CNRS Nantes University UFIP UFIP
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***  CATSPEROSOME  ***

elNémo ID: 210812210550120811

Job options:

ID        	=	 210812210550120811
JOBID     	=	 CATSPEROSOME
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER CATSPEROSOME

HEADER    PROTEIN TRANSPORT                       18-MAR-21   7EEB              
TITLE     STRUCTURE OF THE CATSPERMASOME                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENHANCED GREEN FLUORESCENT PROTEIN,CATION CHANNEL SPERM-   
COMPND   3 ASSOCIATED PROTEIN 1;                                                
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: CATSPER1;                                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CATION CHANNEL SPERM-ASSOCIATED PROTEIN 2;                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: CATSPER2;                                                   
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: CATION CHANNEL SPERM-ASSOCIATED PROTEIN 3;                 
COMPND  13 CHAIN: C;                                                            
COMPND  14 SYNONYM: CATSPER3;                                                   
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: CATION CHANNEL SPERM-ASSOCIATED PROTEIN 4;                 
COMPND  17 CHAIN: D;                                                            
COMPND  18 SYNONYM: CATSPER4;                                                   
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: CATION CHANNEL SPERM-ASSOCIATED PROTEIN SUBUNIT BETA;      
COMPND  21 CHAIN: E;                                                            
COMPND  22 SYNONYM: CATSPER-BETA;                                               
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: CATION CHANNEL SPERM-ASSOCIATED PROTEIN SUBUNIT GAMMA 2;   
COMPND  25 CHAIN: F;                                                            
COMPND  26 MOL_ID: 7;                                                           
COMPND  27 MOLECULE: CATION CHANNEL SPERM-ASSOCIATED PROTEIN SUBUNIT DELTA;     
COMPND  28 CHAIN: G;                                                            
COMPND  29 SYNONYM: CATSPER-DELTA,CATSPERDELTA,TRANSMEMBRANE PROTEIN 146;       
COMPND  30 MOL_ID: 8;                                                           
COMPND  31 MOLECULE: CATION CHANNEL SPERM-ASSOCIATED PROTEIN SUBUNIT EPSILON;   
COMPND  32 CHAIN: H;                                                            
COMPND  33 SYNONYM: CATSPER-EPSILON,CATSPEREPSILON,C1ORF101-LIKE PROTEIN;       
COMPND  34 MOL_ID: 9;                                                           
COMPND  35 MOLECULE: KAZAL-LIKE DOMAIN-CONTAINING PROTEIN;                      
COMPND  36 CHAIN: L;                                                            
COMPND  37 MOL_ID: 10;                                                          
COMPND  38 MOLECULE: TRANSMEMBRANE PROTEIN 249;                                 
COMPND  39 CHAIN: J;                                                            
COMPND  40 MOL_ID: 11;                                                          
COMPND  41 MOLECULE: TRANSMEMBRANE PROTEIN 262;                                 
COMPND  42 CHAIN: M;                                                            
COMPND  43 MOL_ID: 12;                                                          
COMPND  44 MOLECULE: UNKNOWN;                                                   
COMPND  45 CHAIN: N;                                                            
COMPND  46 MOL_ID: 13;                                                          
COMPND  47 MOLECULE: EF-HAND CALCIUM-BINDING DOMAIN-CONTAINING PROTEIN 9;       
COMPND  48 CHAIN: I;                                                            
COMPND  49 MOL_ID: 14;                                                          
COMPND  50 MOLECULE: CATION CHANNEL SPERM-ASSOCIATED PROTEIN SUBUNIT ZETA;      
COMPND  51 CHAIN: K;                                                            
COMPND  52 SYNONYM: CATSPER-ZETA,CATSPERZETA,PROTEIN EXPRESSED IN MALE LEPTOTENE
COMPND  53 AND ZYGOTENE SPERMATOCYTES 622,MLZ-622,TESTIS-EXPRESSED PROTEIN 40   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN CYTOMEGALOVIRUS, MUS MUSCULUS;            
SOURCE   3 ORGANISM_COMMON: HHV-5, HUMAN HERPESVIRUS 5, MOUSE;                  
SOURCE   4 ORGANISM_TAXID: 10359, 10090;                                        
SOURCE   5 GENE: EGFP, CATSPER1;                                                
SOURCE   6 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  14 ORGANISM_COMMON: MOUSE;                                              
SOURCE  15 ORGANISM_TAXID: 10090;                                               
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  18 ORGANISM_COMMON: MOUSE;                                              
SOURCE  19 ORGANISM_TAXID: 10090;                                               
SOURCE  20 MOL_ID: 5;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  22 ORGANISM_COMMON: MOUSE;                                              
SOURCE  23 ORGANISM_TAXID: 10090;                                               
SOURCE  24 MOL_ID: 6;                                                           
SOURCE  25 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  26 ORGANISM_COMMON: MOUSE;                                              
SOURCE  27 ORGANISM_TAXID: 10090;                                               
SOURCE  28 MOL_ID: 7;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  30 ORGANISM_COMMON: MOUSE;                                              
SOURCE  31 ORGANISM_TAXID: 10090;                                               
SOURCE  32 MOL_ID: 8;                                                           
SOURCE  33 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  34 ORGANISM_COMMON: MOUSE;                                              
SOURCE  35 ORGANISM_TAXID: 10090;                                               
SOURCE  36 MOL_ID: 9;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  38 ORGANISM_COMMON: MOUSE;                                              
SOURCE  39 ORGANISM_TAXID: 10090;                                               
SOURCE  40 MOL_ID: 10;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  42 ORGANISM_COMMON: MOUSE;                                              
SOURCE  43 ORGANISM_TAXID: 10090;                                               
SOURCE  44 MOL_ID: 11;                                                          
SOURCE  45 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  46 ORGANISM_COMMON: MOUSE;                                              
SOURCE  47 ORGANISM_TAXID: 10090;                                               
SOURCE  48 MOL_ID: 12;                                                          
SOURCE  49 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  50 ORGANISM_COMMON: MOUSE;                                              
SOURCE  51 ORGANISM_TAXID: 10090;                                               
SOURCE  52 MOL_ID: 13;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  54 ORGANISM_COMMON: MOUSE;                                              
SOURCE  55 ORGANISM_TAXID: 10090;                                               
SOURCE  56 MOL_ID: 14;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  58 ORGANISM_COMMON: MOUSE;                                              
SOURCE  59 ORGANISM_TAXID: 10090                                                
KEYWDS    ION CHANNEL, MEMBRANE PROTEIN, CALCIUM CHANNEL, PROTEIN COMPLEX,      
KEYWDS   2 PROTEIN TRANSPORT                                                    
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.P.WU,M.KE                                                           
REVDAT   2   11-AUG-21 7EEB    1       JRNL                                     
REVDAT   1   28-JUL-21 7EEB    0                                                
JRNL        AUTH   S.LIN,M.KE,Y.ZHANG,Z.YAN,J.WU                                
JRNL        TITL   STRUCTURE OF A MAMMALIAN SPERM CATION CHANNEL COMPLEX.       
JRNL        REF    NATURE                        V. 595   746 2021              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   34225353                                                     
JRNL        DOI    10.1038/S41586-021-03742-6                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : CRYOSPARC                                 
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 2.900                          
REMARK   3   NUMBER OF PARTICLES               : 560730                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 7EEB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300021220.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : MOUSE CATSPERMASOME               
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOT FOR 8 S BEFORE PLUNGING      
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K3 (6K X 4K)             
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 5000.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 81000                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRADECAMERIC                    
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, L, J,         
REMARK 350                    AND CHAINS: M, N, I, K, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X, Y, Z, a, b, c,         
REMARK 350                    AND CHAINS: d                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A  -268                                                      
REMARK 465     TYR A  -267                                                      
REMARK 465     LYS A  -266                                                      
REMARK 465     ASP A  -265                                                      
REMARK 465     HIS A  -264                                                      
REMARK 465     ASP A  -263                                                      
REMARK 465     GLY A  -262                                                      
REMARK 465     ASP A  -261                                                      
REMARK 465     TYR A  -260                                                      
REMARK 465     LYS A  -259                                                      
REMARK 465     ASP A  -258                                                      
REMARK 465     HIS A  -257                                                      
REMARK 465     ASP A  -256                                                      
REMARK 465     ILE A  -255                                                      
REMARK 465     ASP A  -254                                                      
REMARK 465     TYR A  -253                                                      
REMARK 465     LYS A  -252                                                      
REMARK 465     ASP A  -251                                                      
REMARK 465     ASP A  -250                                                      
REMARK 465     ASP A  -249                                                      
REMARK 465     ASP A  -248                                                      
REMARK 465     LYS A  -247                                                      
REMARK 465     MET A  -246                                                      
REMARK 465     VAL A  -245                                                      
REMARK 465     SER A  -244                                                      
REMARK 465     LYS A  -243                                                      
REMARK 465     GLY A  -242                                                      
REMARK 465     GLU A  -241                                                      
REMARK 465     GLU A  -240                                                      
REMARK 465     LEU A  -239                                                      
REMARK 465     PHE A  -238                                                      
REMARK 465     THR A  -237                                                      
REMARK 465     GLY A  -236                                                      
REMARK 465     VAL A  -235                                                      
REMARK 465     VAL A  -234                                                      
REMARK 465     PRO A  -233                                                      
REMARK 465     ILE A  -232                                                      
REMARK 465     LEU A  -231                                                      
REMARK 465     VAL A  -230                                                      
REMARK 465     GLU A  -229                                                      
REMARK 465     LEU A  -228                                                      
REMARK 465     ASP A  -227                                                      
REMARK 465     GLY A  -226                                                      
REMARK 465     ASP A  -225                                                      
REMARK 465     VAL A  -224                                                      
REMARK 465     ASN A  -223                                                      
REMARK 465     GLY A  -222                                                      
REMARK 465     HIS A  -221                                                      
REMARK 465     LYS A  -220                                                      
REMARK 465     PHE A  -219                                                      
REMARK 465     SER A  -218                                                      
REMARK 465     VAL A  -217                                                      
REMARK 465     SER A  -216                                                      
REMARK 465     GLY A  -215                                                      
REMARK 465     GLU A  -214                                                      
REMARK 465     GLY A  -213                                                      
REMARK 465     GLU A  -212                                                      
REMARK 465     GLY A  -211                                                      
REMARK 465     ASP A  -210                                                      
REMARK 465     ALA A  -209                                                      
REMARK 465     THR A  -208                                                      
REMARK 465     TYR A  -207                                                      
REMARK 465     GLY A  -206                                                      
REMARK 465     LYS A  -205                                                      
REMARK 465     LEU A  -204                                                      
REMARK 465     THR A  -203                                                      
REMARK 465     LEU A  -202                                                      
REMARK 465     LYS A  -201                                                      
REMARK 465     PHE A  -200                                                      
REMARK 465     ILE A  -199                                                      
REMARK 465     CYS A  -198                                                      
REMARK 465     THR A  -197                                                      
REMARK 465     THR A  -196                                                      
REMARK 465     GLY A  -195                                                      
REMARK 465     LYS A  -194                                                      
REMARK 465     LEU A  -193                                                      
REMARK 465     PRO A  -192                                                      
REMARK 465     VAL A  -191                                                      
REMARK 465     PRO A  -190                                                      
REMARK 465     TRP A  -189                                                      
REMARK 465     PRO A  -188                                                      
REMARK 465     THR A  -187                                                      
REMARK 465     LEU A  -186                                                      
REMARK 465     VAL A  -185                                                      
REMARK 465     THR A  -184                                                      
REMARK 465     THR A  -183                                                      
REMARK 465     LEU A  -182                                                      
REMARK 465     THR A  -181                                                      
REMARK 465     TYR A  -180                                                      
REMARK 465     GLY A  -179                                                      
REMARK 465     VAL A  -178                                                      
REMARK 465     GLN A  -177                                                      
REMARK 465     CYS A  -176                                                      
REMARK 465     PHE A  -175                                                      
REMARK 465     SER A  -174                                                      
REMARK 465     ARG A  -173                                                      
REMARK 465     TYR A  -172                                                      
REMARK 465     PRO A  -171                                                      
REMARK 465     ASP A  -170                                                      
REMARK 465     HIS A  -169                                                      
REMARK 465     MET A  -168                                                      
REMARK 465     LYS A  -167                                                      
REMARK 465     GLN A  -166                                                      
REMARK 465     HIS A  -165                                                      
REMARK 465     ASP A  -164                                                      
REMARK 465     PHE A  -163                                                      
REMARK 465     PHE A  -162                                                      
REMARK 465     LYS A  -161                                                      
REMARK 465     SER A  -160                                                      
REMARK 465     ALA A  -159                                                      
REMARK 465     MET A  -158                                                      
REMARK 465     PRO A  -157                                                      
REMARK 465     GLU A  -156                                                      
REMARK 465     GLY A  -155                                                      
REMARK 465     TYR A  -154                                                      
REMARK 465     VAL A  -153                                                      
REMARK 465     GLN A  -152                                                      
REMARK 465     GLU A  -151                                                      
REMARK 465     ARG A  -150                                                      
REMARK 465     THR A  -149                                                      
REMARK 465     ILE A  -148                                                      
REMARK 465     PHE A  -147                                                      
REMARK 465     PHE A  -146                                                      
REMARK 465     LYS A  -145                                                      
REMARK 465     ASP A  -144                                                      
REMARK 465     ASP A  -143                                                      
REMARK 465     GLY A  -142                                                      
REMARK 465     ASN A  -141                                                      
REMARK 465     TYR A  -140                                                      
REMARK 465     LYS A  -139                                                      
REMARK 465     THR A  -138                                                      
REMARK 465     ARG A  -137                                                      
REMARK 465     ALA A  -136                                                      
REMARK 465     GLU A  -135                                                      
REMARK 465     VAL A  -134                                                      
REMARK 465     LYS A  -133                                                      
REMARK 465     PHE A  -132                                                      
REMARK 465     GLU A  -131                                                      
REMARK 465     GLY A  -130                                                      
REMARK 465     ASP A  -129                                                      
REMARK 465     THR A  -128                                                      
REMARK 465     LEU A  -127                                                      
REMARK 465     VAL A  -126                                                      
REMARK 465     ASN A  -125                                                      
REMARK 465     ARG A  -124                                                      
REMARK 465     ILE A  -123                                                      
REMARK 465     GLU A  -122                                                      
REMARK 465     LEU A  -121                                                      
REMARK 465     LYS A  -120                                                      
REMARK 465     GLY A  -119                                                      
REMARK 465     ILE A  -118                                                      
REMARK 465     ASP A  -117                                                      
REMARK 465     PHE A  -116                                                      
REMARK 465     LYS A  -115                                                      
REMARK 465     GLU A  -114                                                      
REMARK 465     ASP A  -113                                                      
REMARK 465     GLY A  -112                                                      
REMARK 465     ASN A  -111                                                      
REMARK 465     ILE A  -110                                                      
REMARK 465     LEU A  -109                                                      
REMARK 465     GLY A  -108                                                      
REMARK 465     HIS A  -107                                                      
REMARK 465     LYS A  -106                                                      
REMARK 465     LEU A  -105                                                      
REMARK 465     GLU A  -104                                                      
REMARK 465     TYR A  -103                                                      
REMARK 465     ASN A  -102                                                      
REMARK 465     TYR A  -101                                                      
REMARK 465     ASN A  -100                                                      
REMARK 465     SER A   -99                                                      
REMARK 465     HIS A   -98                                                      
REMARK 465     ASN A   -97                                                      
REMARK 465     VAL A   -96                                                      
REMARK 465     TYR A   -95                                                      
REMARK 465     ILE A   -94                                                      
REMARK 465     MET A   -93                                                      
REMARK 465     ALA A   -92                                                      
REMARK 465     ASP A   -91                                                      
REMARK 465     LYS A   -90                                                      
REMARK 465     GLN A   -89                                                      
REMARK 465     LYS A   -88                                                      
REMARK 465     ASN A   -87                                                      
REMARK 465     GLY A   -86                                                      
REMARK 465     ILE A   -85                                                      
REMARK 465     LYS A   -84                                                      
REMARK 465     VAL A   -83                                                      
REMARK 465     ASN A   -82                                                      
REMARK 465     PHE A   -81                                                      
REMARK 465     LYS A   -80                                                      
REMARK 465     ILE A   -79                                                      
REMARK 465     ARG A   -78                                                      
REMARK 465     HIS A   -77                                                      
REMARK 465     ASN A   -76                                                      
REMARK 465     ILE A   -75                                                      
REMARK 465     GLU A   -74                                                      
REMARK 465     ASP A   -73                                                      
REMARK 465     GLY A   -72                                                      
REMARK 465     SER A   -71                                                      
REMARK 465     VAL A   -70                                                      
REMARK 465     GLN A   -69                                                      
REMARK 465     LEU A   -68                                                      
REMARK 465     ALA A   -67                                                      
REMARK 465     ASP A   -66                                                      
REMARK 465     HIS A   -65                                                      
REMARK 465     TYR A   -64                                                      
REMARK 465     GLN A   -63                                                      
REMARK 465     GLN A   -62                                                      
REMARK 465     ASN A   -61                                                      
REMARK 465     THR A   -60                                                      
REMARK 465     PRO A   -59                                                      
REMARK 465     ILE A   -58                                                      
REMARK 465     GLY A   -57                                                      
REMARK 465     ASP A   -56                                                      
REMARK 465     GLY A   -55                                                      
REMARK 465     PRO A   -54                                                      
REMARK 465     VAL A   -53                                                      
REMARK 465     LEU A   -52                                                      
REMARK 465     LEU A   -51                                                      
REMARK 465     PRO A   -50                                                      
REMARK 465     ASP A   -49                                                      
REMARK 465     ASN A   -48                                                      
REMARK 465     HIS A   -47                                                      
REMARK 465     TYR A   -46                                                      
REMARK 465     LEU A   -45                                                      
REMARK 465     SER A   -44                                                      
REMARK 465     THR A   -43                                                      
REMARK 465     GLN A   -42                                                      
REMARK 465     SER A   -41                                                      
REMARK 465     ALA A   -40                                                      
REMARK 465     LEU A   -39                                                      
REMARK 465     SER A   -38                                                      
REMARK 465     LYS A   -37                                                      
REMARK 465     ASP A   -36                                                      
REMARK 465     PRO A   -35                                                      
REMARK 465     ASN A   -34                                                      
REMARK 465     GLU A   -33                                                      
REMARK 465     LYS A   -32                                                      
REMARK 465     ARG A   -31                                                      
REMARK 465     ASP A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     MET A   -28                                                      
REMARK 465     VAL A   -27                                                      
REMARK 465     LEU A   -26                                                      
REMARK 465     LEU A   -25                                                      
REMARK 465     GLU A   -24                                                      
REMARK 465     PHE A   -23                                                      
REMARK 465     VAL A   -22                                                      
REMARK 465     THR A   -21                                                      
REMARK 465     ALA A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     ILE A   -17                                                      
REMARK 465     THR A   -16                                                      
REMARK 465     LEU A   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     MET A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     GLU A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     TYR A    -9                                                      
REMARK 465     LYS A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     TYR A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     HIS A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     HIS A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     HIS A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     THR A    34                                                      
REMARK 465     LEU A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     ASN A    39                                                      
REMARK 465     GLN A    40                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     TYR A    44                                                      
REMARK 465     TYR A    45                                                      
REMARK 465     ASP A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     PRO A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     HIS A    50                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     MET A    52                                                      
REMARK 465     PHE A    53                                                      
REMARK 465     GLN A    54                                                      
REMARK 465     GLN A    55                                                      
REMARK 465     PRO A    56                                                      
REMARK 465     TYR A    57                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     GLN A    59                                                      
REMARK 465     HIS A    60                                                      
REMARK 465     GLY A    61                                                      
REMARK 465     GLY A    62                                                      
REMARK 465     PHE A    63                                                      
REMARK 465     HIS A    64                                                      
REMARK 465     GLN A    65                                                      
REMARK 465     GLN A    66                                                      
REMARK 465     ASN A    67                                                      
REMARK 465     GLU A    68                                                      
REMARK 465     LEU A    69                                                      
REMARK 465     GLN A    70                                                      
REMARK 465     HIS A    71                                                      
REMARK 465     LEU A    72                                                      
REMARK 465     ARG A    73                                                      
REMARK 465     GLU A    74                                                      
REMARK 465     PHE A    75                                                      
REMARK 465     SER A    76                                                      
REMARK 465     ASP A    77                                                      
REMARK 465     SER A    78                                                      
REMARK 465     HIS A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     ASN A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     PHE A    83                                                      
REMARK 465     SER A    84                                                      
REMARK 465     HIS A    85                                                      
REMARK 465     HIS A    86                                                      
REMARK 465     SER A    87                                                      
REMARK 465     TYR A    88                                                      
REMARK 465     GLN A    89                                                      
REMARK 465     GLN A    90                                                      
REMARK 465     ASP A    91                                                      
REMARK 465     ARG A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     VAL A    95                                                      
REMARK 465     SER A    96                                                      
REMARK 465     THR A    97                                                      
REMARK 465     LEU A    98                                                      
REMARK 465     PRO A    99                                                      
REMARK 465     ASN A   100                                                      
REMARK 465     ASN A   101                                                      
REMARK 465     ILE A   102                                                      
REMARK 465     SER A   103                                                      
REMARK 465     HIS A   104                                                      
REMARK 465     ALA A   105                                                      
REMARK 465     TYR A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     HIS A   110                                                      
REMARK 465     PRO A   111                                                      
REMARK 465     LEU A   112                                                      
REMARK 465     ALA A   113                                                      
REMARK 465     GLU A   114                                                      
REMARK 465     SER A   115                                                      
REMARK 465     GLN A   116                                                      
REMARK 465     HIS A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     GLY A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     PRO A   121                                                      
REMARK 465     GLN A   122                                                      
REMARK 465     SER A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     PRO A   125                                                      
REMARK 465     ARG A   126                                                      
REMARK 465     ILE A   127                                                      
REMARK 465     ASP A   128                                                      
REMARK 465     PRO A   129                                                      
REMARK 465     ASN A   130                                                      
REMARK 465     HIS A   131                                                      
REMARK 465     HIS A   132                                                      
REMARK 465     PRO A   133                                                      
REMARK 465     HIS A   134                                                      
REMARK 465     GLN A   135                                                      
REMARK 465     ASP A   136                                                      
REMARK 465     ASP A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     HIS A   139                                                      
REMARK 465     ARG A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     GLU A   143                                                      
REMARK 465     PRO A   144                                                      
REMARK 465     LEU A   145                                                      
REMARK 465     SER A   146                                                      
REMARK 465     HIS A   147                                                      
REMARK 465     PRO A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     SER A   150                                                      
REMARK 465     THR A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     HIS A   154                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     GLY A   156                                                      
REMARK 465     THR A   157                                                      
REMARK 465     THR A   158                                                      
REMARK 465     HIS A   159                                                      
REMARK 465     GLN A   160                                                      
REMARK 465     GLN A   161                                                      
REMARK 465     TYR A   162                                                      
REMARK 465     HIS A   163                                                      
REMARK 465     GLU A   164                                                      
REMARK 465     ARG A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     HIS A   167                                                      
REMARK 465     HIS A   168                                                      
REMARK 465     LEU A   169                                                      
REMARK 465     ASN A   170                                                      
REMARK 465     PRO A   171                                                      
REMARK 465     GLN A   172                                                      
REMARK 465     GLN A   173                                                      
REMARK 465     ASN A   174                                                      
REMARK 465     ARG A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     HIS A   177                                                      
REMARK 465     ALA A   178                                                      
REMARK 465     ASP A   179                                                      
REMARK 465     THR A   180                                                      
REMARK 465     ILE A   181                                                      
REMARK 465     SER A   182                                                      
REMARK 465     TYR A   183                                                      
REMARK 465     ARG A   184                                                      
REMARK 465     SER A   185                                                      
REMARK 465     SER A   186                                                      
REMARK 465     THR A   187                                                      
REMARK 465     ARG A   188                                                      
REMARK 465     PHE A   189                                                      
REMARK 465     TYR A   190                                                      
REMARK 465     ARG A   191                                                      
REMARK 465     SER A   192                                                      
REMARK 465     HIS A   193                                                      
REMARK 465     ALA A   194                                                      
REMARK 465     PRO A   195                                                      
REMARK 465     PHE A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     ARG A   198                                                      
REMARK 465     GLN A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     ARG A   201                                                      
REMARK 465     PRO A   202                                                      
REMARK 465     HIS A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     ALA A   206                                                      
REMARK 465     ASP A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     ALA A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     HIS A   219                                                      
REMARK 465     GLY A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     HIS A   222                                                      
REMARK 465     PRO A   223                                                      
REMARK 465     HIS A   224                                                      
REMARK 465     HIS A   225                                                      
REMARK 465     LYS A   226                                                      
REMARK 465     GLU A   227                                                      
REMARK 465     GLN A   228                                                      
REMARK 465     ARG A   229                                                      
REMARK 465     HIS A   230                                                      
REMARK 465     TYR A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     GLY A   233                                                      
REMARK 465     ASP A   234                                                      
REMARK 465     HIS A   235                                                      
REMARK 465     MET A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     HIS A   238                                                      
REMARK 465     HIS A   239                                                      
REMARK 465     ILE A   240                                                      
REMARK 465     HIS A   241                                                      
REMARK 465     HIS A   242                                                      
REMARK 465     ARG A   243                                                      
REMARK 465     SER A   244                                                      
REMARK 465     PRO A   245                                                      
REMARK 465     SER A   246                                                      
REMARK 465     ALA A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 465     GLN A   249                                                      
REMARK 465     LEU A   250                                                      
REMARK 465     SER A   251                                                      
REMARK 465     HIS A   252                                                      
REMARK 465     LYS A   253                                                      
REMARK 465     SER A   254                                                      
REMARK 465     HIS A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     THR A   257                                                      
REMARK 465     LEU A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     THR A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     SER A   263                                                      
REMARK 465     HIS A   264                                                      
REMARK 465     VAL A   265                                                      
REMARK 465     GLY A   266                                                      
REMARK 465     SER A   267                                                      
REMARK 465     LYS A   268                                                      
REMARK 465     SER A   269                                                      
REMARK 465     THR A   270                                                      
REMARK 465     ALA A   271                                                      
REMARK 465     SER A   272                                                      
REMARK 465     GLY A   273                                                      
REMARK 465     ALA A   274                                                      
REMARK 465     ARG A   275                                                      
REMARK 465     TYR A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     PHE A   278                                                      
REMARK 465     GLY A   279                                                      
REMARK 465     ALA A   280                                                      
REMARK 465     ARG A   281                                                      
REMARK 465     SER A   282                                                      
REMARK 465     GLN A   283                                                      
REMARK 465     ILE A   284                                                      
REMARK 465     PHE A   285                                                      
REMARK 465     GLY A   286                                                      
REMARK 465     LYS A   287                                                      
REMARK 465     ALA A   288                                                      
REMARK 465     GLN A   289                                                      
REMARK 465     SER A   290                                                      
REMARK 465     ARG A   291                                                      
REMARK 465     GLU A   292                                                      
REMARK 465     SER A   293                                                      
REMARK 465     LEU A   294                                                      
REMARK 465     ARG A   295                                                      
REMARK 465     GLU A   296                                                      
REMARK 465     SER A   297                                                      
REMARK 465     ALA A   298                                                      
REMARK 465     SER A   299                                                      
REMARK 465     LEU A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     GLU A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     ASP A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     VAL A   307                                                      
REMARK 465     GLN A   308                                                      
REMARK 465     LYS A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     LYS A   311                                                      
REMARK 465     LYS A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     GLN A   314                                                      
REMARK 465     ARG A   315                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     LYS A   318                                                      
REMARK 465     LYS A   319                                                      
REMARK 465     ALA A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     GLY A   323                                                      
REMARK 465     ASN A   324                                                      
REMARK 465     ILE A   325                                                      
REMARK 465     PHE A   326                                                      
REMARK 465     GLN A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     LEU A   329                                                      
REMARK 465     TRP A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     LYS A   332                                                      
REMARK 465     ILE A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     LEU A   336                                                      
REMARK 465     GLN A   595                                                      
REMARK 465     ALA A   596                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     ARG A   598                                                      
REMARK 465     VAL A   599                                                      
REMARK 465     HIS A   600                                                      
REMARK 465     GLU A   601                                                      
REMARK 465     LYS A   602                                                      
REMARK 465     LEU A   603                                                      
REMARK 465     LEU A   604                                                      
REMARK 465     ASP A   605                                                      
REMARK 465     ASP A   606                                                      
REMARK 465     SER A   607                                                      
REMARK 465     LEU A   608                                                      
REMARK 465     THR A   609                                                      
REMARK 465     ASP A   610                                                      
REMARK 465     LEU A   611                                                      
REMARK 465     ASN A   612                                                      
REMARK 465     LYS A   613                                                      
REMARK 465     ALA A   614                                                      
REMARK 465     ASP A   615                                                      
REMARK 465     ALA A   616                                                      
REMARK 465     ASN A   617                                                      
REMARK 465     ALA A   618                                                      
REMARK 465     GLN A   619                                                      
REMARK 465     MET A   620                                                      
REMARK 465     THR A   621                                                      
REMARK 465     GLU A   622                                                      
REMARK 465     GLU A   623                                                      
REMARK 465     ALA A   624                                                      
REMARK 465     LEU A   625                                                      
REMARK 465     LYS A   626                                                      
REMARK 465     MET A   627                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     ILE A   630                                                      
REMARK 465     GLU A   631                                                      
REMARK 465     GLY A   632                                                      
REMARK 465     MET A   633                                                      
REMARK 465     PHE A   634                                                      
REMARK 465     GLY A   635                                                      
REMARK 465     ASN A   636                                                      
REMARK 465     MET A   637                                                      
REMARK 465     THR A   638                                                      
REMARK 465     VAL A   639                                                      
REMARK 465     LYS A   640                                                      
REMARK 465     GLN A   641                                                      
REMARK 465     ARG A   642                                                      
REMARK 465     VAL A   643                                                      
REMARK 465     LEU A   644                                                      
REMARK 465     HIS A   645                                                      
REMARK 465     PHE A   646                                                      
REMARK 465     GLN A   647                                                      
REMARK 465     PHE A   648                                                      
REMARK 465     LEU A   649                                                      
REMARK 465     GLN A   650                                                      
REMARK 465     LEU A   651                                                      
REMARK 465     VAL A   652                                                      
REMARK 465     ALA A   653                                                      
REMARK 465     ALA A   654                                                      
REMARK 465     VAL A   655                                                      
REMARK 465     GLU A   656                                                      
REMARK 465     GLN A   657                                                      
REMARK 465     HIS A   658                                                      
REMARK 465     GLN A   659                                                      
REMARK 465     GLN A   660                                                      
REMARK 465     LYS A   661                                                      
REMARK 465     PHE A   662                                                      
REMARK 465     ARG A   663                                                      
REMARK 465     SER A   664                                                      
REMARK 465     GLN A   665                                                      
REMARK 465     ALA A   666                                                      
REMARK 465     TYR A   667                                                      
REMARK 465     VAL A   668                                                      
REMARK 465     ILE A   669                                                      
REMARK 465     ASP A   670                                                      
REMARK 465     GLU A   671                                                      
REMARK 465     LEU A   672                                                      
REMARK 465     VAL A   673                                                      
REMARK 465     ASP A   674                                                      
REMARK 465     MET A   675                                                      
REMARK 465     ALA A   676                                                      
REMARK 465     PHE A   677                                                      
REMARK 465     GLU A   678                                                      
REMARK 465     ALA A   679                                                      
REMARK 465     GLY A   680                                                      
REMARK 465     ASP A   681                                                      
REMARK 465     ASP A   682                                                      
REMARK 465     ASP A   683                                                      
REMARK 465     TYR A   684                                                      
REMARK 465     GLY A   685                                                      
REMARK 465     LYS A   686                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     PHE B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ASP B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     ILE B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     LYS B    19                                                      
REMARK 465     LEU B    20                                                      
REMARK 465     ILE B    21                                                      
REMARK 465     ASP B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     PHE B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     ILE B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     HIS B    29                                                      
REMARK 465     LEU B    30                                                      
REMARK 465     GLN B    31                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     LEU B    33                                                      
REMARK 465     SER B    34                                                      
REMARK 465     GLN B    35                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     VAL B    37                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     ARG B    39                                                      
REMARK 465     HIS B    40                                                      
REMARK 465     THR B    41                                                      
REMARK 465     LEU B    42                                                      
REMARK 465     ARG B    43                                                      
REMARK 465     GLU B    44                                                      
REMARK 465     ILE B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     PRO B    48                                                      
REMARK 465     SER B    49                                                      
REMARK 465     TYR B    50                                                      
REMARK 465     GLN B    51                                                      
REMARK 465     GLN B    52                                                      
REMARK 465     LYS B    53                                                      
REMARK 465     LEU B    54                                                      
REMARK 465     MET B    55                                                      
REMARK 465     SER B    56                                                      
REMARK 465     GLY B    57                                                      
REMARK 465     ASP B    58                                                      
REMARK 465     GLN B    59                                                      
REMARK 465     GLU B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     LEU B    62                                                      
REMARK 465     VAL B    63                                                      
REMARK 465     ARG B    64                                                      
REMARK 465     PHE B    65                                                      
REMARK 465     SER B    66                                                      
REMARK 465     ILE B    67                                                      
REMARK 465     LYS B    68                                                      
REMARK 465     PRO B    69                                                      
REMARK 465     ARG B    70                                                      
REMARK 465     ARG B    71                                                      
REMARK 465     MET B    72                                                      
REMARK 465     GLY B    73                                                      
REMARK 465     HIS B    74                                                      
REMARK 465     ILE B    75                                                      
