 CZ PHE X 640 18 .575 -15 .949 11. .317 0. .00 0. .00 PROC

ATOM 4727 HZ PHE X 640 19 .294 -16 .676 11. .666 0. .00 0. .00 PROC

ATOM 4728 CD2 PHE X 640 17 .880 -14 .148 9. .876 0. .00 0. .00 PROC

ATOM 4729 HD2 PHE X 640 18 .182 -13 .529 9. .044 0. .00 0. .00 PROC

ATOM 4730 CE2 PHE X 640 18 .849 -15 .001 10. .289 0. .00 0. .00 PROC

ATOM 4731 HE2 PHE X 640 19 .765 -15 .108 9. .727 0. .00 0. .00 PROC

ATOM 4732 C PHE X 640 14 .575 -11 .312 8. .690 0. .00 0. .00 PROC

ATOM 4733 O PHE X 640 14 .316 -11 .423 7. .482 0. .00 0. .00 PROC

ATOM 4734 N SER X 641 13 .798 -10 .624 9. .537 0. .00 0. .00 PROC

ATOM 4735 HN SER X 641 14 .015 -10 .479 10. .499 0. .00 0. .00 PROC

ATOM 4736 CA SER X 641 12 .427 -10 .160 9. .192 0. .00 0. .00 PROC

ATOM 4737 HA SER X 641 11 .874 -11 .054 8. .946 0. .00 0. .00 PROC

ATOM 4738 CB SER X 641 11 .766 -9 .387 10. .368 0. .00 0. .00 PROC

ATOM 4739 HB1 SER X 641 12 .480 -8 .704 10. .878 0. .00 0. .00 PROC

ATOM 4740 HB2 SER X 641 10 .838 -8 .854 10. .070 0. .00 0. .00 PROC

ATOM 4741 OG SER X 641 11 .441 -10 .373 11. .364 0. .00 0. .00 PROC

ATOM 4742 HG1 SER X 641 12 .326 -10 .691 11. .559 0. .00 0. .00 PROC

ATOM 4743 C SER X 641 12 .414 -9 .229 7. .969 0. .00 0. .00 PROC

ATOM 4744 O SER X 641 11 .490 -9 .093 7. .172 0. .00 0. .00 PROC

ATOM 4745 N ILE X 642 13 .572 -8 .544 7. .694 0. .00 0. .00 PROC

ATOM 4746 HN ILE X 642 14 .357 -8 .610 8. .306 0. .00 0. .00 PROC

ATOM 4747 CA ILE X 642 13 .832 -7 .621 6. .533 0. .00 0. .00 PROC

ATOM 4748 HA ILE X 642 13 .093 -6 .835 6. .575 0. .00 0. .00 PROC

ATOM 4749 CB ILE X 642 15 .215 -7 .036 6. .703 0. .00 0. .00 PROC

ATOM 4750 HB ILE X 642 15 .935 -7 .882 6. .710 0. .00 0. .00 PROC

ATOM 4751 CG2 ILE X 642 15 .436 -6 .126 5. .489 0. .00 0. .00 PROC ATOM 4752 HG21 ILE X 642 15.560 -6.784 4..602 0..00 0..00 PROC

ATOM 4753 HG22 ILE X 642 14 .511 -5 .526 5. .353 0. .00 0. .00 PROC

ATOM 4754 HG23 ILE X 642 16 .290 -5 .421 5. .577 0. .00 0. .00 PROC

ATOM 4755 CGI ILE X 642 15 .308 -6 .345 8. .002 0. .00 0. .00 PROC

ATOM 4756 HG11 ILE X 642 14 .969 -6 .936 8. .879 0. .00 0. .00 PROC

ATOM 4757 HG12 ILE X 642 16 .371 -6 .137 8. .249 0. .00 0. .00 PROC

ATOM 4758 CD ILE X 642 14 .507 -5 .094 8. .009 0. .00 0. .00 PROC

ATOM 4759 HD1 ILE X 642 13 .422 -5 .260 7. .835 0. .00 0. .00 PROC

ATOM 4760 HD2 ILE X 642 14 .480 -4 .657 9. .030 0. .00 0. .00 PROC

ATOM 4761 HD3 ILE X 642 14 .885 -4 .242 7. .405 0. .00 0. .00 PROC

ATOM 4762 C ILE X 642 13 .661 -8 .230 5. .233 0. .00 0. .00 PROC

ATOM 4763 O ILE X 642 12 .990 -7 .667 4. .384 0. .00 0. .00 PROC

ATOM 4764 N CYS X 643 14 .166 -9 .474 5. .044 0. .00 0. .00 PROC

ATOM 4765 HN CYS X 643 14 .482 -9 .932 5. .871 0. .00 0. .00 PROC

ATOM 4766 CA CYS X 643 14 .126 -10 .351 3. .862 0. .00 0. .00 PROC

ATOM 4767 HA CYS X 643 14 .453 -9 .771 3. .011 0. .00 0. .00 PROC

ATOM 4768 CB CYS X 643 15 .166 -11 .519 3. .995 0. .00 0. .00 PROC

ATOM 4769 HB1 CYS X 643 16 .206 -11 .219 4. .247 0. .00 0. .00 PROC

ATOM 4770 HB2 CYS X 643 14 .910 -12 .176 4. .853 0. .00 0. .00 PROC

ATOM 4771 C CYS X 643 12 .722 -10 .840 3. .695 0. .00 0. .00 PROC

ATOM 4772 O CYS X 643 12 .139 -10 .824 2. .634 0. .00 0. .00 PROC

ATOM 4773 N VAL X 644 12 .186 -11 .272 4. .908 0. .00 0. .00 PROC

ATOM 4774 HN VAL X 644 12 .607 -11 .091 5. .793 0. .00 0. .00 PROC

ATOM 4775 CA VAL X 644 10 .885 -11 .929 5. .011 0. .00 0. .00 PROC

ATOM 4776 HA VAL X 644 11 .005 -12 .749 4. .319 0. .00 0. .00 PROC

ATOM 4777 CB VAL X 644 10 .454 -12 .528 6. .301 0. .00 0. .00 PROC

ATOM 4778 HB VAL X 644 9. .949 -11 .828 7. .001 0. .00 0. .00 PROC

ATOM 4779 CGI VAL X 644 9 .422 -13 .606 6. .065 0. .00 0. .00 PROC

ATOM 4780 HG11 VAL X 644 9 .935 -14 .320 5. .386 0. .00 0. .00 PROC

ATOM 4781 HG12 VAL X 644 9 .041 -14 .171 6. .943 0. .00 0. .00 PROC

ATOM 4782 HG13 VAL X 644 8 .584 -13 .120 5. .522 0. .00 0. .00 PROC

ATOM 4783 CG2 VAL X 644 11 .619 -13 .253 6. .967 0. .00 0. .00 PROC

ATOM 4784 HG21 VAL X 644 12 .241 -12 .425 7. .370 0. .00 0. .00 PROC

ATOM 4785 HG22 VAL X 644 11 .341 -13 .851 7. .861 0. .00 0. .00 PROC

ATOM 4786 HG23 VAL X 644 12 .119 -14 .002 6. .316 0. .00 0. .00 PROC

ATOM 4787 C VAL X 644 9. .683 -11 .082 4. .525 0. .00 0. .00 PROC

ATOM 4788 O VAL X 644 8. .866 -11 .465 3. .613 0. .00 0. .00 PROC

ATOM 4789 N MET X 645 9. .522 -9 .869 5. .141 0. .00 0. .00 PROC

ATOM 4790 HN MET X 645 10 .062 -9 .540 5. .912 0. .00 0. .00 PROC

ATOM 4791 CA MET X 645 8. .617 -8 .851 4. .628 0. .00 0. .00 PROC

ATOM 4792 HA MET X 645 7. .597 -9 .206 4. .594 0. .00 0. .00 PROC

ATOM 4793 CB MET X 645 8. .574 -7 .587 5. .595 0. .00 0. .00 PROC

ATOM 4794 HB1 MET X 645 9 .531 -7 .062 5. .801 0. .00 0. .00 PROC

ATOM 4795 HB2 MET X 645 8 .076 -6 .795 4. .995 0. .00 0. .00 PROC

ATOM 4796 CG MET X 645 7. .746 -7 .839 6. .820 0. .00 0. .00 PROC

ATOM 4797 HG1 MET X 645 6 .770 -8 .293 6. .544 0. .00 0. .00 PROC

ATOM 4798 HG2 MET X 645 8 .290 -8 .653 7. .345 0. .00 0. .00 PROC

ATOM 4799 SD MET X 645 7. .524 -6 .449 7. .920 0. .00 0. .00 PROC

ATOM 4800 C MET X 645 8. .952 -8 .415 3. .121 0. .00 0. .00 PROC

ATOM 4801 O MET X 645 8. .065 -8 .462 2. .255 0. .00 0. .00 PROC

ATOM 4802 N LEU X 646 10 .289 -8 .243 2. .683 0. .00 0. .00 PROC

ATOM 4803 HN LEU X 646 11 .067 -8 .359 3. .296 0. .00 0. .00 PROC

ATOM 4804 CA LEU X 646 10 .531 -7 .944 1. .263 0. .00 0. .00 PROC

ATOM 4805 HA LEU X 646 9. .967 -7 .048 1. .048 0. .00 0. .00 PROC

ATOM 4806 CB LEU X 646 12 .092 -7 .868 1. .103 0. .00 0. .00 PROC

ATOM 4807 HB1 LEU X 646 12 .447 -7 .049 1. .766 0. .00 0. .00 PROC

ATOM 4808 HB2 LEU X 646 12 .654 -8 .721 1. .539 0. .00 0. .00 PROC

ATOM 4809 CG LEU X 646 12 .692 -7 .718 -0. .252 0. .00 0. .00 PROC

ATOM 4810 HG LEU X 646 12 .266 -8 .291 -1. .103 0. .00 0. .00 PROC

ATOM 4811 CD1 LEU X 646 12 .418 -6 .355 -0. .903 0. .00 0. .00 PROC

ATOM 4812 HD11 LEU X 646 12 .948 -6 .274 -1. .876 0. .00 0. .00 PROC

ATOM 4813 HD12 LEU X 646 11 .332 -6 .156 -1. .029 0. .00 0. .00 PROC

ATOM 4814 HD13 LEU X 646 12 .776 -5 .647 -0. .125 0. .00 0. .00 PROC

ATOM 4815 CD2 LEU X 646 14 .178 -8 .003 -0. .179 0. .00 0. .00 PROC

ATOM 4816 HD21 LEU X 646 14 .413 -8 .645 0. .698 0. .00 0. .00 PROC

ATOM 4817 HD22 LEU X 646 14 .631 -8 .488 -1. .069 0. .00 0. .00 PROC ATOM 4818 HD23 LEU X 646 14.742 -7.046 -0..146 0..00 0..00 PROC

ATOM 4819 C LEU X 646 10 .057 -8 .964 0. .267 0. .00 0. .00 PROC

ATOM 4820 O LEU X 646 9. .359 -8 .717 -0. .701 0. .00 0. .00 PROC

ATOM 4821 N ILE X 647 10 .407 -10 .274 0. .449 0. .00 0. .00 PROC

ATOM 4822 HN ILE X 647 11 .078 -10 .540 1. .137 0. .00 0. .00 PROC

ATOM 4823 CA ILE X 647 10 .078 -11 .205 -0. .602 0. .00 0. .00 PROC

ATOM 4824 HA ILE X 647 10 .364 -10 .690 -1. .507 0. .00 0. .00 PROC

ATOM 4825 CB ILE X 647 10 .969 -12 .500 -0. .566 0. .00 0. .00 PROC

ATOM 4826 HB ILE X 647 10 .663 -13 .093 -1. .454 0. .00 0. .00 PROC

ATOM 4827 CG2 ILE X 647 12 .396 -11 .994 -0. .775 0. .00 0. .00 PROC

ATOM 4828 HG21 ILE X 647 12 .449 -11 .269 -1. .616 0. .00 0. .00 PROC

ATOM 4829 HG22 ILE X 647 12 .566 -11 .487 0. .199 0. .00 0. .00 PROC

ATOM 4830 HG23 ILE X 647 13 .187 -12 .771 -0. .834 0. .00 0. .00 PROC

ATOM 4831 CGI ILE X 647 10 .860 -13 .433 0. .665 0. .00 0. .00 PROC

ATOM 4832 HG11 ILE X 647 11 .092 -12 .824 1. .565 0. .00 0. .00 PROC

ATOM 4833 HG12 ILE X 647 9 .790 -13 .730 0. .660 0. .00 0. .00 PROC

ATOM 4834 CD ILE X 647 11 .753 -14 .689 0. .547 0. .00 0. .00 PROC

ATOM 4835 HD1 ILE X 647 12 .840 -14 .478 0. .454 0. .00 0. .00 PROC

ATOM 4836 HD2 ILE X 647 11 .448 -15 .545 1. .185 0. .00 0. .00 PROC

ATOM 4837 HD3 ILE X 647 11 .523 -15 .071 -0. .471 0. .00 0. .00 PROC

ATOM 4838 C ILE X 647 8. .619 -11 .568 -0. .678 0. .00 0. .00 PROC

ATOM 4839 O ILE X 647 8. .066 -11 .864 -1. .730 0. .00 0. .00 PROC

ATOM 4840 N GLY X 648 7. .903 -11 .377 0. .521 0. .00 0. .00 PROC

ATOM 4841 HN GLY X 648 8. .505 -11 .226 1. .301 0. .00 0. .00 PROC

ATOM 4842 CA GLY X 648 6. .446 -11 .508 0. .672 0. .00 0. .00 PROC

ATOM 4843 HA1 GLY X 648 6 .391 -11 .459 1. .750 0. .00 0. .00 PROC

ATOM 4844 HA2 GLY X 648 6 .125 -12 .431 0. .212 0. .00 0. .00 PROC

ATOM 4845 C GLY X 648 5. .749 -10 .339 0. .023 0. .00 0. .00 PROC

ATOM 4846 O GLY X 648 4. .804 -10 .439 -0. .740 0. .00 0. .00 PROC

ATOM 4847 N SER X 649 6. .265 -9 .056 0. .246 0. .00 0. .00 PROC

ATOM 4848 HN SER X 649 7. .096 -8 .977 0. .791 0. .00 0. .00 PROC

ATOM 4849 CA SER X 649 5. .792 -7 .737 -0. .335 0. .00 0. .00 PROC

ATOM 4850 HA SER X 649 4. .797 -7 .574 0. .052 0. .00 0. .00 PROC

ATOM 4851 CB SER X 649 6. .671 -6 .537 0. .054 0. .00 0. .00 PROC

ATOM 4852 HB1 SER X 649 6 .513 -6 .471 1. .152 0. .00 0. .00 PROC

ATOM 4853 HB2 SER X 649 7 .764 -6 .696 -0. .067 0. .00 0. .00 PROC

ATOM 4854 OG SER X 649 6. .190 -5 .248 -0. .377 0. .00 0. .00 PROC

ATOM 4855 HG1 SER X 649 6 .708 -4 .600 0. .106 0. .00 0. .00 PROC

ATOM 4856 C SER X 649 5. .661 -7 .818 -1. .824 0. .00 0. .00 PROC

ATOM 4857 O SER X 649 4. .751 -7 .303 -2. .484 0. .00 0. .00 PROC

ATOM 4858 N LEU X 650 6. .654 -8 .420 -2. .537 0. .00 0. .00 PROC

ATOM 4859 HN LEU X 650 7. .371 -8 .854 -1. .997 0. .00 0. .00 PROC

ATOM 4860 CA LEU X 650 6. .505 -8 .614 -3. .979 0. .00 0. .00 PROC

ATOM 4861 HA LEU X 650 6. .134 -7 .712 -4. .443 0. .00 0. .00 PROC

ATOM 4862 CB LEU X 650 7. .843 -9 .047 -4. .648 0. .00 0. .00 PROC

ATOM 4863 HB1 LEU X 650 8 .241 -9 .996 -4. .230 0. .00 0. .00 PROC

ATOM 4864 HB2 LEU X 650 7 .662 -9 .235 -5. .728 0. .00 0. .00 PROC

ATOM 4865 CG LEU X 650 8. .990 -8 .053 -4. .435 0. .00 0. .00 PROC

ATOM 4866 HG LEU X 650 9. .242 -7 .909 -3. .363 0. .00 0. .00 PROC

ATOM 4867 CD1 LEU X 650 10 .324 -8 .680 -4. .939 0. .00 0. .00 PROC

ATOM 4868 HD11 LEU X 650 10 .423 -8 .679 -6. .046 0. .00 0. .00 PROC

ATOM 4869 HD12 LEU X 650 11 .123 -8 .036 -4. .511 0. .00 0. .00 PROC

ATOM 4870 HD13 LEU X 650 10 .515 -9 .706 -4. .560 0. .00 0. .00 PROC

ATOM 4871 CD2 LEU X 650 8 .812 -6 .784 -5. .255 0. .00 0. .00 PROC

ATOM 4872 HD21 LEU X 650 7 .814 -6 .368 -4. .999 0. .00 0. .00 PROC

ATOM 4873 HD22 LEU X 650 9 .550 -6 .028 -4. .912 0. .00 0. .00 PROC

ATOM 4874 HD23 LEU X 650 8 .964 -7 .001 -6. .334 0. .00 0. .00 PROC

ATOM 4875 C LEU X 650 5. .513 -9 .759 -4. .360 0. .00 0. .00 PROC

ATOM 4876 O LEU X 650 4. .685 -9 .551 -5. .230 0. .00 0. .00 PROC

ATOM 4877 N MET X 651 5. .533 -10 .916 -3. .741 0. .00 0. .00 PROC

ATOM 4878 HN MET X 651 6. .122 -11 .132 -2. .966 0. .00 0. .00 PROC

ATOM 4879 CA MET X 651 4. .586 -12 .011 -4. .071 0. .00 0. .00 PROC

ATOM 4880 HA MET X 651 4. .658 -12 .166 -5. .137 0. .00 0. .00 PROC

ATOM 4881 CB MET X 651 4. .730 -13 .191 -3. .128 0. .00 0. .00 PROC

ATOM 4882 HB1 MET X 651 5 .743 -13 .601 -3. .327 0. .00 0. .00 PROC

ATOM 4883 HB2 MET X 651 4 .833 -12 .744 -2. .116 0. .00 0. .00 PROC ATOM 4884 CG MET X 651 3..742 -14.434 -3..140 0..00 0..00 PROC

ATOM 4885 HG1 MET X 651 2 .751 -13 .932 -3. .169 0. .00 0. .00 PROC

ATOM 4886 HG2 MET X 651 3 .960 -15 .080 -4. .017 0. .00 0. .00 PROC

ATOM 4887 SD MET X 651 3. .607 -15 .495 -1. .712 0. .00 0. .00 PROC

ATOM 4888 C MET X 651 3. .161 -11 .521 -3. .876 0. .00 0. .00 PROC

ATOM 4889 O MET X 651 2. .400 -11 .728 -4. .753 0. .00 0. .00 PROC

ATOM 4890 N TYR X 652 2. .809 -10 .901 -2. .790 0. .00 0. .00 PROC

ATOM 4891 HN TYR X 652 3. .425 -10 .849 -2. .008 0. .00 0. .00 PROC

ATOM 4892 CA TYR X 652 1. .409 -10 .371 -2. .580 0. .00 0. .00 PROC

ATOM 4893 HA TYR X 652 0. .797 -11 .257 -2. .665 0. .00 0. .00 PROC

ATOM 4894 CB TYR X 652 0. .973 -9 .926 -1. .168 0. .00 0. .00 PROC

ATOM 4895 HB1 TYR X 652 1 .794 -9 .308 -0. .745 0. .00 0. .00 PROC

ATOM 4896 HB2 TYR X 652 0 .107 -9 .229 -1. .154 0. .00 0. .00 PROC

ATOM 4897 CG TYR X 652 0. .698 -11 .003 -0. .154 0. .00 0. .00 PROC

ATOM 4898 CD1 TYR X 652 -0 .469 -11 .815 -0. .483 0. .00 0. .00 PROC

ATOM 4899 HD1 TYR X 652 -1 .084 -11 .700 -1. .363 0. .00 0. .00 PROC

ATOM 4900 CE1 TYR X 652 -0 .976 -12 .730 0. .506 0. .00 0. .00 PROC

ATOM 4901 HE1 TYR X 652 -1 .894 -13 .198 0. .184 0. .00 0. .00 PROC

ATOM 4902 CZ TYR X 652 -0 .279 -12 .996 1. .645 0. .00 0. .00 PROC

ATOM 4903 OH TYR X 652 -0 .843 -13 .901 2. .611 0. .00 0. .00 PROC

ATOM 4904 HH TYR X 652 -0 .242 -13 .990 3. .354 0. .00 0. .00 PROC

ATOM 4905 CD2 TYR X 652 1 .346 -11 .277 1. .067 0. .00 0. .00 PROC

ATOM 4906 HD2 TYR X 652 2 .164 -10 .670 1. .425 0. .00 0. .00 PROC

ATOM 4907 CE2 TYR X 652 0 .830 -12 .216 1. .972 0. .00 0. .00 PROC

ATOM 4908 HE2 TYR X 652 1 .273 -12 .291 2. .954 0. .00 0. .00 PROC

ATOM 4909 C TYR X 652 0. .918 -9 .413 -3. .569 0. .00 0. .00 PROC

ATOM 4910 O TYR X 652 -0 .203 -9 .513 -4. .018 0. .00 0. .00 PROC

ATOM 4911 N ALA X 653 1. .775 -8 .386 -3. .899 0. .00 0. .00 PROC

ATOM 4912 HN ALA X 653 2. .688 -8 .333 -3. .501 0. .00 0. .00 PROC

ATOM 4913 CA ALA X 653 1. .460 -7 .335 -4. .929 0. .00 0. .00 PROC

ATOM 4914 HA ALA X 653 0. .582 -6 .873 -4. .503 0. .00 0. .00 PROC

ATOM 4915 CB ALA X 653 2. .558 -6 .354 -5. .083 0. .00 0. .00 PROC

ATOM 4916 HB1 ALA X 653 3 .474 -6 .850 -5. .469 0. .00 0. .00 PROC

ATOM 4917 HB2 ALA X 653 2 .306 -5 .458 -5. .690 0. .00 0. .00 PROC

ATOM 4918 HB3 ALA X 653 2 .761 -6 .054 -4. .033 0. .00 0. .00 PROC

ATOM 4919 C ALA X 653 1. .103 -7 .978 -6. .244 0. .00 0. .00 PROC

ATOM 4920 O ALA X 653 0. .179 -7 .578 -6. .942 0. .00 0. .00 PROC

ATOM 4921 N SER X 654 1. .890 -9 .068 -6. .656 0. .00 0. .00 PROC

ATOM 4922 HN SER X 654 2. .681 -9 .367 -6. .127 0. .00 0. .00 PROC

ATOM 4923 CA SER X 654 1. .618 -9 .985 -7. .821 0. .00 0. .00 PROC

ATOM 4924 HA SER X 654 1. .604 -9 .255 -8. .617 0. .00 0. .00 PROC

ATOM 4925 CB SER X 654 2. .701 -11 .077 -8. .008 0. .00 0. .00 PROC

ATOM 4926 HB1 SER X 654 2 .749 -11 .727 -7. .109 0. .00 0. .00 PROC

ATOM 4927 HB2 SER X 654 2 .594 -11 .578 -8. .993 0. .00 0. .00 PROC

ATOM 4928 OG SER X 654 3. .967 -10 .545 -8. .347 0. .00 0. .00 PROC

ATOM 4929 HG1 SER X 654 4 .325 -10 .100 -7. .576 0. .00 0. .00 PROC

ATOM 4930 C SER X 654 0. .318 -10 .688 -7. .675 0. .00 0. .00 PROC

ATOM 4931 O SER X 654 -0 .554 -10 .483 -8. .500 0. .00 0. .00 PROC

ATOM 4932 N ILE X 655 0. .012 -11 .416 -6. .537 0. .00 0. .00 PROC

ATOM 4933 HN ILE X 655 0. .744 -11 .565 -5. .876 0. .00 0. .00 PROC

ATOM 4934 CA ILE X 655 -1 .274 -11 .961 -6. .251 0. .00 0. .00 PROC

ATOM 4935 HA ILE X 655 -1 .479 -12 .562 -7. .124 0. .00 0. .00 PROC

ATOM 4936 CB ILE X 655 -1 .234 -12 .807 -4. .996 0. .00 0. .00 PROC

ATOM 4937 HB ILE X 655 -0 .913 -12 .144 -4. .164 0. .00 0. .00 PROC

ATOM 4938 CG2 ILE X 655 -2 .649 -13 .339 -4. .624 0. .00 0. .00 PROC

ATOM 4939 HG21 ILE X 655 -3 .052 -13 .943 -5. .465 0. .00 0. .00 PROC

ATOM 4940 HG22 ILE X 655 -2 .647 -14 .037 -3. .759 0. .00 0. .00 PROC

ATOM 4941 HG23 ILE X 655 -3 .376 -12 .602 -4. .222 0. .00 0. .00 PROC

ATOM 4942 CGI ILE X 655 -0 .305 -14 .011 -5. .242 0. .00 0. .00 PROC

ATOM 4943 HG11 ILE X 655 -0 .678 -14 .632 -6. .084 0. .00 0. .00 PROC

ATOM 4944 HG12 ILE X 655 0 .696 -13 .576 -5. .451 0. .00 0. .00 PROC

ATOM 4945 CD ILE X 655 -0 .045 -14 .975 -4. .094 0. .00 0. .00 PROC

ATOM 4946 HD1 ILE X 655 -0 .057 -14 .373 -3. .160 0. .00 0. .00 PROC

ATOM 4947 HD2 ILE X 655 -0 .852 -15 .725 -3. .946 0. .00 0. .00 PROC

ATOM 4948 HD3 ILE X 655 0 .948 -15 .447 -4. .255 0. .00 0. .00 PROC

ATOM 4949 C ILE X 655 -2 .450 -10 .983 -6. .326 0. .00 0. .00 PROC ATOM 4950 O ILE X 655 -3.425 -11.224 -7..018 0..00 0..00 PROC

ATOM 4951 N PHE X 656 -2 .352 -9 .754 -5. .662 0. .00 0. .00 PROC

ATOM 4952 HN PHE X 656 -1 .586 -9 .520 -5. .068 0. .00 0. .00 PROC

ATOM 4953 CA PHE X 656 -3 .338 -8 .690 -5. .769 0. .00 0. .00 PROC

ATOM 4954 HA PHE X 656 -4 .265 -9 .152 -5. .463 0. .00 0. .00 PROC

ATOM 4955 CB PHE X 656 -2 .889 -7 .632 -4. .839 0. .00 0. .00 PROC

ATOM 4956 HB1 PHE X 656 -1 .778 -7 .627 -4. .849 0. .00 0. .00 PROC

ATOM 4957 HB2 PHE X 656 -3 .042 -6 .590 -5. .193 0. .00 0. .00 PROC

ATOM 4958 CG PHE X 656 -3 .478 -7 .767 -3. .485 0. .00 0. .00 PROC

ATOM 4959 CD1 PHE X 656 -4 .440 -6 .878 -2. .962 0. .00 0. .00 PROC

ATOM 4960 HD1 PHE X 656 -4 .888 -6 .183 -3. .657 0. .00 0. .00 PROC

ATOM 4961 CE1 PHE X 656 -4 .997 -7 .081 -1. .692 0. .00 0. .00 PROC

ATOM 4962 HE1 PHE X 656 -5 .830 -6 .476 -1. .366 0. .00 0. .00 PROC

ATOM 4963 CZ PHE X 656 -4 .427 -8 .046 -0. .846 0. .00 0. .00 PROC

ATOM 4964 HZ PHE X 656 -4 .852 -8 .210 0. .133 0. .00 0. .00 PROC

ATOM 4965 CD2 PHE X 656 -2 .974 -8 .740 -2. .671 0. .00 0. .00 PROC

ATOM 4966 HD2 PHE X 656 -2 .166 -9 .380 -2. .992 0. .00 0. .00 PROC

ATOM 4967 CE2 PHE X 656 -3 .377 -8 .877 -1. .365 0. .00 0. .00 PROC

ATOM 4968 HE2 PHE X 656 -2 .998 -9 .674 -0. .742 0. .00 0. .00 PROC

ATOM 4969 C PHE X 656 -3 .593 -8 .152 -7. .150 0. .00 0. .00 PROC

ATOM 4970 O PHE X 656 -4 .713 -8 .004 -7. .700 0. .00 0. .00 PROC

ATOM 4971 N GLY X 657 -2 .529 -7 .890 -7. .877 0. .00 0. .00 PROC

ATOM 4972 HN GLY X 657 -1 .624 -8 .119 -7. .528 0. .00 0. .00 PROC

ATOM 4973 CA GLY X 657 -2 .519 -7 .473 -9. .266 0. .00 0. .00 PROC

ATOM 4974 HA1 GLY X 657 -1 .496 -7 .574 -9. .599 0. .00 0. .00 PROC

ATOM 4975 HA2 GLY X 657 -2 .806 -6 .435 -9. .337 0. .00 0. .00 PROC

ATOM 4976 C GLY X 657 -3 .269 -8 .341 -10. .173 0. .00 0. .00 PROC

ATOM 4977 O GLY X 657 -4 .099 -7 .934 -11. .020 0. .00 0. .00 PROC

ATOM 4978 N ASN X 658 -3 .008 -9 .670 -9. .975 0. .00 0. .00 PROC

ATOM 4979 HN ASN X 658 -2 .364 -10 .007 -9. .292 0. .00 0. .00 PROC

ATOM 4980 CA ASN X 658 -3 .918 -10 .696 -10. .528 0. .00 0. .00 PROC

ATOM 4981 HA ASN X 658 -4 .054 -10 .470 -11. .576 0. .00 0. .00 PROC

ATOM 4982 CB ASN X 658 -3 .179 -12 .105 -10. .355 0. .00 0. .00 PROC

ATOM 4983 HB1 ASN X 658 -2 .594 -12 .288 -9. .428 0. .00 0. .00 PROC

ATOM 4984 HB2 ASN X 658 -3 .974 -12 .881 -10. .346 0. .00 0. .00 PROC

ATOM 4985 CG ASN X 658 -2 .268 -12 .508 -11. .577 0. .00 0. .00 PROC

ATOM 4986 OD1 ASN X 658 -1 .177 -12 .982 -11. .422 0. .00 0. .00 PROC

ATOM 4987 ND2 ASN X 658 -2 .906 -12 .374 -12. .788 0. .00 0. .00 PROC

ATOM 4988 HD21 ASN X 658 -2 .532 -12 .921 -13. .537 0. .00 0. .00 PROC

ATOM 4989 HD22 ASN X 658 -3 .689 -11 .787 -12. .988 0. .00 0. .00 PROC

ATOM 4990 C ASN X 658 -5 .419 -10 .808 -10. .110 0. .00 0. .00 PROC

ATOM 4991 O ASN X 658 -6 .322 -10 .962 -10. .960 0. .00 0. .00 PROC

ATOM 4992 N VAL X 659 -5 .780 -10 .669 -8. .834 0. .00 0. .00 PROC

ATOM 4993 HN VAL X 659 -5 .015 -10 .479 -8. .224 0. .00 0. .00 PROC

ATOM 4994 CA VAL X 659 -7 .154 -10 .827 -8. .329 0. .00 0. .00 PROC

ATOM 4995 HA VAL X 659 -7 .554 -11 .680 -8. .856 0. .00 0. .00 PROC

ATOM 4996 CB VAL X 659 -7 .079 -11 .213 -6. .827 0. .00 0. .00 PROC

ATOM 4997 HB VAL X 659 -6 .047 -11 .585 -6. .649 0. .00 0. .00 PROC

ATOM 4998 CGI VAL X 659 -7 .324 -10 .096 -5. .866 0. .00 0. .00 PROC

ATOM 4999 HG11 VAL X 659 -6 .734 -9 .162 -5. .983 0. .00 0. .00 PROC

ATOM 5000 HG12 VAL X 659 -8 .400 -9 .876 -6. .036 0. .00 0. .00 PROC

ATOM 5001 HG13 VAL X 659 -7 .065 -10 .458 -4. .849 0. .00 0. .00 PROC

ATOM 5002 CG2 VAL X 659 -7 .893 -12 .480 -6. .603 0. .00 0. .00 PROC

ATOM 5003 HG21 VAL X 659 -7 .846 -12 .808 -5. .542 0. .00 0. .00 PROC

ATOM 5004 HG22 VAL X 659 -8 .947 -12 .353 -6. .931 0. .00 0. .00 PROC

ATOM 5005 HG23 VAL X 659 -7 .466 -13 .347 -7. .151 0. .00 0. .00 PROC

ATOM 5006 C VAL X 659 -8 .085 -9 .663 -8. .634 0. .00 0. .00 PROC

ATOM 5007 O VAL X 659 -9 .278 -9 .834 -8. .800 0. .00 0. .00 PROC

ATOM 5008 N SER X 660 -7 .472 -8 .418 -8. .706 0. .00 0. .00 PROC

ATOM 5009 HN SER X 660 -6 .530 -8 .410 -8. .378 0. .00 0. .00 PROC

ATOM 5010 CA SER X 660 -8 .071 -7 .106 -9. .010 0. .00 0. .00 PROC

ATOM 5011 HA SER X 660 -8 .932 -7 .024 -8. .364 0. .00 0. .00 PROC

ATOM 5012 CB SER X 660 -7 .134 -5 .861 -9. .058 0. .00 0. .00 PROC

ATOM 5013 HB1 SER X 660 -6 .503 -5 .796 -9. .970 0. .00 0. .00 PROC

ATOM 5014 HB2 SER X 660 -7 .706 -4 .909 -9. .055 0. .00 0. .00 PROC

ATOM 5015 OG SER X 660 -6 .280 -5 .636 -7. .917 0. .00 0. .00 PROC ATOM 5016 HG1 SER X 660 -5.516 -6.213 -7..979 0..00 0..00 PROC

ATOM 5017 C SER X 660 -8 .766 -7 .095 -10. .374 0. .00 0. .00 PROC

ATOM 5018 O SER X 660 -9 .942 -6 .772 -10. .549 0. .00 0. .00 PROC

ATOM 5019 N ALA X 661 -8 .014 -7 .599 -11. .357 0. .00 0. .00 PROC

ATOM 5020 HN ALA X 661 -7 .169 -8 .070 -11. .114 0. .00 0. .00 PROC

ATOM 5021 CA ALA X 661 -8 .297 -7 .638 -12. .769 0. .00 0. .00 PROC

ATOM 5022 HA ALA X 661 -8 .339 -6 .599 -13. .062 0. .00 0. .00 PROC

ATOM 5023 CB ALA X 661 -7 .225 -8 .201 -13. .678 0. .00 0. .00 PROC

ATOM 5024 HB1 ALA X 661 -7 .431 -7 .902 -14. .728 0. .00 0. .00 PROC

ATOM 5025 HB2 ALA X 661 -6 .224 -7 .766 -13. .472 0. .00 0. .00 PROC

ATOM 5026 HB3 ALA X 661 -7 .191 -9 .311 -13. .714 0. .00 0. .00 PROC

ATOM 5027 C ALA X 661 -9 .536 -8 .355 -13. .229 0. .00 0. .00 PROC

ATOM 5028 O ALA X 661 -10 .179 -7 .964 -14. .183 0. .00 0. .00 PROC

ATOM 5029 N ILE X 662 -9 .899 -9 .404 -12. .576 0. .00 0. .00 PROC

ATOM 5030 HN ILE X 662 -9 .333 -9 .701 -11. .811 0. .00 0. .00 PROC

ATOM 5031 CA ILE X 662 -11 .052 -10 .254 -12. .827 0. .00 0. .00 PROC

ATOM 5032 HA ILE X 662 -11 .230 -10 .315 -13. .891 0. .00 0. .00 PROC

ATOM 5033 CB ILE X 662 -10 .810 -11 .732 -12. .529 0. .00 0. .00 PROC

ATOM 5034 HB ILE X 662 -9 .825 -12 .113 -12. .873 0. .00 0. .00 PROC

ATOM 5035 CG2 ILE X 662 -10 .684 -11 .881 -11. .006 0. .00 0. .00 PROC

ATOM 5036 HG21 ILE X 662 -10 .221 -10 .975 -10. .560 0. .00 0. .00 PROC

ATOM 5037 HG22 ILE X 662 -11 .683 -12 .077 -10. .560 0. .00 0. .00 PROC

ATOM 5038 HG23 ILE X 662 -10 .080 -12 .784 -10. .773 0. .00 0. .00 PROC

ATOM 5039 CGI ILE X 662 -11 .777 -12 .777 -13. .088 0. .00 0. .00 PROC

ATOM 5040 HG11 ILE X 662 -11 .796 -13 .674 -12. .433 0. .00 0. .00 PROC

ATOM 5041 HG12 ILE X 662 -12 .782 -12 .315 -12. .980 0. .00 0. .00 PROC

ATOM 5042 CD ILE X 662 -11 .607 -13 .272 -14. .547 0. .00 0. .00 PROC

ATOM 5043 HD1 ILE X 662 -11 .856 -12 .469 -15. .272 0. .00 0. .00 PROC

ATOM 5044 HD2 ILE X 662 -10 .586 -13 .670 -14. .729 0. .00 0. .00 PROC

ATOM 5045 HD3 ILE X 662 -12 .244 -14 .183 -14. .532 0. .00 0. .00 PROC

ATOM 5046 C ILE X 662 -12 .387 -9 .637 -12. .381 0. .00 0. .00 PROC

ATOM 5047 O ILE X 662 -13 .318 -9 .641 -13. .110 0. .00 0. .00 PROC

ATOM 5048 N ILE X 663 -12 .443 -9 .127 -11. .146 0. .00 0. .00 PROC

ATOM 5049 HN ILE X 663 -11 .656 -8 .988 -10. .550 0. .00 0. .00 PROC

ATOM 5050 CA ILE X 663 -13 .703 -8 .713 -10. .508 0. .00 0. .00 PROC

ATOM 5051 HA ILE X 663 -14 .494 -9 .376 -10. .826 0. .00 0. .00 PROC

ATOM 5052 CB ILE X 663 -13 .635 -8 .778 -8. .947 0. .00 0. .00 PROC

ATOM 5053 HB ILE X 663 -12 .830 -8 .130 -8. .540 0. .00 0. .00 PROC

ATOM 5054 CG2 ILE X 663 -14 .975 -8 .440 -8. .273 0. .00 0. .00 PROC

ATOM 5055 HG21 ILE X 663 -15 .052 -8 .872 -7. .253 0. .00 0. .00 PROC

ATOM 5056 HG22 ILE X 663 -15 .194 -7 .358 -8. .402 0. .00 0. .00 PROC

ATOM 5057 HG23 ILE X 663 -15 .806 -8 .925 -8. .829 0. .00 0. .00 PROC

ATOM 5058 CGI ILE X 663 -13 .240 -10 .204 -8. .538 0. .00 0. .00 PROC

ATOM 5059 HG11 ILE X 663 -12 .250 -10 .347 -9. .023 0. .00 0. .00 PROC

ATOM 5060 HG12 ILE X 663 -13 .029 -10 .188 -7. .448 0. .00 0. .00 PROC

ATOM 5061 CD ILE X 663 -14 .370 -11 .168 -8. .844 0. .00 0. .00 PROC

ATOM 5062 HD1 ILE X 663 -15 .142 -11 .332 -8. .063 0. .00 0. .00 PROC

ATOM 5063 HD2 ILE X 663 -14 .953 -10 .934 -9. .761 0. .00 0. .00 PROC

ATOM 5064 HD3 ILE X 663 -13 .818 -12 .098 -9. .096 0. .00 0. .00 PROC

ATOM 5065 C ILE X 663 -14 .040 -7 .287 -10. .997 0. .00 0. .00 PROC

ATOM 5066 O ILE X 663 -15 .228 -6 .820 -10. .975 0. .00 0. .00 PROC

ATOM 5067 N GLN X 664 -13 .098 -6 .582 -11. .618 0. .00 0. .00 PROC

ATOM 5068 HN GLN X 664 -12 .154 -6 .882 -11. .504 0. .00 0. .00 PROC

ATOM 5069 CA GLN X 664 -13 .283 -5 .534 -12. .606 0. .00 0. .00 PROC

ATOM 5070 HA GLN X 664 -13 .809 -4 .726 -12. .120 0. .00 0. .00 PROC

ATOM 5071 CB GLN X 664 -11 .914 -4 .922 -13. .112 0. .00 0. .00 PROC

ATOM 5072 HB1 GLN X 664 -11 .208 -5 .726 -13. .413 0. .00 0. .00 PROC

ATOM 5073 HB2 GLN X 664 -12 .130 -4 .375 -14. .054 0. .00 0. .00 PROC

ATOM 5074 CG GLN X 664 -11 .110 -4 .106 -12. .155 0. .00 0. .00 PROC

ATOM 5075 HG1 GLN X 664 -11 .659 -3 .144 -12. .062 0. .00 0. .00 PROC

ATOM 5076 HG2 GLN X 664 -11 .085 -4 .519 -11. .124 0. .00 0. .00 PROC

ATOM 5077 CD GLN X 664 -9 .728 -3 .703 -12. .491 0. .00 0. .00 PROC

ATOM 5078 OE1 GLN X 664 -9 .013 -3 .151 -11. .648 0. .00 0. .00 PROC

ATOM 5079 NE2 GLN X 664 -9 .260 -3 .828 -13. .805 0. .00 0. .00 PROC

ATOM 5080 HE21 GLN X 664 -8 .271 -3 .781 -13. .945 0. .00 0. .00 PROC

ATOM 5081 HE22 GLN X 664 -9 .860 -4 .139 -14. .542 0. .00 0. .00 PROC ATOM 5082 C GLN X 664 -14.124 -5.847 -13..839 0..00 0..00 PROC

ATOM 5083 O GLN X 664 -14 .879 -5 .060 -14. .349 0. .00 0. .00 PROC

ATOM 5084 N ARG X 665 -13 .925 -7 .056 -14. .353 0. .00 0. .00 PROC

ATOM 5085 HN ARG X 665 -13 .277 -7 .650 -13. .883 0. .00 0. .00 PROC

ATOM 5086 CA ARG X 665 -14 .592 -7 .560 -15. .537 0. .00 0. .00 PROC

ATOM 5087 HA ARG X 665 -14 .671 -6 .746 -16. .242 0. .00 0. .00 PROC

ATOM 5088 CB ARG X 665 -13 .581 -8 .563 -16. .189 0. .00 0. .00 PROC

ATOM 5089 HB1 ARG X 665 -12 .582 -8 .283 -15. .791 0. .00 0. .00 PROC

ATOM 5090 HB2 ARG X 665 -13 .713 -9 .586 -15. .777 0. .00 0. .00 PROC

ATOM 5091 CG ARG X 665 -13 .585 -8 .600 -17. .739 0. .00 0. .00 PROC

ATOM 5092 HG1 ARG X 665 -14 .666 -8 .461 -17. .953 0. .00 0. .00 PROC

ATOM 5093 HG2 ARG X 665 -12 .978 -7 .786 -18. .191 0. .00 0. .00 PROC

ATOM 5094 CD ARG X 665 -12 .887 -9 .934 -18. .263 0. .00 0. .00 PROC

ATOM 5095 HD1 ARG X 665 -13 .401 -10 .711 -17. .658 0. .00 0. .00 PROC

ATOM 5096 HD2 ARG X 665 -13 .034 -10 .088 -19. .354 0. .00 0. .00 PROC

ATOM 5097 NE ARG X 665 -11 .413 -9 .909 -17. .949 0. .00 0. .00 PROC

ATOM 5098 HE ARG X 665 -10 .995 -9 .075 -17. .590 0. .00 0. .00 PROC

ATOM 5099 CZ ARG X 665 -10 .637 -10 .985 -18. .002 0. .00 0. .00 PROC

ATOM 5100 NH1 ARG X 665 -11 .065 -12 .175 -18. .412 0. .00 0. .00 PROC

ATOM 5101 HH11 ARG X 665 -10 .574 -13 .034 -18. .270 0. .00 0. .00 PROC

ATOM 5102 HH12 ARG X 665 -12 .049 -12 .147 -18. .584 0. .00 0. .00 PROC

ATOM 5103 NH2 ARG X 665 -9 .402 -10 .866 -17. .510 0. .00 0. .00 PROC

ATOM 5104 HH21 ARG X 665 -8 .752 -11 .622 -17. .586 0. .00 0. .00 PROC

ATOM 5105 HH22 ARG X 665 -9 .064 -9 .982 -17. .189 0. .00 0. .00 PROC

ATOM 5106 C ARG X 665 -15 .970 -8 .187 -15. .343 0. .00 0. .00 PROC

ATOM 5107 O ARG X 665 -16 .537 -8 .588 -16. .325 0. .00 0. .00 PROC

ATOM 5108 N LEU X 666 -16 .394 -8 .247 -14. .083 0. .00 0. .00 PROC

ATOM 5109 HN LEU X 666 -15 .871 -7 .762 -13. .387 0. .00 0. .00 PROC

ATOM 5110 CA LEU X 666 -17 .611 -8 .833 -13. .642 0. .00 0. .00 PROC

ATOM 5111 HA LEU X 666 -17 .779 -9 .711 -14. .248 0. .00 0. .00 PROC

ATOM 5112 CB LEU X 666 -17 .385 -9 .231 -12. .195 0. .00 0. .00 PROC

ATOM 5113 HB1 LEU X 666 -16 .511 -9 .916 -12. .164 0. .00 0. .00 PROC

ATOM 5114 HB2 LEU X 666 -17 .275 -8 .287 -11. .619 0. .00 0. .00 PROC

ATOM 5115 CG LEU X 666 -18 .502 -10 .074 -11. .615 0. .00 0. .00 PROC

ATOM 5116 HG LEU X 666 -19 .531 -9 .727 -11. .853 0. .00 0. .00 PROC

ATOM 5117 CD1 LEU X 666 -18 .458 -11 .549 -12. .067 0. .00 0. .00 PROC

ATOM 5118 HD11 LEU X 666 -19 .146 -11 .982 -11. .310 0. .00 0. .00 PROC

ATOM 5119 HD12 LEU X 666 -18 .845 -11 .724 -13. .094 0. .00 0. .00 PROC

ATOM 5120 HD13 LEU X 666 -17 .403 -11 .821 -11. .846 0. .00 0. .00 PROC

ATOM 5121 CD2 LEU X 666 -18 .301 -10 .036 -10. .087 0. .00 0. .00 PROC

ATOM 5122 HD21 LEU X 666 -18 .106 -9 .001 -9. .733 0. .00 0. .00 PROC

ATOM 5123 HD22 LEU X 666 -19 .223 -10 .443 -9. .619 0. .00 0. .00 PROC

ATOM 5124 HD23 LEU X 666 -17 .482 -10 .711 -9. .761 0. .00 0. .00 PROC

ATOM 5125 C LEU X 666 -18 .791 -7 .782 -13. .725 0. .00 0. .00 PROC

ATOM 5126 OT1 LEU X 666 -19 .755 -8 .156 -14. .472 0. .00 0. .00 PROC

ATOM 5127 OT2 LEU X 666 -18 .741 -6 .752 -13. .021 0. .00 0. .00 PROC

ATOM 5128 N MET X 554 -18 .521 2 .805 -5. .138 0. .00 0. .00 PROD

ATOM 5129 HT1 MET X 554 -18 .630 2 .011 -5. .802 0. .00 0. .00 PROD

ATOM 5130 HT2 MET X 554 -18 .292 3 .648 -5. .702 0. .00 0. .00 PROD

ATOM 5131 HT3 MET X 554 -19 .432 3 .035 -4. .692 0. .00 0. .00 PROD

ATOM 5132 CA MET X 554 -17 .496 2 .583 -4. .034 0. .00 0. .00 PROD

ATOM 5133 HA MET X 554 -17 .052 1 .609 -4. .181 0. .00 0. .00 PROD

ATOM 5134 CB MET X 554 -16 .380 3 .617 -4. .216 0. .00 0. .00 PROD

ATOM 5135 HB1 MET X 554 -15 .925 3 .586 -5. .229 0. .00 0. .00 PROD

ATOM 5136 HB2 MET X 554 -16 .771 4 .657 -4. .225 0. .00 0. .00 PROD

ATOM 5137 CG MET X 554 -15 .127 3 .497 -3. .300 0. .00 0. .00 PROD

ATOM 5138 HG1 MET X 554 -15 .419 3 .170 -2. .280 0. .00 0. .00 PROD

ATOM 5139 HG2 MET X 554 -14 .517 2 .622 -3. .612 0. .00 0. .00 PROD

ATOM 5140 C MET X 554 -18 .057 2 .453 -2. .605 0. .00 0. .00 PROD

ATOM 5141 O MET X 554 -18 .195 1 .328 -2. .126 0. .00 0. .00 PROD

ATOM 5142 N CYS X 555 -18 .293 3 .582 -1. .859 0. .00 0. .00 PROD

ATOM 5143 HN CYS X 555 -18 .276 4 .500 -2. .249 0. .00 0. .00 PROD

ATOM 5144 CA CYS X 555 -18 .691 3 .640 -0. .463 0. .00 0. .00 PROD

ATOM 5145 HA CYS X 555 -17 .880 3 .173 0. .075 0. .00 0. .00 PROD

ATOM 5146 CB CYS X 555 -18 .832 5 .097 0. .102 0. .00 0. .00 PROD

ATOM 5147 HB1 CYS X 555 -18 .000 5 .753 -0. .232 0. .00 0. .00 PROD ATOM 5148 HB2 CYS X 555 -19.707 5.540 -0..420 0..00 0..00 PROD