REMARK 465     THR B    76                                                      
REMARK 465     HIS B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     ARG B    79                                                      
REMARK 465     ARG B    80                                                      
REMARK 465     LEU B    81                                                      
REMARK 465     LEU B    82                                                      
REMARK 465     SER B    83                                                      
REMARK 465     ARG B    84                                                      
REMARK 465     LEU B    85                                                      
REMARK 465     ARG B    86                                                      
REMARK 465     VAL B    87                                                      
REMARK 465     ARG B    88                                                      
REMARK 465     CYS B    89                                                      
REMARK 465     SER B    90                                                      
REMARK 465     ARG B    91                                                      
REMARK 465     MET B    92                                                      
REMARK 465     PRO B    93                                                      
REMARK 465     HIS B   375                                                      
REMARK 465     SER B   376                                                      
REMARK 465     GLU B   377                                                      
REMARK 465     SER B   378                                                      
REMARK 465     LEU B   379                                                      
REMARK 465     ARG B   380                                                      
REMARK 465     GLY B   381                                                      
REMARK 465     THR B   382                                                      
REMARK 465     SER B   383                                                      
REMARK 465     LEU B   384                                                      
REMARK 465     GLY B   385                                                      
REMARK 465     LYS B   386                                                      
REMARK 465     VAL B   387                                                      
REMARK 465     SER B   388                                                      
REMARK 465     GLU B   389                                                      
REMARK 465     ASP B   390                                                      
REMARK 465     ILE B   391                                                      
REMARK 465     ILE B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     THR B   394                                                      
REMARK 465     SER B   395                                                      
REMARK 465     ASP B   396                                                      
REMARK 465     ALA B   397                                                      
REMARK 465     SER B   398                                                      
REMARK 465     ASP B   399                                                      
REMARK 465     ASP B   400                                                      
REMARK 465     ASP B   401                                                      
REMARK 465     ASP B   402                                                      
REMARK 465     ASP B   403                                                      
REMARK 465     ASP B   404                                                      
REMARK 465     ASP B   405                                                      
REMARK 465     ASP B   406                                                      
REMARK 465     ASP B   407                                                      
REMARK 465     ASP B   408                                                      
REMARK 465     ASP B   409                                                      
REMARK 465     ASP B   410                                                      
REMARK 465     ASP B   411                                                      
REMARK 465     ASP B   412                                                      
REMARK 465     ASP B   413                                                      
REMARK 465     ASP B   414                                                      
REMARK 465     ASP B   415                                                      
REMARK 465     ASP B   416                                                      
REMARK 465     ASP B   417                                                      
REMARK 465     LYS B   418                                                      
REMARK 465     SER B   419                                                      
REMARK 465     ASP B   420                                                      
REMARK 465     ALA B   421                                                      
REMARK 465     THR B   422                                                      
REMARK 465     GLU B   423                                                      
REMARK 465     SER B   424                                                      
REMARK 465     ASP B   425                                                      
REMARK 465     ASN B   426                                                      
REMARK 465     GLU B   427                                                      
REMARK 465     GLU B   428                                                      
REMARK 465     SER B   429                                                      
REMARK 465     ASP B   430                                                      
REMARK 465     SER B   431                                                      
REMARK 465     GLU B   432                                                      
REMARK 465     ASN B   433                                                      
REMARK 465     SER B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     SER B   436                                                      
REMARK 465     GLU B   437                                                      
REMARK 465     ASN B   438                                                      
REMARK 465     SER B   439                                                      
REMARK 465     GLU B   440                                                      
REMARK 465     SER B   441                                                      
REMARK 465     GLU B   442                                                      
REMARK 465     LYS B   443                                                      
REMARK 465     ILE B   444                                                      
REMARK 465     ASP B   445                                                      
REMARK 465     PRO B   446                                                      
REMARK 465     GLU B   447                                                      
REMARK 465     LYS B   448                                                      
REMARK 465     ASP B   449                                                      
REMARK 465     TYR B   450                                                      
REMARK 465     ALA B   451                                                      
REMARK 465     LYS B   452                                                      
REMARK 465     LYS B   453                                                      
REMARK 465     SER B   454                                                      
REMARK 465     TYR B   455                                                      
REMARK 465     PRO B   456                                                      
REMARK 465     GLU B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     SER B   459                                                      
REMARK 465     HIS B   460                                                      
REMARK 465     PRO B   461                                                      
REMARK 465     GLU B   462                                                      
REMARK 465     LYS B   463                                                      
REMARK 465     SER B   464                                                      
REMARK 465     TYR B   465                                                      
REMARK 465     PRO B   466                                                      
REMARK 465     GLU B   467                                                      
REMARK 465     LYS B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     HIS B   470                                                      
REMARK 465     PRO B   471                                                      
REMARK 465     GLU B   472                                                      
REMARK 465     LYS B   473                                                      
REMARK 465     SER B   474                                                      
REMARK 465     TYR B   475                                                      
REMARK 465     PRO B   476                                                      
REMARK 465     GLU B   477                                                      
REMARK 465     LYS B   478                                                      
REMARK 465     SER B   479                                                      
REMARK 465     HIS B   480                                                      
REMARK 465     PRO B   481                                                      
REMARK 465     LYS B   482                                                      
REMARK 465     LYS B   483                                                      
REMARK 465     SER B   484                                                      
REMARK 465     TYR B   485                                                      
REMARK 465     ASP B   486                                                      
REMARK 465     GLU B   487                                                      
REMARK 465     GLN B   488                                                      
REMARK 465     ALA B   489                                                      
REMARK 465     GLU B   490                                                      
REMARK 465     ALA B   491                                                      
REMARK 465     GLU B   492                                                      
REMARK 465     LYS B   493                                                      
REMARK 465     VAL B   494                                                      
REMARK 465     LYS B   495                                                      
REMARK 465     GLU B   496                                                      
REMARK 465     GLU B   497                                                      
REMARK 465     SER B   498                                                      
REMARK 465     LYS B   499                                                      
REMARK 465     GLU B   500                                                      
REMARK 465     LYS B   501                                                      
REMARK 465     ALA B   502                                                      
REMARK 465     TYR B   503                                                      
REMARK 465     PRO B   504                                                      
REMARK 465     VAL B   505                                                      
REMARK 465     SER B   506                                                      
REMARK 465     HIS B   507                                                      
REMARK 465     SER B   508                                                      
REMARK 465     ILE B   509                                                      
REMARK 465     SER B   510                                                      
REMARK 465     SER B   511                                                      
REMARK 465     HIS B   512                                                      
REMARK 465     GLY B   513                                                      
REMARK 465     SER B   514                                                      
REMARK 465     THR B   515                                                      
REMARK 465     ALA B   516                                                      
REMARK 465     ALA B   517                                                      
REMARK 465     ASP B   518                                                      
REMARK 465     THR B   519                                                      
REMARK 465     ALA B   520                                                      
REMARK 465     PHE B   521                                                      
REMARK 465     LEU B   522                                                      
REMARK 465     GLU B   523                                                      
REMARK 465     ASN B   524                                                      
REMARK 465     LEU B   525                                                      
REMARK 465     ASP B   526                                                      
REMARK 465     TRP B   527                                                      
REMARK 465     GLU B   528                                                      
REMARK 465     THR B   529                                                      
REMARK 465     LEU B   530                                                      
REMARK 465     VAL B   531                                                      
REMARK 465     HIS B   532                                                      
REMARK 465     GLU B   533                                                      
REMARK 465     ASN B   534                                                      
REMARK 465     LEU B   535                                                      
REMARK 465     PRO B   536                                                      
REMARK 465     GLY B   537                                                      
REMARK 465     LEU B   538                                                      
REMARK 465     MET B   539                                                      
REMARK 465     ASP B   540                                                      
REMARK 465     MET B   541                                                      
REMARK 465     ASP B   542                                                      
REMARK 465     GLN B   543                                                      
REMARK 465     ASP B   544                                                      
REMARK 465     ASP B   545                                                      
REMARK 465     ARG B   546                                                      
REMARK 465     ILE B   547                                                      
REMARK 465     VAL B   548                                                      
REMARK 465     TRP B   549                                                      
REMARK 465     PRO B   550                                                      
REMARK 465     ARG B   551                                                      
REMARK 465     ASP B   552                                                      
REMARK 465     SER B   553                                                      
REMARK 465     LEU B   554                                                      
REMARK 465     PHE B   555                                                      
REMARK 465     ARG B   556                                                      
REMARK 465     TYR B   557                                                      
REMARK 465     PHE B   558                                                      
REMARK 465     GLU B   559                                                      
REMARK 465     LEU B   560                                                      
REMARK 465     LEU B   561                                                      
REMARK 465     GLU B   562                                                      
REMARK 465     LYS B   563                                                      
REMARK 465     LEU B   564                                                      
REMARK 465     GLN B   565                                                      
REMARK 465     TYR B   566                                                      
REMARK 465     ASN B   567                                                      
REMARK 465     LEU B   568                                                      
REMARK 465     GLU B   569                                                      
REMARK 465     GLU B   570                                                      
REMARK 465     ARG B   571                                                      
REMARK 465     LYS B   572                                                      
REMARK 465     LYS B   573                                                      
REMARK 465     LEU B   574                                                      
REMARK 465     GLN B   575                                                      
REMARK 465     GLU B   576                                                      
REMARK 465     PHE B   577                                                      
REMARK 465     ALA B   578                                                      
REMARK 465     VAL B   579                                                      
REMARK 465     GLN B   580                                                      
REMARK 465     ALA B   581                                                      
REMARK 465     LEU B   582                                                      
REMARK 465     MET B   583                                                      
REMARK 465     SER B   584                                                      
REMARK 465     PHE B   585                                                      
REMARK 465     GLU B   586                                                      
REMARK 465     ASP B   587                                                      
REMARK 465     LYS B   588                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     PHE C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     ASN C     8                                                      
REMARK 465     PRO C     9                                                      
REMARK 465     VAL C    10                                                      
REMARK 465     ARG C    11                                                      
REMARK 465     VAL C    12                                                      
REMARK 465     LYS C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     SER C    16                                                      
REMARK 465     LEU C    17                                                      
REMARK 465     PHE C    18                                                      
REMARK 465     ALA C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     ALA C    21                                                      
REMARK 465     SER C    22                                                      
REMARK 465     GLU C    23                                                      
REMARK 465     ALA C    24                                                      
REMARK 465     LEU C    25                                                      
REMARK 465     GLN C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     ARG C    28                                                      
REMARK 465     LEU C    29                                                      
REMARK 465     SER C    30                                                      
REMARK 465     LYS C    31                                                      
REMARK 465     ILE C    32                                                      
REMARK 465     LYS C    33                                                      
REMARK 465     ARG C    34                                                      
REMARK 465     LYS C    35                                                      
REMARK 465     ASP C    36                                                      
REMARK 465     LYS C    37                                                      
REMARK 465     SER C   316                                                      
REMARK 465     MET C   317                                                      
REMARK 465     ASN C   318                                                      
REMARK 465     PHE C   319                                                      
REMARK 465     ILE C   320                                                      
REMARK 465     ASP C   321                                                      
REMARK 465     MET C   322                                                      
REMARK 465     VAL C   323                                                      
REMARK 465     GLU C   324                                                      
REMARK 465     GLY C   325                                                      
REMARK 465     PHE C   326                                                      
REMARK 465     LYS C   327                                                      
REMARK 465     LYS C   328                                                      
REMARK 465     THR C   329                                                      
REMARK 465     LEU C   330                                                      
REMARK 465     ARG C   331                                                      
REMARK 465     HIS C   332                                                      
REMARK 465     THR C   333                                                      
REMARK 465     ASP C   334                                                      
REMARK 465     PRO C   335                                                      
REMARK 465     MET C   336                                                      
REMARK 465     VAL C   337                                                      
REMARK 465     LEU C   338                                                      
REMARK 465     ASP C   339                                                      
REMARK 465     ASP C   340                                                      
REMARK 465     PHE C   341                                                      
REMARK 465     SER C   342                                                      
REMARK 465     THR C   343                                                      
REMARK 465     SER C   344                                                      
REMARK 465     LEU C   345                                                      
REMARK 465     SER C   346                                                      
REMARK 465     PHE C   347                                                      
REMARK 465     ILE C   348                                                      
REMARK 465     ASP C   349                                                      
REMARK 465     ILE C   350                                                      
REMARK 465     TYR C   351                                                      
REMARK 465     LEU C   352                                                      
REMARK 465     VAL C   353                                                      
REMARK 465     THR C   354                                                      
REMARK 465     LEU C   355                                                      
REMARK 465     ASP C   356                                                      
REMARK 465     ASN C   357                                                      
REMARK 465     GLN C   358                                                      
REMARK 465     ASP C   359                                                      
REMARK 465     VAL C   360                                                      
REMARK 465     ILE C   361                                                      
REMARK 465     VAL C   362                                                      
REMARK 465     SER C   363                                                      
REMARK 465     LYS C   364                                                      
REMARK 465     LEU C   365                                                      
REMARK 465     GLN C   366                                                      
REMARK 465     GLU C   367                                                      
REMARK 465     LEU C   368                                                      
REMARK 465     TYR C   369                                                      
REMARK 465     CYS C   370                                                      
REMARK 465     GLU C   371                                                      
REMARK 465     ILE C   372                                                      
REMARK 465     VAL C   373                                                      
REMARK 465     ASN C   374                                                      
REMARK 465     VAL C   375                                                      
REMARK 465     LEU C   376                                                      
REMARK 465     SER C   377                                                      
REMARK 465     LEU C   378                                                      
REMARK 465     MET C   379                                                      
REMARK 465     LEU C   380                                                      
REMARK 465     GLU C   381                                                      
REMARK 465     ASP C   382                                                      
REMARK 465     MET C   383                                                      
REMARK 465     PRO C   384                                                      
REMARK 465     LYS C   385                                                      
REMARK 465     GLU C   386                                                      
REMARK 465     SER C   387                                                      
REMARK 465     SER C   388                                                      
REMARK 465     SER C   389                                                      
REMARK 465     SER C   390                                                      
REMARK 465     LEU C   391                                                      
REMARK 465     SER C   392                                                      
REMARK 465     GLY C   393                                                      
REMARK 465     LEU C   394                                                      
REMARK 465     SER C   395                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     TRP D     7                                                      
REMARK 465     TRP D     8                                                      
REMARK 465     GLN D     9                                                      
REMARK 465     GLN D    10                                                      
REMARK 465     VAL D    11                                                      
REMARK 465     GLU D    12                                                      
REMARK 465     ASN D    13                                                      
REMARK 465     ILE D    14                                                      
REMARK 465     ASP D    15                                                      
REMARK 465     ILE D    16                                                      
REMARK 465     THR D    17                                                      
REMARK 465     HIS D    18                                                      
REMARK 465     LEU D    19                                                      
REMARK 465     GLY D    20                                                      
REMARK 465     PRO D    21                                                      
REMARK 465     LYS D    22                                                      
REMARK 465     ARG D    23                                                      
REMARK 465     LYS D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     TYR D    26                                                      
REMARK 465     GLU D    27                                                      
REMARK 465     LEU D    28                                                      
REMARK 465     LEU D    29                                                      
REMARK 465     GLY D    30                                                      
REMARK 465     ARG D    31                                                      
REMARK 465     HIS D    32                                                      
REMARK 465     GLU D    33                                                      
REMARK 465     GLU D    34                                                      
REMARK 465     GLN D    35                                                      
REMARK 465     VAL D    36                                                      
REMARK 465     LEU D    37                                                      
REMARK 465     ILE D    38                                                      
REMARK 465     ASN D    39                                                      
REMARK 465     ARG D    40                                                      
REMARK 465     ARG D    41                                                      
REMARK 465     ASP D    42                                                      
REMARK 465     VAL D    43                                                      
REMARK 465     MET D    44                                                      
REMARK 465     GLU D    45                                                      
REMARK 465     LYS D    46                                                      
REMARK 465     LYS D    47                                                      
REMARK 465     ASP D    48                                                      
REMARK 465     ALA D    49                                                      
REMARK 465     TRP D    50                                                      
REMARK 465     GLY D   293                                                      
REMARK 465     GLU D   294                                                      
REMARK 465     GLU D   295                                                      
REMARK 465     GLU D   296                                                      
REMARK 465     GLY D   297                                                      
REMARK 465     HIS D   298                                                      
REMARK 465     LEU D   299                                                      
REMARK 465     ASN D   300                                                      
REMARK 465     ILE D   301                                                      
REMARK 465     LYS D   302                                                      
REMARK 465     PHE D   303                                                      
REMARK 465     THR D   304                                                      
REMARK 465     GLU D   305                                                      
REMARK 465     THR D   306                                                      
REMARK 465     GLU D   307                                                      
REMARK 465     GLU D   308                                                      
REMARK 465     ASP D   309                                                      
REMARK 465     GLU D   310                                                      
REMARK 465     ASP D   311                                                      
REMARK 465     TRP D   312                                                      
REMARK 465     THR D   313                                                      
REMARK 465     ASP D   314                                                      
REMARK 465     GLU D   315                                                      
REMARK 465     LEU D   316                                                      
REMARK 465     PRO D   317                                                      
REMARK 465     LEU D   318                                                      
REMARK 465     VAL D   319                                                      
REMARK 465     HIS D   320                                                      
REMARK 465     CYS D   321                                                      
REMARK 465     THR D   322                                                      
REMARK 465     GLU D   323                                                      
REMARK 465     ALA D   324                                                      
REMARK 465     ARG D   325                                                      
REMARK 465     LYS D   326                                                      
REMARK 465     ASP D   327                                                      
REMARK 465     THR D   328                                                      
REMARK 465     SER D   329                                                      
REMARK 465     THR D   330                                                      
REMARK 465     VAL D   331                                                      
REMARK 465     PRO D   332                                                      
REMARK 465     LYS D   333                                                      
REMARK 465     GLU D   334                                                      
REMARK 465     PRO D   335                                                      
REMARK 465     LEU D   336                                                      
REMARK 465     VAL D   337                                                      
REMARK 465     GLY D   338                                                      
REMARK 465     GLY D   339                                                      
REMARK 465     PRO D   340                                                      
REMARK 465     LEU D   341                                                      
REMARK 465     SER D   342                                                      
REMARK 465     ASN D   343                                                      
REMARK 465     LEU D   344                                                      
REMARK 465     THR D   345                                                      
REMARK 465     GLU D   346                                                      
REMARK 465     LYS D   347                                                      
REMARK 465     THR D   348                                                      
REMARK 465     CYS D   349                                                      
REMARK 465     ASP D   350                                                      
REMARK 465     ASN D   351                                                      
REMARK 465     PHE D   352                                                      
REMARK 465     CYS D   353                                                      
REMARK 465     LEU D   354                                                      
REMARK 465     VAL D   355                                                      
REMARK 465     LEU D   356                                                      
REMARK 465     GLU D   357                                                      
REMARK 465     ALA D   358                                                      
REMARK 465     ILE D   359                                                      
REMARK 465     GLN D   360                                                      
REMARK 465     GLU D   361                                                      
REMARK 465     ASN D   362                                                      
REMARK 465     LEU D   363                                                      
REMARK 465     MET D   364                                                      
REMARK 465     GLU D   365                                                      
REMARK 465     TYR D   366                                                      
REMARK 465     LYS D   367                                                      
REMARK 465     GLU D   368                                                      
REMARK 465     ILE D   369                                                      
REMARK 465     ARG D   370                                                      
REMARK 465     GLU D   371                                                      
REMARK 465     GLU D   372                                                      
REMARK 465     LEU D   373                                                      
REMARK 465     ASN D   374                                                      
REMARK 465     MET D   375                                                      
REMARK 465     ILE D   376                                                      
REMARK 465     VAL D   377                                                      
REMARK 465     GLU D   378                                                      
REMARK 465     GLU D   379                                                      
REMARK 465     VAL D   380                                                      
REMARK 465     SER D   381                                                      
REMARK 465     SER D   382                                                      
REMARK 465     ILE D   383                                                      
REMARK 465     ARG D   384                                                      
REMARK 465     PHE D   385                                                      
REMARK 465     ASN D   386                                                      
REMARK 465     GLN D   387                                                      
REMARK 465     GLU D   388                                                      
REMARK 465     GLN D   389                                                      
REMARK 465     GLN D   390                                                      
REMARK 465     ASN D   391                                                      
REMARK 465     VAL D   392                                                      
REMARK 465     ILE D   393                                                      
REMARK 465     LEU D   394                                                      
REMARK 465     HIS D   395                                                      
REMARK 465     LYS D   396                                                      
REMARK 465     TYR D   397                                                      
REMARK 465     THR D   398                                                      
REMARK 465     SER D   399                                                      
REMARK 465     LYS D   400                                                      
REMARK 465     SER D   401                                                      
REMARK 465     ALA D   402                                                      
REMARK 465     THR D   403                                                      
REMARK 465     PHE D   404                                                      
REMARK 465     LEU D   405                                                      
REMARK 465     SER D   406                                                      
REMARK 465     GLU D   407                                                      
REMARK 465     PRO D   408                                                      
REMARK 465     PRO D   409                                                      
REMARK 465     GLU D   410                                                      
REMARK 465     GLY D   411                                                      
REMARK 465     ALA D   412                                                      
REMARK 465     ASN D   413                                                      
REMARK 465     LYS D   414                                                      
REMARK 465     GLN D   415                                                      
REMARK 465     ASP D   416                                                      
REMARK 465     LEU D   417                                                      
REMARK 465     ILE D   418                                                      
REMARK 465     THR D   419                                                      
REMARK 465     ALA D   420                                                      
REMARK 465     LEU D   421                                                      
REMARK 465     VAL D   422                                                      
REMARK 465     SER D   423                                                      
REMARK 465     ARG D   424                                                      
REMARK 465     GLU D   425                                                      
REMARK 465     LYS D   426                                                      
REMARK 465     VAL D   427                                                      
REMARK 465     SER D   428                                                      
REMARK 465     ASP D   429                                                      
REMARK 465     SER D   430                                                      
REMARK 465     ASN D   431                                                      
REMARK 465     ILE D   432                                                      
REMARK 465     ASN D   433                                                      
REMARK 465     MET D   434                                                      
REMARK 465     VAL D   435                                                      
REMARK 465     ASN D   436                                                      
REMARK 465     LYS D   437                                                      
REMARK 465     HIS D   438                                                      
REMARK 465     LYS D   439                                                      
REMARK 465     PHE D   440                                                      
REMARK 465     SER D   441                                                      
REMARK 465     HIS D   442                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     PRO E     4                                                      
REMARK 465     LEU E     5                                                      
REMARK 465     ILE E     6                                                      
REMARK 465     TYR E     7                                                      
REMARK 465     VAL E     8                                                      
REMARK 465     MET E     9                                                      
REMARK 465     LEU E    10                                                      
REMARK 465     VAL E    11                                                      
REMARK 465     LEU E    12                                                      
REMARK 465     LEU E    13                                                      
REMARK 465     ASN E    14                                                      
REMARK 465     VAL E    15                                                      
REMARK 465     PHE E    16                                                      
REMARK 465     VAL E    17                                                      
REMARK 465     PHE E    18                                                      
REMARK 465     SER E    19                                                      
REMARK 465     SER E    20                                                      
REMARK 465     GLY E    21                                                      
REMARK 465     ASN E   321                                                      
REMARK 465     ARG E   322                                                      
REMARK 465     THR E   323                                                      
REMARK 465     LEU E   324                                                      
REMARK 465     SER E   325                                                      
REMARK 465     GLU E   326                                                      
REMARK 465     THR E   347                                                      
REMARK 465     ILE E   348                                                      
REMARK 465     LYS E   349                                                      
REMARK 465     ASN E   350                                                      
REMARK 465     GLU E   351                                                      
REMARK 465     LYS E   352                                                      
REMARK 465     PRO E  1087                                                      
REMARK 465     LEU E  1088                                                      
REMARK 465     LYS E  1089                                                      
REMARK 465     ALA E  1090                                                      
REMARK 465     LEU E  1091                                                      
REMARK 465     LYS E  1092                                                      
REMARK 465     LYS E  1093                                                      
REMARK 465     SER E  1094                                                      
REMARK 465     ILE E  1095                                                      
REMARK 465     ARG E  1096                                                      
REMARK 465     GLY E  1097                                                      
REMARK 465     ASN E  1098                                                      
REMARK 465     PRO E  1099                                                      
REMARK 465     GLY E  1100                                                      
REMARK 465     LEU E  1101                                                      
REMARK 465     THR E  1102                                                      
REMARK 465     SER E  1103                                                      
REMARK 465     SER E  1104                                                      
REMARK 465     THR E  1105                                                      
REMARK 465     THR E  1106                                                      
REMARK 465     VAL E  1107                                                      
REMARK 465     SER E  1108                                                      
REMARK 465     SER E  1109                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     ARG F     4                                                      
REMARK 465     PRO F     5                                                      
REMARK 465     ALA F     6                                                      
REMARK 465     MET F     7                                                      
REMARK 465     SER F     8                                                      
REMARK 465     PRO F     9                                                      
REMARK 465     VAL F    10                                                      
REMARK 465     SER F    11                                                      
REMARK 465     PRO F    12                                                      
REMARK 465     VAL F    13                                                      
REMARK 465     TRP F    14                                                      
REMARK 465     PRO F    15                                                      
REMARK 465     ARG F    16                                                      
REMARK 465     LYS F    17                                                      
REMARK 465     PRO F    18                                                      
REMARK 465     ASN F    19                                                      
REMARK 465     LEU F    20                                                      
REMARK 465     TRP F    21                                                      
REMARK 465     ALA F    22                                                      
REMARK 465     PHE F    23                                                      
REMARK 465     TRP F    24                                                      
REMARK 465     VAL F    25                                                      
REMARK 465     LEU F    26                                                      
REMARK 465     ARG F    27                                                      
REMARK 465     LEU F    28                                                      
REMARK 465     VAL F    29                                                      
REMARK 465     LEU F    30                                                      
REMARK 465     LEU F    31                                                      
REMARK 465     LEU F    32                                                      
REMARK 465     SER F    33                                                      
REMARK 465     LEU F    34                                                      
REMARK 465     LYS F    35                                                      
REMARK 465     SER F    36                                                      
REMARK 465     TRP F    37                                                      
REMARK 465     ALA F    38                                                      
REMARK 465     GLU F    39                                                      
REMARK 465     ASP F    40                                                      
REMARK 465     ALA F    41                                                      
REMARK 465     LEU F    42                                                      
REMARK 465     GLN F    43                                                      
REMARK 465     VAL F  1086                                                      
REMARK 465     TRP F  1087                                                      
REMARK 465     PRO F  1088                                                      
REMARK 465     HIS F  1089                                                      
REMARK 465     ILE F  1090                                                      
REMARK 465     VAL F  1091                                                      
REMARK 465     LYS F  1092                                                      
REMARK 465     ALA F  1093                                                      
REMARK 465     TRP F  1094                                                      
REMARK 465     VAL F  1095                                                      
REMARK 465     SER F  1096                                                      
REMARK 465     LEU F  1097                                                      
REMARK 465     ARG F  1098                                                      
REMARK 465     TRP F  1099                                                      
REMARK 465     ARG F  1100                                                      
REMARK 465     ILE F  1101                                                      
REMARK 465     ASN F  1102                                                      
REMARK 465     ASN F  1103                                                      
REMARK 465     ILE F  1104                                                      
REMARK 465     MET F  1105                                                      
REMARK 465     ALA F  1106                                                      
REMARK 465     SER F  1107                                                      
REMARK 465     GLU F  1108                                                      
REMARK 465     SER F  1109                                                      
REMARK 465     TYR F  1110                                                      
REMARK 465     TYR F  1111                                                      
REMARK 465     THR F  1112                                                      
REMARK 465     TYR F  1113                                                      
REMARK 465     ALA F  1114                                                      
REMARK 465     SER F  1115                                                      
REMARK 465     SER F  1116                                                      
REMARK 465     THR F  1117                                                      
REMARK 465     ALA F  1118                                                      
REMARK 465     GLY F  1119                                                      
REMARK 465     PHE F  1120                                                      
REMARK 465     SER F  1121                                                      
REMARK 465     LEU F  1122                                                      
REMARK 465     GLN F  1123                                                      
REMARK 465     SER F  1124                                                      
REMARK 465     HIS F  1125                                                      
REMARK 465     SER F  1126                                                      
REMARK 465     PHE F  1127                                                      
REMARK 465     GLU F  1128                                                      
REMARK 465     GLY F  1129                                                      
REMARK 465     PRO F  1130                                                      
REMARK 465     SER F  1131                                                      
REMARK 465     ARG F  1132                                                      
REMARK 465     ALA F  1133                                                      
REMARK 465     GLY F  1134                                                      
REMARK 465     SER F  1135                                                      
REMARK 465     LYS F  1136                                                      
REMARK 465     GLU F  1137                                                      
REMARK 465     ASP F  1138                                                      
REMARK 465     ASN F  1139                                                      
REMARK 465     VAL F  1140                                                      
REMARK 465     GLN F  1141                                                      
REMARK 465     ALA F  1142                                                      
REMARK 465     LYS F  1143                                                      
REMARK 465     THR F  1144                                                      
REMARK 465     ALA F  1145                                                      
REMARK 465     MET G     1                                                      
REMARK 465     LEU G     2                                                      
REMARK 465     VAL G     3                                                      
REMARK 465     LEU G     4                                                      
REMARK 465     MET G     5                                                      
REMARK 465     LEU G     6                                                      
REMARK 465     ALA G     7                                                      
REMARK 465     ALA G     8                                                      
REMARK 465     ALA G     9                                                      
REMARK 465     VAL G    10                                                      
REMARK 465     ALA G    11                                                      
REMARK 465     THR G    12                                                      
REMARK 465     MET G    13                                                      
REMARK 465     VAL G    14                                                      
REMARK 465     ARG G    15                                                      
REMARK 465     ALA G    16                                                      
REMARK 465     PRO G   547                                                      
REMARK 465     ILE G   548                                                      
REMARK 465     ASN G   549                                                      
REMARK 465     HIS G   550                                                      
REMARK 465     ASN G   551                                                      
REMARK 465     GLY G   552                                                      
REMARK 465     GLU G   553                                                      
REMARK 465     ALA G   554                                                      
REMARK 465     GLN G   555                                                      
REMARK 465     GLU G   632                                                      
REMARK 465     SER G   633                                                      
REMARK 465     ASP G   634                                                      
REMARK 465     ILE G   635                                                      
REMARK 465     GLU G   636                                                      
REMARK 465     ASN G   637                                                      
REMARK 465     GLU G   638                                                      
REMARK 465     GLU G   639                                                      
REMARK 465     PRO G   640                                                      
REMARK 465     PHE G   641                                                      
REMARK 465     GLU G   750                                                      
REMARK 465     LYS G   751                                                      
REMARK 465     GLY G   752                                                      
REMARK 465     GLN G   753                                                      
REMARK 465     ARG G   754                                                      
REMARK 465     LEU G   755                                                      
REMARK 465     LEU G   756                                                      
REMARK 465     GLY G   757                                                      
REMARK 465     PHE G   758                                                      
REMARK 465     CYS G   759                                                      
REMARK 465     TYR G   760                                                      
REMARK 465     GLN G   761                                                      
REMARK 465     ILE G   762                                                      
REMARK 465     LEU G   763                                                      
REMARK 465     GLN G   764                                                      
REMARK 465     LEU G   765                                                      
REMARK 465     CYS G   766                                                      
REMARK 465     LEU G   767                                                      
REMARK 465     GLY G   768                                                      
REMARK 465     VAL G   769                                                      
REMARK 465     CYS G   770                                                      
REMARK 465     PHE G   771                                                      
REMARK 465     CYS G   772                                                      
REMARK 465     THR G   773                                                      
REMARK 465     TRP G   774                                                      
REMARK 465     LEU G   775                                                      
REMARK 465     ARG G   776                                                      
REMARK 465     GLY G   777                                                      