ATOM 5149 C CYS X 555 -19 .990 2 .921 -0. .152 0. .00 0. .00 PROD

ATOM 5150 O CYS X 555 -20 .164 2 .172 0. .809 0. .00 0. .00 PROD

ATOM 5151 N THR X 556 -21 .040 3 .207 -0. .974 0. .00 0. .00 PROD

ATOM 5152 HN THR X 556 -20 .944 3 .788 -1. .779 0. .00 0. .00 PROD

ATOM 5153 CA THR X 556 -22 .401 2 .572 -0. .723 0. .00 0. .00 PROD

ATOM 5154 HA THR X 556 -22 .749 2 .806 0. .272 0. .00 0. .00 PROD

ATOM 5155 CB THR X 556 -23 .494 3 .081 -1. .618 0. .00 0. .00 PROD

ATOM 5156 HB THR X 556 -24 .415 2 .464 -1. .551 0. .00 0. .00 PROD

ATOM 5157 OG1 THR X 556 -23 .204 3 .283 -3. .000 0. .00 0. .00 PROD

ATOM 5158 HG1 THR X 556 -24 .040 3 .219 -3. .468 0. .00 0. .00 PROD

ATOM 5159 CG2 THR X 556 -23 .957 4 .437 -1. .065 0. .00 0. .00 PROD

ATOM 5160 HG21 THR X 556 -24 .279 4 .334 -0. .007 0. .00 0. .00 PROD

ATOM 5161 HG22 THR X 556 -23 .094 5 .128 -0. .953 0. .00 0. .00 PROD

ATOM 5162 HG23 THR X 556 -24 .721 4 .964 -1. .677 0. .00 0. .00 PROD

ATOM 5163 C THR X 556 -22 .287 1 .047 -0. .788 0. .00 0. .00 PROD

ATOM 5164 O THR X 556 -22 .887 0 .346 0. .044 0. .00 0. .00 PROD

ATOM 5165 N PHE X 557 -21 .538 0 .427 -1. .703 0. .00 0. .00 PROD

ATOM 5166 HN PHE X 557 -21 .084 0 .908 -2. .450 0. .00 0. .00 PROD

ATOM 5167 CA PHE X 557 -21 .379 -1 .000 -1. .903 0. .00 0. .00 PROD

ATOM 5168 HA PHE X 557 -22 .329 -1 .503 -1. .792 0. .00 0. .00 PROD

ATOM 5169 CB PHE X 557 -20 .816 -1 .395 -3. .294 0. .00 0. .00 PROD

ATOM 5170 HB1 PHE X 557 -19 .787 -0 .989 -3. .397 0. .00 0. .00 PROD

ATOM 5171 HB2 PHE X 557 -20 .962 -2 .496 -3. .296 0. .00 0. .00 PROD

ATOM 5172 CG PHE X 557 -21 .775 -0 .832 -4. .475 0. .00 0. .00 PROD

ATOM 5173 CD1 PHE X 557 -21 .170 -0 .568 -5. .674 0. .00 0. .00 PROD

ATOM 5174 HD1 PHE X 557 -20 .130 -0 .836 -5. .791 0. .00 0. .00 PROD

ATOM 5175 CE1 PHE X 557 -21 .930 -0 .168 -6. .822 0. .00 0. .00 PROD

ATOM 5176 HE1 PHE X 557 -21 .509 -0 .129 -7. .816 0. .00 0. .00 PROD

ATOM 5177 CZ PHE X 557 -23 .311 -0 .143 -6. .662 0. .00 0. .00 PROD

ATOM 5178 HZ PHE X 557 -23 .770 0 .242 -7. .561 0. .00 0. .00 PROD

ATOM 5179 CD2 PHE X 557 -23 .165 -0 .637 -4. .336 0. .00 0. .00 PROD

ATOM 5180 HD2 PHE X 557 -23 .709 -0 .811 -3. .419 0. .00 0. .00 PROD

ATOM 5181 CE2 PHE X 557 -23 .895 -0 .286 -5. .416 0. .00 0. .00 PROD

ATOM 5182 HE2 PHE X 557 -24 .972 -0 .204 -5. .402 0. .00 0. .00 PROD

ATOM 5183 C PHE X 557 -20 .515 -1 .544 -0. .789 0. .00 0. .00 PROD

ATOM 5184 O PHE X 557 -20 .728 -2 .591 -0. .280 0. .00 0. .00 PROD

ATOM 5185 N ALA X 558 -19 .510 -0 .787 -0. .366 0. .00 0. .00 PROD

ATOM 5186 HN ALA X 558 -19 .279 0 .128 -0. .688 0. .00 0. .00 PROD

ATOM 5187 CA ALA X 558 -18 .528 -1 .183 0. .616 0. .00 0. .00 PROD

ATOM 5188 HA ALA X 558 -18 .285 -2 .217 0. .421 0. .00 0. .00 PROD

ATOM 5189 CB ALA X 558 -17 .254 -0 .308 0. .536 0. .00 0. .00 PROD

ATOM 5190 HB1 ALA X 558 -17 .523 0 .749 0. .749 0. .00 0. .00 PROD

ATOM 5191 HB2 ALA X 558 -16 .378 -0 .689 1. .103 0. .00 0. .00 PROD

ATOM 5192 HB3 ALA X 558 -16 .971 -0 .357 -0. .537 0. .00 0. .00 PROD

ATOM 5193 C ALA X 558 -19 .148 -1 .250 2. .037 0. .00 0. .00 PROD

ATOM 5194 O ALA X 558 -18 .796 -2 .138 2. .833 0. .00 0. .00 PROD

ATOM 5195 N LEU X 559 -20 .191 -0 .412 2. .394 0. .00 0. .00 PROD

ATOM 5196 HN LEU X 559 -20 .557 0 .278 1. .774 0. .00 0. .00 PROD

ATOM 5197 CA LEU X 559 -20 .744 -0 .472 3. .730 0. .00 0. .00 PROD

ATOM 5198 HA LEU X 559 -19 .956 -0 .458 4. .469 0. .00 0. .00 PROD

ATOM 5199 CB LEU X 559 -21 .623 0 .766 4. .051 0. .00 0. .00 PROD

ATOM 5200 HB1 LEU X 559 -22 .273 0 .926 3. .164 0. .00 0. .00 PROD

ATOM 5201 HB2 LEU X 559 -22 .266 0 .544 4. .929 0. .00 0. .00 PROD

ATOM 5202 CG LEU X 559 -20 .708 1 .960 4. .259 0. .00 0. .00 PROD

ATOM 5203 HG LEU X 559 -19 .954 2 .029 3. .446 0. .00 0. .00 PROD

ATOM 5204 CD1 LEU X 559 -21 .568 3 .217 4. .213 0. .00 0. .00 PROD

ATOM 5205 HD11 LEU X 559 -20 .960 4 .116 4. .451 0. .00 0. .00 PROD

ATOM 5206 HD12 LEU X 559 -22 .016 3 .446 3. .222 0. .00 0. .00 PROD

ATOM 5207 HD13 LEU X 559 -22 .403 3 .051 4. .927 0. .00 0. .00 PROD

ATOM 5208 CD2 LEU X 559 -19 .986 1 .827 5. .617 0. .00 0. .00 PROD

ATOM 5209 HD21 LEU X 559 -19 .508 2 .812 5. .808 0. .00 0. .00 PROD

ATOM 5210 HD22 LEU X 559 -20 .810 1 .589 6. .324 0. .00 0. .00 PROD

ATOM 5211 HD23 LEU X 559 -19 .223 1 .030 5. .739 0. .00 0. .00 PROD

ATOM 5212 C LEU X 559 -21 .496 -1 .842 3. .957 0. .00 0. .00 PROD

ATOM 5213 O LEU X 559 -21 .293 -2 .595 4. .946 0. .00 0. .00 PROD ATOM 5214 N ILE X 560 -22.265 -2.327 3..008 0..00 0..00 PROD

ATOM 5215 HN ILE X 560 -22 .499 -1 .735 2. .240 0. .00 0. .00 PROD

ATOM 5216 CA ILE X 560 -22 .869 -3 .682 2. .959 0. .00 0. .00 PROD

ATOM 5217 HA ILE X 560 -23 .481 -3 .821 3. .838 0. .00 0. .00 PROD

ATOM 5218 CB ILE X 560 -23 .665 -3 .918 1. .681 0. .00 0. .00 PROD

ATOM 5219 HB ILE X 560 -23 .014 -3 .874 0. .782 0. .00 0. .00 PROD

ATOM 5220 CG2 ILE X 560 -24 .422 -5 .248 1. .824 0. .00 0. .00 PROD

ATOM 5221 HG21 ILE X 560 -25 .013 -5 .172 2. .762 0. .00 0. .00 PROD

ATOM 5222 HG22 ILE X 560 -25 .190 -5 .400 1. .036 0. .00 0. .00 PROD

ATOM 5223 HG23 ILE X 560 -23 .732 -6 .117 1. .887 0. .00 0. .00 PROD

ATOM 5224 CGI ILE X 560 -24 .706 -2 .784 1. .553 0. .00 0. .00 PROD

ATOM 5225 HG11 ILE X 560 -25 .607 -3 .016 2. .160 0. .00 0. .00 PROD

ATOM 5226 HG12 ILE X 560 -24 .215 -1 .815 1. .783 0. .00 0. .00 PROD

ATOM 5227 CD ILE X 560 -25 .121 -2 .689 0. .068 0. .00 0. .00 PROD

ATOM 5228 HD1 ILE X 560 -24 .153 -2 .658 -0. .476 0. .00 0. .00 PROD

ATOM 5229 HD2 ILE X 560 -25 .657 -3 .585 -0. .312 0. .00 0. .00 PROD

ATOM 5230 HD3 ILE X 560 -25 .619 -1 .735 -0. .209 0. .00 0. .00 PROD

ATOM 5231 C ILE X 560 -21 .818 -4 .762 3. .175 0. .00 0. .00 PROD

ATOM 5232 O ILE X 560 -21 .976 -5 .632 3. .990 0. .00 0. .00 PROD

ATOM 5233 N ALA X 561 -20 .696 -4 .737 2. .404 0. .00 0. .00 PROD

ATOM 5234 HN ALA X 561 -20 .528 -4 .098 1. .657 0. .00 0. .00 PROD

ATOM 5235 CA ALA X 561 -19 .672 -5 .694 2. .616 0. .00 0. .00 PROD

ATOM 5236 HA ALA X 561 -20 .045 -6 .706 2. .554 0. .00 0. .00 PROD

ATOM 5237 CB ALA X 561 -18 .540 -5 .584 1. .596 0. .00 0. .00 PROD

ATOM 5238 HB1 ALA X 561 -18 . Ill -4 .559 1. .637 0. .00 0. .00 PROD

ATOM 5239 HB2 ALA X 561 -17 .811 -6 .417 1. .688 0. .00 0. .00 PROD

ATOM 5240 HB3 ALA X 561 -18 .970 -5 .663 0. .575 0. .00 0. .00 PROD

ATOM 5241 C ALA X 561 -19 .044 -5 .675 4. .050 0. .00 0. .00 PROD

ATOM 5242 O ALA X 561 -18 .949 -6 .700 4. .759 0. .00 0. .00 PROD

ATOM 5243 N HSD X 562 -18 .657 -4 .515 4. .666 0. .00 0. .00 PROD

ATOM 5244 HN HSD X 562 -18 .612 -3 .645 4. .181 0. .00 0. .00 PROD

ATOM 5245 CA HSD X 562 -18 .215 -4 .361 6. .044 0. .00 0. .00 PROD

ATOM 5246 HA HSD X 562 -17 .240 -4 .795 6. .208 0. .00 0. .00 PROD

ATOM 5247 CB HSD X 562 -18 .078 -2 .844 6. .342 0. .00 0. .00 PROD

ATOM 5248 HB1 HSD X 562 -18 .998 -2 .283 6. .072 0. .00 0. .00 PROD

ATOM 5249 HB2 HSD X 562 -18 .023 -2 .703 7. .443 0. .00 0. .00 PROD

ATOM 5250 ND1 HSD X 562 -15 .609 -2 .645 6. .301 0. .00 0. .00 PROD

ATOM 5251 HD1 HSD X 562 -15 .390 -3 .057 7. .185 0. .00 0. .00 PROD

ATOM 5252 CG HSD X 562 -16 .813 -2 .290 5. .737 0. .00 0. .00 PROD

ATOM 5253 CE1 HSD X 562 -14 .620 -2 .023 5. .553 0. .00 0. .00 PROD

ATOM 5254 HE1 HSD X 562 -13 .551 -2 .184 5. .696 0. .00 0. .00 PROD

ATOM 5255 NE2 HSD X 562 -15 .113 -1 .212 4. .598 0. .00 0. .00 PROD

ATOM 5256 CD2 HSD X 562 -16 .497 -1 .422 4. .728 0. .00 0. .00 PROD

ATOM 5257 HD2 HSD X 562 -17 .252 -0 .908 4. .146 0. .00 0. .00 PROD

ATOM 5258 C HSD X 562 -19 .212 -4 .848 7. .123 0. .00 0. .00 PROD

ATOM 5259 O HSD X 562 -18 .806 -5 .575 8. .058 0. .00 0. .00 PROD

ATOM 5260 N TRP X 563 -20 .552 -4 .523 7. .007 0. .00 0. .00 PROD

ATOM 5261 HN TRP X 563 -20 .917 -3 .915 6. .306 0. .00 0. .00 PROD

ATOM 5262 CA TRP X 563 -21 .650 -4 .963 7. .832 0. .00 0. .00 PROD

ATOM 5263 HA TRP X 563 -21 .373 -4 .779 8. .859 0. .00 0. .00 PROD

ATOM 5264 CB TRP X 563 -22 .971 -4 .170 7. .658 0. .00 0. .00 PROD

ATOM 5265 HB1 TRP X 563 -23 .195 -4 .137 6. .570 0. .00 0. .00 PROD

ATOM 5266 HB2 TRP X 563 -23 .681 -4 .745 8. .290 0. .00 0. .00 PROD

ATOM 5267 CG TRP X 563 -23 .017 -2 .732 8. .127 0. .00 0. .00 PROD

ATOM 5268 CD1 TRP X 563 -23 .264 -1 .681 7. .321 0. .00 0. .00 PROD

ATOM 5269 HD1 TRP X 563 -23 .451 -1 .710 6. .257 0. .00 0. .00 PROD

ATOM 5270 NE1 TRP X 563 -23 .217 -0 .533 8. .010 0. .00 0. .00 PROD

ATOM 5271 HE1 TRP X 563 -23 .206 0 .337 7. .568 0. .00 0. .00 PROD

ATOM 5272 CE2 TRP X 563 -22 .994 -0 .825 9. .350 0. .00 0. .00 PROD

ATOM 5273 CD2 TRP X 563 -22 .877 -2 .197 9. .483 0. .00 0. .00 PROD

ATOM 5274 CE3 TRP X 563 -22 .551 -2 .829 10. .623 0. .00 0. .00 PROD

ATOM 5275 HE3 TRP X 563 -22 .456 -3 .902 10. .689 0. .00 0. .00 PROD

ATOM 5276 CZ3 TRP X 563 -22 .349 -2 .023 11. .767 0. .00 0. .00 PROD

ATOM 5277 HZ3 TRP X 563 -22 .285 -2 .514 12. .726 0. .00 0. .00 PROD

ATOM 5278 CZ2 TRP X 563 -22 .768 -0 .045 10. .436 0. .00 0. .00 PROD

ATOM 5279 HZ2 TRP X 563 -22 .981 1 .014 10. .429 0. .00 0. .00 PROD ATOM 5280 CH2 TRP X 563 -22.515 -0.613 11..685 0..00 0..00 PROD

ATOM 5281 HH2 TRP X 563 -22 .354 0 .081 12. .497 0. .00 0. .00 PROD

ATOM 5282 C TRP X 563 -21 .873 -6 .469 7. .843 0. .00 0. .00 PROD

ATOM 5283 O TRP X 563 -22 .269 -7 .082 8. .859 0. .00 0. .00 PROD

ATOM 5284 N LEU X 564 -21 .698 -7 .129 6. .663 0. .00 0. .00 PROD

ATOM 5285 HN LEU X 564 -21 .490 -6 .579 5. .857 0. .00 0. .00 PROD

ATOM 5286 CA LEU X 564 -21 .686 -8 .563 6. .617 0. .00 0. .00 PROD

ATOM 5287 HA LEU X 564 -22 .562 -8 .915 7. .140 0. .00 0. .00 PROD

ATOM 5288 CB LEU X 564 -21 .870 -9 .047 5. .178 0. .00 0. .00 PROD

ATOM 5289 HB1 LEU X 564 -22 .879 -8 .704 4. .861 0. .00 0. .00 PROD

ATOM 5290 HB2 LEU X 564 -21 .140 -8 .587 4. .478 0. .00 0. .00 PROD

ATOM 5291 CG LEU X 564 -21 .767 -10 .515 4. .854 0. .00 0. .00 PROD

ATOM 5292 HG LEU X 564 -20 .741 -10 .812 5. .158 0. .00 0. .00 PROD

ATOM 5293 CD1 LEU X 564 -22 .919 -11 .304 5. .619 0. .00 0. .00 PROD

ATOM 5294 HD11 LEU X 564 -22 .900 -11 .114 6. .714 0. .00 0. .00 PROD

ATOM 5295 HD12 LEU X 564 -23 .872 -10 .815 5. .327 0. .00 0. .00 PROD

ATOM 5296 HD13 LEU X 564 -22 .781 -12 .395 5. .460 0. .00 0. .00 PROD

ATOM 5297 CD2 LEU X 564 -21 .749 -10 .813 3. .388 0. .00 0. .00 PROD

ATOM 5298 HD21 LEU X 564 -21 .020 -10 .145 2. .880 0. .00 0. .00 PROD

ATOM 5299 HD22 LEU X 564 -21 .598 -11 .874 3. .097 0. .00 0. .00 PROD

ATOM 5300 HD23 LEU X 564 -22 .701 -10 .601 2. .856 0. .00 0. .00 PROD

ATOM 5301 C LEU X 564 -20 .500 -9 .199 7. .327 0. .00 0. .00 PROD

ATOM 5302 O LEU X 564 -20 .714 -10 .147 8. .053 0. .00 0. .00 PROD

ATOM 5303 N ALA X 565 -19 .323 -8 .584 7. .101 0. .00 0. .00 PROD

ATOM 5304 HN ALA X 565 -19 .380 -7 .880 6. .398 0. .00 0. .00 PROD

ATOM 5305 CA ALA X 565 -18 .047 -8 .861 7. .806 0. .00 0. .00 PROD

ATOM 5306 HA ALA X 565 -17 .816 -9 .863 7. .473 0. .00 0. .00 PROD

ATOM 5307 CB ALA X 565 -16 .945 -8 .083 7. .273 0. .00 0. .00 PROD

ATOM 5308 HB1 ALA X 565 -16 .991 -7 .041 7. .657 0. .00 0. .00 PROD

ATOM 5309 HB2 ALA X 565 -15 .972 -8 .464 7. .649 0. .00 0. .00 PROD

ATOM 5310 HB3 ALA X 565 -16 .805 -8 .064 6. .171 0. .00 0. .00 PROD

ATOM 5311 C ALA X 565 -18 .236 -8 .802 9. .374 0. .00 0. .00 PROD

ATOM 5312 O ALA X 565 -17 .698 -9 .597 10. .077 0. .00 0. .00 PROD

ATOM 5313 N CYS X 566 -18 .981 -7 .784 9. .842 0. .00 0. .00 PROD

ATOM 5314 HN CYS X 566 -19 .361 -7 .112 9. .210 0. .00 0. .00 PROD

ATOM 5315 CA CYS X 566 -19 .029 -7 .452 11. .282 0. .00 0. .00 PROD

ATOM 5316 HA CYS X 566 -18 .031 -7 .144 11. .554 0. .00 0. .00 PROD

ATOM 5317 CB CYS X 566 -19 .830 -6 .172 11. .591 0. .00 0. .00 PROD

ATOM 5318 HB1 CYS X 566 -20 .890 -6 .338 11. .307 0. .00 0. .00 PROD

ATOM 5319 HB2 CYS X 566 -19 .864 -6 .021 12. .692 0. .00 0. .00 PROD

ATOM 5320 C CYS X 566 -19 .505 -8 .510 12. .183 0. .00 0. .00 PROD

ATOM 5321 O CYS X 566 -19 .094 -8 .566 13. .321 0. .00 0. .00 PROD

ATOM 5322 N ILE X 567 -20 .545 -9 .370 11. .795 0. .00 0. .00 PROD

ATOM 5323 HN ILE X 567 -21 .006 -9 .149 10. .939 0. .00 0. .00 PROD

ATOM 5324 CA ILE X 567 -20 .978 -10 .540 12. .504 0. .00 0. .00 PROD

ATOM 5325 HA ILE X 567 -21 .426 -10 .132 13. .398 0. .00 0. .00 PROD

ATOM 5326 CB ILE X 567 -21 .991 -11 .236 11. .695 0. .00 0. .00 PROD

ATOM 5327 HB ILE X 567 -21 .527 -11 .919 10. .952 0. .00 0. .00 PROD

ATOM 5328 CG2 ILE X 567 -22 .916 -12 .125 12. .579 0. .00 0. .00 PROD

ATOM 5329 HG21 ILE X 567 -23 .801 -12 .575 12. .081 0. .00 0. .00 PROD

ATOM 5330 HG22 ILE X 567 -22 .178 -12 .847 12. .990 0. .00 0. .00 PROD

ATOM 5331 HG23 ILE X 567 -23 .354 -11 .484 13. .373 0. .00 0. .00 PROD

ATOM 5332 CGI ILE X 567 -23 .023 -10 .216 10. .965 0. .00 0. .00 PROD

ATOM 5333 HG11 ILE X 567 -23 .602 -9 .674 11. .743 0. .00 0. .00 PROD

ATOM 5334 HG12 ILE X 567 -22 .566 -9 .377 10. .397 0. .00 0. .00 PROD

ATOM 5335 CD ILE X 567 -23 .954 -10 .978 9. .987 0. .00 0. .00 PROD

ATOM 5336 HD1 ILE X 567 -24 .596 -10 .346 9. .336 0. .00 0. .00 PROD

ATOM 5337 HD2 ILE X 567 -23 .432 -11 .679 9. .301 0. .00 0. .00 PROD

ATOM 5338 HD3 ILE X 567 -24 .601 -11 .694 10. .538 0. .00 0. .00 PROD

ATOM 5339 C ILE X 567 -19 .879 -11 .547 12. .833 0. .00 0. .00 PROD

ATOM 5340 O ILE X 567 -19 .844 -12 .016 13. .975 0. .00 0. .00 PROD

ATOM 5341 N TRP X 568 -18 .945 -11 .836 11. .938 0. .00 0. .00 PROD

ATOM 5342 HN TRP X 568 -19 .051 -11 .616 10. .971 0. .00 0. .00 PROD

ATOM 5343 CA TRP X 568 -17 .817 -12 .663 12. .192 0. .00 0. .00 PROD

ATOM 5344 HA TRP X 568 -18 .153 -13 .642 12. .498 0. .00 0. .00 PROD

ATOM 5345 CB TRP X 568 -16 .945 -12 .913 10. .861 0. .00 0. .00 PROD ATOM 5346 HB1 TRP X 568 -16.696 -11.876 10..548 0..00 0..00 PROD

ATOM 5347 HB2 TRP X 568 -16 .068 -13 .553 11. .099 0. .00 0. .00 PROD

ATOM 5348 CG TRP X 568 -17 .741 -13 .641 9. .863 0. .00 0. .00 PROD

ATOM 5349 CD1 TRP X 568 -18 .384 -13 .182 8. .704 0. .00 0. .00 PROD

ATOM 5350 HD1 TRP X 568 -18 .152 -12 .274 8. .168 0. .00 0. .00 PROD

ATOM 5351 NE1 TRP X 568 -19 .212 -14 .172 8. .159 0. .00 0. .00 PROD

ATOM 5352 HE1 TRP X 568 -19 .947 -14 .000 7. .541 0. .00 0. .00 PROD

ATOM 5353 CE2 TRP X 568 -19 .072 -15 .331 8. .922 0. .00 0. .00 PROD

ATOM 5354 CD2 TRP X 568 -18 .209 -14 .999 9. .986 0. .00 0. .00 PROD

ATOM 5355 CE3 TRP X 568 -17 .885 -15 .917 10. .985 0. .00 0. .00 PROD

ATOM 5356 HE3 TRP X 568 -17 .455 -15 .583 11. .917 0. .00 0. .00 PROD

ATOM 5357 CZ3 TRP X 568 -18 .347 -17 .180 10. .925 0. .00 0. .00 PROD

ATOM 5358 HZ3 TRP X 568 -18 .235 -17 .926 11. .698 0. .00 0. .00 PROD

ATOM 5359 CZ2 TRP X 568 -19 .582 -16 .565 8. .824 0. .00 0. .00 PROD

ATOM 5360 HZ2 TRP X 568 -20 .196 -16 .881 7. .994 0. .00 0. .00 PROD

ATOM 5361 CH2 TRP X 568 -19 .187 -17 .502 9. .834 0. .00 0. .00 PROD

ATOM 5362 HH2 TRP X 568 -19 .721 -18 .439 9. .893 0. .00 0. .00 PROD

ATOM 5363 C TRP X 568 -16 .847 -12 .205 13. .347 0. .00 0. .00 PROD

ATOM 5364 O TRP X 568 -16 .331 -13 .051 14. .080 0. .00 0. .00 PROD

ATOM 5365 N TYR X 569 -16 .591 -10 .895 13. .534 0. .00 0. .00 PROD

ATOM 5366 HN TYR X 569 -17 .005 -10 .208 12. .942 0. .00 0. .00 PROD

ATOM 5367 CA TYR X 569 -15 .831 -10 .346 14. .676 0. .00 0. .00 PROD

ATOM 5368 HA TYR X 569 -14 .964 -10 .990 14. .692 0. .00 0. .00 PROD

ATOM 5369 CB TYR X 569 -15 .211 -9 .019 14. .396 0. .00 0. .00 PROD

ATOM 5370 HB1 TYR X 569 -15 .954 -8 .198 14. .312 0. .00 0. .00 PROD

ATOM 5371 HB2 TYR X 569 -14 .485 -8 .737 15. .188 0. .00 0. .00 PROD

ATOM 5372 CG TYR X 569 -14 .516 -8 .937 13. .082 0. .00 0. .00 PROD

ATOM 5373 CD1 TYR X 569 -15 .181 -8 .822 11. .881 0. .00 0. .00 PROD

ATOM 5374 HD1 TYR X 569 -16 .239 -8 .609 11. .891 0. .00 0. .00 PROD

ATOM 5375 CE1 TYR X 569 -14 .481 -9 .009 10. .644 0. .00 0. .00 PROD

ATOM 5376 HE1 TYR X 569 -14 .954 -8 .675 9. .732 0. .00 0. .00 PROD

ATOM 5377 CZ TYR X 569 -13 .119 -9 .328 10. .700 0. .00 0. .00 PROD

ATOM 5378 OH TYR X 569 -12 .394 -9 .484 9. .488 0. .00 0. .00 PROD

ATOM 5379 HH TYR X 569 -11 .490 -9 .298 9. .752 0. .00 0. .00 PROD

ATOM 5380 CD2 TYR X 569 -13 .175 -9 .347 13. .168 0. .00 0. .00 PROD

ATOM 5381 HD2 TYR X 569 -12 .782 -9 .483 14. .164 0. .00 0. .00 PROD

ATOM 5382 CE2 TYR X 569 -12 .528 -9 .616 11. .932 0. .00 0. .00 PROD

ATOM 5383 HE2 TYR X 569 -11 .477 -9 .851 12. .002 0. .00 0. .00 PROD

ATOM 5384 C TYR X 569 -16 .598 -10 .472 16. .046 0. .00 0. .00 PROD

ATOM 5385 O TYR X 569 -16 .126 -10 .916 17. .065 0. .00 0. .00 PROD

ATOM 5386 N ALA X 570 -17 .903 -10 .106 15. .969 0. .00 0. .00 PROD

ATOM 5387 HN ALA X 570 -18 .316 -10 .044 15. .064 0. .00 0. .00 PROD

ATOM 5388 CA ALA X 570 -18 .852 -9 .978 17. .054 0. .00 0. .00 PROD

ATOM 5389 HA ALA X 570 -18 .497 -9 .253 17. .772 0. .00 0. .00 PROD

ATOM 5390 CB ALA X 570 -20 .163 -9 .434 16. .498 0. .00 0. .00 PROD

ATOM 5391 HB1 ALA X 570 -20 .942 -9 .325 17. .283 0. .00 0. .00 PROD

ATOM 5392 HB2 ALA X 570 -20 .137 -8 .415 16. .055 0. .00 0. .00 PROD

ATOM 5393 HB3 ALA X 570 -20 .632 -10 .130 15. .771 0. .00 0. .00 PROD

ATOM 5394 C ALA X 570 -19 .095 -11 .359 17. .683 0. .00 0. .00 PROD

ATOM 5395 O ALA X 570 -19 .219 -11 .437 18. .904 0. .00 0. .00 PROD

ATOM 5396 N ILE X 571 -19 .277 -12 .408 16. .911 0. .00 0. .00 PROD

ATOM 5397 HN ILE X 571 -19 .261 -12 .273 15. .924 0. .00 0. .00 PROD

ATOM 5398 CA ILE X 571 -19 .875 -13 .677 17. .413 0. .00 0. .00 PROD

ATOM 5399 HA ILE X 571 -20 .882 -13 .467 17. .743 0. .00 0. .00 PROD

ATOM 5400 CB ILE X 571 -20 .082 -14 .661 16. .229 0. .00 0. .00 PROD

ATOM 5401 HB ILE X 571 -20 .682 -14 .014 15. .553 0. .00 0. .00 PROD

ATOM 5402 CG2 ILE X 571 -18 .822 -14 .956 15. .464 0. .00 0. .00 PROD

ATOM 5403 HG21 ILE X 571 -18 .325 -14 .015 15. .144 0. .00 0. .00 PROD

ATOM 5404 HG22 ILE X 571 -18 .040 -15 .514 16. .021 0. .00 0. .00 PROD

ATOM 5405 HG23 ILE X 571 -19 .038 -15 .576 14. .567 0. .00 0. .00 PROD

ATOM 5406 CGI ILE X 571 -20 .866 -15 .974 16. .496 0. .00 0. .00 PROD

ATOM 5407 HG11 ILE X 571 -21 .173 -16 .504 15. .569 0. .00 0. .00 PROD

ATOM 5408 HG12 ILE X 571 -20 .228 -16 .660 17. .093 0. .00 0. .00 PROD

ATOM 5409 CD ILE X 571 -22 .171 -15 .684 17. .187 0. .00 0. .00 PROD

ATOM 5410 HD1 ILE X 571 -22 .748 -16 .629 17. .275 0. .00 0. .00 PROD

ATOM 5411 HD2 ILE X 571 -22 .081 -15 .311 18. .230 0. .00 0. .00 PROD ATOM 5412 HD3 ILE X 571 -22.749 -14.891 16..666 0..00 0..00 PROD

ATOM 5413 C ILE X 571 -19 .243 -14 .322 18. .634 0. .00 0. .00 PROD

ATOM 5414 O ILE X 571 -19 .936 -14 .657 19. .612 0. .00 0. .00 PROD

ATOM 5415 N GLY X 572 -17 .853 -14 .457 18. .713 0. .00 0. .00 PROD

ATOM 5416 HN GLY X 572 -17 .321 -14 .228 17. .902 0. .00 0. .00 PROD

ATOM 5417 CA GLY X 572 -17 .179 -14 .998 19. .920 0. .00 0. .00 PROD

ATOM 5418 HA1 GLY X 572 -16 .169 -15 .224 19. .612 0. .00 0. .00 PROD

ATOM 5419 HA2 GLY X 572 -17 .695 -15 .923 20. .131 0. .00 0. .00 PROD

ATOM 5420 C GLY X 572 -17 .069 -14 .147 21. .098 0. .00 0. .00 PROD

ATOM 5421 O GLY X 572 -16 .575 -14 .517 22. .127 0. .00 0. .00 PROD

ATOM 5422 N ASN X 573 -17 .548 -12 .913 20. .934 0. .00 0. .00 PROD

ATOM 5423 HN ASN X 573 -18 .053 -12 .699 20. .102 0. .00 0. .00 PROD

ATOM 5424 CA ASN X 573 -17 .536 -11 .907 22. .028 0. .00 0. .00 PROD

ATOM 5425 HA ASN X 573 -16 .947 -12 .235 22. .871 0. .00 0. .00 PROD

ATOM 5426 CB ASN X 573 -17 .018 -10 .575 21. .380 0. .00 0. .00 PROD

ATOM 5427 HB1 ASN X 573 -17 .546 -10 .325 20. .434 0. .00 0. .00 PROD

ATOM 5428 HB2 ASN X 573 -17 .146 -9 .737 22. .097 0. .00 0. .00 PROD

ATOM 5429 CG ASN X 573 -15 .467 -10 .773 21. .077 0. .00 0. .00 PROD

ATOM 5430 OD1 ASN X 573 -14 .567 -10 .407 21. .827 0. .00 0. .00 PROD

ATOM 5431 ND2 ASN X 573 -15 .181 -11 .362 19. .894 0. .00 0. .00 PROD

ATOM 5432 HD21 ASN X 573 -14 .225 -11 .283 19. .611 0. .00 0. .00 PROD

ATOM 5433 HD22 ASN X 573 -15 .896 -11 .395 19. .195 0. .00 0. .00 PROD

ATOM 5434 C ASN X 573 -18 .953 -11 .717 22. .573 0. .00 0. .00 PROD

ATOM 5435 O ASN X 573 -19 .220 -10 .994 23. .505 0. .00 0. .00 PROD

ATOM 5436 N MET X 574 -19 .963 -12 .351 22. .100 0. .00 0. .00 PROD

ATOM 5437 HN MET X 574 -19 .772 -12 .779 21. .220 0. .00 0. .00 PROD

ATOM 5438 CA MET X 574 -21 .421 -12 .303 22. .367 0. .00 0. .00 PROD

ATOM 5439 HA MET X 574 -21 .689 -11 .618 23. .158 0. .00 0. .00 PROD

ATOM 5440 CB MET X 574 -22 .281 -11 .967 21. .070 0. .00 0. .00 PROD

ATOM 5441 HB1 MET X 574 -22 .056 -12 .686 20. .253 0. .00 0. .00 PROD

ATOM 5442 HB2 MET X 574 -23 .360 -12 .080 21. .310 0. .00 0. .00 PROD

ATOM 5443 CG MET X 574 -22 .130 -10 .526 20. .558 0. .00 0. .00 PROD

ATOM 5444 HG1 MET X 574 -22 .187 -9 .798 21. .395 0. .00 0. .00 PROD

ATOM 5445 HG2 MET X 574 -21 .166 -10 .411 20. .017 0. .00 0. .00 PROD

ATOM 5446 C MET X 574 -21 .821 -13 .701 22. .822 0. .00 0. .00 PROD

ATOM 5447 O MET X 574 -22 .997 -13 .971 23. .029 0. .00 0. .00 PROD

ATOM 5448 N GLU X 575 -20 .855 -14 .643 22. .912 0. .00 0. .00 PROD

ATOM 5449 HN GLU X 575 -19 .895 -14 .428 22. .750 0. .00 0. .00 PROD

ATOM 5450 CA GLU X 575 -21 .199 -15 .985 23. .351 0. .00 0. .00 PROD

ATOM 5451 HA GLU X 575 -21 .905 -16 .371 22. .631 0. .00 0. .00 PROD

ATOM 5452 CB GLU X 575 -19 .861 -16 .753 23. .245 0. .00 0. .00 PROD

ATOM 5453 HB1 GLU X 575 -19 .374 -16 .665 22. .251 0. .00 0. .00 PROD

ATOM 5454 HB2 GLU X 575 -19 .174 -16 .328 24. .008 0. .00 0. .00 PROD

ATOM 5455 CG GLU X 575 -19 .808 -18 .280 23. .525 0. .00 0. .00 PROD

ATOM 5456 HG1 GLU X 575 -20 .472 -18 .481 24. .393 0. .00 0. .00 PROD

ATOM 5457 HG2 GLU X 575 -20 .146 -18 .765 22. .585 0. .00 0. .00 PROD

ATOM 5458 CD GLU X 575 -18 .410 -18 .851 23. .714 0. .00 0. .00 PROD

ATOM 5459 OE1 GLU X 575 -17 .380 -18 .175 23. .550 0. .00 0. .00 PROD

ATOM 5460 OE2 GLU X 575 -18 .278 -20 .085 24. .003 0. .00 0. .00 PROD

ATOM 5461 C GLU X 575 -21 .624 -16 .014 24. .813 0. .00 0. .00 PROD

ATOM 5462 O GLU X 575 -22 .516 -16 .697 25. .267 0. .00 0. .00 PROD

ATOM 5463 N GLN X 576 -20 .909 -15 .178 25. .670 0. .00 0. .00 PROD

ATOM 5464 HN GLN X 576 -20 .143 -14 .622 25. .357 0. .00 0. .00 PROD

ATOM 5465 CA GLN X 576 -21 .136 -15 .058 27. .109 0. .00 0. .00 PROD

ATOM 5466 HA GLN X 576 -20 .294 -14 .471 27. .445 0. .00 0. .00 PROD

ATOM 5467 CB GLN X 576 -22 .301 -14 .112 27. .382 0. .00 0. .00 PROD

ATOM 5468 HB1 GLN X 576 -23 .134 -14 .389 26. .700 0. .00 0. .00 PROD

ATOM 5469 HB2 GLN X 576 -22 .788 -14 .160 28. .379 0. .00 0. .00 PROD

ATOM 5470 CG GLN X 576 -21 .895 -12 .660 27. .175 0. .00 0. .00 PROD

ATOM 5471 HG1 GLN X 576 -21 .127 -12 .333 27. .908 0. .00 0. .00 PROD

ATOM 5472 HG2 GLN X 576 -21 .452 -12 .487 26. .171 0. .00 0. .00 PROD

ATOM 5473 CD GLN X 576 -23 .108 -11 .666 27. .051 0. .00 0. .00 PROD

ATOM 5474 OE1 GLN X 576 -23 .262 -10 .873 27. .987 0. .00 0. .00 PROD

ATOM 5475 NE2 GLN X 576 -23 .865 -11 .744 25. .943 0. .00 0. .00 PROD

ATOM 5476 HE21 GLN X 576 -24 .662 -11 .141 25. .944 0. .00 0. .00 PROD

ATOM 5477 HE22 GLN X 576 -23 .704 -12 .385 25. .193 0. .00 0. .00 PROD ATOM 5478 C GLN X 576 -21.333 -16.339 27..919 0..00 0..00 PROD

ATOM 5479 O GLN X 576 -22 .414 -16 .540 28. .465 0. .00 0. .00 PROD

ATOM 5480 N PRO X 577 -20 .372 -17 .258 27. .921 0. .00 0. .00 PROD

ATOM 5481 CD PRO X 577 -18 .938 -16 .977 27. .660 0. .00 0. .00 PROD

ATOM 5482 HD1 PRO X 577 -18 .673 -16 .965 26. .581 0. .00 0. .00 PROD

ATOM 5483 HD2 PRO X 577 -18 .621 -16 .088 28. .245 0. .00 0. .00 PROD

ATOM 5484 CA PRO X 577 -20 .544 -18 .617 28. .376 0. .00 0. .00 PROD

ATOM 5485 HA PRO X 577 -21 .340 -19 .021 27. .768 0. .00 0. .00 PROD

ATOM 5486 CB PRO X 577 -19 .201 -19 .299 28. .086 0. .00 0. .00 PROD

ATOM 5487 HB1 PRO X 577 -19 .126 -19 .625 27. .026 0. .00 0. .00 PROD

ATOM 5488 HB2 PRO X 577 -19 .011 -20 .267 28. .597 0. .00 0. .00 PROD

ATOM 5489 CG PRO X 577 -18 .206 -18 .160 28. .302 0. .00 0. .00 PROD

ATOM 5490 HG1 PRO X 577 -17 .233 -18 .361 27. .804 0. .00 0. .00 PROD

ATOM 5491 HG2 PRO X 577 -17 .909 -17 .985 29. .358 0. .00 0. .00 PROD

ATOM 5492 C PRO X 577 -21 .039 -18 .744 29. .824 0. .00 0. .00 PROD

ATOM 5493 O PRO X 577 -20 .402 -18 .165 30. .697 0. .00 0. .00 PROD

ATOM 5494 N HSD X 578 -22 .077 -19 .579 30. .065 0. .00 0. .00 PROD

ATOM 5495 HN HSD X 578 -22 .619 -20 .023 29. .356 0. .00 0. .00 PROD

ATOM 5496 CA HSD X 578 -22 .694 -19 .799 31. .381 0. .00 0. .00 PROD

ATOM 5497 HA HSD X 578 -22 .517 -18 .906 31. .961 0. .00 0. .00 PROD

ATOM 5498 CB HSD X 578 -24 .210 -19 .906 31. .370 0. .00 0. .00 PROD

ATOM 5499 HB1 HSD X 578 -24 .614 -19 .696 32. .383 0. .00 0. .00 PROD

ATOM 5500 HB2 HSD X 578 -24 .698 -19 .067 30. .829 0. .00 0. .00 PROD

ATOM 5501 ND1 HSD X 578 -26 .134 -21 .568 31. .003 0. .00 0. .00 PROD

ATOM 5502 HD1 HSD X 578 -26 .762 -20 .865 31. .336 0. .00 0. .00 PROD

ATOM 5503 CG HSD X 578 -24 .740 -21 .284 30. .968 0. .00 0. .00 PROD

ATOM 5504 CE1 HSD X 578 -26 .314 -22 .839 30. .525 0. .00 0. .00 PROD

ATOM 5505 HE1 HSD X 578 -27 .329 -23 .222 30. .427 0. .00 0. .00 PROD

ATOM 5506 NE2 HSD X 578 -25 .204 -23 .383 30. .136 0. .00 0. .00 PROD

ATOM 5507 CD2 HSD X 578 -24 .221 -22 .430 30. .431 0. .00 0. .00 PROD

ATOM 5508 HD2 HSD X 578 -23 .243 -22 .775 30. .117 0. .00 0. .00 PROD

ATOM 5509 C HSD X 578 -22 .183 -20 .924 32. .217 0. .00 0. .00 PROD

ATOM 5510 O HSD X 578 -22 .809 -21 .432 33. .161 0. .00 0. .00 PROD

ATOM 5511 N MET X 579 -21 .009 -21 .426 31. .760 0. .00 0. .00 PROD

ATOM 5512 HN MET X 579 -20 .594 -21 .069 30. .927 0. .00 0. .00 PROD

ATOM 5513 CA MET X 579 -20 .411 -22 .598 32. .358 0. .00 0. .00 PROD

ATOM 5514 HA MET X 579 -21 .231 -23 .239 32. .647 0. .00 0. .00 PROD

ATOM 5515 CB MET X 579 -19 .427 -23 .200 31. .275 0. .00 0. .00 PROD

ATOM 5516 HB1 MET X 579 -19 .087 -22 .291 30. .734 0. .00 0. .00 PROD

ATOM 5517 HB2 MET X 579 -18 .501 -23 .632 31. .710 0. .00 0. .00 PROD

ATOM 5518 CG MET X 579 -20 .212 -24 .096 30. .181 0. .00 0. .00 PROD

ATOM 5519 HG1 MET X 579 -20 .989 -23 .422 29. .763 0. .00 0. .00 PROD

ATOM 5520 HG2 MET X 579 -19 .546 -24 .403 29. .346 0. .00 0. .00 PROD

ATOM 5521 SD MET X 579 -20 .970 -25 .502 30. .935 0. .00 0. .00 PROD

ATOM 5522 C MET X 579 -19 .516 -22 .275 33. .621 0. .00 0. .00 PROD

ATOM 5523 O MET X 579 -18 .613 -23 .051 34. .025 0. .00 0. .00 PROD

ATOM 5524 N ASP X 580 -19 .668 -21 .045 34. .211 0. .00 0. .00 PROD

ATOM 5525 HN ASP X 580 -20 .282 -20 .466 33. .680 0. .00 0. .00 PROD

ATOM 5526 CA ASP X 580 -18 .906 -20 .525 35. .435 0. .00 0. .00 PROD

ATOM 5527 HA ASP X 580 -19 .538 -19 .683 35. .674 0. .00 0. .00 PROD

ATOM 5528 CB ASP X 580 -18 .824 -21 .466 36. .676 0. .00 0. .00 PROD

ATOM 5529 HB1 ASP X 580 -18 .286 -22 .414 36. .459 0. .00 0. .00 PROD

ATOM 5530 HB2 ASP X 580 -18 .374 -20 .834 37. .471 0. .00 0. .00 PROD

ATOM 5531 CG ASP X 580 -20 .220 -21 .857 37. .051 0. .00 0. .00 PROD

ATOM 5532 OD1 ASP X 580 -21 .027 -20 .933 37. .262 0. .00 0. .00 PROD

ATOM 5533 OD2 ASP X 580 -20 .451 -23 .072 37. .429 0. .00 0. .00 PROD

ATOM 5534 C ASP X 580 -17 .530 -19 .972 35. .009 0. .00 0. .00 PROD

ATOM 5535 O ASP X 580 -17 .011 -20 .143 33. .900 0. .00 0. .00 PROD

ATOM 5536 N SER X 581 -16 .850 -19 .189 35. .745 0. .00 0. .00 PROD

ATOM 5537 HN SER X 581 -15 .996 -19 .021 35. .259 0. .00 0. .00 PROD

ATOM 5538 CA SER X 581 -17 .029 -18 .456 36. .990 0. .00 0. .00 PROD

ATOM 5539 HA SER X 581 -17 .987 -18 .580 37. .473 0. .00 0. .00 PROD

ATOM 5540 CB SER X 581 -16 .076 -19 .080 38. .100 0. .00 0. .00 PROD

ATOM 5541 HB1 SER X 581 -16 .249 -20 .142 38. .374 0. .00 0. .00 PROD

ATOM 5542 HB2 SER X 581 -15 .060 -18 .970 37. .664 0. .00 0. .00 PROD

ATOM 5543 OG SER X 581 -16 .283 -18 .306 39. .286 0. .00 0. .00 PROD ATOM 5544 HG1 SER X 581 -15.667 -18.717 39..897 0..00 0..00 PROD

ATOM 5545 C SER X 581 -16 .617 -17 .080 36. .679 0. .00 0. .00 PROD

ATOM 5546 O SER X 581 -15 .468 -16 .905 36. .281 0. .00 0. .00 PROD

ATOM 5547 N ARG X 582 -17 .513 -16 .064 36. .898 0. .00 0. .00 PROD

ATOM 5548 HN ARG X 582 -18 .327 -16 .247 37. .443 0. .00 0. .00 PROD

ATOM 5549 CA ARG X 582 -17 .275 -14 .595 36. .653 0. .00 0. .00 PROD

ATOM 5550 HA ARG X 582 -17 .035 -14 .436 35. .612 0. .00 0. .00 PROD

ATOM 5551 CB ARG X 582 -18 .475 -13 .566 36. .942 0. .00 0. .00 PROD

ATOM 5552 HB1 ARG X 582 -19 .394 -14 .092 36. .607 0. .00 0. .00 PROD

ATOM 5553 HB2 ARG X 582 -18 .594 -13 .517 38. .046 0. .00 0. .00 PROD

ATOM 5554 CG ARG X 582 -18 .319 -12 .162 36. .311 0. .00 0. .00 PROD

ATOM 5555 HG1 ARG X 582 -17 .471 -11 .590 36. .745 0. .00 0. .00 PROD

ATOM 5556 HG2 ARG X 582 -18 .123 -12 .346 35. .233 0. .00 0. .00 PROD

ATOM 5557 CD ARG X 582 -19 .619 -11 .347 36. .414 0. .00 0. .00 PROD

ATOM 5558 HD1 ARG X 582 -19 .719 -10 .497 35. .706 0. .00 0. .00 PROD

ATOM 5559 HD2 ARG X 582 -20 .447 -12 .026 36. .118 0. .00 0. .00 PROD

ATOM 5560 NE ARG X 582 -19 .817 -10 .979 37. .911 0. .00 0. .00 PROD

ATOM 5561 HE ARG X 582 -20 .167 -11 .635 38. .580 0. .00 0. .00 PROD

ATOM 5562 CZ ARG X 582 -19 .271 -9 .789 38. .432 0. .00 0. .00 PROD

ATOM 5563 NH1 ARG X 582 -18 .441 -8 .989 37. .868 0. .00 0. .00 PROD

ATOM 5564 HH11 ARG X 582 -18 .170 -8 .205 38. .426 0. .00 0. .00 PROD

ATOM 5565 HH12 ARG X 582 -18 .092 -9 .113 36. .939 0. .00 0. .00 PROD

ATOM 5566 NH2 ARG X 582 -19 .618 -9 .413 39. .661 0. .00 0. .00 PROD

ATOM 5567 HH21 ARG X 582 -18 .957 -8 .783 40. .069 0. .00 0. .00 PROD

ATOM 5568 HH22 ARG X 582 -20 .042 -10 .133 40. .210 0. .00 0. .00 PROD

ATOM 5569 C ARG X 582 -16 .104 -13 .979 37. .400 0. .00 0. .00 PROD

ATOM 5570 O ARG X 582 -15 .218 -13 .530 36. .753 0. .00 0. .00 PROD

ATOM 5571 N ILE X 583 -16 .101 -14 .099 38. .731 0. .00 0. .00 PROD

ATOM 5572 HN ILE X 583 -16 .937 -14 .527 39. .066 0. .00 0. .00 PROD

ATOM 5573 CA ILE X 583 -15 .040 -13 .604 39. .593 0. .00 0. .00 PROD

ATOM 5574 HA ILE X 583 -14 .775 -12 .581 39. .372 0. .00 0. .00 PROD

ATOM 5575 CB ILE X 583 -15 .486 -13 .567 41. .017 0. .00 0. .00 PROD

ATOM 5576 HB ILE X 583 -15 .725 -14 .614 41. .299 0. .00 0. .00 PROD

ATOM 5577 CG2 ILE X 583 -14 .348 -13 .141 41. .978 0. .00 0. .00 PROD

ATOM 5578 HG21 ILE X 583 -13 .478 -13 .830 42. .033 0. .00 0. .00 PROD

ATOM 5579 HG22 ILE X 583 -13 .931 -12 .155 41. .680 0. .00 0. .00 PROD

ATOM 5580 HG23 ILE X 583 -14 .870 -13 .163 42. .959 0. .00 0. .00 PROD

ATOM 5581 CGI ILE X 583 -16 .821 -12 .764 41. .261 0. .00 0. .00 PROD

ATOM 5582 HG11 ILE X 583 -17 .600 -13 .047 40. .521 0. .00 0. .00 PROD

ATOM 5583 HG12 ILE X 583 -17 .237 -13 .101 42. .235 0. .00 0. .00 PROD

ATOM 5584 CD ILE X 583 -16 .697 -11 .275 41. .234 0. .00 0. .00 PROD

ATOM 5585 HD1 ILE X 583 -15 .967 -10 .824 41. .939 0. .00 0. .00 PROD

ATOM 5586 HD2 ILE X 583 -16 .178 -10 .888 40. .332 0. .00 0. .00 PROD

ATOM 5587 HD3 ILE X 583 -17 .654 -10 .751 41. .442 0. .00 0. .00 PROD

ATOM 5588 C ILE X 583 -13 .804 -14 .453 39. .446 0. .00 0. .00 PROD

ATOM 5589 O ILE X 583 -12 .661 -13 .962 39. .431 0. .00 0. .00 PROD

ATOM 5590 N GLY X 584 -14 .046 -15 .811 39. .275 0. .00 0. .00 PROD

ATOM 5591 HN GLY X 584 -14 .993 -16 .122 39. .248 0. .00 0. .00 PROD

ATOM 5592 CA GLY X 584 -12 .966 -16 .788 39. .279 0. .00 0. .00 PROD

ATOM 5593 HA1 GLY X 584 -13 .411 -17 .769 39. .210 0. .00 0. .00 PROD

ATOM 5594 HA2 GLY X 584 -12 .322 -16 .716 40. .143 0. .00 0. .00 PROD

ATOM 5595 C GLY X 584 -12 .066 -16 .614 38. .082 0. .00 0. .00 PROD

ATOM 5596 O GLY X 584 -11 .024 -17 .150 38. .232 0. .00 0. .00 PROD

ATOM 5597 N TRP X 585 -12 .337 -15 .946 36. .940 0. .00 0. .00 PROD

ATOM 5598 HN TRP X 585 -13 .211 -15 .502 36. .756 0. .00 0. .00 PROD

ATOM 5599 CA TRP X 585 -11 .388 -15 .728 35. .870 0. .00 0. .00 PROD

ATOM 5600 HA TRP X 585 -10 .959 -16 .688 35. .622 0. .00 0. .00 PROD

ATOM 5601 CB TRP X 585 -12 .037 -15 .062 34. .590 0. .00 0. .00 PROD

ATOM 5602 HB1 TRP X 585 -12 .627 -14 .153 34. .838 0. .00 0. .00 PROD

ATOM 5603 HB2 TRP X 585 -11 .184 -14 .741 33. .956 0. .00 0. .00 PROD

ATOM 5604 CG TRP X 585 -12 .781 -15 .990 33. .669 0. .00 0. .00 PROD

ATOM 5605 CD1 TRP X 585 -12 .295 -17 .159 33. .078 0. .00 0. .00 PROD

ATOM 5606 HD1 TRP X 585 -11 .261 -17 .385 32. .862 0. .00 0. .00 PROD

ATOM 5607 NE1 TRP X 585 -13 .318 -17 .870 32. .473 0. .00 0. .00 PROD

ATOM 5608 HE1 TRP X 585 -13 .298 -18 .552 31. .776 0. .00 0. .00 PROD

ATOM 5609 CE2 TRP X 585 -14 .455 -17 .284 32. .751 0. .00 0. .00 PROD ATOM 5610 CD2 TRP X 585 -14.218 -16.020 33..383 0..00 0..00 PROD

ATOM 5611 CE3 TRP X 585 -15 .281 -15 .166 33. .675 0. .00 0. .00 PROD

ATOM 5612 HE3 TRP X 585 -15 .143 -14 .231 34. .196 0. .00 0. .00 PROD

ATOM 5613 CZ3 TRP X 585 -16 .537 -15 .551 33. .204 0. .00 0. .00 PROD

ATOM 5614 HZ3 TRP X 585 -17 .391 -14 .959 33. .498 0. .00 0. .00 PROD

ATOM 5615 CZ2 TRP X 585 -15 .764 -17 .680 32. .356 0. .00 0. .00 PROD

ATOM 5616 HZ2 TRP X 585 -15 .881 -18 .583 31. .777 0. .00 0. .00 PROD

ATOM 5617 CH2 TRP X 585 -16 .756 -16 .799 32. .501 0. .00 0. .00 PROD

ATOM 5618 HH2 TRP X 585 -17 .766 -17 .066 32. .226 0. .00 0. .00 PROD

ATOM 5619 C TRP X 585 -10 .186 -14 .892 36. .270 0. .00 0. .00 PROD

ATOM 5620 O TRP X 585 -9 .045 -15 .153 35. .744 0. .00 0. .00 PROD

ATOM 5621 N LEU X 586 -10 .399 -13 .930 37. .226 0. .00 0. .00 PROD

ATOM 5622 HN LEU X 586 -11 .315 -13 .789 37. .592 0. .00 0. .00 PROD

ATOM 5623 CA LEU X 586 -9 .464 -13 .048 37. .755 0. .00 0. .00 PROD

ATOM 5624 HA LEU X 586 -8 .829 -12 .642 36. .981 0. .00 0. .00 PROD

ATOM 5625 CB LEU X 586 -10 .206 -11 .918 38. .616 0. .00 0. .00 PROD

ATOM 5626 HB1 LEU X 586 -10 .773 -12 .481 39. .388 0. .00 0. .00 PROD

ATOM 5627 HB2 LEU X 586 -9 .420 -11 .303 39. .103 0. .00 0. .00 PROD

ATOM 5628 CG LEU X 586 -11 .090 -10 .946 37. .795 0. .00 0. .00 PROD

ATOM 5629 HG LEU X 586 -11 .934 -11 .445 37. .272 0. .00 0. .00 PROD

ATOM 5630 CD1 LEU X 586 -11 .670 -9 .960 38. .743 0. .00 0. .00 PROD

ATOM 5631 HD11 LEU X 586 -10 .907 -9 .225 39. .076 0. .00 0. .00 PROD

ATOM 5632 HD12 LEU X 586 -12 .442 -9 .356 38. .222 0. .00 0. .00 PROD

ATOM 5633 HD13 LEU X 586 -12 .018 -10 .441 39. .683 0. .00 0. .00 PROD

ATOM 5634 CD2 LEU X 586 -10 .336 -10 .221 36. .680 0. .00 0. .00 PROD

ATOM 5635 HD21 LEU X 586 -10 .063 -10 .924 35. .864 0. .00 0. .00 PROD

ATOM 5636 HD22 LEU X 586 -11 .014 -9 .447 36. .260 0. .00 0. .00 PROD

ATOM 5637 HD23 LEU X 586 -9 .367 -9 .756 36. .960 0. .00 0. .00 PROD

ATOM 5638 C LEU X 586 -8 .500 -13 .733 38. .714 0. .00 0. .00 PROD

ATOM 5639 O LEU X 586 -7 .375 -13 .260 38. .804 0. .00 0. .00 PROD

ATOM 5640 N HSD X 587 -8 .854 -14 .910 39. .329 0. .00 0. .00 PROD

ATOM 5641 HN HSD X 587 -9 .729 -15 .364 39. .180 0. .00 0. .00 PROD

ATOM 5642 CA HSD X 587 -7 .853 -15 .738 39. .949 0. .00 0. .00 PROD

ATOM 5643 HA HSD X 587 -7 .112 -15 .121 40. .436 0. .00 0. .00 PROD

ATOM 5644 CB HSD X 587 -8 .513 -16 .725 40. .931 0. .00 0. .00 PROD

ATOM 5645 HB1 HSD X 587 -9 .199 -17 .470 40. .474 0. .00 0. .00 PROD

ATOM 5646 HB2 HSD X 587 -7 .785 -17 .339 41. .504 0. .00 0. .00 PROD

ATOM 5647 ND1 HSD X 587 -10 .112 -17 .032 42. .951 0. .00 0. .00 PROD

ATOM 5648 HD1 HSD X 587 -9 .937 -17 .996 43. .152 0. .00 0. .00 PROD

ATOM 5649 CG HSD X 587 -9 .420 -16 .156 42. .064 0. .00 0. .00 PROD

ATOM 5650 CE1 HSD X 587 -10 .742 -16 .170 43. .808 0. .00 0. .00 PROD

ATOM 5651 HE1 HSD X 587 -11 .256 -16 .502 44. .710 0. .00 0. .00 PROD

ATOM 5652 NE2 HSD X 587 -10 .476 -14 .854 43. .558 0. .00 0. .00 PROD

ATOM 5653 CD2 HSD X 587 -9 .680 -14 .874 42. .412 0. .00 0. .00 PROD

ATOM 5654 HD2 HSD X 587 -9 .238 -14 .019 41. .916 0. .00 0. .00 PROD

ATOM 5655 C HSD X 587 -7 .230 -16 .671 38. .913 0. .00 0. .00 PROD

ATOM 5656 O HSD X 587 -6 .049 -16 .982 38. .940 0. .00 0. .00 PROD

ATOM 5657 N ASN X 588 -8 .019 -17 .250 38. .027 0. .00 0. .00 PROD

ATOM 5658 HN ASN X 588 -8 .989 -17 .025 37. .979 0. .00 0. .00 PROD

ATOM 5659 CA ASN X 588 -7 .595 -18 .322 37. .198 0. .00 0. .00 PROD

ATOM 5660 HA ASN X 588 -7 .001 -19 .034 37. .752 0. .00 0. .00 PROD

ATOM 5661 CB ASN X 588 -8 .751 -19 .137 36. .758 0. .00 0. .00 PROD

ATOM 5662 HB1 ASN X 588 -9 .570 -18 .466 36. .419 0. .00 0. .00 PROD

ATOM 5663 HB2 ASN X 588 -8 .577 -19 .711 35. .823 0. .00 0. .00 PROD

ATOM 5664 CG ASN X 588 -9 .271 -20 .071 37. .821 0. .00 0. .00 PROD

ATOM 5665 OD1 ASN X 588 -8 .842 -20 .160 39. .010 0. .00 0. .00 PROD

ATOM 5666 ND2 ASN X 588 -10 .332 -20 .851 37. .405 0. .00 0. .00 PROD

ATOM 5667 HD21 ASN X 588 -10 .865 -21 .484 37. .966 0. .00 0. .00 PROD

ATOM 5668 HD22 ASN X 588 -10 .600 -20 .680 36. .457 0. .00 0. .00 PROD

ATOM 5669 C ASN X 588 -6 .701 -17 .932 35. .994 0. .00 0. .00 PROD

ATOM 5670 O ASN X 588 -5 .957 -18 .779 35. .526 0. .00 0. .00 PROD

ATOM 5671 N LEU X 589 -6 .661 -16 .595 35. .632 0. .00 0. .00 PROD

ATOM 5672 HN LEU X 589 -7 .348 -15 .986 36. .020 0. .00 0. .00 PROD

ATOM 5673 CA LEU X 589 -5 .625 -16 .172 34. .719 0. .00 0. .00 PROD

ATOM 5674 HA LEU X 589 -5 .355 -16 .908 33. .976 0. .00 0. .00 PROD

ATOM 5675 CB LEU X 589 -6 .251 -14 .873 34. .169 0. .00 0. .00 PROD ATOM 5676 HB1 LEU X 589 -7.291 -15.090 33..844 0..00 0..00 PROD

ATOM 5677 HB2 LEU X 589 -6 .275 -14 .117 34. .983 0. .00 0. .00 PROD

ATOM 5678 CG LEU X 589 -5 .504 -14 .369 32. .950 0. .00 0. .00 PROD

ATOM 5679 HG LEU X 589 -4 .515 -14 .066 33. .357 0. .00 0. .00 PROD

ATOM 5680 CD1 LEU X 589 -5 .366 -15 .475 31. .927 0. .00 0. .00 PROD

ATOM 5681 HD11 LEU X 589 -4 .710 -16 .295 32. .290 0. .00 0. .00 PROD

ATOM 5682 HD12 LEU X 589 -6 .364 -15 .890 31. .670 0. .00 0. .00 PROD

ATOM 5683 HD13 LEU X 589 -4 .926 -15 .122 30. .970 0. .00 0. .00 PROD

ATOM 5684 CD2 LEU X 589 -6 .162 -13 .110 32. .421 0. .00 0. .00 PROD

ATOM 5685 HD21 LEU X 589 -7 .179 -13 .412 32. .090 0. .00 0. .00 PROD

ATOM 5686 HD22 LEU X 589 -6 .408 -12 .338 33. .180 0. .00 0. .00 PROD

ATOM 5687 HD23 LEU X 589 -5 .601 -12 .676 31. .565 0. .00 0. .00 PROD

ATOM 5688 C LEU X 589 -4 .310 -15 .868 35. .509 0. .00 0. .00 PROD

ATOM 5689 O LEU X 589 -3 .318 -15 .549 34. .838 0. .00 0. .00 PROD

ATOM 5690 N GLY X 590 -4 .286 -15 .966 36. .869 0. .00 0. .00 PROD

ATOM 5691 HN GLY X 590 -5 .045 -16 .330 37. .403 0. .00 0. .00 PROD

ATOM 5692 CA GLY X 590 -3 .117 -15 .626 37. .638 0. .00 0. .00 PROD

ATOM 5693 HA1 GLY X 590 -3 .377 -15 .772 38. .676 0. .00 0. .00 PROD

ATOM 5694 HA2 GLY X 590 -3 .013 -14 .557 37. .520 0. .00 0. .00 PROD

ATOM 5695 C GLY X 590 -1 .723 -16 .028 37. .336 0. .00 0. .00 PROD

ATOM 5696 O GLY X 590 -0 .874 -15 .166 37. .039 0. .00 0. .00 PROD

ATOM 5697 N ASP X 591 -1 .279 -17 .272 37. .241 0. .00 0. .00 PROD

ATOM 5698 HN ASP X 591 -0 .360 -17 .203 36. .861 0. .00 0. .00 PROD

ATOM 5699 CA ASP X 591 -1 .655 -18 .586 37. .580 0. .00 0. .00 PROD

ATOM 5700 HA ASP X 591 -0 .669 -19 .024 37. .621 0. .00 0. .00 PROD

ATOM 5701 CB ASP X 591 -2 .192 -18 .707 39. .014 0. .00 0. .00 PROD

ATOM 5702 HB1 ASP X 591 -3 .169 -18 .190 39. .132 0. .00 0. .00 PROD

ATOM 5703 HB2 ASP X 591 -2 .345 -19 .755 39. .351 0. .00 0. .00 PROD

ATOM 5704 CG ASP X 591 -1 .154 -18 .132 39. .956 0. .00 0. .00 PROD

ATOM 5705 OD1 ASP X 591 -1 .326 -17 .031 40. .504 0. .00 0. .00 PROD

ATOM 5706 OD2 ASP X 591 -0 .132 -18 .830 40. .106 0. .00 0. .00 PROD

ATOM 5707 C ASP X 591 -2 .416 -19 .322 36. .526 0. .00 0. .00 PROD

ATOM 5708 O ASP X 591 -2 .774 -20 .505 36. .691 0. .00 0. .00 PROD

ATOM 5709 N GLN X 592 -2 .677 -18 .704 35. .382 0. .00 0. .00 PROD

ATOM 5710 HN GLN X 592 -2 .593 -17 .712 35. .346 0. .00 0. .00 PROD

ATOM 5711 CA GLN X 592 -2 .987 -19 .359 34. .075 0. .00 0. .00 PROD

ATOM 5712 HA GLN X 592 -3 .683 -18 .708 33. .567 0. .00 0. .00 PROD

ATOM 5713 CB GLN X 592 -1 .741 -19 .200 33. .197 0. .00 0. .00 PROD

ATOM 5714 HB1 GLN X 592 -0 .885 -19 .682 33. .717 0. .00 0. .00 PROD

ATOM 5715 HB2 GLN X 592 -1 .853 -19 .762 32. .245 0. .00 0. .00 PROD

ATOM 5716 CG GLN X 592 -1 .399 -17 .688 32. .767 0. .00 0. .00 PROD

ATOM 5717 HG1 GLN X 592 -2 .301 -17 .348 32. .213 0. .00 0. .00 PROD

ATOM 5718 HG2 GLN X 592 -1 .192 -16 .990 33. .606 0. .00 0. .00 PROD

ATOM 5719 CD GLN X 592 -0 .090 -17 .713 31. .938 0. .00 0. .00 PROD

ATOM 5720 OE1 GLN X 592 0 .984 -17 .950 32. .433 0. .00 0. .00 PROD

ATOM 5721 NE2 GLN X 592 -0 .244 -17 .468 30. .635 0. .00 0. .00 PROD

ATOM 5722 HE21 GLN X 592 0 .581 -17 .390 30. .075 0. .00 0. .00 PROD

ATOM 5723 HE22 GLN X 592 -1 .133 -17 .230 30. .243 0. .00 0. .00 PROD

ATOM 5724 C GLN X 592 -3 .525 -20 .787 33. .974 0. .00 0. .00 PROD

ATOM 5725 O GLN X 592 -2 .769 -21 .737 33. .628 0. .00 0. .00 PROD

ATOM 5726 N ILE X 593 -4 .826 -21 .019 34. .330 0. .00 0. .00 PROD

ATOM 5727 HN ILE X 593 -5 .294 -20 .242 34. .743 0. .00 0. .00 PROD

ATOM 5728 CA ILE X 593 -5 .442 -22 .337 34. .163 0. .00 0. .00 PROD

ATOM 5729 HA ILE X 593 -4 .861 -23 .013 34. .773 0. .00 0. .00 PROD

ATOM 5730 CB ILE X 593 -6 .768 -22 .359 34. .926 0. .00 0. .00 PROD

ATOM 5731 HB ILE X 593 -7 .311 -21 .485 34. .508 0. .00 0. .00 PROD

ATOM 5732 CG2 ILE X 593 -7 .494 -23 .631 34. .654 0. .00 0. .00 PROD

ATOM 5733 HG21 ILE X 593 -8 .171 -23 .401 33. .804 0. .00 0. .00 PROD

ATOM 5734 HG22 ILE X 593 -6 .811 -24 .506 34. .607 0. .00 0. .00 PROD

ATOM 5735 HG23 ILE X 593 -8 .252 -23 .833 35. .441 0. .00 0. .00 PROD

ATOM 5736 CGI ILE X 593 -6 .674 -22 .130 36. .379 0. .00 0. .00 PROD

ATOM 5737 HG11 ILE X 593 -5 .943 -21 .332 36. .626 0. .00 0. .00 PROD

ATOM 5738 HG12 ILE X 593 -7 .667 -21 .746 36. .696 0. .00 0. .00 PROD

ATOM 5739 CD ILE X 593 -6 .293 -23 .309 37. .302 0. .00 0. .00 PROD

ATOM 5740 HD1 ILE X 593 -5 .388 -23 .719 36. .805 0. .00 0. .00 PROD

ATOM 5741 HD2 ILE X 593 -5 .988 -23 .028 38. .332 0. .00 0. .00 PROD ATOM 5742 HD3 ILE X 593 -7.054 -24. Ill 37..414 0..00 0..00 PROD

ATOM 5743 C ILE X 593 -5 .575 -22 .710 32. .655 0. .00 0. .00 PROD

ATOM 5744 O ILE X 593 -6 .086 -21 .925 31. .847 0. .00 0. .00 PROD

ATOM 5745 N GLY X 594 -5 .151 -23 .931 32. .153 0. .00 0. .00 PROD

ATOM 5746 HN GLY X 594 -4 .650 -24 .468 32. .828 0. .00 0. .00 PROD

ATOM 5747 CA GLY X 594 -5 .086 -24 .162 30. .676 0. .00 0. .00 PROD

ATOM 5748 HA1 GLY X 594 -4 .401 -24 .928 30. .344 0. .00 0. .00 PROD

ATOM 5749 HA2 GLY X 594 -4 .894 -23 .223 30. .177 0. .00 0. .00 PROD

ATOM 5750 C GLY X 594 -6 .404 -24 .583 30. .087 0. .00 0. .00 PROD

ATOM 5751 O GLY X 594 -6 .511 -24 .824 28. .884 0. .00 0. .00 PROD

ATOM 5752 N LYS X 595 -7 .491 -24 .712 30. .850 0. .00 0. .00 PROD

ATOM 5753 HN LYS X 595 -7 .472 -24 .621 31. .843 0. .00 0. .00 PROD

ATOM 5754 CA LYS X 595 -8 .788 -25 .266 30. .456 0. .00 0. .00 PROD

ATOM 5755 HA LYS X 595 -8 .700 -26 .269 30. .066 0. .00 0. .00 PROD

ATOM 5756 CB LYS X 595 -9 .596 -25 .079 31. .759 0. .00 0. .00 PROD

ATOM 5757 HB1 LYS X 595 -9 .464 -24 .007 32. .017 0. .00 0. .00 PROD

ATOM 5758 HB2 LYS X 595 -10 .683 -25 .181 31. .553 0. .00 0. .00 PROD

ATOM 5759 CG LYS X 595 -9 .416 -26 .044 32. .949 0. .00 0. .00 PROD

ATOM 5760 HG1 LYS X 595 -9 .645 -27 .040 32. .516 0. .00 0. .00 PROD

ATOM 5761 HG2 LYS X 595 -8 .365 -25 .996 33. .308 0. .00 0. .00 PROD

ATOM 5762 CD LYS X 595 -10 .365 -25 .758 34. .097 0. .00 0. .00 PROD

ATOM 5763 HD1 LYS X 595 -10 .560 -24 .669 34. .206 0. .00 0. .00 PROD

ATOM 5764 HD2 LYS X 595 -11 .351 -26 .119 33. .733 0. .00 0. .00 PROD

ATOM 5765 CE LYS X 595 -9 .892 -26 .445 35. .338 0. .00 0. .00 PROD

ATOM 5766 HE1 LYS X 595 -9 .565 -27 .485 35. .125 0. .00 0. .00 PROD

ATOM 5767 HE2 LYS X 595 -9 .066 -25 .864 35. .802 0. .00 0. .00 PROD

ATOM 5768 NZ LYS X 595 -11 .006 -26 .512 36. .271 0. .00 0. .00 PROD

ATOM 5769 HZ1 LYS X 595 -11 .199 -25 .512 36. .480 0. .00 0. .00 PROD

ATOM 5770 HZ2 LYS X 595 -11 .859 -26 .915 35. .834 0. .00 0. .00 PROD

ATOM 5771 HZ3 LYS X 595 -10 .699 -27 .089 37. .080 0. .00 0. .00 PROD

ATOM 5772 C LYS X 595 -9 .402 -24 .394 29. .377 0. .00 0. .00 PROD

ATOM 5773 O LYS X 595 -9 .192 -23 .176 29. .411 0. .00 0. .00 PROD

ATOM 5774 N PRO X 596 -10 .225 -24 .836 28. .433 0. .00 0. .00 PROD

ATOM 5775 CD PRO X 596 -10 .571 -26 .195 28. .251 0. .00 0. .00 PROD

ATOM 5776 HD1 PRO X 596 -9 .674 -26 .849 28. .200 0. .00 0. .00 PROD

ATOM 5777 HD2 PRO X 596 -11 .092 -26 .581 29. .153 0. .00 0. .00 PROD

ATOM 5778 CA PRO X 596 -10 .896 -23 .974 27. .472 0. .00 0. .00 PROD

ATOM 5779 HA PRO X 596 -10 .148 -23 .910 26. .696 0. .00 0. .00 PROD

ATOM 5780 CB PRO X 596 -12 .060 -24 .827 26. .872 0. .00 0. .00 PROD

ATOM 5781 HB1 PRO X 596 -12 .448 -24 .687 25. .840 0. .00 0. .00 PROD

ATOM 5782 HB2 PRO X 596 -12 .914 -24 .824 27. .582 0. .00 0. .00 PROD

ATOM 5783 CG PRO X 596 -11 .354 -26 .149 26. .959 0. .00 0. .00 PROD

ATOM 5784 HG1 PRO X 596 -10 .750 -26 .359 26. .051 0. .00 0. .00 PROD

ATOM 5785 HG2 PRO X 596 -12 .157 -26 .917 26. .937 0. .00 0. .00 PROD

ATOM 5786 C PRO X 596 -11 .427 -22 .585 27. .854 0. .00 0. .00 PROD

ATOM 5787 O PRO X 596 -11 .142 -21 .664 27. .094 0. .00 0. .00 PROD

ATOM 5788 N TYR X 597 -12 .182 -22 .358 28. .909 0. .00 0. .00 PROD

ATOM 5789 HN TYR X 597 -12 .314 -23 .019 29. .644 0. .00 0. .00 PROD

ATOM 5790 CA TYR X 597 -12 .772 -21 .036 29. .096 0. .00 0. .00 PROD

ATOM 5791 HA TYR X 597 -12 .953 -20 .454 28. .205 0. .00 0. .00 PROD

ATOM 5792 CB TYR X 597 -14 .169 -21 .105 29. .835 0. .00 0. .00 PROD

ATOM 5793 HB1 TYR X 597 -14 .069 -21 .709 30. .762 0. .00 0. .00 PROD

ATOM 5794 HB2 TYR X 597 -14 .531 -20 .119 30. .197 0. .00 0. .00 PROD

ATOM 5795 CG TYR X 597 -15 .264 -21 .757 28. .989 0. .00 0. .00 PROD

ATOM 5796 CD1 TYR X 597 -15 .943 -21 .058 27. .977 0. .00 0. .00 PROD

ATOM 5797 HD1 TYR X 597 -15 .655 -20 .027 27. .838 0. .00 0. .00 PROD

ATOM 5798 CE1 TYR X 597 -16 .810 -21 .744 27. .203 0. .00 0. .00 PROD

ATOM 5799 HE1 TYR X 597 -17 .316 -21 .275 26. .372 0. .00 0. .00 PROD

ATOM 5800 CZ TYR X 597 -17 .202 -23 .109 27. .448 0. .00 0. .00 PROD

ATOM 5801 OH TYR X 597 -18 .188 -23 .737 26. .648 0. .00 0. .00 PROD

ATOM 5802 HH TYR X 597 -18 .540 -23 .010 26. .129 0. .00 0. .00 PROD

ATOM 5803 CD2 TYR X 597 -15 .582 -23 .116 29. .242 0. .00 0. .00 PROD

ATOM 5804 HD2 TYR X 597 -15 .045 -23 .610 30. .039 0. .00 0. .00 PROD

ATOM 5805 CE2 TYR X 597 -16 .532 -23 .791 28. .444 0. .00 0. .00 PROD

ATOM 5806 HE2 TYR X 597 -16 .573 -24 .843 28. .683 0. .00 0. .00 PROD

ATOM 5807 C TYR X 597 -11 .854 -20 .189 30. .002 0. .00 0. .00 PROD ATOM 5808 O TYR X 597 -12.182 -19.067 30..255 0..00 0..00 PROD

ATOM 5809 N ASN X 598 -10 .742 -20 .757 30. .480 0. .00 0. .00 PROD

ATOM 5810 HN ASN X 598 -10 .613 -21 .720 30. .255 0. .00 0. .00 PROD

ATOM 5811 CA ASN X 598 -9 .857 -20 .096 31. .307 0. .00 0. .00 PROD

ATOM 5812 HA ASN X 598 -10 .315 -19 .186 31. .665 0. .00 0. .00 PROD

ATOM 5813 CB ASN X 598 -9 .413 -20 .822 32. .505 0. .00 0. .00 PROD

ATOM 5814 HB1 ASN X 598 -9 .196 -21 .850 32. .145 0. .00 0. .00 PROD

ATOM 5815 HB2 ASN X 598 -8 .521 -20 .347 32. .968 0. .00 0. .00 PROD

ATOM 5816 CG ASN X 598 -10 .519 -20 .816 33. .574 0. .00 0. .00 PROD

ATOM 5817 OD1 ASN X 598 -10 .702 -19 .808 34. .217 0. .00 0. .00 PROD

ATOM 5818 ND2 ASN X 598 -11 .344 -21 .922 33. .678 0. .00 0. .00 PROD

ATOM 5819 HD21 ASN X 598 -12 .029 -21 .942 34. .405 0. .00 0. .00 PROD

ATOM 5820 HD22 ASN X 598 -11 .315 -22 .740 33. .104 0. .00 0. .00 PROD

ATOM 5821 C ASN X 598 -8 .556 -19 .698 30. .458 0. .00 0. .00 PROD

ATOM 5822 O ASN X 598 -7 .654 -18 .944 30. .972 0. .00 0. .00 PROD

ATOM 5823 N SER X 599 -8 .439 -20 .134 29. .211 0. .00 0. .00 PROD

ATOM 5824 HN SER X 599 -9 .120 -20 .790 28. .896 0. .00 0. .00 PROD

ATOM 5825 CA SER X 599 -7 .368 -19 .886 28. .336 0. .00 0. .00 PROD

ATOM 5826 HA SER X 599 -6 .792 -19 .099 28. .799 0. .00 0. .00 PROD

ATOM 5827 CB SER X 599 -6 .424 -21 .087 28. .172 0. .00 0. .00 PROD

ATOM 5828 HB1 SER X 599 -5 .526 -20 .763 27. .603 0. .00 0. .00 PROD

ATOM 5829 HB2 SER X 599 -6 .064 -21 .466 29. .152 0. .00 0. .00 PROD

ATOM 5830 OG SER X 599 -7 .045 -22 .147 27. .428 0. .00 0. .00 PROD

ATOM 5831 HG1 SER X 599 -6 .521 -22 .950 27. .485 0. .00 0. .00 PROD

ATOM 5832 C SER X 599 -7 .687 -19 .302 26. .954 0. .00 0. .00 PROD

ATOM 5833 O SER X 599 -6 .781 -18 .921 26. .187 0. .00 0. .00 PROD

ATOM 5834 N SER X 600 -8 .970 -19 .338 26. .589 0. .00 0. .00 PROD

ATOM 5835 HN SER X 600 -9 .731 -19 .553 27. .196 0. .00 0. .00 PROD

ATOM 5836 CA SER X 600 -9 .249 -19 .001 25. .230 0. .00 0. .00 PROD

ATOM 5837 HA SER X 600 -8 .533 -19 .458 24. .563 0. .00 0. .00 PROD

ATOM 5838 CB SER X 600 -10 .568 -19 .554 24. .701 0. .00 0. .00 PROD

ATOM 5839 HB1 SER X 600 -11 .433 -19 .218 25. .312 0. .00 0. .00 PROD

ATOM 5840 HB2 SER X 600 -10 .743 -19 .207 23. .660 0. .00 0. .00 PROD

ATOM 5841 OG SER X 600 -10 .567 -20 .958 24. .704 0. .00 0. .00 PROD

ATOM 5842 HG1 SER X 600 -10 .657 -21 .211 25. .626 0. .00 0. .00 PROD

ATOM 5843 C SER X 600 -9 .112 -17 .503 24. .855 0. .00 0. .00 PROD

ATOM 5844 O SER X 600 -8 .704 -17 .192 23. .735 0. .00 0. .00 PROD

ATOM 5845 N GLY X 601 -9 .526 -16 .595 25. .812 0. .00 0. .00 PROD

ATOM 5846 HN GLY X 601 -9 .830 -16 .921 26. .703 0. .00 0. .00 PROD

ATOM 5847 CA GLY X 601 -9 .437 -15 .184 25. .446 0. .00 0. .00 PROD

ATOM 5848 HA1 GLY X 601 -9 .899 -15 .002 24. .487 0. .00 0. .00 PROD

ATOM 5849 HA2 GLY X 601 -8 .370 -15 .024 25. .485 0. .00 0. .00 PROD

ATOM 5850 C GLY X 601 -10 .038 -14 .311 26. .528 0. .00 0. .00 PROD

ATOM 5851 O GLY X 601 -9 .578 -14 .204 27. .657 0. .00 0. .00 PROD

ATOM 5852 N LEU X 602 -11 .053 -13 .556 26. .139 0. .00 0. .00 PROD

ATOM 5853 HN LEU X 602 -11 .502 -13 .513 25. .250 0. .00 0. .00 PROD

ATOM 5854 CA LEU X 602 -11 .832 -12 .794 27. .106 0. .00 0. .00 PROD

ATOM 5855 HA LEU X 602 -11 .088 -12 .135 27. .530 0. .00 0. .00 PROD

ATOM 5856 CB LEU X 602 -12 .743 -11 .925 26. .172 0. .00 0. .00 PROD

ATOM 5857 HB1 LEU X 602 -13 .307 -11 .127 26. .701 0. .00 0. .00 PROD

ATOM 5858 HB2 LEU X 602 -12 .021 -11 .518 25. .431 0. .00 0. .00 PROD

ATOM 5859 CG LEU X 602 -13 .623 -12 .897 25. .349 0. .00 0. .00 PROD

ATOM 5860 HG LEU X 602 -13 .167 -13 .892 25. .161 0. .00 0. .00 PROD

ATOM 5861 CD1 LEU X 602 -14 .901 -13 .219 26. .202 0. .00 0. .00 PROD

ATOM 5862 HD11 LEU X 602 -15 .473 -12 .306 26. .472 0. .00 0. .00 PROD

ATOM 5863 HD12 LEU X 602 -15 .489 -13 .911 25. .563 0. .00 0. .00 PROD

ATOM 5864 HD13 LEU X 602 -14 .626 -13 .841 27. .081 0. .00 0. .00 PROD

ATOM 5865 CD2 LEU X 602 -13 .917 -12 .279 23. .976 0. .00 0. .00 PROD

ATOM 5866 HD21 LEU X 602 -14 .504 -12 .991 23. .357 0. .00 0. .00 PROD

ATOM 5867 HD22 LEU X 602 -14 .462 -11 .312 23. .986 0. .00 0. .00 PROD

ATOM 5868 HD23 LEU X 602 -12 .930 -12 .142 23. .484 0. .00 0. .00 PROD

ATOM 5869 C LEU X 602 -12 .446 -13 .551 28. .278 0. .00 0. .00 PROD

ATOM 5870 O LEU X 602 -12 .600 -14 .795 28. .193 0. .00 0. .00 PROD

ATOM 5871 N GLY X 603 -12 .824 -12 .923 29. .398 0. .00 0. .00 PROD

ATOM 5872 HN GLY X 603 -12 .769 -11 .927 29. .391 0. .00 0. .00 PROD

ATOM 5873 CA GLY X 603 -13 .246 -13 .533 30. .642 0. .00 0. .00 PROD ATOM 5874 HA1 GLY X 603 -12.947 -12.907 31..470 0..00 0..00 PROD

ATOM 5875 HA2 GLY X 603 -12 .800 -14 .515 30. .691 0. .00 0. .00 PROD

ATOM 5876 C GLY X 603 -14 .767 -13 .737 30. .676 0. .00 0. .00 PROD

ATOM 5877 O GLY X 603 -15 .235 -14 .821 30. .305 0. .00 0. .00 PROD

ATOM 5878 N GLY X 604 -15 .617 -12 .764 31. .071 0. .00 0. .00 PROD

ATOM 5879 HN GLY X 604 -16 .605 -12 .894 31. .046 0. .00 0. .00 PROD

ATOM 5880 CA GLY X 604 -15 .246 -11 .408 31. .375 0. .00 0. .00 PROD

ATOM 5881 HA1 GLY X 604 -14 .179 -11 .248 31. .416 0. .00 0. .00 PROD

ATOM 5882 HA2 GLY X 604 -15 .805 -11 .124 32. .254 0. .00 0. .00 PROD

ATOM 5883 C GLY X 604 -15 .785 -10 .529 30. .261 0. .00 0. .00 PROD

ATOM 5884 O GLY X 604 -16 .003 -11 .006 29. .122 0. .00 0. .00 PROD

ATOM 5885 N PRO X 605 -16 .125 -9 .181 30. .447 0. .00 0. .00 PROD

ATOM 5886 CD PRO X 605 -15 .745 -8 .454 31. .696 0. .00 0. .00 PROD

ATOM 5887 HD1 PRO X 605 -16 .453 -8 .656 32. .527 0. .00 0. .00 PROD

ATOM 5888 HD2 PRO X 605 -14 .707 -8 .780 31. .923 0. .00 0. .00 PROD

ATOM 5889 CA PRO X 605 -16 .610 -8 .251 29. .477 0. .00 0. .00 PROD

ATOM 5890 HA PRO X 605 -17 .464 -8 .778 29. .079 0. .00 0. .00 PROD

ATOM 5891 CB PRO X 605 -16 .895 -7 .005 30. .231 0. .00 0. .00 PROD

ATOM 5892 HB1 PRO X 605 -17 .888 -7 .025 30. .729 0. .00 0. .00 PROD

ATOM 5893 HB2 PRO X 605 -16 .998 -6 .053 29. .667 0. .00 0. .00 PROD

ATOM 5894 CG PRO X 605 -15 .856 -6 .987 31. .411 0. .00 0. .00 PROD

ATOM 5895 HG1 PRO X 605 -16 .187 -6 .290 32. .210 0. .00 0. .00 PROD

ATOM 5896 HG2 PRO X 605 -14 .913 -6 .611 30. .959 0. .00 0. .00 PROD

ATOM 5897 C PRO X 605 -15 .605 -7 .973 28. .380 0. .00 0. .00 PROD

ATOM 5898 O PRO X 605 -14 .418 -7 .859 28. .685 0. .00 0. .00 PROD

ATOM 5899 N SER X 606 -16 .010 -7 .887 27. .136 0. .00 0. .00 PROD

ATOM 5900 HN SER X 606 -16 .933 -8 .175 26. .892 0. .00 0. .00 PROD

ATOM 5901 CA SER X 606 -15 .135 -7 .571 25. .959 0. .00 0. .00 PROD

ATOM 5902 HA SER X 606 -14 .119 -7 .367 26. .263 0. .00 0. .00 PROD

ATOM 5903 CB SER X 606 -15 .133 -8 .740 25. .011 0. .00 0. .00 PROD

ATOM 5904 HB1 SER X 606 -14 .530 -9 .545 25. .483 0. .00 0. .00 PROD

ATOM 5905 HB2 SER X 606 -16 .194 -9 .051 24. .894 0. .00 0. .00 PROD

ATOM 5906 OG SER X 606 -14 .565 -8 .345 23. .783 0. .00 0. .00 PROD

ATOM 5907 HG1 SER X 606 -14 .607 -9 .073 23. .158 0. .00 0. .00 PROD

ATOM 5908 C SER X 606 -15 .717 -6 .313 25. .323 0. .00 0. .00 PROD

ATOM 5909 O SER X 606 -16 .920 -6 .098 25. .308 0. .00 0. .00 PROD

ATOM 5910 N ILE X 607 -14 .888 -5 .471 24. .769 0. .00 0. .00 PROD

ATOM 5911 HN ILE X 607 -13 .915 -5 .670 24. .851 0. .00 0. .00 PROD

ATOM 5912 CA ILE X 607 -15 .334 -4 .260 24. .088 0. .00 0. .00 PROD

ATOM 5913 HA ILE X 607 -16 .270 -3 .938 24. .520 0. .00 0. .00 PROD

ATOM 5914 CB ILE X 607 -14 .317 -3 .106 24. .215 0. .00 0. .00 PROD

ATOM 5915 HB ILE X 607 -14 .003 -2 .985 25. .274 0. .00 0. .00 PROD

ATOM 5916 CG2 ILE X 607 -13 .095 -3 .409 23. .302 0. .00 0. .00 PROD

ATOM 5917 HG21 ILE X 607 -12 .709 -4 .426 23. .526 0. .00 0. .00 PROD

ATOM 5918 HG22 ILE X 607 -13 .409 -3 .438 22. .237 0. .00 0. .00 PROD

ATOM 5919 HG23 ILE X 607 -12 .280 -2 .663 23. .423 0. .00 0. .00 PROD

ATOM 5920 CGI ILE X 607 -14 .879 -1 .667 23. .920 0. .00 0. .00 PROD

ATOM 5921 HG11 ILE X 607 -14 .017 -0 .966 23. .888 0. .00 0. .00 PROD

ATOM 5922 HG12 ILE X 607 -15 .320 -1 .674 22. .900 0. .00 0. .00 PROD

ATOM 5923 CD ILE X 607 -15 .955 -1 .216 24. .957 0. .00 0. .00 PROD

ATOM 5924 HD1 ILE X 607 -16 .876 -1 .835 24. .989 0. .00 0. .00 PROD

ATOM 5925 HD2 ILE X 607 -15 .429 -1 .288 25. .933 0. .00 0. .00 PROD

ATOM 5926 HD3 ILE X 607 -16 .404 -0 .202 24. .896 0. .00 0. .00 PROD

ATOM 5927 C ILE X 607 -15 .717 -4 .480 22. .639 0. .00 0. .00 PROD

ATOM 5928 O ILE X 607 -16 .303 -3 .587 21. .968 0. .00 0. .00 PROD

ATOM 5929 N LYS X 608 -15 .496 -5 .729 22. .089 0. .00 0. .00 PROD

ATOM 5930 HN LYS X 608 -15 .027 -6 .455 22. .587 0. .00 0. .00 PROD

ATOM 5931 CA LYS X 608 -15 .695 -6 .108 20. .697 0. .00 0. .00 PROD

ATOM 5932 HA LYS X 608 -15 .458 -5 .397 19. .920 0. .00 0. .00 PROD

ATOM 5933 CB LYS X 608 -14 .886 -7 .368 20. .496 0. .00 0. .00 PROD

ATOM 5934 HB1 LYS X 608 -13 .824 -7 .217 20. .784 0. .00 0. .00 PROD

ATOM 5935 HB2 LYS X 608 -15 .373 -8 .078 21. .199 0. .00 0. .00 PROD

ATOM 5936 CG LYS X 608 -14 .827 -7 .955 19. .103 0. .00 0. .00 PROD

ATOM 5937 HG1 LYS X 608 -14 .246 -8 .900 19. .166 0. .00 0. .00 PROD

ATOM 5938 HG2 LYS X 608 -15 .840 -8 .360 18. .892 0. .00 0. .00 PROD

ATOM 5939 CD LYS X 608 -14 .338 -7 .060 17. .956 0. .00 0. .00 PROD ATOM 5940 HD1 LYS X 608 -14.307 -7.579 16..974 0..00 0..00 PROD

ATOM 5941 HD2 LYS X 608 -15 .065 -6 .227 17. .840 0. .00 0. .00 PROD

ATOM 5942 CE LYS X 608 -13 .014 -6 .403 18. .244 0. .00 0. .00 PROD

ATOM 5943 HE1 LYS X 608 -12 .782 -5 .889 17. .287 0. .00 0. .00 PROD

ATOM 5944 HE2 LYS X 608 -12 .978 -5 .730 19. .127 0. .00 0. .00 PROD

ATOM 5945 NZ LYS X 608 -12 .037 -7 .533 18. .435 0. .00 0. .00 PROD

ATOM 5946 HZ1 LYS X 608 -12 .350 -8 .295 19. .070 0. .00 0. .00 PROD

ATOM 5947 HZ2 LYS X 608 -11 .929 -8 .085 17. .561 0. .00 0. .00 PROD

ATOM 5948 HZ3 LYS X 608 -11 .155 -7 .175 18. .853 0. .00 0. .00 PROD

ATOM 5949 C LYS X 608 -17 .224 -6 .332 20. .340 0. .00 0. .00 PROD

ATOM 5950 O LYS X 608 -17 .724 -6 .336 19. .197 0. .00 0. .00 PROD

ATOM 5951 N ASP X 609 -18 .078 -6 .425 21. .356 0. .00 0. .00 PROD

ATOM 5952 HN ASP X 609 -17 .690 -6 .425 22. .274 0. .00 0. .00 PROD

ATOM 5953 CA ASP X 609 -19 .471 -6 .646 21. .351 0. .00 0. .00 PROD

ATOM 5954 HA ASP X 609 -19 .629 -7 .432 20. .628 0. .00 0. .00 PROD

ATOM 5955 CB ASP X 609 -20 .037 -7 .151 22. .685 0. .00 0. .00 PROD

ATOM 5956 HB1 ASP X 609 -21 .093 -7 .496 22. .711 0. .00 0. .00 PROD

ATOM 5957 HB2 ASP X 609 -19 .533 -8 .134 22. .803 0. .00 0. .00 PROD

ATOM 5958 CG ASP X 609 -19 .692 -6 .327 23. .929 0. .00 0. .00 PROD

ATOM 5959 OD1 ASP X 609 -19 .945 -6 .888 25. .025 0. .00 0. .00 PROD

ATOM 5960 OD2 ASP X 609 -19 .076 -5 .240 23. .760 0. .00 0. .00 PROD

ATOM 5961 C ASP X 609 -20 .264 -5 .456 20. .878 0. .00 0. .00 PROD

ATOM 5962 O ASP X 609 -21 .424 -5 .525 20. .412 0. .00 0. .00 PROD

ATOM 5963 N LYS X 610 -19 .614 -4 .320 21. .009 0. .00 0. .00 PROD

ATOM 5964 HN LYS X 610 -18 .770 -4 .282 21. .538 0. .00 0. .00 PROD

ATOM 5965 CA LYS X 610 -20 .101 -3 .050 20. .598 0. .00 0. .00 PROD

ATOM 5966 HA LYS X 610 -21 .112 -2 .999 20. .974 0. .00 0. .00 PROD

ATOM 5967 CB LYS X 610 -19 .205 -1 .917 21. .162 0. .00 0. .00 PROD

ATOM 5968 HB1 LYS X 610 -18 .156 -2 .003 20. .808 0. .00 0. .00 PROD

ATOM 5969 HB2 LYS X 610 -19 .690 -0 .964 20. .861 0. .00 0. .00 PROD

ATOM 5970 CG LYS X 610 -19 .125 -2 .115 22. .708 0. .00 0. .00 PROD

ATOM 5971 HG1 LYS X 610 -18 .540 -3 .022 22. .969 0. .00 0. .00 PROD

ATOM 5972 HG2 LYS X 610 -18 .589 -1 .193 23. .019 0. .00 0. .00 PROD

ATOM 5973 CD LYS X 610 -20 .415 -2 .134 23. .451 0. .00 0. .00 PROD

ATOM 5974 HD1 LYS X 610 -20 .981 -1 .251 23. .084 0. .00 0. .00 PROD

ATOM 5975 HD2 LYS X 610 -21 .049 -3 .002 23. .170 0. .00 0. .00 PROD

ATOM 5976 CE LYS X 610 -20 .263 -2 .094 24. .983 0. .00 0. .00 PROD

ATOM 5977 HE1 LYS X 610 -19 .671 -1 .184 25. .216 0. .00 0. .00 PROD

ATOM 5978 HE2 LYS X 610 -21 .302 -1 .979 25. .362 0. .00 0. .00 PROD

ATOM 5979 NZ LYS X 610 -19 .583 -3 .298 25. .550 0. .00 0. .00 PROD

ATOM 5980 HZ1 LYS X 610 -19 .290 -3 .964 24. .806 0. .00 0. .00 PROD

ATOM 5981 HZ2 LYS X 610 -18 .771 -3 .021 26. .139 0. .00 0. .00 PROD

ATOM 5982 HZ3 LYS X 610 -20 .299 -3 .742 26. .160 0. .00 0. .00 PROD

ATOM 5983 C LYS X 610 -20 .081 -2 .975 19. .073 0. .00 0. .00 PROD

ATOM 5984 O LYS X 610 -19 .087 -3 .307 18. .447 0. .00 0. .00 PROD

ATOM 5985 N TYR X 611 -21 .153 -2 .537 18. .397 0. .00 0. .00 PROD

ATOM 5986 HN TYR X 611 -21 .996 -2 .186 18. .796 0. .00 0. .00 PROD

ATOM 5987 CA TYR X 611 -21 .136 -2 .483 16. .928 0. .00 0. .00 PROD

ATOM 5988 HA TYR X 611 -20 .849 -3 .481 16. .632 0. .00 0. .00 PROD

ATOM 5989 CB TYR X 611 -22 .545 -2 .221 16. .425 0. .00 0. .00 PROD

ATOM 5990 HB1 TYR X 611 -22 .689 -2 .468 15. .351 0. .00 0. .00 PROD

ATOM 5991 HB2 TYR X 611 -23 .081 -3 .058 16. .922 0. .00 0. .00 PROD

ATOM 5992 CG TYR X 611 -23 .245 -0 .864 16. .699 0. .00 0. .00 PROD

ATOM 5993 CD1 TYR X 611 -24 .374 -0 .806 17. .617 0. .00 0. .00 PROD

ATOM 5994 HD1 TYR X 611 -24 .557 -1 .743 18. .121 0. .00 0. .00 PROD

ATOM 5995 CE1 TYR X 611 -25 .081 0 .364 17. .767 0. .00 0. .00 PROD

ATOM 5996 HE1 TYR X 611 -25 .867 0 .466 18. .500 0. .00 0. .00 PROD

ATOM 5997 CZ TYR X 611 -24 .764 1 .489 17. .015 0. .00 0. .00 PROD

ATOM 5998 OH TYR X 611 -25 .499 2 .695 17. .186 0. .00 0. .00 PROD

ATOM 5999 HH TYR X 611 -26 .144 2 .567 17. .886 0. .00 0. .00 PROD

ATOM 6000 CD2 TYR X 611 -22 .915 0 .275 15. .990 0. .00 0. .00 PROD

ATOM 6001 HD2 TYR X 611 -22 .216 0 .321 15. .167 0. .00 0. .00 PROD

ATOM 6002 CE2 TYR X 611 -23 .659 1 .461 16. .181 0. .00 0. .00 PROD

ATOM 6003 HE2 TYR X 611 -23 .390 2 .206 15. .447 0. .00 0. .00 PROD

ATOM 6004 C TYR X 611 -20 .097 -1 .424 16. .497 0. .00 0. .00 PROD

ATOM 6005 O TYR X 611 -19 .451 -1 .642 15. .484 0. .00 0. .00 PROD ATOM 6006 N VAL X 612 -19.926 -0.276 17..193 0..00 0..00 PROD

ATOM 6007 HN VAL X 612 -20 .475 -0 .097 18. .005 0. .00 0. .00 PROD

ATOM 6008 CA VAL X 612 -18 .949 0 .804 16. .900 0. .00 0. .00 PROD

ATOM 6009 HA VAL X 612 -19 .188 1 .142 15. .903 0. .00 0. .00 PROD

ATOM 6010 CB VAL X 612 -18 .986 1 .933 17. .914 0. .00 0. .00 PROD

ATOM 6011 HB VAL X 612 -18 .432 2 .763 17. .426 0. .00 0. .00 PROD

ATOM 6012 CGI VAL X 612 -20 .461 2 .436 17. .973 0. .00 0. .00 PROD

ATOM 6013 HG11 VAL X 612 -20 .662 3 .501 18. .218 0. .00 0. .00 PROD

ATOM 6014 HG12 VAL X 612 -20 .937 2 .250 16. .986 0. .00 0. .00 PROD

ATOM 6015 HG13 VAL X 612 -21 .053 1 .838 18. .699 0. .00 0. .00 PROD

ATOM 6016 CG2 VAL X 612 -18 .429 1 .604 19. .323 0. .00 0. .00 PROD

ATOM 6017 HG21 VAL X 612 -18 .783 2 .414 19. .996 0. .00 0. .00 PROD

ATOM 6018 HG22 VAL X 612 -18 .737 0 .625 19. .749 0. .00 0. .00 PROD

ATOM 6019 HG23 VAL X 612 -17 .318 1 .609 19. .326 0. .00 0. .00 PROD

ATOM 6020 C VAL X 612 -17 .553 0 .146 16. .797 0. .00 0. .00 PROD

ATOM 6021 O VAL X 612 -16 .823 0 .435 15. .861 0. .00 0. .00 PROD

ATOM 6022 N THR X 613 -17 .233 -0 .791 17. .698 0. .00 0. .00 PROD

ATOM 6023 HN THR X 613 -17 .903 -1 .004 18. .405 0. .00 0. .00 PROD

ATOM 6024 CA THR X 613 -15 .864 -1 .413 17. .709 0. .00 0. .00 PROD

ATOM 6025 HA THR X 613 -15 .046 -0 .709 17. .664 0. .00 0. .00 PROD

ATOM 6026 CB THR X 613 -15 .624 -2 .134 19. .008 0. .00 0. .00 PROD

ATOM 6027 HB THR X 613 -16 .355 -2 .971 18. .998 0. .00 0. .00 PROD

ATOM 6028 OG1 THR X 613 -15 .947 -1 .187 19. .982 0. .00 0. .00 PROD

ATOM 6029 HG1 THR X 613 -16 .106 -1 .628 20. .820 0. .00 0. .00 PROD

ATOM 6030 CG2 THR X 613 -14 .256 -2 .675 19. .291 0. .00 0. .00 PROD

ATOM 6031 HG21 THR X 613 -14 .429 -3 .071 20. .315 0. .00 0. .00 PROD

ATOM 6032 HG22 THR X 613 -13 .864 -3 .384 18. .530 0. .00 0. .00 PROD

ATOM 6033 HG23 THR X 613 -13 .488 -1 .873 19. .319 0. .00 0. .00 PROD

ATOM 6034 C THR X 613 -15 .670 -2 .310 16. .540 0. .00 0. .00 PROD

ATOM 6035 O THR X 613 -14 .575 -2 .393 15. .980 0. .00 0. .00 PROD

ATOM 6036 N ALA X 614 -16 .689 -3 .107 16. .128 0. .00 0. .00 PROD

ATOM 6037 HN ALA X 614 -17 .573 -3 .130 16. .588 0. .00 0. .00 PROD

ATOM 6038 CA ALA X 614 -16 .695 -4 .041 15. .079 0. .00 0. .00 PROD

ATOM 6039 HA ALA X 614 -15 .886 -4 .747 15. .202 0. .00 0. .00 PROD

ATOM 6040 CB ALA X 614 -18 .015 -4 .856 15. .140 0. .00 0. .00 PROD

ATOM 6041 HB1 ALA X 614 -18 .874 -4 .266 14. .754 0. .00 0. .00 PROD

ATOM 6042 HB2 ALA X 614 -17 .803 -5 .775 14. .553 0. .00 0. .00 PROD

ATOM 6043 HB3 ALA X 614 -18 .117 -5 .142 16. .208 0. .00 0. .00 PROD

ATOM 6044 C ALA X 614 -16 .445 -3 .374 13. .749 0. .00 0. .00 PROD

ATOM 6045 O ALA X 614 -15 .879 -3 .921 12. .831 0. .00 0. .00 PROD

ATOM 6046 N LEU X 615 -17 .157 -2 .182 13. .625 0. .00 0. .00 PROD

ATOM 6047 HN LEU X 615 -17 .784 -1 .814 14. .307 0. .00 0. .00 PROD

ATOM 6048 CA LEU X 615 -17 .054 -1 .333 12. .443 0. .00 0. .00 PROD

ATOM 6049 HA LEU X 615 -17 .064 -1 .963 11. .567 0. .00 0. .00 PROD

ATOM 6050 CB LEU X 615 -18 .181 -0 .230 12. .561 0. .00 0. .00 PROD

ATOM 6051 HB1 LEU X 615 -19 .138 -0 .775 12. .704 0. .00 0. .00 PROD

ATOM 6052 HB2 LEU X 615 -17 .963 0 .347 13. .485 0. .00 0. .00 PROD

ATOM 6053 CG LEU X 615 -18 .120 0 .748 11. .315 0. .00 0. .00 PROD

ATOM 6054 HG LEU X 615 -17 .122 1 .234 11. .275 0. .00 0. .00 PROD

ATOM 6055 CD1 LEU X 615 -18 .279 0 .041 9. .988 0. .00 0. .00 PROD

ATOM 6056 HD11 LEU X 615 -19 .333 -0 .306 9. .926 0. .00 0. .00 PROD

ATOM 6057 HD12 LEU X 615 -18 .221 0 .714 9. .106 0. .00 0. .00 PROD

ATOM 6058 HD13 LEU X 615 -17 .473 -0 .694 9. .779 0. .00 0. .00 PROD

ATOM 6059 CD2 LEU X 615 -19 .135 1 .952 11. .460 0. .00 0. .00 PROD

ATOM 6060 HD21 LEU X 615 -18 .933 2 .699 12. .257 0. .00 0. .00 PROD

ATOM 6061 HD22 LEU X 615 -19 .271 2 .552 10. .535 0. .00 0. .00 PROD

ATOM 6062 HD23 LEU X 615 -20 .116 1 .513 11. .740 0. .00 0. .00 PROD

ATOM 6063 C LEU X 615 -15 .665 -0 .664 12. .353 0. .00 0. .00 PROD

ATOM 6064 O LEU X 615 -15 .169 -0 .412 11. .276 0. .00 0. .00 PROD

ATOM 6065 N TYR X 616 -15 .096 -0 .285 13. .520 0. .00 0. .00 PROD

ATOM 6066 HN TYR X 616 -15 .644 -0 .403 14. .345 0. .00 0. .00 PROD

ATOM 6067 CA TYR X 616 -13 .763 0 .316 13. .595 0. .00 0. .00 PROD

ATOM 6068 HA TYR X 616 -13 .727 1 .184 12. .954 0. .00 0. .00 PROD

ATOM 6069 CB TYR X 616 -13 .450 0 .772 15. .060 0. .00 0. .00 PROD

ATOM 6070 HB1 TYR X 616 -14 .229 1 .470 15. .436 0. .00 0. .00 PROD

ATOM 6071 HB2 TYR X 616 -13 .411 -0 .093 15. .756 0. .00 0. .00 PROD ATOM 6072 CG TYR X 616 -12.173 1.484 15..142 0..00 0..00 PROD