REMARK 465     LYS G   778                                                      
REMARK 465     LEU G   779                                                      
REMARK 465     ARG G   780                                                      
REMARK 465     GLN G   781                                                      
REMARK 465     TRP G   782                                                      
REMARK 465     LEU G   783                                                      
REMARK 465     ARG G   784                                                      
REMARK 465     PRO G   785                                                      
REMARK 465     ARG G   786                                                      
REMARK 465     ARG G   787                                                      
REMARK 465     VAL G   788                                                      
REMARK 465     LYS G   789                                                      
REMARK 465     ASP G   790                                                      
REMARK 465     GLN G   791                                                      
REMARK 465     ASN G   792                                                      
REMARK 465     ARG G   793                                                      
REMARK 465     GLY G   794                                                      
REMARK 465     LYS G   795                                                      
REMARK 465     VAL G   796                                                      
REMARK 465     ARG G   797                                                      
REMARK 465     VAL G   798                                                      
REMARK 465     ALA G   799                                                      
REMARK 465     GLN G   800                                                      
REMARK 465     LYS G   801                                                      
REMARK 465     HIS G   802                                                      
REMARK 465     PRO G   803                                                      
REMARK 465     GLU G   804                                                      
REMARK 465     THR G   805                                                      
REMARK 465     MET H     1                                                      
REMARK 465     PRO H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     ALA H     4                                                      
REMARK 465     GLY H     5                                                      
REMARK 465     GLN H     6                                                      
REMARK 465     ARG H     7                                                      
REMARK 465     LYS H     8                                                      
REMARK 465     PRO H     9                                                      
REMARK 465     GLY H    10                                                      
REMARK 465     SER H    11                                                      
REMARK 465     LEU H    12                                                      
REMARK 465     LEU H    13                                                      
REMARK 465     ALA H    14                                                      
REMARK 465     LEU H    15                                                      
REMARK 465     GLN H    16                                                      
REMARK 465     ALA H    17                                                      
REMARK 465     LEU H    18                                                      
REMARK 465     GLN H    19                                                      
REMARK 465     LYS H    20                                                      
REMARK 465     TRP H    21                                                      
REMARK 465     LEU H    22                                                      
REMARK 465     LEU H    23                                                      
REMARK 465     ARG H    24                                                      
REMARK 465     GLY H    25                                                      
REMARK 465     GLY H    26                                                      
REMARK 465     VAL H    27                                                      
REMARK 465     GLY H    28                                                      
REMARK 465     ALA H    29                                                      
REMARK 465     MET H    30                                                      
REMARK 465     LEU H    31                                                      
REMARK 465     ALA H    32                                                      
REMARK 465     ARG H    33                                                      
REMARK 465     GLN H    34                                                      
REMARK 465     VAL H    35                                                      
REMARK 465     VAL H    36                                                      
REMARK 465     ALA H    37                                                      
REMARK 465     ALA H    38                                                      
REMARK 465     LEU H    39                                                      
REMARK 465     LEU H    40                                                      
REMARK 465     LEU H    41                                                      
REMARK 465     TRP H    42                                                      
REMARK 465     LEU H    43                                                      
REMARK 465     SER H    44                                                      
REMARK 465     CYS H    45                                                      
REMARK 465     CYS H    46                                                      
REMARK 465     VAL H    47                                                      
REMARK 465     SER H    48                                                      
REMARK 465     ALA H    49                                                      
REMARK 465     ARG H   768                                                      
REMARK 465     GLU H   769                                                      
REMARK 465     SER H   770                                                      
REMARK 465     LEU H   771                                                      
REMARK 465     SER H   772                                                      
REMARK 465     ILE H   971                                                      
REMARK 465     ILE H   972                                                      
REMARK 465     GLU H   973                                                      
REMARK 465     PRO H   974                                                      
REMARK 465     LEU H   975                                                      
REMARK 465     HIS H   976                                                      
REMARK 465     LYS H   977                                                      
REMARK 465     ARG H   978                                                      
REMARK 465     PRO H   979                                                      
REMARK 465     ALA H   980                                                      
REMARK 465     LYS H   981                                                      
REMARK 465     GLN H   982                                                      
REMARK 465     LYS H   983                                                      
REMARK 465     LYS H   984                                                      
REMARK 465     ASN H   985                                                      
REMARK 465     MET L     1                                                      
REMARK 465     ALA L     2                                                      
REMARK 465     HIS L     3                                                      
REMARK 465     VAL L     4                                                      
REMARK 465     ARG L     5                                                      
REMARK 465     ASN L     6                                                      
REMARK 465     LYS L     7                                                      
REMARK 465     LYS L     8                                                      
REMARK 465     SER L     9                                                      
REMARK 465     ASP L    10                                                      
REMARK 465     ASP L    11                                                      
REMARK 465     LYS L    12                                                      
REMARK 465     LYS L    13                                                      
REMARK 465     ALA L    14                                                      
REMARK 465     MET L    15                                                      
REMARK 465     VAL L    16                                                      
REMARK 465     VAL L    17                                                      
REMARK 465     ALA L    18                                                      
REMARK 465     LYS L    19                                                      
REMARK 465     GLU L    20                                                      
REMARK 465     ASP L    21                                                      
REMARK 465     THR L    22                                                      
REMARK 465     ASN L    23                                                      
REMARK 465     LYS L    24                                                      
REMARK 465     SER L    25                                                      
REMARK 465     GLU L    26                                                      
REMARK 465     SER L    27                                                      
REMARK 465     GLU L    28                                                      
REMARK 465     GLY L    29                                                      
REMARK 465     VAL L    30                                                      
REMARK 465     THR L    31                                                      
REMARK 465     LYS L    32                                                      
REMARK 465     LEU L    33                                                      
REMARK 465     GLN L    34                                                      
REMARK 465     THR L    35                                                      
REMARK 465     TYR L    36                                                      
REMARK 465     LEU L    37                                                      
REMARK 465     LYS L    38                                                      
REMARK 465     THR L    39                                                      
REMARK 465     ILE L    40                                                      
REMARK 465     PRO L    41                                                      
REMARK 465     ILE L    42                                                      
REMARK 465     ALA L    43                                                      
REMARK 465     LYS L    44                                                      
REMARK 465     LYS L    45                                                      
REMARK 465     LYS L    46                                                      
REMARK 465     PHE L    47                                                      
REMARK 465     ALA L    48                                                      
REMARK 465     LYS L    49                                                      
REMARK 465     LEU L    50                                                      
REMARK 465     PRO L    51                                                      
REMARK 465     LYS L    52                                                      
REMARK 465     ARG L    53                                                      
REMARK 465     LYS L    54                                                      
REMARK 465     LYS L    55                                                      
REMARK 465     SER L    56                                                      
REMARK 465     PRO L    57                                                      
REMARK 465     THR L    58                                                      
REMARK 465     SER L    59                                                      
REMARK 465     ALA L    60                                                      
REMARK 465     GLU L    61                                                      
REMARK 465     LEU L    62                                                      
REMARK 465     LEU L    63                                                      
REMARK 465     LEU L    64                                                      
REMARK 465     ILE L    65                                                      
REMARK 465     ASP L    66                                                      
REMARK 465     PRO L    67                                                      
REMARK 465     ARG L    68                                                      
REMARK 465     TYR L    69                                                      
REMARK 465     SER L    70                                                      
REMARK 465     ALA L    71                                                      
REMARK 465     SER L    72                                                      
REMARK 465     LYS L    73                                                      
REMARK 465     GLU L    74                                                      
REMARK 465     GLY L    75                                                      
REMARK 465     PRO L    76                                                      
REMARK 465     LEU L    77                                                      
REMARK 465     GLY L    78                                                      
REMARK 465     LEU L    79                                                      
REMARK 465     GLY L    80                                                      
REMARK 465     PRO L   342                                                      
REMARK 465     PRO L   343                                                      
REMARK 465     THR L   344                                                      
REMARK 465     ILE L   345                                                      
REMARK 465     ASP L   346                                                      
REMARK 465     ARG L   347                                                      
REMARK 465     ARG L   348                                                      
REMARK 465     LEU L   349                                                      
REMARK 465     LYS L   350                                                      
REMARK 465     ASP L   351                                                      
REMARK 465     MET L   352                                                      
REMARK 465     LYS L   353                                                      
REMARK 465     ILE L   354                                                      
REMARK 465     SER L   691                                                      
REMARK 465     LYS L   692                                                      
REMARK 465     THR L   693                                                      
REMARK 465     THR L   694                                                      
REMARK 465     VAL L   695                                                      
REMARK 465     LYS L   696                                                      
REMARK 465     ASP L   697                                                      
REMARK 465     VAL L   698                                                      
REMARK 465     LYS L   699                                                      
REMARK 465     GLU L   700                                                      
REMARK 465     GLN L   701                                                      
REMARK 465     LYS L   702                                                      
REMARK 465     GLU L   703                                                      
REMARK 465     ARG L   704                                                      
REMARK 465     LYS L   705                                                      
REMARK 465     ALA L   706                                                      
REMARK 465     ILE J    42                                                      
REMARK 465     GLU J   108                                                      
REMARK 465     ARG J   109                                                      
REMARK 465     SER J   165                                                      
REMARK 465     VAL J   166                                                      
REMARK 465     ASN J   167                                                      
REMARK 465     ASP J   168                                                      
REMARK 465     LEU J   169                                                      
REMARK 465     ASP J   170                                                      
REMARK 465     VAL J   171                                                      
REMARK 465     ARG I   175                                                      
REMARK 465     LYS I   176                                                      
REMARK 465     LYS I   177                                                      
REMARK 465     ARG I   178                                                      
REMARK 465     ARG I   179                                                      
REMARK 465     LYS I   180                                                      
REMARK 465     ASP I   181                                                      
REMARK 465     ARG I   182                                                      
REMARK 465     GLU I   183                                                      
REMARK 465     ALA I   184                                                      
REMARK 465     ALA I   185                                                      
REMARK 465     ARG I   186                                                      
REMARK 465     GLU I   187                                                      
REMARK 465     ARG I   188                                                      
REMARK 465     GLU I   189                                                      
REMARK 465     LYS I   190                                                      
REMARK 465     GLU I   191                                                      
REMARK 465     LYS I   192                                                      
REMARK 465     GLY I   193                                                      
REMARK 465     LYS I   194                                                      
REMARK 465     ASP I   195                                                      
REMARK 465     LYS I   196                                                      
REMARK 465     GLU I   197                                                      
REMARK 465     LYS I   198                                                      
REMARK 465     TYR I   199                                                      
REMARK 465     LEU I   200                                                      
REMARK 465     HIS I   201                                                      
REMARK 465     LEU I   202                                                      
REMARK 465     LYS I   203                                                      
REMARK 465     LYS I   204                                                      
REMARK 465     ILE I   205                                                      
REMARK 465     TYR I   206                                                      
REMARK 465     SER I   207                                                      
REMARK 465     SER I   208                                                      
REMARK 465     MET I   209                                                      
REMARK 465     LEU I   210                                                      
REMARK 465     SER I   211                                                      
REMARK 465     HIS I   212                                                      
REMARK 465     ARG I   213                                                      
REMARK 465     SER I   214                                                      
REMARK 465     ILE I   215                                                      
REMARK 465     LEU I   216                                                      
REMARK 465     MET K     1                                                      
REMARK 465     GLU K     2                                                      
REMARK 465     GLU K     3                                                      
REMARK 465     SER K     4                                                      
REMARK 465     VAL K     5                                                      
REMARK 465     LYS K     6                                                      
REMARK 465     PRO K     7                                                      
REMARK 465     VAL K     8                                                      
REMARK 465     PRO K     9                                                      
REMARK 465     LYS K    10                                                      
REMARK 465     HIS K    11                                                      
REMARK 465     ALA K    12                                                      
REMARK 465     ASN K    13                                                      
REMARK 465     HIS K    14                                                      
REMARK 465     ARG K    15                                                      
REMARK 465     ARG K    16                                                      
REMARK 465     SER K    17                                                      
REMARK 465     SER K    18                                                      
REMARK 465     VAL K    19                                                      
REMARK 465     ARG K    20                                                      
REMARK 465     SER K    21                                                      
REMARK 465     SER K    22                                                      
REMARK 465     LEU K    23                                                      
REMARK 465     TYR K    24                                                      
REMARK 465     GLY K    25                                                      
REMARK 465     ASP K    26                                                      
REMARK 465     VAL K    27                                                      
REMARK 465     ARG K    28                                                      
REMARK 465     ASP K    29                                                      
REMARK 465     LEU K    30                                                      
REMARK 465     TRP K    31                                                      
REMARK 465     SER K    32                                                      
REMARK 465     THR K    33                                                      
REMARK 465     ALA K    34                                                      
REMARK 465     THR K    35                                                      
REMARK 465     MET K    36                                                      
REMARK 465     SER K    37                                                      
REMARK 465     ARG K   136                                                      
REMARK 465     LEU K   137                                                      
REMARK 465     PRO K   138                                                      
REMARK 465     THR K   163                                                      
REMARK 465     ILE K   164                                                      
REMARK 465     GLY K   165                                                      
REMARK 465     LYS K   187                                                      
REMARK 465     ARG K   188                                                      
REMARK 465     LEU K   189                                                      
REMARK 465     TYR K   190                                                      
REMARK 465     PHE K   191                                                      
REMARK 465     LEU K   192                                                      
REMARK 465     ASP K   193                                                      
REMARK 465     GLN K   194                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET J   1    CG   SD   CE                                        
REMARK 470     LEU J   2    CG   CD1  CD2                                       
REMARK 470     PHE J   3    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE J   4    CG1  CG2  CD1                                       
REMARK 470     ILE J   5    CG1  CG2  CD1                                       
REMARK 470     CYS J   6    SG                                                  
REMARK 470     LEU J   7    CG   CD1  CD2                                       
REMARK 470     VAL J   8    CG1  CG2                                            
REMARK 470     PHE J   9    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE J  10    CG1  CG2  CD1                                       
REMARK 470     SER J  11    OG                                                  
REMARK 470     CYS J  12    SG                                                  
REMARK 470     ASN J  13    CG   OD1  ND2                                       
REMARK 470     VAL J  14    CG1  CG2                                            
REMARK 470     LEU J  15    CG   CD1  CD2                                       
REMARK 470     ARG J  16    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU J  17    CG   CD   OE1  OE2                                  
REMARK 470     VAL J  18    CG1  CG2                                            
REMARK 470     LYS J  19    CG   CD   CE   NZ                                   
REMARK 470     TYR J  20    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN J  21    CG   CD   OE1  NE2                                  
REMARK 470     GLU J  22    CG   CD   OE1  OE2                                  
REMARK 470     THR J  23    OG1  CG2                                            
REMARK 470     TRP J  24    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP J  24    CZ3  CH2                                            
REMARK 470     CYS J  25    SG                                                  
REMARK 470     PHE J  26    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PRO J  27    CG   CD                                             
REMARK 470     TYR J  29    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET J  31    CG   SD   CE                                        
REMARK 470     VAL J  32    CG1  CG2                                            
REMARK 470     ILE J  33    CG1  CG2  CD1                                       
REMARK 470     LEU J  35    CG   CD1  CD2                                       
REMARK 470     TRP J  36    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP J  36    CZ3  CH2                                            
REMARK 470     LEU J  37    CG   CD1  CD2                                       
REMARK 470     MET J  38    CG   SD   CE                                        
REMARK 470     LEU J  39    CG   CD1  CD2                                       
REMARK 470     SER J  40    OG                                                  
REMARK 470     SER J  41    OG                                                  
REMARK 470     PRO J  43    CG   CD                                             
REMARK 470     GLN J  44    CG   CD   OE1  NE2                                  
REMARK 470     ARG J  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG J  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU J  47    CG   CD1  CD2                                       
REMARK 470     VAL J  48    CG1  CG2                                            
REMARK 470     LEU J  49    CG   CD1  CD2                                       
REMARK 470     ASN J  50    CG   OD1  ND2                                       
REMARK 470     HIS J  51    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR J  52    OG1  CG2                                            
REMARK 470     ARG J  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET J  55    CG   SD   CE                                        
REMARK 470     TYR J  56    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS J  57    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE J  58    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER J  59    OG                                                  
REMARK 470     ILE J  60    CG1  CG2  CD1                                       
REMARK 470     GLN J  61    CG   CD   OE1  NE2                                  
REMARK 470     ARG J  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR J  64    OG1  CG2                                            
REMARK 470     VAL J  65    CG1  CG2                                            
REMARK 470     CYS J  66    SG                                                  
REMARK 470     GLN J  67    CG   CD   OE1  NE2                                  
REMARK 470     PRO J  69    CG   CD                                             
REMARK 470     MET J  70    CG   SD   CE                                        
REMARK 470     HIS J  71    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU J  72    CG   CD1  CD2                                       
REMARK 470     VAL J  73    CG1  CG2                                            
REMARK 470     TYR J  74    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL J  75    CG1  CG2                                            
REMARK 470     ARG J  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU J  77    CG   CD1  CD2                                       
REMARK 470     LEU J  79    CG   CD1  CD2                                       
REMARK 470     SER J  80    OG                                                  
REMARK 470     SER J  81    OG                                                  
REMARK 470     ASP J  82    CG   OD1  OD2                                       
REMARK 470     TYR J  84    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG J  87    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE J  88    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE J  89    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN J  90    CG   CD   OE1  NE2                                  
REMARK 470     LEU J  91    CG   CD1  CD2                                       
REMARK 470     VAL J  92    CG1  CG2                                            
REMARK 470     LEU J  93    CG   CD1  CD2                                       
REMARK 470     CYS J  94    SG                                                  
REMARK 470     HIS J  96    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS J  97    CG   CD   CE   NZ                                   
REMARK 470     LEU J  98    CG   CD1  CD2                                       
REMARK 470     GLU J  99    CG   CD   OE1  OE2                                  
REMARK 470     PRO J 100    CG   CD                                             
REMARK 470     LEU J 101    CG   CD1  CD2                                       
REMARK 470     VAL J 102    CG1  CG2                                            
REMARK 470     LEU J 103    CG   CD1  CD2                                       
REMARK 470     VAL J 104    CG1  CG2                                            
REMARK 470     GLN J 105    CG   CD   OE1  NE2                                  
REMARK 470     LEU J 106    CG   CD1  CD2                                       
REMARK 470     SER J 107    OG                                                  
REMARK 470     TYR J 110    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU J 111    CG   CD   OE1  OE2                                  
REMARK 470     GLN J 112    CG   CD   OE1  NE2                                  
REMARK 470     MET J 113    CG   SD   CE                                        
REMARK 470     GLU J 114    CG   CD   OE1  OE2                                  
REMARK 470     PHE J 115    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU J 116    CG   CD1  CD2                                       
REMARK 470     ARG J 118    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS J 119    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU J 120    CG   CD1  CD2                                       
REMARK 470     ARG J 122    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J 123    CG   CD   CE   NZ                                   
REMARK 470     LEU J 124    CG   CD1  CD2                                       
REMARK 470     ASN J 125    CG   OD1  ND2                                       
REMARK 470     ILE J 126    CG1  CG2  CD1                                       
REMARK 470     ASN J 127    CG   OD1  ND2                                       
REMARK 470     TYR J 128    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE J 129    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP J 130    CG   OD1  OD2                                       
REMARK 470     TYR J 131    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU J 132    CG   CD1  CD2                                       
REMARK 470     SER J 134    OG                                                  
REMARK 470     SER J 135    OG                                                  
REMARK 470     TYR J 136    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG J 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS J 138    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL J 139    CG1  CG2                                            
REMARK 470     VAL J 140    CG1  CG2                                            
REMARK 470     ARG J 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS J 142    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP J 143    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP J 143    CZ3  CH2                                            
REMARK 470     PRO J 144    CG   CD                                             
REMARK 470     LEU J 145    CG   CD1  CD2                                       
REMARK 470     SER J 148    OG                                                  
REMARK 470     PHE J 149    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER J 150    OG                                                  
REMARK 470     PRO J 151    CG   CD                                             
REMARK 470     ILE J 153    CG1  CG2  CD1                                       
REMARK 470     VAL J 154    CG1  CG2                                            
REMARK 470     GLN J 155    CG   CD   OE1  NE2                                  
REMARK 470     ARG J 156    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J 157    CG   CD   CE   NZ                                   
REMARK 470     THR J 158    OG1  CG2                                            
REMARK 470     GLN J 159    CG   CD   OE1  NE2                                  
REMARK 470     VAL J 160    CG1  CG2                                            
REMARK 470     TYR J 161    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR J 162    OG1  CG2                                            
REMARK 470     LYS J 163    CG   CD   CE   NZ                                   
REMARK 470     SER J 164    OG                                                  
REMARK 470     MET I   1    CG   SD   CE                                        
REMARK 470     LYS I   2    CG   CD   CE   NZ                                   
REMARK 470     LEU I   3    CG   CD1  CD2                                       
REMARK 470     THR I   4    OG1  CG2                                            
REMARK 470     PRO I   5    CG   CD                                             
REMARK 470     CYS I   7    SG                                                  
REMARK 470     PHE I   8    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU I   9    CG   CD1  CD2                                       
REMARK 470     TRP I  10    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP I  10    CZ3  CH2                                            
REMARK 470     TYR I  11    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU I  12    CG   CD1  CD2                                       
REMARK 470     TYR I  13    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET I  14    CG   SD   CE                                        
REMARK 470     ASP I  15    CG   OD1  OD2                                       
REMARK 470     LYS I  16    CG   CD   CE   NZ                                   
REMARK 470     ILE I  17    CG1  CG2  CD1                                       
REMARK 470     TYR I  18    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     CYS I  19    SG                                                  
REMARK 470     LEU I  20    CG   CD1  CD2                                       
REMARK 470     LEU I  21    CG   CD1  CD2                                       
REMARK 470     SER I  22    OG                                                  
REMARK 470     LEU I  23    CG   CD1  CD2                                       
REMARK 470     ARG I  24    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN I  25    CG   OD1  ND2                                       
REMARK 470     VAL I  26    CG1  CG2                                            
REMARK 470     LYS I  27    CG   CD   CE   NZ                                   
REMARK 470     LEU I  29    CG   CD1  CD2                                       
REMARK 470     MET I  30    CG   SD   CE                                        
REMARK 470     VAL I  31    CG1  CG2                                            
REMARK 470     TYR I  32    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE I  33    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS I  34    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU I  35    CG   CD1  CD2                                       
REMARK 470     LEU I  36    CG   CD1  CD2                                       
REMARK 470     ASP I  37    CG   OD1  OD2                                       
REMARK 470     VAL I  38    CG1  CG2                                            
REMARK 470     HIS I  39    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS I  40    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG I  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN I  42    CG   OD1  ND2                                       
REMARK 470     THR I  43    OG1  CG2                                            
REMARK 470     LEU I  44    CG   CD1  CD2                                       
REMARK 470     ASN I  45    CG   OD1  ND2                                       
REMARK 470     ASP I  46    CG   OD1  OD2                                       
REMARK 470     VAL I  47    CG1  CG2                                            
REMARK 470     LEU I  48    CG   CD1  CD2                                       
REMARK 470     PHE I  49    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE I  50    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS I  51    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE I  52    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU I  53    CG   CD1  CD2                                       
REMARK 470     GLN I  54    CG   CD   OE1  NE2                                  
REMARK 470     HIS I  55    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL I  56    CG1  CG2                                            
REMARK 470     THR I  57    OG1  CG2                                            
REMARK 470     ASN I  58    CG   OD1  ND2                                       
REMARK 470     LEU I  59    CG   CD1  CD2                                       
REMARK 470     ASN I  60    CG   OD1  ND2                                       
REMARK 470     LYS I  61    CG   CD   CE   NZ                                   
REMARK 470     SER I  62    OG                                                  
REMARK 470     GLN I  63    CG   CD   OE1  NE2                                  
REMARK 470     ILE I  64    CG1  CG2  CD1                                       
REMARK 470     MET I  66    CG   SD   CE                                        
REMARK 470     ILE I  67    CG1  CG2  CD1                                       
REMARK 470     PHE I  68    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP I  69    CG   OD1  OD2                                       
REMARK 470     LEU I  70    CG   CD1  CD2                                       
REMARK 470     LEU I  71    CG   CD1  CD2                                       
REMARK 470     ASP I  72    CG   OD1  OD2                                       
REMARK 470     TRP I  73    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP I  73    CZ3  CH2                                            
REMARK 470     THR I  74    OG1  CG2                                            
REMARK 470     VAL I  76    CG1  CG2                                            
REMARK 470     GLU I  78    CG   CD   OE1  OE2                                  
REMARK 470     ILE I  79    CG1  CG2  CD1                                       
REMARK 470     PHE I  81    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP I  82    CG   OD1  OD2                                       
REMARK 470     GLN I  83    CG   CD   OE1  NE2                                  
REMARK 470     PHE I  84    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR I  85    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL I  86    CG1  CG2                                            
REMARK 470     LEU I  87    CG   CD1  CD2                                       
REMARK 470     ILE I  88    CG1  CG2  CD1                                       
REMARK 470     CYS I  89    SG                                                  
REMARK 470     ILE I  90    CG1  CG2  CD1                                       
REMARK 470     LEU I  91    CG   CD1  CD2                                       
REMARK 470     LEU I  92    CG   CD1  CD2                                       
REMARK 470     HIS I  94    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN I  95    CG   CD   OE1  NE2                                  
REMARK 470     ASP I  96    CG   OD1  OD2                                       
REMARK 470     HIS I  97    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU I  98    CG   CD1  CD2                                       
REMARK 470     GLU I  99    CG   CD   OE1  OE2                                  
REMARK 470     ASP I 100    CG   OD1  OD2                                       
REMARK 470     HIS I 101    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE I 102    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET I 103    CG   SD   CE                                        
REMARK 470     TYR I 104    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG I 105    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS I 106    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER I 107    OG                                                  
REMARK 470     ARG I 108    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO I 109    CG   CD                                             
REMARK 470     VAL I 110    CG1  CG2                                            
REMARK 470     PHE I 111    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU I 112    CG   CD   OE1  OE2                                  
REMARK 470     LEU I 113    CG   CD1  CD2                                       
REMARK 470     LEU I 114    CG   CD1  CD2                                       
REMARK 470     ASP I 115    CG   OD1  OD2                                       
REMARK 470     LEU I 116    CG   CD1  CD2                                       
REMARK 470     ASP I 117    CG   OD1  OD2                                       
REMARK 470     GLU I 119    CG   CD   OE1  OE2                                  
REMARK 470     MET I 120    CG   SD   CE                                        
REMARK 470     ASN I 121    CG   OD1  ND2                                       
REMARK 470     ILE I 122    CG1  CG2  CD1                                       
REMARK 470     ASN I 126    CG   OD1  ND2                                       
REMARK 470     PHE I 127    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN I 128    CG   CD   OE1  NE2                                  
REMARK 470     ASN I 129    CG   OD1  ND2                                       
REMARK 470     TYR I 130    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG I 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE I 132    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU I 133    CG   CD1  CD2                                       
REMARK 470     PHE I 134    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN I 135    CG   OD1  ND2                                       
REMARK 470     ILE I 136    CG1  CG2  CD1                                       
REMARK 470     LYS I 137    CG   CD   CE   NZ                                   
REMARK 470     LYS I 138    CG   CD   CE   NZ                                   
REMARK 470     GLN I 139    CG   CD   OE1  NE2                                  
REMARK 470     GLU I 140    CG   CD   OE1  OE2                                  
REMARK 470     LEU I 141    CG   CD1  CD2                                       
REMARK 470     ARG I 142    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP I 143    CG   OD1  OD2                                       
REMARK 470     LEU I 144    CG   CD1  CD2                                       
REMARK 470     PHE I 145    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS I 146    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP I 147    CG   OD1  OD2                                       
REMARK 470     PHE I 148    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP I 149    CG   OD1  OD2                                       
REMARK 470     ILE I 150    CG1  CG2  CD1                                       
REMARK 470     THR I 151    OG1  CG2                                            
REMARK 470     ASP I 153    CG   OD1  OD2                                       
REMARK 470     ARG I 154    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU I 155    CG   CD1  CD2                                       
REMARK 470     LEU I 156    CG   CD1  CD2                                       
REMARK 470     ASN I 157    CG   OD1  ND2                                       
REMARK 470     TYR I 158    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS I 159    CG   CD   CE   NZ                                   
REMARK 470     GLU I 160    CG   CD   OE1  OE2                                  
REMARK 470     PHE I 161    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS I 162    CG   CD   CE   NZ                                   
REMARK 470     LEU I 163    CG   CD1  CD2                                       
REMARK 470     TYR I 164    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR I 165    OG1  CG2                                            
REMARK 470     ILE I 166    CG1  CG2  CD1                                       
REMARK 470     PHE I 167    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     CYS I 168    SG                                                  
REMARK 470     THR I 169    OG1  CG2                                            
REMARK 470     ASP I 170    CG   OD1  OD2                                       
REMARK 470     LYS I 171    CG   CD   CE   NZ                                   
REMARK 470     SER I 172    OG                                                  
REMARK 470     ILE I 173    CG1  CG2  CD1                                       
REMARK 470     ASP I 174    CG   OD1  OD2                                       
REMARK 470     THR K  38    OG1  CG2                                            
REMARK 470     ASN K  40    CG   OD1  ND2                                       
REMARK 470     VAL K  41    CG1  CG2                                            
REMARK 470     SER K  42    OG                                                  
REMARK 470     VAL K  43    CG1  CG2                                            
REMARK 470     SER K  44    OG                                                  
REMARK 470     ASP K  45    CG   OD1  OD2                                       
REMARK 470     VAL K  46    CG1  CG2                                            
REMARK 470     CYS K  47    SG                                                  
REMARK 470     GLU K  48    CG   CD   OE1  OE2                                  
REMARK 470     ASP K  49    CG   OD1  OD2                                       
REMARK 470     PHE K  50    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP K  51    CG   OD1  OD2                                       
REMARK 470     GLU K  52    CG   CD   OE1  OE2                                  
REMARK 470     GLU K  53    CG   CD   OE1  OE2                                  
REMARK 470     LYS K  55    CG   CD   CE   NZ                                   
REMARK 470     SER K  56    OG                                                  
REMARK 470     VAL K  57    CG1  CG2                                            
REMARK 470     ARG K  58    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN K  59    CG   OD1  ND2                                       
REMARK 470     ARG K  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE K  61    CG1  CG2  CD1                                       
REMARK 470     ARG K  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K  63    CG   CD   CE   NZ                                   
REMARK 470     TYR K  64    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER K  65    OG                                                  
REMARK 470     GLN K  66    CG   CD   OE1  NE2                                  
REMARK 470     THR K  67    OG1  CG2                                            
REMARK 470     ILE K  68    CG1  CG2  CD1                                       
REMARK 470     SER K  69    OG                                                  
REMARK 470     ILE K  70    CG1  CG2  CD1                                       
REMARK 470     ARG K  71    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP K  72    CG   OD1  OD2                                       
REMARK 470     SER K  73    OG                                                  
REMARK 470     LEU K  74    CG   CD1  CD2                                       
REMARK 470     ASN K  75    CG   OD1  ND2                                       
REMARK 470     LEU K  76    CG   CD1  CD2                                       
REMARK 470     GLU K  77    CG   CD   OE1  OE2                                  
REMARK 470     PRO K  78    CG   CD                                             
REMARK 470     GLU K  79    CG   CD   OE1  OE2                                  
REMARK 470     GLU K  80    CG   CD   OE1  OE2                                  
REMARK 470     ILE K  81    CG1  CG2  CD1                                       
REMARK 470     GLN K  82    CG   CD   OE1  NE2                                  
REMARK 470     GLN K  83    CG   CD   OE1  NE2                                  
REMARK 470     GLN K  84    CG   CD   OE1  NE2                                  
REMARK 470     ARG K  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG K  87    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU K  88    CG   CD   OE1  OE2                                  
REMARK 470     LEU K  89    CG   CD1  CD2                                       
REMARK 470     GLU K  90    CG   CD   OE1  OE2                                  
REMARK 470     LEU K  91    CG   CD1  CD2                                       
REMARK 470     CYS K  92    SG                                                  
REMARK 470     HIS K  93    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG K  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER K  96    OG                                                  
REMARK 470     LEU K  97    CG   CD1  CD2                                       
REMARK 470     GLU K  98    CG   CD   OE1  OE2                                  
REMARK 470     HIS K  99    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU K 101    CG   CD   OE1  OE2                                  
REMARK 470     ASP K 102    CG   OD1  OD2                                       
REMARK 470     HIS K 103    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU K 104    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 105    CG   CD   OE1  OE2                                  
REMARK 470     SER K 106    OG                                                  
REMARK 470     GLU K 107    CG   CD   OE1  OE2                                  
REMARK 470     THR K 108    OG1  CG2                                            
REMARK 470     SER K 109    OG                                                  
REMARK 470     LEU K 110    CG   CD1  CD2                                       
REMARK 470     SER K 112    OG                                                  
REMARK 470     SER K 113    OG                                                  
REMARK 470     THR K 114    OG1  CG2                                            
REMARK 470     SER K 115    OG                                                  
REMARK 470     GLU K 116    CG   CD   OE1  OE2                                  
REMARK 470     SER K 117    OG                                                  
REMARK 470     LEU K 118    CG   CD1  CD2                                       
REMARK 470     ILE K 119    CG1  CG2  CD1                                       
REMARK 470     PHE K 120    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER K 121    OG                                                  
REMARK 470     LEU K 122    CG   CD1  CD2                                       
REMARK 470     TRP K 123    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP K 123    CZ3  CH2                                            
REMARK 470     LYS K 124    CG   CD   CE   NZ                                   
REMARK 470     PRO K 125    CG   CD                                             
REMARK 470     HIS K 126    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG K 127    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR K 128    OG1  CG2                                            
REMARK 470     TYR K 129    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP K 130    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP K 130    CZ3  CH2                                            
REMARK 470     THR K 131    OG1  CG2                                            
REMARK 470     GLU K 132    CG   CD   OE1  OE2                                  
REMARK 470     GLN K 133    CG   CD   OE1  NE2                                  
REMARK 470     GLN K 134    CG   CD   OE1  NE2                                  
REMARK 470     ASN K 135    CG   OD1  ND2                                       
REMARK 470     LEU K 139    CG   CD1  CD2                                       
REMARK 470     PRO K 140    CG   CD                                             
REMARK 470     LEU K 141    CG   CD1  CD2                                       
REMARK 470     MET K 142    CG   SD   CE                                        
REMARK 470     GLU K 143    CG   CD   OE1  OE2                                  
REMARK 470     LEU K 144    CG   CD1  CD2                                       
REMARK 470     MET K 145    CG   SD   CE                                        
REMARK 470     GLU K 146    CG   CD   OE1  OE2                                  
REMARK 470     THR K 147    OG1  CG2                                            
REMARK 470     GLU K 148    CG   CD   OE1  OE2                                  
REMARK 470     VAL K 149    CG1  CG2                                            
REMARK 470     LEU K 150    CG   CD1  CD2                                       
REMARK 470     ASP K 151    CG   OD1  OD2                                       
REMARK 470     ILE K 152    CG1  CG2  CD1                                       
REMARK 470     LEU K 153    CG   CD1  CD2                                       
REMARK 470     LYS K 154    CG   CD   CE   NZ                                   
REMARK 470     LYS K 155    CG   CD   CE   NZ                                   
REMARK 470     LEU K 157    CG   CD1  CD2                                       
REMARK 470     ILE K 158    CG1  CG2  CD1                                       
REMARK 470     THR K 159    OG1  CG2                                            
REMARK 470     TYR K 160    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG K 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER K 162    OG                                                  
REMARK 470     ARG K 166    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN K 167    CG   OD1  ND2                                       
REMARK 470     HIS K 168    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE K 169    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET K 170    CG   SD   CE                                        
REMARK 470     THR K 171    OG1  CG2                                            
REMARK 470     LYS K 172    CG   CD   CE   NZ                                   
REMARK 470     GLU K 173    CG   CD   OE1  OE2                                  
REMARK 470     LEU K 174    CG   CD1  CD2                                       
REMARK 470     GLN K 175    CG   CD   OE1  NE2                                  
REMARK 470     TYR K 177    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE K 178    CG1  CG2  CD1                                       
REMARK 470     GLU K 179    CG   CD   OE1  OE2                                  
REMARK 470     ILE K 181    CG1  CG2  CD1                                       
REMARK 470     ARG K 182    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K 183    CG   CD   CE   NZ                                   
REMARK 470     ARG K 184    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG K 185    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN K 186    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN F   402     C1   NAG F  1201              1.42            
REMARK 500   SG   CYS E   720     SG   CYS E   818              1.50            
REMARK 500   ND2  ASN H   920     C1   NAG a     1              1.62            
REMARK 500   ND2  ASN H   749     C1   NAG H  1001              1.66            
REMARK 500   ND2  ASN H   502     O5   NAG Y     1              1.71            
REMARK 500   ND2  ASN H   565     C1   NAG Z     1              1.72            
REMARK 500   O    TRP G   579     CG2  ILE G   678              1.80            
REMARK 500   ND2  ASN H   888     C1   NAG c     1              1.80            
REMARK 500   ND2  ASN H    91     C1   NAG V     1              1.86            
REMARK 500   CB   CYS E   831     SG   CYS E  1039              1.87            
REMARK 500   ND2  ASN G   227     O5   NAG G   901              1.87            
REMARK 500   ND2  ASN H   292     C1   NAG X     1              1.90            