ATOM 6073 CD1 TYR X 616 -12 .285 2 .802 14. .705 0. .00 0. .00 PROD

ATOM 6074 HD1 TYR X 616 -13 .246 3 .125 14. .333 0. .00 0. .00 PROD

ATOM 6075 CE1 TYR X 616 -11 .169 3 .639 14. .709 0. .00 0. .00 PROD

ATOM 6076 HE1 TYR X 616 -11 .244 4 .672 14. .403 0. .00 0. .00 PROD

ATOM 6077 CZ TYR X 616 -9 .960 3 .134 15. .128 0. .00 0. .00 PROD

ATOM 6078 OH TYR X 616 -8 .883 4 .059 15. .320 0. .00 0. .00 PROD

ATOM 6079 HH TYR X 616 -9 .332 4 .853 15. .618 0. .00 0. .00 PROD

ATOM 6080 CD2 TYR X 616 -10 .954 0 .994 15. .626 0. .00 0. .00 PROD

ATOM 6081 HD2 TYR X 616 -10 .915 0 .046 16. .143 0. .00 0. .00 PROD

ATOM 6082 CE2 TYR X 616 -9 .804 1 .799 15. .556 0. .00 0. .00 PROD

ATOM 6083 HE2 TYR X 616 -8 .842 1 .454 15. .905 0. .00 0. .00 PROD

ATOM 6084 C TYR X 616 -12 .734 -0 .691 13. .126 0. .00 0. .00 PROD

ATOM 6085 O TYR X 616 -11 .800 -0 .367 12. .408 0. .00 0. .00 PROD

ATOM 6086 N PHE X 617 -12 .940 -1 .937 13. .585 0. .00 0. .00 PROD

ATOM 6087 HN PHE X 617 -13 .672 -2 .183 14. .215 0. .00 0. .00 PROD

ATOM 6088 CA PHE X 617 -12 .023 -3 .005 13. .213 0. .00 0. .00 PROD

ATOM 6089 HA PHE X 617 -11 .054 -2 .537 13. .124 0. .00 0. .00 PROD

ATOM 6090 CB PHE X 617 -12 .169 -4 .216 14. .191 0. .00 0. .00 PROD

ATOM 6091 HB1 PHE X 617 -12 .115 -3 .788 15. .215 0. .00 0. .00 PROD

ATOM 6092 HB2 PHE X 617 -13 .162 -4 .695 14. .048 0. .00 0. .00 PROD

ATOM 6093 CG PHE X 617 -11 .089 -5 .210 13. .875 0. .00 0. .00 PROD

ATOM 6094 CD1 PHE X 617 -9 .826 -4 .907 14. .401 0. .00 0. .00 PROD

ATOM 6095 HD1 PHE X 617 -9 .726 -4 .059 15. .063 0. .00 0. .00 PROD

ATOM 6096 CE1 PHE X 617 -8 .656 -5 .580 13. .933 0. .00 0. .00 PROD

ATOM 6097 HE1 PHE X 617 -7 .653 -5 .296 14. .218 0. .00 0. .00 PROD

ATOM 6098 CZ PHE X 617 -8 .807 -6 .651 12. .975 0. .00 0. .00 PROD

ATOM 6099 HZ PHE X 617 -7 .998 -7 .330 12. .748 0. .00 0. .00 PROD

ATOM 6100 CD2 PHE X 617 -11 .199 -6 .269 12. .942 0. .00 0. .00 PROD

ATOM 6101 HD2 PHE X 617 -12 .189 -6 .457 12. .554 0. .00 0. .00 PROD

ATOM 6102 CE2 PHE X 617 -10 .069 -6 .962 12. .511 0. .00 0. .00 PROD

ATOM 6103 HE2 PHE X 617 -10 .184 -7 .827 11. .874 0. .00 0. .00 PROD

ATOM 6104 C PHE X 617 -12 .174 -3 .469 11. .724 0. .00 0. .00 PROD

ATOM 6105 O PHE X 617 -11 .186 -3 .616 11. .015 0. .00 0. .00 PROD

ATOM 6106 N THR X 618 -13 .383 -3 .627 11. .167 0. .00 0. .00 PROD

ATOM 6107 HN THR X 618 -14 .204 -3 .489 11. .716 0. .00 0. .00 PROD

ATOM 6108 CA THR X 618 -13 .532 -4 .012 9. .776 0. .00 0. .00 PROD

ATOM 6109 HA THR X 618 -12 .935 -4 .907 9. .675 0. .00 0. .00 PROD

ATOM 6110 CB THR X 618 -14 .894 -4 .367 9. .234 0. .00 0. .00 PROD

ATOM 6111 HB THR X 618 -14 .732 -4 .658 8. .174 0. .00 0. .00 PROD

ATOM 6112 OG1 THR X 618 -15 .827 -3 .247 9. .261 0. .00 0. .00 PROD

ATOM 6113 HG1 THR X 618 -16 .693 -3 .477 9. .605 0. .00 0. .00 PROD

ATOM 6114 CG2 THR X 618 -15 .594 -5 .460 9. .950 0. .00 0. .00 PROD

ATOM 6115 HG21 THR X 618 -16 .021 -5 .286 10. .961 0. .00 0. .00 PROD

ATOM 6116 HG22 THR X 618 -16 .525 -5 .738 9. .411 0. .00 0. .00 PROD

ATOM 6117 HG23 THR X 618 -14 .903 -6 .328 10. .017 0. .00 0. .00 PROD

ATOM 6118 C THR X 618 -12 .907 -3 .055 8. .827 0. .00 0. .00 PROD

ATOM 6119 O THR X 618 -12 .150 -3 .551 8. .034 0. .00 0. .00 PROD

ATOM 6120 N PHE X 619 -13 .115 -1 .757 9. .157 0. .00 0. .00 PROD

ATOM 6121 HN PHE X 619 -13 .712 -1 .494 9. .912 0. .00 0. .00 PROD

ATOM 6122 CA PHE X 619 -12 .579 -0 .625 8. .454 0. .00 0. .00 PROD

ATOM 6123 HA PHE X 619 -12 .876 -0 .850 7. .440 0. .00 0. .00 PROD

ATOM 6124 CB PHE X 619 -13 .242 0 .650 8. .801 0. .00 0. .00 PROD

ATOM 6125 HB1 PHE X 619 -14 .345 0 .520 8. .798 0. .00 0. .00 PROD

ATOM 6126 HB2 PHE X 619 -13 .041 1 .057 9. .815 0. .00 0. .00 PROD

ATOM 6127 CG PHE X 619 -12 .964 1 .672 7. .679 0. .00 0. .00 PROD

ATOM 6128 CD1 PHE X 619 -12 .164 2 .772 7. .877 0. .00 0. .00 PROD

ATOM 6129 HD1 PHE X 619 -11 .725 2 .982 8. .841 0. .00 0. .00 PROD

ATOM 6130 CE1 PHE X 619 -11 .831 3 .660 6. .828 0. .00 0. .00 PROD

ATOM 6131 HE1 PHE X 619 -11 .142 4 .485 6. .940 0. .00 0. .00 PROD

ATOM 6132 CZ PHE X 619 -12 .408 3 .441 5. .537 0. .00 0. .00 PROD

ATOM 6133 HZ PHE X 619 -12 .206 4 .133 4. .733 0. .00 0. .00 PROD

ATOM 6134 CD2 PHE X 619 -13 .651 1 .599 6. .501 0. .00 0. .00 PROD

ATOM 6135 HD2 PHE X 619 -14 .404 0 .845 6. .328 0. .00 0. .00 PROD

ATOM 6136 CE2 PHE X 619 -13 .341 2 .473 5. .462 0. .00 0. .00 PROD

ATOM 6137 HE2 PHE X 619 -13 .905 2 .454 4. .541 0. .00 0. .00 PROD ATOM 6138 C PHE X 619 -11.076 -0.549 8..462 0..00 0..00 PROD

ATOM 6139 O PHE X 619 -10 .424 -0 .268 7. .439 0. .00 0. .00 PROD

ATOM 6140 N SER X 620 -10 .435 -0 .855 9. .619 0. .00 0. .00 PROD

ATOM 6141 HN SER X 620 -11 .048 -0 .985 10. .394 0. .00 0. .00 PROD

ATOM 6142 CA SER X 620 -8 .961 -0 .884 9. .772 0. .00 0. .00 PROD

ATOM 6143 HA SER X 620 -8 .578 0 .023 9. .328 0. .00 0. .00 PROD

ATOM 6144 CB SER X 620 -8 .560 -0 .962 11. .330 0. .00 0. .00 PROD

ATOM 6145 HB1 SER X 620 -9 .096 -0 .102 11. .786 0. .00 0. .00 PROD

ATOM 6146 HB2 SER X 620 -8 .977 -1 .966 11. .558 0. .00 0. .00 PROD

ATOM 6147 OG SER X 620 -7 .160 -0 .805 11. .467 0. .00 0. .00 PROD

ATOM 6148 HG1 SER X 620 -6 .970 -0 .397 12. .315 0. .00 0. .00 PROD

ATOM 6149 C SER X 620 -8 .235 -2 .052 8. .986 0. .00 0. .00 PROD

ATOM 6150 O SER X 620 -7 .310 -1 .871 8. .195 0. .00 0. .00 PROD

ATOM 6151 N SER X 621 -8 .758 -3 .252 9. .231 0. .00 0. .00 PROD

ATOM 6152 HN SER X 621 -9 .680 -3 .318 9. .604 0. .00 0. .00 PROD

ATOM 6153 CA SER X 621 -8 .154 -4 .477 8. .732 0. .00 0. .00 PROD

ATOM 6154 HA SER X 621 -7 .102 -4 .273 8. .865 0. .00 0. .00 PROD

ATOM 6155 CB SER X 621 -8 .480 -5 .663 9. .557 0. .00 0. .00 PROD

ATOM 6156 HB1 SER X 621 -7 .840 -6 .479 9. .157 0. .00 0. .00 PROD

ATOM 6157 HB2 SER X 621 -8 .171 -5 .564 10. .619 0. .00 0. .00 PROD

ATOM 6158 OG SER X 621 -9 .759 -6 .131 9. .560 0. .00 0. .00 PROD

ATOM 6159 HG1 SER X 621 -9 .799 -6 .784 10. .262 0. .00 0. .00 PROD

ATOM 6160 C SER X 621 -8 .397 -4 .839 7. .233 0. .00 0. .00 PROD

ATOM 6161 O SER X 621 -7 .463 -5 .285 6. .574 0. .00 0. .00 PROD

ATOM 6162 N LEU X 622 -9 .668 -4 .688 6. .730 0. .00 0. .00 PROD

ATOM 6163 HN LEU X 622 -10 .401 -4 .542 7. .389 0. .00 0. .00 PROD

ATOM 6164 CA LEU X 622 -9 .941 -5 .029 5. .343 0. .00 0. .00 PROD

ATOM 6165 HA LEU X 622 -9 .561 -6 .035 5. .242 0. .00 0. .00 PROD

ATOM 6166 CB LEU X 622 -11 .445 -5 .052 5. .047 0. .00 0. .00 PROD

ATOM 6167 HB1 LEU X 622 -11 .942 -4 .150 5. .463 0. .00 0. .00 PROD

ATOM 6168 HB2 LEU X 622 -11 .436 -4 .898 3. .947 0. .00 0. .00 PROD

ATOM 6169 CG LEU X 622 -12 .189 -6 .281 5. .515 0. .00 0. .00 PROD

ATOM 6170 HG LEU X 622 -11 .677 -7 .184 5. .119 0. .00 0. .00 PROD

ATOM 6171 CD1 LEU X 622 -12 .414 -6 .516 7. .080 0. .00 0. .00 PROD

ATOM 6172 HD11 LEU X 622 -11 .556 -6 .138 7. .676 0. .00 0. .00 PROD

ATOM 6173 HD12 LEU X 622 -13 .313 -5 .923 7. .352 0. .00 0. .00 PROD

ATOM 6174 HD13 LEU X 622 -12 .605 -7 .579 7. .340 0. .00 0. .00 PROD

ATOM 6175 CD2 LEU X 622 -13 .623 -6 .352 4. .825 0. .00 0. .00 PROD

ATOM 6176 HD21 LEU X 622 -13 .459 -6 .321 3. .727 0. .00 0. .00 PROD

ATOM 6177 HD22 LEU X 622 -14 .293 -7 .184 5. .132 0. .00 0. .00 PROD

ATOM 6178 HD23 LEU X 622 -14 .108 -5 .371 5. .016 0. .00 0. .00 PROD

ATOM 6179 C LEU X 622 -9 .250 -4 .004 4. .452 0. .00 0. .00 PROD

ATOM 6180 O LEU X 622 -8 .585 -4 .341 3. .508 0. .00 0. .00 PROD

ATOM 6181 N THR X 623 -9 .288 -2 .675 4. .867 0. .00 0. .00 PROD

ATOM 6182 HN THR X 623 -9 .912 -2 .446 5. .610 0. .00 0. .00 PROD

ATOM 6183 CA THR X 623 -8 .723 -1 .537 4. .128 0. .00 0. .00 PROD

ATOM 6184 HA THR X 623 -9 .087 -1 .598 3. .113 0. .00 0. .00 PROD

ATOM 6185 CB THR X 623 -9 .127 -0 .188 4. .680 0. .00 0. .00 PROD

ATOM 6186 HB THR X 623 -8 .576 0 .068 5. .609 0. .00 0. .00 PROD

ATOM 6187 OG1 THR X 623 -10 .549 -0 .251 4. .907 0. .00 0. .00 PROD

ATOM 6188 HG1 THR X 623 -10 .676 -0 .090 5. .845 0. .00 0. .00 PROD

ATOM 6189 CG2 THR X 623 -9 .059 0 .891 3. .617 0. .00 0. .00 PROD

ATOM 6190 HG21 THR X 623 -9 .624 0 .581 2. .712 0. .00 0. .00 PROD

ATOM 6191 HG22 THR X 623 -9 .561 1 .798 4. .016 0. .00 0. .00 PROD

ATOM 6192 HG23 THR X 623 -8 .016 1 .208 3. .400 0. .00 0. .00 PROD

ATOM 6193 C THR X 623 -7 .156 -1 .620 4. .136 0. .00 0. .00 PROD

ATOM 6194 O THR X 623 -6 .479 -0 .921 3. .368 0. .00 0. .00 PROD

ATOM 6195 N SER X 624 -6 .625 -2 .392 5. .079 0. .00 0. .00 PROD

ATOM 6196 HN SER X 624 -7 .205 -3 .001 5. .615 0. .00 0. .00 PROD

ATOM 6197 CA SER X 624 -5 .199 -2 .622 5. .206 0. .00 0. .00 PROD

ATOM 6198 HA SER X 624 -5 .005 -3 .368 5. .963 0. .00 0. .00 PROD

ATOM 6199 CB SER X 624 -4 .652 -3 .241 3. .981 0. .00 0. .00 PROD

ATOM 6200 HB1 SER X 624 -5 .443 -3 .983 3. .740 0. .00 0. .00 PROD

ATOM 6201 HB2 SER X 624 -4 .623 -2 .460 3. .191 0. .00 0. .00 PROD

ATOM 6202 OG SER X 624 -3 .516 -4 .014 4. .180 0. .00 0. .00 PROD

ATOM 6203 HG1 SER X 624 -3 .818 -4 .878 4. .469 0. .00 0. .00 PROD ATOM 6204 C SER X 624 -4.357 -1.465 5..836 0..00 0..00 PROD

ATOM 6205 O SER X 624 -3 .136 -1 .420 5. .899 0. .00 0. .00 PROD

ATOM 6206 N VAL X 625 -5 .117 -0 .519 6. .427 0. .00 0. .00 PROD

ATOM 6207 HN VAL X 625 -6 .113 -0 .561 6. .408 0. .00 0. .00 PROD

ATOM 6208 CA VAL X 625 -4 .494 0 .508 7. .248 0. .00 0. .00 PROD

ATOM 6209 HA VAL X 625 -3 .771 1 .057 6. .662 0. .00 0. .00 PROD

ATOM 6210 CB VAL X 625 -5 .434 1 .670 7. .673 0. .00 0. .00 PROD

ATOM 6211 HB VAL X 625 -6 .307 1 .213 8. .185 0. .00 0. .00 PROD

ATOM 6212 CGI VAL X 625 -4 .717 2 .759 8. .451 0. .00 0. .00 PROD

ATOM 6213 HG11 VAL X 625 -5 .469 3 .547 8. .671 0. .00 0. .00 PROD

ATOM 6214 HG12 VAL X 625 -4 .408 2 .360 9. .440 0. .00 0. .00 PROD

ATOM 6215 HG13 VAL X 625 -3 .874 3 .217 7. .891 0. .00 0. .00 PROD

ATOM 6216 CG2 VAL X 625 -5 .999 2 .389 6. .470 0. .00 0. .00 PROD

ATOM 6217 HG21 VAL X 625 -5 .225 2 .842 5. .814 0. .00 0. .00 PROD

ATOM 6218 HG22 VAL X 625 -6 .622 1 .676 5. .890 0. .00 0. .00 PROD

ATOM 6219 HG23 VAL X 625 -6 .731 3 .167 6. .775 0. .00 0. .00 PROD

ATOM 6220 C VAL X 625 -3 .838 -0 .100 8. .478 0. .00 0. .00 PROD

ATOM 6221 O VAL X 625 -2 .646 0 .104 8. .793 0. .00 0. .00 PROD

ATOM 6222 N GLY X 626 -4 .570 -1 .085 9. .096 0. .00 0. .00 PROD

ATOM 6223 HN GLY X 626 -5 .473 -1 .347 8. .764 0. .00 0. .00 PROD

ATOM 6224 CA GLY X 626 -4 .116 -1 .796 10. .273 0. .00 0. .00 PROD

ATOM 6225 HA1 GLY X 626 -3 .216 -2 .305 9. .961 0. .00 0. .00 PROD

ATOM 6226 HA2 GLY X 626 -4 .832 -2 .566 10. .518 0. .00 0. .00 PROD

ATOM 6227 C GLY X 626 -3 .796 -1 .002 11. .553 0. .00 0. .00 PROD

ATOM 6228 O GLY X 626 -4 .077 0 .211 11. .800 0. .00 0. .00 PROD

ATOM 6229 N PHE X 627 -3 .177 -1 .764 12. .517 0. .00 0. .00 PROD

ATOM 6230 HN PHE X 627 -2 .616 -2 .533 12. .221 0. .00 0. .00 PROD

ATOM 6231 CA PHE X 627 -2 .945 -1 .386 13. .863 0. .00 0. .00 PROD

ATOM 6232 HA PHE X 627 -2 .301 -2 .141 14. .289 0. .00 0. .00 PROD

ATOM 6233 CB PHE X 627 -2 .057 -0 .140 14. .039 0. .00 0. .00 PROD

ATOM 6234 HB1 PHE X 627 -1 .281 -0 .086 13. .246 0. .00 0. .00 PROD

ATOM 6235 HB2 PHE X 627 -2 .681 0 .773 13. .940 0. .00 0. .00 PROD

ATOM 6236 CG PHE X 627 -1 .429 -0 .104 15. .440 0. .00 0. .00 PROD

ATOM 6237 CD1 PHE X 627 -1 .980 0 .594 16. .545 0. .00 0. .00 PROD

ATOM 6238 HD1 PHE X 627 -3 .018 0 .869 16. .437 0. .00 0. .00 PROD

ATOM 6239 CE1 PHE X 627 -1 .340 0 .780 17. .772 0. .00 0. .00 PROD

ATOM 6240 HE1 PHE X 627 -1 .866 1 .200 18. .618 0. .00 0. .00 PROD

ATOM 6241 CZ PHE X 627 -0 .021 0 .323 17. .984 0. .00 0. .00 PROD

ATOM 6242 HZ PHE X 627 0. .421 0 .507 18. .952 0. .00 0. .00 PROD

ATOM 6243 CD2 PHE X 627 -0 .116 -0 .515 15. .694 0. .00 0. .00 PROD

ATOM 6244 HD2 PHE X 627 0 .388 -0 .969 14. .853 0. .00 0. .00 PROD

ATOM 6245 CE2 PHE X 627 0 .522 -0 .407 16. .956 0. .00 0. .00 PROD

ATOM 6246 HE2 PHE X 627 1 .518 -0 .784 17. .133 0. .00 0. .00 PROD

ATOM 6247 C PHE X 627 -4 .233 -1 .419 14. .663 0. .00 0. .00 PROD

ATOM 6248 O PHE X 627 -5 .248 -0 .846 14. .231 0. .00 0. .00 PROD

ATOM 6249 N GLY X 628 -4 .418 -2 .134 15. .789 0. .00 0. .00 PROD

ATOM 6250 HN GLY X 628 -5 .368 -2 .175 16. .087 0. .00 0. .00 PROD

ATOM 6251 CA GLY X 628 -3 .462 -2 .765 16. .754 0. .00 0. .00 PROD

ATOM 6252 HA1 GLY X 628 -2 .475 -2 .328 16. .793 0. .00 0. .00 PROD

ATOM 6253 HA2 GLY X 628 -3 .418 -3 .830 16. .577 0. .00 0. .00 PROD

ATOM 6254 C GLY X 628 -3 .941 -2 .631 18. .162 0. .00 0. .00 PROD

ATOM 6255 O GLY X 628 -3 .901 -3 .544 18. .953 0. .00 0. .00 PROD

ATOM 6256 N ASN X 629 -4 .453 -1 .427 18. .528 0. .00 0. .00 PROD

ATOM 6257 HN ASN X 629 -4 .568 -0 .667 17. .892 0. .00 0. .00 PROD

ATOM 6258 CA ASN X 629 -5 .092 -1 .323 19. .862 0. .00 0. .00 PROD

ATOM 6259 HA ASN X 629 -4 .543 -1 .851 20. .628 0. .00 0. .00 PROD

ATOM 6260 CB ASN X 629 -5 .320 0 .219 20. .198 0. .00 0. .00 PROD

ATOM 6261 HB1 ASN X 629 -5 .935 0 .727 19. .424 0. .00 0. .00 PROD

ATOM 6262 HB2 ASN X 629 -5 .834 0 .353 21. .174 0. .00 0. .00 PROD

ATOM 6263 CG ASN X 629 -4 .103 1 .126 20. .271 0. .00 0. .00 PROD

ATOM 6264 OD1 ASN X 629 -4 .121 2 .048 19. .439 0. .00 0. .00 PROD

ATOM 6265 ND2 ASN X 629 -3 .096 0 .893 21. .156 0. .00 0. .00 PROD

ATOM 6266 HD21 ASN X 629 -3 .206 0 .053 21. .689 0. .00 0. .00 PROD

ATOM 6267 HD22 ASN X 629 -2 .360 1 .562 21. .259 0. .00 0. .00 PROD

ATOM 6268 C ASN X 629 -6 .389 -2 .102 19. .893 0. .00 0. .00 PROD

ATOM 6269 O ASN X 629 -6 .810 -2 .699 20. .895 0. .00 0. .00 PROD ATOM 6270 N VAL X 630 -7.072 -2.116 18..754 0..00 0..00 PROD

ATOM 6271 HN VAL X 630 -6 .744 -1 .520 18. .025 0. .00 0. .00 PROD

ATOM 6272 CA VAL X 630 -8 .354 -2 .861 18. .655 0. .00 0. .00 PROD

ATOM 6273 HA VAL X 630 -8 .758 -3 .318 19. .546 0. .00 0. .00 PROD

ATOM 6274 CB VAL X 630 -9 .441 -2 .067 17. .930 0. .00 0. .00 PROD

ATOM 6275 HB VAL X 630 -9 .165 -1 .966 16. .859 0. .00 0. .00 PROD

ATOM 6276 CGI VAL X 630 -10 .845 -2 .682 18. .059 0. .00 0. .00 PROD

ATOM 6277 HG11 VAL X 630 -11 .248 -2 .552 19. .086 0. .00 0. .00 PROD

ATOM 6278 HG12 VAL X 630 -11 .702 -2 .304 17. .463 0. .00 0. .00 PROD

ATOM 6279 HG13 VAL X 630 -10 .785 -3 .789 17. .981 0. .00 0. .00 PROD

ATOM 6280 CG2 VAL X 630 -9 .493 -0 .676 18. .501 0. .00 0. .00 PROD

ATOM 6281 HG21 VAL X 630 -8 .522 -0 .156 18. .352 0. .00 0. .00 PROD

ATOM 6282 HG22 VAL X 630 -10 .333 -0 .125 18. .028 0. .00 0. .00 PROD

ATOM 6283 HG23 VAL X 630 -9 .692 -0 .787 19. .588 0. .00 0. .00 PROD

ATOM 6284 C VAL X 630 -7 .922 -3 .988 17. .806 0. .00 0. .00 PROD

ATOM 6285 O VAL X 630 -7 .355 -3 .888 16. .707 0. .00 0. .00 PROD

ATOM 6286 N SER X 631 -8 .077 -5 .235 18. .182 0. .00 0. .00 PROD

ATOM 6287 HN SER X 631 -8 .691 -5 .364 18. .957 0. .00 0. .00 PROD

ATOM 6288 CA SER X 631 -7 .554 -6 .460 17. .605 0. .00 0. .00 PROD

ATOM 6289 HA SER X 631 -7 .713 -6 .394 16. .539 0. .00 0. .00 PROD

ATOM 6290 CB SER X 631 -6 .148 -6 .786 18. .039 0. .00 0. .00 PROD

ATOM 6291 HB1 SER X 631 -5 .553 -5 .857 18. .178 0. .00 0. .00 PROD

ATOM 6292 HB2 SER X 631 -6 .135 -7 .183 19. .077 0. .00 0. .00 PROD

ATOM 6293 OG SER X 631 -5 .514 -7 .528 17. .063 0. .00 0. .00 PROD

ATOM 6294 HG1 SER X 631 -4 .855 -7 .999 17. .578 0. .00 0. .00 PROD

ATOM 6295 C SER X 631 -8 .502 -7 .523 17. .979 0. .00 0. .00 PROD

ATOM 6296 O SER X 631 -9 .287 -7 .314 18. .879 0. .00 0. .00 PROD

ATOM 6297 N PRO X 632 -8 .480 -8 .693 17. .347 0. .00 0. .00 PROD

ATOM 6298 CD PRO X 632 -8 .013 -8 .976 16. .026 0. .00 0. .00 PROD

ATOM 6299 HD1 PRO X 632 -8 .055 -8 .094 15. .351 0. .00 0. .00 PROD

ATOM 6300 HD2 PRO X 632 -6 .926 -9 .181 15. .918 0. .00 0. .00 PROD

ATOM 6301 CA PRO X 632 -9 .160 -9 .881 17. .885 0. .00 0. .00 PROD

ATOM 6302 HA PRO X 632 -10 .203 -9 .653 17. .723 0. .00 0. .00 PROD

ATOM 6303 CB PRO X 632 -8 .880 -10 .948 16. .853 0. .00 0. .00 PROD

ATOM 6304 HB1 PRO X 632 -9 .568 -11 .819 16. .811 0. .00 0. .00 PROD

ATOM 6305 HB2 PRO X 632 -7 .868 -11 .240 17. .207 0. .00 0. .00 PROD

ATOM 6306 CG PRO X 632 -8 .785 -10 .193 15. .567 0. .00 0. .00 PROD

ATOM 6307 HG1 PRO X 632 -9 .780 -9 .974 15. .123 0. .00 0. .00 PROD

ATOM 6308 HG2 PRO X 632 -8 .176 -10 .681 14. .776 0. .00 0. .00 PROD

ATOM 6309 C PRO X 632 -9 .018 -10 .202 19. .296 0. .00 0. .00 PROD

ATOM 6310 O PRO X 632 -7 .940 -10 .270 19. .825 0. .00 0. .00 PROD

ATOM 6311 N ASN X 633 -10 .132 -10 .540 19. .961 0. .00 0. .00 PROD

ATOM 6312 HN ASN X 633 -11 .010 -10 .590 19. .492 0. .00 0. .00 PROD

ATOM 6313 CA ASN X 633 -10 .056 -10 .883 21. .366 0. .00 0. .00 PROD

ATOM 6314 HA ASN X 633 -9 .065 -10 .674 21. .740 0. .00 0. .00 PROD

ATOM 6315 CB ASN X 633 -11 .018 -9 .980 22. .140 0. .00 0. .00 PROD

ATOM 6316 HB1 ASN X 633 -12 .052 -10 .087 21. .749 0. .00 0. .00 PROD

ATOM 6317 HB2 ASN X 633 -11 .035 -10 .038 23. .249 0. .00 0. .00 PROD

ATOM 6318 CG ASN X 633 -10 .631 -8 .548 21. .814 0. .00 0. .00 PROD

ATOM 6319 OD1 ASN X 633 -11 .212 -7 .849 20. .990 0. .00 0. .00 PROD

ATOM 6320 ND2 ASN X 633 -9 .667 -8 .040 22. .527 0. .00 0. .00 PROD

ATOM 6321 HD21 ASN X 633 -9 .310 -7 .121 22. .363 0. .00 0. .00 PROD

ATOM 6322 HD22 ASN X 633 -9 .275 -8 .497 23. .326 0. .00 0. .00 PROD

ATOM 6323 C ASN X 633 -10 .252 -12 .242 21. .858 0. .00 0. .00 PROD

ATOM 6324 O ASN X 633 -10 .201 -12 .556 23. .068 0. .00 0. .00 PROD

ATOM 6325 N THR X 634 -10 .484 -13 .175 20. .925 0. .00 0. .00 PROD

ATOM 6326 HN THR X 634 -10 .752 -13 .039 19. .975 0. .00 0. .00 PROD

ATOM 6327 CA THR X 634 -10 .591 -14 .557 21. .281 0. .00 0. .00 PROD

ATOM 6328 HA THR X 634 -9 .921 -14 .745 22. .107 0. .00 0. .00 PROD

ATOM 6329 CB THR X 634 -12 .080 -14 .976 21. .677 0. .00 0. .00 PROD

ATOM 6330 HB THR X 634 -12 .365 -14 .431 22. .602 0. .00 0. .00 PROD

ATOM 6331 OG1 THR X 634 -12 .161 -16 .343 22. .121 0. .00 0. .00 PROD

ATOM 6332 HG1 THR X 634 -12 .906 -16 .425 22. .721 0. .00 0. .00 PROD

ATOM 6333 CG2 THR X 634 -13 .078 -14 .609 20. .526 0. .00 0. .00 PROD

ATOM 6334 HG21 THR X 634 -12 .744 -15 .217 19. .659 0. .00 0. .00 PROD

ATOM 6335 HG22 THR X 634 -14 .081 -14 .989 20. .814 0. .00 0. .00 PROD ATOM 6336 HG23 THR X 634 -13.025 -13.544 20..211 0..00 0..00 PROD

ATOM 6337 C THR X 634 -10 .092 -15 .505 20. .223 0. .00 0. .00 PROD

ATOM 6338 O THR X 634 -9 .983 -15 .175 19. .052 0. .00 0. .00 PROD

ATOM 6339 N ASN X 635 -9 .762 -16 .757 20. .533 0. .00 0. .00 PROD

ATOM 6340 HN ASN X 635 -9 .773 -17 .066 21. .481 0. .00 0. .00 PROD

ATOM 6341 CA ASN X 635 -9 .255 -17 .773 19. .459 0. .00 0. .00 PROD

ATOM 6342 HA ASN X 635 -8 .452 -17 .382 18. .851 0. .00 0. .00 PROD

ATOM 6343 CB ASN X 635 -8 .912 -19 .047 20. .239 0. .00 0. .00 PROD

ATOM 6344 HB1 ASN X 635 -9 .711 -19 .350 20. .950 0. .00 0. .00 PROD

ATOM 6345 HB2 ASN X 635 -8 .819 -19 .882 19. .513 0. .00 0. .00 PROD

ATOM 6346 CG ASN X 635 -7 .642 -18 .978 21. .142 0. .00 0. .00 PROD

ATOM 6347 OD1 ASN X 635 -6 .789 -18 .116 20. .915 0. .00 0. .00 PROD

ATOM 6348 ND2 ASN X 635 -7 .415 -19 .966 21. .999 0. .00 0. .00 PROD

ATOM 6349 HD21 ASN X 635 -6 .719 -19 .715 22. .672 0. .00 0. .00 PROD

ATOM 6350 HD22 ASN X 635 -8 .199 -20 .534 22. .251 0. .00 0. .00 PROD

ATOM 6351 C ASN X 635 -10 .255 -18 .143 18. .382 0. .00 0. .00 PROD

ATOM 6352 O ASN X 635 -9 .815 -18 .230 17. .231 0. .00 0. .00 PROD

ATOM 6353 N SER X 636 -11 .598 -18 .078 18. .660 0. .00 0. .00 PROD

ATOM 6354 HN SER X 636 -11 .846 -17 .753 19. .569 0. .00 0. .00 PROD

ATOM 6355 CA SER X 636 -12 .525 -18 .201 17. .561 0. .00 0. .00 PROD

ATOM 6356 HA SER X 636 -12 .311 -19 .078 16. .968 0. .00 0. .00 PROD

ATOM 6357 CB SER X 636 -13 .909 -18 .544 18. .146 0. .00 0. .00 PROD

ATOM 6358 HB1 SER X 636 -14 .509 -19 .003 17. .331 0. .00 0. .00 PROD

ATOM 6359 HB2 SER X 636 -13 .774 -19 .334 18. .916 0. .00 0. .00 PROD

ATOM 6360 OG SER X 636 -14 .509 -17 .460 18. .823 0. .00 0. .00 PROD

ATOM 6361 HG1 SER X 636 -14 .978 -17 .886 19. .545 0. .00 0. .00 PROD

ATOM 6362 C SER X 636 -12 .508 -17 .110 16. .621 0. .00 0. .00 PROD

ATOM 6363 O SER X 636 -12 .342 -17 .272 15. .409 0. .00 0. .00 PROD

ATOM 6364 N GLU X 637 -12 .561 -15 .793 17. .089 0. .00 0. .00 PROD

ATOM 6365 HN GLU X 637 -12 .826 -15 .644 18. .038 0. .00 0. .00 PROD

ATOM 6366 CA GLU X 637 -12 .330 -14 .596 16. .262 0. .00 0. .00 PROD

ATOM 6367 HA GLU X 637 -13 .157 -14 .450 15. .583 0. .00 0. .00 PROD

ATOM 6368 CB GLU X 637 -12 .408 -13 .355 17. .112 0. .00 0. .00 PROD

ATOM 6369 HB1 GLU X 637 -13 .208 -13 .500 17. .870 0. .00 0. .00 PROD

ATOM 6370 HB2 GLU X 637 -11 .413 -13 .297 17. .602 0. .00 0. .00 PROD

ATOM 6371 CG GLU X 637 -12 .563 -11 .977 16. .449 0. .00 0. .00 PROD

ATOM 6372 HG1 GLU X 637 -11 .704 -11 .693 15. .803 0. .00 0. .00 PROD

ATOM 6373 HG2 GLU X 637 -13 .384 -11 .907 15. .704 0. .00 0. .00 PROD

ATOM 6374 CD GLU X 637 -12 .602 -10 .723 17. .313 0. .00 0. .00 PROD

ATOM 6375 OE1 GLU X 637 -12 .577 -10 .831 18. .550 0. .00 0. .00 PROD

ATOM 6376 OE2 GLU X 637 -12 .776 -9 .660 16. .647 0. .00 0. .00 PROD

ATOM 6377 C GLU X 637 -11 .054 -14 .626 15. .447 0. .00 0. .00 PROD

ATOM 6378 O GLU X 637 -11 .002 -14 .214 14. .281 0. .00 0. .00 PROD

ATOM 6379 N LYS X 638 -9 .952 -15 .071 16. .048 0. .00 0. .00 PROD

ATOM 6380 HN LYS X 638 -10 .001 -15 .379 16. .995 0. .00 0. .00 PROD

ATOM 6381 CA LYS X 638 -8 .595 -15 .176 15. .434 0. .00 0. .00 PROD

ATOM 6382 HA LYS X 638 -8 .443 -14 .185 15. .033 0. .00 0. .00 PROD

ATOM 6383 CB LYS X 638 -7 .506 -15 .434 16. .467 0. .00 0. .00 PROD

ATOM 6384 HB1 LYS X 638 -7 .675 -16 .390 17. .008 0. .00 0. .00 PROD

ATOM 6385 HB2 LYS X 638 -6 .540 -15 .587 15. .939 0. .00 0. .00 PROD

ATOM 6386 CG LYS X 638 -7 .392 -14 .226 17. .441 0. .00 0. .00 PROD

ATOM 6387 HG1 LYS X 638 -6 .967 -13 .343 16. .917 0. .00 0. .00 PROD

ATOM 6388 HG2 LYS X 638 -8 .398 -13 .888 17. .769 0. .00 0. .00 PROD

ATOM 6389 CD LYS X 638 -6 .546 -14 .595 18. .692 0. .00 0. .00 PROD

ATOM 6390 HD1 LYS X 638 -7 .097 -15 .415 19. .199 0. .00 0. .00 PROD

ATOM 6391 HD2 LYS X 638 -5 .543 -14 .986 18. .417 0. .00 0. .00 PROD

ATOM 6392 CE LYS X 638 -6 .414 -13 .381 19. .559 0. .00 0. .00 PROD

ATOM 6393 HE1 LYS X 638 -5 .788 -12 .713 18. .929 0. .00 0. .00 PROD

ATOM 6394 HE2 LYS X 638 -7 .333 -12 .856 19. .897 0. .00 0. .00 PROD

ATOM 6395 NZ LYS X 638 -5 .668 -13 .656 20. .765 0. .00 0. .00 PROD

ATOM 6396 HZ1 LYS X 638 -6 .287 -14 .148 21. .441 0. .00 0. .00 PROD

ATOM 6397 HZ2 LYS X 638 -4 .793 -14 .136 20. .473 0. .00 0. .00 PROD

ATOM 6398 HZ3 LYS X 638 -5 .468 -12 .744 21. .222 0. .00 0. .00 PROD

ATOM 6399 C LYS X 638 -8 .528 -16 .151 14. .317 0. .00 0. .00 PROD

ATOM 6400 O LYS X 638 -7 .987 -15 .856 13. .280 0. .00 0. .00 PROD

ATOM 6401 N ILE X 639 -9 .159 -17 .352 14. .514 0. .00 0. .00 PROD ATOM 6402 HN ILE X 639 -9.567 -17.644 15..376 0..00 0..00 PROD

ATOM 6403 CA ILE X 639 -9 .236 -18 .277 13. .410 0. .00 0. .00 PROD

ATOM 6404 HA ILE X 639 -8 .318 -18 .230 12. .842 0. .00 0. .00 PROD

ATOM 6405 CB ILE X 639 -9 .304 -19 .765 13. .803 0. .00 0. .00 PROD

ATOM 6406 HB ILE X 639 -8 .637 -19 .867 14. .686 0. .00 0. .00 PROD

ATOM 6407 CG2 ILE X 639 -10 .672 -20 .282 14. .291 0. .00 0. .00 PROD

ATOM 6408 HG21 ILE X 639 -10 .755 -21 .357 14. .557 0. .00 0. .00 PROD

ATOM 6409 HG22 ILE X 639 -11 .010 -19 .651 15. .141 0. .00 0. .00 PROD

ATOM 6410 HG23 ILE X 639 -11 .346 -20 .121 13. .423 0. .00 0. .00 PROD

ATOM 6411 CGI ILE X 639 -8 .818 -20 .733 12. .737 0. .00 0. .00 PROD

ATOM 6412 HG11 ILE X 639 -9 .625 -20 .792 11. .975 0. .00 0. .00 PROD

ATOM 6413 HG12 ILE X 639 -7 .916 -20 .313 12. .242 0. .00 0. .00 PROD

ATOM 6414 CD ILE X 639 -8 .471 -22 .118 13. .205 0. .00 0. .00 PROD

ATOM 6415 HD1 ILE X 639 -7 .591 -22 .070 13. .883 0. .00 0. .00 PROD

ATOM 6416 HD2 ILE X 639 -9 .330 -22 .703 13. .597 0. .00 0. .00 PROD

ATOM 6417 HD3 ILE X 639 -8 .156 -22 .812 12. .396 0. .00 0. .00 PROD

ATOM 6418 C ILE X 639 -10 .375 -17 .978 12. .402 0. .00 0. .00 PROD

ATOM 6419 O ILE X 639 -10 .246 -18 .193 11. .173 0. .00 0. .00 PROD

ATOM 6420 N PHE X 640 -11 .468 -17 .357 12. .810 0. .00 0. .00 PROD

ATOM 6421 HN PHE X 640 -11 .779 -17 .327 13. .756 0. .00 0. .00 PROD

ATOM 6422 CA PHE X 640 -12 .417 -16 .872 11. .775 0. .00 0. .00 PROD

ATOM 6423 HA PHE X 640 -12 .673 -17 .726 11. .164 0. .00 0. .00 PROD

ATOM 6424 CB PHE X 640 -13 .669 -16 .129 12. .426 0. .00 0. .00 PROD

ATOM 6425 HB1 PHE X 640 -13 .321 -15 .526 13. .292 0. .00 0. .00 PROD

ATOM 6426 HB2 PHE X 640 -14 .245 -15 .492 11. .721 0. .00 0. .00 PROD

ATOM 6427 CG PHE X 640 -14 .579 -17 .142 13. .037 0. .00 0. .00 PROD

ATOM 6428 CD1 PHE X 640 -15 .432 -16 .770 14. .122 0. .00 0. .00 PROD

ATOM 6429 HD1 PHE X 640 -15 .354 -15 .774 14. .533 0. .00 0. .00 PROD

ATOM 6430 CE1 PHE X 640 -16 .340 -17 .686 14. .606 0. .00 0. .00 PROD

ATOM 6431 HE1 PHE X 640 -16 .933 -17 .326 15. .433 0. .00 0. .00 PROD

ATOM 6432 CZ PHE X 640 -16 .560 -18 .911 14. .077 0. .00 0. .00 PROD

ATOM 6433 HZ PHE X 640 -17 .274 -19 .619 14. .470 0. .00 0. .00 PROD

ATOM 6434 CD2 PHE X 640 -14 .800 -18 .440 12. .488 0. .00 0. .00 PROD

ATOM 6435 HD2 PHE X 640 -14 .202 -18 .786 11. .658 0. .00 0. .00 PROD

ATOM 6436 CE2 PHE X 640 -15 .745 -19 .304 12. .996 0. .00 0. .00 PROD

ATOM 6437 HE2 PHE X 640 -15 .873 -20 .269 12. .529 0. .00 0. .00 PROD

ATOM 6438 C PHE X 640 -11 .901 -15 .766 10. .898 0. .00 0. .00 PROD

ATOM 6439 O PHE X 640 -12 .064 -15 .756 9. .677 0. .00 0. .00 PROD

ATOM 6440 N SER X 641 -11 .278 -14 .713 11. .482 0. .00 0. .00 PROD

ATOM 6441 HN SER X 641 -11 .202 -14 .825 12. .470 0. .00 0. .00 PROD

ATOM 6442 CA SER X 641 -10 .877 -13 .462 10. .895 0. .00 0. .00 PROD

ATOM 6443 HA SER X 641 -11 .852 -13 .134 10. .565 0. .00 0. .00 PROD

ATOM 6444 CB SER X 641 -10 .233 -12 .423 11. .873 0. .00 0. .00 PROD

ATOM 6445 HB1 SER X 641 -10 .254 -11 .428 11. .380 0. .00 0. .00 PROD

ATOM 6446 HB2 SER X 641 -10 .861 -12 .393 12. .790 0. .00 0. .00 PROD

ATOM 6447 OG SER X 641 -8 .870 -12 .616 12. .140 0. .00 0. .00 PROD

ATOM 6448 HG1 SER X 641 -8 .790 -13 .339 12. .767 0. .00 0. .00 PROD

ATOM 6449 C SER X 641 -10 .148 -13 .555 9. .594 0. .00 0. .00 PROD

ATOM 6450 O SER X 641 -10 .226 -12 .626 8. .752 0. .00 0. .00 PROD

ATOM 6451 N ILE X 642 -9 .343 -14 .618 9. .452 0. .00 0. .00 PROD

ATOM 6452 HN ILE X 642 -9 .307 -15 .309 10. .170 0. .00 0. .00 PROD

ATOM 6453 CA ILE X 642 -8 .388 -14 .718 8. .363 0. .00 0. .00 PROD

ATOM 6454 HA ILE X 642 -7 .998 -13 .721 8. .219 0. .00 0. .00 PROD

ATOM 6455 CB ILE X 642 -7 .208 -15 .637 8. .574 0. .00 0. .00 PROD

ATOM 6456 HB ILE X 642 -6 .744 -15 .995 7. .630 0. .00 0. .00 PROD

ATOM 6457 CG2 ILE X 642 -6 .210 -14 .669 9. .246 0. .00 0. .00 PROD

ATOM 6458 HG21 ILE X 642 -5 .151 -14 .996 9. .315 0. .00 0. .00 PROD

ATOM 6459 HG22 ILE X 642 -6 .176 -13 .649 8. .807 0. .00 0. .00 PROD

ATOM 6460 HG23 ILE X 642 -6 .394 -14 .610 10. .340 0. .00 0. .00 PROD

ATOM 6461 CGI ILE X 642 -7 .521 -16 .803 9. .453 0. .00 0. .00 PROD

ATOM 6462 HG11 ILE X 642 -7 .497 -16 .470 10. .512 0. .00 0. .00 PROD

ATOM 6463 HG12 ILE X 642 -8 .532 -17 .138 9. .134 0. .00 0. .00 PROD

ATOM 6464 CD ILE X 642 -6 .484 -18 .023 9. .343 0. .00 0. .00 PROD

ATOM 6465 HD1 ILE X 642 -6 .602 -18 .667 8. .445 0. .00 0. .00 PROD

ATOM 6466 HD2 ILE X 642 -5 .443 -17 .636 9. .379 0. .00 0. .00 PROD

ATOM 6467 HD3 ILE X 642 -6 .732 -18 .828 10. .067 0. .00 0. .00 PROD ATOM 6468 C ILE X 642 -9.039 -14.934 7..002 0..00 0..00 PROD

ATOM 6469 O ILE X 642 -8 .698 -14 .274 6. .030 0. .00 0. .00 PROD

ATOM 6470 N CYS X 643 -10 .139 -15 .718 6. .924 0. .00 0. .00 PROD

ATOM 6471 HN CYS X 643 -10 .345 -16 .315 7. .695 0. .00 0. .00 PROD

ATOM 6472 CA CYS X 643 -10 .972 -15 .965 5. .795 0. .00 0. .00 PROD

ATOM 6473 HA CYS X 643 -10 .348 -16 .206 4. .947 0. .00 0. .00 PROD

ATOM 6474 CB CYS X 643 -12 .029 -17 .053 6. .112 0. .00 0. .00 PROD

ATOM 6475 HB1 CYS X 643 -12 .809 -16 .719 6. .829 0. .00 0. .00 PROD

ATOM 6476 HB2 CYS X 643 -12 .409 -17 .378 5. .120 0. .00 0. .00 PROD

ATOM 6477 SG CYS X 643 -11 .230 -18 .523 6. .755 0. .00 0. .00 PROD

ATOM 6478 HG1 CYS X 643 -10 .217 -18 .341 5. .919 0. .00 0. .00 PROD

ATOM 6479 C CYS X 643 -11 .648 -14 .737 5. .338 0. .00 0. .00 PROD

ATOM 6480 O CYS X 643 -11 .748 -14 .378 4. .180 0. .00 0. .00 PROD

ATOM 6481 N VAL X 644 -12 .170 -13 .991 6. .348 0. .00 0. .00 PROD

ATOM 6482 HN VAL X 644 -12 .024 -14 .295 7. .287 0. .00 0. .00 PROD

ATOM 6483 CA VAL X 644 -12 .870 -12 .748 6. .084 0. .00 0. .00 PROD

ATOM 6484 HA VAL X 644 -13 .490 -13 .034 5. .247 0. .00 0. .00 PROD

ATOM 6485 CB VAL X 644 -13 .686 -12 .224 7. .249 0. .00 0. .00 PROD

ATOM 6486 HB VAL X 644 -13 .029 -11 .970 8. .108 0. .00 0. .00 PROD

ATOM 6487 CGI VAL X 644 -14 .620 -11 .001 6. .971 0. .00 0. .00 PROD

ATOM 6488 HG11 VAL X 644 -14 .032 -10 .068 7. .102 0. .00 0. .00 PROD

ATOM 6489 HG12 VAL X 644 -14 .916 -10 .981 5. .900 0. .00 0. .00 PROD

ATOM 6490 HG13 VAL X 644 -15 .532 -11 .030 7. .605 0. .00 0. .00 PROD

ATOM 6491 CG2 VAL X 644 -14 .518 -13 .488 7. .776 0. .00 0. .00 PROD

ATOM 6492 HG21 VAL X 644 -15 .349 -13 .755 7. .089 0. .00 0. .00 PROD

ATOM 6493 HG22 VAL X 644 -13 .826 -14 .355 7. .825 0. .00 0. .00 PROD

ATOM 6494 HG23 VAL X 644 -14 .867 -13 .089 8. .752 0. .00 0. .00 PROD

ATOM 6495 C VAL X 644 -11 .959 -11 .671 5. .547 0. .00 0. .00 PROD

ATOM 6496 O VAL X 644 -12 .239 -11 .014 4. .550 0. .00 0. .00 PROD

ATOM 6497 N MET X 645 -10 .764 -11 .412 6. .131 0. .00 0. .00 PROD

ATOM 6498 HN MET X 645 -10 .502 -11 .976 6. .910 0. .00 0. .00 PROD

ATOM 6499 CA MET X 645 -9 .832 -10 .336 5. .856 0. .00 0. .00 PROD

ATOM 6500 HA MET X 645 -10 .394 -9 .423 5. .983 0. .00 0. .00 PROD

ATOM 6501 CB MET X 645 -8 .563 -10 .446 6. .773 0. .00 0. .00 PROD

ATOM 6502 HB1 MET X 645 -8 .939 -10 .587 7. .809 0. .00 0. .00 PROD

ATOM 6503 HB2 MET X 645 -8 .034 -11 .367 6. .448 0. .00 0. .00 PROD

ATOM 6504 CG MET X 645 -7 .616 -9 .194 6. .774 0. .00 0. .00 PROD

ATOM 6505 HG1 MET X 645 -6 .975 -9 .144 5. .868 0. .00 0. .00 PROD

ATOM 6506 HG2 MET X 645 -8 .286 -8 .313 6. .876 0. .00 0. .00 PROD

ATOM 6507 C MET X 645 -9 .379 -10 .515 4. .410 0. .00 0. .00 PROD

ATOM 6508 O MET X 645 -9 .320 -9 .574 3. .637 0. .00 0. .00 PROD

ATOM 6509 N LEU X 646 -8 .934 -11 .809 4. .074 0. .00 0. .00 PROD

ATOM 6510 HN LEU X 646 -8 .965 -12 .612 4. .664 0. .00 0. .00 PROD

ATOM 6511 CA LEU X 646 -8 .473 -11 .982 2. .697 0. .00 0. .00 PROD

ATOM 6512 HA LEU X 646 -7 .770 -11 .179 2. .535 0. .00 0. .00 PROD

ATOM 6513 CB LEU X 646 -7 .634 -13 .236 2. .354 0. .00 0. .00 PROD

ATOM 6514 HB1 LEU X 646 -8 .295 -14 .108 2. .162 0. .00 0. .00 PROD

ATOM 6515 HB2 LEU X 646 -7 .073 -13 .190 1. .397 0. .00 0. .00 PROD

ATOM 6516 CG LEU X 646 -6 .554 -13 .634 3. .336 0. .00 0. .00 PROD

ATOM 6517 HG LEU X 646 -7 .064 -13 .978 4. .261 0. .00 0. .00 PROD

ATOM 6518 CD1 LEU X 646 -5 .793 -14 .898 2. .860 0. .00 0. .00 PROD

ATOM 6519 HD11 LEU X 646 -5 .402 -14 .765 1. .829 0. .00 0. .00 PROD

ATOM 6520 HD12 LEU X 646 -4 .963 -15 .150 3. .554 0. .00 0. .00 PROD

ATOM 6521 HD13 LEU X 646 -6 .404 -15 .826 2. .848 0. .00 0. .00 PROD

ATOM 6522 CD2 LEU X 646 -5 .534 -12 .497 3. .653 0. .00 0. .00 PROD

ATOM 6523 HD21 LEU X 646 -6 .001 -11 .492 3. .725 0. .00 0. .00 PROD

ATOM 6524 HD22 LEU X 646 -4 .767 -12 .635 4. .445 0. .00 0. .00 PROD

ATOM 6525 HD23 LEU X 646 -4 .906 -12 .366 2. .746 0. .00 0. .00 PROD

ATOM 6526 C LEU X 646 -9 .538 -11 .881 1. .627 0. .00 0. .00 PROD

ATOM 6527 O LEU X 646 -9 .338 -11 .266 0. .604 0. .00 0. .00 PROD

ATOM 6528 N ILE X 647 -10 .764 -12 .419 1. .905 0. .00 0. .00 PROD

ATOM 6529 HN ILE X 647 -10 .827 -13 .082 2. .647 0. .00 0. .00 PROD

ATOM 6530 CA ILE X 647 -11 .987 -12 .133 0. .991 0. .00 0. .00 PROD

ATOM 6531 HA ILE X 647 -11 .729 -12 .431 -0. .014 0. .00 0. .00 PROD

ATOM 6532 CB ILE X 647 -13 .191 -12 .960 1. .521 0. .00 0. .00 PROD

ATOM 6533 HB ILE X 647 -13 .322 -12 .671 2. .586 0. .00 0. .00 PROD ATOM 6534 CG2 ILE X 647 -14.475 -12.705 0..757 0..00 0..00 PROD