REMARK 500   OG   SER F   265     O    ASP F   271              1.91            
REMARK 500   OD1  ASN H   749     C1   NAG H  1001              1.92            
REMARK 500   O    TYR F   257     CG2  THR F   297              1.94            
REMARK 500   ND2  ASN H   292     O7   NAG X     1              1.94            
REMARK 500   O    ALA E   890     NH1  ARG E   919              1.94            
REMARK 500   CD1  LEU E   643     NZ   LYS E   694              1.95            
REMARK 500   ND2  ASN E   915     O5   NAG E  1203              1.97            
REMARK 500   ND2  ASN H   920     O5   NAG a     1              1.98            
REMARK 500   OH   TYR E   632     O    LYS E   635              1.99            
REMARK 500   CG   ASN H   749     C1   NAG H  1001              2.00            
REMARK 500   O    LEU L   565     CD   PRO L   568              2.00            
REMARK 500   NE2  GLN G   516     CE   LYS G   518              2.01            
REMARK 500   O    LYS E   996     CD2  HIS E  1000              2.01            
REMARK 500   CG   ASN F   178     C1   NAG R     1              2.02            
REMARK 500   OG   SER E   621     OD2  ASP E   655              2.03            
REMARK 500   ND2  ASN F   356     O5   NAG T     1              2.03            
REMARK 500   O    PHE A   566     ND2  ASN A   570              2.04            
REMARK 500   O    ASN L   486     N    THR L   488              2.04            
REMARK 500   CG   ASN F   402     C1   NAG F  1201              2.07            
REMARK 500   NZ   LYS E   389     OE2  GLU F   163              2.07            
REMARK 500   CG   ASN H   840     O    LYS H   876              2.07            
REMARK 500   CD1  LEU A   535     CD2  TYR A   565              2.07            
REMARK 500   OG   SER E   875     O    ILE E   881              2.08            
REMARK 500   ND2  ASN F   178     O5   NAG R     1              2.08            
REMARK 500   NE   ARG E   945     OD1  ASP E  1050              2.09            
REMARK 500   O    GLU H    90     OG1  THR H    97              2.10            
REMARK 500   N    TRP G   579     O    ILE G   678              2.10            
REMARK 500   ND2  ASN H   749     O5   NAG H  1001              2.11            
REMARK 500   O    SER E   832     N    LEU E   834              2.11            
REMARK 500   N    GLN F   622     O    TYR F   625              2.12            
REMARK 500   ND2  ASN F   103     O5   NAG Q     1              2.13            
REMARK 500   O    ASN F   498     N    GLU F   500              2.13            
REMARK 500   O    TYR G   224     N    ASN G   227              2.13            
REMARK 500   CD1  ILE A   378     CE2  PHE F   903              2.13            
REMARK 500   O    ILE F   450     OG1  THR F   468              2.14            
REMARK 500   CA   CYS E   831     SG   CYS E  1039              2.16            
REMARK 500   OD1  ASN E   118     O5   NAG E  1202              2.16            
REMARK 500   OD1  ASN G   227     O5   NAG G   901              2.16            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO E 754   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    PRO F 645   C   -  N   -  CD  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    PRO H 877   C   -  N   -  CD  ANGL. DEV. = -14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 371       12.47    -69.74                                   
REMARK 500    THR A 374      -11.87     76.08                                   
REMARK 500    SER A 470      145.01    107.46                                   
REMARK 500    THR A 473       19.53     51.22                                   
REMARK 500    ASP A 513       13.47     53.47                                   
REMARK 500    ASP A 515       74.86     60.92                                   
REMARK 500    LEU B  95      -62.06    -97.19                                   
REMARK 500    LEU B 103        1.80    -68.64                                   
REMARK 500    MET B 130       58.28    -95.87                                   
REMARK 500    PHE B 167       -7.32     69.47                                   
REMARK 500    ALA B 199      174.84    173.90                                   
REMARK 500    MET B 239       48.25    -89.98                                   
REMARK 500    GLU B 273      -60.98   -107.40                                   
REMARK 500    TYR B 274       57.31    -97.87                                   
REMARK 500    ASP B 280     -168.38   -125.08                                   
REMARK 500    SER B 310       69.43     85.26                                   
REMARK 500    PHE C  79       32.73     76.12                                   
REMARK 500    ASN C 137       -9.51     75.44                                   
REMARK 500    HIS C 138       60.01     33.41                                   
REMARK 500    ASP C 203       -8.77     65.82                                   
REMARK 500    GLU C 208       -0.08     58.24                                   
REMARK 500    VAL C 226        3.16    -61.20                                   
REMARK 500    THR D  89       49.98    -79.70                                   
REMARK 500    ASN D  90      117.51   -165.15                                   
REMARK 500    LYS D 129       30.18    -87.33                                   
REMARK 500    ALA D 172        8.45    -69.87                                   
REMARK 500    VAL D 173       50.16   -119.34                                   
REMARK 500    GLU D 174      -27.17    -39.34                                   
REMARK 500    PHE D 212       32.64    -95.37                                   
REMARK 500    GLN D 221      -63.28    -91.82                                   
REMARK 500    ARG D 251      117.67   -161.57                                   
REMARK 500    ILE D 273      -50.99   -120.52                                   
REMARK 500    ASN D 276       33.06    -98.34                                   
REMARK 500    GLU E  38      -51.21     68.05                                   
REMARK 500    LEU E  41     -172.30   -172.08                                   
REMARK 500    LEU E  44       -0.74    -59.27                                   
REMARK 500    ASN E  64     -166.61   -125.29                                   
REMARK 500    GLU E  65      -17.90    -49.24                                   
REMARK 500    ILE E 119      -64.00   -106.03                                   
REMARK 500    VAL E 121       -1.12     64.19                                   
REMARK 500    MET E 170       -5.38     68.20                                   
REMARK 500    SER E 187       79.94     55.66                                   
REMARK 500    ASN E 205       78.06   -101.88                                   
REMARK 500    SER E 274       -4.05     72.26                                   
REMARK 500    GLU E 335     -101.44    -22.43                                   
REMARK 500    ASP E 377       -8.39     79.43                                   
REMARK 500    ARG E 396       79.94     59.82                                   
REMARK 500    ASP E 435     -167.04     55.63                                   
REMARK 500    THR E 460       -7.50     70.22                                   
REMARK 500    ASP E 469       -8.25     93.45                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     210 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG V    1                                                       
REMARK 610     NAG X    1                                                       
REMARK 610     NAG Z    1                                                       
REMARK 610     NAG a    1                                                       
REMARK 610     NAG c    1                                                       
REMARK 610     NAG F 1201                                                       
REMARK 610     NAG H 1001                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 701  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 535   O                                                      
REMARK 620 2 ASP D 237   OD1 118.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D1001  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 536   OD1                                                    
REMARK 620 2 ASP D 237   OD1  82.8                                              
REMARK 620 3 ASP D 237   OD2 105.3  44.0                                        
REMARK 620 N                    1     2                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-31076   RELATED DB: EMDB                             
REMARK 900 STRUCTURE OF A MAMMALIAN CALCIUM CHANNEL                             
DBREF  7EEB A -246    -8  UNP    C5MKY7   C5MKY7_HCMV      1    239             
DBREF  7EEB A    1   686  UNP    Q91ZR5   CTSR1_MOUSE      1    686             
DBREF  7EEB B    1   588  UNP    A2ARP9   CTSR2_MOUSE      1    588             
DBREF  7EEB C    1   395  UNP    Q80W99   CTSR3_MOUSE      1    395             
DBREF  7EEB D    1   442  UNP    Q8BVN3   CTSR4_MOUSE      1    442             
DBREF  7EEB E    1  1109  UNP    A2RTF1   CTSRB_MOUSE      1   1109             
DBREF  7EEB F    1  1145  UNP    C6KI89   CTSG2_MOUSE      1   1145             
DBREF  7EEB G    1   805  UNP    E9Q9F6   CTSRD_MOUSE      1    805             
DBREF  7EEB H    1   985  UNP    P0DP43   CTSRE_MOUSE      1    985             
DBREF  7EEB L    1   706  UNP    Q3V161   Q3V161_MOUSE     1    706             
DBREF1 7EEB J    1   171  UNP                  A0A2R8VHF7_MOUSE                 
DBREF2 7EEB J     A0A2R8VHF7                          1         171             
DBREF  7EEB M    1   116  UNP    D3Z338   D3Z338_MOUSE     1    116             
DBREF  7EEB N    5    32  PDB    7EEB     7EEB             5     32             
DBREF  7EEB I    1   216  UNP    Q9DAM2   EFCB9_MOUSE      1    216             
DBREF  7EEB K    1   194  UNP    Q9CQP8   CTSRZ_MOUSE      1    194             
SEQADV 7EEB ASP A -268  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB TYR A -267  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB LYS A -266  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -265  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB HIS A -264  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -263  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB GLY A -262  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -261  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB TYR A -260  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB LYS A -259  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -258  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB HIS A -257  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -256  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ILE A -255  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -254  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB TYR A -253  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB LYS A -252  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -251  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -250  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -249  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB ASP A -248  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB LYS A -247  UNP  C5MKY7              EXPRESSION TAG                 
SEQADV 7EEB GLU A   -7  UNP  C5MKY7              LINKER                         
SEQADV 7EEB ASN A   -6  UNP  C5MKY7              LINKER                         
SEQADV 7EEB LEU A   -5  UNP  C5MKY7              LINKER                         
SEQADV 7EEB TYR A   -4  UNP  C5MKY7              LINKER                         
SEQADV 7EEB PHE A   -3  UNP  C5MKY7              LINKER                         
SEQADV 7EEB GLN A   -2  UNP  C5MKY7              LINKER                         
SEQADV 7EEB GLY A   -1  UNP  C5MKY7              LINKER                         
SEQADV 7EEB SER A    0  UNP  C5MKY7              LINKER                         
SEQRES   1 A  955  ASP TYR LYS ASP HIS ASP GLY ASP TYR LYS ASP HIS ASP          
SEQRES   2 A  955  ILE ASP TYR LYS ASP ASP ASP ASP LYS MET VAL SER LYS          
SEQRES   3 A  955  GLY GLU GLU LEU PHE THR GLY VAL VAL PRO ILE LEU VAL          
SEQRES   4 A  955  GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS PHE SER VAL          
SEQRES   5 A  955  SER GLY GLU GLY GLU GLY ASP ALA THR TYR GLY LYS LEU          
SEQRES   6 A  955  THR LEU LYS PHE ILE CYS THR THR GLY LYS LEU PRO VAL          
SEQRES   7 A  955  PRO TRP PRO THR LEU VAL THR THR LEU THR TYR GLY VAL          
SEQRES   8 A  955  GLN CYS PHE SER ARG TYR PRO ASP HIS MET LYS GLN HIS          
SEQRES   9 A  955  ASP PHE PHE LYS SER ALA MET PRO GLU GLY TYR VAL GLN          
SEQRES  10 A  955  GLU ARG THR ILE PHE PHE LYS ASP ASP GLY ASN TYR LYS          
SEQRES  11 A  955  THR ARG ALA GLU VAL LYS PHE GLU GLY ASP THR LEU VAL          
SEQRES  12 A  955  ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE LYS GLU ASP          
SEQRES  13 A  955  GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR ASN TYR ASN          
SEQRES  14 A  955  SER HIS ASN VAL TYR ILE MET ALA ASP LYS GLN LYS ASN          
SEQRES  15 A  955  GLY ILE LYS VAL ASN PHE LYS ILE ARG HIS ASN ILE GLU          
SEQRES  16 A  955  ASP GLY SER VAL GLN LEU ALA ASP HIS TYR GLN GLN ASN          
SEQRES  17 A  955  THR PRO ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP ASN          
SEQRES  18 A  955  HIS TYR LEU SER THR GLN SER ALA LEU SER LYS ASP PRO          
SEQRES  19 A  955  ASN GLU LYS ARG ASP HIS MET VAL LEU LEU GLU PHE VAL          
SEQRES  20 A  955  THR ALA ALA GLY ILE THR LEU GLY MET ASP GLU LEU TYR          
SEQRES  21 A  955  LYS GLU ASN LEU TYR PHE GLN GLY SER MET ASP GLN SER          
SEQRES  22 A  955  SER ARG ARG ASP GLU SER TYR HIS GLU THR HIS PRO GLY          
SEQRES  23 A  955  SER LEU ASP PRO SER HIS GLN SER HIS PRO HIS PRO HIS          
SEQRES  24 A  955  PRO HIS PRO THR LEU HIS ARG PRO ASN GLN GLY GLY VAL          
SEQRES  25 A  955  TYR TYR ASP SER PRO GLN HIS GLY MET PHE GLN GLN PRO          
SEQRES  26 A  955  TYR GLN GLN HIS GLY GLY PHE HIS GLN GLN ASN GLU LEU          
SEQRES  27 A  955  GLN HIS LEU ARG GLU PHE SER ASP SER HIS ASP ASN ALA          
SEQRES  28 A  955  PHE SER HIS HIS SER TYR GLN GLN ASP ARG ALA GLY VAL          
SEQRES  29 A  955  SER THR LEU PRO ASN ASN ILE SER HIS ALA TYR GLY GLY          
SEQRES  30 A  955  SER HIS PRO LEU ALA GLU SER GLN HIS SER GLY GLY PRO          
SEQRES  31 A  955  GLN SER GLY PRO ARG ILE ASP PRO ASN HIS HIS PRO HIS          
SEQRES  32 A  955  GLN ASP ASP PRO HIS ARG PRO SER GLU PRO LEU SER HIS          
SEQRES  33 A  955  PRO SER SER THR GLY SER HIS GLN GLY THR THR HIS GLN          
SEQRES  34 A  955  GLN TYR HIS GLU ARG SER HIS HIS LEU ASN PRO GLN GLN          
SEQRES  35 A  955  ASN ARG ASP HIS ALA ASP THR ILE SER TYR ARG SER SER          
SEQRES  36 A  955  THR ARG PHE TYR ARG SER HIS ALA PRO PHE SER ARG GLN          
SEQRES  37 A  955  GLU ARG PRO HIS LEU HIS ALA ASP HIS HIS HIS GLU GLY          
SEQRES  38 A  955  HIS HIS ALA HIS SER HIS HIS GLY GLU HIS PRO HIS HIS          
SEQRES  39 A  955  LYS GLU GLN ARG HIS TYR HIS GLY ASP HIS MET HIS HIS          
SEQRES  40 A  955  HIS ILE HIS HIS ARG SER PRO SER ALA SER GLN LEU SER          
SEQRES  41 A  955  HIS LYS SER HIS SER THR LEU ALA THR SER PRO SER HIS          
SEQRES  42 A  955  VAL GLY SER LYS SER THR ALA SER GLY ALA ARG TYR THR          
SEQRES  43 A  955  PHE GLY ALA ARG SER GLN ILE PHE GLY LYS ALA GLN SER          
SEQRES  44 A  955  ARG GLU SER LEU ARG GLU SER ALA SER LEU SER GLU GLY          
SEQRES  45 A  955  GLU ASP HIS VAL GLN LYS ARG LYS LYS ALA GLN ARG ALA          
SEQRES  46 A  955  HIS LYS LYS ALA HIS THR GLY ASN ILE PHE GLN LEU LEU          
SEQRES  47 A  955  TRP GLU LYS ILE SER HIS LEU LEU LEU GLY LEU GLN GLN          
SEQRES  48 A  955  MET ILE LEU SER LEU THR GLN SER LEU GLY PHE GLU THR          
SEQRES  49 A  955  PHE ILE PHE ILE VAL VAL CYS LEU ASN THR VAL ILE LEU          
SEQRES  50 A  955  VAL ALA GLN THR PHE THR GLU LEU GLU ILE ARG GLY GLU          
SEQRES  51 A  955  TRP TYR PHE MET VAL LEU ASP SER ILE PHE LEU SER ILE          
SEQRES  52 A  955  TYR VAL LEU GLU ALA VAL LEU LYS LEU ILE ALA LEU GLY          
SEQRES  53 A  955  LEU GLU TYR PHE TYR ASP PRO TRP ASN ASN LEU ASP PHE          
SEQRES  54 A  955  PHE ILE MET VAL MET ALA VAL LEU ASP PHE VAL LEU LEU          
SEQRES  55 A  955  GLN ILE ASN SER LEU SER TYR SER PHE TYR ASN HIS SER          
SEQRES  56 A  955  LEU PHE ARG ILE LEU LYS VAL PHE LYS SER MET ARG ALA          
SEQRES  57 A  955  LEU ARG ALA ILE ARG VAL LEU ARG ARG LEU SER ILE LEU          
SEQRES  58 A  955  THR SER LEU HIS GLU VAL ALA GLY THR LEU SER GLY SER          
SEQRES  59 A  955  LEU PRO SER ILE THR ALA ILE LEU THR LEU MET PHE THR          
SEQRES  60 A  955  CYS LEU PHE LEU PHE SER VAL VAL LEU ARG ALA LEU PHE          
SEQRES  61 A  955  GLN ASP SER ASP PRO LYS ARG PHE GLN ASN ILE PHE THR          
SEQRES  62 A  955  THR LEU PHE THR LEU PHE THR MET LEU THR LEU ASP ASP          
SEQRES  63 A  955  TRP SER LEU ILE TYR ILE ASP ASN ARG ALA GLN GLY ALA          
SEQRES  64 A  955  TRP TYR ILE ILE PRO ILE LEU MET ILE TYR ILE VAL ILE          
SEQRES  65 A  955  GLN TYR PHE ILE PHE LEU ASN LEU VAL ILE ALA VAL LEU          
SEQRES  66 A  955  VAL ASP ASN PHE GLN MET ALA LEU LEU LYS GLY LEU GLU          
SEQRES  67 A  955  LYS VAL LYS LEU GLU GLN ALA ALA ARG VAL HIS GLU LYS          
SEQRES  68 A  955  LEU LEU ASP ASP SER LEU THR ASP LEU ASN LYS ALA ASP          
SEQRES  69 A  955  ALA ASN ALA GLN MET THR GLU GLU ALA LEU LYS MET GLN          
SEQRES  70 A  955  LEU ILE GLU GLY MET PHE GLY ASN MET THR VAL LYS GLN          
SEQRES  71 A  955  ARG VAL LEU HIS PHE GLN PHE LEU GLN LEU VAL ALA ALA          
SEQRES  72 A  955  VAL GLU GLN HIS GLN GLN LYS PHE ARG SER GLN ALA TYR          
SEQRES  73 A  955  VAL ILE ASP GLU LEU VAL ASP MET ALA PHE GLU ALA GLY          
SEQRES  74 A  955  ASP ASP ASP TYR GLY LYS                                      
SEQRES   1 B  588  MET ALA GLN GLU GLN GLY HIS PHE GLN LEU LEU ARG ALA          
SEQRES   2 B  588  ASP ALA ILE ARG SER LYS LEU ILE ASP THR PHE SER LEU          
SEQRES   3 B  588  ILE GLU HIS LEU GLN GLY LEU SER GLN ALA VAL PRO ARG          
SEQRES   4 B  588  HIS THR LEU ARG GLU ILE LEU ASP PRO SER TYR GLN GLN          
SEQRES   5 B  588  LYS LEU MET SER GLY ASP GLN GLU GLN LEU VAL ARG PHE          
SEQRES   6 B  588  SER ILE LYS PRO ARG ARG MET GLY HIS ILE THR HIS SER          
SEQRES   7 B  588  ARG ARG LEU LEU SER ARG LEU ARG VAL ARG CYS SER ARG          
SEQRES   8 B  588  MET PRO PRO LEU SER LEU TRP ALA GLY TRP VAL LEU ASP          
SEQRES   9 B  588  SER SER VAL PHE SER LYS PHE ILE ILE SER LEU ILE PHE          
SEQRES  10 B  588  LEU ASN THR PHE VAL LEU MET VAL GLU ILE GLU LEU MET          
SEQRES  11 B  588  GLU SER THR ASN THR ALA LEU TRP PRO VAL LYS LEU ALA          
SEQRES  12 B  588  LEU GLU VAL ALA ASP TRP PHE ILE LEU LEU SER PHE ILE          
SEQRES  13 B  588  VAL GLU ILE LEU LEU MET TRP LEU ALA SER PHE SER LEU          
SEQRES  14 B  588  PHE TRP LYS ASP ALA TRP ASN VAL PHE ASP PHE PHE VAL          
SEQRES  15 B  588  THR LEU LEU SER LEU LEU PRO GLU LEU VAL VAL LEU LEU          
SEQRES  16 B  588  GLY VAL PRO ALA HIS SER VAL TRP LEU GLN LEU LEU ARG          
SEQRES  17 B  588  VAL CYS ARG VAL LEU ARG SER LEU LYS LEU PHE ALA ARG          
SEQRES  18 B  588  PHE ARG GLN ILE LYS VAL ILE LEU LEU ALA LEU VAL ARG          
SEQRES  19 B  588  ALA LEU LYS SER MET THR PHE LEU LEU MET LEU LEU LEU          
SEQRES  20 B  588  ILE PHE PHE TYR ILE PHE ALA VAL THR GLY VAL TYR PHE          
SEQRES  21 B  588  PHE ARG GLU TYR SER ARG SER THR ILE GLU GLY LEU GLU          
SEQRES  22 B  588  TYR ASN MET PHE PHE SER ASP LEU LEU ASN SER LEU VAL          
SEQRES  23 B  588  THR VAL PHE ILE LEU PHE THR LEU ASP HIS TRP TYR ALA          
SEQRES  24 B  588  VAL LEU GLN ASP ILE TRP LYS VAL PRO GLU SER SER ARG          
SEQRES  25 B  588  VAL PHE SER SER ILE TYR VAL ILE LEU TRP LEU LEU LEU          
SEQRES  26 B  588  GLY SER ILE ILE PHE ARG ASN ILE ILE VAL ALA MET MET          
SEQRES  27 B  588  VAL THR ASN PHE GLN ASN ILE ARG SER GLU LEU SER GLU          
SEQRES  28 B  588  GLU MET SER HIS LEU GLU VAL GLN TYR LYS ALA ASP MET          
SEQRES  29 B  588  PHE LYS GLN GLN ILE ILE GLN ARG ARG GLN HIS SER GLU          
SEQRES  30 B  588  SER LEU ARG GLY THR SER LEU GLY LYS VAL SER GLU ASP          
SEQRES  31 B  588  ILE ILE GLU THR SER ASP ALA SER ASP ASP ASP ASP ASP          
SEQRES  32 B  588  ASP ASP ASP ASP ASP ASP ASP ASP ASP ASP ASP ASP ASP          
SEQRES  33 B  588  ASP LYS SER ASP ALA THR GLU SER ASP ASN GLU GLU SER          
SEQRES  34 B  588  ASP SER GLU ASN SER GLU SER GLU ASN SER GLU SER GLU          
SEQRES  35 B  588  LYS ILE ASP PRO GLU LYS ASP TYR ALA LYS LYS SER TYR          
SEQRES  36 B  588  PRO GLU LYS SER HIS PRO GLU LYS SER TYR PRO GLU LYS          
SEQRES  37 B  588  SER HIS PRO GLU LYS SER TYR PRO GLU LYS SER HIS PRO          
SEQRES  38 B  588  LYS LYS SER TYR ASP GLU GLN ALA GLU ALA GLU LYS VAL          
SEQRES  39 B  588  LYS GLU GLU SER LYS GLU LYS ALA TYR PRO VAL SER HIS          
SEQRES  40 B  588  SER ILE SER SER HIS GLY SER THR ALA ALA ASP THR ALA          
SEQRES  41 B  588  PHE LEU GLU ASN LEU ASP TRP GLU THR LEU VAL HIS GLU          
SEQRES  42 B  588  ASN LEU PRO GLY LEU MET ASP MET ASP GLN ASP ASP ARG          
SEQRES  43 B  588  ILE VAL TRP PRO ARG ASP SER LEU PHE ARG TYR PHE GLU          
SEQRES  44 B  588  LEU LEU GLU LYS LEU GLN TYR ASN LEU GLU GLU ARG LYS          
SEQRES  45 B  588  LYS LEU GLN GLU PHE ALA VAL GLN ALA LEU MET SER PHE          
SEQRES  46 B  588  GLU ASP LYS                                                  
SEQRES   1 C  395  MET SER GLN HIS PHE HIS HIS ASN PRO VAL ARG VAL LYS          
SEQRES   2 C  395  SER GLY SER LEU PHE ALA THR ALA SER GLU ALA LEU GLN          
SEQRES   3 C  395  ALA ARG LEU SER LYS ILE LYS ARG LYS ASP LYS GLU CYS          
SEQRES   4 C  395  GLN ALA TYR PHE ARG LYS VAL ILE LYS SER THR PHE PHE          
SEQRES   5 C  395  GLN ILE VAL MET ILE THR THR VAL THR THR ASN SER PHE          
SEQRES   6 C  395  LEU LEU VAL LEU GLY THR ASN TYR ASP ILE GLN PHE GLU          
SEQRES   7 C  395  PHE PHE ARG THR PHE GLU VAL SER GLU LEU PHE PHE VAL          
SEQRES   8 C  395  SER VAL TYR VAL CYS GLU PHE LEU MET LYS VAL TYR VAL          
SEQRES   9 C  395  ASP PRO ILE THR TYR TRP LYS ASP GLY TYR ASN ILE LEU          
SEQRES  10 C  395  ASP VAL ILE ILE LEU ILE ILE LEU THR ILE PRO TYR LEU          
SEQRES  11 C  395  LEU ARG LYS ILE LYS GLY ASN HIS SER ALA TYR LEU HIS          
SEQRES  12 C  395  PHE ALA ASP GLY ILE GLN SER LEU ARG ILE LEU LYS LEU          
SEQRES  13 C  395  ILE SER TYR SER ARG GLY ILE ARG THR LEU ILE ILE ALA          
SEQRES  14 C  395  VAL GLY GLU THR VAL TYR THR VAL ALA SER VAL LEU THR          
SEQRES  15 C  395  LEU LEU PHE LEU LEU MET PHE VAL PHE ALA ILE LEU GLY          
SEQRES  16 C  395  PHE CYS LEU PHE GLY VAL THR ASP ARG GLY ASP LEU GLU          
SEQRES  17 C  395  ASN TRP GLY ASN LEU ALA SER ALA PHE PHE THR LEU PHE          
SEQRES  18 C  395  SER LEU ALA THR VAL ASP GLY TRP THR ASP LEU GLN GLU          
SEQRES  19 C  395  GLU LEU ASP LYS ARG LYS PHE THR VAL SER ARG ALA PHE          
SEQRES  20 C  395  THR ILE LEU PHE ILE LEU LEU ALA SER PHE ILE PHE LEU          
SEQRES  21 C  395  ASN MET PHE VAL GLY VAL MET ILE MET HIS THR GLU ASP          
SEQRES  22 C  395  SER MET LYS LYS PHE GLU ARG ASP LEU THR LEU GLU ARG          
SEQRES  23 C  395  ASN LEU ALA ILE MET GLU GLU LYS GLN ILE ILE LEU LYS          
SEQRES  24 C  395  ARG GLN GLN GLU GLU VAL ASN ARG LEU MET ASN THR GLN          
SEQRES  25 C  395  LYS SER GLY SER MET ASN PHE ILE ASP MET VAL GLU GLY          
SEQRES  26 C  395  PHE LYS LYS THR LEU ARG HIS THR ASP PRO MET VAL LEU          
SEQRES  27 C  395  ASP ASP PHE SER THR SER LEU SER PHE ILE ASP ILE TYR          
SEQRES  28 C  395  LEU VAL THR LEU ASP ASN GLN ASP VAL ILE VAL SER LYS          
SEQRES  29 C  395  LEU GLN GLU LEU TYR CYS GLU ILE VAL ASN VAL LEU SER          
SEQRES  30 C  395  LEU MET LEU GLU ASP MET PRO LYS GLU SER SER SER SER          
SEQRES  31 C  395  LEU SER GLY LEU SER                                          
SEQRES   1 D  442  MET SER GLU LYS HIS LYS TRP TRP GLN GLN VAL GLU ASN          
SEQRES   2 D  442  ILE ASP ILE THR HIS LEU GLY PRO LYS ARG LYS ALA TYR          
SEQRES   3 D  442  GLU LEU LEU GLY ARG HIS GLU GLU GLN VAL LEU ILE ASN          
SEQRES   4 D  442  ARG ARG ASP VAL MET GLU LYS LYS ASP ALA TRP ASP VAL          
SEQRES   5 D  442  GLN GLU PHE ILE THR GLN MET TYR ILE LYS GLN LEU LEU          
SEQRES   6 D  442  ARG HIS PRO ALA PHE GLN LEU LEU LEU ALA PHE LEU LEU          
SEQRES   7 D  442  LEU SER ASN ALA ILE THR ILE ALA LEU ARG THR ASN SER          
SEQRES   8 D  442  TYR LEU GLY GLN LYS HIS TYR GLU LEU PHE SER THR ILE          
SEQRES   9 D  442  ASP ASP ILE VAL LEU THR ILE LEU ILE CYS GLU VAL LEU          
SEQRES  10 D  442  LEU GLY TRP LEU ASN GLY PHE TRP ILE PHE TRP LYS ASP          
SEQRES  11 D  442  GLY TRP ASN ILE LEU ASN PHE ALA ILE VAL PHE ILE LEU          
SEQRES  12 D  442  PHE MET GLY PHE PHE ILE LYS GLN LEU ASP MET VAL ALA          
SEQRES  13 D  442  ILE THR TYR PRO LEU ARG VAL LEU ARG LEU VAL HIS VAL          
SEQRES  14 D  442  CYS MET ALA VAL GLU PRO LEU ALA ARG ILE ILE LYS VAL          
SEQRES  15 D  442  ILE LEU GLN SER MET PRO ASP LEU ALA ASN VAL MET ALA          
SEQRES  16 D  442  LEU ILE LEU PHE PHE MET LEU VAL PHE SER VAL PHE GLY          
SEQRES  17 D  442  VAL THR LEU PHE GLY ALA PHE VAL PRO LYS HIS PHE GLN          
SEQRES  18 D  442  ASN MET GLY VAL ALA LEU TYR THR LEU PHE ILE CYS ILE          
SEQRES  19 D  442  THR GLN ASP GLY TRP LEU ASP ILE TYR THR ASP PHE GLN          
SEQRES  20 D  442  MET ASP GLU ARG GLU TYR ALA MET GLU VAL GLY GLY ALA          
SEQRES  21 D  442  ILE TYR PHE ALA VAL PHE ILE THR LEU GLY ALA PHE ILE          
SEQRES  22 D  442  GLY LEU ASN LEU PHE VAL VAL VAL VAL THR THR ASN LEU          
SEQRES  23 D  442  GLU GLN MET MET LYS THR GLY GLU GLU GLU GLY HIS LEU          
SEQRES  24 D  442  ASN ILE LYS PHE THR GLU THR GLU GLU ASP GLU ASP TRP          
SEQRES  25 D  442  THR ASP GLU LEU PRO LEU VAL HIS CYS THR GLU ALA ARG          
SEQRES  26 D  442  LYS ASP THR SER THR VAL PRO LYS GLU PRO LEU VAL GLY          
SEQRES  27 D  442  GLY PRO LEU SER ASN LEU THR GLU LYS THR CYS ASP ASN          
SEQRES  28 D  442  PHE CYS LEU VAL LEU GLU ALA ILE GLN GLU ASN LEU MET          
SEQRES  29 D  442  GLU TYR LYS GLU ILE ARG GLU GLU LEU ASN MET ILE VAL          
SEQRES  30 D  442  GLU GLU VAL SER SER ILE ARG PHE ASN GLN GLU GLN GLN          
SEQRES  31 D  442  ASN VAL ILE LEU HIS LYS TYR THR SER LYS SER ALA THR          
SEQRES  32 D  442  PHE LEU SER GLU PRO PRO GLU GLY ALA ASN LYS GLN ASP          
SEQRES  33 D  442  LEU ILE THR ALA LEU VAL SER ARG GLU LYS VAL SER ASP          
SEQRES  34 D  442  SER ASN ILE ASN MET VAL ASN LYS HIS LYS PHE SER HIS          
SEQRES   1 E 1109  MET GLU SER PRO LEU ILE TYR VAL MET LEU VAL LEU LEU          
SEQRES   2 E 1109  ASN VAL PHE VAL PHE SER SER GLY VAL ILE HIS ASN LYS          
SEQRES   3 E 1109  GLY LYS GLU ARG THR TYR PHE SER CYS SER GLY GLU GLY          
SEQRES   4 E 1109  ILE LEU THR GLY LEU HIS THR ILE LYS LEU PHE LEU THR          
SEQRES   5 E 1109  MET ASP ASN LEU LYS VAL ARG CYS PHE PHE ARG ASN GLU          
SEQRES   6 E 1109  ASN GLN SER PRO SER LYS GLU ILE LEU GLY LEU PHE THR          
SEQRES   7 E 1109  SER GLY GLY LEU ALA PRO ASN MET ILE ILE THR ASN SER          
SEQRES   8 E 1109  THR PHE TYR GLY GLY TYR TYR PHE LYS LEU THR PRO PHE          
SEQRES   9 E 1109  SER ASN ARG LEU GLU TRP LEU ILE ASP ILE PRO ARG GLN          
SEQRES  10 E 1109  ASN ILE THR VAL ASN THR ASP ILE ALA ALA VAL GLU GLN          
SEQRES  11 E 1109  TRP MET ILE LYS ILE THR MET HIS GLU GLY LEU ASN ILE          
SEQRES  12 E 1109  TYR ASP THR GLU GLY THR LEU LEU ASP LEU VAL ARG GLU          
SEQRES  13 E 1109  PRO ILE LEU GLN TRP ASN LEU GLY ARG VAL LEU THR GLU          
SEQRES  14 E 1109  MET GLU VAL ARG ASP LEU TYR PRO GLU VAL ASN ASP ILE          
SEQRES  15 E 1109  LYS VAL THR LYS SER PRO CYS ALA ASN ASP VAL ALA LEU          
SEQRES  16 E 1109  ILE GLY PHE MET MET LYS PRO SER SER ASN GLY VAL PHE          
SEQRES  17 E 1109  ILE GLY LYS THR ILE SER GLY PHE TRP THR TYR LYS GLU          
SEQRES  18 E 1109  CYS ILE TRP HIS ASP LEU THR GLU ILE ILE TYR ALA GLU          
SEQRES  19 E 1109  LEU LYS ASP GLU HIS GLN GLY LEU THR VAL ILE ASP LEU          
SEQRES  20 E 1109  VAL LEU THR ASN HIS PHE LEU VAL ILE LEU THR SER LEU          
SEQRES  21 E 1109  GLY LEU TYR VAL SER SER ASP LEU ARG TYR PRO THR THR          
SEQRES  22 E 1109  SER GLN ILE LYS LEU SER ARG ALA GLU PHE CYS GLY PHE          
SEQRES  23 E 1109  GLU ARG VAL ASP TYR ILE ARG GLY ASN LEU TRP TYR ASN          
SEQRES  24 E 1109  GLU LYS CYS PHE ALA ASN ARG GLU SER PHE GLU VAL ASP          
SEQRES  25 E 1109  TYR VAL THR ILE THR PHE ASN ARG ASN ARG THR LEU SER          
SEQRES  26 E 1109  GLU SER SER SER CYS PHE PHE SER LYS GLU PRO PHE LEU          
SEQRES  27 E 1109  HIS TRP LEU PRO CYS VAL PHE SER THR ILE LYS ASN GLU          
SEQRES  28 E 1109  LYS SER ILE PRO ARG VAL ILE THR PHE LEU ILE ASP GLN          
SEQRES  29 E 1109  GLU THR ASP SER GLY ILE TYR LEU PHE ASN VAL GLN ASP          
SEQRES  30 E 1109  THR LYS GLU THR TYR VAL THR VAL ALA MET LEU LYS ASP          
SEQRES  31 E 1109  GLY LYS PRO SER PRO ARG PRO LYS PHE PRO SER PHE HIS          
SEQRES  32 E 1109  PHE PRO SER THR PHE THR LEU PRO LEU GLY MET ILE PHE          
SEQRES  33 E 1109  HIS PRO ARG SER HIS PHE LEU TYR VAL TYR GLY SER GLN          
SEQRES  34 E 1109  ILE TRP VAL SER MET ASP GLY GLY ASN THR PHE GLU MET          
SEQRES  35 E 1109  LEU CYS ASN LEU PHE SER HIS HIS VAL THR LYS THR SER          
SEQRES  36 E 1109  ASN SER PHE TYR THR SER ASP ILE VAL PHE ILE VAL GLU          
SEQRES  37 E 1109  ASP GLY ARG ILE LEU THR THR LYS ALA GLY LEU THR THR          
SEQRES  38 E 1109  TYR SER GLU LEU GLY ILE LEU LYS ASP ALA ILE PHE THR          
SEQRES  39 E 1109  LEU TYR TYR ASP GLN LEU GLY TYR ILE HIS LYS LEU THR          
SEQRES  40 E 1109  PRO GLU ASN PHE ASP ALA GLY SER LYS LEU LEU GLY HIS          
SEQRES  41 E 1109  GLY ASN SER GLY SER ILE PHE GLY LYS ARG PRO ASP LEU          
SEQRES  42 E 1109  GLY PHE GLU ALA ILE LEU VAL PRO GLN TYR ILE SER THR          
SEQRES  43 E 1109  ASN GLU MET TYR PHE PHE ALA HIS VAL PRO LEU THR MET          
SEQRES  44 E 1109  PRO THR ASN ILE GLN TRP LYS LYS ARG PHE LYS THR ILE          
SEQRES  45 E 1109  HIS LEU GLY LYS THR ILE GLU PHE SER LYS THR GLY LEU          
SEQRES  46 E 1109  ALA ASN ILE LYS ASN VAL TYR MET HIS LYS THR GLU PRO          
SEQRES  47 E 1109  VAL GLY PHE GLN THR SER ILE HIS THR GLU ILE ILE VAL          
SEQRES  48 E 1109  PRO PHE GLY ILE GLU ASN SER LYS ASP SER PRO CYS LEU          
SEQRES  49 E 1109  LEU SER ASP LEU GLU ILE THR TYR SER GLY LYS LEU TYR          
SEQRES  50 E 1109  TYR THR ILE LYS LEU LEU SER LYS ASN PRO LEU HIS GLU          
SEQRES  51 E 1109  LEU LYS SER THR ASP VAL GLU LYS SER VAL LEU ILE PRO          
SEQRES  52 E 1109  GLY TYR SER SER PHE LEU ILE MET ASN ILE THR ASP LYS          
SEQRES  53 E 1109  TRP THR ALA SER ALA LEU ALA THR MET PRO GLN ALA ILE          
SEQRES  54 E 1109  LYS SER ASN LEU LYS PHE LEU THR GLY SER TRP PHE LEU          
SEQRES  55 E 1109  TYR ASN PHE GLY THR ALA GLY GLY ARG LYS TRP SER ILE          
SEQRES  56 E 1109  SER THR ARG GLN CYS ASN TYR TRP ILE GLN GLN ASP SER          
SEQRES  57 E 1109  LEU ASP PHE MET SER LEU ASN LEU VAL LYS TYR ILE ASP          
SEQRES  58 E 1109  VAL GLY ASN THR ILE ASP PHE GLN PHE LYS ILE ILE PRO          
SEQRES  59 E 1109  LYS ALA MET SER THR PHE PRO ILE PRO PRO VAL SER MET          
SEQRES  60 E 1109  VAL VAL GLY ASN PRO GLY LEU VAL GLU VAL LYS THR GLN          
SEQRES  61 E 1109  GLY VAL PHE ASP LEU ASN GLU ASN TYR TYR LEU ASP ILE          
SEQRES  62 E 1109  HIS VAL SER GLY ARG PHE PHE GLN LYS GLY SER THR SER          
SEQRES  63 E 1109  ILE ALA LEU VAL LEU TRP GLU GLY SER SER LYS CYS TYR          
SEQRES  64 E 1109  ALA ILE THR LEU LEU PRO THR ILE LYS SER SER CYS SER          
SEQRES  65 E 1109  TYR LEU ARG THR MET HIS HIS THR PRO GLY ARG HIS ILE          
SEQRES  66 E 1109  PRO PRO GLU ASP TRP ILE SER GLY VAL HIS LYS ASP SER          
SEQRES  67 E 1109  GLN GLY PHE ASN MET ILE LYS THR LEU PRO ILE ASN TYR          
SEQRES  68 E 1109  ARG PRO PRO SER HIS MET GLY ILE SER ILE PRO LEU THR          
SEQRES  69 E 1109  ASP ASN PHE TYR HIS ALA ASP PRO SER LYS PRO ILE PRO          
SEQRES  70 E 1109  ARG ASN GLN PHE HIS LYS SER LYS GLU THR GLY LYS TYR          
SEQRES  71 E 1109  LYS GLN CYS ALA ASN VAL THR SER ARG ALA MET CYS ASN          
SEQRES  72 E 1109  CYS SER GLU HIS GLN LYS PHE SER HIS ALA VAL ALA PHE          
SEQRES  73 E 1109  SER ASP CYS LYS GLU LYS VAL HIS ARG PHE LYS PHE PRO          
SEQRES  74 E 1109  VAL THR GLN TYR PRO VAL VAL LEU GLU ILE PHE ASN GLU          
SEQRES  75 E 1109  ARG ASP LYS ILE SER ALA GLU PRO PRO TYR LEU VAL THR          
SEQRES  76 E 1109  MET THR GLU VAL ASN MET ARG LYS ASN TRP GLN LEU LYS          
SEQRES  77 E 1109  HIS ASN GLU PRO GLU ASN VAL LYS LYS MET LYS HIS TYR          
SEQRES  78 E 1109  LEU GLU PRO LEU LEU LYS THR PRO VAL TYR ASN PRO LEU          
SEQRES  79 E 1109  GLY LEU ASN LEU THR ILE GLN GLY SER GLU LEU PHE HIS          
SEQRES  80 E 1109  PHE LYS VAL SER VAL VAL PRO GLY VAL SER PHE CYS GLU          
SEQRES  81 E 1109  LEU SER GLU GLU PHE GLN ILE TYR VAL ASP GLU VAL PRO          
SEQRES  82 E 1109  LEU PRO PHE PRO GLY HIS ALA LEU ILE ALA VAL ALA THR          
SEQRES  83 E 1109  SER VAL VAL LEU GLY VAL LEU ILE PHE ILE ALA PHE VAL          
SEQRES  84 E 1109  PHE GLN LEU ARG ASN ILE HIS PRO LEU LYS ALA LEU LYS          
SEQRES  85 E 1109  LYS SER ILE ARG GLY ASN PRO GLY LEU THR SER SER THR          
SEQRES  86 E 1109  THR VAL SER SER                                              
SEQRES   1 F 1145  MET VAL SER ARG PRO ALA MET SER PRO VAL SER PRO VAL          
SEQRES   2 F 1145  TRP PRO ARG LYS PRO ASN LEU TRP ALA PHE TRP VAL LEU          
SEQRES   3 F 1145  ARG LEU VAL LEU LEU LEU SER LEU LYS SER TRP ALA GLU          
SEQRES   4 F 1145  ASP ALA LEU GLN HIS CYS THR TRP LEU LEU VAL LEU ASN          
SEQRES   5 F 1145  LYS PHE GLU LYS VAL GLY LEU HIS LEU SER LYS ASP ARG          
SEQRES   6 F 1145  PHE GLN ASP HIS GLU PRO ILE ASP THR VAL ALA LYS VAL          
SEQRES   7 F 1145  PHE GLN LYS LEU THR ASP SER PRO ILE ASP PRO SER GLU          
SEQRES   8 F 1145  ASN TYR LEU SER PHE PRO TYR TYR LEU GLN ILE ASN PHE          
SEQRES   9 F 1145  SER CYS PRO GLY GLN ASN ILE GLU GLU LEU ALA ARG LYS          
SEQRES  10 F 1145  GLY HIS LEU MET GLY MET LYS PRO MET VAL GLN ILE ASN          
SEQRES  11 F 1145  TYR MET TYR SER VAL ASN PHE TYR ARG TRP GLU MET GLU          
SEQRES  12 F 1145  ASN VAL GLN ILE LEU MET GLU ALA ALA PRO MET ARG SER          
SEQRES  13 F 1145  THR GLY TYR CYS PRO ALA GLU ALA MET CYS VAL LEU ASN          
SEQRES  14 F 1145  TRP TYR THR PRO MET PRO PHE LYS ASN GLY SER VAL VAL          
SEQRES  15 F 1145  SER SER VAL ASP ILE TYR THR ASN GLY ILE GLY PRO PHE          
SEQRES  16 F 1145  VAL SER LYS LYS ARG PHE TYR VAL ASN MET ASN GLY PHE          
SEQRES  17 F 1145  LEU LYS ARG ASP ALA SER GLY LYS SER LEU PHE ALA ILE          
SEQRES  18 F 1145  GLY TYR GLU SER LEU VAL LEU LYS SER SER HIS PHE ARG          
SEQRES  19 F 1145  LEU SER LYS SER ARG PRO LEU TRP TYR THR VAL ASN HIS          
SEQRES  20 F 1145  ALA PRO VAL PHE ILE LEU GLY GLY PHE TYR ASP GLU LYS          
SEQRES  21 F 1145  SER ILE LEU PHE SER ASP SER ASN PHE GLN ASP TYR VAL          
SEQRES  22 F 1145  LEU LEU GLU LEU SER ILE ASP SER CYS TRP VAL GLY SER          
SEQRES  23 F 1145  PHE TYR CYS PRO ILE LEU GLY PHE SER ALA THR ILE HIS          
SEQRES  24 F 1145  ASP ALA ILE ALA THR GLU SER THR LEU PHE ILE ARG GLN          
SEQRES  25 F 1145  ASN GLN LEU VAL TYR TYR PHE THR GLY THR TYR ILE THR          
SEQRES  26 F 1145  LEU PHE ASP LYS SER HIS GLY SER SER ARG TRP VAL ARG          
SEQRES  27 F 1145  VAL LEU PRO SER GLU CYS ILE LYS ARG LEU CYS PRO VAL          
SEQRES  28 F 1145  TYR ALA SER GLY ASN GLY SER GLU TYR VAL LEU ALA LEU          
SEQRES  29 F 1145  THR THR GLY LYS ASN GLU GLY TYR ILE HIS ILE GLY THR          
SEQRES  30 F 1145  ILE THR ASP GLY LEU VAL SER PHE GLU MET VAL PRO ASP          
SEQRES  31 F 1145  GLY TRP SER VAL CYS GLU LYS LEU PRO GLY LYS ASN CYS          
SEQRES  32 F 1145  SER ILE ASP TRP ALA THR TYR ILE ALA ASP GLU ARG ASN          
SEQRES  33 F 1145  LEU LEU LEU LEU VAL LYS ILE ASP SER GLY GLN PHE TYR          
SEQRES  34 F 1145  LEU VAL ASN PHE ASN THR GLU PHE LYS THR LEU ASN ILE          
SEQRES  35 F 1145  LEU TYR LYS ILE PRO GLU PHE ILE PRO GLU ALA LYS GLU          
SEQRES  36 F 1145  LEU ASP PHE LEU VAL LEU LEU ASP THR VAL THR TYR THR          
SEQRES  37 F 1145  ASN THR PRO MET THR PRO LYS GLY LEU PHE PHE ASN THR          
SEQRES  38 F 1145  LEU ASN ASN MET LEU TYR ILE TRP GLY ASN PHE ILE LEU          
SEQRES  39 F 1145  GLN SER TYR ASN ARG GLU GLU PHE ILE PHE LEU ALA ASP          
SEQRES  40 F 1145  PHE PRO LYS GLU SER THR ILE LYS TYR MET VAL ASN SER          
SEQRES  41 F 1145  PHE LYS GLY GLN MET ALA VAL VAL THR GLU ASN GLU GLU          
SEQRES  42 F 1145  ILE TRP TYR PHE LEU GLU GLY GLY TYR ASP VAL TYR GLN          
SEQRES  43 F 1145  VAL VAL PRO SER GLN GLY TRP GLU THR TYR HIS ASN LEU          
SEQRES  44 F 1145  GLN LYS MET GLN LYS SER SER PHE HIS SER GLU ASP GLU          
SEQRES  45 F 1145  SER LEU VAL SER LEU PHE PHE GLU ASP GLY LYS LEU PHE          
SEQRES  46 F 1145  GLN LEU VAL TYR LEU PHE ASP VAL GLY LYS GLU ARG LEU          
SEQRES  47 F 1145  VAL LYS ARG LEU LEU PRO VAL GLY THR LEU MET GLU TYR          
SEQRES  48 F 1145  ASN LEU PRO LYS PRO PHE THR VAL VAL ASN GLN GLY ASN          
SEQRES  49 F 1145  TYR GLN ALA ILE SER PHE THR HIS THR CYS PRO PHE LYS          
SEQRES  50 F 1145  GLU ILE HIS LEU ILE ASP VAL PRO LYS LYS HIS HIS ALA          
SEQRES  51 F 1145  SER ARG THR GLU SER TYR VAL ALA LEU PRO PRO LEU VAL          
SEQRES  52 F 1145  SER GLU SER LEU GLY PHE HIS ASN ASN ASN THR LEU ALA          
SEQRES  53 F 1145  VAL TYR GLN GLY LEU VAL TYR TYR LEU LEU TRP LEU HIS          
SEQRES  54 F 1145  SER LYS TYR ASP LYS PRO TYR ALA ASP PRO VAL HIS ASP          
SEQRES  55 F 1145  PRO THR TRP ARG TRP TRP GLN HIS LYS THR LYS ASP LYS          
SEQRES  56 F 1145  ASP TYR PHE PHE TYR LEU PHE SER ASN ARG LEU ALA ALA          
SEQRES  57 F 1145  GLU GLY ILE TYR ILE ASN MET ASN ALA TYR GLN LYS LEU          
SEQRES  58 F 1145  TYR ASN MET SER GLY ASP TYR GLY ILE PRO ASP LEU PHE          
SEQRES  59 F 1145  PHE LEU ASP LYS GLY ASN TRP PHE THR ILE THR VAL VAL          
SEQRES  60 F 1145  LEU LEU SER HIS GLN ASP THR PHE THR SER SER ASP SER          
SEQRES  61 F 1145  GLN GLY PRO THR ILE ASN VAL ASP LYS LYS LEU ALA ILE          
SEQRES  62 F 1145  ALA VAL THR ILE ALA ASP PRO GLU CYS LEU SER VAL THR          
SEQRES  63 F 1145  VAL THR GLN ASP VAL LEU LEU ASN ARG ASN ALA VAL ILE          
SEQRES  64 F 1145  ASN LYS ILE LYS VAL ILE ASP LYS LYS ARG CYS SER GLU          
SEQRES  65 F 1145  GLN GLY MET ILE GLY ARG ASN ILE LYS LYS THR SER MET          
SEQRES  66 F 1145  MET LEU LYS VAL LEU GLY ALA PRO GLY ASN CYS ILE GLN          
SEQRES  67 F 1145  ARG THR TYR LEU GLY GLY ILE ILE GLN GLY PHE LYS VAL          
SEQRES  68 F 1145  VAL PRO ILE PHE ILE GLY CYS PRO PRO GLY LYS ARG LEU          
SEQRES  69 F 1145  ALA PHE ASP VAL SER TYR THR ILE MET HIS SER GLU GLU          
SEQRES  70 F 1145  ILE ASN LYS HIS TYR PHE ASP CYS VAL ILE LYS ASP ALA          
SEQRES  71 F 1145  GLU MET PRO CYS PHE LEU PHE ARG ASP LEU PHE GLN PRO          
SEQRES  72 F 1145  PHE PHE LEU VAL GLN ASP LEU VAL THR GLY ASP SER GLY          
SEQRES  73 F 1145  SER PHE LEU GLY SER TYR VAL LEU LYS VAL VAL GLY GLY          
SEQRES  74 F 1145  GLY ARG THR LEU ASN THR ILE ARG ASP TYR THR GLU GLU          
SEQRES  75 F 1145  GLU ILE PHE ARG TYR ASN SER PRO LEU ASP THR THR ASN          
SEQRES  76 F 1145  SER LEU ILE TRP LYS THR LYS VAL GLU ARG THR THR GLU          
SEQRES  77 F 1145  ASP LYS LYS PHE TYR ILE MET SER HIS GLU SER PRO GLY          
SEQRES  78 F 1145  VAL GLU TRP LEU CYS LEU GLU ASN SER PRO CYS TYR ASP          
SEQRES  79 F 1145  ILE ILE PRO GLN SER ILE TYR PRO PRO GLU PHE PHE PHE          
SEQRES  80 F 1145  LYS LEU LEU VAL SER ASN ARG GLY VAL ASP ASN SER THR          
SEQRES  81 F 1145  TYR CYS ASP TYR LYS LEU THR PHE ILE VAL HIS ILE HIS          
SEQRES  82 F 1145  GLY LEU PRO LEU SER SER LYS ARG THR SER PHE ILE VAL          
SEQRES  83 F 1145  MET VAL SER THR SER PHE PHE ILE ALA LEU VAL VAL PHE          
SEQRES  84 F 1145  TYR ILE LEU PHE CYS LEU VAL TRP PRO HIS ILE VAL LYS          
SEQRES  85 F 1145  ALA TRP VAL SER LEU ARG TRP ARG ILE ASN ASN ILE MET          
SEQRES  86 F 1145  ALA SER GLU SER TYR TYR THR TYR ALA SER SER THR ALA          
SEQRES  87 F 1145  GLY PHE SER LEU GLN SER HIS SER PHE GLU GLY PRO SER          
SEQRES  88 F 1145  ARG ALA GLY SER LYS GLU ASP ASN VAL GLN ALA LYS THR          
SEQRES  89 F 1145  ALA                                                          
SEQRES   1 G  805  MET LEU VAL LEU MET LEU ALA ALA ALA VAL ALA THR MET          
SEQRES   2 G  805  VAL ARG ALA HIS THR LEU CYS ARG VAL HIS THR VAL ARG          
SEQRES   3 G  805  THR GLY LYS VAL PHE LYS SER ASN ILE GLN LEU GLN GLY          
SEQRES   4 G  805  ASP PRO LEU PHE TYR ALA PHE PRO ASN THR PHE VAL LEU          
SEQRES   5 G  805  LYS ASN VAL CYS LYS ALA ASP ILE SER VAL TYR LEU GLY          
SEQRES   6 G  805  GLN LYS VAL PHE LEU THR ILE ASP ASN PHE GLU SER SER          
SEQRES   7 G  805  LEU LEU PRO LEU THR VAL PRO LYS SER LEU ALA VAL GLY          
SEQRES   8 G  805  VAL PRO SER ILE THR SER ALA HIS PHE VAL SER GLY SER          
SEQRES   9 G  805  LEU VAL LEU PHE VAL ILE SER GLY LYS GLY TYR SER TYR          
SEQRES  10 G  805  ASP TYR TYR GLU ASN THR TRP ARG LYS LEU GLU GLY ILE          
SEQRES  11 G  805  SER GLU PRO VAL SER HIS ILE SER GLY ASP VAL CYS CYS          
SEQRES  12 G  805  PHE LYS GLY SER PHE CYS LEU GLU LEU SER ASN ASN LEU          
SEQRES  13 G  805  PHE ALA TYR LEU ARG GLY GLY GLN ILE PRO GLY THR ASN          
SEQRES  14 G  805  ILE TYR PHE SER ASP ASN GLY GLY PHE SER PHE GLN LEU          
SEQRES  15 G  805  MET ASN THR ASP LYS LEU SER HIS LEU THR GLY THR LEU          
SEQRES  16 G  805  GLY GLY ILE PHE HIS LEU HIS SER MET SER GLN VAL GLY          
SEQRES  17 G  805  VAL LEU MET VAL GLU ASN ASN LEU GLY THR PHE HIS TYR          
SEQRES  18 G  805  MET GLU TYR PRO LEU ASN HIS SER MET GLY ILE ALA PHE          
SEQRES  19 G  805  SER TYR LYS ASN LEU LEU GLU VAL ILE MET LYS PRO TYR          
SEQRES  20 G  805  GLN ARG GLY PHE MET VAL LEU TRP ASN GLN LYS SER ILE          
SEQRES  21 G  805  LEU VAL SER SER ASN SER GLY GLN ILE VAL GLU HIS VAL          
SEQRES  22 G  805  ARG LEU ILE ASP GLN LYS ILE PHE THR ASP LEU ASP VAL          
SEQRES  23 G  805  GLU HIS ALA ASN ILE ASN ILE TYR SER VAL ALA SER ASN          
SEQRES  24 G  805  ALA TYR GLU LEU ALA PHE LEU VAL ALA GLU ASP HIS LEU          
SEQRES  25 G  805  TYR TYR GLY SER GLN SER TYR MET GLY THR TYR VAL ILE          
SEQRES  26 G  805  LYS LEU PRO HIS GLN PRO LEU TRP SER THR HIS THR SER          
SEQRES  27 G  805  ILE TYR PHE GLU ASP ILE GLY ILE LEU GLN VAL LEU THR          
SEQRES  28 G  805  PRO VAL ALA ASP PRO HIS PHE ALA ALA TYR ASP PHE ASP          
SEQRES  29 G  805  LYS CYS THR VAL ASN VAL GLN SER SER LEU MET ASP GLU          
SEQRES  30 G  805  LYS LEU ALA LEU GLN PRO CYS ASN VAL GLU LEU LEU GLU          
SEQRES  31 G  805  SER THR MET ILE ASN THR MET PHE THR ILE ASP MET ASN          
SEQRES  32 G  805  SER LYS LEU LYS LEU SER ALA LEU MET ILE PRO ARG LYS          
SEQRES  33 G  805  GLY GLU ASN PRO THR PRO LEU VAL MET VAL SER ASN PRO          
SEQRES  34 G  805  HIS ALA LEU GLY PHE LYS ALA ASN LEU ASN GLU PHE GLY          
SEQRES  35 G  805  ASN THR PHE ASP GLY ASN SER LYS TYR LYS LEU ASP ILE          
SEQRES  36 G  805  GLU LEU LYS GLN GLN HIS HIS TRP GLY ASN SER ASP PHE          
SEQRES  37 G  805  ASN PHE THR ALA SER ILE LYS ARG HIS ALA ILE SER SER          
SEQRES  38 G  805  VAL THR VAL ASP ILE ALA ASP LYS THR LEU SER CYS VAL          
SEQRES  39 G  805  ASP LEU LYS PRO LEU SER THR LEU ILE SER VAL GLY CYS          
SEQRES  40 G  805  ASP MET THR LYS LYS ILE VAL VAL GLN ASN LYS ILE SER          
SEQRES  41 G  805  ALA CYS THR MET GLY ILE LEU ASN PRO VAL GLN LEU GLN          
SEQRES  42 G  805  LYS ASN TYR THR TYR THR ILE GLU LYS GLU ALA TYR ASP          
SEQRES  43 G  805  PRO ILE ASN HIS ASN GLY GLU ALA GLN ASP ASP LEU ILE          
SEQRES  44 G  805  VAL PHE TYR GLU TYR LYS ASP LEU GLY CYS PRO ARG LEU          
SEQRES  45 G  805  VAL TYR TYR ASP LYS PRO TRP LYS PRO VAL VAL GLU LEU          
SEQRES  46 G  805  TRP LYS ASN GLY ILE VAL GLU GLU ILE MET ASN ALA GLU          
SEQRES  47 G  805  TYR VAL ILE SER GLU ILE ASN GLY LEU VAL THR TYR SER          
SEQRES  48 G  805  TYR SER LEU THR ALA ALA THR ALA ASN CYS ARG SER GLN          
SEQRES  49 G  805  PRO GLN ASN TRP SER THR PHE GLU SER ASP ILE GLU ASN          
SEQRES  50 G  805  GLU GLU PRO PHE LEU TRP ASN ARG GLU ASN TYR VAL SER          
SEQRES  51 G  805  CYS HIS GLU ASP ASN LYS ASP ASN PRO LEU LEU TRP PRO          
SEQRES  52 G  805  ASN VAL GLU TYR GLN VAL LEU GLY GLY GLN THR ASN ASN          
SEQRES  53 G  805  LYS ILE ILE PHE GLY GLN ARG ASN GLY ILE TYR THR PHE          
SEQRES  54 G  805  HIS LEU SER VAL VAL ASP PRO TYR TYR SER TYR CYS ASN          
SEQRES  55 G  805  LEU ASN THR ILE PHE SER VAL TYR VAL HIS GLY ALA LEU          
SEQRES  56 G  805  PRO VAL THR LYS PHE GLN PRO LEU LEU THR ILE LEU LEU          
SEQRES  57 G  805  MET VAL THR THR THR LEU LEU THR ALA TRP LEU ALA TYR          
SEQRES  58 G  805  ALA ILE PRO LYS GLN LEU ARG SER GLU LYS GLY GLN ARG          
SEQRES  59 G  805  LEU LEU GLY PHE CYS TYR GLN ILE LEU GLN LEU CYS LEU          
SEQRES  60 G  805  GLY VAL CYS PHE CYS THR TRP LEU ARG GLY LYS LEU ARG          
SEQRES  61 G  805  GLN TRP LEU ARG PRO ARG ARG VAL LYS ASP GLN ASN ARG          
SEQRES  62 G  805  GLY LYS VAL ARG VAL ALA GLN LYS HIS PRO GLU THR              
SEQRES   1 H  985  MET PRO SER ALA GLY GLN ARG LYS PRO GLY SER LEU LEU          
SEQRES   2 H  985  ALA LEU GLN ALA LEU GLN LYS TRP LEU LEU ARG GLY GLY          
SEQRES   3 H  985  VAL GLY ALA MET LEU ALA ARG GLN VAL VAL ALA ALA LEU          
SEQRES   4 H  985  LEU LEU TRP LEU SER CYS CYS VAL SER ALA LEU TRP ARG          
SEQRES   5 H  985  TYR TYR ILE ASN SER GLN ASP TYR SER ILE PHE SER THR          
SEQRES   6 H  985  ARG SER SER ILE LYS LEU GLU TYR GLU GLY ASN SER PHE          
SEQRES   7 H  985  VAL SER TRP LYS ILE PRO GLU SER CYS LYS VAL GLU ASN          
SEQRES   8 H  985  THR THR SER PRO LYS THR THR LEU HIS CYS LYS ARG ALA          
SEQRES   9 H  985  GLY ILE HIS THR ILE LYS PRO ILE ALA GLY ASN GLN GLU          
SEQRES  10 H  985  VAL GLU ARG HIS LEU THR VAL ASP ASN SER TYR ILE CYS          
SEQRES  11 H  985  TYR LEU TRP TYR PHE THR VAL VAL ASP VAL TYR TYR ASN          
SEQRES  12 H  985  LEU SER GLN ILE VAL THR ILE TRP VAL TYR ASP PRO GLU          
SEQRES  13 H  985  SER ALA SER THR GLU GLU LEU ILE TRP THR ALA LYS LYS          
SEQRES  14 H  985  PRO SER LEU SER SER ARG VAL LEU THR LYS GLN MET ASN          
SEQRES  15 H  985  THR LEU GLY GLN ARG PRO PHE ILE PHE THR VAL GLU LYS          
SEQRES  16 H  985  ARG LEU THR TYR HIS PRO GLY PRO LEU THR SER GLU GLY          
SEQRES  17 H  985  THR TRP VAL ILE HIS LEU PRO MET SER SER ASP ASP ILE          
SEQRES  18 H  985  ALA LYS VAL ILE ARG GLY ASN LYS VAL ALA PHE GLN ASP          
SEQRES  19 H  985  CYS PHE ILE ALA ASN LEU TYR PHE MET LEU THR TYR PRO          
SEQRES  20 H  985  MET THR ILE ILE SER GLU PRO PRO GLY TYR GLU PRO LEU          
SEQRES  21 H  985  THR VAL PRO PRO GLY SER PRO LEU MET LEU SER TRP ASP          
SEQRES  22 H  985  THR CYS ILE SER THR PHE ALA LEU LEU ALA THR ASP GLN          
SEQRES  23 H  985  GLU THR PHE GLN THR ASN ASP SER PHE GLN THR TRP THR          
SEQRES  24 H  985  ARG VAL ARG ALA PRO PRO GLY ILE LEU SER ASP ALA GLN          
SEQRES  25 H  985  ARG HIS SER LEU ARG ASP VAL ILE ILE PHE ASP GLN GLY          
SEQRES  26 H  985  THR LEU PHE LEU VAL ASP GLY THR VAL TYR LEU ARG THR          
SEQRES  27 H  985  GLU ASP GLU PHE THR LYS LEU ASP GLU SER ARG GLY ILE          
SEQRES  28 H  985  SER GLU THR GLY ILE LEU GLY PHE SER LYS ARG ARG TRP          
SEQRES  29 H  985  CYS GLN ILE ARG TYR LEU TYR LYS LEU ALA SER LYS LYS          
SEQRES  30 H  985  SER ILE LEU ILE ALA TRP SER LYS THR THR VAL TYR ALA          
SEQRES  31 H  985  GLY TYR ALA THR PHE ARG PHE VAL THR LEU THR ASP THR          
SEQRES  32 H  985  ALA LYS LEU LYS ASP PHE LEU LYS LEU PRO GLN THR ASP          
SEQRES  33 H  985  THR LEU GLU VAL MET SER VAL GLU TYR LEU TRP HIS PRO          
SEQRES  34 H  985  LEU GLU ALA ALA VAL LEU LEU SER HIS CYS SER VAL CYS          
SEQRES  35 H  985  THR THR ASN THR ARG ASN ILE ARG ILE VAL ILE TYR SER          
SEQRES  36 H  985  ALA ILE PHE GLN THR TRP THR LEU GLN ASP PHE GLU LEU          
SEQRES  37 H  985  GLN LEU PRO LYS GLU ALA ILE LEU GLU PHE ARG PHE LEU          
SEQRES  38 H  985  TYR SER ALA MET PRO ASP ILE ILE MET TRP ASP GLN HIS          
SEQRES  39 H  985  HIS VAL TYR TYR SER TYR LYS ASN PHE THR VAL VAL GLY          
SEQRES  40 H  985  THR ILE SER THR PRO SER GLY GLU THR ASN LEU SER SER          
SEQRES  41 H  985  LEU SER GLN GLY SER LYS ILE HIS GLN VAL LEU THR ASP          
SEQRES  42 H  985  ARG ILE GLY ASN VAL VAL VAL LYS MET GLU ASN ASN VAL          
SEQRES  43 H  985  MET PHE TYR ILE LYS ALA ASP ILE THR GLU ALA VAL ILE          
SEQRES  44 H  985  LEU HIS THR TRP VAL ASN THR THR ALA LYS THR VAL VAL          
SEQRES  45 H  985  LEU PHE ASP LYS SER PHE GLU VAL CYS ILE LEU TYR TYR          
SEQRES  46 H  985  ASN GLU ASN LEU ASP GLU LYS TYR GLN LEU GLN THR GLN          
SEQRES  47 H  985  PRO TYR PRO LEU ILE LEU GLU LEU GLN SER ILE ASN LYS          
SEQRES  48 H  985  ASP LEU GLY ASP TRP CYS PRO TYR LEU ALA PHE GLN HIS          
SEQRES  49 H  985  ASN ILE HIS SER GLN PHE TYR HIS MET ASP LYS GLY GLU          
SEQRES  50 H  985  SER LEU THR ILE TRP SER GLN ILE VAL TYR PRO GLU ASN          
SEQRES  51 H  985  ARG GLY LEU TYR ILE VAL VAL GLU HIS TYR GLY SER SER          
SEQRES  52 H  985  VAL MET THR TRP THR GLN ASN LEU GLU TYR GLU ILE ALA          
SEQRES  53 H  985  SER GLY PHE CYS THR LYS THR MET ILE THR ARG PHE PHE          
SEQRES  54 H  985  GLN THR THR ASN TYR GLU LEU VAL ASP ASN TYR TYR GLN          
SEQRES  55 H  985  LEU GLN LYS GLU ASN THR GLY LEU MET LEU LEU GLN PHE          
SEQRES  56 H  985  ARG PRO SER GLU PHE SER ARG THR CYS LEU THR ALA LYS          
SEQRES  57 H  985  PRO VAL PHE GLU ILE ASP VAL GLY CYS ASP SER SER LYS          
SEQRES  58 H  985  TYR ILE MET VAL ARG GLY PHE ASN LYS SER ARG CYS GLN          
SEQRES  59 H  985  ARG ARG ASP PHE SER TYR VAL ILE ASP LYS GLU LEU LEU          
SEQRES  60 H  985  ARG GLU SER LEU SER ASP ASN LEU LYS VAL ARG TYR ASP          
SEQRES  61 H  985  VAL ALA LYS TYR GLY CYS PRO LEU THR LEU GLU LEU GLY          
SEQRES  62 H  985  GLN MET PHE GLN PRO ILE VAL GLU LEU TYR ASP GLU ASN          
SEQRES  63 H  985  GLY PHE ILE LYS ILE VAL ASP ALA ASN PHE ILE LEU TRP          
SEQRES  64 H  985  GLU ILE HIS GLY ARG ASN ASP TYR THR PHE ASN SER THR          
SEQRES  65 H  985  MET GLU GLN ASN GLY CYS ILE ASN GLU ALA GLN THR TRP          
SEQRES  66 H  985  ASP SER MET ILE GLU GLU ASN PRO ASP ILE PRO LEU ASP          
SEQRES  67 H  985  ASP VAL TRP GLY PRO GLN ASN TYR ARG PRO CYS PHE SER          
SEQRES  68 H  985  TYR ALA ILE GLY LYS PRO GLY ASP LEU GLY GLN PRO TYR          
SEQRES  69 H  985  GLU ILE LEU ASN TYR SER ASN LYS ASN HIS ILE LYS TRP          
SEQRES  70 H  985  PRO MET THR TYR ALA GLY MET TYR VAL TYR ARG LEU LYS          
SEQRES  71 H  985  ILE LEU ASP PRO ASN TYR SER PHE CYS ASN LEU THR THR          
SEQRES  72 H  985  ILE PHE ALA ILE GLU SER LEU GLY MET ILE PRO ARG SER          
SEQRES  73 H  985  SER VAL TYR LEU VAL ALA ALA LEU ILE PHE VAL LEU MET          
SEQRES  74 H  985  LEU THR PHE ILE SER ILE LEU VAL LEU SER TYR PHE TRP          
SEQRES  75 H  985  TYR LEU LYS ILE TYR ARG GLN PHE ILE ILE GLU PRO LEU          
SEQRES  76 H  985  HIS LYS ARG PRO ALA LYS GLN LYS LYS ASN                      
SEQRES   1 L  706  MET ALA HIS VAL ARG ASN LYS LYS SER ASP ASP LYS LYS          
SEQRES   2 L  706  ALA MET VAL VAL ALA LYS GLU ASP THR ASN LYS SER GLU          
SEQRES   3 L  706  SER GLU GLY VAL THR LYS LEU GLN THR TYR LEU LYS THR          
SEQRES   4 L  706  ILE PRO ILE ALA LYS LYS LYS PHE ALA LYS LEU PRO LYS          
SEQRES   5 L  706  ARG LYS LYS SER PRO THR SER ALA GLU LEU LEU LEU ILE          
SEQRES   6 L  706  ASP PRO ARG TYR SER ALA SER LYS GLU GLY PRO LEU GLY          
SEQRES   7 L  706  LEU GLY PRO ILE VAL LEU PRO PHE VAL GLN ARG PHE ASN          
SEQRES   8 L  706  ASN ILE ASP GLY PHE MET THR LEU TYR VAL ALA ALA VAL          
SEQRES   9 L  706  LEU ILE HIS GLY ALA LEU PHE ALA VAL VAL ASP MET THR          
SEQRES  10 L  706  LEU ASN ILE TYR GLN VAL GLN PHE SER LEU THR ARG THR          
SEQRES  11 L  706  GLU TRP TYR LEU MET ASP PHE SER ASP TYR ILE ALA SER          
SEQRES  12 L  706  PHE VAL VAL ALA ILE ILE ILE ALA HIS PHE GLY SER LYS          
SEQRES  13 L  706  GLY ASN ARG THR ARG TRP ILE ALA ALA SER CYS ILE LEU          
SEQRES  14 L  706  MET GLY LEU GLU SER MET LEU PHE ALA PHE PRO PHE PHE          
SEQRES  15 L  706  THR TYR GLU ILE ILE ILE PRO GLY ARG GLN SER ILE GLU          
SEQRES  16 L  706  LEU CYS MET GLU GLU ASN GLU LYS ARG ASN ILE ILE CYS          
SEQRES  17 L  706  GLY ASN SER VAL PRO ASN ARG SER LYS CYS ILE TYR PHE          
SEQRES  18 L  706  HIS ILE GLY GLY GLN CYS ILE HIS GLY ILE ALA GLY MET          
SEQRES  19 L  706  PRO ILE TYR ILE LEU GLY ILE THR PHE ILE PHE ASP HIS          
SEQRES  20 L  706  ILE PRO THR SER SER CYS GLY PHE TYR LEU ALA ILE GLY          
SEQRES  21 L  706  HIS SER ALA TYR LEU ILE GLY TYR LEU LEU GLY MET VAL          
SEQRES  22 L  706  GLY GLY LEU GLN ASN PHE GLN PRO PRO PRO LYS GLU LYS          
SEQRES  23 L  706  THR VAL GLU ILE GLU PRO ALA LYS VAL TYR GLN LEU LEU          
SEQRES  24 L  706  GLN SER GLY TRP TRP LYS THR PHE LEU ILE ILE ALA ALA          
SEQRES  25 L  706  ILE SER PHE CYS VAL SER PHE MET MET VAL CYS PHE PRO          
SEQRES  26 L  706  THR SER LEU PRO GLY ALA HIS LYS LEU ARG LEU ALA LYS          
SEQRES  27 L  706  ARG LYS GLU PRO PRO THR ILE ASP ARG ARG LEU LYS ASP          
SEQRES  28 L  706  MET LYS ILE GLN PRO HIS LEU LYS GLY PHE LEU HIS ASN          
SEQRES  29 L  706  ILE TRP HIS ILE LEU LYS ASN PRO LEU MET LEU THR GLN          
SEQRES  30 L  706  ALA ILE CYS LYS VAL SER GLU TYR LEU THR PHE ASN THR          
SEQRES  31 L  706  SER LEU TYR PHE LEU PRO HIS HIS LEU GLN THR GLN PHE          
SEQRES  32 L  706  LEU ILE THR PRO GLY ILE ALA SER LEU LEU THR GLY ALA          
SEQRES  33 L  706  PHE VAL LEU PRO GLY GLY ILE ILE GLY HIS PHE LEU GLY          
SEQRES  34 L  706  GLY LEU ILE VAL ASP ARG LEU GLU MET THR ASN LYS ASN          
SEQRES  35 L  706  LYS LEU LYS PHE THR LEU VAL THR THR VAL VAL SER VAL          
SEQRES  36 L  706  GLY LEU PHE LEU LEU ILE PHE PHE VAL GLU CYS GLN THR          
SEQRES  37 L  706  THR THR PHE ALA GLY ILE ASN GLU ASP TYR ASP GLY TYR          
SEQRES  38 L  706  GLY GLN LEU GLY ASN LEU THR ALA ASP CYS ASN GLU TYR          
SEQRES  39 L  706  CYS ASP CYS THR THR SER LEU TYR THR SER ILE CYS GLY          
SEQRES  40 L  706  ARG ASP GLU LYS GLU TYR PHE SER PRO CYS PHE ALA GLY          
SEQRES  41 L  706  CYS LYS ALA THR LYS VAL SER GLN THR GLU LYS THR TYR          
SEQRES  42 L  706  TYR ASN CYS SER CYS ILE LYS GLU GLY LEU ALA ALA SER          
SEQRES  43 L  706  ASP ASP GLU GLY GLN PHE ILE ASP ALA ILE ALA GLY THR          
SEQRES  44 L  706  CYS ASP SER ASP CYS LEU LYS LEU PRO LEU PHE PHE ALA          
SEQRES  45 L  706  PHE TYR PHE SER ALA THR VAL PHE SER ASN MET CYS SER          
SEQRES  46 L  706  ILE PRO VAL ILE SER ILE ILE LEU GLN SER VAL PRO ALA          
SEQRES  47 L  706  ASN PHE THR SER LEU SER LEU GLY VAL THR TYR ALA ILE          
SEQRES  48 L  706  VAL LYS PHE VAL ALA SER VAL PRO ALA PRO LEU LEU PHE          
SEQRES  49 L  706  ARG LEU SER SER ALA ILE ALA CYS ILE TYR TRP ASP ASN          
SEQRES  50 L  706  ASN ARG CYS GLY GLY LYS GLU ARG CYS TRP ILE TYR ASN          
SEQRES  51 L  706  LYS ASN ILE LEU VAL TYR GLU PHE MET GLY ILE TRP MET          
SEQRES  52 L  706  SER SER GLN LEU ILE ILE VAL LEU LEU ASN ILE TYR ALA          
SEQRES  53 L  706  ILE GLN ILE HIS ASP VAL VAL VAL HIS GLY GLU ILE THR          
SEQRES  54 L  706  GLU SER LYS THR THR VAL LYS ASP VAL LYS GLU GLN LYS          
SEQRES  55 L  706  GLU ARG LYS ALA                                              
SEQRES   1 J  171  MET LEU PHE ILE ILE CYS LEU VAL PHE ILE SER CYS ASN          
SEQRES   2 J  171  VAL LEU ARG GLU VAL LYS TYR GLN GLU THR TRP CYS PHE          
SEQRES   3 J  171  PRO ALA TYR GLY MET VAL ILE GLY LEU TRP LEU MET LEU          
SEQRES   4 J  171  SER SER ILE PRO GLN ARG ARG LEU VAL LEU ASN HIS THR          
SEQRES   5 J  171  ARG GLY MET TYR HIS PHE SER ILE GLN GLY ARG THR VAL          
SEQRES   6 J  171  CYS GLN GLY PRO MET HIS LEU VAL TYR VAL ARG LEU ALA          
SEQRES   7 J  171  LEU SER SER ASP ALA TYR GLY GLY ARG PHE PHE GLN LEU          
SEQRES   8 J  171  VAL LEU CYS GLY HIS LYS LEU GLU PRO LEU VAL LEU VAL          
SEQRES   9 J  171  GLN LEU SER GLU ARG TYR GLU GLN MET GLU PHE LEU GLY          
SEQRES  10 J  171  ARG HIS LEU ALA ARG LYS LEU ASN ILE ASN TYR PHE ASP          
SEQRES  11 J  171  TYR LEU ALA SER SER TYR ARG HIS VAL VAL ARG HIS TRP          
SEQRES  12 J  171  PRO LEU GLY ALA SER PHE SER PRO GLY ILE VAL GLN ARG          
SEQRES  13 J  171  LYS THR GLN VAL TYR THR LYS SER SER VAL ASN ASP LEU          
SEQRES  14 J  171  ASP VAL                                                      
SEQRES   1 M  116  MET ARG TRP ARG ASP ARG ILE ALA VAL LEU CYS PHE PRO          
SEQRES   2 M  116  PRO GLY LEU MET LEU THR VAL ALA ALA LEU ILE LEU PHE          
SEQRES   3 M  116  PHE ILE HIS MET GLY VAL PHE ALA SER ASP VAL HIS ASN          
SEQRES   4 M  116  PHE CYS VAL ILE HIS ASN TYR ASP HIS MET SER PHE ARG          
SEQRES   5 M  116  TYR THR VAL VAL LEU ILE PHE SER GLN VAL ILE SER ILE          
SEQRES   6 M  116  GLY TRP ALA ALA MET GLY SER LEU TYR ALA GLU MET THR          
SEQRES   7 M  116  GLY ASP LYS PHE LEU ARG CYS PHE ALA LEU THR ILE LEU          
SEQRES   8 M  116  ILE LEU ASN GLY ALA MET PHE PHE ASN ARG LEU CYS LEU          
SEQRES   9 M  116  GLU PHE LEU ALA ILE ASN TYR ARG GLU GLU ARG HIS              
SEQRES   1 N   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 N   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 N   28  UNK UNK                                                      
SEQRES   1 I  216  MET LYS LEU THR PRO GLY CYS PHE LEU TRP TYR LEU TYR          
SEQRES   2 I  216  MET ASP LYS ILE TYR CYS LEU LEU SER LEU ARG ASN VAL          
SEQRES   3 I  216  LYS ALA LEU MET VAL TYR PHE HIS LEU LEU ASP VAL HIS          
SEQRES   4 I  216  HIS ARG ASN THR LEU ASN ASP VAL LEU PHE PHE HIS PHE          
SEQRES   5 I  216  LEU GLN HIS VAL THR ASN LEU ASN LYS SER GLN ILE GLY          
SEQRES   6 I  216  MET ILE PHE ASP LEU LEU ASP TRP THR ALA VAL GLY GLU          
SEQRES   7 I  216  ILE GLY PHE ASP GLN PHE TYR VAL LEU ILE CYS ILE LEU          
SEQRES   8 I  216  LEU ALA HIS GLN ASP HIS LEU GLU ASP HIS PHE MET TYR          
SEQRES   9 I  216  ARG HIS SER ARG PRO VAL PHE GLU LEU LEU ASP LEU ASP          
SEQRES  10 I  216  GLY GLU MET ASN ILE GLY ALA ALA ASN PHE GLN ASN TYR          
SEQRES  11 I  216  ARG PHE LEU PHE ASN ILE LYS LYS GLN GLU LEU ARG ASP          
SEQRES  12 I  216  LEU PHE HIS ASP PHE ASP ILE THR GLY ASP ARG LEU LEU          
SEQRES  13 I  216  ASN TYR LYS GLU PHE LYS LEU TYR THR ILE PHE CYS THR          
SEQRES  14 I  216  ASP LYS SER ILE ASP ARG LYS LYS ARG ARG LYS ASP ARG          
SEQRES  15 I  216  GLU ALA ALA ARG GLU ARG GLU LYS GLU LYS GLY LYS ASP          
SEQRES  16 I  216  LYS GLU LYS TYR LEU HIS LEU LYS LYS ILE TYR SER SER          
SEQRES  17 I  216  MET LEU SER HIS ARG SER ILE LEU                              
SEQRES   1 K  194  MET GLU GLU SER VAL LYS PRO VAL PRO LYS HIS ALA ASN          
SEQRES   2 K  194  HIS ARG ARG SER SER VAL ARG SER SER LEU TYR GLY ASP          
SEQRES   3 K  194  VAL ARG ASP LEU TRP SER THR ALA THR MET SER THR ALA          
SEQRES   4 K  194  ASN VAL SER VAL SER ASP VAL CYS GLU ASP PHE ASP GLU          
SEQRES   5 K  194  GLU GLY LYS SER VAL ARG ASN ARG ILE ARG LYS TYR SER          
SEQRES   6 K  194  GLN THR ILE SER ILE ARG ASP SER LEU ASN LEU GLU PRO          
SEQRES   7 K  194  GLU GLU ILE GLN GLN GLN ALA ARG ARG GLU LEU GLU LEU          
SEQRES   8 K  194  CYS HIS GLY ARG SER LEU GLU HIS GLY GLU ASP HIS GLU          
SEQRES   9 K  194  GLU SER GLU THR SER LEU ALA SER SER THR SER GLU SER          
SEQRES  10 K  194  LEU ILE PHE SER LEU TRP LYS PRO HIS ARG THR TYR TRP          
SEQRES  11 K  194  THR GLU GLN GLN ASN ARG LEU PRO LEU PRO LEU MET GLU          
SEQRES  12 K  194  LEU MET GLU THR GLU VAL LEU ASP ILE LEU LYS LYS ALA          
SEQRES  13 K  194  LEU ILE THR TYR ARG SER THR ILE GLY ARG ASN HIS PHE          
SEQRES  14 K  194  MET THR LYS GLU LEU GLN GLY TYR ILE GLU GLY ILE ARG          
SEQRES  15 K  194  LYS ARG ARG ASN LYS ARG LEU TYR PHE LEU ASP GLN              
HET    NAG  O   1      14                                                       
HET    NAG  O   2      14                                                       
HET    BMA  O   3      11                                                       
HET    BMA  O   4      11                                                       
HET    BMA  O   5      11                                                       
HET    BMA  O   6      11                                                       
HET    BMA  O   7      11                                                       
HET    NAG  P   1      14                                                       
HET    NAG  P   2      14                                                       
HET    NAG  Q   1      14                                                       
HET    NAG  Q   2      14                                                       
HET    BMA  Q   3      11                                                       
HET    NAG  R   1      14                                                       
HET    NAG  R   2      14                                                       
HET    BMA  R   3      11                                                       
HET    NAG  S   1      14                                                       
HET    NAG  S   2      14                                                       
HET    NAG  T   1      14                                                       
HET    NAG  T   2      14                                                       
HET    NAG  U   1      14                                                       
HET    NAG  U   2      14                                                       
HET    BMA  U   3      11                                                       
HET    NAG  V   1      14                                                       
HET    NAG  V   2      14                                                       
HET    NAG  W   1      14                                                       
HET    NAG  W   2      14                                                       
HET    BMA  W   3      11                                                       
HET    NAG  X   1      14                                                       
HET    NAG  X   2      14                                                       
HET    NAG  Y   1      14                                                       
HET    NAG  Y   2      14                                                       
HET    BMA  Y   3      11                                                       
HET    BMA  Y   4      11                                                       
HET    BMA  Y   5      11                                                       
HET    NAG  Z   1      14                                                       
HET    NAG  Z   2      14                                                       
HET    BMA  Z   3      11                                                       
HET    BMA  Z   4      11                                                       
HET    BMA  Z   5      11                                                       
HET    BMA  Z   6      11                                                       
HET    BMA  Z   7      11                                                       
HET    NAG  a   1      14                                                       
HET    NAG  a   2      14                                                       
HET    NAG  b   1      14                                                       
HET    NAG  b   2      14                                                       
HET    BMA  b   3      11                                                       
HET    NAG  c   1      14                                                       
HET    NAG  c   2      14                                                       
HET    BMA  c   3      11                                                       
HET    BMA  c   4      11                                                       
HET    BMA  c   5      11                                                       
HET    NAG  d   1      14                                                       
HET    NAG  d   2      14                                                       
HET     NA  A 701       1                                                       
HET    9Z9  A 702      39                                                       
HET    9Z9  A 703      39                                                       
HET    9Z9  A 704      39                                                       
HET     NA  D1001       1                                                       
HET    NAG  E1201      14                                                       
HET    NAG  E1202      14                                                       
HET    NAG  E1203      14                                                       
HET    NAG  E1204      14                                                       
HET    NAG  F1201      14                                                       
HET    NAG  G 901      14                                                       
HET    NAG  G 902      14                                                       
HET    NAG  G 903      14                                                       
HET    NAG  H1001      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM      NA SODIUM ION                                                       
HETNAM     9Z9 (3BETA,14BETA,17BETA,25R)-3-[4-METHOXY-3-                        
HETNAM   2 9Z9  (METHOXYMETHYL)BUTOXY]SPIROST-5-EN                              
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
FORMUL  15  NAG    41(C8 H15 N O6)                                              
FORMUL  15  BMA    21(C6 H12 O6)                                                
FORMUL  31   NA    2(NA 1+)                                                     
FORMUL  32  9Z9    3(C34 H56 O5)                                                
HELIX    1 AA1 GLY A  339  GLN A  349  1                                  11    
HELIX    2 AA2 GLY A  352  GLN A  371  1                                  20    
HELIX    3 AA3 GLY A  380  ASP A  413  1                                  34    
HELIX    4 AA4 ASP A  413  ILE A  435  1                                  23    
HELIX    5 AA5 SER A  439  ASN A  444  1                                   6    
HELIX    6 AA6 HIS A  445  MET A  457  1                                  13    
HELIX    7 AA7 LEU A  460  SER A  470  1                                  11    
HELIX    8 AA8 LEU A  475  PHE A  511  1                                  37    
HELIX    9 AA9 ASP A  515  GLN A  520  1                                   6    
HELIX   10 AB1 ASN A  521  LEU A  533  1                                  13    
HELIX   11 AB2 ASP A  537  GLY A  549  1                                  13    
HELIX   12 AB3 TYR A  552  PHE A  568  1                                  17    
HELIX   13 AB4 PHE A  568  GLU A  594  1                                  27    
HELIX   14 AB5 LEU B   95  LEU B  103  1                                   9    
HELIX   15 AB6 SER B  105  LEU B  129  1                                  25    
HELIX   16 AB7 LEU B  137  SER B  166  1                                  30    
HELIX   17 AB8 SER B  168  LYS B  172  5                                   5    
HELIX   18 AB9 ASP B  173  GLY B  196  1                                  24    
HELIX   19 AC1 SER B  201  CYS B  210  1                                  10    
HELIX   20 AC2 ARG B  211  ARG B  214  5                                   4    
HELIX   21 AC3 SER B  215  ARG B  221  1                                   7    
HELIX   22 AC4 GLN B  224  MET B  239  1                                  16    
HELIX   23 AC5 MET B  239  PHE B  261  1                                  23    
HELIX   24 AC6 ASP B  280  THR B  293  1                                  14    
HELIX   25 AC7 HIS B  296  LYS B  306  1                                  11    
HELIX   26 AC8 PHE B  314  GLY B  326  1                                  13    
HELIX   27 AC9 ILE B  328  GLN B  374  1                                  47    
HELIX   28 AD1 CYS C   39  LYS C   48  1                                  10    
HELIX   29 AD2 SER C   49  GLY C   70  1                                  22    
HELIX   30 AD3 ASN C   72  GLU C   78  1                                   7    
HELIX   31 AD4 PHE C   79  VAL C  104  1                                  26    
HELIX   32 AD5 ILE C  107  LYS C  111  5                                   5    
HELIX   33 AD6 ASP C  112  ILE C  134  1                                  23    
HELIX   34 AD7 TYR C  141  ILE C  148  1                                   8    
HELIX   35 AD8 GLN C  149  TYR C  159  5                                  11    
HELIX   36 AD9 SER C  160  GLU C  172  1                                  13    
HELIX   37 AE1 THR C  173  GLY C  200  1                                  28    
HELIX   38 AE2 ASN C  212  THR C  225  1                                  14    
HELIX   39 AE3 GLY C  228  LYS C  238  1                                  11    
HELIX   40 AE4 VAL C  243  SER C  256  1                                  14    
HELIX   41 AE5 PHE C  259  GLY C  315  1                                  57    
HELIX   42 AE6 GLN D   53  ARG D   66  1                                  14    
HELIX   43 AE7 HIS D   67  THR D   89  1                                  23    
HELIX   44 AE8 ASN D   90  HIS D   97  1                                   8    
HELIX   45 AE9 HIS D   97  ASN D  122  1                                  26    
HELIX   46 AF1 GLY D  123  TRP D  128  1                                   6    
HELIX   47 AF2 GLY D  131  ILE D  149  1                                  19    
HELIX   48 AF3 MET D  154  TYR D  159  1                                   6    
HELIX   49 AF4 PRO D  160  ARG D  165  1                                   6    
HELIX   50 AF5 ARG D  165  MET D  171  1                                   7    
HELIX   51 AF6 LEU D  176  GLY D  213  1                                  38    
HELIX   52 AF7 ASN D  222  THR D  235  1                                  14    
HELIX   53 AF8 GLY D  238  MET D  248  1                                  11    
HELIX   54 AF9 TYR D  253  ALA D  271  1                                  19    
HELIX   55 AG1 LEU D  277  THR D  292  1                                  16    
HELIX   56 AG2 GLU E   72  GLY E   80  1                                   9    
HELIX   57 AG3 PRO E  115  ILE E  119  5                                   5    
HELIX   58 AG4 GLU E  156  TRP E  161  1                                   6    
HELIX   59 AG5 VAL E  172  PRO E  177  5                                   6    
HELIX   60 AG6 LEU E  227  LEU E  235  1                                   9    
HELIX   61 AG7 GLU E  287  ARG E  293  1                                   7    
HELIX   62 AG8 PRO E  560  ARG E  568  5                                   9    
HELIX   63 AG9 LYS E  570  LEU E  574  5                                   5    
HELIX   64 AH1 SER E  621  LEU E  625  5                                   5    
HELIX   65 AH2 MET E  685  ILE E  689  5                                   5    
HELIX   66 AH3 LEU E  696  TRP E  700  5                                   5    
HELIX   67 AH4 PRO E  846  GLY E  853  1                                   8    
HELIX   68 AH5 HIS E  902  THR E  907  1                                   6    
HELIX   69 AH6 SER E  925  SER E  931  1                                   7    
HELIX   70 AH7 PHE E  936  LYS E  940  5                                   5    
HELIX   71 AH8 LYS E  997  LYS E 1007  1                                  11    
HELIX   72 AH9 HIS E 1059  HIS E 1086  1                                  28    
HELIX   73 AI1 VAL F   75  LEU F   82  1                                   8    
HELIX   74 AI2 ASN F  110  MET F  121  1                                  12    
HELIX   75 AI3 LYS F  229  LEU F  235  1                                   7    
HELIX   76 AI4 SER F  393  LYS F  397  5                                   5    
HELIX   77 AI5 ALA F  412  GLU F  414  5                                   3    
HELIX   78 AI6 SER F  550  GLN F  563  1                                  14    
HELIX   79 AI7 PRO F  604  TYR F  611  1                                   8    
HELIX   80 AI8 LYS F  646  ARG F  652  1                                   7    
HELIX   81 AI9 ASN F  671  TYR F  692  1                                  22    
HELIX   82 AJ1 PRO F  703  GLN F  709  1                                   7    
HELIX   83 AJ2 HIS F  710  LYS F  713  5                                   4    
HELIX   84 AJ3 ASP F  714  ASN F  724  1                                  11    
HELIX   85 AJ4 ASN F  734  ASN F  736  5                                   3    
HELIX   86 AJ5 THR F  776  SER F  780  5                                   5    
HELIX   87 AJ6 ASN F  786  LEU F  791  1                                   6    
HELIX   88 AJ7 ASP F  799  LEU F  803  5                                   5    
HELIX   89 AJ8 MET F  835  ASN F  839  5                                   5    
HELIX   90 AJ9 ASP F  887  ASN F  899  1                                  13    
HELIX   91 AK1 THR F  960  SER F  969  1                                  10    
HELIX   92 AK2 THR F  987  LYS F  991  5                                   5    
HELIX   93 AK3 SER F 1058  PHE F 1083  1                                  26    
HELIX   94 AK4 GLY G  146  ASN G  155  1                                  10    
HELIX   95 AK5 ASN G  184  SER G  189  5                                   6    
HELIX   96 AK6 ASP G  285  ASN G  290  1                                   6    
HELIX   97 AK7 VAL G  370  LEU G  374  1                                   5    
HELIX   98 AK8 GLN G  460  GLY G  464  1                                   5    
HELIX   99 AK9 ASP G  467  ALA G  472  1                                   6    
HELIX  100 AL1 ASN G  528  LYS G  534  1                                   7    
HELIX  101 AL2 GLU G  563  GLY G  568  1                                   6    
HELIX  102 AL3 LEU G  724  TYR G  741  1                                  18    
HELIX  103 AL4 TYR G  741  ARG G  748  1                                   8    
HELIX  104 AL5 SER H  159  ILE H  164  1                                   6    
HELIX  105 AL6 SER H  171  LEU H  184  1                                  14    
HELIX  106 AL7 SER H  309  HIS H  314  1                                   6    
HELIX  107 AL8 GLN H  366  LEU H  373  1                                   8    
HELIX  108 AL9 ALA H  393  PHE H  395  5                                   3    
HELIX  109 AM1 THR H  403  LEU H  410  1                                   8    
HELIX  110 AM2 ASN H  517  SER H  522  1                                   6    
HELIX  111 AM3 PRO H  601  GLY H  614  1                                  14    
HELIX  112 AM4 ASN H  699  ASN H  707  1                                   9    
HELIX  113 AM5 ASP H  780  GLY H  785  1                                   6    
HELIX  114 AM6 THR H  832  GLY H  837  1                                   6    
HELIX  115 AM7 THR H  844  ASN H  852  1                                   9    
HELIX  116 AM8 PRO H  856  TRP H  861  1                                   6    
HELIX  117 AM9 PRO H  868  TYR H  872  5                                   5    
HELIX  118 AN1 SER H  937  TYR H  967  1                                  31    
HELIX  119 AN2 LEU L   84  PHE L   90  1                                   7    
HELIX  120 AN3 ASN L   92  PHE L  125  1                                  34    
HELIX  121 AN4 THR L  128  ILE L  148  1                                  21    
HELIX  122 AN5 ILE L  148  GLY L  157  1                                  10    
HELIX  123 AN6 ASN L  158  PHE L  177  1                                  20    
HELIX  124 AN7 ALA L  178  TYR L  184  1                                   7    
HELIX  125 AN8 LYS L  203  ILE L  207  5                                   5    
HELIX  126 AN9 ARG L  215  ILE L  248  1                                  34    
HELIX  127 AO1 PRO L  249  GLN L  280  1                                  32    
HELIX  128 AO2 GLU L  289  PHE L  324  1                                  36    
HELIX  129 AO3 LEU L  328  LYS L  340  1                                  13    
HELIX  130 AO4 HIS L  357  ASN L  371  1                                  15    
HELIX  131 AO5 ASN L  371  GLN L  402  1                                  32    
HELIX  132 AO6 THR L  406  ALA L  416  1                                  11    
HELIX  133 AO7 PHE L  417  GLU L  437  1                                  21    
HELIX  134 AO8 THR L  439  CYS L  466  1                                  28    
HELIX  135 AO9 ALA L  489  CYS L  495  1                                   7    
HELIX  136 AP1 LEU L  565  SER L  595  1                                  31    
HELIX  137 AP2 PRO L  597  PHE L  600  5                                   4    
HELIX  138 AP3 THR L  601  PHE L  614  1                                  14    
HELIX  139 AP4 VAL L  618  CYS L  632  1                                  15    
HELIX  140 AP5 ASN L  652  THR L  689  1                                  38    
HELIX  141 AP6 LEU J    2  GLU J   17  1                                  16    
HELIX  142 AP7 TYR J   29  SER J   41  1                                  13    
HELIX  143 AP8 GLU J  111  LEU J  124  1                                  14    
HELIX  144 AP9 TYR J  128  ALA J  133  1                                   6    
HELIX  145 AQ1 PHE J  149  VAL J  160  1                                  12    
HELIX  146 AQ2 ARG M    2  LEU M   10  1                                   9    
HELIX  147 AQ3 PRO M   13  VAL M   42  1                                  30    
HELIX  148 AQ4 TYR M   53  GLY M   79  1                                  27    
HELIX  149 AQ5 ASP M   80  LEU M  102  1                                  23    
HELIX  150 AQ6 LEU M  102  ALA M  108  1                                   7    
HELIX  151 AQ7 UNK N   11  UNK N   30  1                                  20    
HELIX  152 AQ8 THR I    4  TYR I   18  1                                  15    
HELIX  153 AQ9 ARG I   24  ASP I   37  1                                  14    
HELIX  154 AR1 ASP I   46  THR I   57  1                                  12    
HELIX  155 AR2 ASN I   60  ASP I   72  1                                  13    
HELIX  156 AR3 PHE I   81  LEU I   92  1                                  12    
HELIX  157 AR4 ASP I   96  HIS I  106  1                                  11    
HELIX  158 AR5 GLY I  123  PHE I  134  1                                  12    
HELIX  159 AR6 LYS I  137  ASP I  149  1                                  13    
HELIX  160 AR7 ASN I  157  ASP I  174  1                                  18    
HELIX  161 AR8 SER K   42  CYS K   47  1                                   6    
HELIX  162 AR9 SER K   56  ASN K   75  1                                  20    
HELIX  163 AS1 GLU K   77  GLY K   94  1                                  18    
HELIX  164 AS2 GLU K  101  SER K  112  1                                  12    
HELIX  165 AS3 SER K  112  ASN K  135  1                                  24    
HELIX  166 AS4 LEU K  139  SER K  162  1                                  24    
HELIX  167 AS5 HIS K  168  ASN K  186  1                                  19    
SHEET    1 AA1 3 PHE E  33  SER E  36  0                                        
SHEET    2 AA1 3 LEU E  56  PHE E  62 -1  O  PHE E  61   N  SER E  34           
SHEET    3 AA1 3 TRP E 110  ILE E 114 -1  O  ILE E 114   N  LEU E  56           
SHEET    1 AA2 5 ILE E  47  LEU E  51  0                                        
SHEET    2 AA2 5 ASP E 145  ASP E 152  1  O  LEU E 151   N  LEU E  51           
SHEET    3 AA2 5 TRP E 131  THR E 136 -1  N  ILE E 133   O  GLY E 148           
SHEET    4 AA2 5 ASN E  85  THR E  89 -1  N  ASN E  85   O  THR E 136           
SHEET    5 AA2 5 TYR E  94  TYR E  98 -1  O  TYR E  97   N  MET E  86           
SHEET    1 AA3 5 ARG E 165  VAL E 166  0                                        
SHEET    2 AA3 5 CYS E 222  ASP E 226 -1  O  ASP E 226   N  ARG E 165           
SHEET    3 AA3 5 PHE E 208  THR E 212 -1  N  ILE E 209   O  HIS E 225           
SHEET    4 AA3 5 LEU E 195  MET E 200 -1  N  ILE E 196   O  GLY E 210           
SHEET    5 AA3 5 VAL E 179  THR E 185 -1  N  ASN E 180   O  MET E 199           
SHEET    1 AA4 4 VAL E 244  LEU E 249  0                                        
SHEET    2 AA4 4 LEU E 254  THR E 258 -1  O  VAL E 255   N  VAL E 248           
SHEET    3 AA4 4 GLY E 261  SER E 265 -1  O  TYR E 263   N  ILE E 256           
SHEET    4 AA4 4 LEU E 278  ALA E 281 -1  O  SER E 279   N  VAL E 264           
SHEET    1 AA5 3 GLY E 294  TYR E 298  0                                        
SHEET    2 AA5 3 VAL E 314  PHE E 318 -1  O  THR E 315   N  TRP E 297           
SHEET    3 AA5 3 CYS E 330  SER E 333 -1  O  PHE E 331   N  ILE E 316           
SHEET    1 AA6 4 PRO E 355  ASP E 363  0                                        
SHEET    2 AA6 4 SER E 368  VAL E 375 -1  O  ILE E 370   N  LEU E 361           
SHEET    3 AA6 4 THR E 381  LYS E 389 -1  O  THR E 384   N  TYR E 371           
SHEET    4 AA6 4 LYS E 392  PRO E 393 -1  O  LYS E 392   N  LYS E 389           
SHEET    1 AA7 4 PRO E 355  ASP E 363  0                                        
SHEET    2 AA7 4 SER E 368  VAL E 375 -1  O  ILE E 370   N  LEU E 361           
SHEET    3 AA7 4 THR E 381  LYS E 389 -1  O  THR E 384   N  TYR E 371           
SHEET    4 AA7 4 PHE E 399  HIS E 403 -1  O  PHE E 402   N  VAL E 383           
SHEET    1 AA8 4 PRO E 411  PHE E 416  0                                        
SHEET    2 AA8 4 LEU E 423  GLY E 427 -1  O  TYR E 424   N  ILE E 415           
SHEET    3 AA8 4 GLN E 429  SER E 433 -1  O  TRP E 431   N  VAL E 425           
SHEET    4 AA8 4 GLU E 441  ASN E 445 -1  O  GLU E 441   N  VAL E 432           
SHEET    1 AA9 4 VAL E 451  ASN E 456  0                                        
SHEET    2 AA9 4 ASP E 462  VAL E 467 -1  O  VAL E 464   N  SER E 455           
SHEET    3 AA9 4 ARG E 471  LYS E 476 -1  O  LEU E 473   N  PHE E 465           
SHEET    4 AA9 4 SER E 483  ILE E 487 -1  O  SER E 483   N  THR E 474           
SHEET    1 AB1 3 THR E 494  TYR E 497  0                                        
SHEET    2 AB1 3 ILE E 503  THR E 507 -1  O  LEU E 506   N  THR E 494           
SHEET    3 AB1 3 ASN E 510  ASP E 512 -1  O  ASN E 510   N  THR E 507           
SHEET    1 AB2 6 ILE E 538  TYR E 543  0                                        
SHEET    2 AB2 6 GLU E 548  HIS E 554 -1  O  HIS E 554   N  ILE E 538           
SHEET    3 AB2 6 PHE E 601  ILE E 609 -1  O  THR E 607   N  MET E 549           
SHEET    4 AB2 6 LEU E 585  MET E 593 -1  N  ASN E 587   O  GLU E 608           
SHEET    5 AB2 6 LYS E 576  GLU E 579 -1  N  LYS E 576   O  ILE E 588           
SHEET    6 AB2 6 SER E 714  THR E 717 -1  O  SER E 714   N  GLU E 579           
SHEET    1 AB3 7 LEU E 693  PHE E 695  0                                        
SHEET    2 AB3 7 LEU E 628  TYR E 632 -1  N  LEU E 628   O  PHE E 695           
SHEET    3 AB3 7 TYR E 638  LEU E 642 -1  O  LYS E 641   N  GLU E 629           
SHEET    4 AB3 7 THR E 678  THR E 684 -1  O  ALA E 679   N  ILE E 640           
SHEET    5 AB3 7 SER E 667  ILE E 673 -1  N  ASN E 672   O  SER E 680           
SHEET    6 AB3 7 LYS E 658  LEU E 661 -1  N  VAL E 660   O  PHE E 668           
SHEET    7 AB3 7 PHE E 701  TYR E 703 -1  O  PHE E 701   N  LEU E 661           
SHEET    1 AB4 4 TYR E 722  GLN E 725  0                                        
SHEET    2 AB4 4 THR E 745  PRO E 754 -1  O  LYS E 751   N  GLN E 725           
SHEET    3 AB4 4 TYR E 789  GLY E 797 -1  O  VAL E 795   N  ILE E 746           
SHEET    4 AB4 4 VAL E 775  PHE E 783 -1  N  VAL E 782   O  TYR E 790           
SHEET    1 AB5 4 VAL E 737  ILE E 740  0                                        
SHEET    2 AB5 4 THR E 826  SER E 829  1  O  LYS E 828   N  LYS E 738           
SHEET    3 AB5 4 GLY E 803  VAL E 810 -1  N  THR E 805   O  ILE E 827           
SHEET    4 AB5 4 SER E 766  VAL E 769 -1  N  SER E 766   O  VAL E 810           
SHEET    1 AB6 4 VAL E 737  ILE E 740  0                                        
SHEET    2 AB6 4 THR E 826  SER E 829  1  O  LYS E 828   N  LYS E 738           
SHEET    3 AB6 4 GLY E 803  VAL E 810 -1  N  THR E 805   O  ILE E 827           
SHEET    4 AB6 4 THR E 822  LEU E 823 -1  O  LEU E 823   N  LEU E 809           
SHEET    1 AB7 3 THR E 836  HIS E 839  0                                        
SHEET    2 AB7 3 LEU E 957  ASN E 961 -1  O  GLU E 958   N  HIS E 838           
SHEET    3 AB7 3 ASP E 964  SER E 967 -1  O  ASP E 964   N  ASN E 961           
SHEET    1 AB8 5 ILE E 864  THR E 866  0                                        
SHEET    2 AB8 5 LYS E 942  PHE E 946 -1  O  VAL E 943   N  LYS E 865           
SHEET    3 AB8 5 SER E1042  VAL E1049  1  O  TYR E1048   N  PHE E 946           
SHEET    4 AB8 5 LEU E1025  VAL E1032 -1  N  VAL E1030   O  GLU E1043           
SHEET    5 AB8 5 VAL E 974  GLU E 978 -1  N  THR E 975   O  SER E1031           
SHEET    1 AB9 3 VAL E 950  PRO E 954  0                                        
SHEET    2 AB9 3 ASN E1017  ILE E1020 -1  O  LEU E1018   N  TYR E 953           
SHEET    3 AB9 3 TRP E 985  LYS E 988 -1  N  GLN E 986   O  THR E1019           
SHEET    1 AC1 4 THR F  46  ASN F  52  0                                        
SHEET    2 AC1 4 TYR F  99  SER F 105 -1  O  GLN F 101   N  VAL F  50           
SHEET    3 AC1 4 LEU F 168  PRO F 173 -1  O  THR F 172   N  LEU F 100           
SHEET    4 AC1 4 ALA F 152  ARG F 155 -1  N  ALA F 152   O  TYR F 171           
SHEET    1 AC2 6 LYS F 199  TYR F 202  0                                        
SHEET    2 AC2 6 VAL F 182  TYR F 188 -1  N  VAL F 185   O  PHE F 201           
SHEET    3 AC2 6 MET F 126  MET F 132 -1  N  MET F 126   O  TYR F 188           
SHEET    4 AC2 6 ASN F 144  GLU F 150 -1  O  MET F 149   N  VAL F 127           
SHEET    5 AC2 6 THR F 653  ALA F 658  1  O  GLU F 654   N  GLN F 146           
SHEET    6 AC2 6 TYR F 738  LEU F 741 -1  O  GLN F 739   N  VAL F 657           
SHEET    1 AC3 2 LEU F 209  LYS F 210  0                                        
SHEET    2 AC3 2 LEU F 218  PHE F 219 -1  O  LEU F 218   N  LYS F 210           
SHEET    1 AC4 4 GLY F 222  TYR F 223  0                                        
SHEET    2 AC4 4 VAL F 273  LEU F 277 -1  O  GLU F 276   N  TYR F 223           
SHEET    3 AC4 4 SER F 261  ASP F 266 -1  N  PHE F 264   O  VAL F 273           
SHEET    4 AC4 4 VAL F 250  LEU F 253 -1  N  PHE F 251   O  SER F 265           
SHEET    1 AC5 5 TRP F 242  TYR F 243  0                                        
SHEET    2 AC5 5 HIS F 299  THR F 304  1  O  ALA F 303   N  TRP F 242           
SHEET    3 AC5 5 THR F 307  GLN F 312 -1  O  ARG F 311   N  HIS F 299           
SHEET    4 AC5 5 LEU F 315  THR F 320 -1  O  LEU F 315   N  GLN F 312           
SHEET    5 AC5 5 VAL F 337  VAL F 339 -1  O  VAL F 337   N  TYR F 318           
SHEET    1 AC6 4 ILE F 345  PRO F 350  0                                        
SHEET    2 AC6 4 GLU F 359  THR F 365 -1  O  LEU F 364   N  ARG F 347           
SHEET    3 AC6 4 ILE F 373  THR F 379 -1  O  HIS F 374   N  ALA F 363           
SHEET    4 AC6 4 LEU F 382  MET F 387 -1  O  GLU F 386   N  ILE F 375           
SHEET    1 AC7 4 CYS F 403  ILE F 411  0                                        
SHEET    2 AC7 4 ASN F 416  ILE F 423 -1  O  LEU F 418   N  THR F 409           
SHEET    3 AC7 4 PHE F 428  ASN F 434 -1  O  TYR F 429   N  VAL F 421           
SHEET    4 AC7 4 THR F 439  ILE F 446 -1  O  TYR F 444   N  LEU F 430           
SHEET    1 AC8 5 PHE F 458  VAL F 460  0                                        
SHEET    2 AC8 5 ILE F 503  LEU F 505 -1  O  PHE F 504   N  LEU F 459           
SHEET    3 AC8 5 ILE F 493  SER F 496 -1  N  GLN F 495   O  ILE F 503           
SHEET    4 AC8 5 MET F 485  GLY F 490 -1  N  LEU F 486   O  SER F 496           
SHEET    5 AC8 5 PRO F 474  ASN F 480 -1  N  ASN F 480   O  MET F 485           
SHEET    1 AC9 4 ILE F 514  ASN F 519  0                                        
SHEET    2 AC9 4 GLN F 524  THR F 529 -1  O  ALA F 526   N  VAL F 518           
SHEET    3 AC9 4 ILE F 534  LEU F 538 -1  O  PHE F 537   N  MET F 525           
SHEET    4 AC9 4 VAL F 544  GLN F 546 -1  O  TYR F 545   N  TYR F 536           
SHEET    1 AD1 3 GLU F 572  GLU F 580  0                                        
SHEET    2 AD1 3 LYS F 583  LEU F 590 -1  O  LYS F 583   N  GLU F 580           
SHEET    3 AD1 3 ARG F 597  LEU F 602 -1  O  ARG F 601   N  GLN F 586           
SHEET    1 AD2 2 PHE F 617  GLN F 622  0                                        
SHEET    2 AD2 2 TYR F 625  PHE F 630 -1  O  TYR F 625   N  GLN F 622           
SHEET    1 AD3 4 GLU F 638  ILE F 642  0                                        
SHEET    2 AD3 4 TRP F 761  LEU F 769 -1  O  LEU F 769   N  GLU F 638           
SHEET    3 AD3 4 ALA F 817  ILE F 825 -1  O  ILE F 822   N  ILE F 764           
SHEET    4 AD3 4 SER F 804  LEU F 812 -1  N  LEU F 812   O  ALA F 817           
SHEET    1 AD4 2 LEU F 662  VAL F 663  0                                        
SHEET    2 AD4 2 ILE F 731  TYR F 732 -1  O  TYR F 732   N  LEU F 662           
SHEET    1 AD5 4 PHE F 754  LEU F 756  0                                        
SHEET    2 AD5 4 PHE F 869  ILE F 876  1  O  PHE F 875   N  PHE F 754           
SHEET    3 AD5 4 LYS F 841  VAL F 849 -1  N  MET F 845   O  VAL F 872           
SHEET    4 AD5 4 ILE F 793  ILE F 797 -1  N  ALA F 794   O  LYS F 848           
SHEET    1 AD6 2 ILE F 857  THR F 860  0                                        
SHEET    2 AD6 2 GLY F 863  ILE F 866 -1  O  GLY F 863   N  THR F 860           
SHEET    1 AD7 3 LYS F 882  PHE F 886  0                                        
SHEET    2 AD7 3 PHE F 925  ASP F 929 -1  O  LEU F 926   N  ALA F 885           
SHEET    3 AD7 3 SER F 935  SER F 937 -1  O  GLY F 936   N  VAL F 927           
SHEET    1 AD8 5 CYS F 914  LEU F 916  0                                        
SHEET    2 AD8 5 LEU F1046  HIS F1053  1  O  HIS F1051   N  PHE F 915           
SHEET    3 AD8 5 GLU F1024  SER F1032 -1  N  VAL F1031   O  LEU F1046           
SHEET    4 AD8 5 VAL F 943  GLY F 950 -1  N  GLY F 950   O  PHE F1026           
SHEET    5 AD8 5 ARG F 957  ASP F 958 -1  O  ARG F 957   N  GLY F 949           
SHEET    1 AD9 2 TRP F 979  LYS F 980  0                                        
SHEET    2 AD9 2 GLU F1003  TRP F1004 -1  O  GLU F1003   N  LYS F 980           
SHEET    1 AE1 4 VAL G  22  VAL G  25  0                                        
SHEET    2 AE1 4 ASP G 362  ASN G 369 -1  O  PHE G 363   N  VAL G  25           
SHEET    3 AE1 4 ILE G 346  VAL G 353 -1  N  THR G 351   O  ASP G 364           
SHEET    4 AE1 4 SER G 338  ASP G 343 -1  N  SER G 338   O  LEU G 350           
SHEET    1 AE2 2 ASP G  40  PRO G  41  0                                        
SHEET    2 AE2 2 THR G  83  VAL G  84 -1  O  VAL G  84   N  ASP G  40           
SHEET    1 AE3 5 PHE G  43  TYR G  44  0                                        
SHEET    2 AE3 5 SER G  94  HIS G  99  1  O  ILE G  95   N  PHE G  43           
SHEET    3 AE3 5 LEU G 105  ILE G 110 -1  O  VAL G 109   N  THR G  96           
SHEET    4 AE3 5 LYS G 113  ASP G 118 -1  O  TYR G 117   N  VAL G 106           
SHEET    5 AE3 5 TRP G 124  LYS G 126 -1  O  ARG G 125   N  SER G 116           
SHEET    1 AE4 3 PHE G  50  LYS G  53  0                                        
SHEET    2 AE4 3 SER G  61  LEU G  64 -1  O  LEU G  64   N  PHE G  50           
SHEET    3 AE4 3 PHE G  69  THR G  71 -1  O  PHE G  69   N  TYR G  63           
SHEET    1 AE5 4 HIS G 136  GLY G 139  0                                        
SHEET    2 AE5 4 LEU G 156  TYR G 159 -1  O  TYR G 159   N  HIS G 136           
SHEET    3 AE5 4 ILE G 170  SER G 173 -1  O  TYR G 171   N  ALA G 158           
SHEET    4 AE5 4 GLN G 181  MET G 183 -1  O  GLN G 181   N  PHE G 172           
SHEET    1 AE6 4 THR G 194  LEU G 201  0                                        
SHEET    2 AE6 4 GLN G 206  VAL G 212 -1  O  GLN G 206   N  LEU G 201           
SHEET    3 AE6 4 LEU G 216  TYR G 221 -1  O  HIS G 220   N  VAL G 209           
SHEET    4 AE6 4 SER G 229  MET G 230 -1  O  SER G 229   N  TYR G 221           
SHEET    1 AE7 4 THR G 194  LEU G 201  0                                        
SHEET    2 AE7 4 GLN G 206  VAL G 212 -1  O  GLN G 206   N  LEU G 201           
SHEET    3 AE7 4 LEU G 216  TYR G 221 -1  O  HIS G 220   N  VAL G 209           
SHEET    4 AE7 4 PHE G 234  SER G 235 -1  O  PHE G 234   N  GLY G 217           
SHEET    1 AE8 4 GLU G 241  MET G 244  0                                        
SHEET    2 AE8 4 MET G 252  ASN G 256 -1  O  TRP G 255   N  GLU G 241           
SHEET    3 AE8 4 SER G 259  SER G 263 -1  O  LEU G 261   N  LEU G 254           
SHEET    4 AE8 4 GLU G 271  HIS G 272 -1  O  GLU G 271   N  VAL G 262           
SHEET    1 AE9 6 ILE G 280  ASP G 283  0                                        
SHEET    2 AE9 6 ARG G 274  ASP G 277 -1  N  LEU G 275   O  THR G 282           
SHEET    3 AE9 6 TYR G 323  LYS G 326  1  O  VAL G 324   N  ILE G 276           
SHEET    4 AE9 6 HIS G 311  SER G 316 -1  N  TYR G 314   O  ILE G 325           
SHEET    5 AE9 6 LEU G 303  VAL G 307 -1  N  PHE G 305   O  TYR G 313           
SHEET    6 AE9 6 ILE G 293  SER G 298 -1  N  TYR G 294   O  LEU G 306           
SHEET    1 AF1 4 VAL G 386  GLU G 390  0                                        
SHEET    2 AF1 4 LEU G 406  PRO G 414 -1  O  LEU G 411   N  GLU G 390           
SHEET    3 AF1 4 SER G 449  GLN G 459 -1  O  TYR G 451   N  MET G 412           
SHEET    4 AF1 4 LEU G 432  ASN G 443 -1  N  ASN G 439   O  LYS G 452           
SHEET    1 AF2 4 PHE G 398  ILE G 400  0                                        
SHEET    2 AF2 4 LEU G 499  VAL G 505  1  O  SER G 504   N  PHE G 398           
SHEET    3 AF2 4 ALA G 478  ILE G 486 -1  N  SER G 480   O  ILE G 503           
SHEET    4 AF2 4 PRO G 422  VAL G 426 -1  N  LEU G 423   O  ASP G 485           
SHEET    1 AF3 3 LYS G 512  VAL G 515  0                                        
SHEET    2 AF3 3 VAL G 583  LYS G 587 -1  O  TRP G 586   N  LYS G 512           
SHEET    3 AF3 3 ILE G 590  ILE G 594 -1  O  GLU G 593   N  LEU G 585           
SHEET    1 AF4 2 THR G 537  THR G 539  0                                        
SHEET    2 AF4 2 ILE G 559  PHE G 561 -1  O  VAL G 560   N  TYR G 538           
SHEET    1 AF5 4 ARG G 571  TYR G 574  0                                        
SHEET    2 AF5 4 ASN G 704  HIS G 712  1  O  TYR G 710   N  ARG G 571           
SHEET    3 AF5 4 ILE G 686  VAL G 693 -1  N  TYR G 687   O  VAL G 709           
SHEET    4 AF5 4 TYR G 599  GLU G 603 -1  N  VAL G 600   O  SER G 692           
SHEET    1 AF6 2 TYR G 610  TYR G 612  0                                        
SHEET    2 AF6 2 ILE G 678  PHE G 680 -1  O  ILE G 679   N  SER G 611           
SHEET    1 AF7 4 TRP H  51  ILE H  55  0                                        
SHEET    2 AF7 4 SER H  68  TYR H  73 -1  O  GLU H  72   N  ARG H  52           
SHEET    3 AF7 4 THR H  97  CYS H 101 -1  O  LEU H  99   N  ILE H  69           
SHEET    4 AF7 4 CYS H  87  GLU H  90 -1  N  LYS H  88   O  HIS H 100           
SHEET    1 AF8 3 SER H  80  LYS H  82  0                                        
SHEET    2 AF8 3 GLY H 105  ILE H 112 -1  O  LYS H 110   N  LYS H  82           
SHEET    3 AF8 3 ARG H 120  VAL H 124 -1  O  VAL H 124   N  GLY H 105           
SHEET    1 AF9 4 TRP H 210  PRO H 215  0                                        
SHEET    2 AF9 4 SER H 145  TYR H 153 -1  N  GLN H 146   O  LEU H 214           
SHEET    3 AF9 4 ILE H 129  VAL H 140 -1  N  VAL H 138   O  ILE H 147           
SHEET    4 AF9 4 PHE H 236  ILE H 237  1  O  PHE H 236   N  TYR H 131           
SHEET    1 AG1 4 LEU H 197  TYR H 199  0                                        
SHEET    2 AG1 4 PHE H 189  THR H 192 -1  N  THR H 192   O  LEU H 197           
SHEET    3 AG1 4 ALA H 222  ARG H 226 -1  O  VAL H 224   N  PHE H 191           
SHEET    4 AG1 4 LEU H 240  MET H 243 -1  O  PHE H 242   N  LYS H 223           
SHEET    1 AG2 2 GLU H 258  PRO H 259  0                                        
SHEET    2 AG2 2 ARG H 302  ALA H 303 -1  O  ALA H 303   N  GLU H 258           
SHEET    1 AG3 4 MET H 269  TRP H 272  0                                        
SHEET    2 AG3 4 ALA H 280  ALA H 283 -1  O  ALA H 283   N  MET H 269           
SHEET    3 AG3 4 THR H 288  THR H 291 -1  O  PHE H 289   N  LEU H 282           
SHEET    4 AG3 4 THR H 299  ARG H 300 -1  O  THR H 299   N  GLN H 290           
SHEET    1 AG4 4 LEU H 316  ILE H 321  0                                        
SHEET    2 AG4 4 THR H 326  VAL H 330 -1  O  LEU H 329   N  ARG H 317           
SHEET    3 AG4 4 THR H 333  ARG H 337 -1  O  ARG H 337   N  THR H 326           
SHEET    4 AG4 4 LYS H 344  LEU H 345 -1  O  LEU H 345   N  VAL H 334           
SHEET    1 AG5 4 GLY H 358  SER H 360  0                                        
SHEET    2 AG5 4 LEU H 380  TRP H 383 -1  O  ILE H 381   N  SER H 360           
SHEET    3 AG5 4 THR H 387  GLY H 391 -1  O  TYR H 389   N  ALA H 382           
SHEET    4 AG5 4 PHE H 397  ASP H 402 -1  O  THR H 401   N  VAL H 388           
SHEET    1 AG6 4 LEU H 418  TYR H 425  0                                        
SHEET    2 AG6 4 GLU H 431  HIS H 438 -1  O  LEU H 435   N  SER H 422           
SHEET    3 AG6 4 THR H 446  SER H 455 -1  O  TYR H 454   N  ALA H 432           
SHEET    4 AG6 4 THR H 460  LEU H 463 -1  O  THR H 460   N  SER H 455           
SHEET    1 AG7 4 LEU H 418  TYR H 425  0                                        
SHEET    2 AG7 4 GLU H 431  HIS H 438 -1  O  LEU H 435   N  SER H 422           
SHEET    3 AG7 4 THR H 446  SER H 455 -1  O  TYR H 454   N  ALA H 432           
SHEET    4 AG7 4 GLN H 469  PRO H 471 -1  O  LEU H 470   N  ARG H 447           
SHEET    1 AG8 4 GLU H 477  PHE H 480  0                                        
SHEET    2 AG8 4 ILE H 488  TRP H 491 -1  O  ILE H 489   N  ARG H 479           
SHEET    3 AG8 4 VAL H 496  TYR H 500 -1  O  TYR H 497   N  MET H 490           
SHEET    4 AG8 4 VAL H 505  THR H 508 -1  O  VAL H 505   N  TYR H 500           
SHEET    1 AG9 4 ILE H 527  THR H 532  0                                        
SHEET    2 AG9 4 ASN H 537  MET H 542 -1  O  LYS H 541   N  GLN H 529           
SHEET    3 AG9 4 MET H 547  LYS H 551 -1  O  ILE H 550   N  VAL H 538           
SHEET    4 AG9 4 VAL H 558  ILE H 559 -1  O  VAL H 558   N  TYR H 549           
SHEET    1 AH1 3 LYS H 569  PHE H 574  0                                        
SHEET    2 AH1 3 VAL H 580  TYR H 585 -1  O  LEU H 583   N  VAL H 571           
SHEET    3 AH1 3 LEU H 595  PRO H 599 -1  O  GLN H 598   N  ILE H 582           
SHEET    1 AH2 4 ALA H 621  HIS H 624  0                                        
SHEET    2 AH2 4 LEU H 639  PRO H 648 -1  O  VAL H 646   N  ALA H 621           
SHEET    3 AH2 4 PHE H 679  PHE H 689 -1  O  THR H 686   N  ILE H 641           
SHEET    4 AH2 4 THR H 666  ALA H 676 -1  N  ALA H 676   O  PHE H 679           
SHEET    1 AH3 4 PHE H 630  MET H 633  0                                        
SHEET    2 AH3 4 VAL H 730  VAL H 735  1  O  ASP H 734   N  TYR H 631           
SHEET    3 AH3 4 GLY H 709  PRO H 717 -1  N  LEU H 713   O  PHE H 731           
SHEET    4 AH3 4 ILE H 655  GLY H 661 -1  N  VAL H 656   O  ARG H 716           
SHEET    1 AH4 3 TYR H 742  VAL H 745  0                                        
SHEET    2 AH4 3 VAL H 800  TYR H 803 -1  O  TYR H 803   N  TYR H 742           
SHEET    3 AH4 3 PHE H 808  ILE H 811 -1  O  LYS H 810   N  LEU H 802           
SHEET    1 AH5 2 PHE H 758  ILE H 762  0                                        
SHEET    2 AH5 2 LEU H 775  TYR H 779 -1  O  VAL H 777   N  TYR H 760           
SHEET    1 AH6 4 LEU H 788  THR H 789  0                                        
SHEET    2 AH6 4 THR H 922  GLU H 928  1  O  GLU H 928   N  LEU H 788           
SHEET    3 AH6 4 MET H 904  ILE H 911 -1  N  LEU H 909   O  THR H 923           
SHEET    4 AH6 4 PHE H 816  GLU H 820 -1  N  TRP H 819   O  ARG H 908           
SHEET    1 AH7 2 THR H 828  PHE H 829  0                                        
SHEET    2 AH7 2 ILE H 895  LYS H 896 -1  O  LYS H 896   N  THR H 828           
SHEET    1 AH8 2 SER L 504  CYS L 506  0                                        
SHEET    2 AH8 2 GLU L 512  PHE L 514 -1  O  TYR L 513   N  ILE L 505           
SHEET    1 AH9 3 CYS L 521  ALA L 523  0                                        
SHEET    2 AH9 3 THR L 532  CYS L 536 -1  O  TYR L 534   N  ALA L 523           
SHEET    3 AH9 3 ALA L 555  ILE L 556 -1  O  ALA L 555   N  TYR L 533           
SHEET    1 AI1 2 TYR L 634  TRP L 635  0                                        
SHEET    2 AI1 2 CYS L 646  ILE L 648 -1  O  TRP L 647   N  TYR L 634           
SHEET    1 AI2 3 VAL J  48  ASN J  50  0                                        
SHEET    2 AI2 3 MET J  55  ILE J  60 -1  O  MET J  55   N  ASN J  50           
SHEET    3 AI2 3 ARG J  63  PRO J  69 -1  O  CYS J  66   N  PHE J  58           
SHEET    1 AI3 2 ALA J  78  SER J  81  0                                        
SHEET    2 AI3 2 ARG J  87  GLN J  90 -1  O  PHE J  88   N  SER J  80           
SHEET    1 AI4 2 THR I  43  ASN I  45  0                                        
SHEET    2 AI4 2 GLU I  78  GLY I  80 -1  O  ILE I  79   N  LEU I  44           
SSBOND   1 CYS E   35    CYS E   60                          1555   1555  2.03  
SSBOND   2 CYS E  189    CYS E  302                          1555   1555  2.03  
SSBOND   3 CYS E  330    CYS E  343                          1555   1555  2.03  
SSBOND   4 CYS E  831    CYS E 1039                          1555   1555  1.93  
SSBOND   5 CYS E  913    CYS E  922                          1555   1555  2.66  
SSBOND   6 CYS E  924    CYS E  939                          1555   1555  2.03  
SSBOND   7 CYS F   45    CYS F  106                          1555   1555  2.03  
SSBOND   8 CYS F  160    CYS F  166                          1555   1555  2.03  
SSBOND   9 CYS F  289    CYS F  344                          1555   1555  2.03  
SSBOND  10 CYS F  395    CYS F  403                          1555   1555  2.03  
SSBOND  11 CYS F  634    CYS F  856                          1555   1555  2.03  
SSBOND  12 CYS F  802    CYS F  830                          1555   1555  2.04  
SSBOND  13 CYS F  878    CYS F 1042                          1555   1555  2.03  
SSBOND  14 CYS F  905    CYS F  914                          1555   1555  1.81  
SSBOND  15 CYS F 1006    CYS F 1012                          1555   1555  2.03  
SSBOND  16 CYS G   20    CYS G  366                          1555   1555  2.02  
SSBOND  17 CYS G   56    CYS G  143                          1555   1555  2.02  
SSBOND  18 CYS G  142    CYS G  149                          1555   1555  2.04  
SSBOND  19 CYS G  384    CYS G  493                          1555   1555  2.03  
SSBOND  20 CYS G  507    CYS G  701                          1555   1555  2.03  
SSBOND  21 CYS G  522    CYS G  569                          1555   1555  2.04  
SSBOND  22 CYS G  621    CYS G  651                          1555   1555  2.03  
SSBOND  23 CYS H   87    CYS H  101                          1555   1555  2.66  
SSBOND  24 CYS H  130    CYS H  235                          1555   1555  2.03  
SSBOND  25 CYS H  275    CYS H  365                          1555   1555  2.03  
SSBOND  26 CYS H  439    CYS H  442                          1555   1555  2.04  
SSBOND  27 CYS H  617    CYS H  724                          1555   1555  2.03  
SSBOND  28 CYS H  737    CYS H  919                          1555   1555  2.02  
SSBOND  29 CYS H  753    CYS H  786                          1555   1555  2.52  
SSBOND  30 CYS H  838    CYS H  869                          1555   1555  2.04  
SSBOND  31 CYS L  491    CYS L  538                          1555   1555  2.03  
SSBOND  32 CYS L  497    CYS L  517                          1555   1555  2.02  
SSBOND  33 CYS L  506    CYS L  560                          1555   1555  2.03  
SSBOND  34 CYS L  521    CYS L  536                          1555   1555  2.03  
LINK         ND2 ASN E  90                 C1  NAG O   1     1555   1555  1.50  
LINK         ND2 ASN E 118                 C1  NAG E1202     1555   1555  1.58  
LINK         ND2 ASN E 672                 C1  NAG E1201     1555   1555  1.46  
LINK         ND2 ASN E 915                 C1  NAG E1203     1555   1555  1.45  
LINK         ND2 ASN E 923                 C1  NAG E1204     1555   1555  1.58  
LINK         ND2 ASN E1017                 C1  NAG P   1     1555   1555  1.51  
LINK         ND2 ASN F 103                 C1  NAG Q   1     1555   1555  1.60  
LINK         ND2 ASN F 178                 C1  NAG R   1     1555   1555  1.27  
LINK         ND2 ASN F 356                 C1  NAG T   1     1555   1555  1.41  
LINK         ND2 ASN F 672                 C1  NAG S   1     1555   1555  1.26  
LINK         ND2 ASN G 227                 C1  NAG G 901     1555   1555  1.29  
LINK         ND2 ASN G 469                 C1  NAG G 903     1555   1555  1.57  
LINK         ND2 ASN G 535                 C1  NAG G 902     1555   1555  1.42  
LINK         ND2 ASN G 627                 C1  NAG U   1     1555   1555  1.53  
LINK         ND2 ASN H 143                 C1  NAG W   1     1555   1555  1.49  
LINK         ND2 ASN H 502                 C1  NAG Y   1     1555   1555  1.27  
LINK         ND2 ASN H 830                 C1  NAG b   1     1555   1555  1.51  
LINK         ND2 ASN L 535                 C1  NAG d   1     1555   1555  1.44  
LINK         O4  NAG O   1                 C1  NAG O   2     1555   1555  1.45  
LINK         O4  NAG O   2                 C1  BMA O   3     1555   1555  1.45  
LINK         O3  BMA O   3                 C1  BMA O   4     1555   1555  1.44  
LINK         O6  BMA O   3                 C1  BMA O   6     1555   1555  1.44  
LINK         O2  BMA O   4                 C1  BMA O   5     1555   1555  1.46  
LINK         O3  BMA O   6                 C1  BMA O   7     1555   1555  1.46  
LINK         O4  NAG P   1                 C1  NAG P   2     1555   1555  1.44  
LINK         O4  NAG Q   1                 C1  NAG Q   2     1555   1555  1.44  
LINK         O4  NAG Q   2                 C1  BMA Q   3     1555   1555  1.45  
LINK         O4  NAG R   1                 C1  NAG R   2     1555   1555  1.44  
LINK         O4  NAG R   2                 C1  BMA R   3     1555   1555  1.45  
LINK         O4  NAG S   1                 C1  NAG S   2     1555   1555  1.45  
LINK         O4  NAG T   1                 C1  NAG T   2     1555   1555  1.44  
LINK         O4  NAG U   1                 C1  NAG U   2     1555   1555  1.44  
LINK         O4  NAG U   2                 C1  BMA U   3     1555   1555  1.44  
LINK         O4  NAG V   1                 C1  NAG V   2     1555   1555  1.44  
LINK         O4  NAG W   1                 C1  NAG W   2     1555   1555  1.44  
LINK         O4  NAG W   2                 C1  BMA W   3     1555   1555  1.43  
LINK         O4  NAG X   1                 C1  NAG X   2     1555   1555  1.44  
LINK         O4  NAG Y   1                 C1  NAG Y   2     1555   1555  1.44  
LINK         O4  NAG Y   2                 C1  BMA Y   3     1555   1555  1.46  
LINK         O3  BMA Y   3                 C1  BMA Y   4     1555   1555  1.45  
LINK         O6  BMA Y   3                 C1  BMA Y   5     1555   1555  1.45  
LINK         O4  NAG Z   1                 C1  NAG Z   2     1555   1555  1.44  
LINK         O4  NAG Z   2                 C1  BMA Z   3     1555   1555  1.44  
LINK         O6  BMA Z   3                 C1  BMA Z   4     1555   1555  1.44  
LINK         O3  BMA Z   3                 C1  BMA Z   7     1555   1555  1.44  
LINK         O3  BMA Z   4                 C1  BMA Z   5     1555   1555  1.46  
LINK         O6  BMA Z   4                 C1  BMA Z   6     1555   1555  1.44  
LINK         O4  NAG a   1                 C1  NAG a   2     1555   1555  1.44  
LINK         O4  NAG b   1                 C1  NAG b   2     1555   1555  1.44  
LINK         O4  NAG b   2                 C1  BMA b   3     1555   1555  1.45  
LINK         O4  NAG c   1                 C1  NAG c   2     1555   1555  1.49  
LINK         O4  NAG c   2                 C1  BMA c   3     1555   1555  1.45  
LINK         O3  BMA c   3                 C1  BMA c   4     1555   1555  1.46  
LINK         O6  BMA c   3                 C1  BMA c   5     1555   1555  1.45  
LINK         O4  NAG d   1                 C1  NAG d   2     1555   1555  1.45  
LINK         O   LEU A 535                NA    NA A 701     1555   1555  3.10  
LINK         OD1 ASP A 536                NA    NA D1001     1555   1555  2.76  
LINK        NA    NA A 701                 OD1 ASP D 237     1555   1555  2.77  
LINK         OD1 ASP D 237                NA    NA D1001     1555   1555  2.48  
LINK         OD2 ASP D 237                NA    NA D1001     1555   1555  3.14  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   LEU A 337     244.129 255.431 165.856  1.00149.29           N  
ATOM      2  CA  LEU A 337     242.935 254.600 165.914  1.00149.29           C  
ATOM      3  C   LEU A 337     243.022 253.454 164.914  1.00149.29           C  
ATOM      4  O   LEU A 337     242.276 252.482 165.001  1.00149.29           O  
ATOM      5  CB  LEU A 337     241.685 255.435 165.647  1.00149.29           C  
ATOM      6  CG  LEU A 337     241.428 256.603 166.598  1.00149.29           C  
ATOM      7  CD1 LEU A 337     240.267 257.442 166.094  1.00149.29           C  
ATOM      8  CD2 LEU A 337     241.164 256.112 168.010  1.00149.29           C  
ATOM      9  N   LEU A 338     243.941 253.577 163.955  1.00150.08           N  
ATOM     10  CA  LEU A 338     244.162 252.536 162.962  1.00150.08           C  
ATOM     11  C   LEU A 338     245.480 251.803 163.136  1.00150.08           C  
ATOM     12  O   LEU A 338     245.592 250.658 162.691  1.00150.08           O  
ATOM     13  CB  LEU A 338     244.119 253.123 161.542  1.00150.08           C  
ATOM     14  CG  LEU A 338     242.749 253.293 160.886  1.00150.08           C  
ATOM     15  CD1 LEU A 338     242.043 254.536 161.408  1.00150.08           C  
ATOM     16  CD2 LEU A 338     242.891 253.340 159.376  1.00150.08           C  
ATOM     17  N   GLY A 339     246.474 252.432 163.753  1.00152.51           N  
ATOM     18  CA  GLY A 339     247.745 251.784 163.984  1.00152.51           C  
ATOM     19  C   GLY A 339     247.849 251.296 165.408  1.00152.51           C  
ATOM     20  O   GLY A 339     248.323 250.186 165.663  1.00152.51           O  
ATOM     21  N   LEU A 340     247.384 252.121 166.348  1.00152.26           N  
ATOM     22  CA  LEU A 340     247.408 251.733 167.753  1.00152.26           C  
ATOM     23  C   LEU A 340     246.471 250.559 168.012  1.00152.26           C  
ATOM     24  O   LEU A 340     246.882 249.538 168.579  1.00152.26           O  
ATOM     25  CB  LEU A 340     247.072 252.947 168.628  1.00152.26           C  
ATOM     26  CG  LEU A 340     245.739 253.695 168.499  1.00152.26           C  
ATOM     27  CD1 LEU A 340     244.685 253.137 169.436  1.00152.26           C  
ATOM     28  CD2 LEU A 340     245.922 255.187 168.721  1.00152.26           C  
ATOM     29  N   GLN A 341     245.219 250.667 167.563  1.00150.54           N  
ATOM     30  CA  GLN A 341     244.289 249.559 167.728  1.00150.54           C  
ATOM     31  C   GLN A 341     244.775 248.329 166.982  1.00150.54           C  
ATOM     32  O   GLN A 341     244.619 247.205 167.462  1.00150.54           O  
ATOM     33  CB  GLN A 341     242.889 249.950 167.256  1.00150.54           C  
ATOM     34  CG  GLN A 341     242.201 250.997 168.111  1.00150.54           C  
ATOM     35  CD  GLN A 341     240.716 251.083 167.826  1.00150.54           C  
ATOM     36  OE1 GLN A 341     240.130 250.163 167.258  1.00150.54           O  
ATOM     37  NE2 GLN A 341     240.099 252.192 168.215  1.00150.54           N  
ATOM     38  N   GLN A 342     245.379 248.520 165.811  1.00152.88           N  
ATOM     39  CA  GLN A 342     245.806 247.365 165.031  1.00152.88           C  
ATOM     40  C   GLN A 342     246.969 246.642 165.696  1.00152.88           C  
ATOM     41  O   GLN A 342     247.030 245.408 165.668  1.00152.88           O  
ATOM     42  CB  GLN A 342     246.178 247.784 163.614  1.00152.88           C  
ATOM     43  CG  GLN A 342     246.442 246.616 162.681  1.00152.88           C  
ATOM     44  CD  GLN A 342     247.866 246.112 162.761  1.00152.88           C  
ATOM     45  OE1 GLN A 342     248.132 244.931 162.535  1.00152.88           O  
ATOM     46  NE2 GLN A 342     248.792 247.008 163.086  1.00152.88           N  
ATOM     47  N   MET A 343     247.918 247.377 166.282  1.00154.40           N  
ATOM     48  CA  MET A 343     248.988 246.671 166.977  1.00154.40           C  
ATOM     49  C   MET A 343     248.477 246.040 168.261  1.00154.40           C  
ATOM     50  O   MET A 343     248.946 244.963 168.647  1.00154.40           O  
ATOM     51  CB  MET A 343     250.185 247.581 167.265  1.00154.40           C  
ATOM     52  CG  MET A 343     249.921 248.874 168.006  1.00154.40           C  
ATOM     53  SD  MET A 343     251.462 249.820 168.041  1.00154.40           S  
ATOM     54  CE  MET A 343     250.892 251.515 168.038  1.00154.40           C  
ATOM     55  N   ILE A 344     247.502 246.673 168.919  1.00151.98           N  
ATOM     56  CA  ILE A 344     246.853 246.029 170.056  1.00151.98           C  
ATOM     57  C   ILE A 344     246.228 244.710 169.625  1.00151.98           C  
ATOM     58  O   ILE A 344     246.347 243.694 170.315  1.00151.98           O  
ATOM     59  CB  ILE A 344     245.814 246.973 170.685  1.00151.98           C  
ATOM     60  CG1 ILE A 344     246.517 248.108 171.423  1.00151.98           C  
ATOM     61  CG2 ILE A 344     244.927 246.218 171.639  1.00151.98           C  
ATOM     62  CD1 ILE A 344     245.582 248.992 172.209  1.00151.98           C  
ATOM     63  N   LEU A 345     245.575 244.701 168.464  1.00151.40           N  
ATOM     64  CA  LEU A 345     245.076 243.458 167.883  1.00151.40           C  
ATOM     65  C   LEU A 345     246.201 242.446 167.717  1.00151.40           C  
ATOM     66  O   LEU A 345     246.222 241.395 168.370  1.00151.40           O  
ATOM     67  CB  LEU A 345     244.429 243.748 166.529  1.00151.40           C  
ATOM     68  CG  LEU A 345     242.916 243.885 166.404  1.00151.40           C  
ATOM     69  CD1 LEU A 345     242.421 245.089 167.158  1.00151.40           C  
ATOM     70  CD2 LEU A 345     242.545 244.000 164.938  1.00151.40           C  
ATOM     71  N   SER A 346     247.181 242.781 166.876  1.00154.20           N  
ATOM     72  CA  SER A 346     248.198 241.814 166.475  1.00154.20           C  
ATOM     73  C   SER A 346     249.055 241.376 167.652  1.00154.20           C  
ATOM     74  O   SER A 346     249.822 240.414 167.539  1.00154.20           O  
ATOM     75  CB  SER A 346     249.065 242.398 165.363  1.00154.20           C  
ATOM     76  OG  SER A 346     248.255 242.979 164.357  1.00154.20           O  
ATOM     77  N   LEU A 347     248.958 242.078 168.777  1.00154.90           N  
ATOM     78  CA  LEU A 347     249.491 241.554 170.025  1.00154.90           C  
ATOM     79  C   LEU A 347     248.457 240.746 170.799  1.00154.90           C  
ATOM     80  O   LEU A 347     248.834 239.900 171.615  1.00154.90           O  
ATOM     81  CB  LEU A 347     250.010 242.703 170.888  1.00154.90           C  
ATOM     82  CG  LEU A 347     251.378 243.235 170.461  1.00154.90           C  
ATOM     83  CD1 LEU A 347     251.499 244.707 170.799  1.00154.90           C  
ATOM     84  CD2 LEU A 347     252.499 242.433 171.106  1.00154.90           C  
ATOM     85  N   THR A 348     247.167 240.977 170.544  1.00151.56           N  
ATOM     86  CA  THR A 348     246.117 240.306 171.300  1.00151.56           C  
ATOM     87  C   THR A 348     245.873 238.897 170.784  1.00151.56           C  
ATOM     88  O   THR A 348     245.954 237.927 171.545  1.00151.56           O  
ATOM     89  CB  THR A 348     244.833 241.128 171.237  1.00151.56           C  
ATOM     90  OG1 THR A 348     245.108 242.468 171.660  1.00151.56           O  
ATOM     91  CG2 THR A 348     243.767 240.519 172.129  1.00151.56           C  
ATOM     92  N   GLN A 349     245.576 238.755 169.494  1.00152.00           N  
ATOM     93  CA  GLN A 349     245.400 237.409 168.961  1.00152.00           C  
ATOM     94  C   GLN A 349     246.717 236.658 168.816  1.00152.00           C  
ATOM     95  O   GLN A 349     246.729 235.566 168.237  1.00152.00           O  
ATOM     96  CB  GLN A 349     244.679 237.421 167.608  1.00152.00           C  
ATOM     97  CG  GLN A 349     245.516 237.930 166.448  1.00152.00           C  
ATOM     98  CD  GLN A 349     245.272 239.386 166.148  1.00152.00           C  
ATOM     99  OE1 GLN A 349     244.602 240.083 166.906  1.00152.00           O  
ATOM    100  NE2 GLN A 349     245.821 239.859 165.038  1.00152.00           N  
ATOM    101  N   SER A 350     247.810 237.211 169.333  1.00152.12           N  
ATOM    102  CA  SER A 350     249.115 236.588 169.191  1.00152.12           C  
ATOM    103  C   SER A 350     249.145 235.232 169.885  1.00152.12           C  
ATOM    104  O   SER A 350     248.494 235.017 170.910  1.00152.12           O  
ATOM    105  CB  SER A 350     250.192 237.498 169.769  1.00152.12           C  
ATOM    106  OG  SER A 350     250.317 238.671 168.990  1.00152.12           O  
ATOM    107  N   LEU A 351     249.924 234.315 169.315  1.00151.87           N  
ATOM    108  CA  LEU A 351     250.023 232.947 169.805  1.00151.87           C  
ATOM    109  C   LEU A 351     250.837 232.832 171.087  1.00151.87           C  