ATOM 6535 HG21 ILE X 647 -14 .311 -12 .835 -0. .334 0. .00 0. .00 PROD

ATOM 6536 HG22 ILE X 647 -15 .265 -13 .350 1. .199 0. .00 0. .00 PROD

ATOM 6537 HG23 ILE X 647 -14 .762 -11 .633 0. .798 0. .00 0. .00 PROD

ATOM 6538 CGI ILE X 647 -12 .766 -14 .480 1. .428 0. .00 0. .00 PROD

ATOM 6539 HG11 ILE X 647 -12 .765 -14 .822 0. .371 0. .00 0. .00 PROD

ATOM 6540 HG12 ILE X 647 -11 .738 -14 .719 1. .774 0. .00 0. .00 PROD

ATOM 6541 CD ILE X 647 -13 .759 -15 .412 2. .195 0. .00 0. .00 PROD

ATOM 6542 HD1 ILE X 647 -14 .636 -15 .555 1. .528 0. .00 0. .00 PROD

ATOM 6543 HD2 ILE X 647 -13 .345 -16 .418 2. .420 0. .00 0. .00 PROD

ATOM 6544 HD3 ILE X 647 -13 .990 -14 .996 3. .199 0. .00 0. .00 PROD

ATOM 6545 C ILE X 647 -12 .329 -10 .706 0. .846 0. .00 0. .00 PROD

ATOM 6546 O ILE X 647 -12 .639 -10 .291 -0. .278 0. .00 0. .00 PROD

ATOM 6547 N GLY X 648 -12 .191 -9 .908 1. .879 0. .00 0. .00 PROD

ATOM 6548 HN GLY X 648 -12 .016 -10 .393 2. .732 0. .00 0. .00 PROD

ATOM 6549 CA GLY X 648 -12 .523 -8 .498 1. .852 0. .00 0. .00 PROD

ATOM 6550 HA1 GLY X 648 -12 .635 -8 .182 2. .879 0. .00 0. .00 PROD

ATOM 6551 HA2 GLY X 648 -13 .410 -8 .299 1. .268 0. .00 0. .00 PROD

ATOM 6552 C GLY X 648 -11 .429 -7 .584 1. .289 0. .00 0. .00 PROD

ATOM 6553 O GLY X 648 -11 .668 -6 .464 0. .947 0. .00 0. .00 PROD

ATOM 6554 N SER X 649 -10 .190 -8 .021 1. .172 0. .00 0. .00 PROD

ATOM 6555 HN SER X 649 -9 .945 -8 .892 1. .591 0. .00 0. .00 PROD

ATOM 6556 CA SER X 649 -9 .057 -7 .429 0. .499 0. .00 0. .00 PROD

ATOM 6557 HA SER X 649 -9 .017 -6 .399 0. .823 0. .00 0. .00 PROD

ATOM 6558 CB SER X 649 -7 .649 -8 .055 0. .971 0. .00 0. .00 PROD

ATOM 6559 HB1 SER X 649 -7 .734 -9 .120 0. .665 0. .00 0. .00 PROD

ATOM 6560 HB2 SER X 649 -6 .763 -7 .568 0. .511 0. .00 0. .00 PROD

ATOM 6561 OG SER X 649 -7 .456 -7 .976 2. .441 0. .00 0. .00 PROD

ATOM 6562 HG1 SER X 649 -8 .197 -8 .416 2. .864 0. .00 0. .00 PROD

ATOM 6563 C SER X 649 -9 .131 -7 .620 -0. .964 0. .00 0. .00 PROD

ATOM 6564 O SER X 649 -8 .740 -6 .792 -1. .790 0. .00 0. .00 PROD

ATOM 6565 N LEU X 650 -9 .654 -8 .809 -1. .311 0. .00 0. .00 PROD

ATOM 6566 HN LEU X 650 -10 .016 -9 .384 -0. .582 0. .00 0. .00 PROD

ATOM 6567 CA LEU X 650 -9 .842 -9 .278 -2. .732 0. .00 0. .00 PROD

ATOM 6568 HA LEU X 650 -8 .849 -9 .133 -3. .131 0. .00 0. .00 PROD

ATOM 6569 CB LEU X 650 -10 .211 -10 .767 -2. .658 0. .00 0. .00 PROD

ATOM 6570 HB1 LEU X 650 -9 .550 -11 .163 -1. .858 0. .00 0. .00 PROD

ATOM 6571 HB2 LEU X 650 -11 .227 -10 .935 -2. .242 0. .00 0. .00 PROD

ATOM 6572 CG LEU X 650 -10 .016 -11 .691 -3. .899 0. .00 0. .00 PROD

ATOM 6573 HG LEU X 650 -8 .949 -11 .678 -4. .210 0. .00 0. .00 PROD

ATOM 6574 CD1 LEU X 650 -10 .417 -13 .130 -3. .519 0. .00 0. .00 PROD

ATOM 6575 HD11 LEU X 650 -9 .831 -13 .545 -2. .671 0. .00 0. .00 PROD

ATOM 6576 HD12 LEU X 650 -11 .514 -13 .221 -3. .368 0. .00 0. .00 PROD

ATOM 6577 HD13 LEU X 650 -10 .228 -13 .781 -4. .400 0. .00 0. .00 PROD

ATOM 6578 CD2 LEU X 650 -10 .891 -11 .459 -5. .115 0. .00 0. .00 PROD

ATOM 6579 HD21 LEU X 650 -11 .991 -11 .391 -4. .977 0. .00 0. .00 PROD

ATOM 6580 HD22 LEU X 650 -10 .545 -10 .448 -5. .419 0. .00 0. .00 PROD

ATOM 6581 HD23 LEU X 650 -10 .605 -12 .229 -5. .864 0. .00 0. .00 PROD

ATOM 6582 C LEU X 650 -10 .788 -8 .389 -3. .483 0. .00 0. .00 PROD

ATOM 6583 O LEU X 650 -10 .397 -7 .786 -4. .494 0. .00 0. .00 PROD

ATOM 6584 N MET X 651 -11 .999 -8 .185 -2. .839 0. .00 0. .00 PROD

ATOM 6585 HN MET X 651 -12 .244 -8 .721 -2. .035 0. .00 0. .00 PROD

ATOM 6586 CA MET X 651 -12 .977 -7 .217 -3. .332 0. .00 0. .00 PROD

ATOM 6587 HA MET X 651 -13 .007 -7 .442 -4. .388 0. .00 0. .00 PROD

ATOM 6588 CB MET X 651 -14 .272 -7 .647 -2. .686 0. .00 0. .00 PROD

ATOM 6589 HB1 MET X 651 -13 .944 -7 .762 -1. .631 0. .00 0. .00 PROD

ATOM 6590 HB2 MET X 651 -15 .066 -6 .888 -2. .852 0. .00 0. .00 PROD

ATOM 6591 CG MET X 651 -14 .945 -9 .021 -3. .012 0. .00 0. .00 PROD

ATOM 6592 HG1 MET X 651 -14 .978 -9 .126 -4. .118 0. .00 0. .00 PROD

ATOM 6593 HG2 MET X 651 -14 .165 -9 .730 -2. .661 0. .00 0. .00 PROD

ATOM 6594 C MET X 651 -12 .619 -5 .741 -3. .156 0. .00 0. .00 PROD

ATOM 6595 O MET X 651 -12 .877 -4 .959 -4. .086 0. .00 0. .00 PROD

ATOM 6596 N TYR X 652 -11 .859 -5 .444 -2. .170 0. .00 0. .00 PROD

ATOM 6597 HN TYR X 652 -11 .579 -6 .132 -1. .505 0. .00 0. .00 PROD

ATOM 6598 CA TYR X 652 -11 .342 -4 .027 -1. .971 0. .00 0. .00 PROD

ATOM 6599 HA TYR X 652 -12 .284 -3 .507 -2. .060 0. .00 0. .00 PROD ATOM 6600 CB TYR X 652 -10.829 -3.809 -0..604 0..00 0..00 PROD

ATOM 6601 HB1 TYR X 652 -11 .624 -4 .283 0. .011 0. .00 0. .00 PROD

ATOM 6602 HB2 TYR X 652 -9 .846 -4 .264 -0. .357 0. .00 0. .00 PROD

ATOM 6603 CG TYR X 652 -10 .795 -2 .307 -0. .176 0. .00 0. .00 PROD

ATOM 6604 CD1 TYR X 652 -9 .510 -1 .655 -0. .074 0. .00 0. .00 PROD

ATOM 6605 HD1 TYR X 652 -8 .672 -2 .316 -0. .245 0. .00 0. .00 PROD

ATOM 6606 CE1 TYR X 652 -9 .480 -0 .292 0. .266 0. .00 0. .00 PROD

ATOM 6607 HE1 TYR X 652 -8 .527 0 .210 0. .341 0. .00 0. .00 PROD

ATOM 6608 CZ TYR X 652 -10 .622 0 .507 0. .532 0. .00 0. .00 PROD

ATOM 6609 OH TYR X 652 -10 .599 1 .850 0. .796 0. .00 0. .00 PROD

ATOM 6610 HH TYR X 652 -9 .720 2 .121 1. .071 0. .00 0. .00 PROD

ATOM 6611 CD2 TYR X 652 -11 .933 -1 .578 0. .248 0. .00 0. .00 PROD

ATOM 6612 HD2 TYR X 652 -12 .886 -2 .085 0. .247 0. .00 0. .00 PROD

ATOM 6613 CE2 TYR X 652 -11 .844 -0 .228 0. .450 0. .00 0. .00 PROD

ATOM 6614 HE2 TYR X 652 -12 .704 0 .307 0. .825 0. .00 0. .00 PROD

ATOM 6615 C TYR X 652 -10 .441 -3 .594 -3. .114 0. .00 0. .00 PROD

ATOM 6616 O TYR X 652 -10 .526 -2 .509 -3. .705 0. .00 0. .00 PROD

ATOM 6617 N ALA X 653 -9 .600 -4 .575 -3. .512 0. .00 0. .00 PROD

ATOM 6618 HN ALA X 653 -9 .522 -5 .402 -2. .961 0. .00 0. .00 PROD

ATOM 6619 CA ALA X 653 -8 .725 -4 .492 -4. .663 0. .00 0. .00 PROD

ATOM 6620 HA ALA X 653 -8 .053 -3 .669 -4. .469 0. .00 0. .00 PROD

ATOM 6621 CB ALA X 653 -7 .887 -5 .816 -4. .773 0. .00 0. .00 PROD

ATOM 6622 HB1 ALA X 653 -8 .352 -6 .651 -5. .340 0. .00 0. .00 PROD

ATOM 6623 HB2 ALA X 653 -6 .910 -5 .563 -5. .236 0. .00 0. .00 PROD

ATOM 6624 HB3 ALA X 653 -7 .729 -6 .198 -3. .741 0. .00 0. .00 PROD

ATOM 6625 C ALA X 653 -9 .418 -4 .199 -5. .991 0. .00 0. .00 PROD

ATOM 6626 O ALA X 653 -8 .965 -3 .392 -6. .781 0. .00 0. .00 PROD

ATOM 6627 N SER X 654 -10 .602 -4 .828 -6. .249 0. .00 0. .00 PROD

ATOM 6628 HN SER X 654 -11 .213 -5 .198 -5. .554 0. .00 0. .00 PROD

ATOM 6629 CA SER X 654 -11 .347 -4 .588 -7. .434 0. .00 0. .00 PROD

ATOM 6630 HA SER X 654 -10 .636 -4 .409 -8. .227 0. .00 0. .00 PROD

ATOM 6631 CB SER X 654 -12 .246 -5 .760 -7. .773 0. .00 0. .00 PROD

ATOM 6632 HB1 SER X 654 -12 .781 -5 .455 -8. .698 0. .00 0. .00 PROD

ATOM 6633 HB2 SER X 654 -11 .633 -6 .671 -7. .946 0. .00 0. .00 PROD

ATOM 6634 OG SER X 654 -13 .186 -6 .164 -6. .804 0. .00 0. .00 PROD

ATOM 6635 HG1 SER X 654 -13 .629 -6 .962 -7. .100 0. .00 0. .00 PROD

ATOM 6636 C SER X 654 -12 .109 -3 .321 -7. .412 0. .00 0. .00 PROD

ATOM 6637 O SER X 654 -12 .221 -2 .703 -8. .445 0. .00 0. .00 PROD

ATOM 6638 N ILE X 655 -12 .543 -2 .867 -6. .239 0. .00 0. .00 PROD

ATOM 6639 HN ILE X 655 -12 .379 -3 .473 -5. .465 0. .00 0. .00 PROD

ATOM 6640 CA ILE X 655 -13 .310 -1 .595 -6. .148 0. .00 0. .00 PROD

ATOM 6641 HA ILE X 655 -14 .140 -1 .677 -6. .834 0. .00 0. .00 PROD

ATOM 6642 CB ILE X 655 -14 .040 -1 .524 -4. .800 0. .00 0. .00 PROD

ATOM 6643 HB ILE X 655 -13 .311 -1 .851 -4. .027 0. .00 0. .00 PROD

ATOM 6644 CG2 ILE X 655 -14 .667 -0 .137 -4. .649 0. .00 0. .00 PROD

ATOM 6645 HG21 ILE X 655 -15 .260 -0 .099 -3. .710 0. .00 0. .00 PROD

ATOM 6646 HG22 ILE X 655 -13 .869 0 .636 -4. .664 0. .00 0. .00 PROD

ATOM 6647 HG23 ILE X 655 -15 .312 -0 .044 -5. .548 0. .00 0. .00 PROD

ATOM 6648 CGI ILE X 655 -15 .168 -2 .663 -4. .847 0. .00 0. .00 PROD

ATOM 6649 HG11 ILE X 655 -15 .904 -2 .469 -5. .657 0. .00 0. .00 PROD

ATOM 6650 HG12 ILE X 655 -14 .719 -3 .661 -5. .037 0. .00 0. .00 PROD

ATOM 6651 CD ILE X 655 -15 .789 -2 .794 -3. .439 0. .00 0. .00 PROD

ATOM 6652 HD1 ILE X 655 -14 .938 -2 .957 -2. .744 0. .00 0. .00 PROD

ATOM 6653 HD2 ILE X 655 -16 .275 -1 .873 -3. .052 0. .00 0. .00 PROD

ATOM 6654 HD3 ILE X 655 -16 .442 -3 .693 -3. .446 0. .00 0. .00 PROD

ATOM 6655 C ILE X 655 -12 .376 -0 .360 -6. .277 0. .00 0. .00 PROD

ATOM 6656 O ILE X 655 -12 .563 0 .658 -6. .908 0. .00 0. .00 PROD

ATOM 6657 N PHE X 656 -11 .098 -0 .546 -5. .846 0. .00 0. .00 PROD

ATOM 6658 HN PHE X 656 -10 .814 -1 .371 -5. .365 0. .00 0. .00 PROD

ATOM 6659 CA PHE X 656 -10 .065 0 .410 -5. .883 0. .00 0. .00 PROD

ATOM 6660 HA PHE X 656 -10 .442 1 .380 -5. .595 0. .00 0. .00 PROD

ATOM 6661 CB PHE X 656 -8 .951 -0 .133 -4. .986 0. .00 0. .00 PROD

ATOM 6662 HB1 PHE X 656 -9 .378 -0 .309 -3. .976 0. .00 0. .00 PROD

ATOM 6663 HB2 PHE X 656 -8 .690 -1 .188 -5. .216 0. .00 0. .00 PROD

ATOM 6664 CG PHE X 656 -7 .768 0 .788 -4. .768 0. .00 0. .00 PROD

ATOM 6665 CD1 PHE X 656 -6 .479 0 .245 -4. .924 0. .00 0. .00 PROD ATOM 6666 HD1 PHE X 656 -6.299 -0.801 -5..127 0..00 0..00 PROD

ATOM 6667 CE1 PHE X 656 -5 .395 1 .104 -4. .694 0. .00 0. .00 PROD

ATOM 6668 HE1 PHE X 656 -4 .424 0 .718 -4. .966 0. .00 0. .00 PROD

ATOM 6669 CZ PHE X 656 -5 .619 2 .409 -4. .381 0. .00 0. .00 PROD

ATOM 6670 HZ PHE X 656 -4 .760 3 .021 -4. .148 0. .00 0. .00 PROD

ATOM 6671 CD2 PHE X 656 -8 .040 2 .033 -4. .289 0. .00 0. .00 PROD

ATOM 6672 HD2 PHE X 656 -9 .002 2 .505 -4. .154 0. .00 0. .00 PROD

ATOM 6673 CE2 PHE X 656 -6 .925 2 .906 -4. .150 0. .00 0. .00 PROD

ATOM 6674 HE2 PHE X 656 -7 .223 3 .920 -3. .927 0. .00 0. .00 PROD

ATOM 6675 C PHE X 656 -9 .510 0 .552 -7. .260 0. .00 0. .00 PROD

ATOM 6676 O PHE X 656 -9 .275 1 .631 -7. .741 0. .00 0. .00 PROD

ATOM 6677 N GLY X 657 -9 .461 -0 .612 -7. .971 0. .00 0. .00 PROD

ATOM 6678 HN GLY X 657 -9 .627 -1 .541 -7. .649 0. .00 0. .00 PROD

ATOM 6679 CA GLY X 657 -9 .003 -0 .617 -9. .359 0. .00 0. .00 PROD

ATOM 6680 HA1 GLY X 657 -8 .830 -1 .665 -9. .554 0. .00 0. .00 PROD

ATOM 6681 HA2 GLY X 657 -7 .999 -0 .227 -9. .424 0. .00 0. .00 PROD

ATOM 6682 C GLY X 657 -9 .942 -0 .025 -10. .379 0. .00 0. .00 PROD

ATOM 6683 O GLY X 657 -9 .522 0 .630 -11. .318 0. .00 0. .00 PROD

ATOM 6684 N ASN X 658 -11 .257 -0 .047 -10. .104 0. .00 0. .00 PROD

ATOM 6685 HN ASN X 658 -11 .659 -0 .588 -9. .370 0. .00 0. .00 PROD

ATOM 6686 CA ASN X 658 -12 .324 0 .665 -10. .875 0. .00 0. .00 PROD

ATOM 6687 HA ASN X 658 -12 .234 0 .470 -11. .934 0. .00 0. .00 PROD

ATOM 6688 CB ASN X 658 -13 .739 0 .218 -10. .500 0. .00 0. .00 PROD

ATOM 6689 HB1 ASN X 658 -13 .744 0 .003 -9. .410 0. .00 0. .00 PROD

ATOM 6690 HB2 ASN X 658 -14 .394 1 .077 -10. .764 0. .00 0. .00 PROD

ATOM 6691 CG ASN X 658 -14 .037 -1 .074 -11. .197 0. .00 0. .00 PROD

ATOM 6692 OD1 ASN X 658 -13 .473 -1 .549 -12. .198 0. .00 0. .00 PROD

ATOM 6693 ND2 ASN X 658 -14 .878 -1 .907 -10. .637 0. .00 0. .00 PROD

ATOM 6694 HD21 ASN X 658 -15 .437 -1 .729 -9. .827 0. .00 0. .00 PROD

ATOM 6695 HD22 ASN X 658 -15 .036 -2 .779 -11. .100 0. .00 0. .00 PROD

ATOM 6696 C ASN X 658 -12 .324 2 .165 -10. .760 0. .00 0. .00 PROD

ATOM 6697 O ASN X 658 -12 .519 2 .816 -11. .810 0. .00 0. .00 PROD

ATOM 6698 N VAL X 659 -12 .154 2 .765 -9. .522 0. .00 0. .00 PROD

ATOM 6699 HN VAL X 659 -12 . Ill 2 .285 -8. .650 0. .00 0. .00 PROD

ATOM 6700 CA VAL X 659 -12 .070 4 .192 -9. .374 0. .00 0. .00 PROD

ATOM 6701 HA VAL X 659 -12 .777 4 .618 -10. .070 0. .00 0. .00 PROD

ATOM 6702 CB VAL X 659 -12 .351 4 .602 -7. .891 0. .00 0. .00 PROD

ATOM 6703 HB VAL X 659 -12 .341 5 .708 -7. .995 0. .00 0. .00 PROD

ATOM 6704 CGI VAL X 659 -13 .762 4 .083 -7. .392 0. .00 0. .00 PROD

ATOM 6705 HG11 VAL X 659 -14 .508 4 .295 -8. .188 0. .00 0. .00 PROD

ATOM 6706 HG12 VAL X 659 -13 .951 3 .026 -7. .106 0. .00 0. .00 PROD

ATOM 6707 HG13 VAL X 659 -14 .016 4 .727 -6. .523 0. .00 0. .00 PROD

ATOM 6708 CG2 VAL X 659 -11 .198 4 . Ill -7. .041 0. .00 0. .00 PROD

ATOM 6709 HG21 VAL X 659 -11 .450 4 .309 -5. .977 0. .00 0. .00 PROD

ATOM 6710 HG22 VAL X 659 -11 .147 3 .003 -7. .105 0. .00 0. .00 PROD

ATOM 6711 HG23 VAL X 659 -10 .231 4 .644 -7. .161 0. .00 0. .00 PROD

ATOM 6712 C VAL X 659 -10 .747 4 .605 -10. .027 0. .00 0. .00 PROD

ATOM 6713 O VAL X 659 -10 .754 5 .627 -10. .818 0. .00 0. .00 PROD

ATOM 6714 N SER X 660 -9 .582 3 .915 -9. .838 0. .00 0. .00 PROD

ATOM 6715 HN SER X 660 -9 .555 3 .185 -9. .160 0. .00 0. .00 PROD

ATOM 6716 CA SER X 660 -8 .303 4 .259 -10. .422 0. .00 0. .00 PROD

ATOM 6717 HA SER X 660 -7 .938 5 .082 -9. .825 0. .00 0. .00 PROD

ATOM 6718 CB SER X 660 -7 .321 3 .029 -10. .253 0. .00 0. .00 PROD

ATOM 6719 HB1 SER X 660 -7 .258 2 .667 -9. .205 0. .00 0. .00 PROD

ATOM 6720 HB2 SER X 660 -7 .604 2 .161 -10. .887 0. .00 0. .00 PROD

ATOM 6721 OG SER X 660 -5 .948 3 .346 -10. .503 0. .00 0. .00 PROD

ATOM 6722 HG1 SER X 660 -5 .316 2 .713 -10. .155 0. .00 0. .00 PROD

ATOM 6723 C SER X 660 -8 .201 4 .634 -11. .898 0. .00 0. .00 PROD

ATOM 6724 O SER X 660 -7 .607 5 .619 -12. .346 0. .00 0. .00 PROD

ATOM 6725 N ALA X 661 -8 .909 3 .864 -12. .702 0. .00 0. .00 PROD

ATOM 6726 HN ALA X 661 -9 .422 3 .106 -12. .306 0. .00 0. .00 PROD

ATOM 6727 CA ALA X 661 -9 .048 3 .884 -14. .130 0. .00 0. .00 PROD

ATOM 6728 HA ALA X 661 -8 .087 4 .008 -14. .608 0. .00 0. .00 PROD

ATOM 6729 CB ALA X 661 -9 .791 2 .650 -14. .478 0. .00 0. .00 PROD

ATOM 6730 HB1 ALA X 661 -10 .793 2 .635 -14. .000 0. .00 0. .00 PROD

ATOM 6731 HB2 ALA X 661 -10 .003 2 .507 -15. .559 0. .00 0. .00 PROD ATOM 6732 HB3 ALA X 661 -9.218 1.795 -14..059 0..00 0..00 PROD

ATOM 6733 C ALA X 661 -9 .791 5 .120 -14. .619 0. .00 0. .00 PROD

ATOM 6734 O ALA X 661 -9 .360 5 .821 -15. .549 0. .00 0. .00 PROD

ATOM 6735 N ILE X 662 -10 .960 5 .421 -14. .071 0. .00 0. .00 PROD

ATOM 6736 HN ILE X 662 -11 .358 4 .913 -13. .311 0. .00 0. .00 PROD

ATOM 6737 CA ILE X 662 -11 .861 6 .564 -14. .452 0. .00 0. .00 PROD

ATOM 6738 HA ILE X 662 -12 .219 6 .454 -15. .466 0. .00 0. .00 PROD

ATOM 6739 CB ILE X 662 -13 .125 6 .630 -13. .572 0. .00 0. .00 PROD

ATOM 6740 HB ILE X 662 -12 .863 6 .674 -12. .493 0. .00 0. .00 PROD

ATOM 6741 CG2 ILE X 662 -14 .005 7 .868 -13. .903 0. .00 0. .00 PROD

ATOM 6742 HG21 ILE X 662 -14 .157 7 .947 -15. .000 0. .00 0. .00 PROD

ATOM 6743 HG22 ILE X 662 -14 .976 7 .820 -13. .365 0. .00 0. .00 PROD

ATOM 6744 HG23 ILE X 662 -13 .495 8 .763 -13. .487 0. .00 0. .00 PROD

ATOM 6745 CGI ILE X 662 -13 .888 5 .295 -13. .662 0. .00 0. .00 PROD

ATOM 6746 HG11 ILE X 662 -13 .203 4 .424 -13. .738 0. .00 0. .00 PROD

ATOM 6747 HG12 ILE X 662 -14 .423 5 .048 -12. .720 0. .00 0. .00 PROD

ATOM 6748 CD ILE X 662 -14 .845 5 .154 -14. .785 0. .00 0. .00 PROD

ATOM 6749 HD1 ILE X 662 -14 .470 5 .733 -15. .657 0. .00 0. .00 PROD

ATOM 6750 HD2 ILE X 662 -14 .900 4 .102 -15. .137 0. .00 0. .00 PROD

ATOM 6751 HD3 ILE X 662 -15 .818 5 .653 -14. .590 0. .00 0. .00 PROD

ATOM 6752 C ILE X 662 -11 .222 7 .963 -14. .316 0. .00 0. .00 PROD

ATOM 6753 O ILE X 662 -11 .367 8 .834 -15. .164 0. .00 0. .00 PROD

ATOM 6754 N ILE X 663 -10 .463 8 .201 -13. .254 0. .00 0. .00 PROD

ATOM 6755 HN ILE X 663 -10 .399 7 .562 -12. .491 0. .00 0. .00 PROD

ATOM 6756 CA ILE X 663 -10 .075 9 .535 -12. .870 0. .00 0. .00 PROD

ATOM 6757 HA ILE X 663 -10 .821 10 .208 -13. .267 0. .00 0. .00 PROD

ATOM 6758 CB ILE X 663 -10 .081 9 .672 -11. .303 0. .00 0. .00 PROD

ATOM 6759 HB ILE X 663 -9 .281 9 .051 -10. .845 0. .00 0. .00 PROD

ATOM 6760 CG2 ILE X 663 -9 .896 11 .191 -10. .999 0. .00 0. .00 PROD

ATOM 6761 HG21 ILE X 663 -8 .874 11 .415 -11. .375 0. .00 0. .00 PROD

ATOM 6762 HG22 ILE X 663 -10 .666 11 .669 -11. .641 0. .00 0. .00 PROD

ATOM 6763 HG23 ILE X 663 -10 .049 11 .503 -9. .944 0. .00 0. .00 PROD

ATOM 6764 CGI ILE X 663 -11 .375 9 .215 -10. .629 0. .00 0. .00 PROD

ATOM 6765 HG11 ILE X 663 -11 .655 8 .191 -10. .959 0. .00 0. .00 PROD

ATOM 6766 HG12 ILE X 663 -11 .186 9 .109 -9. .540 0. .00 0. .00 PROD

ATOM 6767 CD ILE X 663 -12 .628 10 .021 -10. .835 0. .00 0. .00 PROD

ATOM 6768 HD1 ILE X 663 -13 .058 9 .738 -11. .819 0. .00 0. .00 PROD

ATOM 6769 HD2 ILE X 663 -13 .421 9 .810 -10. .086 0. .00 0. .00 PROD

ATOM 6770 HD3 ILE X 663 -12 .431 11 .114 -10. .812 0. .00 0. .00 PROD

ATOM 6771 C ILE X 663 -8 .689 9 .842 -13. .491 0. .00 0. .00 PROD

ATOM 6772 O ILE X 663 -8 .176 10 .922 -13. .569 0. .00 0. .00 PROD

ATOM 6773 N GLN X 664 -8 .083 8 .822 -14. .107 0. .00 0. .00 PROD

ATOM 6774 HN GLN X 664 -8 .342 7 .878 -13. .921 0. .00 0. .00 PROD

ATOM 6775 CA GLN X 664 -6 .978 9 .029 -15. .144 0. .00 0. .00 PROD

ATOM 6776 HA GLN X 664 -6 .219 9 .698 -14. .765 0. .00 0. .00 PROD

ATOM 6777 CB GLN X 664 -6 .271 7 .635 -15. .392 0. .00 0. .00 PROD

ATOM 6778 HB1 GLN X 664 -7 .142 6 .962 -15. .238 0. .00 0. .00 PROD

ATOM 6779 HB2 GLN X 664 -6 .050 7 .577 -16. .479 0. .00 0. .00 PROD

ATOM 6780 CG GLN X 664 -5 .220 7 .245 -14. .374 0. .00 0. .00 PROD

ATOM 6781 HG1 GLN X 664 -4 .318 7 .881 -14. .505 0. .00 0. .00 PROD

ATOM 6782 HG2 GLN X 664 -5 .625 7 .380 -13. .348 0. .00 0. .00 PROD

ATOM 6783 CD GLN X 664 -4 .752 5 .819 -14. .589 0. .00 0. .00 PROD

ATOM 6784 OE1 GLN X 664 -3 .816 5 .650 -15. .361 0. .00 0. .00 PROD

ATOM 6785 NE2 GLN X 664 -5 .244 4 .878 -13. .782 0. .00 0. .00 PROD

ATOM 6786 HE21 GLN X 664 -5 .987 5 .088 -13. .147 0. .00 0. .00 PROD

ATOM 6787 HE22 GLN X 664 -4 .813 3 .976 -13. .768 0. .00 0. .00 PROD

ATOM 6788 C GLN X 664 -7 .413 9 .579 -16. .525 0. .00 0. .00 PROD

ATOM 6789 O GLN X 664 -6 .614 9 .966 -17. .411 0. .00 0. .00 PROD

ATOM 6790 N ARG X 665 -8 .792 9 .553 -16. .812 0. .00 0. .00 PROD

ATOM 6791 HN ARG X 665 -9 .366 9 .275 -16. .045 0. .00 0. .00 PROD

ATOM 6792 CA ARG X 665 -9 .511 9 .844 -18. .065 0. .00 0. .00 PROD

ATOM 6793 HA ARG X 665 -8 .763 9 .895 -18. .843 0. .00 0. .00 PROD

ATOM 6794 CB ARG X 665 -10 .568 8 .724 -18. .376 0. .00 0. .00 PROD

ATOM 6795 HB1 ARG X 665 -11 .319 8 .817 -17. .562 0. .00 0. .00 PROD

ATOM 6796 HB2 ARG X 665 -11 .012 8 .993 -19. .358 0. .00 0. .00 PROD

ATOM 6797 CG ARG X 665 -10 .159 7 .276 -18. .603 0. .00 0. .00 PROD ATOM 6798 HG1 ARG X 665 -9.683 7.286 -19..606 0..00 0..00 PROD

ATOM 6799 HG2 ARG X 665 -9 .407 7 .056 -17. .815 0. .00 0. .00 PROD

ATOM 6800 CD ARG X 665 -11 .291 6 .228 -18. .535 0. .00 0. .00 PROD

ATOM 6801 HD1 ARG X 665 -11 .697 6 .155 -17. .503 0. .00 0. .00 PROD

ATOM 6802 HD2 ARG X 665 -12 .100 6 .430 -19. .270 0. .00 0. .00 PROD

ATOM 6803 NE ARG X 665 -10 .676 4 .956 -19. .009 0. .00 0. .00 PROD

ATOM 6804 HE ARG X 665 -9 .696 4 .935 -19. .207 0. .00 0. .00 PROD

ATOM 6805 CZ ARG X 665 -11 .266 3 .788 -19. .066 0. .00 0. .00 PROD

ATOM 6806 NH1 ARG X 665 -12 .579 3 .637 -18. .879 0. .00 0. .00 PROD

ATOM 6807 HH11 ARG X 665 -12 .922 2 .699 -18. .943 0. .00 0. .00 PROD

ATOM 6808 HH12 ARG X 665 -13 .134 4 .464 -18. .962 0. .00 0. .00 PROD

ATOM 6809 NH2 ARG X 665 -10 .495 2 .777 -19. .347 0. .00 0. .00 PROD

ATOM 6810 HH21 ARG X 665 -10 .920 1 .879 -19. .455 0. .00 0. .00 PROD

ATOM 6811 HH22 ARG X 665 -9 .569 3 .019 -19. .637 0. .00 0. .00 PROD

ATOM 6812 C ARG X 665 -10 .175 11 .259 -18. .055 0. .00 0. .00 PROD

ATOM 6813 O ARG X 665 -10 .770 11 .754 -19. .044 0. .00 0. .00 PROD

ATOM 6814 N LEU X 666 -9 .976 11 .977 -16. .926 0. .00 0. .00 PROD

ATOM 6815 HN LEU X 666 -9 .350 11 .646 -16. .223 0. .00 0. .00 PROD

ATOM 6816 CA LEU X 666 -10 .169 13 .416 -16. .684 0. .00 0. .00 PROD

ATOM 6817 HA LEU X 666 -11 .180 13 .756 -16. .854 0. .00 0. .00 PROD

ATOM 6818 CB LEU X 666 -9 .970 13 .832 -15. .246 0. .00 0. .00 PROD

ATOM 6819 HB1 LEU X 666 -8 .934 13 .576 -14. .938 0. .00 0. .00 PROD

ATOM 6820 HB2 LEU X 666 -10 .134 14 .931 -15. .221 0. .00 0. .00 PROD

ATOM 6821 CG LEU X 666 -11 .008 13 .257 -14. .179 0. .00 0. .00 PROD

ATOM 6822 HG LEU X 666 -10 .420 12 .427 -13. .730 0. .00 0. .00 PROD

ATOM 6823 CD1 LEU X 666 -11 .230 14 .171 -12. .983 0. .00 0. .00 PROD

ATOM 6824 HD11 LEU X 666 -12 .074 14 .851 -13. .227 0. .00 0. .00 PROD

ATOM 6825 HD12 LEU X 666 -11 .409 13 .601 -12. .047 0. .00 0. .00 PROD

ATOM 6826 HD13 LEU X 666 -10 .272 14 .692 -12. .770 0. .00 0. .00 PROD

ATOM 6827 CD2 LEU X 666 -12 .349 12 .649 -14. .671 0. .00 0. .00 PROD

ATOM 6828 HD21 LEU X 666 -13 .096 12 .433 -13. .878 0. .00 0. .00 PROD

ATOM 6829 HD22 LEU X 666 -12 .861 13 .437 -15. .264 0. .00 0. .00 PROD

ATOM 6830 HD23 LEU X 666 -12 .130 11 .755 -15. .292 0. .00 0. .00 PROD

ATOM 6831 C LEU X 666 -9 .229 14 .158 -17. .580 0. .00 0. .00 PROD

ATOM 6832 OT1 LEU X 666 -9 .769 14 .967 -18. .379 0. .00 0. .00 PROD

ATOM 6833 OT2 LEU X 666 -7 .982 14 .038 -17. .537 0. .00 0. .00 PROD

END

Table B

CRYSTl 0.000 0..000 0.000 90.00 90.00 9C1.00 p :1 1

ATOM 1 N TYR X 542 -14 .289 0 .008 -21. 246 0 .00 0. .00 PROA

ATOM 2 HT1 TYR X 542 -14 .002 -0 .965 -21. 016 0 .00 0. .00 PROA

ATOM 3 HT2 TYR X 542 -13 .854 0 .228 -22. 165 0 .00 0. .00 PROA

ATOM 4 HT3 TYR X 542 -15 .325 -0 .049 -21. 306 0 .00 0. .00 PROA

ATOM 5 CA TYR X 542 -13 .812 1 .026 -20. 312 0 .00 0. .00 PROA

ATOM 6 HA TYR X 542 -12 .736 1 .101 -20. 370 0 .00 0. .00 PROA

ATOM 7 CB TYR X 542 -14 .302 2 .405 -20. 828 0 .00 0. .00 PROA

ATOM 8 HB1 TYR X 542 -15 .389 2 .587 -20. 691 0 .00 0. .00 PROA

ATOM 9 HB2 TYR X 542 -14 .020 2 .476 -21. 900 0 .00 0. .00 PROA

ATOM 10 CG TYR X 542 -13 .699 3 .612 -20. 044 0 .00 0. .00 PROA

ATOM 11 CD1 TYR X 542 -14 .391 4 .126 -18. 941 0 .00 0. .00 PROA

ATOM 12 HD1 TYR X 542 -15 .297 3 .677 -18. 561 0 .00 0. .00 PROA

ATOM 13 CE1 TYR X 542 -14 .028 5 .395 -18. 359 0 .00 0. .00 PROA

ATOM 14 HE1 TYR X 542 -14 .702 5 .895 -17. 678 0 .00 0. .00 PROA

ATOM 15 CZ TYR X 542 -12 .925 6 .015 -18. 877 0 .00 0. .00 PROA

ATOM 16 OH TYR X 542 -12 .632 7 .326 -18. 478 0 .00 0. .00 PROA

ATOM 17 HH TYR X 542 -13 .316 7 .638 -17. 880 0 .00 0. .00 PROA

ATOM 18 CD2 TYR X 542 -12 .529 4 .326 -20. 519 0 .00 0. .00 PROA

ATOM 19 HD2 TYR X 542 -11 .936 3 .857 -21. 290 0 .00 0. .00 PROA

ATOM 20 CE2 TYR X 542 -12 .183 5 .522 -19. 905 0 .00 0. .00 PROA

ATOM 21 HE2 TYR X 542 -11 .322 6 .088 -20. 228 0 .00 0. .00 PROA

ATOM 22 C TYR X 542 -14 .254 0 .764 -18. 840 0 .00 0. .00 PROA

ATOM 23 O TYR X 542 -15 .398 0 .464 -18. 610 0 .00 0. .00 PROA

ATOM 24 N SER X 543 -13 .399 0 .823 -17. 853 0 .00 0. .00 PROA

ATOM 25 HN SER X 543 -12 .451 1 .057 -18. 055 0 .00 0. .00 PROA

ATOM 26 CA SER X 543 -13 .699 0 .852 -16. 409 0 .00 0. .00 PROA

ATOM 27 HA SER X 543 -12 .759 1 .054 -15. 917 0 .00 0. .00 PROA

ATOM 28 CB SER X 543 -14 .659 1 .885 -15. 857 0 .00 0. .00 PROA

ATOM 29 HB1 SER X 543 -14 .717 1 .654 -14. 771 0 .00 0. .00 PROA

ATOM 30 HB2 SER X 543 -15 .685 1 .774 -16. 267 0 .00 0. .00 PROA

ATOM 31 OG SER X 543 -14 .257 3 .242 -15. 991 0 .00 0. .00 PROA

ATOM 32 HG1 SER X 543 -15 .116 3 .636 -15. 820 0 .00 0. .00 PROA

ATOM 33 C SER X 543 -14 .122 -0 .523 -15. 839 0 .00 0. .00 PROA

ATOM 34 O SER X 543 -14 .802 -0 .660 -14. 806 0 .00 0. .00 PROA

ATOM 35 N GLU X 544 -13 .691 -1 .622 -16. 540 0 .00 0. .00 PROA

ATOM 36 HN GLU X 544 -13 .246 -1 .647 -17. 432 0 .00 0. .00 PROA

ATOM 37 CA GLU X 544 -13 .749 -2 .950 -16. 039 0 .00 0. .00 PROA

ATOM 38 HA GLU X 544 -14 .663 -3 .192 -15. 518 0 .00 0. .00 PROA

ATOM 39 CB GLU X 544 -13 .513 -3 .909 -17. 191 0 .00 0. .00 PROA

ATOM 40 HB1 GLU X 544 -13 .498 -4 .924 -16. 740 0 .00 0. .00 PROA

ATOM 41 HB2 GLU X 544 -12 .575 -3 .877 -17. 786 0 .00 0. .00 PROA

ATOM 42 CG GLU X 544 -14 .661 -4 .051 -18. 219 0 .00 0. .00 PROA

ATOM 43 HG1 GLU X 544 -15 .603 -4 .035 -17. 631 0 .00 0. .00 PROA

ATOM 44 HG2 GLU X 544 -14 .733 -5 .051 -18. 698 0 .00 0. .00 PROA

ATOM 45 CD GLU X 544 -14 .721 -3 .025 -19. 340 0 .00 0. .00 PROA

ATOM 46 OE1 GLU X 544 -15 .767 -2 .854 -20. 047 0 .00 0. .00 PROA

ATOM 47 OE2 GLU X 544 -13 .717 -2 .282 -19. 449 0 .00 0. .00 PROA

ATOM 48 C GLU X 544 -12 .828 -3 .344 -14. 870 0 .00 0. .00 PROA

ATOM 49 O GLU X 544 -11 .786 -2 .674 -14. 529 0 .00 0. .00 PROA

ATOM 50 N TYR X 545 -13 .264 -4 .403 -14. 004 0 .00 0. .00 PROA

ATOM 51 HN TYR X 545 -14 .159 -4 .790 -14. 214 0 .00 0. .00 PROA

ATOM 52 CA TYR X 545 -12 .669 -4 .742 -12. 701 0 .00 0. .00 PROA

ATOM 53 HA TYR X 545 -11 .691 -4 .322 -12. 523 0 .00 0. .00 PROA

ATOM 54 CB TYR X 545 -13 .436 -4 .134 -11. 522 0 .00 0. .00 PROA

ATOM 55 HB1 TYR X 545 -14 .443 -4 .578 -11. 372 0 .00 0. .00 PROA

ATOM 56 HB2 TYR X 545 -13 .578 -3 .035 -11. 594 0 .00 0. .00 PROA

ATOM 57 CG TYR X 545 -12 .674 -4 .335 -10. 235 0 .00 0. .00 PROA

ATOM 58 CD1 TYR X 545 -13 .014 -5 .509 -9. 515 0 .00 0. .00 PROA

ATOM 59 HD1 TYR X 545 -13 .565 -6 .337 -9. 937 0 .00 0. .00 PROA

ATOM 60 CE1 TYR X 545 -12 .224 -5 .857 -8. 428 0 .00 0. .00 PROA

ATOM 61 HE1 TYR X 545 -12 .388 -6 .803 -7. 934 0 .00 0. .00 PROA

ATOM 62 CZ TYR X 545 -11 .293 -4 .940 -7. 830 0 .00 0. .00 PROA

ATOM 63 OH TYR X 545 -10 .699 -5 .226 -6. 625 0 .00 0. .00 PROA

ATOM 64 HH TYR X 545 -10 .085 -4 .515 -6. 425 0 .00 0. .00 PROA

ATOM 65 CD2 TYR X 545 -11 .801 -3 .410 -9. 678 0 .00 0. .00 PROA ATOM 66 HD2 TYR X 545 -11.757 -2.452 -10..173 0..00 0..00 PROA

ATOM 67 CE2 TYR X 545 -11 .184 -3 .672 -8. .510 0. .00 0. .00 PROA

ATOM 68 HE2 TYR X 545 -10 .433 -2 .944 -8. .243 0. .00 0. .00 PROA

ATOM 69 C TYR X 545 -12 .650 -6 .305 -12. .702 0. .00 0. .00 PROA

ATOM 70 O TYR X 545 -13 .604 -6 .929 -13. .037 0. .00 0. .00 PROA

ATOM 71 N GLY X 546 -11 .479 -6 .907 -12. .352 0. .00 0. .00 PROA

ATOM 72 HN GLY X 546 -10 .844 -6 .243 -11. .966 0. .00 0. .00 PROA

ATOM 73 CA GLY X 546 -11 .107 -8 .317 -12. .499 0. .00 0. .00 PROA

ATOM 74 HA1 GLY X 546 -10 .246 -8 .378 -11. .850 0. .00 0. .00 PROA

ATOM 75 HA2 GLY X 546 -10 .783 -8 .399 -13. .526 0. .00 0. .00 PROA

ATOM 76 C GLY X 546 -12 .075 -9 .411 -12. .122 0. .00 0. .00 PROA

ATOM 77 O GLY X 546 -12 .727 -9 .298 -11. .116 0. .00 0. .00 PROA

ATOM 78 N ALA X 547 -12 .148 -10 .555 -12. .770 0. .00 0. .00 PROA

ATOM 79 HN ALA X 547 -11 .643 -10 .700 -13. .618 0. .00 0. .00 PROA

ATOM 80 CA ALA X 547 -12 .851 -11 .690 -12. .190 0. .00 0. .00 PROA

ATOM 81 HA ALA X 547 -13 .871 -11 .337 -12. .186 0. .00 0. .00 PROA

ATOM 82 CB ALA X 547 -12 .801 -12 .903 -13. .108 0. .00 0. .00 PROA

ATOM 83 HB1 ALA X 547 -13 .456 -13 .707 -12. .708 0. .00 0. .00 PROA

ATOM 84 HB2 ALA X 547 -11 .726 -13 .141 -13. .259 0. .00 0. .00 PROA

ATOM 85 HB3 ALA X 547 -13 .254 -12 .566 -14. .064 0. .00 0. .00 PROA

ATOM 86 C ALA X 547 -12 .326 -12 .130 -10. .836 0. .00 0. .00 PROA

ATOM 87 O ALA X 547 -11 .131 -12 .054 -10. .577 0. .00 0. .00 PROA

ATOM 88 N ALA X 548 -13 .217 -12 .720 -10. .025 0. .00 0. .00 PROA

ATOM 89 HN ALA X 548 -14 .109 -12 .987 -10. .380 0. .00 0. .00 PROA

ATOM 90 CA ALA X 548 -12 .960 -13 .289 -8. .703 0. .00 0. .00 PROA

ATOM 91 HA ALA X 548 -12 .691 -12 .409 -8. .139 0. .00 0. .00 PROA

ATOM 92 CB ALA X 548 -14 .202 -13 .928 -8. .060 0. .00 0. .00 PROA

ATOM 93 HB1 ALA X 548 -14 .616 -14 .748 -8. .685 0. .00 0. .00 PROA

ATOM 94 HB2 ALA X 548 -15 .073 -13 .239 -8. .092 0. .00 0. .00 PROA

ATOM 95 HB3 ALA X 548 -14 .008 -14 .348 -7. .050 0. .00 0. .00 PROA

ATOM 96 C ALA X 548 -11 .906 -14 .348 -8. .596 0. .00 0. .00 PROA

ATOM 97 O ALA X 548 -11 .124 -14 .314 -7. .640 0. .00 0. .00 PROA

ATOM 98 N VAL X 549 -11 .855 -15 .350 -9. .547 0. .00 0. .00 PROA

ATOM 99 HN VAL X 549 -12 .568 -15 .261 -10. .239 0. .00 0. .00 PROA

ATOM 100 CA VAL X 549 -10 .898 -16 .350 -9. .566 0. .00 0. .00 PROA

ATOM 101 HA VAL X 549 -10 .988 -16 .774 -8. .577 0. .00 0. .00 PROA

ATOM 102 CB VAL X 549 -11 .208 -17 .451 -10. .636 0. .00 0. .00 PROA

ATOM 103 HB VAL X 549 -10 .374 -18 .185 -10. .661 0. .00 0. .00 PROA

ATOM 104 CGI VAL X 549 -12 .444 -18 .163 -10. .153 0. .00 0. .00 PROA

ATOM 105 HG11 VAL X 549 -12 .259 -18 .752 -9. .229 0. .00 0. .00 PROA

ATOM 106 HG12 VAL X 549 -12 .583 -18 .955 -10. .920 0. .00 0. .00 PROA

ATOM 107 HG13 VAL X 549 -13 .327 -17 .491 -10. .103 0. .00 0. .00 PROA

ATOM 108 CG2 VAL X 549 -11 .285 -16 .836 -12. .027 0. .00 0. .00 PROA

ATOM 109 HG21 VAL X 549 -10 .458 -16 .125 -12. .237 0. .00 0. .00 PROA

ATOM 110 HG22 VAL X 549 -12 .278 -16 .369 -12. .199 0. .00 0. .00 PROA

ATOM 111 HG23 VAL X 549 -11 .250 -17 .743 -12. .668 0. .00 0. .00 PROA

ATOM 112 C VAL X 549 -9 .561 -15 .862 -9. .779 0. .00 0. .00 PROA

ATOM 113 O VAL X 549 -8 .576 -16 .434 -9. .386 0. .00 0. .00 PROA

ATOM 114 N LEU X 550 -9 .392 -14 .646 -10. .425 0. .00 0. .00 PROA

ATOM 115 HN LEU X 550 -10 .189 -14 .069 -10. .588 0. .00 0. .00 PROA

ATOM 116 CA LEU X 550 -8 .047 -14 .098 -10. .712 0. .00 0. .00 PROA

ATOM 117 HA LEU X 550 -7 .448 -14 .941 -11. .023 0. .00 0. .00 PROA

ATOM 118 CB LEU X 550 -8 .057 -12 .747 -11. .608 0. .00 0. .00 PROA

ATOM 119 HB1 LEU X 550 -8 .659 -12 .027 -11. .014 0. .00 0. .00 PROA

ATOM 120 HB2 LEU X 550 -8 .511 -13 .033 -12. .581 0. .00 0. .00 PROA

ATOM 121 CG LEU X 550 -6 .716 -12 .141 -11. .888 0. .00 0. .00 PROA

ATOM 122 HG LEU X 550 -6 .151 -12 .107 -10. .932 0. .00 0. .00 PROA

ATOM 123 CD1 LEU X 550 -5 .895 -12 .781 -13. .004 0. .00 0. .00 PROA

ATOM 124 HD11 LEU X 550 -6 .014 -13 .883 -12. .932 0. .00 0. .00 PROA

ATOM 125 HD12 LEU X 550 -4 .853 -12 .401 -12. .947 0. .00 0. .00 PROA

ATOM 126 HD13 LEU X 550 -6 .245 -12 .506 -14. .022 0. .00 0. .00 PROA

ATOM 127 CD2 LEU X 550 -6 .870 -10 .691 -12. .214 0. .00 0. .00 PROA

ATOM 128 HD21 LEU X 550 -5 .834 -10 .377 -12. .464 0. .00 0. .00 PROA

ATOM 129 HD22 LEU X 550 -7 .241 -10 .118 -11. .337 0. .00 0. .00 PROA

ATOM 130 HD23 LEU X 550 -7 .593 -10 .539 -13. .044 0. .00 0. .00 PROA

ATOM 131 C LEU X 550 -7 .455 -13 .668 -9. .341 0. .00 0. .00 PROA ATOM 132 O LEU X 550 -6.335 -14.067 -9..058 0..00 0..00 PROA