ATOM    110  O   LEU A 351     251.207 231.719 171.470  1.00151.87           O  
ATOM    111  CB  LEU A 351     250.629 232.043 168.729  1.00151.87           C  
ATOM    112  CG  LEU A 351     250.271 232.323 167.265  1.00151.87           C  
ATOM    113  CD1 LEU A 351     251.019 231.375 166.338  1.00151.87           C  
ATOM    114  CD2 LEU A 351     248.771 232.225 167.035  1.00151.87           C  
ATOM    115  N   GLY A 352     251.148 233.947 171.739  1.00150.88           N  
ATOM    116  CA  GLY A 352     251.771 233.908 173.045  1.00150.88           C  
ATOM    117  C   GLY A 352     250.875 234.529 174.096  1.00150.88           C  
ATOM    118  O   GLY A 352     250.891 234.131 175.263  1.00150.88           O  
ATOM    119  N   PHE A 353     250.086 235.517 173.676  1.00148.30           N  
ATOM    120  CA  PHE A 353     249.111 236.134 174.566  1.00148.30           C  
ATOM    121  C   PHE A 353     248.115 235.097 175.062  1.00148.30           C  
ATOM    122  O   PHE A 353     247.803 235.029 176.258  1.00148.30           O  
ATOM    123  CB  PHE A 353     248.404 237.259 173.814  1.00148.30           C  
ATOM    124  CG  PHE A 353     247.476 238.078 174.649  1.00148.30           C  
ATOM    125  CD1 PHE A 353     247.953 239.130 175.405  1.00148.30           C  
ATOM    126  CD2 PHE A 353     246.119 237.821 174.649  1.00148.30           C  
ATOM    127  CE1 PHE A 353     247.094 239.901 176.159  1.00148.30           C  
ATOM    128  CE2 PHE A 353     245.256 238.588 175.401  1.00148.30           C  
ATOM    129  CZ  PHE A 353     245.744 239.629 176.157  1.00148.30           C  
ATOM    130  N   GLU A 354     247.629 234.258 174.147  1.00149.87           N  
ATOM    131  CA  GLU A 354     246.709 233.194 174.524  1.00149.87           C  
ATOM    132  C   GLU A 354     247.350 232.216 175.497  1.00149.87           C  
ATOM    133  O   GLU A 354     246.727 231.833 176.491  1.00149.87           O  
ATOM    134  CB  GLU A 354     246.196 232.480 173.271  1.00149.87           C  
ATOM    135  CG  GLU A 354     247.264 231.993 172.287  1.00149.87           C  
ATOM    136  CD  GLU A 354     247.857 230.642 172.635  1.00149.87           C  
ATOM    137  OE1 GLU A 354     247.282 229.923 173.470  1.00149.87           O  
ATOM    138  OE2 GLU A 354     248.901 230.287 172.054  1.00149.87           O  
ATOM    139  N   THR A 355     248.593 231.805 175.243  1.00146.48           N  
ATOM    140  CA  THR A 355     249.222 230.839 176.137  1.00146.48           C  
ATOM    141  C   THR A 355     249.478 231.451 177.508  1.00146.48           C  
ATOM    142  O   THR A 355     249.291 230.790 178.533  1.00146.48           O  
ATOM    143  CB  THR A 355     250.519 230.309 175.525  1.00146.48           C  
ATOM    144  OG1 THR A 355     250.232 229.684 174.270  1.00146.48           O  
ATOM    145  CG2 THR A 355     251.149 229.274 176.439  1.00146.48           C  
ATOM    146  N   PHE A 356     249.892 232.716 177.542  1.00142.70           N  
ATOM    147  CA  PHE A 356     250.089 233.414 178.806  1.00142.70           C  
ATOM    148  C   PHE A 356     248.799 233.443 179.616  1.00142.70           C  
ATOM    149  O   PHE A 356     248.792 233.116 180.812  1.00142.70           O  
ATOM    150  CB  PHE A 356     250.601 234.825 178.498  1.00142.70           C  
ATOM    151  CG  PHE A 356     250.702 235.738 179.686  1.00142.70           C  
ATOM    152  CD1 PHE A 356     251.662 235.535 180.658  1.00142.70           C  
ATOM    153  CD2 PHE A 356     249.870 236.837 179.798  1.00142.70           C  
ATOM    154  CE1 PHE A 356     251.768 236.392 181.738  1.00142.70           C  
ATOM    155  CE2 PHE A 356     249.972 237.697 180.874  1.00142.70           C  
ATOM    156  CZ  PHE A 356     250.923 237.473 181.843  1.00142.70           C  
ATOM    157  N   ILE A 357     247.684 233.778 178.966  1.00139.92           N  
ATOM    158  CA  ILE A 357     246.417 233.851 179.682  1.00139.92           C  
ATOM    159  C   ILE A 357     245.950 232.468 180.120  1.00139.92           C  
ATOM    160  O   ILE A 357     245.393 232.312 181.210  1.00139.92           O  
ATOM    161  CB  ILE A 357     245.361 234.567 178.829  1.00139.92           C  
ATOM    162  CG1 ILE A 357     245.785 236.020 178.613  1.00139.92           C  
ATOM    163  CG2 ILE A 357     243.990 234.456 179.470  1.00139.92           C  
ATOM    164  CD1 ILE A 357     246.322 236.685 179.859  1.00139.92           C  
ATOM    165  N   PHE A 358     246.149 231.446 179.290  1.00142.30           N  
ATOM    166  CA  PHE A 358     245.754 230.107 179.721  1.00142.30           C  
ATOM    167  C   PHE A 358     246.617 229.602 180.865  1.00142.30           C  
ATOM    168  O   PHE A 358     246.123 228.875 181.731  1.00142.30           O  
ATOM    169  CB  PHE A 358     245.766 229.109 178.561  1.00142.30           C  
ATOM    170  CG  PHE A 358     245.081 229.600 177.319  1.00142.30           C  
ATOM    171  CD1 PHE A 358     244.028 230.498 177.400  1.00142.30           C  
ATOM    172  CD2 PHE A 358     245.442 229.117 176.075  1.00142.30           C  
ATOM    173  CE1 PHE A 358     243.386 230.940 176.264  1.00142.30           C  
ATOM    174  CE2 PHE A 358     244.790 229.551 174.935  1.00142.30           C  
ATOM    175  CZ  PHE A 358     243.767 230.464 175.029  1.00142.30           C  
ATOM    176  N   ILE A 359     247.893 229.978 180.900  1.00131.78           N  
ATOM    177  CA  ILE A 359     248.711 229.658 182.063  1.00131.78           C  
ATOM    178  C   ILE A 359     248.140 230.335 183.301  1.00131.78           C  
ATOM    179  O   ILE A 359     248.021 229.719 184.368  1.00131.78           O  
ATOM    180  CB  ILE A 359     250.174 230.063 181.815  1.00131.78           C  
ATOM    181  CG1 ILE A 359     250.814 229.141 180.776  1.00131.78           C  
ATOM    182  CG2 ILE A 359     250.957 230.036 183.111  1.00131.78           C  
ATOM    183  CD1 ILE A 359     251.000 227.721 181.245  1.00131.78           C  
ATOM    184  N   VAL A 360     247.757 231.605 183.171  1.00127.08           N  
ATOM    185  CA  VAL A 360     247.149 232.302 184.300  1.00127.08           C  
ATOM    186  C   VAL A 360     245.889 231.585 184.759  1.00127.08           C  
ATOM    187  O   VAL A 360     245.675 231.386 185.958  1.00127.08           O  
ATOM    188  CB  VAL A 360     246.861 233.769 183.940  1.00127.08           C  
ATOM    189  CG1 VAL A 360     245.897 234.368 184.930  1.00127.08           C  
ATOM    190  CG2 VAL A 360     248.151 234.567 183.938  1.00127.08           C  
ATOM    191  N   VAL A 361     245.035 231.188 183.820  1.00123.40           N  
ATOM    192  CA  VAL A 361     243.742 230.623 184.190  1.00123.40           C  
ATOM    193  C   VAL A 361     243.907 229.235 184.797  1.00123.40           C  
ATOM    194  O   VAL A 361     243.194 228.867 185.737  1.00123.40           O  
ATOM    195  CB  VAL A 361     242.798 230.618 182.979  1.00123.40           C  
ATOM    196  CG1 VAL A 361     241.673 229.627 183.180  1.00123.40           C  
ATOM    197  CG2 VAL A 361     242.239 232.005 182.773  1.00123.40           C  
ATOM    198  N   CYS A 362     244.847 228.443 184.288  1.00119.65           N  
ATOM    199  CA  CYS A 362     245.083 227.141 184.899  1.00119.65           C  
ATOM    200  C   CYS A 362     245.706 227.288 186.285  1.00119.65           C  
ATOM    201  O   CYS A 362     245.407 226.500 187.189  1.00119.65           O  
ATOM    202  CB  CYS A 362     245.939 226.267 183.983  1.00119.65           C  
ATOM    203  SG  CYS A 362     247.678 226.717 183.845  1.00119.65           S  
ATOM    204  N   LEU A 363     246.545 228.305 186.496  1.00117.21           N  
ATOM    205  CA  LEU A 363     247.029 228.550 187.851  1.00117.21           C  
ATOM    206  C   LEU A 363     245.896 228.976 188.776  1.00117.21           C  
ATOM    207  O   LEU A 363     245.810 228.521 189.922  1.00117.21           O  
ATOM    208  CB  LEU A 363     248.128 229.608 187.848  1.00117.21           C  
ATOM    209  CG  LEU A 363     249.476 229.218 187.249  1.00117.21           C  
ATOM    210  CD1 LEU A 363     250.480 230.328 187.494  1.00117.21           C  
ATOM    211  CD2 LEU A 363     249.965 227.901 187.809  1.00117.21           C  
ATOM    212  N   ASN A 364     245.022 229.860 188.301  1.00113.83           N  
ATOM    213  CA  ASN A 364     243.907 230.300 189.128  1.00113.83           C  
ATOM    214  C   ASN A 364     242.990 229.136 189.470  1.00113.83           C  
ATOM    215  O   ASN A 364     242.476 229.052 190.587  1.00113.83           O  
ATOM    216  CB  ASN A 364     243.125 231.403 188.426  1.00113.83           C  
ATOM    217  CG  ASN A 364     242.013 231.951 189.286  1.00113.83           C  
ATOM    218  OD1 ASN A 364     242.219 232.861 190.084  1.00113.83           O  
ATOM    219  ND2 ASN A 364     240.826 231.380 189.148  1.00113.83           N  
ATOM    220  N   THR A 365     242.778 228.217 188.529  1.00110.24           N  
ATOM    221  CA  THR A 365     241.917 227.087 188.839  1.00110.24           C  
ATOM    222  C   THR A 365     242.619 226.065 189.723  1.00110.24           C  
ATOM    223  O   THR A 365     241.952 225.369 190.496  1.00110.24           O  
ATOM    224  CB  THR A 365     241.391 226.424 187.565  1.00110.24           C  
ATOM    225  OG1 THR A 365     240.383 225.467 187.913  1.00110.24           O  
ATOM    226  CG2 THR A 365     242.484 225.702 186.842  1.00110.24           C  
ATOM    227  N   VAL A 366     243.947 225.960 189.668  1.00106.42           N  
ATOM    228  CA  VAL A 366     244.585 225.038 190.601  1.00106.42           C  
ATOM    229  C   VAL A 366     244.542 225.610 192.016  1.00106.42           C  
ATOM    230  O   VAL A 366     244.345 224.875 192.988  1.00106.42           O  
ATOM    231  CB  VAL A 366     246.013 224.670 190.154  1.00106.42           C  
ATOM    232  CG1 VAL A 366     246.984 225.800 190.361  1.00106.42           C  
ATOM    233  CG2 VAL A 366     246.483 223.427 190.878  1.00106.42           C  
ATOM    234  N   ILE A 367     244.663 226.932 192.153  1.00105.12           N  
ATOM    235  CA  ILE A 367     244.414 227.567 193.448  1.00105.12           C  
ATOM    236  C   ILE A 367     242.972 227.348 193.891  1.00105.12           C  
ATOM    237  O   ILE A 367     242.696 227.082 195.068  1.00105.12           O  
ATOM    238  CB  ILE A 367     244.746 229.067 193.379  1.00105.12           C  
ATOM    239  CG1 ILE A 367     246.221 229.277 193.095  1.00105.12           C  
ATOM    240  CG2 ILE A 367     244.359 229.769 194.642  1.00105.12           C  
ATOM    241  CD1 ILE A 367     246.541 230.698 192.770  1.00105.12           C  
ATOM    242  N   LEU A 368     242.030 227.489 192.965  1.00103.18           N  
ATOM    243  CA  LEU A 368     240.623 227.433 193.322  1.00103.18           C  
ATOM    244  C   LEU A 368     240.200 226.029 193.704  1.00103.18           C  
ATOM    245  O   LEU A 368     239.242 225.857 194.463  1.00103.18           O  
ATOM    246  CB  LEU A 368     239.793 227.947 192.158  1.00103.18           C  
ATOM    247  CG  LEU A 368     238.528 228.695 192.521  1.00103.18           C  
ATOM    248  CD1 LEU A 368     238.836 229.695 193.600  1.00103.18           C  
ATOM    249  CD2 LEU A 368     238.065 229.407 191.288  1.00103.18           C  
ATOM    250  N   VAL A 369     240.884 225.014 193.181  1.00102.39           N  
ATOM    251  CA  VAL A 369     240.632 223.658 193.645  1.00102.39           C  
ATOM    252  C   VAL A 369     241.479 223.325 194.868  1.00102.39           C  
ATOM    253  O   VAL A 369     241.152 222.387 195.605  1.00102.39           O  
ATOM    254  CB  VAL A 369     240.866 222.653 192.508  1.00102.39           C  
ATOM    255  CG1 VAL A 369     242.339 222.504 192.226  1.00102.39           C  
ATOM    256  CG2 VAL A 369     240.237 221.319 192.836  1.00102.39           C  
ATOM    257  N   ALA A 370     242.560 224.067 195.115  1.00103.13           N  
ATOM    258  CA  ALA A 370     243.231 223.958 196.404  1.00103.13           C  
ATOM    259  C   ALA A 370     242.328 224.437 197.529  1.00103.13           C  
ATOM    260  O   ALA A 370     242.246 223.800 198.583  1.00103.13           O  
ATOM    261  CB  ALA A 370     244.530 224.756 196.391  1.00103.13           C  
ATOM    262  N   GLN A 371     241.619 225.522 197.309  1.00101.65           N  
ATOM    263  CA  GLN A 371     240.815 226.139 198.362  1.00101.65           C  
ATOM    264  C   GLN A 371     239.632 225.340 198.754  1.00101.65           C  
ATOM    265  O   GLN A 371     238.785 225.926 199.421  1.00101.65           O  
ATOM    266  CB  GLN A 371     240.326 227.523 197.948  1.00101.65           C  
ATOM    267  CG  GLN A 371     241.392 228.561 197.787  1.00101.65           C  
ATOM    268  CD  GLN A 371     240.817 229.890 197.358  1.00101.65           C  
ATOM    269  OE1 GLN A 371     239.619 230.007 197.117  1.00101.65           O  
ATOM    270  NE2 GLN A 371     241.664 230.904 197.274  1.00101.65           N  
ATOM    271  N   THR A 372     239.427 224.079 198.401  1.00101.73           N  
ATOM    272  CA  THR A 372     238.216 223.363 198.783  1.00101.73           C  
ATOM    273  C   THR A 372     238.512 222.162 199.674  1.00101.73           C  
ATOM    274  O   THR A 372     237.896 221.107 199.542  1.00101.73           O  
ATOM    275  CB  THR A 372     237.437 222.934 197.547  1.00101.73           C  
ATOM    276  OG1 THR A 372     236.301 222.168 197.945  1.00101.73           O  
ATOM    277  CG2 THR A 372     238.299 222.101 196.632  1.00101.73           C  
ATOM    278  N   PHE A 373     239.445 222.317 200.607  1.00106.38           N  
ATOM    279  CA  PHE A 373     239.768 221.284 201.582  1.00106.38           C  
ATOM    280  C   PHE A 373     239.585 221.714 203.028  1.00106.38           C  
ATOM    281  O   PHE A 373     239.216 220.879 203.854  1.00106.38           O  
ATOM    282  CB  PHE A 373     241.214 220.801 201.396  1.00106.38           C  
ATOM    283  CG  PHE A 373     241.433 219.994 200.151  1.00106.38           C  
ATOM    284  CD1 PHE A 373     240.370 219.451 199.462  1.00106.38           C  
ATOM    285  CD2 PHE A 373     242.703 219.784 199.667  1.00106.38           C  
ATOM    286  CE1 PHE A 373     240.572 218.710 198.326  1.00106.38           C  
ATOM    287  CE2 PHE A 373     242.906 219.047 198.530  1.00106.38           C  
ATOM    288  CZ  PHE A 373     241.839 218.513 197.860  1.00106.38           C  
ATOM    289  N   THR A 374     239.807 222.994 203.339  1.00111.82           N  
ATOM    290  CA  THR A 374     239.779 223.601 204.671  1.00111.82           C  
ATOM    291  C   THR A 374     241.020 223.278 205.490  1.00111.82           C  
ATOM    292  O   THR A 374     241.269 223.932 206.506  1.00111.82           O  
ATOM    293  CB  THR A 374     238.538 223.192 205.472  1.00111.82           C  
ATOM    294  OG1 THR A 374     238.622 221.803 205.805  1.00111.82           O  
ATOM    295  CG2 THR A 374     237.275 223.454 204.677  1.00111.82           C  
ATOM    296  N   GLU A 375     241.842 222.330 205.045  1.00114.06           N  
ATOM    297  CA  GLU A 375     243.134 222.146 205.688  1.00114.06           C  
ATOM    298  C   GLU A 375     244.226 222.955 205.019  1.00114.06           C  
ATOM    299  O   GLU A 375     245.256 223.210 205.645  1.00114.06           O  
ATOM    300  CB  GLU A 375     243.563 220.671 205.701  1.00114.06           C  
ATOM    301  CG  GLU A 375     242.716 219.749 206.563  1.00114.06           C  
ATOM    302  CD  GLU A 375     241.465 219.268 205.862  1.00114.06           C  
ATOM    303  OE1 GLU A 375     241.291 219.601 204.675  1.00114.06           O  
ATOM    304  OE2 GLU A 375     240.657 218.559 206.497  1.00114.06           O  
ATOM    305  N   LEU A 376     244.021 223.352 203.767  1.00110.87           N  
ATOM    306  CA  LEU A 376     244.950 224.209 203.051  1.00110.87           C  
ATOM    307  C   LEU A 376     244.461 225.642 202.952  1.00110.87           C  
ATOM    308  O   LEU A 376     245.259 226.566 203.101  1.00110.87           O  
ATOM    309  CB  LEU A 376     245.210 223.670 201.643  1.00110.87           C  
ATOM    310  CG  LEU A 376     245.307 222.153 201.487  1.00110.87           C  
ATOM    311  CD1 LEU A 376     245.626 221.796 200.052  1.00110.87           C  
ATOM    312  CD2 LEU A 376     246.340 221.563 202.425  1.00110.87           C  
ATOM    313  N   GLU A 377     243.154 225.820 202.748  1.00108.87           N  
ATOM    314  CA  GLU A 377     242.558 227.177 202.626  1.00108.87           C  
ATOM    315  C   GLU A 377     242.768 227.970 203.923  1.00108.87           C  
ATOM    316  O   GLU A 377     243.030 229.186 203.830  1.00108.87           O  
ATOM    317  CB  GLU A 377     241.071 227.076 202.283  1.00108.87           C  
ATOM    318  CG  GLU A 377     240.239 226.440 203.382  1.00108.87           C  
ATOM    319  CD  GLU A 377     238.818 226.966 203.486  1.00108.87           C  
ATOM    320  OE1 GLU A 377     237.959 226.498 202.713  1.00108.87           O  
ATOM    321  OE2 GLU A 377     238.574 227.841 204.340  1.00108.87           O  
ATOM    322  N   ILE A 378     242.645 227.313 205.082  1.00105.79           N  
ATOM    323  CA  ILE A 378     242.786 227.991 206.368  1.00105.79           C  
ATOM    324  C   ILE A 378     244.241 228.341 206.630  1.00105.79           C  
ATOM    325  O   ILE A 378     244.554 229.449 207.078  1.00105.79           O  
ATOM    326  CB  ILE A 378     242.197 227.139 207.503  1.00105.79           C  
ATOM    327  CG1 ILE A 378     240.675 227.183 207.450  1.00105.79           C  
ATOM    328  CG2 ILE A 378     242.687 227.641 208.843  1.00105.79           C  
ATOM    329  CD1 ILE A 378     240.000 226.450 208.563  1.00105.79           C  
ATOM    330  N   ARG A 379     245.156 227.413 206.354  1.00104.37           N  
ATOM    331  CA  ARG A 379     246.568 227.763 206.416  1.00104.37           C  
ATOM    332  C   ARG A 379     246.884 228.871 205.426  1.00104.37           C  
ATOM    333  O   ARG A 379     247.114 230.022 205.809  1.00104.37           O  
ATOM    334  CB  ARG A 379     247.437 226.540 206.132  1.00104.37           C  
ATOM    335  CG  ARG A 379     247.165 225.360 207.014  1.00104.37           C  
ATOM    336  CD  ARG A 379     247.418 225.688 208.463  1.00104.37           C  
ATOM    337  NE  ARG A 379     247.236 224.513 209.305  1.00104.37           N  
ATOM    338  CZ  ARG A 379     247.160 224.551 210.627  1.00104.37           C  
ATOM    339  NH1 ARG A 379     246.997 223.433 211.312  1.00104.37           N  
ATOM    340  NH2 ARG A 379     247.245 225.709 211.258  1.00104.37           N  
ATOM    341  N   GLY A 380     246.834 228.555 204.140  1.00107.28           N  
ATOM    342  CA  GLY A 380     247.331 229.465 203.137  1.00107.28           C  
ATOM    343  C   GLY A 380     246.356 230.533 202.703  1.00107.28           C  
ATOM    344  O   GLY A 380     246.269 230.827 201.512  1.00107.28           O  
ATOM    345  N   GLU A 381     245.647 231.113 203.674  1.00106.71           N  
ATOM    346  CA  GLU A 381     244.680 232.221 203.443  1.00106.71           C  
ATOM    347  C   GLU A 381     245.376 233.537 203.050  1.00106.71           C  
ATOM    348  O   GLU A 381     244.807 234.265 202.213  1.00106.71           O  
ATOM    349  CB  GLU A 381     243.806 232.425 204.683  1.00106.71           C  
ATOM    350  CG  GLU A 381     242.595 231.510 204.726  1.00106.71           C  
ATOM    351  CD  GLU A 381     241.336 232.098 204.112  1.00106.71           C  
ATOM    352  OE1 GLU A 381     241.461 232.991 203.251  1.00106.71           O  
ATOM    353  OE2 GLU A 381     240.233 231.661 204.496  1.00106.71           O  
ATOM    354  N   TRP A 382     246.534 233.848 203.652  1.00104.48           N  
ATOM    355  CA  TRP A 382     247.202 235.125 203.451  1.00104.48           C  
ATOM    356  C   TRP A 382     247.872 235.195 202.093  1.00104.48           C  
ATOM    357  O   TRP A 382     247.960 236.274 201.501  1.00104.48           O  
ATOM    358  CB  TRP A 382     248.224 235.364 204.558  1.00104.48           C  
ATOM    359  CG  TRP A 382     248.679 236.779 204.642  1.00104.48           C  
ATOM    360  CD1 TRP A 382     248.063 237.801 205.294  1.00104.48           C  
ATOM    361  CD2 TRP A 382     249.844 237.338 204.030  1.00104.48           C  
ATOM    362  NE1 TRP A 382     248.778 238.961 205.139  1.00104.48           N  
ATOM    363  CE2 TRP A 382     249.876 238.701 204.364  1.00104.48           C  
ATOM    364  CE3 TRP A 382     250.867 236.815 203.239  1.00104.48           C  
ATOM    365  CZ2 TRP A 382     250.886 239.545 203.935  1.00104.48           C  
ATOM    366  CZ3 TRP A 382     251.868 237.657 202.815  1.00104.48           C  
ATOM    367  CH2 TRP A 382     251.872 239.005 203.164  1.00104.48           C  
ATOM    368  N   TYR A 383     248.343 234.063 201.580  1.00107.21           N  
ATOM    369  CA  TYR A 383     248.891 234.050 200.233  1.00107.21           C  
ATOM    370  C   TYR A 383     247.798 234.019 199.177  1.00107.21           C  
ATOM    371  O   TYR A 383     247.982 234.575 198.090  1.00107.21           O  
ATOM    372  CB  TYR A 383     249.832 232.862 200.059  1.00107.21           C  
ATOM    373  CG  TYR A 383     250.903 232.792 201.120  1.00107.21           C  
ATOM    374  CD1 TYR A 383     251.623 233.920 201.485  1.00107.21           C  
ATOM    375  CD2 TYR A 383     251.185 231.598 201.764  1.00107.21           C  
ATOM    376  CE1 TYR A 383     252.599 233.858 202.462  1.00107.21           C  
ATOM    377  CE2 TYR A 383     252.157 231.526 202.739  1.00107.21           C  
ATOM    378  CZ  TYR A 383     252.861 232.655 203.085  1.00107.21           C  
ATOM    379  OH  TYR A 383     253.829 232.572 204.058  1.00107.21           O  
ATOM    380  N   PHE A 384     246.664 233.384 199.469  1.00102.90           N  
ATOM    381  CA  PHE A 384     245.595 233.320 198.481  1.00102.90           C  
ATOM    382  C   PHE A 384     245.001 234.691 198.203  1.00102.90           C  
ATOM    383  O   PHE A 384     244.690 235.002 197.051  1.00102.90           O  
ATOM    384  CB  PHE A 384     244.509 232.349 198.923  1.00102.90           C  
ATOM    385  CG  PHE A 384     244.919 230.915 198.837  1.00102.90           C  
ATOM    386  CD1 PHE A 384     246.100 230.562 198.222  1.00102.90           C  
ATOM    387  CD2 PHE A 384     244.129 229.923 199.371  1.00102.90           C  
ATOM    388  CE1 PHE A 384     246.481 229.250 198.143  1.00102.90           C  
ATOM    389  CE2 PHE A 384     244.510 228.611 199.296  1.00102.90           C  
ATOM    390  CZ  PHE A 384     245.684 228.274 198.679  1.00102.90           C  
ATOM    391  N   MET A 385     244.819 235.526 199.229  1.00107.53           N  
ATOM    392  CA  MET A 385     244.302 236.865 198.944  1.00107.53           C  
ATOM    393  C   MET A 385     245.278 237.673 198.099  1.00107.53           C  
ATOM    394  O   MET A 385     244.866 238.413 197.195  1.00107.53           O  
ATOM    395  CB  MET A 385     243.947 237.620 200.221  1.00107.53           C  
ATOM    396  CG  MET A 385     242.639 237.182 200.840  1.00107.53           C  
ATOM    397  SD  MET A 385     242.665 235.592 201.661  1.00107.53           S  
ATOM    398  CE  MET A 385     243.561 236.050 203.138  1.00107.53           C  
ATOM    399  N   VAL A 386     246.575 237.534 198.362  1.00108.83           N  
ATOM    400  CA  VAL A 386     247.574 238.212 197.543  1.00108.83           C  
ATOM    401  C   VAL A 386     247.479 237.741 196.098  1.00108.83           C  
ATOM    402  O   VAL A 386     247.407 238.547 195.157  1.00108.83           O  
ATOM    403  CB  VAL A 386     248.978 237.979 198.126  1.00108.83           C  
ATOM    404  CG1 VAL A 386     250.034 238.243 197.085  1.00108.83           C  
ATOM    405  CG2 VAL A 386     249.194 238.879 199.320  1.00108.83           C  
ATOM    406  N   LEU A 387     247.446 236.424 195.905  1.00107.06           N  
ATOM    407  CA  LEU A 387     247.386 235.879 194.556  1.00107.06           C  
ATOM    408  C   LEU A 387     246.116 236.318 193.847  1.00107.06           C  
ATOM    409  O   LEU A 387     246.126 236.567 192.638  1.00107.06           O  
ATOM    410  CB  LEU A 387     247.478 234.358 194.605  1.00107.06           C  
ATOM    411  CG  LEU A 387     248.869 233.825 194.921  1.00107.06           C  
ATOM    412  CD1 LEU A 387     248.870 232.320 194.982  1.00107.06           C  
ATOM    413  CD2 LEU A 387     249.840 234.310 193.879  1.00107.06           C  
ATOM    414  N   ASP A 388     245.012 236.433 194.577  1.00110.03           N  
ATOM    415  CA  ASP A 388     243.763 236.766 193.913  1.00110.03           C  
ATOM    416  C   ASP A 388     243.684 238.243 193.563  1.00110.03           C  
ATOM    417  O   ASP A 388     243.088 238.600 192.541  1.00110.03           O  
ATOM    418  CB  ASP A 388     242.585 236.325 194.768  1.00110.03           C  
ATOM    419  CG  ASP A 388     242.320 234.846 194.635  1.00110.03           C  
ATOM    420  OD1 ASP A 388     243.210 234.143 194.121  1.00110.03           O  
ATOM    421  OD2 ASP A 388     241.232 234.381 195.028  1.00110.03           O  
ATOM    422  N   SER A 389     244.298 239.116 194.356  1.00112.73           N  
ATOM    423  CA  SER A 389     244.426 240.493 193.892  1.00112.73           C  
ATOM    424  C   SER A 389     245.302 240.565 192.646  1.00112.73           C  
ATOM    425  O   SER A 389     245.016 241.334 191.715  1.00112.73           O  
ATOM    426  CB  SER A 389     244.977 241.380 194.999  1.00112.73           C  
ATOM    427  OG  SER A 389     244.067 241.438 196.079  1.00112.73           O  
ATOM    428  N   ILE A 390     246.365 239.760 192.608  1.00113.43           N  
ATOM    429  CA  ILE A 390     247.203 239.698 191.414  1.00113.43           C  
ATOM    430  C   ILE A 390     246.376 239.298 190.202  1.00113.43           C  
ATOM    431  O   ILE A 390     246.468 239.912 189.130  1.00113.43           O  
ATOM    432  CB  ILE A 390     248.375 238.729 191.647  1.00113.43           C  
ATOM    433  CG1 ILE A 390     249.492 239.432 192.420  1.00113.43           C  
ATOM    434  CG2 ILE A 390     248.855 238.136 190.336  1.00113.43           C  
ATOM    435  CD1 ILE A 390     250.609 238.526 192.846  1.00113.43           C  
ATOM    436  N   PHE A 391     245.547 238.272 190.354  1.00113.97           N  
ATOM    437  CA  PHE A 391     244.719 237.824 189.243  1.00113.97           C  
ATOM    438  C   PHE A 391     243.703 238.881 188.842  1.00113.97           C  
ATOM    439  O   PHE A 391     243.368 239.008 187.662  1.00113.97           O  
ATOM    440  CB  PHE A 391     244.026 236.520 189.605  1.00113.97           C  
ATOM    441  CG  PHE A 391     244.952 235.357 189.674  1.00113.97           C  
ATOM    442  CD1 PHE A 391     245.948 235.203 188.740  1.00113.97           C  
ATOM    443  CD2 PHE A 391     244.828 234.418 190.672  1.00113.97           C  
ATOM    444  CE1 PHE A 391     246.798 234.131 188.795  1.00113.97           C  
ATOM    445  CE2 PHE A 391     245.674 233.348 190.729  1.00113.97           C  
ATOM    446  CZ  PHE A 391     246.661 233.201 189.794  1.00113.97           C  
ATOM    447  N   LEU A 392     243.189 239.643 189.806  1.00119.00           N  
ATOM    448  CA  LEU A 392     242.279 240.726 189.450  1.00119.00           C  
ATOM    449  C   LEU A 392     242.974 241.754 188.572  1.00119.00           C  
ATOM    450  O   LEU A 392     242.403 242.224 187.581  1.00119.00           O  
ATOM    451  CB  LEU A 392     241.721 241.398 190.701  1.00119.00           C  
ATOM    452  CG  LEU A 392     241.003 242.723 190.434  1.00119.00           C  
ATOM    453  CD1 LEU A 392     239.721 242.481 189.672  1.00119.00           C  
ATOM    454  CD2 LEU A 392     240.725 243.476 191.721  1.00119.00           C  
ATOM    455  N   SER A 393     244.209 242.116 188.920  1.00123.80           N  
ATOM    456  CA  SER A 393     244.954 243.056 188.082  1.00123.80           C  
ATOM    457  C   SER A 393     245.188 242.485 186.685  1.00123.80           C  
ATOM    458  O   SER A 393     245.047 243.194 185.676  1.00123.80           O  
ATOM    459  CB  SER A 393     246.281 243.414 188.747  1.00123.80           C  
ATOM    460  OG  SER A 393     247.203 242.343 188.671  1.00123.80           O  
ATOM    461  N   ILE A 394     245.543 241.203 186.608  1.00125.01           N  
ATOM    462  CA  ILE A 394     245.767 240.573 185.308  1.00125.01           C  
ATOM    463  C   ILE A 394     244.497 240.614 184.470  1.00125.01           C  
ATOM    464  O   ILE A 394     244.537 240.866 183.258  1.00125.01           O  
ATOM    465  CB  ILE A 394     246.270 239.133 185.494  1.00125.01           C  
ATOM    466  CG1 ILE A 394     247.649 239.139 186.144  1.00125.01           C  
ATOM    467  CG2 ILE A 394     246.294 238.398 184.172  1.00125.01           C  
ATOM    468  CD1 ILE A 394     248.741 239.599 185.234  1.00125.01           C  
ATOM    469  N   TYR A 395     243.353 240.357 185.094  1.00124.58           N  
ATOM    470  CA  TYR A 395     242.108 240.372 184.344  1.00124.58           C  
ATOM    471  C   TYR A 395     241.722 241.784 183.935  1.00124.58           C  
ATOM    472  O   TYR A 395     241.095 241.964 182.887  1.00124.58           O  
ATOM    473  CB  TYR A 395     241.000 239.716 185.155  1.00124.58           C  
ATOM    474  CG  TYR A 395     241.143 238.220 185.249  1.00124.58           C  
ATOM    475  CD1 TYR A 395     242.002 237.534 184.405  1.00124.58           C  
ATOM    476  CD2 TYR A 395     240.433 237.495 186.190  1.00124.58           C  
ATOM    477  CE1 TYR A 395     242.145 236.167 184.494  1.00124.58           C  
ATOM    478  CE2 TYR A 395     240.570 236.129 186.283  1.00124.58           C  
ATOM    479  CZ  TYR A 395     241.426 235.470 185.434  1.00124.58           C  
ATOM    480  OH  TYR A 395     241.565 234.107 185.526  1.00124.58           O  
ATOM    481  N   VAL A 396     242.090 242.798 184.729  1.00130.98           N  
ATOM    482  CA  VAL A 396     241.929 244.179 184.267  1.00130.98           C  
ATOM    483  C   VAL A 396     242.698 244.385 182.976  1.00130.98           C  
ATOM    484  O   VAL A 396     242.155 244.862 181.967  1.00130.98           O  
ATOM    485  CB  VAL A 396     242.390 245.182 185.340  1.00130.98           C  
ATOM    486  CG1 VAL A 396     242.313 246.587 184.783  1.00130.98           C  
ATOM    487  CG2 VAL A 396     241.546 245.087 186.587  1.00130.98           C  
ATOM    488  N   LEU A 397     243.978 244.014 182.995  1.00134.34           N  
ATOM    489  CA  LEU A 397     244.797 244.058 181.792  1.00134.34           C  
ATOM    490  C   LEU A 397     244.051 243.456 180.614  1.00134.34           C  
ATOM    491  O   LEU A 397     243.770 244.133 179.617  1.00134.34           O  
ATOM    492  CB  LEU A 397     246.106 243.305 182.032  1.00134.34           C  
ATOM    493  CG  LEU A 397     247.209 243.350 180.974  1.00134.34           C  
ATOM    494  CD1 LEU A 397     248.549 243.142 181.635  1.00134.34           C  
ATOM    495  CD2 LEU A 397     247.008 242.291 179.902  1.00134.34           C  
ATOM    496  N   GLU A 398     243.712 242.175 180.729  1.00137.26           N  
ATOM    497  CA  GLU A 398     243.184 241.454 179.578  1.00137.26           C  
ATOM    498  C   GLU A 398     241.864 242.038 179.100  1.00137.26           C  
ATOM    499  O   GLU A 398     241.672 242.236 177.896  1.00137.26           O  
ATOM    500  CB  GLU A 398     243.022 239.977 179.909  1.00137.26           C  
ATOM    501  CG  GLU A 398     242.305 239.196 178.831  1.00137.26           C  
ATOM    502  CD  GLU A 398     242.375 237.710 179.070  1.00137.26           C  
ATOM    503  OE1 GLU A 398     243.101 237.306 179.996  1.00137.26           O  
ATOM    504  OE2 GLU A 398     241.706 236.948 178.345  1.00137.26           O  
ATOM    505  N   ALA A 399     240.941 242.330 180.018  1.00136.74           N  
ATOM    506  CA  ALA A 399     239.619 242.778 179.599  1.00136.74           C  
ATOM    507  C   ALA A 399     239.680 244.149 178.942  1.00136.74           C  
ATOM    508  O   ALA A 399     239.076 244.365 177.883  1.00136.74           O  
ATOM    509  CB  ALA A 399     238.664 242.791 180.788  1.00136.74           C  
ATOM    510  N   VAL A 400     240.414 245.092 179.543  1.00135.63           N  
ATOM    511  CA  VAL A 400     240.500 246.416 178.935  1.00135.63           C  
ATOM    512  C   VAL A 400     241.194 246.339 177.584  1.00135.63           C  
ATOM    513  O   VAL A 400     240.754 246.963 176.609  1.00135.63           O  
ATOM    514  CB  VAL A 400     241.210 247.404 179.874  1.00135.63           C  
ATOM    515  CG1 VAL A 400     241.380 248.737 179.180  1.00135.63           C  
ATOM    516  CG2 VAL A 400     240.423 247.578 181.150  1.00135.63           C  
ATOM    517  N   LEU A 401     242.288 245.578 177.499  1.00137.72           N  
ATOM    518  CA  LEU A 401     243.015 245.503 176.241  1.00137.72           C  
ATOM    519  C   LEU A 401     242.159 244.879 175.152  1.00137.72           C  
ATOM    520  O   LEU A 401     242.160 245.349 174.009  1.00137.72           O  
ATOM    521  CB  LEU A 401     244.310 244.718 176.429  1.00137.72           C  
ATOM    522  CG  LEU A 401     245.444 245.511 177.084  1.00137.72           C  
ATOM    523  CD1 LEU A 401     246.770 244.784 176.944  1.00137.72           C  
ATOM    524  CD2 LEU A 401     245.538 246.912 176.509  1.00137.72           C  
ATOM    525  N   LYS A 402     241.405 243.832 175.489  1.00138.37           N  
ATOM    526  CA  LYS A 402     240.562 243.194 174.487  1.00138.37           C  
ATOM    527  C   LYS A 402     239.439 244.117 174.043  1.00138.37           C  
ATOM    528  O   LYS A 402     239.093 244.151 172.856  1.00138.37           O  
ATOM    529  CB  LYS A 402     240.005 241.882 175.030  1.00138.37           C  
ATOM    530  CG  LYS A 402     240.733 240.658 174.511  1.00138.37           C  
ATOM    531  CD  LYS A 402     240.232 239.383 175.169  1.00138.37           C  
ATOM    532  CE  LYS A 402     238.950 238.897 174.523  1.00138.37           C  
ATOM    533  NZ  LYS A 402     238.816 237.423 174.621  1.00138.37           N  
ATOM    534  N   LEU A 403     238.853 244.873 174.974  1.00138.71           N  
ATOM    535  CA  LEU A 403     237.789 245.791 174.585  1.00138.71           C  
ATOM    536  C   LEU A 403     238.321 246.869 173.651  1.00138.71           C  
ATOM    537  O   LEU A 403     237.722 247.148 172.604  1.00138.71           O  
ATOM    538  CB  LEU A 403     237.151 246.419 175.823  1.00138.71           C  
ATOM    539  CG  LEU A 403     235.987 247.384 175.571  1.00138.71           C  
ATOM    540  CD1 LEU A 403     235.046 246.837 174.523  1.00138.71           C  
ATOM    541  CD2 LEU A 403     235.237 247.686 176.851  1.00138.71           C  
ATOM    542  N   ILE A 404     239.461 247.469 174.004  1.00140.81           N  
ATOM    543  CA  ILE A 404     240.055 248.497 173.150  1.00140.81           C  
ATOM    544  C   ILE A 404     240.403 247.925 171.784  1.00140.81           C  
ATOM    545  O   ILE A 404     240.198 248.575 170.752  1.00140.81           O  
ATOM    546  CB  ILE A 404     241.286 249.121 173.831  1.00140.81           C  
ATOM    547  CG1 ILE A 404     240.850 249.986 175.011  1.00140.81           C  
ATOM    548  CG2 ILE A 404     242.091 249.929 172.841  1.00140.81           C  
ATOM    549  CD1 ILE A 404     239.861 251.062 174.634  1.00140.81           C  
ATOM    550  N   ALA A 405     240.930 246.702 171.752  1.00143.08           N  
ATOM    551  CA  ALA A 405     241.253 246.069 170.481  1.00143.08           C  
ATOM    552  C   ALA A 405     240.011 245.911 169.615  1.00143.08           C  
ATOM    553  O   ALA A 405     239.923 246.479 168.522  1.00143.08           O  
ATOM    554  CB  ALA A 405     241.907 244.711 170.728  1.00143.08           C  
ATOM    555  N   LEU A 406     239.026 245.158 170.102  1.00140.42           N  
ATOM    556  CA  LEU A 406     237.952 244.655 169.255  1.00140.42           C  
ATOM    557  C   LEU A 406     236.590 245.259 169.578  1.00140.42           C  
ATOM    558  O   LEU A 406     235.591 244.544 169.508  1.00140.42           O  
ATOM    559  CB  LEU A 406     237.880 243.134 169.362  1.00140.42           C  
ATOM    560  CG  LEU A 406     239.151 242.356 169.033  1.00140.42           C  
ATOM    561  CD1 LEU A 406     238.867 240.864 168.995  1.00140.42           C  
ATOM    562  CD2 LEU A 406     239.718 242.817 167.713  1.00140.42           C  
ATOM    563  N   GLY A 407     236.534 246.525 169.994  1.00140.05           N  
ATOM    564  CA  GLY A 407     235.278 247.264 169.929  1.00140.05           C  
ATOM    565  C   GLY A 407     234.117 246.527 170.559  1.00140.05           C  
ATOM    566  O   GLY A 407     234.242 245.930 171.629  1.00140.05           O  
ATOM    567  N   LEU A 408     232.970 246.544 169.879  1.00142.41           N  
ATOM    568  CA  LEU A 408     231.826 245.754 170.319  1.00142.41           C  
ATOM    569  C   LEU A 408     231.861 244.325 169.801  1.00142.41           C  
ATOM    570  O   LEU A 408     231.031 243.508 170.219  1.00142.41           O  
ATOM    571  CB  LEU A 408     230.522 246.420 169.894  1.00142.41           C  
ATOM    572  CG  LEU A 408     230.157 247.660 170.703  1.00142.41           C  
ATOM    573  CD1 LEU A 408     229.108 248.486 169.986  1.00142.41           C  
ATOM    574  CD2 LEU A 408     229.657 247.245 172.067  1.00142.41           C  
ATOM    575  N   GLU A 409     232.796 244.001 168.907  1.00148.08           N  
ATOM    576  CA  GLU A 409     232.994 242.607 168.536  1.00148.08           C  
ATOM    577  C   GLU A 409     233.421 241.785 169.742  1.00148.08           C  
ATOM    578  O   GLU A 409     233.186 240.573 169.792  1.00148.08           O  
ATOM    579  CB  GLU A 409     234.035 242.510 167.422  1.00148.08           C  
ATOM    580  CG  GLU A 409     233.456 242.618 166.029  1.00148.08           C  
ATOM    581  CD  GLU A 409     232.202 241.791 165.860  1.00148.08           C  
ATOM    582  OE1 GLU A 409     231.094 242.365 165.933  1.00148.08           O  
ATOM    583  OE2 GLU A 409     232.323 240.566 165.652  1.00148.08           O  
ATOM    584  N   TYR A 410     234.072 242.430 170.706  1.00148.71           N  
ATOM    585  CA  TYR A 410     234.374 241.780 171.976  1.00148.71           C  
ATOM    586  C   TYR A 410     233.091 241.409 172.710  1.00148.71           C  
ATOM    587  O   TYR A 410     232.925 240.271 173.158  1.00148.71           O  
ATOM    588  CB  TYR A 410     235.248 242.692 172.840  1.00148.71           C  
ATOM    589  CG  TYR A 410     235.283 242.305 174.302  1.00148.71           C  
ATOM    590  CD1 TYR A 410     234.361 242.824 175.197  1.00148.71           C  
ATOM    591  CD2 TYR A 410     236.238 241.424 174.785  1.00148.71           C  
ATOM    592  CE1 TYR A 410     234.380 242.467 176.524  1.00148.71           C  
ATOM    593  CE2 TYR A 410     236.266 241.065 176.114  1.00148.71           C  
ATOM    594  CZ  TYR A 410     235.334 241.589 176.981  1.00148.71           C  
ATOM    595  OH  TYR A 410     235.347 241.242 178.314  1.00148.71           O  
ATOM    596  N   PHE A 411     232.165 242.360 172.837  1.00148.43           N  
ATOM    597  CA  PHE A 411     230.870 242.048 173.427  1.00148.43           C  
ATOM    598  C   PHE A 411     230.089 241.052 172.587  1.00148.43           C  
ATOM    599  O   PHE A 411     229.111 240.477 173.074  1.00148.43           O  
ATOM    600  CB  PHE A 411     230.038 243.318 173.591  1.00148.43           C  
ATOM    601  CG  PHE A 411     230.117 243.929 174.958  1.00148.43           C  
ATOM    602  CD1 PHE A 411     231.325 244.382 175.460  1.00148.43           C  
ATOM    603  CD2 PHE A 411     228.978 244.072 175.730  1.00148.43           C  
ATOM    604  CE1 PHE A 411     231.396 244.950 176.713  1.00148.43           C  
ATOM    605  CE2 PHE A 411     229.043 244.641 176.982  1.00148.43           C  
ATOM    606  CZ  PHE A 411     230.252 245.081 177.474  1.00148.43           C  
ATOM    607  N   TYR A 412     230.489 240.852 171.334  1.00155.32           N  
ATOM    608  CA  TYR A 412     229.701 240.021 170.433  1.00155.32           C  
ATOM    609  C   TYR A 412     229.783 238.546 170.821  1.00155.32           C  
ATOM    610  O   TYR A 412     228.759 237.857 170.882  1.00155.32           O  
ATOM    611  CB  TYR A 412     230.173 240.259 168.994  1.00155.32           C  
ATOM    612  CG  TYR A 412     229.300 239.667 167.915  1.00155.32           C  
ATOM    613  CD1 TYR A 412     227.985 240.087 167.751  1.00155.32           C  
ATOM    614  CD2 TYR A 412     229.798 238.718 167.036  1.00155.32           C  
ATOM    615  CE1 TYR A 412     227.181 239.554 166.754  1.00155.32           C  
ATOM    616  CE2 TYR A 412     229.004 238.179 166.036  1.00155.32           C  
ATOM    617  CZ  TYR A 412     227.698 238.600 165.899  1.00155.32           C  
ATOM    618  OH  TYR A 412     226.914 238.064 164.903  1.00155.32           O  
ATOM    619  N   ASP A 413     230.991 238.050 171.115  1.00160.83           N  
ATOM    620  CA  ASP A 413     231.236 236.634 171.384  1.00160.83           C  
ATOM    621  C   ASP A 413     230.877 236.282 172.828  1.00160.83           C  
ATOM    622  O   ASP A 413     231.244 237.009 173.754  1.00160.83           O  
ATOM    623  CB  ASP A 413     232.697 236.285 171.114  1.00160.83           C  
ATOM    624  CG  ASP A 413     232.980 234.799 171.247  1.00160.83           C  
ATOM    625  OD1 ASP A 413     232.592 234.020 170.351  1.00160.83           O  
ATOM    626  OD2 ASP A 413     233.596 234.409 172.257  1.00160.83           O  
ATOM    627  N   PRO A 414     230.172 235.165 173.049  1.00160.61           N  
ATOM    628  CA  PRO A 414     229.680 234.859 174.399  1.00160.61           C  
ATOM    629  C   PRO A 414     230.730 234.259 175.323  1.00160.61           C  
ATOM    630  O   PRO A 414     230.597 234.354 176.549  1.00160.61           O  
ATOM    631  CB  PRO A 414     228.530 233.873 174.141  1.00160.61           C  
ATOM    632  CG  PRO A 414     228.618 233.486 172.691  1.00160.61           C  
ATOM    633  CD  PRO A 414     229.819 234.120 172.081  1.00160.61           C  
ATOM    634  N   TRP A 415     231.784 233.662 174.758  1.00155.33           N  
ATOM    635  CA  TRP A 415     232.860 233.145 175.598  1.00155.33           C  
ATOM    636  C   TRP A 415     233.461 234.248 176.453  1.00155.33           C  
ATOM    637  O   TRP A 415     233.677 234.063 177.654  1.00155.33           O  
ATOM    638  CB  TRP A 415     233.949 232.490 174.747  1.00155.33           C  
ATOM    639  CG  TRP A 415     233.867 230.996 174.668  1.00155.33           C  
ATOM    640  CD1 TRP A 415     233.745 230.238 173.541  1.00155.33           C  
ATOM    641  CD2 TRP A 415     233.915 230.075 175.764  1.00155.33           C  
ATOM    642  NE1 TRP A 415     233.710 228.904 173.866  1.00155.33           N  
ATOM    643  CE2 TRP A 415     233.811 228.778 175.225  1.00155.33           C  
ATOM    644  CE3 TRP A 415     234.031 230.221 177.150  1.00155.33           C  
ATOM    645  CZ2 TRP A 415     233.822 227.639 176.022  1.00155.33           C  
ATOM    646  CZ3 TRP A 415     234.039 229.089 177.938  1.00155.33           C  
ATOM    647  CH2 TRP A 415     233.936 227.815 177.373  1.00155.33           C  
ATOM    648  N   ASN A 416     233.731 235.376 175.786  1.00153.44           N  
ATOM    649  CA  ASN A 416     234.242 236.621 176.414  1.00153.44           C  
ATOM    650  C   ASN A 416     233.142 237.206 177.308  1.00153.44           C  
ATOM    651  O   ASN A 416     233.470 237.653 178.425  1.00153.44           O  
ATOM    652  CB  ASN A 416     234.685 237.635 175.356  1.00153.44           C  
ATOM    653  CG  ASN A 416     235.790 237.113 174.462  1.00153.44           C  
ATOM    654  OD1 ASN A 416     236.240 235.980 174.621  1.00153.44           O  
ATOM    655  ND2 ASN A 416     236.233 237.930 173.521  1.00153.44           N  
ATOM    656  N   ASN A 417     231.885 237.187 176.838  1.00155.55           N  
ATOM    657  CA  ASN A 417     230.794 237.744 177.631  1.00155.55           C  
ATOM    658  C   ASN A 417     230.764 237.110 179.016  1.00155.55           C  
ATOM    659  O   ASN A 417     230.548 237.795 180.027  1.00155.55           O  
ATOM    660  CB  ASN A 417     229.465 237.532 176.914  1.00155.55           C  
ATOM    661  CG  ASN A 417     229.316 238.423 175.711  1.00155.55           C  
ATOM    662  OD1 ASN A 417     228.783 238.015 174.685  1.00155.55           O  
ATOM    663  ND2 ASN A 417     229.795 239.654 175.826  1.00155.55           N  
ATOM    664  N   LEU A 418     230.983 235.797 179.076  1.00147.19           N  
ATOM    665  CA  LEU A 418     231.193 235.126 180.351  1.00147.19           C  
ATOM    666  C   LEU A 418     232.330 235.774 181.128  1.00147.19           C  
ATOM    667  O   LEU A 418     232.198 236.070 182.322  1.00147.19           O  
ATOM    668  CB  LEU A 418     231.477 233.647 180.097  1.00147.19           C  
ATOM    669  CG  LEU A 418     231.619 232.689 181.271  1.00147.19           C  
ATOM    670  CD1 LEU A 418     231.085 231.334 180.884  1.00147.19           C  
ATOM    671  CD2 LEU A 418     233.083 232.567 181.630  1.00147.19           C  
ATOM    672  N   ASP A 419     233.458 236.014 180.454  1.00142.98           N  
ATOM    673  CA  ASP A 419     234.615 236.604 181.117  1.00142.98           C  
ATOM    674  C   ASP A 419     234.307 238.003 181.619  1.00142.98           C  
ATOM    675  O   ASP A 419     234.751 238.392 182.699  1.00142.98           O  
ATOM    676  CB  ASP A 419     235.800 236.647 180.162  1.00142.98           C  
ATOM    677  CG  ASP A 419     237.125 236.631 180.881  1.00142.98           C  
ATOM    678  OD1 ASP A 419     237.191 237.142 182.014  1.00142.98           O  
ATOM    679  OD2 ASP A 419     238.104 236.102 180.312  1.00142.98           O  
ATOM    680  N   PHE A 420     233.562 238.782 180.837  1.00139.08           N  
ATOM    681  CA  PHE A 420     233.212 240.130 181.260  1.00139.08           C  
ATOM    682  C   PHE A 420     232.324 240.106 182.492  1.00139.08           C  
ATOM    683  O   PHE A 420     232.504 240.915 183.408  1.00139.08           O  
ATOM    684  CB  PHE A 420     232.524 240.881 180.126  1.00139.08           C  
ATOM    685  CG  PHE A 420     232.220 242.306 180.453  1.00139.08           C  
ATOM    686  CD1 PHE A 420     233.207 243.266 180.379  1.00139.08           C  
ATOM    687  CD2 PHE A 420     230.949 242.685 180.836  1.00139.08           C  
ATOM    688  CE1 PHE A 420     232.934 244.577 180.688  1.00139.08           C  
ATOM    689  CE2 PHE A 420     230.671 243.994 181.138  1.00139.08           C  
ATOM    690  CZ  PHE A 420     231.667 244.944 181.064  1.00139.08           C  
ATOM    691  N   PHE A 421     231.355 239.191 182.536  1.00134.86           N  
ATOM    692  CA  PHE A 421     230.512 239.100 183.725  1.00134.86           C  
ATOM    693  C   PHE A 421     231.326 238.678 184.944  1.00134.86           C  
ATOM    694  O   PHE A 421     231.134 239.206 186.049  1.00134.86           O  
ATOM    695  CB  PHE A 421     229.365 238.128 183.486  1.00134.86           C  
ATOM    696  CG  PHE A 421     228.713 237.654 184.743  1.00134.86           C  
ATOM    697  CD1 PHE A 421     227.763 238.435 185.371  1.00134.86           C  
ATOM    698  CD2 PHE A 421     229.040 236.430 185.291  1.00134.86           C  
ATOM    699  CE1 PHE A 421     227.157 238.012 186.523  1.00134.86           C  
ATOM    700  CE2 PHE A 421     228.437 235.999 186.442  1.00134.86           C  
ATOM    701  CZ  PHE A 421     227.492 236.790 187.060  1.00134.86           C  
ATOM    702  N   ILE A 422     232.234 237.719 184.759  1.00132.01           N  
ATOM    703  CA  ILE A 422     233.121 237.305 185.842  1.00132.01           C  
ATOM    704  C   ILE A 422     233.943 238.487 186.327  1.00132.01           C  
ATOM    705  O   ILE A 422     234.113 238.699 187.534  1.00132.01           O  
ATOM    706  CB  ILE A 422     234.022 236.153 185.369  1.00132.01           C  
ATOM    707  CG1 ILE A 422     233.238 234.847 185.327  1.00132.01           C  
ATOM    708  CG2 ILE A 422     235.231 236.025 186.262  1.00132.01           C  
ATOM    709  CD1 ILE A 422     234.052 233.682 184.872  1.00132.01           C  
ATOM    710  N   MET A 423     234.474 239.265 185.386  1.00130.68           N  
ATOM    711  CA  MET A 423     235.202 240.484 185.703  1.00130.68           C  
ATOM    712  C   MET A 423     234.375 241.436 186.551  1.00130.68           C  
ATOM    713  O   MET A 423     234.865 242.001 187.537  1.00130.68           O  
ATOM    714  CB  MET A 423     235.620 241.171 184.410  1.00130.68           C  
ATOM    715  CG  MET A 423     236.569 242.261 184.695  1.00130.68           C  
ATOM    716  SD  MET A 423     238.237 241.661 184.810  1.00130.68           S  
ATOM    717  CE  MET A 423     238.951 243.164 185.390  1.00130.68           C  
ATOM    718  N   VAL A 424     233.133 241.667 186.145  1.00129.91           N  
ATOM    719  CA  VAL A 424     232.276 242.587 186.878  1.00129.91           C  
ATOM    720  C   VAL A 424     232.078 242.099 188.304  1.00129.91           C  
ATOM    721  O   VAL A 424     232.175 242.877 189.260  1.00129.91           O  
ATOM    722  CB  VAL A 424     230.941 242.760 186.137  1.00129.91           C  
ATOM    723  CG1 VAL A 424     229.964 243.549 186.980  1.00129.91           C  
ATOM    724  CG2 VAL A 424     231.182 243.458 184.818  1.00129.91           C  
ATOM    725  N   MET A 425     231.829 240.800 188.475  1.00130.72           N  
ATOM    726  CA  MET A 425     231.691 240.262 189.828  1.00130.72           C  
ATOM    727  C   MET A 425     232.965 240.462 190.638  1.00130.72           C  
ATOM    728  O   MET A 425     232.906 240.821 191.821  1.00130.72           O  
ATOM    729  CB  MET A 425     231.312 238.781 189.782  1.00130.72           C  
ATOM    730  CG  MET A 425     229.943 238.510 189.188  1.00130.72           C  
ATOM    731  SD  MET A 425     228.639 239.288 190.155  1.00130.72           S  
ATOM    732  CE  MET A 425     228.266 240.720 189.153  1.00130.72           C  
ATOM    733  N   ALA A 426     234.125 240.233 190.017  1.00125.61           N  
ATOM    734  CA  ALA A 426     235.391 240.360 190.734  1.00125.61           C  
ATOM    735  C   ALA A 426     235.609 241.785 191.216  1.00125.61           C  
ATOM    736  O   ALA A 426     235.948 242.017 192.382  1.00125.61           O  
ATOM    737  CB  ALA A 426     236.549 239.915 189.845  1.00125.61           C  
ATOM    738  N   VAL A 427     235.398 242.760 190.337  1.00125.34           N  
ATOM    739  CA  VAL A 427     235.634 244.141 190.739  1.00125.34           C  
ATOM    740  C   VAL A 427     234.617 244.569 191.791  1.00125.34           C  
ATOM    741  O   VAL A 427     234.951 245.305 192.733  1.00125.34           O  
ATOM    742  CB  VAL A 427     235.639 245.074 189.511  1.00125.34           C  
ATOM    743  CG1 VAL A 427     234.277 245.136 188.853  1.00125.34           C  
ATOM    744  CG2 VAL A 427     236.110 246.465 189.901  1.00125.34           C  
ATOM    745  N   LEU A 428     233.369 244.103 191.671  1.00128.13           N  
ATOM    746  CA  LEU A 428     232.363 244.481 192.657  1.00128.13           C  
ATOM    747  C   LEU A 428     232.688 243.918 194.031  1.00128.13           C  
ATOM    748  O   LEU A 428     232.577 244.628 195.036  1.00128.13           O  
ATOM    749  CB  LEU A 428     230.975 244.029 192.216  1.00128.13           C  
ATOM    750  CG  LEU A 428     230.396 244.693 190.972  1.00128.13           C  
ATOM    751  CD1 LEU A 428     229.084 244.037 190.590  1.00128.13           C  
ATOM    752  CD2 LEU A 428     230.199 246.173 191.210  1.00128.13           C  
ATOM    753  N   ASP A 429     233.081 242.648 194.112  1.00125.73           N  
ATOM    754  CA  ASP A 429     233.382 242.122 195.436  1.00125.73           C  
ATOM    755  C   ASP A 429     234.665 242.731 195.988  1.00125.73           C  
ATOM    756  O   ASP A 429     234.798 242.883 197.204  1.00125.73           O  
ATOM    757  CB  ASP A 429     233.400 240.585 195.423  1.00125.73           C  
ATOM    758  CG  ASP A 429     234.662 239.981 194.826  1.00125.73           C  
ATOM    759  OD1 ASP A 429     235.686 240.664 194.635  1.00125.73           O  
ATOM    760  OD2 ASP A 429     234.619 238.767 194.542  1.00125.73           O  
ATOM    761  N   PHE A 430     235.598 243.121 195.115  1.00122.37           N  
ATOM    762  CA  PHE A 430     236.774 243.859 195.565  1.00122.37           C  
ATOM    763  C   PHE A 430     236.378 245.159 196.252  1.00122.37           C  
ATOM    764  O   PHE A 430     236.806 245.444 197.380  1.00122.37           O  
ATOM    765  CB  PHE A 430     237.674 244.131 194.363  1.00122.37           C  
ATOM    766  CG  PHE A 430     238.806 245.078 194.630  1.00122.37           C  
ATOM    767  CD1 PHE A 430     238.633 246.443 194.517  1.00122.37           C  
ATOM    768  CD2 PHE A 430     240.060 244.595 194.934  1.00122.37           C  
ATOM    769  CE1 PHE A 430     239.678 247.302 194.742  1.00122.37           C  
ATOM    770  CE2 PHE A 430     241.107 245.452 195.153  1.00122.37           C  
ATOM    771  CZ  PHE A 430     240.916 246.804 195.054  1.00122.37           C  
ATOM    772  N   VAL A 431     235.558 245.967 195.582  1.00122.99           N  
ATOM    773  CA  VAL A 431     235.209 247.251 196.178  1.00122.99           C  
ATOM    774  C   VAL A 431     234.347 247.052 197.417  1.00122.99           C  
ATOM    775  O   VAL A 431     234.476 247.798 198.396  1.00122.99           O  
ATOM    776  CB  VAL A 431     234.531 248.175 195.150  1.00122.99           C  
ATOM    777  CG1 VAL A 431     235.480 248.457 193.994  1.00122.99           C  
ATOM    778  CG2 VAL A 431     233.222 247.597 194.655  1.00122.99           C  
ATOM    779  N   LEU A 432     233.471 246.045 197.413  1.00123.39           N  
ATOM    780  CA  LEU A 432     232.670 245.776 198.600  1.00123.39           C  
ATOM    781  C   LEU A 432     233.552 245.380 199.771  1.00123.39           C  
ATOM    782  O   LEU A 432     233.334 245.825 200.901  1.00123.39           O  
ATOM    783  CB  LEU A 432     231.648 244.682 198.317  1.00123.39           C  
ATOM    784  CG  LEU A 432     230.852 244.276 199.555  1.00123.39           C  
ATOM    785  CD1 LEU A 432     229.825 245.344 199.893  1.00123.39           C  
ATOM    786  CD2 LEU A 432     230.187 242.929 199.358  1.00123.39           C  
ATOM    787  N   LEU A 433     234.563 244.553 199.518  1.00122.50           N  
ATOM    788  CA  LEU A 433     235.501 244.198 200.569  1.00122.50           C  
ATOM    789  C   LEU A 433     236.175 245.435 201.133  1.00122.50           C  
ATOM    790  O   LEU A 433     236.278 245.590 202.354  1.00122.50           O  
ATOM    791  CB  LEU A 433     236.545 243.229 200.032  1.00122.50           C  
ATOM    792  CG  LEU A 433     237.556 242.787 201.079  1.00122.50           C  
ATOM    793  CD1 LEU A 433     236.994 241.613 201.856  1.00122.50           C  
ATOM    794  CD2 LEU A 433     238.876 242.434 200.427  1.00122.50           C  
ATOM    795  N   GLN A 434     236.631 246.338 200.260  1.00121.64           N  
ATOM    796  CA  GLN A 434     237.277 247.543 200.774  1.00121.64           C  
ATOM    797  C   GLN A 434     236.308 248.455 201.512  1.00121.64           C  
ATOM    798  O   GLN A 434     236.739 249.256 202.348  1.00121.64           O  
ATOM    799  CB  GLN A 434     237.964 248.325 199.663  1.00121.64           C  
ATOM    800  CG  GLN A 434     239.144 247.623 199.069  1.00121.64           C  
ATOM    801  CD  GLN A 434     240.215 248.605 198.663  1.00121.64           C  
ATOM    802  OE1 GLN A 434     240.354 249.668 199.267  1.00121.64           O  
ATOM    803  NE2 GLN A 434     240.987 248.255 197.651  1.00121.64           N  
ATOM    804  N   ILE A 435     235.011 248.355 201.237  1.00124.11           N  
ATOM    805  CA  ILE A 435     234.060 249.252 201.884  1.00124.11           C  
ATOM    806  C   ILE A 435     233.456 248.580 203.112  1.00124.11           C  
ATOM    807  O   ILE A 435     232.494 249.081 203.703  1.00124.11           O  
ATOM    808  CB  ILE A 435     232.976 249.719 200.893  1.00124.11           C  
ATOM    809  CG1 ILE A 435     232.341 251.025 201.368  1.00124.11           C  
ATOM    810  CG2 ILE A 435     231.928 248.656 200.684  1.00124.11           C  
ATOM    811  CD1 ILE A 435     233.344 252.128 201.601  1.00124.11           C  
ATOM    812  N   ASN A 436     234.027 247.453 203.526  1.00123.07           N  
ATOM    813  CA  ASN A 436     233.619 246.795 204.758  1.00123.07           C  
ATOM    814  C   ASN A 436     234.841 246.424 205.578  1.00123.07           C  
ATOM    815  O   ASN A 436     235.985 246.547 205.135  1.00123.07           O  
ATOM    816  CB  ASN A 436     232.779 245.536 204.508  1.00123.07           C  
ATOM    817  CG  ASN A 436     231.473 245.835 203.824  1.00123.07           C  
ATOM    818  OD1 ASN A 436     231.324 245.630 202.626  1.00123.07           O  
ATOM    819  ND2 ASN A 436     230.519 246.350 204.583  1.00123.07           N  
ATOM    820  N   SER A 437     234.569 245.958 206.792  1.00120.04           N  
ATOM    821  CA  SER A 437     235.601 245.525 207.722  1.00120.04           C  
ATOM    822  C   SER A 437     235.727 244.012 207.643  1.00120.04           C  
ATOM    823  O   SER A 437     234.765 243.290 207.919  1.00120.04           O  
ATOM    824  CB  SER A 437     235.261 245.971 209.141  1.00120.04           C  
ATOM    825  OG  SER A 437     234.844 247.324 209.148  1.00120.04           O  
ATOM    826  N   LEU A 438     236.908 243.536 207.271  1.00114.38           N  
ATOM    827  CA  LEU A 438     237.112 242.121 206.979  1.00114.38           C  
ATOM    828  C   LEU A 438     237.221 241.379 208.306  1.00114.38           C  
ATOM    829  O   LEU A 438     238.308 241.192 208.854  1.00114.38           O  
ATOM    830  CB  LEU A 438     238.356 241.935 206.124  1.00114.38           C  
ATOM    831  CG  LEU A 438     238.682 240.514 205.696  1.00114.38           C  
ATOM    832  CD1 LEU A 438     237.451 239.959 205.037  1.00114.38           C  
ATOM    833  CD2 LEU A 438     239.853 240.489 204.741  1.00114.38           C  
ATOM    834  N   SER A 439     236.077 240.940 208.827  1.00103.16           N  
ATOM    835  CA  SER A 439     236.000 240.358 210.160  1.00103.16           C  
ATOM    836  C   SER A 439     235.123 239.111 210.102  1.00103.16           C  
ATOM    837  O   SER A 439     234.778 238.622 209.025  1.00103.16           O  
ATOM    838  CB  SER A 439     235.478 241.398 211.156  1.00103.16           C  
ATOM    839  OG  SER A 439     234.252 241.947 210.712  1.00103.16           O  
ATOM    840  N   TYR A 440     234.771 238.580 211.274  1.00 91.66           N  
ATOM    841  CA  TYR A 440     233.979 237.354 211.321  1.00 91.66           C  
ATOM    842  C   TYR A 440     232.544 237.590 210.875  1.00 91.66           C  
ATOM    843  O   TYR A 440     231.947 236.735 210.207  1.00 91.66           O  
ATOM    844  CB  TYR A 440     233.988 236.766 212.727  1.00 91.66           C  
ATOM    845  CG  TYR A 440     232.830 235.835 212.974  1.00 91.66           C  
ATOM    846  CD1 TYR A 440     232.833 234.552 212.465  1.00 91.66           C  
ATOM    847  CD2 TYR A 440     231.724 236.247 213.695  1.00 91.66           C  
ATOM    848  CE1 TYR A 440     231.778 233.705 212.678  1.00 91.66           C  
ATOM    849  CE2 TYR A 440     230.661 235.407 213.907  1.00 91.66           C  
ATOM    850  CZ  TYR A 440     230.694 234.138 213.398  1.00 91.66           C  