ATOM 133 N PHE X 551 -8 .254 -13 .003 -8. .476 0. .00 0. .00 PROA

ATOM 134 HN PHE X 551 -9 .217 -13 .024 -8. .733 0. .00 0. .00 PROA

ATOM 135 CA PHE X 551 -7 .945 -12 .627 -7. .069 0. .00 0. .00 PROA

ATOM 136 HA PHE X 551 -7 .006 -12 .099 -7. .003 0. .00 0. .00 PROA

ATOM 137 CB PHE X 551 -8 .928 -11 .573 -6. .513 0. .00 0. .00 PROA

ATOM 138 HB1 PHE X 551 -8 .714 -11 .390 -5. .438 0. .00 0. .00 PROA

ATOM 139 HB2 PHE X 551 -9 .982 -11 .922 -6. .473 0. .00 0. .00 PROA

ATOM 140 CG PHE X 551 -8 .846 -10 .338 -7. .331 0. .00 0. .00 PROA

ATOM 141 CD1 PHE X 551 -7 .820 -9 .431 -7. .050 0. .00 0. .00 PROA

ATOM 142 HD1 PHE X 551 -7 .079 -9 .633 -6. .291 0. .00 0. .00 PROA

ATOM 143 CE1 PHE X 551 -7 .705 -8 .181 -7. .686 0. .00 0. .00 PROA

ATOM 144 HE1 PHE X 551 -6 .954 -7 .522 -7. .275 0. .00 0. .00 PROA

ATOM 145 CZ PHE X 551 -8 .670 -7 .765 -8. .594 0. .00 0. .00 PROA

ATOM 146 HZ PHE X 551 -8 .604 -6 .746 -8. .944 0. .00 0. .00 PROA

ATOM 147 CD2 PHE X 551 -9 .680 -9 .952 -8. .368 0. .00 0. .00 PROA

ATOM 148 HD2 PHE X 551 -10 .474 -10 .647 -8. .598 0. .00 0. .00 PROA

ATOM 149 CE2 PHE X 551 -9 .695 -8 .678 -9. .013 0. .00 0. .00 PROA

ATOM 150 HE2 PHE X 551 -10 .365 -8 .502 -9. .842 0. .00 0. .00 PROA

ATOM 151 C PHE X 551 -7 .752 -13 .848 -6. .239 0. .00 0. .00 PROA

ATOM 152 O PHE X 551 -6 .790 -13 .750 -5. .416 0. .00 0. .00 PROA

ATOM 153 N LEU X 552 -8 .521 -14 .890 -6. .339 0. .00 0. .00 PROA

ATOM 154 HN LEU X 552 -9 .313 -14 .840 -6. .942 0. .00 0. .00 PROA

ATOM 155 CA LEU X 552 -8 .224 -16 .161 -5. .685 0. .00 0. .00 PROA

ATOM 156 HA LEU X 552 -8 .199 -16 .021 -4. .614 0. .00 0. .00 PROA

ATOM 157 CB LEU X 552 -9 .338 -17 .237 -5. .937 0. .00 0. .00 PROA

ATOM 158 HB1 LEU X 552 -9 .385 -17 .395 -7. .036 0. .00 0. .00 PROA

ATOM 159 HB2 LEU X 552 -10 .287 -16 .669 -5. .828 0. .00 0. .00 PROA

ATOM 160 CG LEU X 552 -9 .316 -18 .518 -5. .149 0. .00 0. .00 PROA

ATOM 161 HG LEU X 552 -8 .296 -18 .937 -5. .288 0. .00 0. .00 PROA

ATOM 162 CD1 LEU X 552 -9 .599 -18 .350 -3. .697 0. .00 0. .00 PROA

ATOM 163 HD11 LEU X 552 -10 .648 -18 .027 -3. .522 0. .00 0. .00 PROA

ATOM 164 HD12 LEU X 552 -8 .866 -17 .575 -3. .387 0. .00 0. .00 PROA

ATOM 165 HD13 LEU X 552 -9 .489 -19 .253 -3. .060 0. .00 0. .00 PROA

ATOM 166 CD2 LEU X 552 -10 .388 -19 .443 -5. .768 0. .00 0. .00 PROA

ATOM 167 HD21 LEU X 552 -10 .124 -20 .419 -5. .308 0. .00 0. .00 PROA

ATOM 168 HD22 LEU X 552 -10 .276 -19 .439 -6. .873 0. .00 0. .00 PROA

ATOM 169 HD23 LEU X 552 -11 .404 -19 .118 -5. .459 0. .00 0. .00 PROA

ATOM 170 C LEU X 552 -6 .881 -16 .727 -5. .920 0. .00 0. .00 PROA

ATOM 171 O LEU X 552 -6 .150 -17 .193 -5. .020 0. .00 0. .00 PROA

ATOM 172 N LEU X 553 -6 .456 -16 .684 -7. .204 0. .00 0. .00 PROA

ATOM 173 HN LEU X 553 -7 .006 -16 .238 -7. .905 0. .00 0. .00 PROA

ATOM 174 CA LEU X 553 -5 .038 -17 .066 -7. .512 0. .00 0. .00 PROA

ATOM 175 HA LEU X 553 -4 .906 -18 .091 -7. .197 0. .00 0. .00 PROA

ATOM 176 CB LEU X 553 -4 .798 -17 .285 -8. .988 0. .00 0. .00 PROA

ATOM 177 HB1 LEU X 553 -5 .172 -16 .463 -9. .635 0. .00 0. .00 PROA

ATOM 178 HB2 LEU X 553 -5 .313 -18 .212 -9. .318 0. .00 0. .00 PROA

ATOM 179 CG LEU X 553 -3 .314 -17 .483 -9. .462 0. .00 0. .00 PROA

ATOM 180 HG LEU X 553 -2 .748 -16 .583 -9. .139 0. .00 0. .00 PROA

ATOM 181 CD1 LEU X 553 -2 .575 -18 .701 -8. .852 0. .00 0. .00 PROA

ATOM 182 HD11 LEU X 553 -2 .309 -18 .655 -7. .775 0. .00 0. .00 PROA

ATOM 183 HD12 LEU X 553 -1 .731 -18 .937 -9. .535 0. .00 0. .00 PROA

ATOM 184 HD13 LEU X 553 -3 .254 -19 .579 -8. .810 0. .00 0. .00 PROA

ATOM 185 CD2 LEU X 553 -3 .347 -17 .515 -11. .018 0. .00 0. .00 PROA

ATOM 186 HD21 LEU X 553 -2 .385 -17 .196 -11. .474 0. .00 0. .00 PROA

ATOM 187 HD22 LEU X 553 -4 .126 -16 .838 -11. .428 0. .00 0. .00 PROA

ATOM 188 HD23 LEU X 553 -3 .640 -18 .526 -11. .372 0. .00 0. .00 PROA

ATOM 189 C LEU X 553 -3 .933 -16 .207 -6. .915 0. .00 0. .00 PROA

ATOM 190 O LEU X 553 -2 .989 -16 .688 -6. .348 0. .00 0. .00 PROA

ATOM 191 N MET X 554 -4 .027 -14 .866 -7. .021 0. .00 0. .00 PROA

ATOM 192 HN MET X 554 -4 .804 -14 .443 -7. .481 0. .00 0. .00 PROA

ATOM 193 CA MET X 554 -3 .041 -13 .828 -6. .650 0. .00 0. .00 PROA

ATOM 194 HA MET X 554 -2 .083 -14 .031 -7. .104 0. .00 0. .00 PROA

ATOM 195 CB MET X 554 -3 .605 -12 .395 -7. .132 0. .00 0. .00 PROA

ATOM 196 HB1 MET X 554 -2 .970 -11 .549 -6. .792 0. .00 0. .00 PROA

ATOM 197 HB2 MET X 554 -4 .603 -12 .210 -6. .681 0. .00 0. .00 PROA ATOM 198 CG MET X 554 -3.584 -12.244 -8..632 0..00 0..00 PROA

ATOM 199 HG1 MET X 554 -4 .029 -11 .253 -8. .866 0. .00 0. .00 PROA

ATOM 200 HG2 MET X 554 -4 .332 -12 .939 -9. .071 0. .00 0. .00 PROA

ATOM 201 C MET X 554 -2 .908 -13 .897 -5. .115 0. .00 0. .00 PROA

ATOM 202 O MET X 554 -1 .832 -13 .668 -4. .561 0. .00 0. .00 PROA

ATOM 203 N CYS X 555 -4 .020 -14 .143 -4. .362 0. .00 0. .00 PROA

ATOM 204 HN CYS X 555 -4 .894 -14 .273 -4. .823 0. .00 0. .00 PROA

ATOM 205 CA CYS X 555 -3 .899 -14 .454 -2. .931 0. .00 0. .00 PROA

ATOM 206 HA CYS X 555 -3 .442 -13 .588 -2. .476 0. .00 0. .00 PROA

ATOM 207 CB CYS X 555 -5 .299 -14 .517 -2. .377 0. .00 0. .00 PROA

ATOM 208 HB1 CYS X 555 -5 .918 -15 .370 -2. .729 0. .00 0. .00 PROA

ATOM 209 HB2 CYS X 555 -5 .902 -13 .619 -2. .631 0. .00 0. .00 PROA

ATOM 210 C CYS X 555 -3 .091 -15 .647 -2. .553 0. .00 0. .00 PROA

ATOM 211 O CYS X 555 -2 .360 -15 .628 -1. .600 0. .00 0. .00 PROA

ATOM 212 N THR X 556 -3 .168 -16 .744 -3. .343 0. .00 0. .00 PROA

ATOM 213 HN THR X 556 -3 .783 -16 .739 -4. .128 0. .00 0. .00 PROA

ATOM 214 CA THR X 556 -2 .321 -17 .982 -3. .135 0. .00 0. .00 PROA

ATOM 215 HA THR X 556 -2 .519 -18 .214 -2. .099 0. .00 0. .00 PROA

ATOM 216 CB THR X 556 -2 .582 -19 .091 -4. .171 0. .00 0. .00 PROA

ATOM 217 HB THR X 556 -2 .546 -18 .843 -5. .253 0. .00 0. .00 PROA

ATOM 218 OG1 THR X 556 -3 .835 -19 .745 -3. .910 0. .00 0. .00 PROA

ATOM 219 HG1 THR X 556 -4 .573 -19 .300 -4. .332 0. .00 0. .00 PROA

ATOM 220 CG2 THR X 556 -1 .565 -20 .195 -3. .929 0. .00 0. .00 PROA

ATOM 221 HG21 THR X 556 -1 .600 -20 .635 -2. .910 0. .00 0. .00 PROA

ATOM 222 HG22 THR X 556 -0 .533 -19 .866 -4. .180 0. .00 0. .00 PROA

ATOM 223 HG23 THR X 556 -1 .783 -21 .110 -4. .520 0. .00 0. .00 PROA

ATOM 224 C THR X 556 -0 .880 -17 .632 -3. .155 0. .00 0. .00 PROA

ATOM 225 O THR X 556 -0 .145 -17 .990 -2. .255 0. .00 0. .00 PROA

ATOM 226 N PHE X 557 -0 .455 -16 .737 -4. .161 0. .00 0. .00 PROA

ATOM 227 HN PHE X 557 -1 .215 -16 .503 -4. .763 0. .00 0. .00 PROA

ATOM 228 CA PHE X 557 0. .937 -16 .249 -4. .284 0. .00 0. .00 PROA

ATOM 229 HA PHE X 557 1. .428 -17 .210 -4. .340 0. .00 0. .00 PROA

ATOM 230 CB PHE X 557 1. .099 -15 .417 -5. .619 0. .00 0. .00 PROA

ATOM 231 HB1 PHE X 557 2 .101 -14 .951 -5. .735 0. .00 0. .00 PROA

ATOM 232 HB2 PHE X 557 0 .370 -14 .580 -5. .660 0. .00 0. .00 PROA

ATOM 233 CG PHE X 557 0. .752 -16 .160 -6. .860 0. .00 0. .00 PROA

ATOM 234 CD1 PHE X 557 0 .570 -15 .316 -7. .947 0. .00 0. .00 PROA

ATOM 235 HD1 PHE X 557 0 .372 -14 .255 -7. .944 0. .00 0. .00 PROA

ATOM 236 CE1 PHE X 557 0 .609 -15 .875 -9. .253 0. .00 0. .00 PROA

ATOM 237 HE1 PHE X 557 0 .438 -15 .155 -10. .039 0. .00 0. .00 PROA

ATOM 238 CZ PHE X 557 0. .768 -17 .290 -9. .477 0. .00 0. .00 PROA

ATOM 239 HZ PHE X 557 0. .927 -17 .590 -10. .502 0. .00 0. .00 PROA

ATOM 240 CD2 PHE X 557 0 .697 -17 .563 -7. .025 0. .00 0. .00 PROA

ATOM 241 HD2 PHE X 557 0 .914 -18 .169 -6. .157 0. .00 0. .00 PROA

ATOM 242 CE2 PHE X 557 0 .754 -18 .117 -8. .340 0. .00 0. .00 PROA

ATOM 243 HE2 PHE X 557 0 .813 -19 .164 -8. .596 0. .00 0. .00 PROA

ATOM 244 C PHE X 557 1. .458 -15 .455 -3. .097 0. .00 0. .00 PROA

ATOM 245 O PHE X 557 2. .550 -15 .493 -2. .630 0. .00 0. .00 PROA

ATOM 246 N ALA X 558 0. .503 -14 .559 -2. .598 0. .00 0. .00 PROA

ATOM 247 HN ALA X 558 -0 .471 -14 .690 -2. .767 0. .00 0. .00 PROA

ATOM 248 CA ALA X 558 0. .891 -13 .731 -1. .535 0. .00 0. .00 PROA

ATOM 249 HA ALA X 558 1. .844 -13 .267 -1. .742 0. .00 0. .00 PROA

ATOM 250 CB ALA X 558 -0 .298 -12 .729 -1. .494 0. .00 0. .00 PROA

ATOM 251 HB1 ALA X 558 -1 .209 -13 .167 -1. .031 0. .00 0. .00 PROA

ATOM 252 HB2 ALA X 558 -0 .534 -12 .429 -2. .537 0. .00 0. .00 PROA

ATOM 253 HB3 ALA X 558 -0 .144 -11 .810 -0. .889 0. .00 0. .00 PROA

ATOM 254 C ALA X 558 1. .028 -14 .417 -0. .137 0. .00 0. .00 PROA

ATOM 255 O ALA X 558 1. .960 -14 .133 0. .609 0. .00 0. .00 PROA

ATOM 256 N LEU X 559 0. .216 -15 .437 0. .078 0. .00 0. .00 PROA

ATOM 257 HN LEU X 559 -0 .463 -15 .652 -0. .620 0. .00 0. .00 PROA

ATOM 258 CA LEU X 559 0. .419 -16 .423 1. .217 0. .00 0. .00 PROA

ATOM 259 HA LEU X 559 0. .572 -15 .761 2. .056 0. .00 0. .00 PROA

ATOM 260 CB LEU X 559 -0 .769 -17 .358 1. .470 0. .00 0. .00 PROA

ATOM 261 HB1 LEU X 559 -0 .647 -17 .918 2. .421 0. .00 0. .00 PROA

ATOM 262 HB2 LEU X 559 -0 .845 -18 .088 0. .635 0. .00 0. .00 PROA

ATOM 263 CG LEU X 559 -2 .072 -16 .552 1. .723 0. .00 0. .00 PROA ATOM 264 HG LEU X 559 -2.145 -15.768 0..939 0..00 0..00 PROA

ATOM 265 CD1 LEU X 559 -3 .337 -17 .428 1. .679 0. .00 0. .00 PROA

ATOM 266 HD11 LEU X 559 -3 .316 -18 .035 0. .749 0. .00 0. .00 PROA

ATOM 267 HD12 LEU X 559 -4 .257 -16 .809 1. .757 0. .00 0. .00 PROA

ATOM 268 HD13 LEU X 559 -3 .304 -18 .175 2. .501 0. .00 0. .00 PROA

ATOM 269 CD2 LEU X 559 -2 .020 -15 .854 3. .101 0. .00 0. .00 PROA

ATOM 270 HD21 LEU X 559 -2 .155 -16 .693 3. .816 0. .00 0. .00 PROA

ATOM 271 HD22 LEU X 559 -2 .989 -15 .311 3. .133 0. .00 0. .00 PROA

ATOM 272 HD23 LEU X 559 -1 .076 -15 .308 3. .315 0. .00 0. .00 PROA

ATOM 273 C LEU X 559 1. .677 -17 .204 1. .139 0. .00 0. .00 PROA

ATOM 274 O LEU X 559 2. .369 -17 .394 2. .136 0. .00 0. .00 PROA

ATOM 275 N ILE X 560 2. .099 -17 .731 -0. .059 0. .00 0. .00 PROA

ATOM 276 HN ILE X 560 1. .611 -17 .600 -0. .919 0. .00 0. .00 PROA

ATOM 277 CA ILE X 560 3. .378 -18 .385 -0. .207 0. .00 0. .00 PROA

ATOM 278 HA ILE X 560 3. .408 -19 .124 0. .580 0. .00 0. .00 PROA

ATOM 279 CB ILE X 560 3. .530 -19 .119 -1. .545 0. .00 0. .00 PROA

ATOM 280 HB ILE X 560 3. .476 -18 .377 -2. .370 0. .00 0. .00 PROA

ATOM 281 CG2 ILE X 560 5 .006 -19 .665 -1. .736 0. .00 0. .00 PROA

ATOM 282 HG21 ILE X 560 5 .772 -18 .944 -2. .094 0. .00 0. .00 PROA

ATOM 283 HG22 ILE X 560 4 .995 -20 .665 -2. .220 0. .00 0. .00 PROA

ATOM 284 HG23 ILE X 560 5 .269 -19 .954 -0. .696 0. .00 0. .00 PROA

ATOM 285 CGI ILE X 560 2 .375 -20 .233 -1. .669 0. .00 0. .00 PROA

ATOM 286 HG11 ILE X 560 1 .394 -19 .942 -1. .235 0. .00 0. .00 PROA

ATOM 287 HG12 ILE X 560 2 .680 -21 .122 -1. .077 0. .00 0. .00 PROA

ATOM 288 CD ILE X 560 2. .099 -20 .558 -3. .098 0. .00 0. .00 PROA

ATOM 289 HD1 ILE X 560 1 .272 -21 .300 -3. .090 0. .00 0. .00 PROA

ATOM 290 HD2 ILE X 560 2 .983 -20 .993 -3. .611 0. .00 0. .00 PROA

ATOM 291 HD3 ILE X 560 1 .694 -19 .757 -3. .753 0. .00 0. .00 PROA

ATOM 292 C ILE X 560 4. .503 -17 .427 0. .166 0. .00 0. .00 PROA

ATOM 293 O ILE X 560 5. .482 -17 .845 0. .799 0. .00 0. .00 PROA

ATOM 294 N ALA X 561 4. .492 -16 .189 -0. .255 0. .00 0. .00 PROA

ATOM 295 HN ALA X 561 3. .895 -15 .989 -1. .028 0. .00 0. .00 PROA

ATOM 296 CA ALA X 561 5. .465 -15 .170 0. .099 0. .00 0. .00 PROA

ATOM 297 HA ALA X 561 6. .447 -15 .572 -0. .103 0. .00 0. .00 PROA

ATOM 298 CB ALA X 561 5. .202 -13 .983 -0. .807 0. .00 0. .00 PROA

ATOM 299 HB1 ALA X 561 4 .194 -13 .562 -0. .604 0. .00 0. .00 PROA

ATOM 300 HB2 ALA X 561 5 .093 -14 .413 -1. .825 0. .00 0. .00 PROA

ATOM 301 HB3 ALA X 561 6 .024 -13 .236 -0. .839 0. .00 0. .00 PROA

ATOM 302 C ALA X 561 5. .406 -14 .810 1. .564 0. .00 0. .00 PROA

ATOM 303 O ALA X 561 6. .460 -14 .669 2. .231 0. .00 0. .00 PROA

ATOM 304 N HSD X 562 4. .167 -14 .582 2. .112 0. .00 0. .00 PROA

ATOM 305 HN HSD X 562 3. .338 -14 .560 1. .559 0. .00 0. .00 PROA

ATOM 306 CA HSD X 562 4. .006 -14 .351 3. .532 0. .00 0. .00 PROA

ATOM 307 HA HSD X 562 4. .634 -13 .510 3. .785 0. .00 0. .00 PROA

ATOM 308 CB HSD X 562 2. .597 -13 .914 3. .881 0. .00 0. .00 PROA

ATOM 309 HB1 HSD X 562 2 .406 -14 .000 4. .972 0. .00 0. .00 PROA

ATOM 310 HB2 HSD X 562 1 .865 -14 .653 3. .489 0. .00 0. .00 PROA

ATOM 311 ND1 HSD X 562 2 .435 -11 .920 2. .294 0. .00 0. .00 PROA

ATOM 312 HD1 HSD X 562 3 .255 -11 .979 1. .725 0. .00 0. .00 PROA

ATOM 313 CG HSD X 562 1. .995 -12 .674 3. .338 0. .00 0. .00 PROA

ATOM 314 CE1 HSD X 562 1 .628 -10 .891 2. .100 0. .00 0. .00 PROA

ATOM 315 HE1 HSD X 562 1 .616 -10 .049 1. .407 0. .00 0. .00 PROA

ATOM 316 NE2 HSD X 562 0 .657 -10 .831 2. .980 0. .00 0. .00 PROA

ATOM 317 CD2 HSD X 562 0 .860 -11 .993 3. .762 0. .00 0. .00 PROA

ATOM 318 HD2 HSD X 562 0 .346 -12 .377 4. .635 0. .00 0. .00 PROA

ATOM 319 C HSD X 562 4. .568 -15 .461 4. .411 0. .00 0. .00 PROA

ATOM 320 O HSD X 562 5. .190 -15 .222 5. .389 0. .00 0. .00 PROA

ATOM 321 N TRP X 563 4. .344 -16 .769 4. .153 0. .00 0. .00 PROA

ATOM 322 HN TRP X 563 3. .785 -16 .916 3. .340 0. .00 0. .00 PROA

ATOM 323 CA TRP X 563 4. .844 -17 .914 4. .806 0. .00 0. .00 PROA

ATOM 324 HA TRP X 563 4. .739 -17 .748 5. .868 0. .00 0. .00 PROA

ATOM 325 CB TRP X 563 4. .015 -19 .162 4. .213 0. .00 0. .00 PROA

ATOM 326 HB1 TRP X 563 4 .149 -19 .203 3. . Ill 0. .00 0. .00 PROA

ATOM 327 HB2 TRP X 563 2 .928 -18 .994 4. .367 0. .00 0. .00 PROA

ATOM 328 CG TRP X 563 4. .402 -20 .532 4. .745 0. .00 0. .00 PROA

ATOM 329 CD1 TRP X 563 5 .217 -21 .443 4. .068 0. .00 0. .00 PROA ATOM 330 HD1 TRP X 563 5.845 -21.264 3..208 0..00 0..00 PROA

ATOM 331 NE1 TRP X 563 5 .545 -22 .406 5. .032 0. .00 0. .00 PROA

ATOM 332 HE1 TRP X 563 6 .275 -23 .046 5. .129 0. .00 0. .00 PROA

ATOM 333 CE2 TRP X 563 4 .843 -22 .279 6. .121 0. .00 0. .00 PROA

ATOM 334 CD2 TRP X 563 3 .998 -21 .145 6. .010 0. .00 0. .00 PROA

ATOM 335 CE3 TRP X 563 3 .198 -20 .734 7. .136 0. .00 0. .00 PROA

ATOM 336 HE3 TRP X 563 2 .608 -19 .830 7. .110 0. .00 0. .00 PROA

ATOM 337 CZ3 TRP X 563 3 .163 -21 .600 8. .211 0. .00 0. .00 PROA

ATOM 338 HZ3 TRP X 563 2 .374 -21 .496 8. .941 0. .00 0. .00 PROA

ATOM 339 CZ2 TRP X 563 4 .785 -23 .156 7. .264 0. .00 0. .00 PROA

ATOM 340 HZ2 TRP X 563 5 .313 -24 .097 7. .207 0. .00 0. .00 PROA

ATOM 341 CH2 TRP X 563 3 .840 -22 .799 8. .276 0. .00 0. .00 PROA

ATOM 342 HH2 TRP X 563 3 .687 -23 .401 9. .159 0. .00 0. .00 PROA

ATOM 343 C TRP X 563 6. .361 -18 .083 4. .641 0. .00 0. .00 PROA

ATOM 344 O TRP X 563 7. .107 -18 .427 5. .542 0. .00 0. .00 PROA

ATOM 345 N LEU X 564 6. .950 -17 .790 3. .404 0. .00 0. .00 PROA

ATOM 346 HN LEU X 564 6. .395 -17 .592 2. .600 0. .00 0. .00 PROA

ATOM 347 CA LEU X 564 8. .371 -17 .767 3. .157 0. .00 0. .00 PROA

ATOM 348 HA LEU X 564 8. .737 -18 .736 3. .463 0. .00 0. .00 PROA

ATOM 349 CB LEU X 564 8. .681 -17 .380 1. .625 0. .00 0. .00 PROA

ATOM 350 HB1 LEU X 564 8 .347 -16 .340 1. .422 0. .00 0. .00 PROA

ATOM 351 HB2 LEU X 564 7 .926 -17 .888 0. .988 0. .00 0. .00 PROA

ATOM 352 CG LEU X 564 10 .057 -17 .697 1. .048 0. .00 0. .00 PROA

ATOM 353 HG LEU X 564 10 .753 -17 .099 1. .675 0. .00 0. .00 PROA

ATOM 354 CD1 LEU X 564 10 .482 -19 .213 1. .200 0. .00 0. .00 PROA

ATOM 355 HD11 LEU X 564 9 .515 -19 .757 1. .142 0. .00 0. .00 PROA

ATOM 356 HD12 LEU X 564 11 .101 -19 .349 2. .112 0. .00 0. .00 PROA

ATOM 357 HD13 LEU X 564 11 .084 -19 .545 0. .328 0. .00 0. .00 PROA

ATOM 358 CD2 LEU X 564 9 .988 -17 .150 -0. .311 0. .00 0. .00 PROA

ATOM 359 HD21 LEU X 564 9 .181 -17 .520 -0. .978 0. .00 0. .00 PROA

ATOM 360 HD22 LEU X 564 10 .924 -17 .499 -0. .798 0. .00 0. .00 PROA

ATOM 361 HD23 LEU X 564 9 .829 -16 .052 -0. .252 0. .00 0. .00 PROA

ATOM 362 C LEU X 564 9. .071 -16 .769 4. .062 0. .00 0. .00 PROA

ATOM 363 O LEU X 564 10 .155 -16 .944 4. .633 0. .00 0. .00 PROA

ATOM 364 N ALA X 565 8. .418 -15 .570 4. .190 0. .00 0. .00 PROA

ATOM 365 HN ALA X 565 7. .553 -15 .430 3. .715 0. .00 0. .00 PROA

ATOM 366 CA ALA X 565 8. .796 -14 .608 5. .163 0. .00 0. .00 PROA

ATOM 367 HA ALA X 565 9. .762 -14 .169 4. .963 0. .00 0. .00 PROA

ATOM 368 CB ALA X 565 8. .003 -13 .276 5. .043 0. .00 0. .00 PROA

ATOM 369 HB1 ALA X 565 6 .936 -13 .492 5. .266 0. .00 0. .00 PROA

ATOM 370 HB2 ALA X 565 8 .088 -12 .848 4. .021 0. .00 0. .00 PROA

ATOM 371 HB3 ALA X 565 8 .389 -12 .523 5. .762 0. .00 0. .00 PROA

ATOM 372 C ALA X 565 8. .861 -15 .130 6. .575 0. .00 0. .00 PROA

ATOM 373 O ALA X 565 9. .874 -14 .884 7. .243 0. .00 0. .00 PROA

ATOM 374 N CYS X 566 7. .776 -15 .839 7. .006 0. .00 0. .00 PROA

ATOM 375 HN CYS X 566 6. .923 -15 .938 6. .498 0. .00 0. .00 PROA

ATOM 376 CA CYS X 566 7. .693 -16 .516 8. .269 0. .00 0. .00 PROA

ATOM 377 HA CYS X 566 8. .006 -15 .805 9. .019 0. .00 0. .00 PROA

ATOM 378 CB CYS X 566 6. .273 -17 .128 8. .511 0. .00 0. .00 PROA

ATOM 379 HB1 CYS X 566 6 .143 -17 .664 9. .475 0. .00 0. .00 PROA

ATOM 380 HB2 CYS X 566 6 .116 -17 .902 7. .729 0. .00 0. .00 PROA

ATOM 381 C CYS X 566 8. .780 -17 .553 8. .560 0. .00 0. .00 PROA

ATOM 382 O CYS X 566 9. .371 -17 .581 9. .587 0. .00 0. .00 PROA

ATOM 383 N ILE X 567 8. .989 -18 .493 7. .619 0. .00 0. .00 PROA

ATOM 384 HN ILE X 567 8. .519 -18 .539 6. .741 0. .00 0. .00 PROA

ATOM 385 CA ILE X 567 10 .127 -19 .395 7. .638 0. .00 0. .00 PROA

ATOM 386 HA ILE X 567 10 .076 -19 .921 8. .580 0. .00 0. .00 PROA

ATOM 387 CB ILE X 567 10 .204 -20 .269 6. .410 0. .00 0. .00 PROA

ATOM 388 HB ILE X 567 10 .110 -19 .799 5. .408 0. .00 0. .00 PROA

ATOM 389 CG2 ILE X 567 11 .453 -21 .236 6. .335 0. .00 0. .00 PROA

ATOM 390 HG21 ILE X 567 11 .476 -21 .926 7. .206 0. .00 0. .00 PROA

ATOM 391 HG22 ILE X 567 12 .360 -20 .595 6. .316 0. .00 0. .00 PROA

ATOM 392 HG23 ILE X 567 11 .377 -21 .808 5. .385 0. .00 0. .00 PROA

ATOM 393 CGI ILE X 567 8 .930 -21 .175 6. .452 0. .00 0. .00 PROA

ATOM 394 HG11 ILE X 567 8 .794 -21 .635 5. .450 0. .00 0. .00 PROA

ATOM 395 HG12 ILE X 567 8 .061 -20 .491 6. .564 0. .00 0. .00 PROA ATOM 396 CD ILE X 567 8..936 -22.230 7..545 0..00 0..00 PROA

ATOM 397 HD1 ILE X 567 9 .280 -21 .778 8. .500 0. .00 0. .00 PROA

ATOM 398 HD2 ILE X 567 9 .477 -23 .178 7. .337 0. .00 0. .00 PROA

ATOM 399 HD3 ILE X 567 7 .889 -22 .591 7. .633 0. .00 0. .00 PROA

ATOM 400 C ILE X 567 11 .513 -18 .639 7. .661 0. .00 0. .00 PROA

ATOM 401 O ILE X 567 12 .312 -19 .065 8. .509 0. .00 0. .00 PROA

ATOM 402 N TRP X 568 11 .823 -17 .679 6. .749 0. .00 0. .00 PROA

ATOM 403 HN TRP X 568 11 .133 -17 .351 6. .107 0. .00 0. .00 PROA

ATOM 404 CA TRP X 568 13 .101 -16 .902 6. .702 0. .00 0. .00 PROA

ATOM 405 HA TRP X 568 13 .850 -17 .679 6. .670 0. .00 0. .00 PROA

ATOM 406 CB TRP X 568 13 .158 -16 .043 5. .409 0. .00 0. .00 PROA

ATOM 407 HB1 TRP X 568 12 .341 -15 .294 5. .331 0. .00 0. .00 PROA

ATOM 408 HB2 TRP X 568 13 .074 -16 .745 4. .552 0. .00 0. .00 PROA

ATOM 409 CG TRP X 568 14 .475 -15 .333 5. .217 0. .00 0. .00 PROA

ATOM 410 CD1 TRP X 568 14 .625 -14 .073 4. .830 0. .00 0. .00 PROA

ATOM 411 HD1 TRP X 568 13 .846 -13 .503 4. .344 0. .00 0. .00 PROA

ATOM 412 NE1 TRP X 568 15 .863 -13 .614 4. .970 0. .00 0. .00 PROA

ATOM 413 HE1 TRP X 568 16 .213 -12 .719 4. .798 0. .00 0. .00 PROA

ATOM 414 CE2 TRP X 568 16 .620 -14 .615 5. .400 0. .00 0. .00 PROA

ATOM 415 CD2 TRP X 568 15 .794 -15 .807 5. .499 0. .00 0. .00 PROA

ATOM 416 CE3 TRP X 568 16 .335 -16 .979 5. .982 0. .00 0. .00 PROA

ATOM 417 HE3 TRP X 568 15 .711 -17 .823 6. .239 0. .00 0. .00 PROA

ATOM 418 CZ3 TRP X 568 17 .719 -17 .048 6. .179 0. .00 0. .00 PROA

ATOM 419 HZ3 TRP X 568 18 .174 -17 .996 6. .425 0. .00 0. .00 PROA

ATOM 420 CZ2 TRP X 568 17 .947 -14 .650 5. .693 0. .00 0. .00 PROA

ATOM 421 HZ2 TRP X 568 18 .677 -13 .854 5. .651 0. .00 0. .00 PROA

ATOM 422 CH2 TRP X 568 18 .490 -15 .900 6. .065 0. .00 0. .00 PROA

ATOM 423 HH2 TRP X 568 19 .563 -15 .887 6. .191 0. .00 0. .00 PROA

ATOM 424 C TRP X 568 13 .415 -16 .174 7. .952 0. .00 0. .00 PROA

ATOM 425 O TRP X 568 14 .479 -16 .333 8. .470 0. .00 0. .00 PROA

ATOM 426 N TYR X 569 12 .452 -15 .438 8. .575 0. .00 0. .00 PROA

ATOM 427 HN TYR X 569 11 .538 -15 .405 8. .178 0. .00 0. .00 PROA

ATOM 428 CA TYR X 569 12 .620 -14 .681 9. .806 0. .00 0. .00 PROA

ATOM 429 HA TYR X 569 13 .511 -14 .072 9. .777 0. .00 0. .00 PROA

ATOM 430 CB TYR X 569 11 .330 -13 .865 10. .083 0. .00 0. .00 PROA

ATOM 431 HB1 TYR X 569 10 .533 -14 .635 10. .162 0. .00 0. .00 PROA

ATOM 432 HB2 TYR X 569 10 .931 -13 .214 9. .275 0. .00 0. .00 PROA

ATOM 433 CG TYR X 569 11 .341 -12 .907 11. .361 0. .00 0. .00 PROA

ATOM 434 CD1 TYR X 569 10 .193 -12 .826 12. .155 0. .00 0. .00 PROA

ATOM 435 HD1 TYR X 569 9 .298 -13 .373 11. .898 0. .00 0. .00 PROA

ATOM 436 CE1 TYR X 569 10 .240 -11 .990 13. .265 0. .00 0. .00 PROA

ATOM 437 HE1 TYR X 569 9 .385 -11 .984 13. .924 0. .00 0. .00 PROA

ATOM 438 CZ TYR X 569 11 .399 -11 .242 13. .627 0. .00 0. .00 PROA

ATOM 439 OH TYR X 569 11 .399 -10 .704 14. .892 0. .00 0. .00 PROA

ATOM 440 HH TYR X 569 12 .107 -11 .042 15. .444 0. .00 0. .00 PROA

ATOM 441 CD2 TYR X 569 12 .495 -12 .199 11. .752 0. .00 0. .00 PROA

ATOM 442 HD2 TYR X 569 13 .431 -12 .268 11. .219 0. .00 0. .00 PROA

ATOM 443 CE2 TYR X 569 12 .529 -11 .365 12. .884 0. .00 0. .00 PROA

ATOM 444 HE2 TYR X 569 13 .452 -10 .908 13. .208 0. .00 0. .00 PROA

ATOM 445 C TYR X 569 12 .939 -15 .596 10. .908 0. .00 0. .00 PROA

ATOM 446 O TYR X 569 13 .821 -15 .355 11. .676 0. .00 0. .00 PROA

ATOM 447 N ALA X 570 12 .189 -16 .723 10. .999 0. .00 0. .00 PROA

ATOM 448 HN ALA X 570 11 .515 -16 .814 10. .270 0. .00 0. .00 PROA

ATOM 449 CA ALA X 570 12 .377 -17 .756 11. .955 0. .00 0. .00 PROA

ATOM 450 HA ALA X 570 12 .302 -17 .387 12. .967 0. .00 0. .00 PROA

ATOM 451 CB ALA X 570 11 .211 -18 .726 11. .831 0. .00 0. .00 PROA

ATOM 452 HB1 ALA X 570 11 .150 -19 .461 12. .662 0. .00 0. .00 PROA

ATOM 453 HB2 ALA X 570 11 .184 -19 .170 10. .813 0. .00 0. .00 PROA

ATOM 454 HB3 ALA X 570 10 .248 -18 .185 11. .950 0. .00 0. .00 PROA

ATOM 455 C ALA X 570 13 .764 -18 .460 12. .000 0. .00 0. .00 PROA

ATOM 456 O ALA X 570 14 .357 -18 .694 13. .055 0. .00 0. .00 PROA

ATOM 457 N ILE X 571 14 .271 -18 .865 10. .808 0. .00 0. .00 PROA

ATOM 458 HN ILE X 571 13 .709 -18 .820 9. .986 0. .00 0. .00 PROA

ATOM 459 CA ILE X 571 15 .469 -19 .622 10. .820 0. .00 0. .00 PROA

ATOM 460 HA ILE X 571 15 .711 -20 .102 11. .756 0. .00 0. .00 PROA

ATOM 461 CB ILE X 571 15 .282 -20 .798 9. .796 0. .00 0. .00 PROA ATOM 462 HB ILE X 571 16.146 -21.486 9..924 0..00 0..00 PROA

ATOM 463 CG2 ILE X 571 14 .058 -21 .638 10. .244 0. .00 0. .00 PROA

ATOM 464 HG21 ILE X 571 14 .075 -22 .071 11. .267 0. .00 0. .00 PROA

ATOM 465 HG22 ILE X 571 14 .088 -22 .579 9. .654 0. .00 0. .00 PROA

ATOM 466 HG23 ILE X 571 13 .094 -21 .145 9. .995 0. .00 0. .00 PROA

ATOM 467 CGI ILE X 571 15 .271 -20 .509 8. .319 0. .00 0. .00 PROA

ATOM 468 HG11 ILE X 571 14 .724 -19 .578 8. .059 0. .00 0. .00 PROA

ATOM 469 HG12 ILE X 571 14 .705 -21 .308 7. .794 0. .00 0. .00 PROA

ATOM 470 CD ILE X 571 16 .635 -20 .542 7. .677 0. .00 0. .00 PROA

ATOM 471 HD1 ILE X 571 17 .136 -21 .514 7. .485 0. .00 0. .00 PROA

ATOM 472 HD2 ILE X 571 17 .362 -19 .992 8. .311 0. .00 0. .00 PROA

ATOM 473 HD3 ILE X 571 16 .471 -20 .098 6. .672 0. .00 0. .00 PROA

ATOM 474 C ILE X 571 16 .712 -18 .797 10. .619 0. .00 0. .00 PROA

ATOM 475 O ILE X 571 17 .803 -19 .403 10. .720 0. .00 0. .00 PROA

ATOM 476 N GLY X 572 16 .627 -17 .499 10. .289 0. .00 0. .00 PROA

ATOM 477 HN GLY X 572 15 .760 -17 .007 10. .247 0. .00 0. .00 PROA

ATOM 478 CA GLY X 572 17 .779 -16 .666 9. .920 0. .00 0. .00 PROA

ATOM 479 HA1 GLY X 572 17 .343 -15 .719 9. .639 0. .00 0. .00 PROA

ATOM 480 HA2 GLY X 572 18 .356 -17 .175 9. .162 0. .00 0. .00 PROA

ATOM 481 C GLY X 572 18 .834 -16 .398 10. .927 0. .00 0. .00 PROA

ATOM 482 O GLY X 572 19 .986 -16 .127 10. .664 0. .00 0. .00 PROA

ATOM 483 N ASN X 573 18 .331 -16 .319 12. .149 0. .00 0. .00 PROA

ATOM 484 HN ASN X 573 17 .369 -16 .527 12. .306 0. .00 0. .00 PROA

ATOM 485 CA ASN X 573 19 .038 -15 .807 13. .343 0. .00 0. .00 PROA

ATOM 486 HA ASN X 573 20 .107 -15 .891 13. .218 0. .00 0. .00 PROA

ATOM 487 CB ASN X 573 18 .595 -14 .310 13. .382 0. .00 0. .00 PROA

ATOM 488 HB1 ASN X 573 17 .539 -14 .205 13. .711 0. .00 0. .00 PROA

ATOM 489 HB2 ASN X 573 18 .674 -13 .866 12. .367 0. .00 0. .00 PROA

ATOM 490 CG ASN X 573 19 .618 -13 .430 14. .194 0. .00 0. .00 PROA

ATOM 491 OD1 ASN X 573 20 .780 -13 .817 14. .350 0. .00 0. .00 PROA

ATOM 492 ND2 ASN X 573 19 .079 -12 .323 14. .745 0. .00 0. .00 PROA

ATOM 493 HD21 ASN X 573 19 .732 -11 .754 15. .245 0. .00 0. .00 PROA

ATOM 494 HD22 ASN X 573 18 .150 -12 .044 14. .501 0. .00 0. .00 PROA

ATOM 495 C ASN X 573 18 .699 -16 .554 14. .672 0. .00 0. .00 PROA

ATOM 496 O ASN X 573 18 .346 -15 .906 15. .639 0. .00 0. .00 PROA

ATOM 497 N MET X 574 18 .757 -17 .934 14. .732 0. .00 0. .00 PROA

ATOM 498 HN MET X 574 19 .068 -18 .445 13. .934 0. .00 0. .00 PROA

ATOM 499 CA MET X 574 18 .405 -18 .732 15. .944 0. .00 0. .00 PROA

ATOM 500 HA MET X 574 17 .367 -18 .466 16. .074 0. .00 0. .00 PROA

ATOM 501 CB MET X 574 18 .580 -20 .284 15. .643 0. .00 0. .00 PROA

ATOM 502 HB1 MET X 574 18 .504 -20 .772 16. .638 0. .00 0. .00 PROA

ATOM 503 HB2 MET X 574 19 .580 -20 .383 15. .169 0. .00 0. .00 PROA

ATOM 504 CG MET X 574 17 .419 -20 .785 14. .665 0. .00 0. .00 PROA

ATOM 505 HG1 MET X 574 17 .513 -20 .101 13. .794 0. .00 0. .00 PROA

ATOM 506 HG2 MET X 574 16 .453 -20 .724 15. .212 0. .00 0. .00 PROA

ATOM 507 C MET X 574 19 .227 -18 .257 17. .187 0. .00 0. .00 PROA

ATOM 508 O MET X 574 20 .389 -17 .954 17. .065 0. .00 0. .00 PROA

ATOM 509 N GLU X 575 18 .652 -18 .280 18. .481 0. .00 0. .00 PROA

ATOM 510 HN GLU X 575 17 .667 -18 .433 18. .447 0. .00 0. .00 PROA

ATOM 511 CA GLU X 575 19 .151 -17 .872 19. .796 0. .00 0. .00 PROA

ATOM 512 HA GLU X 575 20 .188 -17 .639 19. .603 0. .00 0. .00 PROA

ATOM 513 CB GLU X 575 18 .596 -16 .545 20. .385 0. .00 0. .00 PROA

ATOM 514 HB1 GLU X 575 19 .024 -16 .475 21. .408 0. .00 0. .00 PROA

ATOM 515 HB2 GLU X 575 17 .485 -16 .576 20. .370 0. .00 0. .00 PROA

ATOM 516 CG GLU X 575 19 .148 -15 .350 19. .660 0. .00 0. .00 PROA

ATOM 517 HG1 GLU X 575 18 .712 -15 .237 18. .644 0. .00 0. .00 PROA

ATOM 518 HG2 GLU X 575 20 .259 -15 .377 19. .636 0. .00 0. .00 PROA

ATOM 519 CD GLU X 575 18 .949 -14 .002 20. .415 0. .00 0. .00 PROA

ATOM 520 OE1 GLU X 575 19 .559 -13 .863 21. .481 0. .00 0. .00 PROA

ATOM 521 OE2 GLU X 575 18 .127 -13 .175 20. .016 0. .00 0. .00 PROA

ATOM 522 C GLU X 575 18 .988 -19 .079 20. .733 0. .00 0. .00 PROA

ATOM 523 O GLU X 575 18 .101 -19 .918 20. .543 0. .00 0. .00 PROA

ATOM 524 N GLN X 576 19 .745 -19 .070 21. .865 0. .00 0. .00 PROA

ATOM 525 HN GLN X 576 20 .542 -18 .489 22. .012 0. .00 0. .00 PROA

ATOM 526 CA GLN X 576 19 .697 -20 .207 22. .696 0. .00 0. .00 PROA

ATOM 527 HA GLN X 576 20 .314 -20 .915 22. .163 0. .00 0. .00 PROA ATOM 528 CB GLN X 576 20.532 -19.919 24..037 0..00 0..00 PROA

ATOM 529 HB1 GLN X 576 21 .608 -19 .752 23. .821 0. .00 0. .00 PROA

ATOM 530 HB2 GLN X 576 20 .549 -20 .787 24. .731 0. .00 0. .00 PROA

ATOM 531 CG GLN X 576 20 .087 -18 .618 24. .846 0. .00 0. .00 PROA

ATOM 532 HG1 GLN X 576 19 .052 -18 .675 25. .245 0. .00 0. .00 PROA

ATOM 533 HG2 GLN X 576 20 .107 -17 .816 24. .078 0. .00 0. .00 PROA

ATOM 534 CD GLN X 576 21 .022 -18 .189 25. .955 0. .00 0. .00 PROA

ATOM 535 OE1 GLN X 576 21 .685 -17 .125 25. .929 0. .00 0. .00 PROA

ATOM 536 NE2 GLN X 576 21 .114 -19 .069 26. .892 0. .00 0. .00 PROA

ATOM 537 HE21 GLN X 576 20 .630 -19 .941 26. .820 0. .00 0. .00 PROA

ATOM 538 HE22 GLN X 576 21 .586 -18 .777 27. .724 0. .00 0. .00 PROA

ATOM 539 C GLN X 576 18 .360 -20 .702 23. .242 0. .00 0. .00 PROA

ATOM 540 O GLN X 576 17 .522 -19 .881 23. .624 0. .00 0. .00 PROA

ATOM 541 N PRO X 577 18 .065 -21 .981 23. .295 0. .00 0. .00 PROA

ATOM 542 CD PRO X 577 18 .748 -23 .013 22. .527 0. .00 0. .00 PROA

ATOM 543 HD1 PRO X 577 19 .822 -23 .066 22. .808 0. .00 0. .00 PROA

ATOM 544 HD2 PRO X 577 18 .575 -22 .770 21. .457 0. .00 0. .00 PROA

ATOM 545 CA PRO X 577 16 .667 -22 .402 23. .575 0. .00 0. .00 PROA

ATOM 546 HA PRO X 577 15 .830 -21 .793 23. .266 0. .00 0. .00 PROA

ATOM 547 CB PRO X 577 16 .547 -23 .792 22. .922 0. .00 0. .00 PROA

ATOM 548 HB1 PRO X 577 16 .161 -23 .744 21. .881 0. .00 0. .00 PROA

ATOM 549 HB2 PRO X 577 16 .059 -24 .581 23. .532 0. .00 0. .00 PROA

ATOM 550 CG PRO X 577 18 .005 -24 .268 22. .741 0. .00 0. .00 PROA

ATOM 551 HG1 PRO X 577 18 .442 -24 .687 23. .673 0. .00 0. .00 PROA

ATOM 552 HG2 PRO X 577 18 .116 -24 .867 21. .812 0. .00 0. .00 PROA

ATOM 553 C PRO X 577 16 .534 -22 .548 25. .037 0. .00 0. .00 PROA

ATOM 554 O PRO X 577 15 .443 -22 .540 25. .562 0. .00 0. .00 PROA

ATOM 555 N HSD X 578 17 .643 -22 .706 25. .717 0. .00 0. .00 PROA

ATOM 556 HN HSD X 578 18 .472 -22 .752 25. .164 0. .00 0. .00 PROA

ATOM 557 CA HSD X 578 17 .779 -23 .065 27. .113 0. .00 0. .00 PROA

ATOM 558 HA HSD X 578 16 .844 -23 .073 27. .654 0. .00 0. .00 PROA

ATOM 559 CB HSD X 578 18 .481 -24 .446 27. .475 0. .00 0. .00 PROA

ATOM 560 HB1 HSD X 578 18 .619 -24 .345 28. .573 0. .00 0. .00 PROA

ATOM 561 HB2 HSD X 578 19 .397 -24 .633 26. .874 0. .00 0. .00 PROA

ATOM 562 ND1 HSD X 578 16 .455 -25 .841 27. .878 0. .00 0. .00 PROA

ATOM 563 HD1 HSD X 578 16 .052 -25 .277 28. .598 0. .00 0. .00 PROA

ATOM 564 CG HSD X 578 17 .625 -25 .626 27. .225 0. .00 0. .00 PROA

ATOM 565 CE1 HSD X 578 15 .996 -27 .070 27. .490 0. .00 0. .00 PROA

ATOM 566 HE1 HSD X 578 15 .023 -27 .497 27. .731 0. .00 0. .00 PROA

ATOM 567 NE2 HSD X 578 16 .768 -27 .678 26. .639 0. .00 0. .00 PROA

ATOM 568 CD2 HSD X 578 17 .860 -26 .788 26. .491 0. .00 0. .00 PROA

ATOM 569 HD2 HSD X 578 18 .668 -27 .095 25. .839 0. .00 0. .00 PROA

ATOM 570 C HSD X 578 18 .546 -21 .921 27. .632 0. .00 0. .00 PROA

ATOM 571 O HSD X 578 19 .577 -21 .570 27. .057 0. .00 0. .00 PROA

ATOM 572 N MET X 579 18 .054 -21 .228 28. .691 0. .00 0. .00 PROA

ATOM 573 HN MET X 579 17 .328 -21 .569 29. .284 0. .00 0. .00 PROA

ATOM 574 CA MET X 579 18 .687 -20 .095 29. .287 0. .00 0. .00 PROA

ATOM 575 HA MET X 579 19 .752 -20 .270 29. .254 0. .00 0. .00 PROA

ATOM 576 CB MET X 579 18 .262 -18 .800 28. .683 0. .00 0. .00 PROA

ATOM 577 HB1 MET X 579 18 .557 -18 .810 27. .613 0. .00 0. .00 PROA

ATOM 578 HB2 MET X 579 18 .790 -17 .886 29. .029 0. .00 0. .00 PROA

ATOM 579 CG MET X 579 16 .701 -18 .436 28. .919 0. .00 0. .00 PROA

ATOM 580 HG1 MET X 579 16 .749 -17 .504 28. .317 0. .00 0. .00 PROA

ATOM 581 HG2 MET X 579 16 .652 -18 .267 30. .016 0. .00 0. .00 PROA

ATOM 582 C MET X 579 18 .481 -20 .058 30. .819 0. .00 0. .00 PROA

ATOM 583 O MET X 579 17 .571 -20 .733 31. .345 0. .00 0. .00 PROA

ATOM 584 N ASP X 580 19 .262 -19 .283 31. .569 0. .00 0. .00 PROA

ATOM 585 HN ASP X 580 19 .965 -18 .670 31. .217 0. .00 0. .00 PROA

ATOM 586 CA ASP X 580 19 .285 -19 .337 32. .995 0. .00 0. .00 PROA

ATOM 587 HA ASP X 580 19 .315 -20 .376 33. .288 0. .00 0. .00 PROA

ATOM 588 CB ASP X 580 20 .487 -18 .599 33. .448 0. .00 0. .00 PROA

ATOM 589 HB1 ASP X 580 20 .480 -18 .708 34. .554 0. .00 0. .00 PROA

ATOM 590 HB2 ASP X 580 20 .439 -17 .546 33. .096 0. .00 0. .00 PROA

ATOM 591 CG ASP X 580 21 .696 -19 .239 32. .915 0. .00 0. .00 PROA

ATOM 592 OD1 ASP X 580 21 .889 -20 .473 33. .133 0. .00 0. .00 PROA

ATOM 593 OD2 ASP X 580 22 .401 -18 .487 32. .171 0. .00 0. .00 PROA ATOM 594 C ASP X 580 17.995 -18.698 33..551 0..00 0..00 PROA

ATOM 595 O ASP X 580 17 .389 -17 .842 32. .949 0. .00 0. .00 PROA

ATOM 596 N SER X 581 17 .754 -19 .071 34. .832 0. .00 0. .00 PROA

ATOM 597 HN SER X 581 18 .439 -19 .609 35. .318 0. .00 0. .00 PROA

ATOM 598 CA SER X 581 16 .580 -18 .597 35. .682 0. .00 0. .00 PROA

ATOM 599 HA SER X 581 15 .635 -18 .887 35. .247 0. .00 0. .00 PROA

ATOM 600 CB SER X 581 16 .381 -19 .511 36. .998 0. .00 0. .00 PROA

ATOM 601 HB1 SER X 581 17 .264 -19 .551 37. .671 0. .00 0. .00 PROA

ATOM 602 HB2 SER X 581 16 .144 -20 .564 36. .734 0. .00 0. .00 PROA

ATOM 603 OG SER X 581 15 .329 -19 .037 37. .800 0. .00 0. .00 PROA

ATOM 604 HG1 SER X 581 14 .802 -19 .806 38. .028 0. .00 0. .00 PROA

ATOM 605 C SER X 581 16 .503 -17 .107 35. .906 0. .00 0. .00 PROA

ATOM 606 O SER X 581 15 .501 -16 .458 35. .703 0. .00 0. .00 PROA

ATOM 607 N ARG X 582 17 .641 -16 .544 36. .220 0. .00 0. .00 PROA

ATOM 608 HN ARG X 582 18 .443 -17 .040 36. .545 0. .00 0. .00 PROA

ATOM 609 CA ARG X 582 17 .828 -15 .101 36. .301 0. .00 0. .00 PROA

ATOM 610 HA ARG X 582 17 .223 -14 .634 37. .064 0. .00 0. .00 PROA

ATOM 611 CB ARG X 582 19 .316 -14 .953 36. .757 0. .00 0. .00 PROA

ATOM 612 HB1 ARG X 582 19 .865 -15 .573 36. .016 0. .00 0. .00 PROA

ATOM 613 HB2 ARG X 582 19 .453 -15 .451 37. .741 0. .00 0. .00 PROA

ATOM 614 CG ARG X 582 19 .909 -13 .592 36. .841 0. .00 0. .00 PROA

ATOM 615 HG1 ARG X 582 19 .906 -13 .152 35. .821 0. .00 0. .00 PROA

ATOM 616 HG2 ARG X 582 20 .943 -13 .732 37. .224 0. .00 0. .00 PROA

ATOM 617 CD ARG X 582 19 .245 -12 .488 37. .764 0. .00 0. .00 PROA

ATOM 618 HD1 ARG X 582 19 .186 -12 .988 38. .755 0. .00 0. .00 PROA

ATOM 619 HD2 ARG X 582 18 .212 -12 .184 37. .490 0. .00 0. .00 PROA

ATOM 620 NE ARG X 582 20 .179 -11 .284 37. .740 0. .00 0. .00 PROA

ATOM 621 HE ARG X 582 20 .580 -10 .823 36. .948 0. .00 0. .00 PROA

ATOM 622 CZ ARG X 582 20 .120 -10 .430 38. .753 0. .00 0. .00 PROA

ATOM 623 NH1 ARG X 582 19 .443 -10 .604 39. .857 0. .00 0. .00 PROA

ATOM 624 HH11 ARG X 582 19 .705 -9 .929 40. .547 0. .00 0. .00 PROA

ATOM 625 HH12 ARG X 582 19 .170 -11 .509 40. .186 0. .00 0. .00 PROA

ATOM 626 NH2 ARG X 582 20 .987 -9 .477 38. .719 0. .00 0. .00 PROA

ATOM 627 HH21 ARG X 582 21 .787 -9 .688 38. .158 0. .00 0. .00 PROA

ATOM 628 HH22 ARG X 582 21 .250 -9 .262 39. .660 0. .00 0. .00 PROA

ATOM 629 C ARG X 582 17 .601 -14 .329 35. .007 0. .00 0. .00 PROA

ATOM 630 O ARG X 582 16 .887 -13 .358 34. .983 0. .00 0. .00 PROA

ATOM 631 N ILE X 583 18 .194 -14 .806 33. .886 0. .00 0. .00 PROA

ATOM 632 HN ILE X 583 18 .852 -15 .551 33. .970 0. .00 0. .00 PROA

ATOM 633 CA ILE X 583 18 .113 -14 .154 32. .546 0. .00 0. .00 PROA

ATOM 634 HA ILE X 583 18 .226 -13 .094 32. .724 0. .00 0. .00 PROA

ATOM 635 CB ILE X 583 19 .072 -14 .882 31. .564 0. .00 0. .00 PROA

ATOM 636 HB ILE X 583 18 .845 -15 .969 31. .579 0. .00 0. .00 PROA

ATOM 637 CG2 ILE X 583 18 .848 -14 .414 30. .070 0. .00 0. .00 PROA

ATOM 638 HG21 ILE X 583 17 .918 -14 .934 29. .753 0. .00 0. .00 PROA

ATOM 639 HG22 ILE X 583 19 .678 -14 .724 29. .400 0. .00 0. .00 PROA

ATOM 640 HG23 ILE X 583 18 .707 -13 .313 30. .106 0. .00 0. .00 PROA

ATOM 641 CGI ILE X 583 20 .511 -14 .575 32. .096 0. .00 0. .00 PROA

ATOM 642 HG11 ILE X 583 21 .257 -15 .144 31. .501 0. .00 0. .00 PROA

ATOM 643 HG12 ILE X 583 20 .468 -14 .911 33. .154 0. .00 0. .00 PROA

ATOM 644 CD ILE X 583 20 .998 -13 .123 31. .978 0. .00 0. .00 PROA

ATOM 645 HD1 ILE X 583 20 .310 -12 .435 32. .514 0. .00 0. .00 PROA

ATOM 646 HD2 ILE X 583 20 .991 -12 .799 30. .915 0. .00 0. .00 PROA

ATOM 647 HD3 ILE X 583 22 .055 -12 .977 32. .286 0. .00 0. .00 PROA

ATOM 648 C ILE X 583 16 .718 -14 .253 32. .099 0. .00 0. .00 PROA

ATOM 649 O ILE X 583 16 .110 -13 .331 31. .660 0. .00 0. .00 PROA

ATOM 650 N GLY X 584 15 .972 -15 .369 32. .432 0. .00 0. .00 PROA

ATOM 651 HN GLY X 584 16 .415 -16 .168 32. .831 0. .00 0. .00 PROA

ATOM 652 CA GLY X 584 14 .577 -15 .618 32. .106 0. .00 0. .00 PROA

ATOM 653 HA1 GLY X 584 14 .307 -16 .630 32. .370 0. .00 0. .00 PROA

ATOM 654 HA2 GLY X 584 14 .469 -15 .503 31. .038 0. .00 0. .00 PROA

ATOM 655 C GLY X 584 13 .629 -14 .702 32. .901 0. .00 0. .00 PROA

ATOM 656 O GLY X 584 12 .671 -14 .146 32. .336 0. .00 0. .00 PROA

ATOM 657 N TRP X 585 13 .956 -14 .465 34. .217 0. .00 0. .00 PROA

ATOM 658 HN TRP X 585 14 .675 -14 .979 34. .679 0. .00 0. .00 PROA

ATOM 659 CA TRP X 585 13 .285 -13 .384 35. .019 0. .00 0. .00 PROA ATOM 660 HA TRP X 585 12.243 -13.543 34..787 0..00 0..00 PROA

ATOM 661 CB TRP X 585 13 .492 -13 .658 36. .571 0. .00 0. .00 PROA

ATOM 662 HB1 TRP X 585 14 .588 -13 .702 36. .748 0. .00 0. .00 PROA

ATOM 663 HB2 TRP X 585 13 .219 -14 .698 36. .853 0. .00 0. .00 PROA

ATOM 664 CG TRP X 585 13 .110 -12 .648 37. .673 0. .00 0. .00 PROA

ATOM 665 CD1 TRP X 585 11 .844 -12 .494 38. .297 0. .00 0. .00 PROA

ATOM 666 HD1 TRP X 585 10 .887 -12 .970 38. .144 0. .00 0. .00 PROA

ATOM 667 NE1 TRP X 585 11 .913 -11 .496 39. .237 0. .00 0. .00 PROA

ATOM 668 HE1 TRP X 585 11 .110 -11 .055 39. .573 0. .00 0. .00 PROA

ATOM 669 CE2 TRP X 585 13 .145 -11 .015 39. .245 0. .00 0. .00 PROA

ATOM 670 CD2 TRP X 585 13 .849 -11 .602 38. .207 0. .00 0. .00 PROA

ATOM 671 CE3 TRP X 585 15 .168 -11 .051 37. .882 0. .00 0. .00 PROA

ATOM 672 HE3 TRP X 585 15 .703 -11 .511 37. .065 0. .00 0. .00 PROA

ATOM 673 CZ3 TRP X 585 15 .658 -10 .009 38. .635 0. .00 0. .00 PROA

ATOM 674 HZ3 TRP X 585 16 .615 -9 .568 38. .399 0. .00 0. .00 PROA

ATOM 675 CZ2 TRP X 585 13 .651 -10 .023 40. .061 0. .00 0. .00 PROA

ATOM 676 HZ2 TRP X 585 13 .090 -9 .676 40. .916 0. .00 0. .00 PROA

ATOM 677 CH2 TRP X 585 14 .910 -9 .500 39. .730 0. .00 0. .00 PROA

ATOM 678 HH2 TRP X 585 15 .360 -8 .731 40. .340 0. .00 0. .00 PROA

ATOM 679 C TRP X 585 13 .424 -11 .968 34. .562 0. .00 0. .00 PROA

ATOM 680 O TRP X 585 12 .480 -11 .169 34. .497 0. .00 0. .00 PROA

ATOM 681 N LEU X 586 14 .639 -11 .606 34. .176 0. .00 0. .00 PROA

ATOM 682 HN LEU X 586 15 .402 -12 .227 34. .342 0. .00 0. .00 PROA

ATOM 683 CA LEU X 586 14 .888 -10 .319 33. .476 0. .00 0. .00 PROA

ATOM 684 HA LEU X 586 14 .534 -9 .561 34. .159 0. .00 0. .00 PROA

ATOM 685 CB LEU X 586 16 .339 -9 .896 33. .194 0. .00 0. .00 PROA

ATOM 686 HB1 LEU X 586 16 .404 -8 .982 32. .565 0. .00 0. .00 PROA

ATOM 687 HB2 LEU X 586 16 .799 -10 .784 32. .709 0. .00 0. .00 PROA

ATOM 688 CG LEU X 586 17 .249 -9 .642 34. .398 0. .00 0. .00 PROA

ATOM 689 HG LEU X 586 17 .248 -10 .569 35. .011 0. .00 0. .00 PROA

ATOM 690 CD1 LEU X 586 18 .643 -9 .181 33. .929 0. .00 0. .00 PROA

ATOM 691 HD11 LEU X 586 18 .714 -8 .173 33. .466 0. .00 0. .00 PROA

ATOM 692 HD12 LEU X 586 19 .041 -9 .823 33. .115 0. .00 0. .00 PROA

ATOM 693 HD13 LEU X 586 19 .480 -9 .264 34. .655 0. .00 0. .00 PROA

ATOM 694 CD2 LEU X 586 16 .689 -8 .556 35. .286 0. .00 0. .00 PROA

ATOM 695 HD21 LEU X 586 17 .509 -8 .354 36. .007 0. .00 0. .00 PROA

ATOM 696 HD22 LEU X 586 15 .845 -8 .899 35. .922 0. .00 0. .00 PROA

ATOM 697 HD23 LEU X 586 16 .395 -7 .699 34. .643 0. .00 0. .00 PROA

ATOM 698 C LEU X 586 14 .039 -10 .173 32. .163 0. .00 0. .00 PROA

ATOM 699 O LEU X 586 13 .499 -9 .099 31. .889 0. .00 0. .00 PROA

ATOM 700 N HSD X 587 13 .944 -11 .184 31. .330 0. .00 0. .00 PROA

ATOM 701 HN HSD X 587 14 .484 -12 .012 31. .460 0. .00 0. .00 PROA

ATOM 702 CA HSD X 587 12 .962 -11 .240 30. .220 0. .00 0. .00 PROA

ATOM 703 HA HSD X 587 13 .084 -10 .352 29. .617 0. .00 0. .00 PROA

ATOM 704 CB HSD X 587 12 .896 -12 .475 29. .301 0. .00 0. .00 PROA

ATOM 705 HB1 HSD X 587 12 .169 -12 .255 28. .491 0. .00 0. .00 PROA

ATOM 706 HB2 HSD X 587 12 .733 -13 .419 29. .865 0. .00 0. .00 PROA

ATOM 707 ND1 HSD X 587 14 .597 -11 .371 27. .682 0. .00 0. .00 PROA

ATOM 708 HD1 HSD X 587 14 .171 -10 .468 27. .631 0. .00 0. .00 PROA

ATOM 709 CG HSD X 587 14 .227 -12 .405 28. .544 0. .00 0. .00 PROA

ATOM 710 CE1 HSD X 587 15 .839 -11 .639 27. .203 0. .00 0. .00 PROA

ATOM 711 HE1 HSD X 587 16 .204 -11 .015 26. .387 0. .00 0. .00 PROA

ATOM 712 NE2 HSD X 587 16 .299 -12 .795 27. .667 0. .00 0. .00 PROA

ATOM 713 CD2 HSD X 587 15 .298 -13 .283 28. .563 0. .00 0. .00 PROA

ATOM 714 HD2 HSD X 587 15 .515 -14 .040 29. .306 0. .00 0. .00 PROA

ATOM 715 C HSD X 587 11 .566 -10 .967 30. .674 0. .00 0. .00 PROA

ATOM 716 O HSD X 587 10 .972 -10 .228 29. .963 0. .00 0. .00 PROA

ATOM 717 N ASN X 588 11 .080 -11 .453 31. .828 0. .00 0. .00 PROA

ATOM 718 HN ASN X 588 11 .694 -12 .079 32. .303 0. .00 0. .00 PROA

ATOM 719 CA ASN X 588 9. .763 -11 .234 32. .448 0. .00 0. .00 PROA

ATOM 720 HA ASN X 588 9. .082 -11 .507 31. .655 0. .00 0. .00 PROA

ATOM 721 CB ASN X 588 9. .508 -12 .067 33. .757 0. .00 0. .00 PROA

ATOM 722 HB1 ASN X 588 8 .445 -11 .948 34. .057 0. .00 0. .00 PROA

ATOM 723 HB2 ASN X 588 10 .197 -11 .694 34. .544 0. .00 0. .00 PROA

ATOM 724 CG ASN X 588 9. .666 -13 .621 33. .519 0. .00 0. .00 PROA

ATOM 725 OD1 ASN X 588 9 .991 -14 .368 34. .393 0. .00 0. .00 PROA ATOM 726 ND2 ASN X 588 9.348 -14.142 32..283 0..00 0..00 PROA

ATOM 727 HD21 ASN X 588 9 .453 -15 .129 32. .159 0. .00 0. .00 PROA

ATOM 728 HD22 ASN X 588 9 .091 -13 .538 31. .529 0. .00 0. .00 PROA

ATOM 729 C ASN X 588 9. .471 -9 .753 32. .795 0. .00 0. .00 PROA

ATOM 730 O ASN X 588 8. .454 -9 .259 32. .401 0. .00 0. .00 PROA

ATOM 731 N LEU X 589 10 .434 -9 .039 33. .431 0. .00 0. .00 PROA

ATOM 732 HN LEU X 589 11 .168 -9 .497 33. .927 0. .00 0. .00 PROA

ATOM 733 CA LEU X 589 10 .369 -7 .636 33. .680 0. .00 0. .00 PROA

ATOM 734 HA LEU X 589 9. .367 -7 .489 34. .055 0. .00 0. .00 PROA

ATOM 735 CB LEU X 589 11 .450 -7 .147 34. .770 0. .00 0. .00 PROA

ATOM 736 HB1 LEU X 589 11 .459 -6 .037 34. .744 0. .00 0. .00 PROA

ATOM 737 HB2 LEU X 589 12 .325 -7 .471 34. .167 0. .00 0. .00 PROA

ATOM 738 CG LEU X 589 11 .411 -7 .866 36. .045 0. .00 0. .00 PROA

ATOM 739 HG LEU X 589 11 .557 -8 .939 35. .800 0. .00 0. .00 PROA

ATOM 740 CD1 LEU X 589 12 .691 -7 .453 36. .898 0. .00 0. .00 PROA

ATOM 741 HD11 LEU X 589 13 .565 -7 .825 36. .321 0. .00 0. .00 PROA

ATOM 742 HD12 LEU X 589 12 .759 -7 .992 37. .867 0. .00 0. .00 PROA

ATOM 743 HD13 LEU X 589 12 .648 -6 .366 37. .125 0. .00 0. .00 PROA

ATOM 744 CD2 LEU X 589 10 .192 -7 .573 36. .930 0. .00 0. .00 PROA

ATOM 745 HD21 LEU X 589 10 .177 -8 .196 37. .850 0. .00 0. .00 PROA

ATOM 746 HD22 LEU X 589 9 .221 -7 .708 36. .408 0. .00 0. .00 PROA

ATOM 747 HD23 LEU X 589 10 .198 -6 .526 37. .304 0. .00 0. .00 PROA

ATOM 748 C LEU X 589 10 .531 -6 .831 32. .341 0. .00 0. .00 PROA

ATOM 749 O LEU X 589 9. .845 -5 .889 32. .100 0. .00 0. .00 PROA

ATOM 750 N GLY X 590 11 .394 -7 .339 31. .448 0. .00 0. .00 PROA

ATOM 751 HN GLY X 590 11 .893 -8 .193 31. .570 0. .00 0. .00 PROA

ATOM 752 CA GLY X 590 11 .566 -6 .811 30. .100 0. .00 0. .00 PROA

ATOM 753 HA1 GLY X 590 12 .220 -7 .415 29. .489 0. .00 0. .00 PROA

ATOM 754 HA2 GLY X 590 11 .975 -5 .811 30. .095 0. .00 0. .00 PROA

ATOM 755 C GLY X 590 10 .261 -6 .819 29. .260 0. .00 0. .00 PROA

ATOM 756 O GLY X 590 9. .857 -5 .877 28. .622 0. .00 0. .00 PROA

ATOM 757 N ASP X 591 9. .552 -7 .949 29. .253 0. .00 0. .00 PROA

ATOM 758 HN ASP X 591 10 .048 -8 .738 29. .606 0. .00 0. .00 PROA

ATOM 759 CA ASP X 591 8. .250 -8 .113 28. .619 0. .00 0. .00 PROA

ATOM 760 HA ASP X 591 8. .313 -7 .910 27. .560 0. .00 0. .00 PROA

ATOM 761 CB ASP X 591 7. .705 -9 .583 28. .790 0. .00 0. .00 PROA

ATOM 762 HB1 ASP X 591 7 .184 -9 .740 29. .759 0. .00 0. .00 PROA

ATOM 763 HB2 ASP X 591 8 .636 -10 .189 28. .774 0. .00 0. .00 PROA

ATOM 764 CG ASP X 591 6. .816 -9 .949 27. .681 0. .00 0. .00 PROA

ATOM 765 OD1 ASP X 591 6 .915 -9 .378 26. .573 0. .00 0. .00 PROA

ATOM 766 OD2 ASP X 591 6 .175 -11 .014 27. .846 0. .00 0. .00 PROA

ATOM 767 C ASP X 591 7. .302 -7 .098 29. .251 0. .00 0. .00 PROA

ATOM 768 O ASP X 591 6. .343 -6 .568 28. .681 0. .00 0. .00 PROA

ATOM 769 N GLN X 592 7. .474 -6 .937 30. .583 0. .00 0. .00 PROA

ATOM 770 HN GLN X 592 8. .221 -7 .445 31. .006 0. .00 0. .00 PROA

ATOM 771 CA GLN X 592 6. .602 -6 .022 31. .376 0. .00 0. .00 PROA

ATOM 772 HA GLN X 592 5. .616 -6 .286 31. .023 0. .00 0. .00 PROA

ATOM 773 CB GLN X 592 6. .821 -6 .469 32. .831 0. .00 0. .00 PROA

ATOM 774 HB1 GLN X 592 7 .884 -6 .758 32. .974 0. .00 0. .00 PROA

ATOM 775 HB2 GLN X 592 6 .247 -7 .408 32. .981 0. .00 0. .00 PROA

ATOM 776 CG GLN X 592 6. .375 -5 .380 33. .870 0. .00 0. .00 PROA

ATOM 777 HG1 GLN X 592 5 .270 -5 .464 33. .946 0. .00 0. .00 PROA

ATOM 778 HG2 GLN X 592 6 .644 -4 .360 33. .520 0. .00 0. .00 PROA

ATOM 779 CD GLN X 592 6. .932 -5 .723 35. .206 0. .00 0. .00 PROA

ATOM 780 OE1 GLN X 592 7 .900 -5 .136 35. .805 0. .00 0. .00 PROA

ATOM 781 NE2 GLN X 592 6 .333 -6 .701 35. .886 0. .00 0. .00 PROA

ATOM 782 HE21 GLN X 592 6 .608 -6 .751 36. .847 0. .00 0. .00 PROA

ATOM 783 HE22 GLN X 592 5 .507 -7 .159 35. .558 0. .00 0. .00 PROA

ATOM 784 C GLN X 592 6. .662 -4 .553 31. .023 0. .00 0. .00 PROA

ATOM 785 O GLN X 592 5. .692 -3 .961 30. .683 0. .00 0. .00 PROA

ATOM 786 N ILE X 593 7. .914 -4 .041 30. .979 0. .00 0. .00 PROA

ATOM 787 HN ILE X 593 8. .674 -4 .575 31. .340 0. .00 0. .00 PROA

ATOM 788 CA ILE X 593 8. .166 -2 .598 31. .042 0. .00 0. .00 PROA

ATOM 789 HA ILE X 593 7. .384 -2 .129 30. .463 0. .00 0. .00 PROA

ATOM 790 CB ILE X 593 8. .305 -2 .107 32. .477 0. .00 0. .00 PROA

ATOM 791 HB ILE X 593 7. .494 -2 .569 33. .081 0. .00 0. .00 PROA ATOM 792 CG2 ILE X 593 9.646 -2.604 33..033 0..00 0..00 PROA

ATOM 793 HG21 ILE X 593 10 .507 -1 .997 32. .679 0. .00 0. .00 PROA

ATOM 794 HG22 ILE X 593 9 .879 -3 .627 32. .668 0. .00 0. .00 PROA

ATOM 795 HG23 ILE X 593 9 .625 -2 .613 34. .144 0. .00 0. .00 PROA

ATOM 796 CGI ILE X 593 8 .078 -0 .649 32. .615 0. .00 0. .00 PROA

ATOM 797 HG11 ILE X 593 9 .017 -0 .122 32. .344 0. .00 0. .00 PROA

ATOM 798 HG12 ILE X 593 8 .001 -0 .474 33. .710 0. .00 0. .00 PROA

ATOM 799 CD ILE X 593 6. .909 0 .051 31. .880 0. .00 0. .00 PROA

ATOM 800 HD1 ILE X 593 5 .952 -0 .427 32. .179 0. .00 0. .00 PROA

ATOM 801 HD2 ILE X 593 6 .999 0 .004 30. .774 0. .00 0. .00 PROA

ATOM 802 HD3 ILE X 593 6 .804 1 .132 32. .113 0. .00 0. .00 PROA

ATOM 803 C ILE X 593 9. .311 -2 .206 30. .105 0. .00 0. .00 PROA

ATOM 804 O ILE X 593 10 .017 -1 .193 30. .263 0. .00 0. .00 PROA

ATOM 805 N GLY X 594 9. .548 -3 .091 29. .120 0. .00 0. .00 PROA

ATOM 806 HN GLY X 594 8. .908 -3 .831 28. .923 0. .00 0. .00 PROA

ATOM 807 CA GLY X 594 10 .579 -2 .896 28. .077 0. .00 0. .00 PROA

ATOM 808 HA1 GLY X 594 10 .483 -3 .767 27. .445 0. .00 0. .00 PROA

ATOM 809 HA2 GLY X 594 11 .492 -2 .891 28. .655 0. .00 0. .00 PROA

ATOM 810 C GLY X 594 10 .407 -1 .689 27. .182 0. .00 0. .00 PROA

ATOM 811 O GLY X 594 9. .244 -1 .243 27. .046 0. .00 0. .00 PROA

ATOM 812 N LYS X 595 11 .437 -1 .156 26. .463 0. .00 0. .00 PROA

ATOM 813 HN LYS X 595 12 .284 -1 .678 26. .397 0. .00 0. .00 PROA

ATOM 814 CA LYS X 595 11 .308 0 .088 25. .700 0. .00 0. .00 PROA

ATOM 815 HA LYS X 595 10 .422 0 .639 25. .977 0. .00 0. .00 PROA

ATOM 816 CB LYS X 595 12 .530 0 .925 26. .094 0. .00 0. .00 PROA

ATOM 817 HB1 LYS X 595 12 .428 1 .931 25. .634 0. .00 0. .00 PROA

ATOM 818 HB2 LYS X 595 13 .454 0 .526 25. .623 0. .00 0. .00 PROA

ATOM 819 CG LYS X 595 12 .843 1 .112 27. .655 0. .00 0. .00 PROA

ATOM 820 HG1 LYS X 595 13 .626 1 .900 27. .686 0. .00 0. .00 PROA

ATOM 821 HG2 LYS X 595 13 .399 0 .184 27. .910 0. .00 0. .00 PROA

ATOM 822 CD LYS X 595 11 .635 1 .542 28. .414 0. .00 0. .00 PROA

ATOM 823 HD1 LYS X 595 12 .068 1 .598 29. .436 0. .00 0. .00 PROA

ATOM 824 HD2 LYS X 595 10 .791 0 .819 28. .408 0. .00 0. .00 PROA

ATOM 825 CE LYS X 595 11 .081 2 .945 28. .084 0. .00 0. .00 PROA

ATOM 826 HE1 LYS X 595 10 .664 2 .846 27. .059 0. .00 0. .00 PROA

ATOM 827 HE2 LYS X 595 11 .782 3 .796 28. .224 0. .00 0. .00 PROA

ATOM 828 NZ LYS X 595 9. .927 3 .107 28. .951 0. .00 0. .00 PROA

ATOM 829 HZ1 LYS X 595 9 .345 3 .893 28. .598 0. .00 0. .00 PROA

ATOM 830 HZ2 LYS X 595 10 .185 3 .253 29. .948 0. .00 0. .00 PROA

ATOM 831 HZ3 LYS X 595 9 .394 2 .221 28. .844 0. .00 0. .00 PROA

ATOM 832 C LYS X 595 11 .212 -0 .263 24. .176 0. .00 0. .00 PROA

ATOM 833 O LYS X 595 11 .903 -1 .161 23. .791 0. .00 0. .00 PROA

ATOM 834 N PRO X 596 10 .405 0 .409 23. .274 0. .00 0. .00 PROA

ATOM 835 CD PRO X 596 9. .429 1 .384 23. .725 0. .00 0. .00 PROA

ATOM 836 HD1 PRO X 596 9 .778 2 .245 24. .333 0. .00 0. .00 PROA

ATOM 837 HD2 PRO X 596 8 .665 0 .772 24. .250 0. .00 0. .00 PROA

ATOM 838 CA PRO X 596 10 .241 0 .004 21. .922 0. .00 0. .00 PROA

ATOM 839 HA PRO X 596 10 .067 -1 .060 21. .868 0. .00 0. .00 PROA

ATOM 840 CB PRO X 596 8. .961 0 .721 21. .501 0. .00 0. .00 PROA

ATOM 841 HB1 PRO X 596 8 .071 0 .082 21. .686 0. .00 0. .00 PROA

ATOM 842 HB2 PRO X 596 8 .817 0 .926 20. .419 0. .00 0. .00 PROA

ATOM 843 CG PRO X 596 8. .807 1 .950 22. .414 0. .00 0. .00 PROA

ATOM 844 HG1 PRO X 596 9 .379 2 .827 22. .042 0. .00 0. .00 PROA

ATOM 845 HG2 PRO X 596 7 .741 2 .227 22. .554 0. .00 0. .00 PROA

ATOM 846 C PRO X 596 11 .423 0 .315 21. .013 0. .00 0. .00 PROA

ATOM 847 O PRO X 596 11 .664 -0 .496 20. .101 0. .00 0. .00 PROA

ATOM 848 N TYR X 597 12 .178 1 .387 21. .119 0. .00 0. .00 PROA

ATOM 849 HN TYR X 597 12 .126 1 .995 21. .907 0. .00 0. .00 PROA

ATOM 850 CA TYR X 597 13 .301 1 .630 20. .196 0. .00 0. .00 PROA

ATOM 851 HA TYR X 597 13 .282 1 .058 19. .280 0. .00 0. .00 PROA

ATOM 852 CB TYR X 597 13 .355 3 .044 19. .653 0. .00 0. .00 PROA

ATOM 853 HB1 TYR X 597 14 .026 3 .234 18. .788 0. .00 0. .00 PROA

ATOM 854 HB2 TYR X 597 13 .663 3 .764 20. .441 0. .00 0. .00 PROA

ATOM 855 CG TYR X 597 12 .015 3 .407 19. .026 0. .00 0. .00 PROA

ATOM 856 CD1 TYR X 597 11 .494 2 .899 17. .819 0. .00 0. .00 PROA

ATOM 857 HD1 TYR X 597 12 .194 2 .269 17. .289 0. .00 0. .00 PROA ATOM 858 CE1 TYR X 597 10.228 3.263 17..408 0..00 0..00 PROA

ATOM 859 HE1 TYR X 597 9 .810 2 .959 16. .460 0. .00 0. .00 PROA

ATOM 860 CZ TYR X 597 9. .425 4 .079 18. .232 0. .00 0. .00 PROA

ATOM 861 OH TYR X 597 8. .068 4 .275 17. .833 0. .00 0. .00 PROA

ATOM 862 HH TYR X 597 7. .793 5 .108 18. .225 0. .00 0. .00 PROA

ATOM 863 CD2 TYR X 597 11 .198 4 .187 19. .852 0. .00 0. .00 PROA

ATOM 864 HD2 TYR X 597 11 .632 4 .624 20. .740 0. .00 0. .00 PROA

ATOM 865 CE2 TYR X 597 9 .933 4 .603 19. .413 0. .00 0. .00 PROA

ATOM 866 HE2 TYR X 597 9 .291 5 .203 20. .041 0. .00 0. .00 PROA

ATOM 867 C TYR X 597 14 .654 1 .438 20. .957 0. .00 0. .00 PROA

ATOM 868 O TYR X 597 15 .646 0 .965 20. .425 0. .00 0. .00 PROA

ATOM 869 N ASN X 598 14 .659 1 .885 22. .222 0. .00 0. .00 PROA

ATOM 870 HN ASN X 598 13 .846 2 .257 22. .664 0. .00 0. .00 PROA

ATOM 871 CA ASN X 598 15 .803 1 .688 23. .125 0. .00 0. .00 PROA

ATOM 872 HA ASN X 598 16 .735 2 .017 22. .690 0. .00 0. .00 PROA

ATOM 873 CB ASN X 598 15 .628 2 .611 24. .400 0. .00 0. .00 PROA

ATOM 874 HB1 ASN X 598 14 .807 2 .157 24. .994 0. .00 0. .00 PROA

ATOM 875 HB2 ASN X 598 15 .474 3 .614 23. .946 0. .00 0. .00 PROA

ATOM 876 CG ASN X 598 16 .832 2 .515 25. .367 0. .00 0. .00 PROA

ATOM 877 OD1 ASN X 598 17 .903 1 .971 25. .114 0. .00 0. .00 PROA

ATOM 878 ND2 ASN X 598 16 .575 3 .010 26. .620 0. .00 0. .00 PROA

ATOM 879 HD21 ASN X 598 17 .380 3 .028 27. .213 0. .00 0. .00 PROA

ATOM 880 HD22 ASN X 598 15 .703 3 .455 26. .824 0. .00 0. .00 PROA

ATOM 881 C ASN X 598 16 .085 0 .205 23. .355 0. .00 0. .00 PROA

ATOM 882 O ASN X 598 15 .187 -0 .441 23. .896 0. .00 0. .00 PROA

ATOM 883 N SER X 599 17 .214 -0 .307 22. .838 0. .00 0. .00 PROA

ATOM 884 HN SER X 599 17 .835 0 .373 22. .455 0. .00 0. .00 PROA

ATOM 885 CA SER X 599 17 .524 -1 .740 22. .821 0. .00 0. .00 PROA

ATOM 886 HA SER X 599 16 .773 -2 .279 23. .379 0. .00 0. .00 PROA

ATOM 887 CB SER X 599 17 .688 -2 .205 21. .376 0. .00 0. .00 PROA

ATOM 888 HB1 SER X 599 17 .887 -3 .281 21. .185 0. .00 0. .00 PROA

ATOM 889 HB2 SER X 599 18 .528 -1 .606 20. .964 0. .00 0. .00 PROA

ATOM 890 OG SER X 599 16 .583 -1 .674 20. .598 0. .00 0. .00 PROA

ATOM 891 HG1 SER X 599 16 .568 -0 .728 20. .764 0. .00 0. .00 PROA

ATOM 892 C SER X 599 18 .772 -1 .931 23. .647 0. .00 0. .00 PROA

ATOM 893 O SER X 599 19 .517 -2 .906 23. .479 0. .00 0. .00 PROA

ATOM 894 N SER X 600 19 .110 -0 .859 24. .436 0. .00 0. .00 PROA

ATOM 895 HN SER X 600 18 .426 -0 .136 24. .377 0. .00 0. .00 PROA

ATOM 896 CA SER X 600 20 .148 -0 .912 25. .421 0. .00 0. .00 PROA

ATOM 897 HA SER X 600 21 .007 -1 .252 24. .861 0. .00 0. .00 PROA

ATOM 898 CB SER X 600 20 .536 0 .486 25. .813 0. .00 0. .00 PROA

ATOM 899 HB1 SER X 600 20 .469 1 .304 25. .064 0. .00 0. .00 PROA

ATOM 900 HB2 SER X 600 21 .611 0 .317 26. .037 0. .00 0. .00 PROA

ATOM 901 OG SER X 600 19 .767 0 .902 26. .909 0. .00 0. .00 PROA

ATOM 902 HG1 SER X 600 18 .971 1 .195 26. .459 0. .00 0. .00 PROA

ATOM 903 C SER X 600 19 .934 -1 .880 26. .529 0. .00 0. .00 PROA

ATOM 904 O SER X 600 20 .894 -2 .532 26. .908 0. .00 0. .00 PROA

ATOM 905 N GLY X 601 18 .724 -2 .058 27. .040 0. .00 0. .00 PROA

ATOM 906 HN GLY X 601 17 .955 -1 .488 26. .760 0. .00 0. .00 PROA

ATOM 907 CA GLY X 601 18 .286 -2 .972 28. .119 0. .00 0. .00 PROA

ATOM 908 HA1 GLY X 601 17 .461 -2 .436 28. .563 0. .00 0. .00 PROA

ATOM 909 HA2 GLY X 601 19 .159 -3 .135 28. .734 0. .00 0. .00 PROA

ATOM 910 C GLY X 601 17 .861 -4 .313 27. .508 0. .00 0. .00 PROA

ATOM 911 O GLY X 601 17 .810 -4 .471 26. .307 0. .00 0. .00 PROA

ATOM 912 N LEU X 602 17 .419 -5 .221 28. .402 0. .00 0. .00 PROA

ATOM 913 HN LEU X 602 17 .436 -5 .017 29. .377 0. .00 0. .00 PROA

ATOM 914 CA LEU X 602 16 .708 -6 .434 28. .058 0. .00 0. .00 PROA

ATOM 915 HA LEU X 602 17 .221 -6 .790 27. .176 0. .00 0. .00 PROA

ATOM 916 CB LEU X 602 16 .776 -7 .594 29. .085 0. .00 0. .00 PROA

ATOM 917 HB1 LEU X 602 16 .092 -8 .410 28. .769 0. .00 0. .00 PROA

ATOM 918 HB2 LEU X 602 16 .599 -7 .155 30. .090 0. .00 0. .00 PROA

ATOM 919 CG LEU X 602 18 .089 -8 .402 29. .198 0. .00 0. .00 PROA

ATOM 920 HG LEU X 602 18 .499 -8 .456 28. .167 0. .00 0. .00 PROA

ATOM 921 CD1 LEU X 602 19 .298 -7 .690 29. .879 0. .00 0. .00 PROA

ATOM 922 HD11 LEU X 602 19 .698 -6 .963 29. .139 0. .00 0. .00 PROA

ATOM 923 HD12 LEU X 602 20 .133 -8 .337 30. .225 0. .00 0. .00 PROA ATOM 924 HD13 LEU X 602 19.030 -7.163 30..820 0..00 0..00 PROA

ATOM 925 CD2 LEU X 602 18 .014 -9 .799 29. .889 0. .00 0. .00 PROA

ATOM 926 HD21 LEU X 602 17 .226 -10 .385 29. .369 0. .00 0. .00 PROA

ATOM 927 HD22 LEU X 602 17 .753 -9 .742 30. .967 0. .00 0. .00 PROA

ATOM 928 HD23 LEU X 602 18 .931 -10 .410 29. .742 0. .00 0. .00 PROA

ATOM 929 C LEU X 602 15 .197 -6 .234 27. .758 0. .00 0. .00 PROA

ATOM 930 O LEU X 602 14 .467 -5 .509 28. .453 0. .00 0. .00 PROA

ATOM 931 N GLY X 603 14 .761 -6 .961 26. .738 0. .00 0. .00 PROA

ATOM 932 HN GLY X 603 15 .414 -7 .559 26. .280 0. .00 0. .00 PROA

ATOM 933 CA GLY X 603 13 .378 -7 .018 26. .277 0. .00 0. .00 PROA

ATOM 934 HA1 GLY X 603 13 .401 -7 .066 25. .199 0. .00 0. .00 PROA

ATOM 935 HA2 GLY X 603 12 .809 -6 .202 26. .696 0. .00 0. .00 PROA

ATOM 936 C GLY X 603 12 .636 -8 .217 26. .832 0. .00 0. .00 PROA

ATOM 937 O GLY X 603 13 .112 -8 .897 27. .712 0. .00 0. .00 PROA

ATOM 938 N GLY X 604 11 .510 -8 .502 26. .268 0. .00 0. .00 PROA

ATOM 939 HN GLY X 604 11 .204 -7 .950 25. .496 0. .00 0. .00 PROA

ATOM 940 CA GLY X 604 10 .745 -9 .705 26. .506 0. .00 0. .00 PROA

ATOM 941 HA1 GLY X 604 9 .825 -9 .553 25. .962 0. .00 0. .00 PROA

ATOM 942 HA2 GLY X 604 10 .664 -9 .918 27. .562 0. .00 0. .00 PROA

ATOM 943 C GLY X 604 11 .434 -10 .937 25. .912 0. .00 0. .00 PROA

ATOM 944 O GLY X 604 12 .544 -10 .758 25. .365 0. .00 0. .00 PROA

ATOM 945 N PRO X 605 10 .869 -12 .149 26. .029 0. .00 0. .00 PROA

ATOM 946 CD PRO X 605 9. .572 -12 .338 26. .653 0. .00 0. .00 PROA

ATOM 947 HD1 PRO X 605 8 .907 -11 .642 26. .098 0. .00 0. .00 PROA

ATOM 948 HD2 PRO X 605 9 .421 -12 .096 27. .726 0. .00 0. .00 PROA

ATOM 949 CA PRO X 605 11 .096 -13 .300 25. .139 0. .00 0. .00 PROA

ATOM 950 HA PRO X 605 12 .143 -13 .567 25. .147 0. .00 0. .00 PROA

ATOM 951 CB PRO X 605 10 .315 -14 .439 25. .687 0. .00 0. .00 PROA

ATOM 952 HB1 PRO X 605 10 .946 -14 .882 26. .487 0. .00 0. .00 PROA

ATOM 953 HB2 PRO X 605 9 .972 -15 .270 25. .035 0. .00 0. .00 PROA

ATOM 954 CG PRO X 605 9. .149 -13 .795 26. .469 0. .00 0. .00 PROA

ATOM 955 HG1 PRO X 605 8 .233 -13 .606 25. .870 0. .00 0. .00 PROA

ATOM 956 HG2 PRO X 605 8 .905 -14 .399 27. .370 0. .00 0. .00 PROA

ATOM 957 C PRO X 605 10 .776 -13 .063 23. .702 0. .00 0. .00 PROA

ATOM 958 O PRO X 605 9. .571 -12 .769 23. .332 0. .00 0. .00 PROA

ATOM 959 N SER X 606 11 .763 -13 .127 22. .780 0. .00 0. .00 PROA

ATOM 960 HN SER X 606 12 .569 -13 .676 22. .987 0. .00 0. .00 PROA

ATOM 961 CA SER X 606 11 .830 -12 .484 21. .495 0. .00 0. .00 PROA

ATOM 962 HA SER X 606 11 .503 -11 .455 21. .522 0. .00 0. .00 PROA

ATOM 963 CB SER X 606 13 .310 -12 .378 21. .030 0. .00 0. .00 PROA

ATOM 964 HB1 SER X 606 13 .775 -13 .327 20. .688 0. .00 0. .00 PROA

ATOM 965 HB2 SER X 606 13 .932 -12 .096 21. .906 0. .00 0. .00 PROA

ATOM 966 OG SER X 606 13 .432 -11 .277 20. .043 0. .00 0. .00 PROA

ATOM 967 HG1 SER X 606 14 .367 -11 .169 19. .856 0. .00 0. .00 PROA

ATOM 968 C SER X 606 10 .905 -13 .161 20. .517 0. .00 0. .00 PROA

ATOM 969 O SER X 606 10 .607 -14 .359 20. .446 0. .00 0. .00 PROA

ATOM 970 N ILE X 607 10 .451 -12 .228 19. .657 0. .00 0. .00 PROA

ATOM 971 HN ILE X 607 10 .750 -11 .289 19. .810 0. .00 0. .00 PROA

ATOM 972 CA ILE X 607 9. .443 -12 .362 18. .680 0. .00 0. .00 PROA

ATOM 973 HA ILE X 607 8. .593 -12 .717 19. .245 0. .00 0. .00 PROA

ATOM 974 CB ILE X 607 9. .069 -10 .994 18. .064 0. .00 0. .00 PROA

ATOM 975 HB ILE X 607 9. .801 -10 .670 17. .294 0. .00 0. .00 PROA

ATOM 976 CG2 ILE X 607 7 .666 -11 .094 17. .408 0. .00 0. .00 PROA

ATOM 977 HG21 ILE X 607 6 .924 -11 .403 18. .175 0. .00 0. .00 PROA

ATOM 978 HG22 ILE X 607 7 .604 -11 .772 16. .530 0. .00 0. .00 PROA

ATOM 979 HG23 ILE X 607 7 .508 -10 .066 17. .017 0. .00 0. .00 PROA

ATOM 980 CGI ILE X 607 9 .043 -9 .843 19. .118 0. .00 0. .00 PROA

ATOM 981 HG11 ILE X 607 8 .702 -8 .900 18. .641 0. .00 0. .00 PROA

ATOM 982 HG12 ILE X 607 10 .112 -9 .669 19. .367 0. .00 0. .00 PROA

ATOM 983 CD ILE X 607 8. .274 -10 .018 20. .451 0. .00 0. .00 PROA

ATOM 984 HD1 ILE X 607 8 .628 -10 .874 21. .065 0. .00 0. .00 PROA

ATOM 985 HD2 ILE X 607 7 .234 -10 .407 20. .408 0. .00 0. .00 PROA

ATOM 986 HD3 ILE X 607 8 .332 -9 .211 21. .212 0. .00 0. .00 PROA

ATOM 987 C ILE X 607 9. .616 -13 .473 17. .567 0. .00 0. .00 PROA

ATOM 988 O ILE X 607 8. .724 -14 .273 17. .245 0. .00 0. .00 PROA

ATOM 989 N LYS X 608 10 .789 -13 .731 17. .067 0. .00 0. .00 PROA ATOM 990 HN LYS X 608 11.525 -13.119 17..347 0..00 0..00 PROA

ATOM 991 CA LYS X 608 11 .217 -14 .798 16. .160 0. .00 0. .00 PROA

ATOM 992 HA LYS X 608 10 .409 -14 .925 15. .455 0. .00 0. .00 PROA

ATOM 993 CB LYS X 608 12 .547 -14 .356 15. .440 0. .00 0. .00 PROA

ATOM 994 HB1 LYS X 608 12 .256 -13 .375 15. .007 0. .00 0. .00 PROA

ATOM 995 HB2 LYS X 608 12 .780 -15 .009 14. .572 0. .00 0. .00 PROA

ATOM 996 CG LYS X 608 13 .796 -14 .002 16. .281 0. .00 0. .00 PROA

ATOM 997 HG1 LYS X 608 13 .548 -13 .386 17. .172 0. .00 0. .00 PROA

ATOM 998 HG2 LYS X 608 14 .330 -13 .244 15. .670 0. .00 0. .00 PROA

ATOM 999 CD LYS X 608 14 .796 -15 .154 16. .507 0. .00 0. .00 PROA

ATOM 1000 HD1 LYS X 608 15 .057 -15 .661 15. .554 0. .00 0. .00 PROA

ATOM 1001 HD2 LYS X 608 14 .196 -15 .928 17. .031 0. .00 0. .00 PROA

ATOM 1002 CE LYS X 608 16 .126 -14 .840 17. .241 0. .00 0. .00 PROA

ATOM 1003 HE1 LYS X 608 16 .708 -14 .050 16. .721 0. .00 0. .00 PROA

ATOM 1004 HE2 LYS X 608 16 .728 -15 .757 17. .418 0. .00 0. .00 PROA

ATOM 1005 NZ LYS X 608 15 .954 -14 .229 18. .623 0. .00 0. .00 PROA

ATOM 1006 HZ1 LYS X 608 16 .810 -14 .244 19. .212 0. .00 0. .00 PROA

ATOM 1007 HZ2 LYS X 608 15 .241 -14 .752 19. .171 0. .00 0. .00 PROA

ATOM 1008 HZ3 LYS X 608 15 .540 -13 .275 18. .648 0. .00 0. .00 PROA

ATOM 1009 C LYS X 608 11 .603 -16 .049 16. .810 0. .00 0. .00 PROA

ATOM 1010 O LYS X 608 11 .848 -16 .993 16. .018 0. .00 0. .00 PROA

ATOM 1011 N ASP X 609 11 .666 -16 .175 18. .206 0. .00 0. .00 PROA

ATOM 1012 HN ASP X 609 11 .307 -15 .401 18. .722 0. .00 0. .00 PROA

ATOM 1013 CA ASP X 609 12 .104 -17 .412 18. .808 0. .00 0. .00 PROA

ATOM 1014 HA ASP X 609 13 .010 -17 .820 18. .385 0. .00 0. .00 PROA

ATOM 1015 CB ASP X 609 12 .265 -17 .209 20. .283 0. .00 0. .00 PROA

ATOM 1016 HB1 ASP X 609 12 .450 -18 .177 20. .795 0. .00 0. .00 PROA

ATOM 1017 HB2 ASP X 609 11 .335 -16 .760 20. .692 0. .00 0. .00 PROA

ATOM 1018 CG ASP X 609 13 .397 -16 .322 20. .661 0. .00 0. .00 PROA

ATOM 1019 OD1 ASP X 609 13 .619 -16 .213 21. .858 0. .00 0. .00 PROA

ATOM 1020 OD2 ASP X 609 14 .083 -15 .810 19. .747 0. .00 0. .00 PROA

ATOM 1021 C ASP X 609 11 .082 -18 .563 18. .544 0. .00 0. .00 PROA

ATOM 1022 O ASP X 609 11 .422 -19 .707 18. .168 0. .00 0. .00 PROA

ATOM 1023 N LYS X 610 9. .691 -18 .331 18. .520 0. .00 0. .00 PROA

ATOM 1024 HN LYS X 610 9. .331 -17 .402 18. .505 0. .00 0. .00 PROA

ATOM 1025 CA LYS X 610 8. .750 -19 .451 18. .358 0. .00 0. .00 PROA

ATOM 1026 HA LYS X 610 9. .218 -20 .360 18. .008 0. .00 0. .00 PROA

ATOM 1027 CB LYS X 610 7. .837 -19 .843 19. .614 0. .00 0. .00 PROA

ATOM 1028 HB1 LYS X 610 7 .465 -20 .877 19. .451 0. .00 0. .00 PROA

ATOM 1029 HB2 LYS X 610 6 .911 -19 .230 19. .644 0. .00 0. .00 PROA

ATOM 1030 CG LYS X 610 8. .464 -19 .732 20. .987 0. .00 0. .00 PROA

ATOM 1031 HG1 LYS X 610 7 .703 -19 .545 21. .774 0. .00 0. .00 PROA

ATOM 1032 HG2 LYS X 610 9 .043 -18 .800 20. .810 0. .00 0. .00 PROA

ATOM 1033 CD LYS X 610 9. .429 -20 .890 21. .369 0. .00 0. .00 PROA

ATOM 1034 HD1 LYS X 610 10 .236 -20 .938 20. .607 0. .00 0. .00 PROA

ATOM 1035 HD2 LYS X 610 8 .769 -21 .765 21. .185 0. .00 0. .00 PROA

ATOM 1036 CE LYS X 610 10 .042 -20 .752 22. .755 0. .00 0. .00 PROA

ATOM 1037 HE1 LYS X 610 9 .233 -20 .888 23. .505 0. .00 0. .00 PROA

ATOM 1038 HE2 LYS X 610 10 .573 -19 .776 22. .778 0. .00 0. .00 PROA

ATOM 1039 NZ LYS X 610 11 .042 -21 .759 22. .950 0. .00 0. .00 PROA

ATOM 1040 HZ1 LYS X 610 10 .656 -22 .725 22. .921 0. .00 0. .00 PROA

ATOM 1041 HZ2 LYS X 610 11 .571 -21 .654 23. .840 0. .00 0. .00 PROA

ATOM 1042 HZ3 LYS X 610 11 .834 -21 .608 22. .293 0. .00 0. .00 PROA

ATOM 1043 C LYS X 610 7. .975 -18 .896 17. .166 0. .00 0. .00 PROA

ATOM 1044 O LYS X 610 7. .637 -17 .702 17. .148 0. .00 0. .00 PROA

ATOM 1045 N TYR X 611 7. .669 -19 .848 16. .218 0. .00 0. .00 PROA

ATOM 1046 HN TYR X 611 8. .034 -20 .745 16. .455 0. .00 0. .00 PROA

ATOM 1047 CA TYR X 611 7. .053 -19 .672 14. .942 0. .00 0. .00 PROA

ATOM 1048 HA TYR X 611 7. .718 -19 .011 14. .406 0. .00 0. .00 PROA

ATOM 1049 CB TYR X 611 6. .817 -20 .953 14. .093 0. .00 0. .00 PROA

ATOM 1050 HB1 TYR X 611 6 .096 -21 .716 14. .456 0. .00 0. .00 PROA

ATOM 1051 HB2 TYR X 611 7 .779 -21 .508 14. .119 0. .00 0. .00 PROA

ATOM 1052 CG TYR X 611 6. .525 -20 .583 12. .715 0. .00 0. .00 PROA

ATOM 1053 CD1 TYR X 611 7 .596 -20 .268 11. .890 0. .00 0. .00 PROA

ATOM 1054 HD1 TYR X 611 8 .595 -20 .163 12. .285 0. .00 0. .00 PROA

ATOM 1055 CE1 TYR X 611 7 .330 -20 .086 10. .507 0. .00 0. .00 PROA ATOM 1056 HE1 TYR X 611 8.097 -19.780 9..811 0..00 0..00 PROA