ATOM    851  OH  TYR A 440     229.638 233.291 213.611  1.00 91.66           O  
ATOM    852  N   SER A 441     231.960 238.726 211.259  1.00102.42           N  
ATOM    853  CA  SER A 441     230.567 238.988 210.920  1.00102.42           C  
ATOM    854  C   SER A 441     230.392 239.161 209.421  1.00102.42           C  
ATOM    855  O   SER A 441     229.277 239.047 208.901  1.00102.42           O  
ATOM    856  CB  SER A 441     230.069 240.223 211.656  1.00102.42           C  
ATOM    857  OG  SER A 441     228.735 240.509 211.292  1.00102.42           O  
ATOM    858  N   PHE A 442     231.481 239.458 208.710  1.00113.83           N  
ATOM    859  CA  PHE A 442     231.424 239.518 207.258  1.00113.83           C  
ATOM    860  C   PHE A 442     231.806 238.194 206.615  1.00113.83           C  
ATOM    861  O   PHE A 442     231.382 237.914 205.491  1.00113.83           O  
ATOM    862  CB  PHE A 442     232.320 240.629 206.736  1.00113.83           C  
ATOM    863  CG  PHE A 442     231.997 241.032 205.342  1.00113.83           C  
ATOM    864  CD1 PHE A 442     230.689 240.990 204.893  1.00113.83           C  
ATOM    865  CD2 PHE A 442     232.992 241.424 204.468  1.00113.83           C  
ATOM    866  CE1 PHE A 442     230.373 241.344 203.605  1.00113.83           C  
ATOM    867  CE2 PHE A 442     232.688 241.782 203.174  1.00113.83           C  
ATOM    868  CZ  PHE A 442     231.374 241.741 202.739  1.00113.83           C  
ATOM    869  N   TYR A 443     232.615 237.381 207.291  1.00110.93           N  
ATOM    870  CA  TYR A 443     232.836 236.016 206.830  1.00110.93           C  
ATOM    871  C   TYR A 443     231.539 235.228 206.842  1.00110.93           C  
ATOM    872  O   TYR A 443     231.280 234.426 205.938  1.00110.93           O  
ATOM    873  CB  TYR A 443     233.865 235.318 207.711  1.00110.93           C  
ATOM    874  CG  TYR A 443     235.295 235.686 207.440  1.00110.93           C  
ATOM    875  CD1 TYR A 443     235.624 236.715 206.583  1.00110.93           C  
ATOM    876  CD2 TYR A 443     236.321 235.028 208.089  1.00110.93           C  
ATOM    877  CE1 TYR A 443     236.940 237.046 206.353  1.00110.93           C  
ATOM    878  CE2 TYR A 443     237.640 235.357 207.872  1.00110.93           C  
ATOM    879  CZ  TYR A 443     237.945 236.368 207.004  1.00110.93           C  
ATOM    880  OH  TYR A 443     239.259 236.699 206.780  1.00110.93           O  
ATOM    881  N   ASN A 444     230.722 235.427 207.864  1.00117.14           N  
ATOM    882  CA  ASN A 444     229.493 234.665 207.992  1.00117.14           C  
ATOM    883  C   ASN A 444     228.312 235.399 207.368  1.00117.14           C  
ATOM    884  O   ASN A 444     227.173 234.938 207.478  1.00117.14           O  
ATOM    885  CB  ASN A 444     229.240 234.353 209.474  1.00117.14           C  
ATOM    886  CG  ASN A 444     228.171 233.295 209.691  1.00117.14           C  
ATOM    887  OD1 ASN A 444     227.592 232.761 208.747  1.00117.14           O  
ATOM    888  ND2 ASN A 444     227.919 232.975 210.950  1.00117.14           N  
ATOM    889  N   HIS A 445     228.548 236.536 206.723  1.00122.21           N  
ATOM    890  CA  HIS A 445     227.493 237.176 205.949  1.00122.21           C  
ATOM    891  C   HIS A 445     227.291 236.435 204.637  1.00122.21           C  
ATOM    892  O   HIS A 445     228.254 236.125 203.931  1.00122.21           O  
ATOM    893  CB  HIS A 445     227.825 238.638 205.680  1.00122.21           C  
ATOM    894  CG  HIS A 445     226.663 239.427 205.166  1.00122.21           C  
ATOM    895  ND1 HIS A 445     226.694 240.104 203.967  1.00122.21           N  
ATOM    896  CD2 HIS A 445     225.428 239.630 205.681  1.00122.21           C  
ATOM    897  CE1 HIS A 445     225.533 240.702 203.771  1.00122.21           C  
ATOM    898  NE2 HIS A 445     224.747 240.431 204.797  1.00122.21           N  
ATOM    899  N   SER A 446     226.033 236.157 204.307  1.00123.31           N  
ATOM    900  CA  SER A 446     225.745 235.335 203.138  1.00123.31           C  
ATOM    901  C   SER A 446     226.196 235.998 201.846  1.00123.31           C  
ATOM    902  O   SER A 446     226.637 235.310 200.921  1.00123.31           O  
ATOM    903  CB  SER A 446     224.254 235.023 203.084  1.00123.31           C  
ATOM    904  OG  SER A 446     223.817 234.464 204.310  1.00123.31           O  
ATOM    905  N   LEU A 447     226.099 237.323 201.760  1.00121.25           N  
ATOM    906  CA  LEU A 447     226.419 238.001 200.511  1.00121.25           C  
ATOM    907  C   LEU A 447     227.904 237.923 200.192  1.00121.25           C  
ATOM    908  O   LEU A 447     228.280 237.884 199.019  1.00121.25           O  
ATOM    909  CB  LEU A 447     225.942 239.450 200.579  1.00121.25           C  
ATOM    910  CG  LEU A 447     225.981 240.284 199.306  1.00121.25           C  
ATOM    911  CD1 LEU A 447     224.911 241.347 199.379  1.00121.25           C  
ATOM    912  CD2 LEU A 447     227.324 240.933 199.158  1.00121.25           C  
ATOM    913  N   PHE A 448     228.756 237.888 201.212  1.00119.15           N  
ATOM    914  CA  PHE A 448     230.184 237.704 200.979  1.00119.15           C  
ATOM    915  C   PHE A 448     230.459 236.378 200.276  1.00119.15           C  
ATOM    916  O   PHE A 448     231.151 236.330 199.250  1.00119.15           O  
ATOM    917  CB  PHE A 448     230.919 237.790 202.317  1.00119.15           C  
ATOM    918  CG  PHE A 448     232.314 237.254 202.290  1.00119.15           C  
ATOM    919  CD1 PHE A 448     233.288 237.855 201.522  1.00119.15           C  
ATOM    920  CD2 PHE A 448     232.658 236.166 203.061  1.00119.15           C  
ATOM    921  CE1 PHE A 448     234.571 237.368 201.510  1.00119.15           C  
ATOM    922  CE2 PHE A 448     233.943 235.677 203.048  1.00119.15           C  
ATOM    923  CZ  PHE A 448     234.897 236.282 202.277  1.00119.15           C  
ATOM    924  N   ARG A 449     229.891 235.291 200.798  1.00115.75           N  
ATOM    925  CA  ARG A 449     230.047 233.989 200.160  1.00115.75           C  
ATOM    926  C   ARG A 449     229.432 233.972 198.767  1.00115.75           C  
ATOM    927  O   ARG A 449     230.030 233.442 197.825  1.00115.75           O  
ATOM    928  CB  ARG A 449     229.424 232.909 201.041  1.00115.75           C  
ATOM    929  CG  ARG A 449     230.423 232.201 201.937  1.00115.75           C  
ATOM    930  CD  ARG A 449     229.762 231.128 202.777  1.00115.75           C  
ATOM    931  NE  ARG A 449     228.719 231.656 203.645  1.00115.75           N  
ATOM    932  CZ  ARG A 449     228.401 231.132 204.823  1.00115.75           C  
ATOM    933  NH1 ARG A 449     229.036 230.052 205.255  1.00115.75           N  
ATOM    934  NH2 ARG A 449     227.444 231.672 205.563  1.00115.75           N  
ATOM    935  N   ILE A 450     228.241 234.553 198.612  1.00118.48           N  
ATOM    936  CA  ILE A 450     227.589 234.561 197.306  1.00118.48           C  
ATOM    937  C   ILE A 450     228.464 235.263 196.282  1.00118.48           C  
ATOM    938  O   ILE A 450     228.605 234.808 195.144  1.00118.48           O  
ATOM    939  CB  ILE A 450     226.200 235.212 197.402  1.00118.48           C  
ATOM    940  CG1 ILE A 450     225.191 234.217 197.973  1.00118.48           C  
ATOM    941  CG2 ILE A 450     225.755 235.695 196.046  1.00118.48           C  
ATOM    942  CD1 ILE A 450     223.855 234.826 198.339  1.00118.48           C  
ATOM    943  N   LEU A 451     229.068 236.382 196.665  1.00118.84           N  
ATOM    944  CA  LEU A 451     230.005 237.023 195.763  1.00118.84           C  
ATOM    945  C   LEU A 451     231.250 236.179 195.561  1.00118.84           C  
ATOM    946  O   LEU A 451     231.921 236.322 194.536  1.00118.84           O  
ATOM    947  CB  LEU A 451     230.371 238.407 196.292  1.00118.84           C  
ATOM    948  CG  LEU A 451     229.501 239.579 195.822  1.00118.84           C  
ATOM    949  CD1 LEU A 451     229.752 239.881 194.360  1.00118.84           C  
ATOM    950  CD2 LEU A 451     228.025 239.326 196.051  1.00118.84           C  
ATOM    951  N   LYS A 452     231.568 235.293 196.504  1.00116.06           N  
ATOM    952  CA  LYS A 452     232.758 234.464 196.346  1.00116.06           C  
ATOM    953  C   LYS A 452     232.560 233.314 195.366  1.00116.06           C  
ATOM    954  O   LYS A 452     233.516 232.933 194.684  1.00116.06           O  
ATOM    955  CB  LYS A 452     233.215 233.910 197.693  1.00116.06           C  
ATOM    956  CG  LYS A 452     234.528 233.174 197.601  1.00116.06           C  
ATOM    957  CD  LYS A 452     235.053 232.775 198.954  1.00116.06           C  
ATOM    958  CE  LYS A 452     235.955 233.841 199.521  1.00116.06           C  
ATOM    959  NZ  LYS A 452     236.018 233.754 200.998  1.00116.06           N  
ATOM    960  N   VAL A 453     231.360 232.734 195.281  1.00114.92           N  
ATOM    961  CA  VAL A 453     231.173 231.612 194.364  1.00114.92           C  
ATOM    962  C   VAL A 453     231.382 232.058 192.928  1.00114.92           C  
ATOM    963  O   VAL A 453     231.918 231.312 192.104  1.00114.92           O  
ATOM    964  CB  VAL A 453     229.791 230.965 194.536  1.00114.92           C  
ATOM    965  CG1 VAL A 453     228.696 231.943 194.230  1.00114.92           C  
ATOM    966  CG2 VAL A 453     229.663 229.773 193.621  1.00114.92           C  
ATOM    967  N   PHE A 454     230.966 233.277 192.599  1.00121.72           N  
ATOM    968  CA  PHE A 454     231.110 233.729 191.226  1.00121.72           C  
ATOM    969  C   PHE A 454     232.572 233.770 190.827  1.00121.72           C  
ATOM    970  O   PHE A 454     232.896 233.617 189.646  1.00121.72           O  
ATOM    971  CB  PHE A 454     230.429 235.081 191.062  1.00121.72           C  
ATOM    972  CG  PHE A 454     228.930 234.995 191.119  1.00121.72           C  
ATOM    973  CD1 PHE A 454     228.299 233.764 191.113  1.00121.72           C  
ATOM    974  CD2 PHE A 454     228.156 236.132 191.210  1.00121.72           C  
ATOM    975  CE1 PHE A 454     226.932 233.671 191.171  1.00121.72           C  
ATOM    976  CE2 PHE A 454     226.786 236.044 191.272  1.00121.72           C  
ATOM    977  CZ  PHE A 454     226.174 234.813 191.251  1.00121.72           C  
ATOM    978  N   LYS A 455     233.467 233.925 191.804  1.00118.95           N  
ATOM    979  CA  LYS A 455     234.885 233.705 191.551  1.00118.95           C  
ATOM    980  C   LYS A 455     235.143 232.274 191.103  1.00118.95           C  
ATOM    981  O   LYS A 455     235.981 232.030 190.234  1.00118.95           O  
ATOM    982  CB  LYS A 455     235.702 234.035 192.799  1.00118.95           C  
ATOM    983  CG  LYS A 455     237.099 233.423 192.823  1.00118.95           C  
ATOM    984  CD  LYS A 455     237.961 234.067 193.892  1.00118.95           C  
ATOM    985  CE  LYS A 455     237.339 233.894 195.261  1.00118.95           C  
ATOM    986  NZ  LYS A 455     238.113 234.599 196.317  1.00118.95           N  
ATOM    987  N   SER A 456     234.350 231.345 191.638  1.00114.88           N  
ATOM    988  CA  SER A 456     234.486 229.926 191.231  1.00114.88           C  
ATOM    989  C   SER A 456     234.223 229.852 189.724  1.00114.88           C  
ATOM    990  O   SER A 456     234.775 228.946 189.069  1.00114.88           O  
ATOM    991  CB  SER A 456     233.555 229.030 192.006  1.00114.88           C  
ATOM    992  OG  SER A 456     233.828 229.103 193.398  1.00114.88           O  
ATOM    993  N   MET A 457     233.383 230.760 189.212  1.00122.79           N  
ATOM    994  CA  MET A 457     233.061 230.769 187.792  1.00122.79           C  
ATOM    995  C   MET A 457     234.292 230.947 186.920  1.00122.79           C  
ATOM    996  O   MET A 457     234.258 230.564 185.749  1.00122.79           O  
ATOM    997  CB  MET A 457     232.048 231.866 187.484  1.00122.79           C  
ATOM    998  CG  MET A 457     230.757 231.726 188.248  1.00122.79           C  
ATOM    999  SD  MET A 457     229.589 230.620 187.450  1.00122.79           S  
ATOM   1000  CE  MET A 457     228.329 231.793 186.987  1.00122.79           C  
ATOM   1001  N   ARG A 458     235.376 231.523 187.450  1.00125.11           N  
ATOM   1002  CA  ARG A 458     236.599 231.611 186.660  1.00125.11           C  
ATOM   1003  C   ARG A 458     237.054 230.243 186.183  1.00125.11           C  
ATOM   1004  O   ARG A 458     237.604 230.125 185.084  1.00125.11           O  
ATOM   1005  CB  ARG A 458     237.720 232.295 187.449  1.00125.11           C  
ATOM   1006  CG  ARG A 458     237.394 233.685 187.969  1.00125.11           C  
ATOM   1007  CD  ARG A 458     237.964 233.899 189.357  1.00125.11           C  
ATOM   1008  NE  ARG A 458     238.084 235.301 189.725  1.00125.11           N  
ATOM   1009  CZ  ARG A 458     239.217 235.985 189.666  1.00125.11           C  
ATOM   1010  NH1 ARG A 458     240.333 235.380 189.287  1.00125.11           N  
ATOM   1011  NH2 ARG A 458     239.238 237.262 190.017  1.00125.11           N  
ATOM   1012  N   ALA A 459     236.799 229.192 186.963  1.00130.46           N  
ATOM   1013  CA  ALA A 459     237.217 227.866 186.534  1.00130.46           C  
ATOM   1014  C   ALA A 459     236.588 227.471 185.209  1.00130.46           C  
ATOM   1015  O   ALA A 459     237.135 226.614 184.511  1.00130.46           O  
ATOM   1016  CB  ALA A 459     236.876 226.829 187.602  1.00130.46           C  
ATOM   1017  N   LEU A 460     235.464 228.088 184.839  1.00138.09           N  
ATOM   1018  CA  LEU A 460     234.846 227.783 183.554  1.00138.09           C  
ATOM   1019  C   LEU A 460     235.782 228.111 182.399  1.00138.09           C  
ATOM   1020  O   LEU A 460     235.828 227.385 181.401  1.00138.09           O  
ATOM   1021  CB  LEU A 460     233.528 228.541 183.397  1.00138.09           C  
ATOM   1022  CG  LEU A 460     232.254 227.932 183.981  1.00138.09           C  
ATOM   1023  CD1 LEU A 460     232.186 228.138 185.469  1.00138.09           C  
ATOM   1024  CD2 LEU A 460     231.039 228.532 183.319  1.00138.09           C  
ATOM   1025  N   ARG A 461     236.579 229.165 182.565  1.00147.78           N  
ATOM   1026  CA  ARG A 461     237.520 229.558 181.487  1.00147.78           C  
ATOM   1027  C   ARG A 461     238.435 228.361 181.214  1.00147.78           C  
ATOM   1028  O   ARG A 461     238.898 228.219 180.065  1.00147.78           O  
ATOM   1029  CB  ARG A 461     238.329 230.789 181.906  1.00147.78           C  
ATOM   1030  CG  ARG A 461     239.652 230.944 181.170  1.00147.78           C  
ATOM   1031  CD  ARG A 461     239.533 231.836 179.948  1.00147.78           C  
ATOM   1032  NE  ARG A 461     238.556 232.900 180.132  1.00147.78           N  
ATOM   1033  CZ  ARG A 461     237.508 233.104 179.342  1.00147.78           C  
ATOM   1034  NH1 ARG A 461     237.297 232.312 178.304  1.00147.78           N  
ATOM   1035  NH2 ARG A 461     236.675 234.098 179.591  1.00147.78           N  
ATOM   1036  N   ALA A 462     238.688 227.544 182.242  1.00150.96           N  
ATOM   1037  CA  ALA A 462     239.578 226.397 182.096  1.00150.96           C  
ATOM   1038  C   ALA A 462     239.142 225.477 180.965  1.00150.96           C  
ATOM   1039  O   ALA A 462     239.994 224.889 180.290  1.00150.96           O  
ATOM   1040  CB  ALA A 462     239.650 225.617 183.407  1.00150.96           C  
ATOM   1041  N   ILE A 463     237.834 225.355 180.720  1.00155.32           N  
ATOM   1042  CA  ILE A 463     237.401 224.524 179.600  1.00155.32           C  
ATOM   1043  C   ILE A 463     238.012 225.001 178.290  1.00155.32           C  
ATOM   1044  O   ILE A 463     238.430 224.177 177.465  1.00155.32           O  
ATOM   1045  CB  ILE A 463     235.861 224.432 179.504  1.00155.32           C  
ATOM   1046  CG1 ILE A 463     235.253 223.740 180.730  1.00155.32           C  
ATOM   1047  CG2 ILE A 463     235.450 223.733 178.228  1.00155.32           C  
ATOM   1048  CD1 ILE A 463     234.902 224.612 181.886  1.00155.32           C  
ATOM   1049  N   ARG A 464     238.163 226.322 178.139  1.00161.37           N  
ATOM   1050  CA  ARG A 464     238.766 226.879 176.897  1.00161.37           C  
ATOM   1051  C   ARG A 464     240.174 226.291 176.746  1.00161.37           C  
ATOM   1052  O   ARG A 464     240.520 225.875 175.622  1.00161.37           O  
ATOM   1053  CB  ARG A 464     238.821 228.407 176.981  1.00161.37           C  
ATOM   1054  CG  ARG A 464     239.423 229.076 175.754  1.00161.37           C  
ATOM   1055  CD  ARG A 464     239.454 230.588 175.877  1.00161.37           C  
ATOM   1056  NE  ARG A 464     240.028 231.229 174.702  1.00161.37           N  
ATOM   1057  CZ  ARG A 464     240.170 232.541 174.555  1.00161.37           C  
ATOM   1058  NH1 ARG A 464     240.705 233.029 173.448  1.00161.37           N  
ATOM   1059  NH2 ARG A 464     239.776 233.361 175.513  1.00161.37           N  
ATOM   1060  N   VAL A 465     240.934 226.224 177.844  1.00165.07           N  
ATOM   1061  CA  VAL A 465     242.259 225.613 177.831  1.00165.07           C  
ATOM   1062  C   VAL A 465     242.148 224.149 177.447  1.00165.07           C  
ATOM   1063  O   VAL A 465     242.891 223.649 176.594  1.00165.07           O  
ATOM   1064  CB  VAL A 465     242.937 225.770 179.202  1.00165.07           C  
ATOM   1065  CG1 VAL A 465     244.275 225.047 179.218  1.00165.07           C  
ATOM   1066  CG2 VAL A 465     243.080 227.228 179.561  1.00165.07           C  
ATOM   1067  N   LEU A 466     241.193 223.447 178.056  1.00165.71           N  
ATOM   1068  CA  LEU A 466     241.024 222.029 177.774  1.00165.71           C  
ATOM   1069  C   LEU A 466     240.646 221.810 176.320  1.00165.71           C  
ATOM   1070  O   LEU A 466     240.994 220.780 175.733  1.00165.71           O  
ATOM   1071  CB  LEU A 466     239.977 221.431 178.708  1.00165.71           C  
ATOM   1072  CG  LEU A 466     240.515 220.819 180.004  1.00165.71           C  
ATOM   1073  CD1 LEU A 466     241.179 221.870 180.879  1.00165.71           C  
ATOM   1074  CD2 LEU A 466     239.410 220.125 180.767  1.00165.71           C  
ATOM   1075  N   ARG A 467     239.967 222.796 175.737  1.00164.17           N  
ATOM   1076  CA  ARG A 467     239.588 222.705 174.305  1.00164.17           C  
ATOM   1077  C   ARG A 467     240.829 222.732 173.401  1.00164.17           C  
ATOM   1078  O   ARG A 467     240.872 221.910 172.469  1.00164.17           O  
ATOM   1079  CB  ARG A 467     238.648 223.852 173.927  1.00164.17           C  
ATOM   1080  CG  ARG A 467     237.296 223.807 174.624  1.00164.17           C  
ATOM   1081  CD  ARG A 467     236.231 224.473 173.774  1.00164.17           C  
ATOM   1082  NE  ARG A 467     236.255 223.914 172.435  1.00164.17           N  
ATOM   1083  CZ  ARG A 467     235.611 224.418 171.396  1.00164.17           C  
ATOM   1084  NH1 ARG A 467     234.888 225.515 171.534  1.00164.17           N  
ATOM   1085  NH2 ARG A 467     235.692 223.825 170.219  1.00164.17           N  
ATOM   1086  N   ARG A 468     241.805 223.611 173.665  1.00175.49           N  
ATOM   1087  CA  ARG A 468     242.977 223.710 172.744  1.00175.49           C  
ATOM   1088  C   ARG A 468     243.864 222.473 172.871  1.00175.49           C  
ATOM   1089  O   ARG A 468     244.230 221.899 171.831  1.00175.49           O  
ATOM   1090  CB  ARG A 468     243.746 225.017 172.958  1.00175.49           C  
ATOM   1091  CG  ARG A 468     245.219 224.964 172.573  1.00175.49           C  
ATOM   1092  CD  ARG A 468     245.548 224.439 171.189  1.00175.49           C  
ATOM   1093  NE  ARG A 468     246.766 225.031 170.634  1.00175.49           N  
ATOM   1094  CZ  ARG A 468     247.989 224.496 170.673  1.00175.49           C  
ATOM   1095  NH1 ARG A 468     248.198 223.327 171.256  1.00175.49           N  
ATOM   1096  NH2 ARG A 468     249.007 225.137 170.126  1.00175.49           N  
ATOM   1097  N   LEU A 469     244.135 222.067 174.108  1.00178.53           N  
ATOM   1098  CA  LEU A 469     244.954 220.869 174.400  1.00178.53           C  
ATOM   1099  C   LEU A 469     244.195 219.701 173.773  1.00178.53           C  
ATOM   1100  O   LEU A 469     244.840 218.813 173.190  1.00178.53           O  
ATOM   1101  CB  LEU A 469     244.972 220.745 175.926  1.00178.53           C  
ATOM   1102  CG  LEU A 469     245.938 219.732 176.531  1.00178.53           C  
ATOM   1103  CD1 LEU A 469     245.772 219.697 178.039  1.00178.53           C  
ATOM   1104  CD2 LEU A 469     245.730 218.350 175.940  1.00178.53           C  
ATOM   1105  N   SER A 470     242.862 219.772 173.895  1.00173.03           N  
ATOM   1106  CA  SER A 470     241.850 218.794 173.417  1.00173.03           C  
ATOM   1107  C   SER A 470     241.252 218.035 174.604  1.00173.03           C  
ATOM   1108  O   SER A 470     241.981 217.720 175.560  1.00173.03           O  
ATOM   1109  CB  SER A 470     242.446 217.824 172.434  1.00173.03           C  
ATOM   1110  OG  SER A 470     243.079 216.742 173.109  1.00173.03           O  
ATOM   1111  N   ILE A 471     239.964 217.725 174.480  1.00161.23           N  
ATOM   1112  CA  ILE A 471     239.160 216.937 175.453  1.00161.23           C  
ATOM   1113  C   ILE A 471     239.156 215.542 174.842  1.00161.23           C  
ATOM   1114  O   ILE A 471     238.535 214.615 175.401  1.00161.23           O  
ATOM   1115  CB  ILE A 471     237.738 217.534 175.445  1.00161.23           C  
ATOM   1116  CG1 ILE A 471     237.643 218.805 176.288  1.00161.23           C  
ATOM   1117  CG2 ILE A 471     236.681 216.522 175.846  1.00161.23           C  
ATOM   1118  CD1 ILE A 471     238.179 218.642 177.685  1.00161.23           C  
ATOM   1119  N   LEU A 472     239.858 215.450 173.711  1.00159.85           N  
ATOM   1120  CA  LEU A 472     239.816 214.295 172.815  1.00159.85           C  
ATOM   1121  C   LEU A 472     238.528 214.266 172.014  1.00159.85           C  
ATOM   1122  O   LEU A 472     238.342 213.340 171.216  1.00159.85           O  
ATOM   1123  CB  LEU A 472     239.972 212.937 173.522  1.00159.85           C  
ATOM   1124  CG  LEU A 472     241.360 212.456 173.944  1.00159.85           C  
ATOM   1125  CD1 LEU A 472     241.760 213.031 175.289  1.00159.85           C  
ATOM   1126  CD2 LEU A 472     241.408 210.935 173.960  1.00159.85           C  
ATOM   1127  N   THR A 473     237.637 215.242 172.187  1.00152.34           N  
ATOM   1128  CA  THR A 473     236.329 215.248 171.528  1.00152.34           C  
ATOM   1129  C   THR A 473     235.598 213.928 171.743  1.00152.34           C  
ATOM   1130  O   THR A 473     234.676 213.583 171.004  1.00152.34           O  
ATOM   1131  CB  THR A 473     236.442 215.566 170.032  1.00152.34           C  
ATOM   1132  OG1 THR A 473     237.534 214.848 169.444  1.00152.34           O  
ATOM   1133  CG2 THR A 473     236.622 217.062 169.817  1.00152.34           C  
ATOM   1134  N   SER A 474     236.014 213.176 172.763  1.00143.91           N  
ATOM   1135  CA  SER A 474     235.364 211.907 173.047  1.00143.91           C  
ATOM   1136  C   SER A 474     233.882 212.112 173.301  1.00143.91           C  
ATOM   1137  O   SER A 474     233.064 211.236 172.997  1.00143.91           O  
ATOM   1138  CB  SER A 474     236.032 211.241 174.247  1.00143.91           C  
ATOM   1139  OG  SER A 474     237.423 211.093 174.035  1.00143.91           O  
ATOM   1140  N   LEU A 475     233.525 213.270 173.844  1.00138.79           N  
ATOM   1141  CA  LEU A 475     232.142 213.677 174.025  1.00138.79           C  
ATOM   1142  C   LEU A 475     231.737 214.778 173.050  1.00138.79           C  
ATOM   1143  O   LEU A 475     230.781 215.512 173.309  1.00138.79           O  
ATOM   1144  CB  LEU A 475     231.918 214.089 175.482  1.00138.79           C  
ATOM   1145  CG  LEU A 475     232.505 215.396 176.011  1.00138.79           C  
ATOM   1146  CD1 LEU A 475     231.855 215.751 177.301  1.00138.79           C  
ATOM   1147  CD2 LEU A 475     233.981 215.235 176.252  1.00138.79           C  
ATOM   1148  N   HIS A 476     232.450 214.901 171.925  1.00137.72           N  
ATOM   1149  CA  HIS A 476     232.009 215.785 170.849  1.00137.72           C  
ATOM   1150  C   HIS A 476     230.694 215.309 170.252  1.00137.72           C  
ATOM   1151  O   HIS A 476     229.821 216.121 169.932  1.00137.72           O  
ATOM   1152  CB  HIS A 476     233.081 215.855 169.765  1.00137.72           C  
ATOM   1153  CG  HIS A 476     232.760 216.782 168.633  1.00137.72           C  
ATOM   1154  ND1 HIS A 476     233.419 216.726 167.423  1.00137.72           N  
ATOM   1155  CD2 HIS A 476     231.868 217.795 168.529  1.00137.72           C  
ATOM   1156  CE1 HIS A 476     232.940 217.658 166.619  1.00137.72           C  
ATOM   1157  NE2 HIS A 476     231.998 218.321 167.266  1.00137.72           N  
ATOM   1158  N   GLU A 477     230.536 213.997 170.096  1.00137.24           N  
ATOM   1159  CA  GLU A 477     229.335 213.452 169.475  1.00137.24           C  
ATOM   1160  C   GLU A 477     228.126 213.593 170.391  1.00137.24           C  
ATOM   1161  O   GLU A 477     227.050 214.028 169.958  1.00137.24           O  
ATOM   1162  CB  GLU A 477     229.568 211.988 169.109  1.00137.24           C  
ATOM   1163  CG  GLU A 477     230.858 211.730 168.333  1.00137.24           C  
ATOM   1164  CD  GLU A 477     232.102 211.693 169.211  1.00137.24           C  
ATOM   1165  OE1 GLU A 477     232.076 212.264 170.321  1.00137.24           O  
ATOM   1166  OE2 GLU A 477     233.112 211.095 168.786  1.00137.24           O  
ATOM   1167  N   VAL A 478     228.284 213.226 171.664  1.00128.68           N  
ATOM   1168  CA  VAL A 478     227.185 213.348 172.615  1.00128.68           C  
ATOM   1169  C   VAL A 478     226.788 214.807 172.770  1.00128.68           C  
ATOM   1170  O   VAL A 478     225.599 215.146 172.805  1.00128.68           O  
ATOM   1171  CB  VAL A 478     227.572 212.717 173.965  1.00128.68           C  
ATOM   1172  CG1 VAL A 478     226.433 212.824 174.939  1.00128.68           C  
ATOM   1173  CG2 VAL A 478     227.959 211.264 173.779  1.00128.68           C  
ATOM   1174  N   ALA A 479     227.779 215.694 172.859  1.00128.49           N  
ATOM   1175  CA  ALA A 479     227.491 217.118 172.951  1.00128.49           C  
ATOM   1176  C   ALA A 479     226.783 217.620 171.701  1.00128.49           C  
ATOM   1177  O   ALA A 479     225.842 218.415 171.791  1.00128.49           O  
ATOM   1178  CB  ALA A 479     228.780 217.899 173.185  1.00128.49           C  
ATOM   1179  N   GLY A 480     227.215 217.166 170.525  1.00125.63           N  
ATOM   1180  CA  GLY A 480     226.557 217.587 169.301  1.00125.63           C  
ATOM   1181  C   GLY A 480     225.105 217.161 169.253  1.00125.63           C  
ATOM   1182  O   GLY A 480     224.232 217.926 168.831  1.00125.63           O  
ATOM   1183  N   THR A 481     224.818 215.942 169.709  1.00119.14           N  
ATOM   1184  CA  THR A 481     223.440 215.474 169.637  1.00119.14           C  
ATOM   1185  C   THR A 481     222.565 216.117 170.708  1.00119.14           C  
ATOM   1186  O   THR A 481     221.386 216.387 170.457  1.00119.14           O  
ATOM   1187  CB  THR A 481     223.386 213.958 169.731  1.00119.14           C  
ATOM   1188  OG1 THR A 481     224.387 213.403 168.872  1.00119.14           O  
ATOM   1189  CG2 THR A 481     222.043 213.487 169.232  1.00119.14           C  
ATOM   1190  N   LEU A 482     223.176 216.442 171.848  1.00114.67           N  
ATOM   1191  CA  LEU A 482     222.462 217.197 172.906  1.00114.67           C  
ATOM   1192  C   LEU A 482     222.136 218.574 172.311  1.00114.67           C  
ATOM   1193  O   LEU A 482     221.050 219.112 172.608  1.00114.67           O  
ATOM   1194  CB  LEU A 482     223.372 217.324 174.131  1.00114.67           C  
ATOM   1195  CG  LEU A 482     222.730 216.952 175.467  1.00114.67           C  
ATOM   1196  CD1 LEU A 482     221.363 217.602 175.611  1.00114.67           C  
ATOM   1197  CD2 LEU A 482     222.621 215.442 175.614  1.00114.67           C  
ATOM   1198  N   SER A 483     223.064 219.110 171.504  1.00116.36           N  
ATOM   1199  CA  SER A 483     222.934 220.443 170.858  1.00116.36           C  
ATOM   1200  C   SER A 483     221.736 220.387 169.907  1.00116.36           C  
ATOM   1201  O   SER A 483     220.918 221.328 169.926  1.00116.36           O  
ATOM   1202  CB  SER A 483     224.199 220.805 170.125  1.00116.36           C  
ATOM   1203  OG  SER A 483     224.078 222.079 169.509  1.00116.36           O  
ATOM   1204  N   GLY A 484     221.624 219.296 169.142  1.00110.49           N  
ATOM   1205  CA  GLY A 484     220.478 219.096 168.274  1.00110.49           C  
ATOM   1206  C   GLY A 484     219.174 218.944 169.032  1.00110.49           C  
ATOM   1207  O   GLY A 484     218.123 219.383 168.562  1.00110.49           O  
ATOM   1208  N   SER A 485     219.219 218.322 170.206  1.00108.97           N  
ATOM   1209  CA  SER A 485     217.997 218.030 170.947  1.00108.97           C  
ATOM   1210  C   SER A 485     217.440 219.243 171.684  1.00108.97           C  
ATOM   1211  O   SER A 485     216.225 219.329 171.891  1.00108.97           O  
ATOM   1212  CB  SER A 485     218.253 216.906 171.945  1.00108.97           C  
ATOM   1213  OG  SER A 485     217.036 216.327 172.361  1.00108.97           O  
ATOM   1214  N   LEU A 486     218.301 220.176 172.079  1.00109.81           N  
ATOM   1215  CA  LEU A 486     217.889 221.261 172.969  1.00109.81           C  
ATOM   1216  C   LEU A 486     216.688 222.088 172.514  1.00109.81           C  
ATOM   1217  O   LEU A 486     215.911 222.506 173.388  1.00109.81           O  
ATOM   1218  CB  LEU A 486     219.081 222.191 173.224  1.00109.81           C  
ATOM   1219  CG  LEU A 486     220.138 221.631 174.171  1.00109.81           C  
ATOM   1220  CD1 LEU A 486     221.477 222.211 173.807  1.00109.81           C  
ATOM   1221  CD2 LEU A 486     219.803 221.923 175.620  1.00109.81           C  
ATOM   1222  N   PRO A 487     216.497 222.416 171.229  1.00107.20           N  
ATOM   1223  CA  PRO A 487     215.372 223.305 170.883  1.00107.20           C  
ATOM   1224  C   PRO A 487     214.020 222.812 171.364  1.00107.20           C  
ATOM   1225  O   PRO A 487     213.198 223.617 171.816  1.00107.20           O  
ATOM   1226  CB  PRO A 487     215.438 223.367 169.350  1.00107.20           C  
ATOM   1227  CG  PRO A 487     216.319 222.224 168.943  1.00107.20           C  
ATOM   1228  CD  PRO A 487     217.314 222.125 170.041  1.00107.20           C  
ATOM   1229  N   SER A 488     213.766 221.509 171.291  1.00104.88           N  
ATOM   1230  CA  SER A 488     212.513 220.972 171.805  1.00104.88           C  
ATOM   1231  C   SER A 488     212.579 220.698 173.301  1.00104.88           C  
ATOM   1232  O   SER A 488     211.541 220.701 173.980  1.00104.88           O  
ATOM   1233  CB  SER A 488     212.156 219.700 171.044  1.00104.88           C  
ATOM   1234  OG  SER A 488     213.253 218.811 171.041  1.00104.88           O  
ATOM   1235  N   ILE A 489     213.783 220.448 173.821  1.00104.67           N  
ATOM   1236  CA  ILE A 489     213.949 220.237 175.255  1.00104.67           C  
ATOM   1237  C   ILE A 489     213.516 221.475 176.014  1.00104.67           C  
ATOM   1238  O   ILE A 489     212.793 221.394 177.012  1.00104.67           O  
ATOM   1239  CB  ILE A 489     215.404 219.864 175.579  1.00104.67           C  
ATOM   1240  CG1 ILE A 489     215.709 218.472 175.052  1.00104.67           C  
ATOM   1241  CG2 ILE A 489     215.637 219.906 177.065  1.00104.67           C  
ATOM   1242  CD1 ILE A 489     214.622 217.504 175.351  1.00104.67           C  
ATOM   1243  N   THR A 490     213.943 222.642 175.541  1.00104.94           N  
ATOM   1244  CA  THR A 490     213.535 223.888 176.175  1.00104.94           C  
ATOM   1245  C   THR A 490     212.020 224.027 176.181  1.00104.94           C  
ATOM   1246  O   THR A 490     211.430 224.427 177.191  1.00104.94           O  
ATOM   1247  CB  THR A 490     214.179 225.065 175.449  1.00104.94           C  
ATOM   1248  OG1 THR A 490     213.857 224.996 174.055  1.00104.94           O  
ATOM   1249  CG2 THR A 490     215.689 225.011 175.600  1.00104.94           C  
ATOM   1250  N   ALA A 491     211.371 223.682 175.067  1.00104.73           N  
ATOM   1251  CA  ALA A 491     209.926 223.860 174.953  1.00104.73           C  
ATOM   1252  C   ALA A 491     209.177 222.959 175.921  1.00104.73           C  
ATOM   1253  O   ALA A 491     208.281 223.410 176.647  1.00104.73           O  
ATOM   1254  CB  ALA A 491     209.478 223.585 173.521  1.00104.73           C  
ATOM   1255  N   ILE A 492     209.518 221.671 175.942  1.00100.09           N  
ATOM   1256  CA  ILE A 492     208.807 220.793 176.864  1.00100.09           C  
ATOM   1257  C   ILE A 492     209.146 221.128 178.306  1.00100.09           C  
ATOM   1258  O   ILE A 492     208.298 220.999 179.200  1.00100.09           O  
ATOM   1259  CB  ILE A 492     209.065 219.315 176.545  1.00100.09           C  
ATOM   1260  CG1 ILE A 492     208.072 218.480 177.331  1.00100.09           C  
ATOM   1261  CG2 ILE A 492     210.487 218.925 176.862  1.00100.09           C  
ATOM   1262  CD1 ILE A 492     206.660 218.707 176.897  1.00100.09           C  
ATOM   1263  N   LEU A 493     210.368 221.591 178.557  1.00104.27           N  
ATOM   1264  CA  LEU A 493     210.761 221.962 179.905  1.00104.27           C  
ATOM   1265  C   LEU A 493     209.940 223.145 180.402  1.00104.27           C  
ATOM   1266  O   LEU A 493     209.442 223.138 181.536  1.00104.27           O  
ATOM   1267  CB  LEU A 493     212.259 222.266 179.907  1.00104.27           C  
ATOM   1268  CG  LEU A 493     213.057 222.480 181.185  1.00104.27           C  
ATOM   1269  CD1 LEU A 493     214.455 221.932 180.984  1.00104.27           C  
ATOM   1270  CD2 LEU A 493     213.116 223.951 181.537  1.00104.27           C  
ATOM   1271  N   THR A 494     209.750 224.157 179.556  1.00103.79           N  
ATOM   1272  CA  THR A 494     208.955 225.297 179.987  1.00103.79           C  
ATOM   1273  C   THR A 494     207.477 224.945 180.088  1.00103.79           C  
ATOM   1274  O   THR A 494     206.773 225.486 180.947  1.00103.79           O  
ATOM   1275  CB  THR A 494     209.164 226.487 179.058  1.00103.79           C  
ATOM   1276  OG1 THR A 494     208.506 227.631 179.609  1.00103.79           O  
ATOM   1277  CG2 THR A 494     208.595 226.216 177.692  1.00103.79           C  
ATOM   1278  N   LEU A 495     206.993 224.022 179.257  1.00 98.20           N  
ATOM   1279  CA  LEU A 495     205.611 223.575 179.400  1.00 98.20           C  
ATOM   1280  C   LEU A 495     205.390 222.889 180.748  1.00 98.20           C  
ATOM   1281  O   LEU A 495     204.396 223.153 181.444  1.00 98.20           O  
ATOM   1282  CB  LEU A 495     205.253 222.651 178.239  1.00 98.20           C  
ATOM   1283  CG  LEU A 495     203.828 222.113 178.160  1.00 98.20           C  
ATOM   1284  CD1 LEU A 495     202.862 223.231 177.903  1.00 98.20           C  
ATOM   1285  CD2 LEU A 495     203.722 221.086 177.063  1.00 98.20           C  
ATOM   1286  N   MET A 496     206.318 222.017 181.152  1.00 98.74           N  
ATOM   1287  CA  MET A 496     206.119 221.327 182.423  1.00 98.74           C  
ATOM   1288  C   MET A 496     206.328 222.259 183.607  1.00 98.74           C  
ATOM   1289  O   MET A 496     205.680 222.089 184.644  1.00 98.74           O  
ATOM   1290  CB  MET A 496     207.024 220.103 182.541  1.00 98.74           C  
ATOM   1291  CG  MET A 496     208.475 220.325 182.239  1.00 98.74           C  
ATOM   1292  SD  MET A 496     209.480 219.041 182.992  1.00 98.74           S  
ATOM   1293  CE  MET A 496     209.775 219.770 184.598  1.00 98.74           C  
ATOM   1294  N   PHE A 497     207.173 223.276 183.436  1.00104.24           N  
ATOM   1295  CA  PHE A 497     207.322 224.285 184.513  1.00104.24           C  
ATOM   1296  C   PHE A 497     205.984 225.017 184.635  1.00104.24           C  
ATOM   1297  O   PHE A 497     205.518 225.236 185.760  1.00104.24           O  
ATOM   1298  CB  PHE A 497     208.456 225.266 184.207  1.00104.24           C  
ATOM   1299  CG  PHE A 497     208.311 226.645 184.806  1.00104.24           C  
ATOM   1300  CD1 PHE A 497     207.682 226.833 186.025  1.00104.24           C  
ATOM   1301  CD2 PHE A 497     208.808 227.759 184.150  1.00104.24           C  
ATOM   1302  CE1 PHE A 497     207.546 228.101 186.568  1.00104.24           C  
ATOM   1303  CE2 PHE A 497     208.670 229.027 184.691  1.00104.24           C  
ATOM   1304  CZ  PHE A 497     208.043 229.196 185.903  1.00104.24           C  
ATOM   1305  N   THR A 498     205.381 225.375 183.499  1.00105.19           N  
ATOM   1306  CA  THR A 498     204.092 226.061 183.547  1.00105.19           C  
ATOM   1307  C   THR A 498     203.049 225.235 184.293  1.00105.19           C  
ATOM   1308  O   THR A 498     202.279 225.771 185.103  1.00105.19           O  
ATOM   1309  CB  THR A 498     203.625 226.366 182.127  1.00105.19           C  
ATOM   1310  OG1 THR A 498     204.455 227.390 181.569  1.00105.19           O  
ATOM   1311  CG2 THR A 498     202.182 226.821 182.119  1.00105.19           C  
ATOM   1312  N   CYS A 499     202.999 223.929 184.021  1.00101.02           N  
ATOM   1313  CA  CYS A 499     202.089 223.061 184.768  1.00101.02           C  
ATOM   1314  C   CYS A 499     202.412 223.083 186.260  1.00101.02           C  
ATOM   1315  O   CYS A 499     201.513 223.196 187.110  1.00101.02           O  
ATOM   1316  CB  CYS A 499     202.163 221.639 184.221  1.00101.02           C  
ATOM   1317  SG  CYS A 499     201.037 220.469 185.013  1.00101.02           S  
ATOM   1318  N   LEU A 500     203.703 222.983 186.591  1.00100.62           N  
ATOM   1319  CA  LEU A 500     204.153 223.144 187.969  1.00100.62           C  
ATOM   1320  C   LEU A 500     203.608 224.422 188.576  1.00100.62           C  
ATOM   1321  O   LEU A 500     203.109 224.425 189.704  1.00100.62           O  
ATOM   1322  CB  LEU A 500     205.685 223.160 188.004  1.00100.62           C  
ATOM   1323  CG  LEU A 500     206.506 223.168 189.296  1.00100.62           C  
ATOM   1324  CD1 LEU A 500     207.856 222.535 189.058  1.00100.62           C  
ATOM   1325  CD2 LEU A 500     206.712 224.579 189.775  1.00100.62           C  
ATOM   1326  N   PHE A 501     203.694 225.520 187.831  1.00110.51           N  
ATOM   1327  CA  PHE A 501     203.389 226.826 188.392  1.00110.51           C  
ATOM   1328  C   PHE A 501     201.897 226.980 188.649  1.00110.51           C  
ATOM   1329  O   PHE A 501     201.489 227.515 189.688  1.00110.51           O  
ATOM   1330  CB  PHE A 501     203.883 227.901 187.438  1.00110.51           C  
ATOM   1331  CG  PHE A 501     203.675 229.281 187.935  1.00110.51           C  
ATOM   1332  CD1 PHE A 501     204.500 229.798 188.912  1.00110.51           C  
ATOM   1333  CD2 PHE A 501     202.644 230.054 187.455  1.00110.51           C  
ATOM   1334  CE1 PHE A 501     204.318 231.068 189.376  1.00110.51           C  
ATOM   1335  CE2 PHE A 501     202.459 231.320 187.922  1.00110.51           C  
ATOM   1336  CZ  PHE A 501     203.294 231.829 188.883  1.00110.51           C  
ATOM   1337  N   LEU A 502     201.068 226.510 187.716  1.00104.63           N  
ATOM   1338  CA  LEU A 502     199.624 226.552 187.931  1.00104.63           C  
ATOM   1339  C   LEU A 502     199.218 225.709 189.133  1.00104.63           C  
ATOM   1340  O   LEU A 502     198.444 226.158 189.992  1.00104.63           O  
ATOM   1341  CB  LEU A 502     198.886 226.080 186.683  1.00104.63           C  
ATOM   1342  CG  LEU A 502     198.575 227.167 185.664  1.00104.63           C  
ATOM   1343  CD1 LEU A 502     197.717 226.610 184.545  1.00104.63           C  
ATOM   1344  CD2 LEU A 502     197.896 228.325 186.347  1.00104.63           C  
ATOM   1345  N   PHE A 503     199.722 224.472 189.207  1.00100.46           N  
ATOM   1346  CA  PHE A 503     199.373 223.627 190.344  1.00100.46           C  
ATOM   1347  C   PHE A 503     199.856 224.236 191.649  1.00100.46           C  
ATOM   1348  O   PHE A 503     199.188 224.121 192.679  1.00100.46           O  
ATOM   1349  CB  PHE A 503     199.950 222.231 190.170  1.00100.46           C  
ATOM   1350  CG  PHE A 503     198.995 221.252 189.575  1.00100.46           C  
ATOM   1351  CD1 PHE A 503     198.013 220.678 190.352  1.00100.46           C  
ATOM   1352  CD2 PHE A 503     199.095 220.884 188.250  1.00100.46           C  
ATOM   1353  CE1 PHE A 503     197.143 219.771 189.818  1.00100.46           C  
ATOM   1354  CE2 PHE A 503     198.226 219.978 187.713  1.00100.46           C  
ATOM   1355  CZ  PHE A 503     197.251 219.421 188.499  1.00100.46           C  
ATOM   1356  N   SER A 504     201.020 224.883 191.629  1.00106.78           N  
ATOM   1357  CA  SER A 504     201.519 225.534 192.832  1.00106.78           C  
ATOM   1358  C   SER A 504     200.603 226.668 193.260  1.00106.78           C  
ATOM   1359  O   SER A 504     200.311 226.824 194.451  1.00106.78           O  
ATOM   1360  CB  SER A 504     202.935 226.048 192.594  1.00106.78           C  
ATOM   1361  OG  SER A 504     202.943 227.073 191.620  1.00106.78           O  
ATOM   1362  N   VAL A 505     200.135 227.468 192.299  1.00107.67           N  
ATOM   1363  CA  VAL A 505     199.219 228.559 192.621  1.00107.67           C  
ATOM   1364  C   VAL A 505     197.959 228.014 193.278  1.00107.67           C  
ATOM   1365  O   VAL A 505     197.524 228.495 194.333  1.00107.67           O  
ATOM   1366  CB  VAL A 505     198.884 229.370 191.356  1.00107.67           C  
ATOM   1367  CG1 VAL A 505     197.642 230.210 191.579  1.00107.67           C  
ATOM   1368  CG2 VAL A 505     200.055 230.249 190.952  1.00107.67           C  
ATOM   1369  N   VAL A 506     197.363 226.984 192.677  1.00108.58           N  
ATOM   1370  CA  VAL A 506     196.105 226.483 193.219  1.00108.58           C  
ATOM   1371  C   VAL A 506     196.328 225.814 194.573  1.00108.58           C  
ATOM   1372  O   VAL A 506     195.494 225.927 195.478  1.00108.58           O  
ATOM   1373  CB  VAL A 506     195.407 225.547 192.218  1.00108.58           C  
ATOM   1374  CG1 VAL A 506     195.042 226.307 190.963  1.00108.58           C  
ATOM   1375  CG2 VAL A 506     196.264 224.372 191.880  1.00108.58           C  
ATOM   1376  N   LEU A 507     197.453 225.119 194.745  1.00106.25           N  
ATOM   1377  CA  LEU A 507     197.708 224.456 196.018  1.00106.25           C  
ATOM   1378  C   LEU A 507     197.934 225.466 197.132  1.00106.25           C  
ATOM   1379  O   LEU A 507     197.488 225.255 198.266  1.00106.25           O  
ATOM   1380  CB  LEU A 507     198.902 223.517 195.890  1.00106.25           C  
ATOM   1381  CG  LEU A 507     198.530 222.072 195.566  1.00106.25           C  
ATOM   1382  CD1 LEU A 507     199.767 221.293 195.241  1.00106.25           C  
ATOM   1383  CD2 LEU A 507     197.795 221.421 196.715  1.00106.25           C  
ATOM   1384  N   ARG A 508     198.625 226.566 196.832  1.00110.58           N  
ATOM   1385  CA  ARG A 508     198.720 227.648 197.803  1.00110.58           C  
ATOM   1386  C   ARG A 508     197.346 228.208 198.129  1.00110.58           C  
ATOM   1387  O   ARG A 508     197.026 228.443 199.300  1.00110.58           O  
ATOM   1388  CB  ARG A 508     199.634 228.757 197.284  1.00110.58           C  
ATOM   1389  CG  ARG A 508     199.833 229.864 198.295  1.00110.58           C  
ATOM   1390  CD  ARG A 508     200.005 229.292 199.682  1.00110.58           C  
ATOM   1391  NE  ARG A 508     199.478 230.195 200.694  1.00110.58           N  
ATOM   1392  CZ  ARG A 508     199.333 229.868 201.970  1.00110.58           C  
ATOM   1393  NH1 ARG A 508     198.826 230.743 202.823  1.00110.58           N  
ATOM   1394  NH2 ARG A 508     199.702 228.667 202.390  1.00110.58           N  
ATOM   1395  N   ALA A 509     196.510 228.407 197.111  1.00114.82           N  
ATOM   1396  CA  ALA A 509     195.179 228.945 197.362  1.00114.82           C  
ATOM   1397  C   ALA A 509     194.389 228.048 198.306  1.00114.82           C  
ATOM   1398  O   ALA A 509     193.705 228.534 199.211  1.00114.82           O  
ATOM   1399  CB  ALA A 509     194.429 229.130 196.046  1.00114.82           C  
ATOM   1400  N   LEU A 510     194.483 226.735 198.121  1.00114.00           N  
ATOM   1401  CA  LEU A 510     193.611 225.815 198.843  1.00114.00           C  
ATOM   1402  C   LEU A 510     194.156 225.404 200.209  1.00114.00           C  
ATOM   1403  O   LEU A 510     193.478 225.566 201.227  1.00114.00           O  
ATOM   1404  CB  LEU A 510     193.359 224.573 197.988  1.00114.00           C  
ATOM   1405  CG  LEU A 510     192.839 224.876 196.591  1.00114.00           C  
ATOM   1406  CD1 LEU A 510     192.901 223.640 195.713  1.00114.00           C  
ATOM   1407  CD2 LEU A 510     191.433 225.416 196.678  1.00114.00           C  
ATOM   1408  N   PHE A 511     195.371 224.858 200.251  1.00111.41           N  
ATOM   1409  CA  PHE A 511     195.796 224.035 201.378  1.00111.41           C  
ATOM   1410  C   PHE A 511     196.649 224.784 202.393  1.00111.41           C  
ATOM   1411  O   PHE A 511     197.460 224.168 203.086  1.00111.41           O  
ATOM   1412  CB  PHE A 511     196.536 222.804 200.871  1.00111.41           C  
ATOM   1413  CG  PHE A 511     195.640 221.658 200.575  1.00111.41           C  
ATOM   1414  CD1 PHE A 511     194.975 221.010 201.591  1.00111.41           C  
ATOM   1415  CD2 PHE A 511     195.434 221.248 199.277  1.00111.41           C  
ATOM   1416  CE1 PHE A 511     194.139 219.958 201.319  1.00111.41           C  
ATOM   1417  CE2 PHE A 511     194.601 220.198 198.999  1.00111.41           C  
ATOM   1418  CZ  PHE A 511     193.952 219.552 200.020  1.00111.41           C  
ATOM   1419  N   GLN A 512     196.456 226.089 202.533  1.00117.84           N  
ATOM   1420  CA  GLN A 512     197.059 226.779 203.656  1.00117.84           C  
ATOM   1421  C   GLN A 512     196.513 226.205 204.957  1.00117.84           C  
ATOM   1422  O   GLN A 512     195.475 225.552 204.986  1.00117.84           O  
ATOM   1423  CB  GLN A 512     196.767 228.275 203.587  1.00117.84           C  
ATOM   1424  CG  GLN A 512     195.315 228.631 203.847  1.00117.84           C  
ATOM   1425  CD  GLN A 512     194.454 228.521 202.606  1.00117.84           C  
ATOM   1426  OE1 GLN A 512     194.844 227.901 201.620  1.00117.84           O  
ATOM   1427  NE2 GLN A 512     193.273 229.118 202.652  1.00117.84           N  
ATOM   1428  N   ASP A 513     197.263 226.414 206.035  1.00120.09           N  
ATOM   1429  CA  ASP A 513     196.898 226.027 207.398  1.00120.09           C  
ATOM   1430  C   ASP A 513     196.527 224.550 207.507  1.00120.09           C  
ATOM   1431  O   ASP A 513     195.973 224.109 208.519  1.00120.09           O  
ATOM   1432  CB  ASP A 513     195.797 226.966 207.943  1.00120.09           C  
ATOM   1433  CG  ASP A 513     194.383 226.659 207.430  1.00120.09           C  
ATOM   1434  OD1 ASP A 513     194.044 225.513 207.073  1.00120.09           O  
ATOM   1435  OD2 ASP A 513     193.590 227.619 207.369  1.00120.09           O  
ATOM   1436  N   SER A 514     196.844 223.786 206.471  1.00119.66           N  
ATOM   1437  CA  SER A 514     196.848 222.329 206.505  1.00119.66           C  
ATOM   1438  C   SER A 514     198.291 221.939 206.226  1.00119.66           C  
ATOM   1439  O   SER A 514     198.679 221.759 205.071  1.00119.66           O  
ATOM   1440  CB  SER A 514     195.886 221.742 205.480  1.00119.66           C  
ATOM   1441  OG  SER A 514     194.591 222.294 205.631  1.00119.66           O  
ATOM   1442  N   ASP A 515     199.077 221.823 207.288  1.00118.24           N  
ATOM   1443  CA  ASP A 515     200.531 221.762 207.227  1.00118.24           C  
ATOM   1444  C   ASP A 515     201.102 223.032 206.609  1.00118.24           C  
ATOM   1445  O   ASP A 515     201.525 223.036 205.444  1.00118.24           O  
ATOM   1446  CB  ASP A 515     201.002 220.528 206.463  1.00118.24           C  
ATOM   1447  CG  ASP A 515     201.318 219.379 207.380  1.00118.24           C  
ATOM   1448  OD1 ASP A 515     201.580 219.627 208.574  1.00118.24           O  
ATOM   1449  OD2 ASP A 515     201.301 218.230 206.908  1.00118.24           O  
ATOM   1450  N   PRO A 516     201.112 224.136 207.359  1.00119.82           N  
ATOM   1451  CA  PRO A 516     201.788 225.348 206.880  1.00119.82           C  
ATOM   1452  C   PRO A 516     203.288 225.205 206.827  1.00119.82           C  
ATOM   1453  O   PRO A 516     203.949 226.042 206.207  1.00119.82           O  
ATOM   1454  CB  PRO A 516     201.389 226.403 207.911  1.00119.82           C  
ATOM   1455  CG  PRO A 516     201.138 225.609 209.156  1.00119.82           C  
ATOM   1456  CD  PRO A 516     200.557 224.304 208.711  1.00119.82           C  
ATOM   1457  N   LYS A 517     203.853 224.180 207.461  1.00116.17           N  
ATOM   1458  CA  LYS A 517     205.298 224.009 207.415  1.00116.17           C  
ATOM   1459  C   LYS A 517     205.772 223.745 205.995  1.00116.17           C  
ATOM   1460  O   LYS A 517     206.918 224.052 205.655  1.00116.17           O  
ATOM   1461  CB  LYS A 517     205.718 222.873 208.346  1.00116.17           C  
ATOM   1462  CG  LYS A 517     207.206 222.837 208.639  1.00116.17           C  
ATOM   1463  CD  LYS A 517     207.659 221.459 209.081  1.00116.17           C  
ATOM   1464  CE  LYS A 517     209.162 221.305 208.928  1.00116.17           C  
ATOM   1465  NZ  LYS A 517     209.905 221.877 210.086  1.00116.17           N  
ATOM   1466  N   ARG A 518     204.897 223.196 205.155  1.00105.09           N  
ATOM   1467  CA  ARG A 518     205.277 222.796 203.806  1.00105.09           C  
ATOM   1468  C   ARG A 518     205.136 223.948 202.819  1.00105.09           C  
ATOM   1469  O   ARG A 518     206.084 224.290 202.108  1.00105.09           O  
ATOM   1470  CB  ARG A 518     204.426 221.603 203.368  1.00105.09           C  
ATOM   1471  CG  ARG A 518     204.963 220.850 202.175  1.00105.09           C  
ATOM   1472  CD  ARG A 518     205.872 219.739 202.652  1.00105.09           C  
ATOM   1473  NE  ARG A 518     205.257 218.987 203.738  1.00105.09           N  
ATOM   1474  CZ  ARG A 518     205.752 217.870 204.254  1.00105.09           C  
ATOM   1475  NH1 ARG A 518     205.113 217.257 205.237  1.00105.09           N  
ATOM   1476  NH2 ARG A 518     206.889 217.372 203.799  1.00105.09           N  
ATOM   1477  N   PHE A 519     203.951 224.545 202.744  1.00108.02           N  
ATOM   1478  CA  PHE A 519     203.671 225.598 201.772  1.00108.02           C  
ATOM   1479  C   PHE A 519     202.891 226.766 202.383  1.00108.02           C  
ATOM   1480  O   PHE A 519     201.839 227.168 201.884  1.00108.02           O  
ATOM   1481  CB  PHE A 519     203.003 225.037 200.522  1.00108.02           C  
ATOM   1482  CG  PHE A 519     201.944 224.025 200.767  1.00108.02           C  
ATOM   1483  CD1 PHE A 519     200.755 224.359 201.349  1.00108.02           C  
ATOM   1484  CD2 PHE A 519     202.167 222.706 200.423  1.00108.02           C  
ATOM   1485  CE1 PHE A 519     199.812 223.402 201.564  1.00108.02           C  
ATOM   1486  CE2 PHE A 519     201.216 221.752 200.628  1.00108.02           C  
ATOM   1487  CZ  PHE A 519     200.042 222.096 201.203  1.00108.02           C  
ATOM   1488  N   GLN A 520     203.403 227.337 203.480  1.00110.92           N  
ATOM   1489  CA  GLN A 520     202.813 228.570 204.000  1.00110.92           C  
ATOM   1490  C   GLN A 520     203.129 229.776 203.125  1.00110.92           C  
ATOM   1491  O   GLN A 520     202.466 230.812 203.241  1.00110.92           O  
ATOM   1492  CB  GLN A 520     203.292 228.855 205.420  1.00110.92           C  
ATOM   1493  CG  GLN A 520     204.690 229.435 205.509  1.00110.92           C  
ATOM   1494  CD  GLN A 520     205.224 229.441 206.929  1.00110.92           C  
ATOM   1495  OE1 GLN A 520     204.457 229.454 207.890  1.00110.92           O  
ATOM   1496  NE2 GLN A 520     206.544 229.451 207.068  1.00110.92           N  
ATOM   1497  N   ASN A 521     204.142 229.677 202.276  1.00106.73           N  
ATOM   1498  CA  ASN A 521     204.540 230.742 201.371  1.00106.73           C  
ATOM   1499  C   ASN A 521     204.429 230.249 199.938  1.00106.73           C  
ATOM   1500  O   ASN A 521     204.579 229.059 199.673  1.00106.73           O  
ATOM   1501  CB  ASN A 521     205.977 231.182 201.658  1.00106.73           C  
ATOM   1502  CG  ASN A 521     206.372 232.428 200.901  1.00106.73           C  
ATOM   1503  OD1 ASN A 521     205.587 232.980 200.135  1.00106.73           O  
ATOM   1504  ND2 ASN A 521     207.602 232.874 201.105  1.00106.73           N  
ATOM   1505  N   ILE A 522     204.198 231.169 199.003  1.00103.56           N  
ATOM   1506  CA  ILE A 522     204.089 230.767 197.603  1.00103.56           C  
ATOM   1507  C   ILE A 522     205.370 230.096 197.134  1.00103.56           C  
ATOM   1508  O   ILE A 522     205.334 229.101 196.398  1.00103.56           O  
ATOM   1509  CB  ILE A 522     203.724 231.971 196.716  1.00103.56           C  
ATOM   1510  CG1 ILE A 522     203.610 231.538 195.253  1.00103.56           C  
ATOM   1511  CG2 ILE A 522     204.733 233.092 196.872  1.00103.56           C  
ATOM   1512  CD1 ILE A 522     202.520 230.545 194.990  1.00103.56           C  
ATOM   1513  N   PHE A 523     206.522 230.617 197.556  1.00100.54           N  
ATOM   1514  CA  PHE A 523     207.789 230.052 197.112  1.00100.54           C  
ATOM   1515  C   PHE A 523     207.971 228.641 197.636  1.00100.54           C  
ATOM   1516  O   PHE A 523     208.457 227.761 196.918  1.00100.54           O  
ATOM   1517  CB  PHE A 523     208.937 230.948 197.553  1.00100.54           C  
ATOM   1518  CG  PHE A 523     208.851 232.328 197.001  1.00100.54           C  
ATOM   1519  CD1 PHE A 523     209.089 232.562 195.662  1.00100.54           C  
ATOM   1520  CD2 PHE A 523     208.495 233.389 197.812  1.00100.54           C  
ATOM   1521  CE1 PHE A 523     208.997 233.831 195.146  1.00100.54           C  
ATOM   1522  CE2 PHE A 523     208.399 234.656 197.303  1.00100.54           C  
ATOM   1523  CZ  PHE A 523     208.650 234.879 195.967  1.00100.54           C  
ATOM   1524  N   THR A 524     207.583 228.396 198.882  1.00 99.60           N  
ATOM   1525  CA  THR A 524     207.695 227.038 199.384  1.00 99.60           C  
ATOM   1526  C   THR A 524     206.616 226.117 198.824  1.00 99.60           C  
ATOM   1527  O   THR A 524     206.877 224.918 198.693  1.00 99.60           O  
ATOM   1528  CB  THR A 524     207.718 227.028 200.915  1.00 99.60           C  
ATOM   1529  OG1 THR A 524     207.954 225.699 201.383  1.00 99.60           O  
ATOM   1530  CG2 THR A 524     206.457 227.537 201.490  1.00 99.60           C  
ATOM   1531  N   THR A 525     205.452 226.637 198.415  1.00 98.78           N  
ATOM   1532  CA  THR A 525     204.556 225.827 197.590  1.00 98.78           C  
ATOM   1533  C   THR A 525     205.272 225.367 196.340  1.00 98.78           C  
ATOM   1534  O   THR A 525     205.258 224.182 195.992  1.00 98.78           O  
ATOM   1535  CB  THR A 525     203.315 226.603 197.149  1.00 98.78           C  
ATOM   1536  OG1 THR A 525     203.696 227.565 196.161  1.00 98.78           O  
ATOM   1537  CG2 THR A 525     202.663 227.326 198.274  1.00 98.78           C  
ATOM   1538  N   LEU A 526     205.880 226.314 195.632  1.00 91.98           N  
ATOM   1539  CA  LEU A 526     206.469 226.004 194.341  1.00 91.98           C  
ATOM   1540  C   LEU A 526     207.618 225.019 194.496  1.00 91.98           C  
ATOM   1541  O   LEU A 526     207.754 224.077 193.707  1.00 91.98           O  
ATOM   1542  CB  LEU A 526     206.910 227.298 193.670  1.00 91.98           C  
ATOM   1543  CG  LEU A 526     207.163 227.261 192.173  1.00 91.98           C  
ATOM   1544  CD1 LEU A 526     206.815 228.603 191.581  1.00 91.98           C  
ATOM   1545  CD2 LEU A 526     208.606 226.922 191.902  1.00 91.98           C  
ATOM   1546  N   PHE A 527     208.434 225.195 195.534  1.00 88.18           N  
ATOM   1547  CA  PHE A 527     209.505 224.237 195.777  1.00 88.18           C  
ATOM   1548  C   PHE A 527     208.962 222.868 196.161  1.00 88.18           C  
ATOM   1549  O   PHE A 527     209.525 221.849 195.758  1.00 88.18           O  
ATOM   1550  CB  PHE A 527     210.455 224.740 196.853  1.00 88.18           C  
ATOM   1551  CG  PHE A 527     211.738 223.976 196.901  1.00 88.18           C  
ATOM   1552  CD1 PHE A 527     212.744 224.231 195.990  1.00 88.18           C  
ATOM   1553  CD2 PHE A 527     211.923 222.972 197.831  1.00 88.18           C  
ATOM   1554  CE1 PHE A 527     213.915 223.521 196.024  1.00 88.18           C  
ATOM   1555  CE2 PHE A 527     213.092 222.258 197.864  1.00 88.18           C  
ATOM   1556  CZ  PHE A 527     214.090 222.536 196.960  1.00 88.18           C  
ATOM   1557  N   THR A 528     207.893 222.814 196.959  1.00 86.86           N  
ATOM   1558  CA  THR A 528     207.319 221.523 197.321  1.00 86.86           C  
ATOM   1559  C   THR A 528     206.812 220.782 196.095  1.00 86.86           C  
ATOM   1560  O   THR A 528     207.004 219.570 195.966  1.00 86.86           O  
ATOM   1561  CB  THR A 528     206.192 221.715 198.320  1.00 86.86           C  
ATOM   1562  OG1 THR A 528     206.730 222.218 199.544  1.00 86.86           O  
ATOM   1563  CG2 THR A 528     205.518 220.408 198.589  1.00 86.86           C  
ATOM   1564  N   LEU A 529     206.173 221.493 195.176  1.00 87.79           N  
ATOM   1565  CA  LEU A 529     205.740 220.846 193.941  1.00 87.79           C  
ATOM   1566  C   LEU A 529     206.939 220.399 193.101  1.00 87.79           C  
ATOM   1567  O   LEU A 529     206.946 219.285 192.557  1.00 87.79           O  
ATOM   1568  CB  LEU A 529     204.836 221.790 193.150  1.00 87.79           C  
ATOM   1569  CG  LEU A 529     203.347 221.875 193.521  1.00 87.79           C  
ATOM   1570  CD1 LEU A 529     202.617 220.589 193.303  1.00 87.79           C  
ATOM   1571  CD2 LEU A 529     203.147 222.298 194.948  1.00 87.79           C  
ATOM   1572  N   PHE A 530     207.977 221.235 193.009  1.00 79.87           N  
ATOM   1573  CA  PHE A 530     209.155 220.853 192.233  1.00 79.87           C  
ATOM   1574  C   PHE A 530     209.825 219.616 192.809  1.00 79.87           C  
ATOM   1575  O   PHE A 530     210.257 218.731 192.064  1.00 79.87           O  
ATOM   1576  CB  PHE A 530     210.152 222.004 192.177  1.00 79.87           C  
ATOM   1577  CG  PHE A 530     211.532 221.591 191.770  1.00 79.87           C  
ATOM   1578  CD1 PHE A 530     211.834 221.360 190.449  1.00 79.87           C  
ATOM   1579  CD2 PHE A 530     212.528 221.452 192.710  1.00 79.87           C  
ATOM   1580  CE1 PHE A 530     213.100 220.986 190.074  1.00 79.87           C  
ATOM   1581  CE2 PHE A 530     213.786 221.076 192.342  1.00 79.87           C  
ATOM   1582  CZ  PHE A 530     214.075 220.847 191.022  1.00 79.87           C  
ATOM   1583  N   THR A 531     209.942 219.544 194.130  1.00 80.52           N  
ATOM   1584  CA  THR A 531     210.545 218.379 194.748  1.00 80.52           C  
ATOM   1585  C   THR A 531     209.624 217.175 194.724  1.00 80.52           C  
ATOM   1586  O   THR A 531     210.106 216.052 194.870  1.00 80.52           O  
ATOM   1587  CB  THR A 531     210.958 218.671 196.186  1.00 80.52           C  
ATOM   1588  OG1 THR A 531     211.698 217.559 196.687  1.00 80.52           O  
ATOM   1589  CG2 THR A 531     209.764 218.816 197.051  1.00 80.52           C  
ATOM   1590  N   MET A 532     208.316 217.374 194.560  1.00 80.01           N  
ATOM   1591  CA  MET A 532     207.454 216.241 194.256  1.00 80.01           C  