ATOM 1057 CZ TYR X 611 6. .059 -20 .410 10. .015 0. .00 0. .00 PROA

ATOM 1058 OH TYR X 611 5. .957 -20 .392 8. .647 0. .00 0. .00 PROA

ATOM 1059 HH TYR X 611 5. .116 -20 .761 8. .368 0. .00 0. .00 PROA

ATOM 1060 CD2 TYR X 611 5 .206 -20 .675 12. .262 0. .00 0. .00 PROA

ATOM 1061 HD2 TYR X 611 4 .404 -20 .927 12. .940 0. .00 0. .00 PROA

ATOM 1062 CE2 TYR X 611 5 .030 -20 .675 10. .876 0. .00 0. .00 PROA

ATOM 1063 HE2 TYR X 611 4 .049 -20 .889 10. .479 0. .00 0. .00 PROA

ATOM 1064 C TYR X 611 5. .700 -19 .003 15. .106 0. .00 0. .00 PROA

ATOM 1065 O TYR X 611 5. .427 -17 .968 14. .551 0. .00 0. .00 PROA

ATOM 1066 N VAL X 612 4. .859 -19 .501 16. .100 0. .00 0. .00 PROA

ATOM 1067 HN VAL X 612 5. .028 -20 .361 16. .575 0. .00 0. .00 PROA

ATOM 1068 CA VAL X 612 3. .549 -18 .900 16. .387 0. .00 0. .00 PROA

ATOM 1069 HA VAL X 612 2. .907 -18 .970 15. .521 0. .00 0. .00 PROA

ATOM 1070 CB VAL X 612 2. .836 -19 .718 17. .511 0. .00 0. .00 PROA

ATOM 1071 HB VAL X 612 3. .064 -20 .737 17. .134 0. .00 0. .00 PROA

ATOM 1072 CGI VAL X 612 3 .528 -19 .633 18. .860 0. .00 0. .00 PROA

ATOM 1073 HG11 VAL X 612 3 .234 -20 .475 19. .523 0. .00 0. .00 PROA

ATOM 1074 HG12 VAL X 612 3 .205 -18 .726 19. .415 0. .00 0. .00 PROA

ATOM 1075 HG13 VAL X 612 4 .621 -19 .768 18. .719 0. .00 0. .00 PROA

ATOM 1076 CG2 VAL X 612 1 .372 -19 .470 17. .626 0. .00 0. .00 PROA

ATOM 1077 HG21 VAL X 612 1 .004 -20 .176 18. .401 0. .00 0. .00 PROA

ATOM 1078 HG22 VAL X 612 0 .840 -19 .705 16. .679 0. .00 0. .00 PROA

ATOM 1079 HG23 VAL X 612 1 .000 -18 .452 17. .872 0. .00 0. .00 PROA

ATOM 1080 C VAL X 612 3. .719 -17 .407 16. .726 0. .00 0. .00 PROA

ATOM 1081 O VAL X 612 2. .953 -16 .621 16. .226 0. .00 0. .00 PROA

ATOM 1082 N THR X 613 4. .636 -16 .967 17. .548 0. .00 0. .00 PROA

ATOM 1083 HN THR X 613 5. .255 -17 .612 17. .989 0. .00 0. .00 PROA

ATOM 1084 CA THR X 613 4. .811 -15 .529 17. .784 0. .00 0. .00 PROA

ATOM 1085 HA THR X 613 3. .861 -15 .060 17. .996 0. .00 0. .00 PROA

ATOM 1086 CB THR X 613 5. .823 -15 .353 18. .870 0. .00 0. .00 PROA

ATOM 1087 HB THR X 613 6. .854 -15 .337 18. .455 0. .00 0. .00 PROA

ATOM 1088 OG1 THR X 613 5 .731 -16 .443 19. .849 0. .00 0. .00 PROA

ATOM 1089 HG1 THR X 613 6 .627 -16 .477 20. .190 0. .00 0. .00 PROA

ATOM 1090 CG2 THR X 613 5 .548 -14 .094 19. .622 0. .00 0. .00 PROA

ATOM 1091 HG21 THR X 613 5 .901 -13 .187 19. .086 0. .00 0. .00 PROA

ATOM 1092 HG22 THR X 613 6 .024 -14 .037 20. .624 0. .00 0. .00 PROA

ATOM 1093 HG23 THR X 613 4 .476 -13 .914 19. .854 0. .00 0. .00 PROA

ATOM 1094 C THR X 613 5. .270 -14 .793 16. .491 0. .00 0. .00 PROA

ATOM 1095 O THR X 613 4. .745 -13 .707 16. .149 0. .00 0. .00 PROA

ATOM 1096 N ALA X 614 6. .197 -15 .417 15. .690 0. .00 0. .00 PROA

ATOM 1097 HN ALA X 614 6. .345 -16 .392 15. .838 0. .00 0. .00 PROA

ATOM 1098 CA ALA X 614 6. .819 -14 .823 14. .467 0. .00 0. .00 PROA

ATOM 1099 HA ALA X 614 6. .995 -13 .771 14. .638 0. .00 0. .00 PROA

ATOM 1100 CB ALA X 614 7. .932 -15 .636 13. .992 0. .00 0. .00 PROA

ATOM 1101 HB1 ALA X 614 7 .545 -16 .624 13. .664 0. .00 0. .00 PROA

ATOM 1102 HB2 ALA X 614 8 .414 -15 .981 14. .932 0. .00 0. .00 PROA

ATOM 1103 HB3 ALA X 614 8 .646 -15 .257 13. .229 0. .00 0. .00 PROA

ATOM 1104 C ALA X 614 5. .863 -14 .794 13. .297 0. .00 0. .00 PROA

ATOM 1105 O ALA X 614 5. .943 -13 .904 12. .458 0. .00 0. .00 PROA

ATOM 1106 N LEU X 615 4. .780 -15 .639 13. .293 0. .00 0. .00 PROA

ATOM 1107 HN LEU X 615 4. .793 -16 .299 14. .040 0. .00 0. .00 PROA

ATOM 1108 CA LEU X 615 3. .741 -15 .880 12. .313 0. .00 0. .00 PROA

ATOM 1109 HA LEU X 615 4. .142 -15 .900 11. .310 0. .00 0. .00 PROA

ATOM 1110 CB LEU X 615 3. .019 -17 .184 12. .509 0. .00 0. .00 PROA

ATOM 1111 HB1 LEU X 615 2 .839 -17 .330 13. .596 0. .00 0. .00 PROA

ATOM 1112 HB2 LEU X 615 3 .779 -17 .981 12. .362 0. .00 0. .00 PROA

ATOM 1113 CG LEU X 615 1. .811 -17 .510 11. .704 0. .00 0. .00 PROA

ATOM 1114 HG LEU X 615 0. .977 -16 .835 11. .993 0. .00 0. .00 PROA

ATOM 1115 CD1 LEU X 615 2 .121 -17 .509 10. .226 0. .00 0. .00 PROA

ATOM 1116 HD11 LEU X 615 3 .169 -17 .794 9. .992 0. .00 0. .00 PROA

ATOM 1117 HD12 LEU X 615 1 .987 -16 .451 9. .915 0. .00 0. .00 PROA

ATOM 1118 HD13 LEU X 615 1 .440 -18 .153 9. .631 0. .00 0. .00 PROA

ATOM 1119 CD2 LEU X 615 1 .218 -18 .967 12. .018 0. .00 0. .00 PROA

ATOM 1120 HD21 LEU X 615 2 .015 -19 .710 11. .804 0. .00 0. .00 PROA

ATOM 1121 HD22 LEU X 615 0 .364 -19 .377 11. .437 0. .00 0. .00 PROA ATOM 1122 HD23 LEU X 615 0.889 -18.966 13..079 0..00 0..00 PROA

ATOM 1123 C LEU X 615 2. .768 -14 .700 12. .296 0. .00 0. .00 PROA

ATOM 1124 O LEU X 615 2. .644 -13 .865 11. .395 0. .00 0. .00 PROA

ATOM 1125 N TYR X 616 2. .058 -14 .479 13. .432 0. .00 0. .00 PROA

ATOM 1126 HN TYR X 616 2. .290 -15 .023 14. .234 0. .00 0. .00 PROA

ATOM 1127 CA TYR X 616 1. .074 -13 .407 13. .622 0. .00 0. .00 PROA

ATOM 1128 HA TYR X 616 0. .453 -13 .338 12. .741 0. .00 0. .00 PROA

ATOM 1129 CB TYR X 616 0. .126 -13 .547 14. .813 0. .00 0. .00 PROA

ATOM 1130 HB1 TYR X 616 -0 .537 -12 .668 14. .964 0. .00 0. .00 PROA

ATOM 1131 HB2 TYR X 616 0 .715 -13 .511 15. .755 0. .00 0. .00 PROA

ATOM 1132 CG TYR X 616 -0 .622 -14 .832 14. .774 0. .00 0. .00 PROA

ATOM 1133 CD1 TYR X 616 -0 .343 -15 .877 15. .706 0. .00 0. .00 PROA

ATOM 1134 HD1 TYR X 616 0 .291 -15 .707 16. .564 0. .00 0. .00 PROA

ATOM 1135 CE1 TYR X 616 -0 .732 -17 .155 15. .436 0. .00 0. .00 PROA

ATOM 1136 HE1 TYR X 616 -0 .494 -17 .933 16. .146 0. .00 0. .00 PROA

ATOM 1137 CZ TYR X 616 -1 .531 -17 .430 14. .371 0. .00 0. .00 PROA

ATOM 1138 OH TYR X 616 -1 .814 -18 .828 14. .139 0. .00 0. .00 PROA

ATOM 1139 HH TYR X 616 -1 .291 -19 .477 14. .615 0. .00 0. .00 PROA

ATOM 1140 CD2 TYR X 616 -1 .391 -15 .193 13. .612 0. .00 0. .00 PROA

ATOM 1141 HD2 TYR X 616 -1 .460 -14 .458 12. .824 0. .00 0. .00 PROA

ATOM 1142 CE2 TYR X 616 -1 .860 -16 .478 13. .404 0. .00 0. .00 PROA

ATOM 1143 HE2 TYR X 616 -2 .488 -16 .682 12. .549 0. .00 0. .00 PROA

ATOM 1144 C TYR X 616 1. .663 -11 .991 13. .557 0. .00 0. .00 PROA

ATOM 1145 O TYR X 616 1. .139 -11 .024 13. .014 0. .00 0. .00 PROA

ATOM 1146 N PHE X 617 2. .907 -11 .838 13. .969 0. .00 0. .00 PROA

ATOM 1147 HN PHE X 617 3. .391 -12 .638 14. .316 0. .00 0. .00 PROA

ATOM 1148 CA PHE X 617 3. .696 -10 .641 13. .773 0. .00 0. .00 PROA

ATOM 1149 HA PHE X 617 3. .074 -9 .805 14. .055 0. .00 0. .00 PROA

ATOM 1150 CB PHE X 617 4. .964 -10 .783 14. .584 0. .00 0. .00 PROA

ATOM 1151 HB1 PHE X 617 5 .406 -11 .767 14. .317 0. .00 0. .00 PROA

ATOM 1152 HB2 PHE X 617 4 .951 -10 .861 15. .692 0. .00 0. .00 PROA

ATOM 1153 CG PHE X 617 6. .016 -9 .693 14. .301 0. .00 0. .00 PROA

ATOM 1154 CD1 PHE X 617 5 .963 -8 .581 15. .031 0. .00 0. .00 PROA

ATOM 1155 HD1 PHE X 617 5 .262 -8 .476 15. .846 0. .00 0. .00 PROA

ATOM 1156 CE1 PHE X 617 7 .011 -7 .610 14. .962 0. .00 0. .00 PROA

ATOM 1157 HE1 PHE X 617 7 .099 -6 .773 15. .638 0. .00 0. .00 PROA

ATOM 1158 CZ PHE X 617 7. .988 -7 .695 13. .977 0. .00 0. .00 PROA

ATOM 1159 HZ PHE X 617 8. .868 -7 .072 13. .908 0. .00 0. .00 PROA

ATOM 1160 CD2 PHE X 617 7 .054 -9 .843 13. .357 0. .00 0. .00 PROA

ATOM 1161 HD2 PHE X 617 7 .148 -10 .758 12. .790 0. .00 0. .00 PROA

ATOM 1162 CE2 PHE X 617 8 .002 -8 .852 13. .168 0. .00 0. .00 PROA

ATOM 1163 HE2 PHE X 617 8 .895 -8 .949 12. .569 0. .00 0. .00 PROA

ATOM 1164 C PHE X 617 3. .953 -10 .357 12. .304 0. .00 0. .00 PROA

ATOM 1165 O PHE X 617 3. .694 -9 .293 11. .726 0. .00 0. .00 PROA

ATOM 1166 N THR X 618 4. .548 -11 .392 11. .594 0. .00 0. .00 PROA

ATOM 1167 HN THR X 618 4. .997 -12 .131 12. .092 0. .00 0. .00 PROA

ATOM 1168 CA THR X 618 4. .928 -11 .244 10. .180 0. .00 0. .00 PROA

ATOM 1169 HA THR X 618 5. .488 -10 .324 10. .102 0. .00 0. .00 PROA

ATOM 1170 CB THR X 618 5. .729 -12 .465 9. .698 0. .00 0. .00 PROA

ATOM 1171 HB THR X 618 5. .289 -13 .421 10. .055 0. .00 0. .00 PROA

ATOM 1172 OG1 THR X 618 6 .928 -12 .503 10. .449 0. .00 0. .00 PROA

ATOM 1173 HG1 THR X 618 6 .849 -12 .955 11. .291 0. .00 0. .00 PROA

ATOM 1174 CG2 THR X 618 6 .099 -12 .495 8. .205 0. .00 0. .00 PROA

ATOM 1175 HG21 THR X 618 6 .611 -13 .415 7. .851 0. .00 0. .00 PROA

ATOM 1176 HG22 THR X 618 6 .711 -11 .612 7. .922 0. .00 0. .00 PROA

ATOM 1177 HG23 THR X 618 5 .199 -12 .324 7. .576 0. .00 0. .00 PROA

ATOM 1178 C THR X 618 3. .711 -10 .921 9. .320 0. .00 0. .00 PROA

ATOM 1179 O THR X 618 3. .684 -10 .047 8. .427 0. .00 0. .00 PROA

ATOM 1180 N PHE X 619 2. .607 -11 .652 9. .503 0. .00 0. .00 PROA

ATOM 1181 HN PHE X 619 2. .644 -12 .349 10. .215 0. .00 0. .00 PROA

ATOM 1182 CA PHE X 619 1. .318 -11 .401 8. .768 0. .00 0. .00 PROA

ATOM 1183 HA PHE X 619 1. .479 -11 .630 7. .725 0. .00 0. .00 PROA

ATOM 1184 CB PHE X 619 0. .301 -12 .482 9. .288 0. .00 0. .00 PROA

ATOM 1185 HB1 PHE X 619 -0 .725 -12 .128 9. .052 0. .00 0. .00 PROA

ATOM 1186 HB2 PHE X 619 0 .410 -12 .504 10. .393 0. .00 0. .00 PROA

ATOM 1187 CG PHE X 619 0. .456 -13 .862 8. .805 0. .00 0. .00 PROA ATOM 1188 CD1 PHE X 619 -0.544 -14.767 9..123 0..00 0..00 PROA

ATOM 1189 HD1 PHE X 619 -1 .351 -14 .531 9. .801 0. .00 0. .00 PROA

ATOM 1190 CE1 PHE X 619 -0 .522 -16 .015 8. .492 0. .00 0. .00 PROA

ATOM 1191 HE1 PHE X 619 -1 .380 -16 .648 8. .662 0. .00 0. .00 PROA

ATOM 1192 CZ PHE X 619 0. .477 -16 .376 7. .598 0. .00 0. .00 PROA

ATOM 1193 HZ PHE X 619 0. .417 -17 .350 7. .136 0. .00 0. .00 PROA

ATOM 1194 CD2 PHE X 619 1 .588 -14 .279 8. .037 0. .00 0. .00 PROA

ATOM 1195 HD2 PHE X 619 2 .458 -13 .655 7. .900 0. .00 0. .00 PROA

ATOM 1196 CE2 PHE X 619 1 .527 -15 .508 7. .371 0. .00 0. .00 PROA

ATOM 1197 HE2 PHE X 619 2 .293 -15 .835 6. .684 0. .00 0. .00 PROA

ATOM 1198 C PHE X 619 0. .636 -10 .006 8. .845 0. .00 0. .00 PROA

ATOM 1199 O PHE X 619 0. .356 -9 .291 7. .857 0. .00 0. .00 PROA

ATOM 1200 N SER X 620 0. .533 -9 .563 10. .139 0. .00 0. .00 PROA

ATOM 1201 HN SER X 620 0. .789 -10 .185 10. .874 0. .00 0. .00 PROA

ATOM 1202 CA SER X 620 0. .101 -8 .261 10. .501 0. .00 0. .00 PROA

ATOM 1203 HA SER X 620 -0 .922 -8 .079 10. .207 0. .00 0. .00 PROA

ATOM 1204 CB SER X 620 0. .058 -8 .033 12. .068 0. .00 0. .00 PROA

ATOM 1205 HB1 SER X 620 -0 .420 -7 .063 12. .321 0. .00 0. .00 PROA

ATOM 1206 HB2 SER X 620 0 .999 -7 .955 12. .653 0. .00 0. .00 PROA

ATOM 1207 OG SER X 620 -0 .755 -9 .031 12. .673 0. .00 0. .00 PROA

ATOM 1208 HG1 SER X 620 -0 .151 -9 .702 12. .997 0. .00 0. .00 PROA

ATOM 1209 C SER X 620 1. .021 -7 .211 9. .990 0. .00 0. .00 PROA

ATOM 1210 O SER X 620 0. .492 -6 .245 9. .524 0. .00 0. .00 PROA

ATOM 1211 N SER X 621 2. .381 -7 .371 10. .003 0. .00 0. .00 PROA

ATOM 1212 HN SER X 621 2. .828 -8 .084 10. .537 0. .00 0. .00 PROA

ATOM 1213 CA SER X 621 3. .289 -6 .419 9. .424 0. .00 0. .00 PROA

ATOM 1214 HA SER X 621 3. .177 -5 .421 9. .819 0. .00 0. .00 PROA

ATOM 1215 CB SER X 621 4. .750 -6 .744 9. .823 0. .00 0. .00 PROA

ATOM 1216 HB1 SER X 621 5 .508 -6 .107 9. .318 0. .00 0. .00 PROA

ATOM 1217 HB2 SER X 621 4 .822 -7 .814 9. .531 0. .00 0. .00 PROA

ATOM 1218 OG SER X 621 5. .011 -6 .709 11. .234 0. .00 0. .00 PROA

ATOM 1219 HG1 SER X 621 4 .608 -7 .491 11. .618 0. .00 0. .00 PROA

ATOM 1220 C SER X 621 3. .177 -6 .257 7. .991 0. .00 0. .00 PROA

ATOM 1221 O SER X 621 3. .230 -5 .135 7. .457 0. .00 0. .00 PROA

ATOM 1222 N LEU X 622 3. .170 -7 .358 7. .191 0. .00 0. .00 PROA

ATOM 1223 HN LEU X 622 3. .190 -8 .255 7. .626 0. .00 0. .00 PROA

ATOM 1224 CA LEU X 622 3. .153 -7 .321 5. .753 0. .00 0. .00 PROA

ATOM 1225 HA LEU X 622 3. .784 -6 .530 5. .374 0. .00 0. .00 PROA

ATOM 1226 CB LEU X 622 3. .376 -8 .744 5. .125 0. .00 0. .00 PROA

ATOM 1227 HB1 LEU X 622 3 .243 -8 .785 4. .023 0. .00 0. .00 PROA

ATOM 1228 HB2 LEU X 622 2 .728 -9 .483 5. .642 0. .00 0. .00 PROA

ATOM 1229 CG LEU X 622 4. .815 -9 .263 5. .512 0. .00 0. .00 PROA

ATOM 1230 HG LEU X 622 4. .991 -8 .959 6. .566 0. .00 0. .00 PROA

ATOM 1231 CD1 LEU X 622 4 .895 -10 .875 5. .380 0. .00 0. .00 PROA

ATOM 1232 HD11 LEU X 622 4 .636 -11 .100 4. .324 0. .00 0. .00 PROA

ATOM 1233 HD12 LEU X 622 4 .072 -11 .382 5. .929 0. .00 0. .00 PROA

ATOM 1234 HD13 LEU X 622 5 .919 -11 .254 5. .588 0. .00 0. .00 PROA

ATOM 1235 CD2 LEU X 622 5 .826 -8 .663 4. .498 0. .00 0. .00 PROA

ATOM 1236 HD21 LEU X 622 5 .353 -8 .877 3. .516 0. .00 0. .00 PROA

ATOM 1237 HD22 LEU X 622 6 .856 -9 .067 4. .599 0. .00 0. .00 PROA

ATOM 1238 HD23 LEU X 622 5 .917 -7 .562 4. .615 0. .00 0. .00 PROA

ATOM 1239 C LEU X 622 1. .800 -6 .757 5. .316 0. .00 0. .00 PROA

ATOM 1240 O LEU X 622 1. .756 -5 .884 4. .418 0. .00 0. .00 PROA

ATOM 1241 N THR X 623 0. .667 -7 .182 6. .015 0. .00 0. .00 PROA

ATOM 1242 HN THR X 623 0. .727 -7 .871 6. .733 0. .00 0. .00 PROA

ATOM 1243 CA THR X 623 -0 .676 -6 .632 5. .671 0. .00 0. .00 PROA

ATOM 1244 HA THR X 623 -0 .603 -6 .560 4. .596 0. .00 0. .00 PROA

ATOM 1245 CB THR X 623 -1 .895 -7 .399 6. .084 0. .00 0. .00 PROA

ATOM 1246 HB THR X 623 -2 .868 -6 .915 5. .855 0. .00 0. .00 PROA

ATOM 1247 OG1 THR X 623 -1 .869 -8 .009 7. .316 0. .00 0. .00 PROA

ATOM 1248 HG1 THR X 623 -1 .124 -8 .614 7. .336 0. .00 0. .00 PROA

ATOM 1249 CG2 THR X 623 -2 .086 -8 .561 5. .021 0. .00 0. .00 PROA

ATOM 1250 HG21 THR X 623 -1 .067 -8 .969 4. .852 0. .00 0. .00 PROA

ATOM 1251 HG22 THR X 623 -2 .299 -8 .158 4. .008 0. .00 0. .00 PROA

ATOM 1252 HG23 THR X 623 -2 .764 -9 .378 5. .349 0. .00 0. .00 PROA

ATOM 1253 C THR X 623 -0 .889 -5 .269 6. .113 0. .00 0. .00 PROA ATOM 1254 O THR X 623 -1.823 -4.645 5..770 0..00 0..00 PROA

ATOM 1255 N SER X 624 0. .005 -4 .727 6. .965 0. .00 0. .00 PROA

ATOM 1256 HN SER X 624 0. .696 -5 .291 7. .410 0. .00 0. .00 PROA

ATOM 1257 CA SER X 624 0. .039 -3 .286 7. .286 0. .00 0. .00 PROA

ATOM 1258 HA SER X 624 0. .886 -3 .108 7. .932 0. .00 0. .00 PROA

ATOM 1259 CB SER X 624 0. .250 -2 .373 6. .071 0. .00 0. .00 PROA

ATOM 1260 HB1 SER X 624 0 .171 -1 .312 6. .390 0. .00 0. .00 PROA

ATOM 1261 HB2 SER X 624 -0 .592 -2 .453 5. .350 0. .00 0. .00 PROA

ATOM 1262 OG SER X 624 1. .420 -2 .732 5. .382 0. .00 0. .00 PROA

ATOM 1263 HG1 SER X 624 2 .107 -2 .357 5. .938 0. .00 0. .00 PROA

ATOM 1264 C SER X 624 -1 .061 -2 .988 8. .306 0. .00 0. .00 PROA

ATOM 1265 O SER X 624 -1 .745 -1 .942 8. .338 0. .00 0. .00 PROA

ATOM 1266 N VAL X 625 -1 .282 -3 .894 9. .271 0. .00 0. .00 PROA

ATOM 1267 HN VAL X 625 -0 .923 -4 .824 9. .245 0. .00 0. .00 PROA

ATOM 1268 CA VAL X 625 -2 .090 -3 .597 10. .461 0. .00 0. .00 PROA

ATOM 1269 HA VAL X 625 -2 .946 -3 .047 10. .099 0. .00 0. .00 PROA

ATOM 1270 CB VAL X 625 -2 .619 -4 .884 11. .150 0. .00 0. .00 PROA

ATOM 1271 HB VAL X 625 -1 .758 -5 .584 11. .093 0. .00 0. .00 PROA

ATOM 1272 CGI VAL X 625 -2 .947 -4 .786 12. .610 0. .00 0. .00 PROA

ATOM 1273 HG11 VAL X 625 -2 .063 -4 .613 13. .261 0. .00 0. .00 PROA

ATOM 1274 HG12 VAL X 625 -3 .328 -5 .771 12. .956 0. .00 0. .00 PROA

ATOM 1275 HG13 VAL X 625 -3 .661 -3 .956 12. .798 0. .00 0. .00 PROA

ATOM 1276 CG2 VAL X 625 -3 .903 -5 .454 10. .360 0. .00 0. .00 PROA

ATOM 1277 HG21 VAL X 625 -3 .653 -5 .622 9. .291 0. .00 0. .00 PROA

ATOM 1278 HG22 VAL X 625 -4 .764 -4 .753 10. .319 0. .00 0. .00 PROA

ATOM 1279 HG23 VAL X 625 -4 .378 -6 .323 10. .863 0. .00 0. .00 PROA

ATOM 1280 C VAL X 625 -1 .239 -2 .783 11. .414 0. .00 0. .00 PROA

ATOM 1281 O VAL X 625 -0 .191 -3 .275 11. .886 0. .00 0. .00 PROA

ATOM 1282 N GLY X 626 -1 .783 -1 .595 11. .827 0. .00 0. .00 PROA

ATOM 1283 HN GLY X 626 -2 .534 -1 .203 11. .303 0. .00 0. .00 PROA

ATOM 1284 CA GLY X 626 -1 .239 -0 .809 12. .958 0. .00 0. .00 PROA

ATOM 1285 HA1 GLY X 626 -1 .636 0 .191 13. .046 0. .00 0. .00 PROA

ATOM 1286 HA2 GLY X 626 -0 .162 -0 .867 12. .900 0. .00 0. .00 PROA

ATOM 1287 C GLY X 626 -1 .630 -1 .370 14. .242 0. .00 0. .00 PROA

ATOM 1288 O GLY X 626 -2 .771 -1 .548 14. .544 0. .00 0. .00 PROA

ATOM 1289 N PHE X 627 -0 .639 -1 .611 15. .063 0. .00 0. .00 PROA

ATOM 1290 HN PHE X 627 0. .304 -1 .561 14. .744 0. .00 0. .00 PROA

ATOM 1291 CA PHE X 627 -0 .895 -2 .424 16. .251 0. .00 0. .00 PROA

ATOM 1292 HA PHE X 627 -1 .940 -2 .330 16. .505 0. .00 0. .00 PROA

ATOM 1293 CB PHE X 627 -0 .268 -3 .859 16. .097 0. .00 0. .00 PROA

ATOM 1294 HB1 PHE X 627 0 .832 -3 .882 16. .251 0. .00 0. .00 PROA

ATOM 1295 HB2 PHE X 627 -0 .590 -4 .103 15. .062 0. .00 0. .00 PROA

ATOM 1296 CG PHE X 627 -0 .938 -4 .963 16. .999 0. .00 0. .00 PROA

ATOM 1297 CD1 PHE X 627 -2 .352 -5 .026 16. .978 0. .00 0. .00 PROA

ATOM 1298 HD1 PHE X 627 -2 .904 -4 .307 16. .390 0. .00 0. .00 PROA

ATOM 1299 CE1 PHE X 627 -3 .006 -6 .144 17. .570 0. .00 0. .00 PROA

ATOM 1300 HE1 PHE X 627 -4 .080 -6 .220 17. .656 0. .00 0. .00 PROA

ATOM 1301 CZ PHE X 627 -2 .265 -6 .975 18. .411 0. .00 0. .00 PROA

ATOM 1302 HZ PHE X 627 -2 .728 -7 .765 18. .983 0. .00 0. .00 PROA

ATOM 1303 CD2 PHE X 627 -0 .187 -5 .870 17. .785 0. .00 0. .00 PROA

ATOM 1304 HD2 PHE X 627 0 .877 -5 .891 17. .601 0. .00 0. .00 PROA

ATOM 1305 CE2 PHE X 627 -0 .886 -6 .914 18. .438 0. .00 0. .00 PROA

ATOM 1306 HE2 PHE X 627 -0 .286 -7 .635 18. .972 0. .00 0. .00 PROA

ATOM 1307 C PHE X 627 -0 .305 -1 .700 17. .431 0. .00 0. .00 PROA

ATOM 1308 O PHE X 627 -0 .811 -1 .777 18. .536 0. .00 0. .00 PROA

ATOM 1309 N GLY X 628 0. .795 -0 .999 17. .330 0. .00 0. .00 PROA

ATOM 1310 HN GLY X 628 1. .213 -0 .934 16. .427 0. .00 0. .00 PROA

ATOM 1311 CA GLY X 628 1. .403 -0 .308 18. .450 0. .00 0. .00 PROA

ATOM 1312 HA1 GLY X 628 0 .664 0 .334 18. .907 0. .00 0. .00 PROA

ATOM 1313 HA2 GLY X 628 2 .168 0 .256 17. .938 0. .00 0. .00 PROA

ATOM 1314 C GLY X 628 2. .119 -1 .077 19. .490 0. .00 0. .00 PROA

ATOM 1315 O GLY X 628 2. .311 -0 .659 20. .583 0. .00 0. .00 PROA

ATOM 1316 N ASN X 629 2. .474 -2 .285 19. .148 0. .00 0. .00 PROA

ATOM 1317 HN ASN X 629 2. .473 -2 .570 18. .192 0. .00 0. .00 PROA

ATOM 1318 CA ASN X 629 2. .861 -3 .247 20. .173 0. .00 0. .00 PROA

ATOM 1319 HA ASN X 629 3. .591 -2 .739 20. .786 0. .00 0. .00 PROA ATOM 1320 CB ASN X 629 1..644 -3.873 20..874 0..00 0..00 PROA

ATOM 1321 HB1 ASN X 629 1 .499 -4 .898 20. .471 0. .00 0. .00 PROA

ATOM 1322 HB2 ASN X 629 0 .805 -3 .263 20. .476 0. .00 0. .00 PROA

ATOM 1323 CG ASN X 629 1. .618 -3 .839 22. .406 0. .00 0. .00 PROA

ATOM 1324 OD1 ASN X 629 2 .639 -3 .545 23. .000 0. .00 0. .00 PROA

ATOM 1325 ND2 ASN X 629 0 .419 -3 .974 22. .975 0. .00 0. .00 PROA

ATOM 1326 HD21 ASN X 629 0 .287 -3 .740 23. .939 0. .00 0. .00 PROA

ATOM 1327 HD22 ASN X 629 -0 .334 -4 .499 22. .581 0. .00 0. .00 PROA

ATOM 1328 C ASN X 629 3. .729 -4 .218 19. .430 0. .00 0. .00 PROA

ATOM 1329 O ASN X 629 3. .650 -4 .246 18. .227 0. .00 0. .00 PROA

ATOM 1330 N VAL X 630 4. .590 -4 .870 20. .208 0. .00 0. .00 PROA

ATOM 1331 HN VAL X 630 4. .654 -4 .650 21. .179 0. .00 0. .00 PROA

ATOM 1332 CA VAL X 630 5. .526 -5 .887 19. .748 0. .00 0. .00 PROA

ATOM 1333 HA VAL X 630 5. .809 -6 .378 20. .668 0. .00 0. .00 PROA

ATOM 1334 CB VAL X 630 4. .928 -7 .066 18. .951 0. .00 0. .00 PROA

ATOM 1335 HB VAL X 630 4. .533 -6 .772 17. .955 0. .00 0. .00 PROA

ATOM 1336 CGI VAL X 630 5 .979 -8 .235 18. .877 0. .00 0. .00 PROA

ATOM 1337 HG11 VAL X 630 6 .818 -7 .877 18. .242 0. .00 0. .00 PROA

ATOM 1338 HG12 VAL X 630 5 .569 -9 .224 18. .579 0. .00 0. .00 PROA

ATOM 1339 HG13 VAL X 630 6 .432 -8 .206 19. .891 0. .00 0. .00 PROA

ATOM 1340 CG2 VAL X 630 3 .704 -7 .544 19. .749 0. .00 0. .00 PROA

ATOM 1341 HG21 VAL X 630 3 .303 -8 .534 19. .443 0. .00 0. .00 PROA

ATOM 1342 HG22 VAL X 630 2 .827 -6 .863 19. .704 0. .00 0. .00 PROA

ATOM 1343 HG23 VAL X 630 3 .906 -7 .616 20. .839 0. .00 0. .00 PROA

ATOM 1344 C VAL X 630 6. .732 -5 .270 19. .110 0. .00 0. .00 PROA

ATOM 1345 O VAL X 630 6. .780 -4 .592 18. .093 0. .00 0. .00 PROA

ATOM 1346 N SER X 631 7. .915 -5 .527 19. .612 0. .00 0. .00 PROA

ATOM 1347 HN SER X 631 7. .933 -5 .953 20. .513 0. .00 0. .00 PROA

ATOM 1348 CA SER X 631 9. .172 -5 .126 19. .049 0. .00 0. .00 PROA

ATOM 1349 HA SER X 631 9. .019 -4 .761 18. .045 0. .00 0. .00 PROA

ATOM 1350 CB SER X 631 9. .827 -3 .881 19. .808 0. .00 0. .00 PROA

ATOM 1351 HB1 SER X 631 9 .824 -4 .026 20. .910 0. .00 0. .00 PROA

ATOM 1352 HB2 SER X 631 9 .160 -2 .992 19. .828 0. .00 0. .00 PROA

ATOM 1353 OG SER X 631 11 .059 -3 .499 19. .298 0. .00 0. .00 PROA

ATOM 1354 HG1 SER X 631 11 .059 -2 .548 19. .431 0. .00 0. .00 PROA

ATOM 1355 C SER X 631 10 .131 -6 .281 19. .059 0. .00 0. .00 PROA

ATOM 1356 O SER X 631 10 .412 -6 .890 20. .130 0. .00 0. .00 PROA

ATOM 1357 N PRO X 632 10 .740 -6 .567 17. .916 0. .00 0. .00 PROA

ATOM 1358 CD PRO X 632 10 .276 -6 .241 16. .579 0. .00 0. .00 PROA

ATOM 1359 HD1 PRO X 632 10 .510 -5 .166 16. .419 0. .00 0. .00 PROA

ATOM 1360 HD2 PRO X 632 9 .173 -6 .315 16. .476 0. .00 0. .00 PROA

ATOM 1361 CA PRO X 632 11 .990 -7 .407 17. .887 0. .00 0. .00 PROA

ATOM 1362 HA PRO X 632 11 .632 -8 .369 18. .225 0. .00 0. .00 PROA

ATOM 1363 CB PRO X 632 12 .407 -7 .337 16. .406 0. .00 0. .00 PROA

ATOM 1364 HB1 PRO X 632 12 .997 -8 .205 16. .040 0. .00 0. .00 PROA

ATOM 1365 HB2 PRO X 632 13 .049 -6 .431 16. .407 0. .00 0. .00 PROA

ATOM 1366 CG PRO X 632 11 .122 -7 .106 15. .675 0. .00 0. .00 PROA

ATOM 1367 HG1 PRO X 632 11 .168 -6 .751 14. .623 0. .00 0. .00 PROA

ATOM 1368 HG2 PRO X 632 10 .716 -8 .135 15. .572 0. .00 0. .00 PROA

ATOM 1369 C PRO X 632 12 .998 -6 .823 18. .843 0. .00 0. .00 PROA

ATOM 1370 O PRO X 632 13 .054 -5 .564 18. .930 0. .00 0. .00 PROA

ATOM 1371 N ASN X 633 13 .784 -7 .610 19. .538 0. .00 0. .00 PROA

ATOM 1372 HN ASN X 633 13 .703 -8 .600 19. .627 0. .00 0. .00 PROA

ATOM 1373 CA ASN X 633 14 .655 -7 .037 20. .579 0. .00 0. .00 PROA

ATOM 1374 HA ASN X 633 14 .022 -6 .342 21. . Ill 0. .00 0. .00 PROA

ATOM 1375 CB ASN X 633 15 .125 -8 .343 21. .388 0. .00 0. .00 PROA

ATOM 1376 HB1 ASN X 633 15 .938 -8 .000 22. .062 0. .00 0. .00 PROA

ATOM 1377 HB2 ASN X 633 15 .485 -9 .104 20. .663 0. .00 0. .00 PROA

ATOM 1378 CG ASN X 633 14 .067 -8 .939 22. .356 0. .00 0. .00 PROA

ATOM 1379 OD1 ASN X 633 12 .917 -8 .416 22. .329 0. .00 0. .00 PROA

ATOM 1380 ND2 ASN X 633 14 .394 -9 .821 23. .316 0. .00 0. .00 PROA

ATOM 1381 HD21 ASN X 633 13 .771 -10 .121 24. .038 0. .00 0. .00 PROA

ATOM 1382 HD22 ASN X 633 15 .344 -10 .126 23. .380 0. .00 0. .00 PROA

ATOM 1383 C ASN X 633 15 .912 -6 .344 20. .087 0. .00 0. .00 PROA

ATOM 1384 O ASN X 633 16 .054 -5 .161 20. .241 0. .00 0. .00 PROA

ATOM 1385 N THR X 634 16 .857 -7 .135 19. .569 0. .00 0. .00 PROA ATOM 1386 HN THR X 634 16.603 -8.048 19..259 0..00 0..00 PROA

ATOM 1387 CA THR X 634 18 .285 -6 .780 19. .339 0. .00 0. .00 PROA

ATOM 1388 HA THR X 634 18 .508 -6 .091 20. .140 0. .00 0. .00 PROA

ATOM 1389 CB THR X 634 19 .394 -7 .903 19. .298 0. .00 0. .00 PROA

ATOM 1390 HB THR X 634 20 .404 -7 .469 19. .142 0. .00 0. .00 PROA

ATOM 1391 OG1 THR X 634 19 .141 -8 .847 18. .325 0. .00 0. .00 PROA

ATOM 1392 HG1 THR X 634 18 .287 -9 .203 18. .581 0. .00 0. .00 PROA

ATOM 1393 CG2 THR X 634 19 .479 -8 .608 20. .659 0. .00 0. .00 PROA

ATOM 1394 HG21 THR X 634 18 .819 -9 .479 20. .859 0. .00 0. .00 PROA

ATOM 1395 HG22 THR X 634 19 .518 -7 .926 21. .535 0. .00 0. .00 PROA

ATOM 1396 HG23 THR X 634 20 .465 -9 .108 20. .550 0. .00 0. .00 PROA

ATOM 1397 C THR X 634 18 .428 -5 .892 18. .151 0. .00 0. .00 PROA

ATOM 1398 O THR X 634 17 .575 -5 .731 17. .242 0. .00 0. .00 PROA

ATOM 1399 N ASN X 635 19 .623 -5 .202 18. .005 0. .00 0. .00 PROA

ATOM 1400 HN ASN X 635 20 .178 -5 .154 18. .831 0. .00 0. .00 PROA

ATOM 1401 CA ASN X 635 20 .053 -4 .427 16. .893 0. .00 0. .00 PROA

ATOM 1402 HA ASN X 635 19 .217 -3 .751 16. .791 0. .00 0. .00 PROA

ATOM 1403 CB ASN X 635 21 .481 -3 .884 17. .152 0. .00 0. .00 PROA

ATOM 1404 HB1 ASN X 635 21 .822 -3 .275 16. .288 0. .00 0. .00 PROA

ATOM 1405 HB2 ASN X 635 22 .235 -4 .700 17. .146 0. .00 0. .00 PROA

ATOM 1406 CG ASN X 635 21 .605 -2 .954 18. .322 0. .00 0. .00 PROA

ATOM 1407 OD1 ASN X 635 20 .606 -2 .467 18. .855 0. .00 0. .00 PROA

ATOM 1408 ND2 ASN X 635 22 .847 -2 .780 18. .792 0. .00 0. .00 PROA

ATOM 1409 HD21 ASN X 635 22 .863 -2 .359 19. .699 0. .00 0. .00 PROA

ATOM 1410 HD22 ASN X 635 23 .668 -3 .195 18. .399 0. .00 0. .00 PROA

ATOM 1411 C ASN X 635 19 .977 -5 .194 15. .574 0. .00 0. .00 PROA

ATOM 1412 O ASN X 635 19 .421 -4 .675 14. .549 0. .00 0. .00 PROA

ATOM 1413 N SER X 636 20 .470 -6 .430 15. .637 0. .00 0. .00 PROA

ATOM 1414 HN SER X 636 21 .005 -6 .609 16. .459 0. .00 0. .00 PROA

ATOM 1415 CA SER X 636 20 .390 -7 .542 14. .637 0. .00 0. .00 PROA

ATOM 1416 HA SER X 636 20 .833 -7 .291 13. .685 0. .00 0. .00 PROA

ATOM 1417 CB SER X 636 21 .071 -8 .768 15. .281 0. .00 0. .00 PROA

ATOM 1418 HB1 SER X 636 20 .557 -8 .883 16. .259 0. .00 0. .00 PROA

ATOM 1419 HB2 SER X 636 22 .164 -8 .637 15. .431 0. .00 0. .00 PROA

ATOM 1420 OG SER X 636 20 .832 -9 .966 14. .470 0. .00 0. .00 PROA

ATOM 1421 HG1 SER X 636 21 .599 -10 .014 13. .895 0. .00 0. .00 PROA

ATOM 1422 C SER X 636 18 .998 -7 .898 14. .180 0. .00 0. .00 PROA

ATOM 1423 O SER X 636 18 .783 -7 .771 12. .998 0. .00 0. .00 PROA

ATOM 1424 N GLU X 637 18 .040 -8 .082 15. .138 0. .00 0. .00 PROA

ATOM 1425 HN GLU X 637 18 .226 -7 .714 16. .045 0. .00 0. .00 PROA

ATOM 1426 CA GLU X 637 16 .608 -8 .372 14. .784 0. .00 0. .00 PROA

ATOM 1427 HA GLU X 637 16 .581 -9 .133 14. .018 0. .00 0. .00 PROA

ATOM 1428 CB GLU X 637 15 .880 -9 .023 16. .009 0. .00 0. .00 PROA

ATOM 1429 HB1 GLU X 637 14 .822 -9 .216 15. .733 0. .00 0. .00 PROA

ATOM 1430 HB2 GLU X 637 15 .885 -8 .262 16. .819 0. .00 0. .00 PROA

ATOM 1431 CG GLU X 637 16 .479 -10 .346 16. .458 0. .00 0. .00 PROA

ATOM 1432 HG1 GLU X 637 17 .590 -10 .361 16. .455 0. .00 0. .00 PROA

ATOM 1433 HG2 GLU X 637 16 .003 -11 .124 15. .823 0. .00 0. .00 PROA

ATOM 1434 CD GLU X 637 16 .118 -10 .595 17. .932 0. .00 0. .00 PROA

ATOM 1435 OE1 GLU X 637 15 .420 -11 .583 18. .287 0. .00 0. .00 PROA

ATOM 1436 OE2 GLU X 637 16 .581 -9 .780 18. .773 0. .00 0. .00 PROA

ATOM 1437 C GLU X 637 15 .768 -7 .208 14. .211 0. .00 0. .00 PROA

ATOM 1438 O GLU X 637 14 .957 -7 .333 13. .330 0. .00 0. .00 PROA

ATOM 1439 N LYS X 638 16 .087 -5 .990 14. .744 0. .00 0. .00 PROA

ATOM 1440 HN LYS X 638 16 .545 -5 .876 15. .622 0. .00 0. .00 PROA

ATOM 1441 CA LYS X 638 15 .441 -4 .734 14. .363 0. .00 0. .00 PROA

ATOM 1442 HA LYS X 638 14 .369 -4 .861 14. .395 0. .00 0. .00 PROA

ATOM 1443 CB LYS X 638 15 .646 -3 .608 15. .383 0. .00 0. .00 PROA

ATOM 1444 HB1 LYS X 638 15 .462 -2 .672 14. .813 0. .00 0. .00 PROA

ATOM 1445 HB2 LYS X 638 16 .737 -3 .525 15. .579 0. .00 0. .00 PROA

ATOM 1446 CG LYS X 638 14 .785 -3 .706 16. .618 0. .00 0. .00 PROA

ATOM 1447 HG1 LYS X 638 15 .340 -4 .425 17. .258 0. .00 0. .00 PROA

ATOM 1448 HG2 LYS X 638 13 .750 -4 .078 16. .458 0. .00 0. .00 PROA

ATOM 1449 CD LYS X 638 14 .771 -2 .287 17. .359 0. .00 0. .00 PROA

ATOM 1450 HD1 LYS X 638 14 .413 -1 .460 16. .709 0. .00 0. .00 PROA

ATOM 1451 HD2 LYS X 638 15 .849 -2 .185 17. .606 0. .00 0. .00 PROA ATOM 1452 CE LYS X 638 13.818 -2.131 18..574 0..00 0..00 PROA

ATOM 1453 HE1 LYS X 638 12 .734 -2 .099 18. .333 0. .00 0. .00 PROA

ATOM 1454 HE2 LYS X 638 14 .040 -1 .179 19. .102 0. .00 0. .00 PROA

ATOM 1455 NZ LYS X 638 14 .059 -3 .217 19. .567 0. .00 0. .00 PROA

ATOM 1456 HZ1 LYS X 638 13 .544 -4 .044 19. .206 0. .00 0. .00 PROA

ATOM 1457 HZ2 LYS X 638 13 .655 -2 .820 20. .439 0. .00 0. .00 PROA

ATOM 1458 HZ3 LYS X 638 15 .061 -3 .439 19. .736 0. .00 0. .00 PROA

ATOM 1459 C LYS X 638 15 .825 -4 .296 12. .963 0. .00 0. .00 PROA

ATOM 1460 O LYS X 638 14 .918 -3 .938 12. .213 0. .00 0. .00 PROA

ATOM 1461 N ILE X 639 17 .068 -4 .475 12. .480 0. .00 0. .00 PROA

ATOM 1462 HN ILE X 639 17 .809 -4 .743 13. .090 0. .00 0. .00 PROA

ATOM 1463 CA ILE X 639 17 .363 -4 .551 11. .029 0. .00 0. .00 PROA

ATOM 1464 HA ILE X 639 17 .039 -3 .625 10. .578 0. .00 0. .00 PROA

ATOM 1465 CB ILE X 639 18 .868 -4 .414 10. .922 0. .00 0. .00 PROA

ATOM 1466 HB ILE X 639 19 .325 -5 .165 11. .602 0. .00 0. .00 PROA

ATOM 1467 CG2 ILE X 639 19 .369 -4 .552 9. .470 0. .00 0. .00 PROA

ATOM 1468 HG21 ILE X 639 18 .813 -3 .941 8. .727 0. .00 0. .00 PROA

ATOM 1469 HG22 ILE X 639 19 .205 -5 .599 9. .135 0. .00 0. .00 PROA

ATOM 1470 HG23 ILE X 639 20 .466 -4 .383 9. .415 0. .00 0. .00 PROA

ATOM 1471 CGI ILE X 639 19 .253 -3 .065 11. .521 0. .00 0. .00 PROA

ATOM 1472 HG11 ILE X 639 18 .617 -2 .810 12. .395 0. .00 0. .00 PROA

ATOM 1473 HG12 ILE X 639 18 .903 -2 .251 10. .850 0. .00 0. .00 PROA

ATOM 1474 CD ILE X 639 20 .763 -2 .819 11. .757 0. .00 0. .00 PROA

ATOM 1475 HD1 ILE X 639 20 .867 -1 .883 12. .347 0. .00 0. .00 PROA

ATOM 1476 HD2 ILE X 639 21 .240 -2 .739 10. .757 0. .00 0. .00 PROA

ATOM 1477 HD3 ILE X 639 21 .249 -3 .666 12. .287 0. .00 0. .00 PROA

ATOM 1478 C ILE X 639 16 .720 -5 .730 10. .236 0. .00 0. .00 PROA

ATOM 1479 O ILE X 639 16 .078 -5 .528 9. .222 0. .00 0. .00 PROA

ATOM 1480 N PHE X 640 17 .050 -6 .936 10. .667 0. .00 0. .00 PROA

ATOM 1481 HN PHE X 640 17 .851 -6 .993 11. .257 0. .00 0. .00 PROA

ATOM 1482 CA PHE X 640 16 .647 -8 .210 10. .057 0. .00 0. .00 PROA

ATOM 1483 HA PHE X 640 17 .106 -8 .181 9. .080 0. .00 0. .00 PROA

ATOM 1484 CB PHE X 640 17 .280 -9 .436 10. .864 0. .00 0. .00 PROA

ATOM 1485 HB1 PHE X 640 17 .113 -9 .462 11. .962 0. .00 0. .00 PROA

ATOM 1486 HB2 PHE X 640 18 .362 -9 .189 10. .900 0. .00 0. .00 PROA

ATOM 1487 CG PHE X 640 16 .969 -10 .788 10. .178 0. .00 0. .00 PROA

ATOM 1488 CD1 PHE X 640 17 .283 -10 .933 8. .823 0. .00 0. .00 PROA

ATOM 1489 HD1 PHE X 640 17 .569 -10 .050 8. .272 0. .00 0. .00 PROA

ATOM 1490 CE1 PHE X 640 17 .067 -12 .091 8. .180 0. .00 0. .00 PROA

ATOM 1491 HE1 PHE X 640 17 .377 -12 .154 7. .147 0. .00 0. .00 PROA

ATOM 1492 CZ PHE X 640 16 .639 -13 .248 8. .820 0. .00 0. .00 PROA

ATOM 1493 HZ PHE X 640 16 .628 -14 .244 8. .402 0. .00 0. .00 PROA

ATOM 1494 CD2 PHE X 640 16 .582 -11 .977 10. .856 0. .00 0. .00 PROA

ATOM 1495 HD2 PHE X 640 16 .353 -11 .890 11. .908 0. .00 0. .00 PROA

ATOM 1496 CE2 PHE X 640 16 .302 -13 .143 10. .202 0. .00 0. .00 PROA

ATOM 1497 HE2 PHE X 640 15 .943 -13 .972 10. .794 0. .00 0. .00 PROA

ATOM 1498 C PHE X 640 15 .197 -8 .331 9. .692 0. .00 0. .00 PROA

ATOM 1499 O PHE X 640 14 .937 -8 .745 8. .553 0. .00 0. .00 PROA

ATOM 1500 N SER X 641 14 .284 -8 .002 10. .560 0. .00 0. .00 PROA

ATOM 1501 HN SER X 641 14 .581 -7 .564 11. .406 0. .00 0. .00 PROA

ATOM 1502 CA SER X 641 12 .858 -8 .144 10. .453 0. .00 0. .00 PROA

ATOM 1503 HA SER X 641 12 .630 -9 .133 10. .084 0. .00 0. .00 PROA

ATOM 1504 CB SER X 641 12 .102 -7 .787 11. .770 0. .00 0. .00 PROA

ATOM 1505 HB1 SER X 641 12 .195 -8 .642 12. .473 0. .00 0. .00 PROA

ATOM 1506 HB2 SER X 641 11 .021 -7 .729 11. .520 0. .00 0. .00 PROA

ATOM 1507 OG SER X 641 12 .530 -6 .608 12. .425 0. .00 0. .00 PROA

ATOM 1508 HG1 SER X 641 13 .426 -6 .708 12. .756 0. .00 0. .00 PROA

ATOM 1509 C SER X 641 12 .344 -7 .290 9. .356 0. .00 0. .00 PROA

ATOM 1510 O SER X 641 11 .654 -7 .762 8. .439 0. .00 0. .00 PROA

ATOM 1511 N ILE X 642 12 .702 -6 .016 9. .207 0. .00 0. .00 PROA

ATOM 1512 HN ILE X 642 13 .424 -5 .541 9. .705 0. .00 0. .00 PROA

ATOM 1513 CA ILE X 642 12 .365 -5 .104 8. .115 0. .00 0. .00 PROA

ATOM 1514 HA ILE X 642 11 .352 -5 .353 7. .835 0. .00 0. .00 PROA

ATOM 1515 CB ILE X 642 12 .468 -3 .610 8. .516 0. .00 0. .00 PROA

ATOM 1516 HB ILE X 642 13 .558 -3 .396 8. .550 0. .00 0. .00 PROA

ATOM 1517 CG2 ILE X 642 11 .739 -2 .742 7. .466 0. .00 0. .00 PROA ATOM 1518 HG21 ILE X 642 11.760 -1.694 7..834 0..00 0..00 PROA

ATOM 1519 HG22 ILE X 642 10 .664 -3 .003 7. .368 0. .00 0. .00 PROA

ATOM 1520 HG23 ILE X 642 12 .200 -2 .855 6. .462 0. .00 0. .00 PROA

ATOM 1521 CGI ILE X 642 11 .944 -3 .387 9. .950 0. .00 0. .00 PROA

ATOM 1522 HG11 ILE X 642 12 .661 -3 .959 10. .577 0. .00 0. .00 PROA<