ATOM   1592  C   MET A 532     207.762 215.693 192.881  1.00 80.01           C  
ATOM   1593  O   MET A 532     207.660 214.487 192.642  1.00 80.01           O  
ATOM   1594  CB  MET A 532     205.993 216.650 194.302  1.00 80.01           C  
ATOM   1595  CG  MET A 532     205.108 215.566 193.788  1.00 80.01           C  
ATOM   1596  SD  MET A 532     203.391 215.890 194.098  1.00 80.01           S  
ATOM   1597  CE  MET A 532     203.553 216.644 195.695  1.00 80.01           C  
ATOM   1598  N   LEU A 533     208.150 216.570 191.966  1.00 75.93           N  
ATOM   1599  CA  LEU A 533     208.365 216.144 190.591  1.00 75.93           C  
ATOM   1600  C   LEU A 533     209.525 215.161 190.464  1.00 75.93           C  
ATOM   1601  O   LEU A 533     209.662 214.519 189.420  1.00 75.93           O  
ATOM   1602  CB  LEU A 533     208.578 217.379 189.715  1.00 75.93           C  
ATOM   1603  CG  LEU A 533     208.586 217.297 188.195  1.00 75.93           C  
ATOM   1604  CD1 LEU A 533     207.994 218.561 187.637  1.00 75.93           C  
ATOM   1605  CD2 LEU A 533     209.980 217.154 187.689  1.00 75.93           C  
ATOM   1606  N   THR A 534     210.360 215.021 191.495  1.00 73.00           N  
ATOM   1607  CA  THR A 534     211.378 213.976 191.531  1.00 73.00           C  
ATOM   1608  C   THR A 534     210.944 212.736 192.302  1.00 73.00           C  
ATOM   1609  O   THR A 534     211.673 211.739 192.297  1.00 73.00           O  
ATOM   1610  CB  THR A 534     212.675 214.490 192.153  1.00 73.00           C  
ATOM   1611  OG1 THR A 534     212.408 215.006 193.457  1.00 73.00           O  
ATOM   1612  CG2 THR A 534     213.290 215.570 191.299  1.00 73.00           C  
ATOM   1613  N   LEU A 535     209.742 212.755 192.888  1.00 71.56           N  
ATOM   1614  CA  LEU A 535     209.130 211.611 193.614  1.00 71.56           C  
ATOM   1615  C   LEU A 535     209.926 211.148 194.832  1.00 71.56           C  
ATOM   1616  O   LEU A 535     210.067 209.943 194.996  1.00 71.56           O  
ATOM   1617  CB  LEU A 535     208.973 210.489 192.596  1.00 71.56           C  
ATOM   1618  CG  LEU A 535     208.441 210.980 191.263  1.00 71.56           C  
ATOM   1619  CD1 LEU A 535     208.085 209.824 190.355  1.00 71.56           C  
ATOM   1620  CD2 LEU A 535     207.248 211.882 191.487  1.00 71.56           C  
ATOM   1621  N   ASP A 536     210.409 212.071 195.660  1.00 74.38           N  
ATOM   1622  CA  ASP A 536     211.137 211.714 196.871  1.00 74.38           C  
ATOM   1623  C   ASP A 536     210.279 212.064 198.074  1.00 74.38           C  
ATOM   1624  O   ASP A 536     210.027 213.241 198.340  1.00 74.38           O  
ATOM   1625  CB  ASP A 536     212.486 212.414 196.937  1.00 74.38           C  
ATOM   1626  CG  ASP A 536     213.420 211.761 197.921  1.00 74.38           C  
ATOM   1627  OD1 ASP A 536     213.001 210.777 198.561  1.00 74.38           O  
ATOM   1628  OD2 ASP A 536     214.570 212.226 198.059  1.00 74.38           O  
ATOM   1629  N   ASP A 537     209.836 211.034 198.795  1.00 78.10           N  
ATOM   1630  CA  ASP A 537     209.008 211.181 199.990  1.00 78.10           C  
ATOM   1631  C   ASP A 537     207.665 211.826 199.676  1.00 78.10           C  
ATOM   1632  O   ASP A 537     207.055 212.453 200.540  1.00 78.10           O  
ATOM   1633  CB  ASP A 537     209.732 211.984 201.072  1.00 78.10           C  
ATOM   1634  CG  ASP A 537     210.915 211.247 201.649  1.00 78.10           C  
ATOM   1635  OD1 ASP A 537     210.787 210.034 201.904  1.00 78.10           O  
ATOM   1636  OD2 ASP A 537     211.971 211.884 201.854  1.00 78.10           O  
ATOM   1637  N   TRP A 538     207.185 211.671 198.442  1.00 73.49           N  
ATOM   1638  CA  TRP A 538     205.968 212.362 198.048  1.00 73.49           C  
ATOM   1639  C   TRP A 538     204.752 211.832 198.786  1.00 73.49           C  
ATOM   1640  O   TRP A 538     203.761 212.549 198.924  1.00 73.49           O  
ATOM   1641  CB  TRP A 538     205.764 212.265 196.541  1.00 73.49           C  
ATOM   1642  CG  TRP A 538     205.112 211.021 196.088  1.00 73.49           C  
ATOM   1643  CD1 TRP A 538     205.724 209.927 195.583  1.00 73.49           C  
ATOM   1644  CD2 TRP A 538     203.710 210.742 196.069  1.00 73.49           C  
ATOM   1645  NE1 TRP A 538     204.797 208.974 195.261  1.00 73.49           N  
ATOM   1646  CE2 TRP A 538     203.550 209.454 195.556  1.00 73.49           C  
ATOM   1647  CE3 TRP A 538     202.575 211.457 196.447  1.00 73.49           C  
ATOM   1648  CZ2 TRP A 538     202.307 208.866 195.406  1.00 73.49           C  
ATOM   1649  CZ3 TRP A 538     201.347 210.868 196.304  1.00 73.49           C  
ATOM   1650  CH2 TRP A 538     201.221 209.589 195.788  1.00 73.49           C  
ATOM   1651  N   SER A 539     204.789 210.587 199.251  1.00 77.14           N  
ATOM   1652  CA  SER A 539     203.693 210.110 200.080  1.00 77.14           C  
ATOM   1653  C   SER A 539     203.705 210.760 201.445  1.00 77.14           C  
ATOM   1654  O   SER A 539     202.653 210.857 202.082  1.00 77.14           O  
ATOM   1655  CB  SER A 539     203.751 208.595 200.236  1.00 77.14           C  
ATOM   1656  OG  SER A 539     205.014 208.186 200.717  1.00 77.14           O  
ATOM   1657  N   LEU A 540     204.872 211.210 201.903  1.00 84.93           N  
ATOM   1658  CA  LEU A 540     204.964 211.774 203.240  1.00 84.93           C  
ATOM   1659  C   LEU A 540     204.106 213.012 203.369  1.00 84.93           C  
ATOM   1660  O   LEU A 540     203.508 213.248 204.419  1.00 84.93           O  
ATOM   1661  CB  LEU A 540     206.411 212.093 203.589  1.00 84.93           C  
ATOM   1662  CG  LEU A 540     207.217 210.834 203.864  1.00 84.93           C  
ATOM   1663  CD1 LEU A 540     208.541 211.174 204.492  1.00 84.93           C  
ATOM   1664  CD2 LEU A 540     206.422 209.905 204.767  1.00 84.93           C  
ATOM   1665  N   ILE A 541     204.029 213.820 202.317  1.00 89.38           N  
ATOM   1666  CA  ILE A 541     203.223 215.023 202.426  1.00 89.38           C  
ATOM   1667  C   ILE A 541     201.742 214.674 202.414  1.00 89.38           C  
ATOM   1668  O   ILE A 541     200.941 215.333 203.086  1.00 89.38           O  
ATOM   1669  CB  ILE A 541     203.602 216.026 201.330  1.00 89.38           C  
ATOM   1670  CG1 ILE A 541     203.432 215.438 199.958  1.00 89.38           C  
ATOM   1671  CG2 ILE A 541     205.073 216.352 201.395  1.00 89.38           C  
ATOM   1672  CD1 ILE A 541     203.629 216.469 198.941  1.00 89.38           C  
ATOM   1673  N   TYR A 542     201.346 213.631 201.685  1.00 88.92           N  
ATOM   1674  CA  TYR A 542     199.962 213.184 201.773  1.00 88.92           C  
ATOM   1675  C   TYR A 542     199.629 212.731 203.185  1.00 88.92           C  
ATOM   1676  O   TYR A 542     198.597 213.118 203.745  1.00 88.92           O  
ATOM   1677  CB  TYR A 542     199.693 212.060 200.781  1.00 88.92           C  
ATOM   1678  CG  TYR A 542     198.651 211.079 201.254  1.00 88.92           C  
ATOM   1679  CD1 TYR A 542     197.308 211.415 201.276  1.00 88.92           C  
ATOM   1680  CD2 TYR A 542     199.013 209.816 201.677  1.00 88.92           C  
ATOM   1681  CE1 TYR A 542     196.360 210.518 201.703  1.00 88.92           C  
ATOM   1682  CE2 TYR A 542     198.074 208.915 202.111  1.00 88.92           C  
ATOM   1683  CZ  TYR A 542     196.751 209.269 202.124  1.00 88.92           C  
ATOM   1684  OH  TYR A 542     195.818 208.360 202.556  1.00 88.92           O  
ATOM   1685  N   ILE A 543     200.492 211.910 203.783  1.00 90.53           N  
ATOM   1686  CA  ILE A 543     200.210 211.429 205.131  1.00 90.53           C  
ATOM   1687  C   ILE A 543     200.200 212.588 206.114  1.00 90.53           C  
ATOM   1688  O   ILE A 543     199.333 212.669 206.995  1.00 90.53           O  
ATOM   1689  CB  ILE A 543     201.219 210.349 205.552  1.00 90.53           C  
ATOM   1690  CG1 ILE A 543     201.439 209.357 204.423  1.00 90.53           C  
ATOM   1691  CG2 ILE A 543     200.709 209.612 206.772  1.00 90.53           C  
ATOM   1692  CD1 ILE A 543     202.741 208.634 204.519  1.00 90.53           C  
ATOM   1693  N   ASP A 544     201.162 213.501 205.981  1.00100.92           N  
ATOM   1694  CA  ASP A 544     201.249 214.642 206.881  1.00100.92           C  
ATOM   1695  C   ASP A 544     199.989 215.485 206.819  1.00100.92           C  
ATOM   1696  O   ASP A 544     199.470 215.912 207.856  1.00100.92           O  
ATOM   1697  CB  ASP A 544     202.469 215.487 206.528  1.00100.92           C  
ATOM   1698  CG  ASP A 544     203.728 215.020 207.219  1.00100.92           C  
ATOM   1699  OD1 ASP A 544     203.623 214.358 208.272  1.00100.92           O  
ATOM   1700  OD2 ASP A 544     204.828 215.333 206.716  1.00100.92           O  
ATOM   1701  N   ASN A 545     199.481 215.744 205.613  1.00104.34           N  
ATOM   1702  CA  ASN A 545     198.231 216.481 205.499  1.00104.34           C  
ATOM   1703  C   ASN A 545     197.079 215.702 206.110  1.00104.34           C  
ATOM   1704  O   ASN A 545     196.298 216.249 206.895  1.00104.34           O  
ATOM   1705  CB  ASN A 545     197.940 216.796 204.038  1.00104.34           C  
ATOM   1706  CG  ASN A 545     198.599 218.065 203.584  1.00104.34           C  
ATOM   1707  OD1 ASN A 545     199.517 218.561 204.225  1.00104.34           O  
ATOM   1708  ND2 ASN A 545     198.132 218.606 202.476  1.00104.34           N  
ATOM   1709  N   ARG A 546     196.968 214.414 205.779  1.00101.96           N  
ATOM   1710  CA  ARG A 546     195.857 213.608 206.273  1.00101.96           C  
ATOM   1711  C   ARG A 546     195.831 213.540 207.788  1.00101.96           C  
ATOM   1712  O   ARG A 546     194.768 213.331 208.379  1.00101.96           O  
ATOM   1713  CB  ARG A 546     195.944 212.199 205.702  1.00101.96           C  
ATOM   1714  CG  ARG A 546     194.659 211.422 205.760  1.00101.96           C  
ATOM   1715  CD  ARG A 546     194.738 210.244 204.814  1.00101.96           C  
ATOM   1716  NE  ARG A 546     193.815 209.164 205.144  1.00101.96           N  
ATOM   1717  CZ  ARG A 546     193.850 208.455 206.267  1.00101.96           C  
ATOM   1718  NH1 ARG A 546     192.961 207.491 206.464  1.00101.96           N  
ATOM   1719  NH2 ARG A 546     194.774 208.693 207.186  1.00101.96           N  
ATOM   1720  N   ALA A 547     196.987 213.692 208.431  1.00113.13           N  
ATOM   1721  CA  ALA A 547     197.037 213.579 209.883  1.00113.13           C  
ATOM   1722  C   ALA A 547     196.228 214.682 210.555  1.00113.13           C  
ATOM   1723  O   ALA A 547     195.360 214.410 211.392  1.00113.13           O  
ATOM   1724  CB  ALA A 547     198.489 213.611 210.354  1.00113.13           C  
ATOM   1725  N   GLN A 548     196.490 215.935 210.195  1.00119.42           N  
ATOM   1726  CA  GLN A 548     195.878 217.078 210.860  1.00119.42           C  
ATOM   1727  C   GLN A 548     194.903 217.835 209.983  1.00119.42           C  
ATOM   1728  O   GLN A 548     193.825 218.207 210.449  1.00119.42           O  
ATOM   1729  CB  GLN A 548     196.957 218.045 211.361  1.00119.42           C  
ATOM   1730  CG  GLN A 548     197.780 218.703 210.264  1.00119.42           C  
ATOM   1731  CD  GLN A 548     198.791 219.692 210.801  1.00119.42           C  
ATOM   1732  OE1 GLN A 548     198.872 219.925 212.005  1.00119.42           O  
ATOM   1733  NE2 GLN A 548     199.574 220.273 209.909  1.00119.42           N  
ATOM   1734  N   GLY A 549     195.242 218.060 208.721  1.00120.02           N  
ATOM   1735  CA  GLY A 549     194.348 218.747 207.822  1.00120.02           C  
ATOM   1736  C   GLY A 549     193.359 217.766 207.240  1.00120.02           C  
ATOM   1737  O   GLY A 549     192.626 217.103 207.978  1.00120.02           O  
ATOM   1738  N   ALA A 550     193.320 217.659 205.922  1.00112.27           N  
ATOM   1739  CA  ALA A 550     192.401 216.743 205.281  1.00112.27           C  
ATOM   1740  C   ALA A 550     193.001 216.207 203.992  1.00112.27           C  
ATOM   1741  O   ALA A 550     193.965 216.752 203.455  1.00112.27           O  
ATOM   1742  CB  ALA A 550     191.068 217.414 205.018  1.00112.27           C  
ATOM   1743  N   TRP A 551     192.405 215.128 203.506  1.00105.44           N  
ATOM   1744  CA  TRP A 551     192.971 214.310 202.452  1.00105.44           C  
ATOM   1745  C   TRP A 551     192.584 214.763 201.063  1.00105.44           C  
ATOM   1746  O   TRP A 551     192.837 214.027 200.107  1.00105.44           O  
ATOM   1747  CB  TRP A 551     192.540 212.861 202.648  1.00105.44           C  
ATOM   1748  CG  TRP A 551     191.116 212.722 203.052  1.00105.44           C  
ATOM   1749  CD1 TRP A 551     190.651 212.366 204.276  1.00105.44           C  
ATOM   1750  CD2 TRP A 551     189.965 212.923 202.226  1.00105.44           C  
ATOM   1751  NE1 TRP A 551     189.282 212.338 204.271  1.00105.44           N  
ATOM   1752  CE2 TRP A 551     188.836 212.676 203.021  1.00105.44           C  
ATOM   1753  CE3 TRP A 551     189.780 213.287 200.891  1.00105.44           C  
ATOM   1754  CZ2 TRP A 551     187.541 212.783 202.528  1.00105.44           C  
ATOM   1755  CZ3 TRP A 551     188.498 213.393 200.405  1.00105.44           C  
ATOM   1756  CH2 TRP A 551     187.395 213.143 201.220  1.00105.44           C  
ATOM   1757  N   TYR A 552     191.970 215.899 200.882  1.00108.72           N  
ATOM   1758  CA  TYR A 552     191.564 216.196 199.485  1.00108.72           C  
ATOM   1759  C   TYR A 552     192.806 216.292 198.593  1.00108.72           C  
ATOM   1760  O   TYR A 552     192.666 216.352 197.390  1.00108.72           O  
ATOM   1761  CB  TYR A 552     190.687 217.452 199.407  1.00108.72           C  
ATOM   1762  CG  TYR A 552     190.371 218.072 200.737  1.00108.72           C  
ATOM   1763  CD1 TYR A 552     189.604 217.392 201.651  1.00108.72           C  
ATOM   1764  CD2 TYR A 552     190.939 219.267 201.115  1.00108.72           C  
ATOM   1765  CE1 TYR A 552     189.358 217.923 202.898  1.00108.72           C  
ATOM   1766  CE2 TYR A 552     190.701 219.817 202.354  1.00108.72           C  
ATOM   1767  CZ  TYR A 552     189.908 219.137 203.248  1.00108.72           C  
ATOM   1768  OH  TYR A 552     189.671 219.664 204.476  1.00108.72           O  
ATOM   1769  N   ILE A 553     193.994 216.360 199.176  1.00 98.16           N  
ATOM   1770  CA  ILE A 553     195.196 216.503 198.372  1.00 98.16           C  
ATOM   1771  C   ILE A 553     195.506 215.250 197.576  1.00 98.16           C  
ATOM   1772  O   ILE A 553     196.379 215.283 196.705  1.00 98.16           O  
ATOM   1773  CB  ILE A 553     196.358 216.876 199.305  1.00 98.16           C  
ATOM   1774  CG1 ILE A 553     197.536 217.416 198.499  1.00 98.16           C  
ATOM   1775  CG2 ILE A 553     196.766 215.674 200.114  1.00 98.16           C  
ATOM   1776  CD1 ILE A 553     198.559 218.154 199.308  1.00 98.16           C  
ATOM   1777  N   ILE A 554     194.805 214.150 197.817  1.00 91.75           N  
ATOM   1778  CA  ILE A 554     195.210 212.908 197.168  1.00 91.75           C  
ATOM   1779  C   ILE A 554     194.833 212.906 195.688  1.00 91.75           C  
ATOM   1780  O   ILE A 554     195.668 212.489 194.874  1.00 91.75           O  
ATOM   1781  CB  ILE A 554     194.685 211.674 197.923  1.00 91.75           C  
ATOM   1782  CG1 ILE A 554     195.552 210.481 197.575  1.00 91.75           C  
ATOM   1783  CG2 ILE A 554     193.285 211.307 197.561  1.00 91.75           C  
ATOM   1784  CD1 ILE A 554     196.964 210.631 198.043  1.00 91.75           C  
ATOM   1785  N   PRO A 555     193.658 213.380 195.254  1.00 87.87           N  
ATOM   1786  CA  PRO A 555     193.432 213.391 193.805  1.00 87.87           C  
ATOM   1787  C   PRO A 555     194.307 214.408 193.104  1.00 87.87           C  
ATOM   1788  O   PRO A 555     194.784 214.155 191.992  1.00 87.87           O  
ATOM   1789  CB  PRO A 555     191.938 213.727 193.682  1.00 87.87           C  
ATOM   1790  CG  PRO A 555     191.397 213.624 195.061  1.00 87.87           C  
ATOM   1791  CD  PRO A 555     192.521 214.024 195.927  1.00 87.87           C  
ATOM   1792  N   ILE A 556     194.554 215.549 193.745  1.00 88.36           N  
ATOM   1793  CA  ILE A 556     195.422 216.557 193.153  1.00 88.36           C  
ATOM   1794  C   ILE A 556     196.819 215.995 192.954  1.00 88.36           C  
ATOM   1795  O   ILE A 556     197.416 216.138 191.885  1.00 88.36           O  
ATOM   1796  CB  ILE A 556     195.449 217.820 194.028  1.00 88.36           C  
ATOM   1797  CG1 ILE A 556     194.043 218.382 194.184  1.00 88.36           C  
ATOM   1798  CG2 ILE A 556     196.377 218.858 193.433  1.00 88.36           C  
ATOM   1799  CD1 ILE A 556     193.915 219.375 195.304  1.00 88.36           C  
ATOM   1800  N   LEU A 557     197.358 215.335 193.978  1.00 85.61           N  
ATOM   1801  CA  LEU A 557     198.714 214.815 193.868  1.00 85.61           C  
ATOM   1802  C   LEU A 557     198.788 213.663 192.879  1.00 85.61           C  
ATOM   1803  O   LEU A 557     199.757 213.557 192.123  1.00 85.61           O  
ATOM   1804  CB  LEU A 557     199.237 214.390 195.236  1.00 85.61           C  
ATOM   1805  CG  LEU A 557     199.471 215.580 196.167  1.00 85.61           C  
ATOM   1806  CD1 LEU A 557     200.257 215.200 197.409  1.00 85.61           C  
ATOM   1807  CD2 LEU A 557     200.133 216.706 195.426  1.00 85.61           C  
ATOM   1808  N   MET A 558     197.781 212.793 192.855  1.00 81.33           N  
ATOM   1809  CA  MET A 558     197.801 211.707 191.887  1.00 81.33           C  
ATOM   1810  C   MET A 558     197.755 212.237 190.461  1.00 81.33           C  
ATOM   1811  O   MET A 558     198.510 211.777 189.598  1.00 81.33           O  
ATOM   1812  CB  MET A 558     196.646 210.748 192.155  1.00 81.33           C  
ATOM   1813  CG  MET A 558     196.976 209.681 193.181  1.00 81.33           C  
ATOM   1814  SD  MET A 558     195.525 208.938 193.927  1.00 81.33           S  
ATOM   1815  CE  MET A 558     195.047 207.766 192.666  1.00 81.33           C  
ATOM   1816  N   ILE A 559     196.898 213.223 190.194  1.00 83.32           N  
ATOM   1817  CA  ILE A 559     196.820 213.788 188.850  1.00 83.32           C  
ATOM   1818  C   ILE A 559     198.104 214.531 188.505  1.00 83.32           C  
ATOM   1819  O   ILE A 559     198.589 214.478 187.365  1.00 83.32           O  
ATOM   1820  CB  ILE A 559     195.591 214.700 188.734  1.00 83.32           C  
ATOM   1821  CG1 ILE A 559     194.313 213.873 188.833  1.00 83.32           C  
ATOM   1822  CG2 ILE A 559     195.630 215.465 187.435  1.00 83.32           C  
ATOM   1823  CD1 ILE A 559     194.132 212.878 187.706  1.00 83.32           C  
ATOM   1824  N   TYR A 560     198.672 215.235 189.482  1.00 84.01           N  
ATOM   1825  CA  TYR A 560     199.940 215.916 189.285  1.00 84.01           C  
ATOM   1826  C   TYR A 560     201.016 214.939 188.853  1.00 84.01           C  
ATOM   1827  O   TYR A 560     201.741 215.177 187.879  1.00 84.01           O  
ATOM   1828  CB  TYR A 560     200.365 216.590 190.583  1.00 84.01           C  
ATOM   1829  CG  TYR A 560     201.512 217.526 190.388  1.00 84.01           C  
ATOM   1830  CD1 TYR A 560     201.664 218.213 189.206  1.00 84.01           C  
ATOM   1831  CD2 TYR A 560     202.517 217.614 191.326  1.00 84.01           C  
ATOM   1832  CE1 TYR A 560     202.718 219.046 189.013  1.00 84.01           C  
ATOM   1833  CE2 TYR A 560     203.599 218.421 191.122  1.00 84.01           C  
ATOM   1834  CZ  TYR A 560     203.694 219.142 189.965  1.00 84.01           C  
ATOM   1835  OH  TYR A 560     204.770 219.968 189.758  1.00 84.01           O  
ATOM   1836  N   ILE A 561     201.161 213.848 189.602  1.00 81.81           N  
ATOM   1837  CA  ILE A 561     202.198 212.873 189.307  1.00 81.81           C  
ATOM   1838  C   ILE A 561     201.963 212.265 187.939  1.00 81.81           C  
ATOM   1839  O   ILE A 561     202.890 212.149 187.133  1.00 81.81           O  
ATOM   1840  CB  ILE A 561     202.253 211.797 190.402  1.00 81.81           C  
ATOM   1841  CG1 ILE A 561     202.726 212.413 191.708  1.00 81.81           C  
ATOM   1842  CG2 ILE A 561     203.183 210.690 189.998  1.00 81.81           C  
ATOM   1843  CD1 ILE A 561     203.942 213.226 191.530  1.00 81.81           C  
ATOM   1844  N   VAL A 562     200.713 211.901 187.645  1.00 81.27           N  
ATOM   1845  CA  VAL A 562     200.382 211.399 186.315  1.00 81.27           C  
ATOM   1846  C   VAL A 562     200.955 212.324 185.256  1.00 81.27           C  
ATOM   1847  O   VAL A 562     201.845 211.943 184.485  1.00 81.27           O  
ATOM   1848  CB  VAL A 562     198.863 211.259 186.149  1.00 81.27           C  
ATOM   1849  CG1 VAL A 562     198.530 211.115 184.694  1.00 81.27           C  
ATOM   1850  CG2 VAL A 562     198.359 210.076 186.923  1.00 81.27           C  
ATOM   1851  N   ILE A 563     200.511 213.584 185.271  1.00 84.56           N  
ATOM   1852  CA  ILE A 563     200.868 214.519 184.206  1.00 84.56           C  
ATOM   1853  C   ILE A 563     202.375 214.682 184.115  1.00 84.56           C  
ATOM   1854  O   ILE A 563     202.969 214.523 183.044  1.00 84.56           O  
ATOM   1855  CB  ILE A 563     200.183 215.875 184.431  1.00 84.56           C  
ATOM   1856  CG1 ILE A 563     198.704 215.796 184.074  1.00 84.56           C  
ATOM   1857  CG2 ILE A 563     200.855 216.944 183.616  1.00 84.56           C  
ATOM   1858  CD1 ILE A 563     197.975 217.096 184.259  1.00 84.56           C  
ATOM   1859  N   GLN A 564     203.024 214.966 185.238  1.00 85.69           N  
ATOM   1860  CA  GLN A 564     204.423 215.368 185.168  1.00 85.69           C  
ATOM   1861  C   GLN A 564     205.361 214.186 184.988  1.00 85.69           C  
ATOM   1862  O   GLN A 564     206.166 214.162 184.053  1.00 85.69           O  
ATOM   1863  CB  GLN A 564     204.797 216.172 186.401  1.00 85.69           C  
ATOM   1864  CG  GLN A 564     203.931 217.366 186.556  1.00 85.69           C  
ATOM   1865  CD  GLN A 564     204.581 218.595 185.978  1.00 85.69           C  
ATOM   1866  OE1 GLN A 564     205.491 218.498 185.161  1.00 85.69           O  
ATOM   1867  NE2 GLN A 564     204.120 219.761 186.396  1.00 85.69           N  
ATOM   1868  N   TYR A 565     205.420 213.326 185.991  1.00 82.20           N  
ATOM   1869  CA  TYR A 565     206.395 212.230 185.848  1.00 82.20           C  
ATOM   1870  C   TYR A 565     205.993 211.274 184.719  1.00 82.20           C  
ATOM   1871  O   TYR A 565     206.847 210.935 183.907  1.00 82.20           O  
ATOM   1872  CB  TYR A 565     206.591 211.519 187.188  1.00 82.20           C  
ATOM   1873  CG  TYR A 565     207.656 210.454 187.165  1.00 82.20           C  
ATOM   1874  CD1 TYR A 565     208.373 210.195 186.011  1.00 82.20           C  
ATOM   1875  CD2 TYR A 565     207.950 209.709 188.289  1.00 82.20           C  
ATOM   1876  CE1 TYR A 565     209.342 209.217 185.959  1.00 82.20           C  
ATOM   1877  CE2 TYR A 565     208.924 208.729 188.258  1.00 82.20           C  
ATOM   1878  CZ  TYR A 565     209.621 208.484 187.090  1.00 82.20           C  
ATOM   1879  OH  TYR A 565     210.584 207.524 187.028  1.00 82.20           O  
ATOM   1880  N   PHE A 566     204.730 210.859 184.675  1.00 78.41           N  
ATOM   1881  CA  PHE A 566     204.275 209.863 183.672  1.00 78.41           C  
ATOM   1882  C   PHE A 566     204.192 210.333 182.223  1.00 78.41           C  
ATOM   1883  O   PHE A 566     204.488 209.498 181.388  1.00 78.41           O  
ATOM   1884  CB  PHE A 566     203.073 209.066 184.164  1.00 78.41           C  
ATOM   1885  CG  PHE A 566     203.432 208.114 185.271  1.00 78.41           C  
ATOM   1886  CD1 PHE A 566     204.654 207.472 185.272  1.00 78.41           C  
ATOM   1887  CD2 PHE A 566     202.565 207.885 186.323  1.00 78.41           C  
ATOM   1888  CE1 PHE A 566     204.996 206.616 186.302  1.00 78.41           C  
ATOM   1889  CE2 PHE A 566     202.910 207.022 187.348  1.00 78.41           C  
ATOM   1890  CZ  PHE A 566     204.120 206.384 187.334  1.00 78.41           C  
ATOM   1891  N   ILE A 567     203.757 211.555 181.921  1.00 83.51           N  
ATOM   1892  CA  ILE A 567     203.642 211.916 180.473  1.00 83.51           C  
ATOM   1893  C   ILE A 567     204.644 212.983 180.039  1.00 83.51           C  
ATOM   1894  O   ILE A 567     204.726 213.184 178.844  1.00 83.51           O  
ATOM   1895  CB  ILE A 567     202.220 212.389 180.129  1.00 83.51           C  
ATOM   1896  CG1 ILE A 567     201.132 211.436 180.618  1.00 83.51           C  
ATOM   1897  CG2 ILE A 567     202.090 212.649 178.646  1.00 83.51           C  
ATOM   1898  CD1 ILE A 567     199.893 212.157 181.060  1.00 83.51           C  
ATOM   1899  N   PHE A 568     205.342 213.662 180.949  1.00 86.18           N  
ATOM   1900  CA  PHE A 568     206.240 214.757 180.491  1.00 86.18           C  
ATOM   1901  C   PHE A 568     207.709 214.341 180.388  1.00 86.18           C  
ATOM   1902  O   PHE A 568     208.316 214.561 179.336  1.00 86.18           O  
ATOM   1903  CB  PHE A 568     206.035 215.984 181.375  1.00 86.18           C  
ATOM   1904  CG  PHE A 568     205.026 216.942 180.807  1.00 86.18           C  
ATOM   1905  CD1 PHE A 568     204.966 217.164 179.444  1.00 86.18           C  
ATOM   1906  CD2 PHE A 568     204.133 217.604 181.626  1.00 86.18           C  
ATOM   1907  CE1 PHE A 568     204.037 218.038 178.912  1.00 86.18           C  
ATOM   1908  CE2 PHE A 568     203.202 218.476 181.093  1.00 86.18           C  
ATOM   1909  CZ  PHE A 568     203.158 218.693 179.739  1.00 86.18           C  
ATOM   1910  N   LEU A 569     208.251 213.760 181.453  1.00 84.74           N  
ATOM   1911  CA  LEU A 569     209.622 213.267 181.501  1.00 84.74           C  
ATOM   1912  C   LEU A 569     209.830 212.171 180.469  1.00 84.74           C  
ATOM   1913  O   LEU A 569     210.890 212.085 179.833  1.00 84.74           O  
ATOM   1914  CB  LEU A 569     209.964 212.762 182.901  1.00 84.74           C  
ATOM   1915  CG  LEU A 569     210.403 213.791 183.943  1.00 84.74           C  
ATOM   1916  CD1 LEU A 569     211.696 214.445 183.506  1.00 84.74           C  
ATOM   1917  CD2 LEU A 569     209.348 214.833 184.211  1.00 84.74           C  
ATOM   1918  N   ASN A 570     208.820 211.330 180.278  1.00 84.32           N  
ATOM   1919  CA  ASN A 570     208.910 210.347 179.216  1.00 84.32           C  
ATOM   1920  C   ASN A 570     208.964 211.015 177.852  1.00 84.32           C  
ATOM   1921  O   ASN A 570     209.542 210.460 176.918  1.00 84.32           O  
ATOM   1922  CB  ASN A 570     207.747 209.371 179.315  1.00 84.32           C  
ATOM   1923  CG  ASN A 570     207.575 208.820 180.708  1.00 84.32           C  
ATOM   1924  OD1 ASN A 570     208.547 208.529 181.392  1.00 84.32           O  
ATOM   1925  ND2 ASN A 570     206.334 208.668 181.134  1.00 84.32           N  
ATOM   1926  N   LEU A 571     208.389 212.208 177.711  1.00 85.35           N  
ATOM   1927  CA  LEU A 571     208.597 212.954 176.477  1.00 85.35           C  
ATOM   1928  C   LEU A 571     210.049 213.348 176.310  1.00 85.35           C  
ATOM   1929  O   LEU A 571     210.581 213.322 175.195  1.00 85.35           O  
ATOM   1930  CB  LEU A 571     207.735 214.203 176.429  1.00 85.35           C  
ATOM   1931  CG  LEU A 571     206.316 214.070 175.935  1.00 85.35           C  
ATOM   1932  CD1 LEU A 571     205.694 215.425 176.086  1.00 85.35           C  
ATOM   1933  CD2 LEU A 571     206.341 213.647 174.496  1.00 85.35           C  
ATOM   1934  N   VAL A 572     210.699 213.769 177.392  1.00 84.43           N  
ATOM   1935  CA  VAL A 572     212.112 214.109 177.263  1.00 84.43           C  
ATOM   1936  C   VAL A 572     212.900 212.886 176.821  1.00 84.43           C  
ATOM   1937  O   VAL A 572     213.736 212.959 175.911  1.00 84.43           O  
ATOM   1938  CB  VAL A 572     212.656 214.702 178.572  1.00 84.43           C  
ATOM   1939  CG1 VAL A 572     214.127 214.945 178.450  1.00 84.43           C  
ATOM   1940  CG2 VAL A 572     211.967 216.000 178.866  1.00 84.43           C  
ATOM   1941  N   ILE A 573     212.613 211.735 177.425  1.00 85.69           N  
ATOM   1942  CA  ILE A 573     213.305 210.507 177.035  1.00 85.69           C  
ATOM   1943  C   ILE A 573     213.039 210.187 175.568  1.00 85.69           C  
ATOM   1944  O   ILE A 573     213.956 209.848 174.810  1.00 85.69           O  
ATOM   1945  CB  ILE A 573     212.892 209.342 177.948  1.00 85.69           C  
ATOM   1946  CG1 ILE A 573     213.294 209.634 179.390  1.00 85.69           C  
ATOM   1947  CG2 ILE A 573     213.533 208.060 177.491  1.00 85.69           C  
ATOM   1948  CD1 ILE A 573     212.373 209.009 180.409  1.00 85.69           C  
ATOM   1949  N   ALA A 574     211.782 210.305 175.142  1.00 89.98           N  
ATOM   1950  CA  ALA A 574     211.425 209.977 173.768  1.00 89.98           C  
ATOM   1951  C   ALA A 574     212.124 210.887 172.772  1.00 89.98           C  
ATOM   1952  O   ALA A 574     212.661 210.420 171.761  1.00 89.98           O  
ATOM   1953  CB  ALA A 574     209.914 210.061 173.590  1.00 89.98           C  
ATOM   1954  N   VAL A 575     212.124 212.190 173.031  1.00 90.81           N  
ATOM   1955  CA  VAL A 575     212.725 213.100 172.071  1.00 90.81           C  
ATOM   1956  C   VAL A 575     214.233 212.907 172.031  1.00 90.81           C  
ATOM   1957  O   VAL A 575     214.846 212.986 170.961  1.00 90.81           O  
ATOM   1958  CB  VAL A 575     212.320 214.553 172.369  1.00 90.81           C  
ATOM   1959  CG1 VAL A 575     212.880 215.004 173.667  1.00 90.81           C  
ATOM   1960  CG2 VAL A 575     212.790 215.458 171.264  1.00 90.81           C  
ATOM   1961  N   LEU A 576     214.859 212.611 173.175  1.00 92.63           N  
ATOM   1962  CA  LEU A 576     216.291 212.329 173.148  1.00 92.63           C  
ATOM   1963  C   LEU A 576     216.597 211.075 172.340  1.00 92.63           C  
ATOM   1964  O   LEU A 576     217.557 211.052 171.554  1.00 92.63           O  
ATOM   1965  CB  LEU A 576     216.842 212.207 174.565  1.00 92.63           C  
ATOM   1966  CG  LEU A 576     217.462 213.462 175.173  1.00 92.63           C  
ATOM   1967  CD1 LEU A 576     216.418 214.457 175.567  1.00 92.63           C  
ATOM   1968  CD2 LEU A 576     218.289 213.096 176.372  1.00 92.63           C  
ATOM   1969  N   VAL A 577     215.796 210.021 172.509  1.00 97.39           N  
ATOM   1970  CA  VAL A 577     216.053 208.794 171.762  1.00 97.39           C  
ATOM   1971  C   VAL A 577     215.885 209.034 170.271  1.00 97.39           C  
ATOM   1972  O   VAL A 577     216.680 208.550 169.460  1.00 97.39           O  
ATOM   1973  CB  VAL A 577     215.147 207.655 172.253  1.00 97.39           C  
ATOM   1974  CG1 VAL A 577     215.300 206.457 171.352  1.00 97.39           C  
ATOM   1975  CG2 VAL A 577     215.497 207.284 173.673  1.00 97.39           C  
ATOM   1976  N   ASP A 578     214.857 209.789 169.883  1.00104.06           N  
ATOM   1977  CA  ASP A 578     214.672 210.069 168.463  1.00104.06           C  
ATOM   1978  C   ASP A 578     215.820 210.898 167.905  1.00104.06           C  
ATOM   1979  O   ASP A 578     216.268 210.672 166.773  1.00104.06           O  
ATOM   1980  CB  ASP A 578     213.350 210.782 168.219  1.00104.06           C  
ATOM   1981  CG  ASP A 578     213.093 211.024 166.745  1.00104.06           C  
ATOM   1982  OD1 ASP A 578     212.693 210.071 166.043  1.00104.06           O  
ATOM   1983  OD2 ASP A 578     213.300 212.164 166.283  1.00104.06           O  
ATOM   1984  N   ASN A 579     216.300 211.873 168.672  1.00104.22           N  
ATOM   1985  CA  ASN A 579     217.407 212.680 168.182  1.00104.22           C  
ATOM   1986  C   ASN A 579     218.652 211.836 167.972  1.00104.22           C  
ATOM   1987  O   ASN A 579     219.342 211.969 166.951  1.00104.22           O  
ATOM   1988  CB  ASN A 579     217.681 213.835 169.136  1.00104.22           C  
ATOM   1989  CG  ASN A 579     216.504 214.766 169.258  1.00104.22           C  
ATOM   1990  OD1 ASN A 579     216.223 215.290 170.329  1.00104.22           O  
ATOM   1991  ND2 ASN A 579     215.801 214.975 168.156  1.00104.22           N  
ATOM   1992  N   PHE A 580     218.947 210.940 168.909  1.00109.62           N  
ATOM   1993  CA  PHE A 580     220.128 210.112 168.708  1.00109.62           C  
ATOM   1994  C   PHE A 580     219.915 209.106 167.587  1.00109.62           C  
ATOM   1995  O   PHE A 580     220.874 208.719 166.914  1.00109.62           O  
ATOM   1996  CB  PHE A 580     220.521 209.425 170.004  1.00109.62           C  
ATOM   1997  CG  PHE A 580     221.412 210.261 170.868  1.00109.62           C  
ATOM   1998  CD1 PHE A 580     220.901 211.331 171.573  1.00109.62           C  
ATOM   1999  CD2 PHE A 580     222.757 209.993 170.964  1.00109.62           C  
ATOM   2000  CE1 PHE A 580     221.712 212.107 172.363  1.00109.62           C  
ATOM   2001  CE2 PHE A 580     223.568 210.771 171.752  1.00109.62           C  
ATOM   2002  CZ  PHE A 580     223.043 211.827 172.450  1.00109.62           C  
ATOM   2003  N   GLN A 581     218.671 208.700 167.339  1.00114.20           N  
ATOM   2004  CA  GLN A 581     218.409 207.872 166.168  1.00114.20           C  
ATOM   2005  C   GLN A 581     218.723 208.622 164.879  1.00114.20           C  
ATOM   2006  O   GLN A 581     219.291 208.045 163.940  1.00114.20           O  
ATOM   2007  CB  GLN A 581     216.964 207.389 166.178  1.00114.20           C  
ATOM   2008  CG  GLN A 581     216.784 206.129 166.981  1.00114.20           C  
ATOM   2009  CD  GLN A 581     217.763 205.065 166.562  1.00114.20           C  
ATOM   2010  OE1 GLN A 581     217.710 204.573 165.441  1.00114.20           O  
ATOM   2011  NE2 GLN A 581     218.673 204.710 167.454  1.00114.20           N  
ATOM   2012  N   MET A 582     218.358 209.905 164.804  1.00121.38           N  
ATOM   2013  CA  MET A 582     218.733 210.660 163.612  1.00121.38           C  
ATOM   2014  C   MET A 582     220.246 210.726 163.488  1.00121.38           C  
ATOM   2015  O   MET A 582     220.797 210.590 162.389  1.00121.38           O  
ATOM   2016  CB  MET A 582     218.183 212.086 163.610  1.00121.38           C  
ATOM   2017  CG  MET A 582     216.694 212.242 163.710  1.00121.38           C  
ATOM   2018  SD  MET A 582     216.289 213.965 164.087  1.00121.38           S  
ATOM   2019  CE  MET A 582     217.523 214.398 165.300  1.00121.38           C  
ATOM   2020  N   ALA A 583     220.931 210.958 164.609  1.00123.15           N  
ATOM   2021  CA  ALA A 583     222.390 210.990 164.579  1.00123.15           C  
ATOM   2022  C   ALA A 583     222.952 209.688 164.024  1.00123.15           C  
ATOM   2023  O   ALA A 583     223.898 209.694 163.225  1.00123.15           O  
ATOM   2024  CB  ALA A 583     222.934 211.254 165.981  1.00123.15           C  
ATOM   2025  N   LEU A 584     222.370 208.561 164.428  1.00126.26           N  
ATOM   2026  CA  LEU A 584     222.858 207.269 163.960  1.00126.26           C  
ATOM   2027  C   LEU A 584     222.615 207.079 162.469  1.00126.26           C  
ATOM   2028  O   LEU A 584     223.482 206.555 161.760  1.00126.26           O  
ATOM   2029  CB  LEU A 584     222.214 206.143 164.760  1.00126.26           C  
ATOM   2030  CG  LEU A 584     223.007 205.722 165.991  1.00126.26           C  
ATOM   2031  CD1 LEU A 584     224.299 205.072 165.554  1.00126.26           C  
ATOM   2032  CD2 LEU A 584     223.315 206.915 166.854  1.00126.26           C  
ATOM   2033  N   LEU A 585     221.443 207.476 161.971  1.00132.93           N  
ATOM   2034  CA  LEU A 585     221.213 207.322 160.536  1.00132.93           C  
ATOM   2035  C   LEU A 585     222.167 208.204 159.744  1.00132.93           C  
ATOM   2036  O   LEU A 585     222.676 207.792 158.692  1.00132.93           O  
ATOM   2037  CB  LEU A 585     219.757 207.628 160.167  1.00132.93           C  
ATOM   2038  CG  LEU A 585     219.104 208.999 160.372  1.00132.93           C  
ATOM   2039  CD1 LEU A 585     219.389 209.928 159.206  1.00132.93           C  
ATOM   2040  CD2 LEU A 585     217.605 208.864 160.574  1.00132.93           C  
ATOM   2041  N   LYS A 586     222.422 209.420 160.237  1.00138.10           N  
ATOM   2042  CA  LYS A 586     223.397 210.289 159.589  1.00138.10           C  
ATOM   2043  C   LYS A 586     224.758 209.615 159.537  1.00138.10           C  
ATOM   2044  O   LYS A 586     225.436 209.633 158.506  1.00138.10           O  
ATOM   2045  CB  LYS A 586     223.500 211.625 160.325  1.00138.10           C  
ATOM   2046  CG  LYS A 586     222.220 212.440 160.400  1.00138.10           C  
ATOM   2047  CD  LYS A 586     221.766 212.916 159.039  1.00138.10           C  
ATOM   2048  CE  LYS A 586     220.587 213.867 159.157  1.00138.10           C  
ATOM   2049  NZ  LYS A 586     219.345 213.197 159.614  1.00138.10           N  
ATOM   2050  N   GLY A 587     225.172 209.009 160.650  1.00147.76           N  
ATOM   2051  CA  GLY A 587     226.457 208.330 160.671  1.00147.76           C  
ATOM   2052  C   GLY A 587     226.519 207.155 159.715  1.00147.76           C  
ATOM   2053  O   GLY A 587     227.540 206.928 159.063  1.00147.76           O  
ATOM   2054  N   LEU A 588     225.432 206.388 159.623  1.00152.22           N  
ATOM   2055  CA  LEU A 588     225.412 205.227 158.737  1.00152.22           C  
ATOM   2056  C   LEU A 588     225.538 205.652 157.279  1.00152.22           C  
ATOM   2057  O   LEU A 588     226.362 205.115 156.524  1.00152.22           O  
ATOM   2058  CB  LEU A 588     224.128 204.425 158.956  1.00152.22           C  
ATOM   2059  CG  LEU A 588     224.149 203.239 159.923  1.00152.22           C  
ATOM   2060  CD1 LEU A 588     224.932 202.083 159.345  1.00152.22           C  
ATOM   2061  CD2 LEU A 588     224.725 203.637 161.264  1.00152.22           C  
ATOM   2062  N   GLU A 589     224.735 206.635 156.866  1.00157.78           N  
ATOM   2063  CA  GLU A 589     224.837 207.118 155.493  1.00157.78           C  
ATOM   2064  C   GLU A 589     226.191 207.766 155.232  1.00157.78           C  
ATOM   2065  O   GLU A 589     226.757 207.605 154.146  1.00157.78           O  
ATOM   2066  CB  GLU A 589     223.677 208.065 155.174  1.00157.78           C  
ATOM   2067  CG  GLU A 589     223.581 209.320 156.022  1.00157.78           C  
ATOM   2068  CD  GLU A 589     224.414 210.464 155.498  1.00157.78           C  
ATOM   2069  OE1 GLU A 589     224.780 210.441 154.304  1.00157.78           O  
ATOM   2070  OE2 GLU A 589     224.690 211.398 156.278  1.00157.78           O  
ATOM   2071  N   LYS A 590     226.746 208.473 156.222  1.00160.87           N  
ATOM   2072  CA  LYS A 590     228.050 209.101 156.036  1.00160.87           C  
ATOM   2073  C   LYS A 590     229.153 208.065 155.861  1.00160.87           C  
ATOM   2074  O   LYS A 590     230.029 208.227 155.003  1.00160.87           O  
ATOM   2075  CB  LYS A 590     228.366 210.023 157.213  1.00160.87           C  
ATOM   2076  CG  LYS A 590     227.943 211.468 157.001  1.00160.87           C  
ATOM   2077  CD  LYS A 590     228.659 212.404 157.962  1.00160.87           C  
ATOM   2078  CE  LYS A 590     228.359 213.860 157.639  1.00160.87           C  
ATOM   2079  NZ  LYS A 590     229.257 214.805 158.364  1.00160.87           N  
ATOM   2080  N   VAL A 591     229.140 207.002 156.667  1.00164.14           N  
ATOM   2081  CA  VAL A 591     230.186 205.994 156.546  1.00164.14           C  
ATOM   2082  C   VAL A 591     230.016 205.201 155.258  1.00164.14           C  
ATOM   2083  O   VAL A 591     231.000 204.719 154.685  1.00164.14           O  
ATOM   2084  CB  VAL A 591     230.222 205.082 157.787  1.00164.14           C  
ATOM   2085  CG1 VAL A 591     228.984 204.209 157.867  1.00164.14           C  
ATOM   2086  CG2 VAL A 591     231.483 204.228 157.785  1.00164.14           C  
ATOM   2087  N   LYS A 592     228.780 205.050 154.772  1.00167.59           N  
ATOM   2088  CA  LYS A 592     228.615 204.439 153.457  1.00167.59           C  
ATOM   2089  C   LYS A 592     228.999 205.391 152.332  1.00167.59           C  
ATOM   2090  O   LYS A 592     229.229 204.945 151.202  1.00167.59           O  
ATOM   2091  CB  LYS A 592     227.183 203.949 153.258  1.00167.59           C  
ATOM   2092  CG  LYS A 592     227.014 202.467 153.482  1.00167.59           C  
ATOM   2093  CD  LYS A 592     225.685 202.004 152.927  1.00167.59           C  
ATOM   2094  CE  LYS A 592     225.518 200.500 153.040  1.00167.59           C  
ATOM   2095  NZ  LYS A 592     224.238 200.055 152.421  1.00167.59           N  
ATOM   2096  N   LEU A 593     229.060 206.697 152.608  1.00170.21           N  
ATOM   2097  CA  LEU A 593     229.443 207.638 151.560  1.00170.21           C  
ATOM   2098  C   LEU A 593     230.858 207.369 151.068  1.00170.21           C  
ATOM   2099  O   LEU A 593     231.117 207.402 149.860  1.00170.21           O  
ATOM   2100  CB  LEU A 593     229.310 209.078 152.058  1.00170.21           C  
ATOM   2101  CG  LEU A 593     227.899 209.670 152.015  1.00170.21           C  
ATOM   2102  CD1 LEU A 593     227.884 211.071 152.598  1.00170.21           C  
ATOM   2103  CD2 LEU A 593     227.355 209.670 150.596  1.00170.21           C  
ATOM   2104  N   GLU A 594     231.781 207.092 151.982  1.00175.49           N  
ATOM   2105  CA  GLU A 594     233.156 206.798 151.601  1.00175.49           C  
ATOM   2106  C   GLU A 594     233.242 205.491 150.822  1.00175.49           C  
ATOM   2107  O   GLU A 594     234.278 204.828 150.823  1.00175.49           O  
ATOM   2108  CB  GLU A 594     234.057 206.729 152.833  1.00175.49           C  
ATOM   2109  CG  GLU A 594     234.188 208.035 153.595  1.00175.49           C  
ATOM   2110  CD  GLU A 594     235.327 208.000 154.594  1.00175.49           C  
ATOM   2111  OE1 GLU A 594     235.934 206.923 154.760  1.00175.49           O  
ATOM   2112  OE2 GLU A 594     235.620 209.046 155.207  1.00175.49           O  
TER    2113      GLU A 594                                                      
ATOM   2114  N   PRO B  94     174.308 247.516 160.291  1.00169.47           N  
ATOM   2115  CA  PRO B  94     175.644 246.955 160.514  1.00169.47           C  
ATOM   2116  C   PRO B  94     175.842 246.504 161.957  1.00169.47           C  
ATOM   2117  O   PRO B  94     176.656 247.088 162.670  1.00169.47           O  
ATOM   2118  CB  PRO B  94     176.569 248.124 160.175  1.00169.47           C  
ATOM   2119  CG  PRO B  94     175.766 249.335 160.519  1.00169.47           C  
ATOM   2120  CD  PRO B  94     174.327 248.989 160.235  1.00169.47           C  
ATOM   2121  N   LEU B  95     175.119 245.465 162.375  1.00169.35           N  
ATOM   2122  CA  LEU B  95     175.045 245.094 163.783  1.00169.35           C  
ATOM   2123  C   LEU B  95     176.015 243.976 164.146  1.00169.35           C  
ATOM   2124  O   LEU B  95     176.921 244.193 164.955  1.00169.35           O  
ATOM   2125  CB  LEU B  95     173.601 244.706 164.128  1.00169.35           C  
ATOM   2126  CG  LEU B  95     172.563 245.742 163.678  1.00169.35           C  
ATOM   2127  CD1 LEU B  95     171.144 245.294 163.995  1.00169.35           C  
ATOM   2128  CD2 LEU B  95     172.848 247.103 164.300  1.00169.35           C  
ATOM   2129  N   SER B  96     175.872 242.786 163.555  1.00170.51           N  
ATOM   2130  CA  SER B  96     176.869 241.743 163.777  1.00170.51           C  
ATOM   2131  C   SER B  96     178.204 242.115 163.150  1.00170.51           C  
ATOM   2132  O   SER B  96     179.261 241.678 163.626  1.00170.51           O  
ATOM   2133  CB  SER B  96     176.378 240.411 163.219  1.00170.51           C  
ATOM   2134  OG  SER B  96     175.189 240.002 163.867  1.00170.51           O  
ATOM   2135  N   LEU B  97     178.169 242.920 162.086  1.00172.30           N  
ATOM   2136  CA  LEU B  97     179.397 243.412 161.480  1.00172.30           C  
ATOM   2137  C   LEU B  97     180.226 244.196 162.481  1.00172.30           C  
ATOM   2138  O   LEU B  97     181.459 244.167 162.423  1.00172.30           O  
ATOM   2139  CB  LEU B  97     179.067 244.281 160.268  1.00172.30           C  
ATOM   2140  CG  LEU B  97     178.038 243.722 159.280  1.00172.30           C  
ATOM   2141  CD1 LEU B  97     177.593 244.803 158.316  1.00172.30           C  
ATOM   2142  CD2 LEU B  97     178.592 242.526 158.523  1.00172.30           C  
ATOM   2143  N   TRP B  98     179.573 244.879 163.420  1.00175.73           N  
ATOM   2144  CA  TRP B  98     180.309 245.625 164.433  1.00175.73           C  
ATOM   2145  C   TRP B  98     181.157 244.704 165.303  1.00175.73           C  
ATOM   2146  O   TRP B  98     182.360 244.937 165.489  1.00175.73           O  
ATOM   2147  CB  TRP B  98     179.341 246.426 165.300  1.00175.73           C  
ATOM   2148  CG  TRP B  98     180.056 247.169 166.367  1.00175.73           C  
ATOM   2149  CD1 TRP B  98     179.853 247.073 167.712  1.00175.73           C  
ATOM   2150  CD2 TRP B  98     181.126 248.100 166.187  1.00175.73           C  
ATOM   2151  NE1 TRP B  98     180.720 247.902 168.380  1.00175.73           N  
ATOM   2152  CE2 TRP B  98     181.513 248.544 167.465  1.00175.73           C  
ATOM   2153  CE3 TRP B  98     181.787 248.613 165.065  1.00175.73           C  
ATOM   2154  CZ2 TRP B  98     182.529 249.476 167.654  1.00175.73           C  
ATOM   2155  CZ3 TRP B  98     182.793 249.530 165.254  1.00175.73           C  
ATOM   2156  CH2 TRP B  98     183.163 249.946 166.536  1.00175.73           C  
ATOM   2157  N   ALA B  99     180.534 243.665 165.869  1.00173.78           N  
ATOM   2158  CA  ALA B  99     181.269 242.728 166.711  1.00173.78           C  
ATOM   2159  C   ALA B  99     182.346 242.015 165.912  1.00173.78           C  
ATOM   2160  O   ALA B  99     183.474 241.839 166.390  1.00173.78           O  
ATOM   2161  CB  ALA B  99     180.311 241.720 167.340  1.00173.78           C  
ATOM   2162  N   GLY B 100     182.018 241.613 164.683  1.00172.68           N  
ATOM   2163  CA  GLY B 100     183.021 241.005 163.828  1.00172.68           C  
ATOM   2164  C   GLY B 100     184.224 241.901 163.612  1.00172.68           C  
ATOM   2165  O   GLY B 100     185.366 241.440 163.657  1.00172.68           O  
ATOM   2166  N   TRP B 101     183.989 243.195 163.383  1.00173.55           N  
ATOM   2167  CA  TRP B 101     185.107 244.105 163.165  1.00173.55           C  
ATOM   2168  C   TRP B 101     185.939 244.281 164.425  1.00173.55           C  
ATOM   2169  O   TRP B 101     187.170 244.163 164.388  1.00173.55           O  
ATOM   2170  CB  TRP B 101     184.627 245.471 162.688  1.00173.55           C  
ATOM   2171  CG  TRP B 101     185.800 246.357 162.450  1.00173.55           C  
ATOM   2172  CD1 TRP B 101     186.770 246.189 161.508  1.00173.55           C  
ATOM   2173  CD2 TRP B 101     186.186 247.498 163.223  1.00173.55           C  
ATOM   2174  NE1 TRP B 101     187.714 247.183 161.614  1.00173.55           N  
ATOM   2175  CE2 TRP B 101     187.379 247.998 162.663  1.00173.55           C  
ATOM   2176  CE3 TRP B 101     185.629 248.158 164.318  1.00173.55           C  
ATOM   2177  CZ2 TRP B 101     188.024 249.127 163.162  1.00173.55           C  
ATOM   2178  CZ3 TRP B 101     186.269 249.281 164.813  1.00173.55           C  
ATOM   2179  CH2 TRP B 101     187.454 249.753 164.234  1.00173.55           C  
ATOM   2180  N   VAL B 102     185.291 244.591 165.549  1.00171.05           N  
ATOM   2181  CA  VAL B 102     186.058 244.929 166.743  1.00171.05           C  
ATOM   2182  C   VAL B 102     186.847 243.723 167.226  1.00171.05           C  
ATOM   2183  O   VAL B 102     187.999 243.850 167.659  1.00171.05           O  
ATOM   2184  CB  VAL B 102     185.148 245.492 167.850  1.00171.05           C  
ATOM   2185  CG1 VAL B 102     184.641 246.854 167.456  1.00171.05           C  
ATOM   2186  CG2 VAL B 102     184.001 244.550 168.146  1.00171.05           C  
ATOM   2187  N   LEU B 103     186.256 242.531 167.132  1.00168.11           N  
ATOM   2188  CA  LEU B 103     186.958 241.327 167.551  1.00168.11           C  
ATOM   2189  C   LEU B 103     188.121 240.995 166.632  1.00168.11           C  
ATOM   2190  O   LEU B 103     188.789 239.977 166.840  1.00168.11           O  
ATOM   2191  CB  LEU B 103     185.981 240.160 167.606  1.00168.11           C  
ATOM   2192  CG  LEU B 103     185.296 239.899 168.943  1.00168.11           C  
ATOM   2193  CD1 LEU B 103     184.569 241.129 169.423  1.00168.11           C  
ATOM   2194  CD2 LEU B 103     184.319 238.771 168.747  1.00168.11           C  
ATOM   2195  N   ASP B 104     188.372 241.827 165.622  1.00169.10           N  
ATOM   2196  CA  ASP B 104     189.415 241.562 164.643  1.00169.10           C  
ATOM   2197  C   ASP B 104     190.608 242.502 164.773  1.00169.10           C  
ATOM   2198  O   ASP B 104     191.675 242.199 164.231  1.00169.10           O  
ATOM   2199  CB  ASP B 104     188.818 241.653 163.239  1.00169.10           C  
ATOM   2200  CG  ASP B 104     189.590 240.849 162.226  1.00169.10           C  
ATOM   2201  OD1 ASP B 104     189.550 239.604 162.304  1.00169.10           O  
ATOM   2202  OD2 ASP B 104     190.220 241.464 161.340  1.00169.10           O  
ATOM   2203  N   SER B 105     190.457 243.629 165.467  1.00161.09           N  
ATOM   2204  CA  SER B 105     191.567 244.559 165.632  1.00161.09           C  
ATOM   2205  C   SER B 105     192.717 243.893 166.376  1.00161.09           C  
ATOM   2206  O   SER B 105     192.510 243.174 167.358  1.00161.09           O  
ATOM   2207  CB  SER B 105     191.106 245.806 166.385  1.00161.09           C  
ATOM   2208  OG  SER B 105     189.924 246.335 165.813  1.00161.09           O  
ATOM   2209  N   SER B 106     193.942 244.139 165.900  1.00155.58           N  
ATOM   2210  CA  SER B 106     195.106 243.451 166.451  1.00155.58           C  
ATOM   2211  C   SER B 106     195.590 244.091 167.747  1.00155.58           C  
ATOM   2212  O   SER B 106     196.036 243.385 168.658  1.00155.58           O  
ATOM   2213  CB  SER B 106     196.237 243.419 165.426  1.00155.58           C  
ATOM   2214  OG  SER B 106     197.329 242.652 165.904  1.00155.58           O  
ATOM   2215  N   VAL B 107     195.528 245.421 167.847  1.00151.69           N  
ATOM   2216  CA  VAL B 107     195.840 246.074 169.115  1.00151.69           C  
ATOM   2217  C   VAL B 107     194.805 245.699 170.169  1.00151.69           C  
ATOM   2218  O   VAL B 107     195.129 245.546 171.351  1.00151.69           O  
ATOM   2219  CB  VAL B 107     195.940 247.600 168.916  1.00151.69           C  
ATOM   2220  CG1 VAL B 107     196.011 248.322 170.255  1.00151.69           C  
ATOM   2221  CG2 VAL B 107     197.148 247.939 168.059  1.00151.69           C  
ATOM   2222  N   PHE B 108     193.553 245.526 169.752  1.00153.33           N  
ATOM   2223  CA  PHE B 108     192.505 245.064 170.654  1.00153.33           C  
ATOM   2224  C   PHE B 108     192.821 243.674 171.202  1.00153.33           C  
ATOM   2225  O   PHE B 108     192.675 243.418 172.405  1.00153.33           O  
ATOM   2226  CB  PHE B 108     191.181 245.099 169.886  1.00153.33           C  
ATOM   2227  CG  PHE B 108     190.009 244.504 170.602  1.00153.33           C  
ATOM   2228  CD1 PHE B 108     189.801 243.136 170.626  1.00153.33           C  
ATOM   2229  CD2 PHE B 108     189.073 245.327 171.194  1.00153.33           C  
ATOM   2230  CE1 PHE B 108     188.706 242.605 171.262  1.00153.33           C  
ATOM   2231  CE2 PHE B 108     187.974 244.798 171.827  1.00153.33           C  
ATOM   2232  CZ  PHE B 108     187.791 243.438 171.859  1.00153.33           C  
ATOM   2233  N   SER B 109     193.266 242.763 170.334  1.00150.56           N  
ATOM   2234  CA  SER B 109     193.633 241.424 170.788  1.00150.56           C  
ATOM   2235  C   SER B 109     194.877 241.453 171.670  1.00150.56           C  
ATOM   2236  O   SER B 109     194.969 240.705 172.652  1.00150.56           O  
ATOM   2237  CB  SER B 109     193.850 240.507 169.588  1.00150.56           C  
ATOM   2238  OG  SER B 109     194.973 240.926 168.833  1.00150.56           O  
ATOM   2239  N   LYS B 110     195.858 242.285 171.322  1.00148.87           N  
ATOM   2240  CA  LYS B 110     197.021 242.443 172.187  1.00148.87           C  
ATOM   2241  C   LYS B 110     196.593 242.919 173.565  1.00148.87           C  
ATOM   2242  O   LYS B 110     197.089 242.433 174.590  1.00148.87           O  
ATOM   2243  CB  LYS B 110     198.011 243.423 171.555  1.00148.87           C  
ATOM   2244  CG  LYS B 110     199.323 243.571 172.306  1.00148.87           C  
ATOM   2245  CD  LYS B 110     200.441 244.048 171.387  1.00148.87           C  
ATOM   2246  CE  LYS B 110     201.003 242.895 170.564  1.00148.87           C  
ATOM   2247  NZ  LYS B 110     202.335 243.206 169.979  1.00148.87           N  
ATOM   2248  N   PHE B 111     195.636 243.843 173.608  1.00147.48           N  
ATOM   2249  CA  PHE B 111     195.106 244.288 174.885  1.00147.48           C  
ATOM   2250  C   PHE B 111     194.457 243.138 175.645  1.00147.48           C  
ATOM   2251  O   PHE B 111     194.709 242.968 176.839  1.00147.48           O  
ATOM   2252  CB  PHE B 111     194.114 245.429 174.675  1.00147.48           C  
ATOM   2253  CG  PHE B 111     193.949 246.311 175.876  1.00147.48           C  
ATOM   2254  CD1 PHE B 111     195.036 246.993 176.401  1.00147.48           C  
ATOM   2255  CD2 PHE B 111     192.714 246.452 176.486  1.00147.48           C  
ATOM   2256  CE1 PHE B 111     194.895 247.803 177.507  1.00147.48           C  
ATOM   2257  CE2 PHE B 111     192.565 247.263 177.594  1.00147.48           C  
ATOM   2258  CZ  PHE B 111     193.658 247.938 178.106  1.00147.48           C  
ATOM   2259  N   ILE B 112     193.640 242.320 174.976  1.00147.56           N  
ATOM   2260  CA  ILE B 112     192.932 241.293 175.743  1.00147.56           C  
ATOM   2261  C   ILE B 112     193.904 240.239 176.253  1.00147.56           C  
ATOM   2262  O   ILE B 112     193.724 239.699 177.353  1.00147.56           O  
ATOM   2263  CB  ILE B 112     191.790 240.640 174.944  1.00147.56           C  
ATOM   2264  CG1 ILE B 112     192.312 239.864 173.745  1.00147.56           C  
ATOM   2265  CG2 ILE B 112     190.859 241.703 174.443  1.00147.56           C  
ATOM   2266  CD1 ILE B 112     191.265 239.016 173.073  1.00147.56           C  
ATOM   2267  N   ILE B 113     194.947 239.919 175.483  1.00147.18           N  
ATOM   2268  CA  ILE B 113     195.926 238.973 176.010  1.00147.18           C  
ATOM   2269  C   ILE B 113     196.685 239.603 177.172  1.00147.18           C  
ATOM   2270  O   ILE B 113     197.078 238.906 178.119  1.00147.18           O  
ATOM   2271  CB  ILE B 113     196.869 238.452 174.905  1.00147.18           C  
ATOM   2272  CG1 ILE B 113     197.833 239.533 174.421  1.00147.18           C  
ATOM   2273  CG2 ILE B 113     196.069 237.882 173.748  1.00147.18           C  
ATOM   2274  CD1 ILE B 113     198.874 239.029 173.447  1.00147.18           C  
ATOM   2275  N   SER B 114     196.791 240.937 177.135  1.00147.97           N  
ATOM   2276  CA  SER B 114     197.398 241.705 178.252  1.00147.97           C  
ATOM   2277  C   SER B 114     196.511 241.487 179.484  1.00147.97           C  
ATOM   2278  O   SER B 114     197.062 241.247 180.577  1.00147.97           O  
ATOM   2279  CB  SER B 114     197.499 243.166 177.900  1.00147.97           C  
ATOM   2280  OG  SER B 114     198.079 243.902 178.967  1.00147.97           O  
ATOM   2281  N   LEU B 115     195.184 241.533 179.293  1.00148.29           N  
ATOM   2282  CA  LEU B 115     194.228 241.271 180.370  1.00148.29           C  
ATOM   2283  C   LEU B 115     194.370 239.861 180.925  1.00148.29           C  
ATOM   2284  O   LEU B 115     194.273 239.657 182.140  1.00148.29           O  
ATOM   2285  CB  LEU B 115     192.788 241.500 179.913  1.00148.29           C  
ATOM   2286  CG  LEU B 115     192.152 242.890 179.820  1.00148.29           C  
ATOM   2287  CD1 LEU B 115     192.786 243.833 178.836  1.00148.29           C  
ATOM   2288  CD2 LEU B 115     190.682 242.707 179.485  1.00148.29           C  
ATOM   2289  N   ILE B 116     194.563 238.872 180.056  1.00151.59           N  
ATOM   2290  CA  ILE B 116     194.723 237.503 180.547  1.00151.59           C  
ATOM   2291  C   ILE B 116     195.983 237.389 181.402  1.00151.59           C  
ATOM   2292  O   ILE B 116     195.954 236.877 182.530  1.00151.59           O  
ATOM   2293  CB  ILE B 116     194.747 236.504 179.379  1.00151.59           C  
ATOM   2294  CG1 ILE B 116     193.615 236.801 178.402  1.00151.59           C  
ATOM   2295  CG2 ILE B 116     194.619 235.088 179.905  1.00151.59           C  
ATOM   2296  CD1 ILE B 116     193.821 236.191 177.037  1.00151.59           C  
ATOM   2297  N   PHE B 117     197.108 237.871 180.878  1.00154.32           N  
ATOM   2298  CA  PHE B 117     198.356 237.846 181.635  1.00154.32           C  
ATOM   2299  C   PHE B 117     198.191 238.544 182.984  1.00154.32           C  
ATOM   2300  O   PHE B 117     198.634 238.041 184.028  1.00154.32           O  
ATOM   2301  CB  PHE B 117     199.454 238.489 180.779  1.00154.32           C  
ATOM   2302  CG  PHE B 117     200.720 238.810 181.518  1.00154.32           C  
ATOM   2303  CD1 PHE B 117     201.479 237.812 182.099  1.00154.32           C  
ATOM   2304  CD2 PHE B 117     201.181 240.114 181.576  1.00154.32           C  
ATOM   2305  CE1 PHE B 117     202.651 238.115 182.758  1.00154.32           C  
ATOM   2306  CE2 PHE B 117     202.348 240.421 182.232  1.00154.32           C  
ATOM   2307  CZ  PHE B 117     203.085 239.421 182.826  1.00154.32           C  
ATOM   2308  N   LEU B 118     197.490 239.676 182.988  1.00152.75           N  
ATOM   2309  CA  LEU B 118     197.342 240.449 184.213  1.00152.75           C  
ATOM   2310  C   LEU B 118     196.416 239.775 185.212  1.00152.75           C  
ATOM   2311  O   LEU B 118     196.678 239.831 186.413  1.00152.75           O  
ATOM   2312  CB  LEU B 118     196.861 241.865 183.905  1.00152.75           C  
ATOM   2313  CG  LEU B 118     197.958 242.912 183.694  1.00152.75           C  
ATOM   2314  CD1 LEU B 118     198.754 243.063 184.973  1.00152.75           C  
ATOM   2315  CD2 LEU B 118     198.883 242.573 182.547  1.00152.75           C  
ATOM   2316  N   ASN B 119     195.318 239.154 184.772  1.00156.39           N  
ATOM   2317  CA  ASN B 119     194.470 238.539 185.790  1.00156.39           C  
ATOM   2318  C   ASN B 119     195.185 237.340 186.386  1.00156.39           C  
ATOM   2319  O   ASN B 119     195.094 237.086 187.598  1.00156.39           O  
ATOM   2320  CB  ASN B 119     193.083 238.149 185.255  1.00156.39           C  
ATOM   2321  CG  ASN B 119     193.099 236.990 184.273  1.00156.39           C  
ATOM   2322  OD1 ASN B 119     194.105 236.327 184.070  1.00156.39           O  
ATOM   2323  ND2 ASN B 119     191.949 236.733 183.671  1.00156.39           N  
ATOM   2324  N   THR B 120     195.940 236.620 185.550  1.00156.80           N  
ATOM   2325  CA  THR B 120     196.760 235.538 186.074  1.00156.80           C  
ATOM   2326  C   THR B 120     197.692 236.047 187.160  1.00156.80           C  
ATOM   2327  O   THR B 120     197.755 235.469 188.248  1.00156.80           O  
ATOM   2328  CB  THR B 120     197.559 234.875 184.951  1.00156.80           C  
ATOM   2329  OG1 THR B 120     198.363 235.855 184.285  1.00156.80           O  
ATOM   2330  CG2 THR B 120     196.630 234.228 183.952  1.00156.80           C  
ATOM   2331  N   PHE B 121     198.390 237.152 186.905  1.00154.86           N  
ATOM   2332  CA  PHE B 121     199.371 237.615 187.878  1.00154.86           C  
ATOM   2333  C   PHE B 121     198.785 238.464 189.000  1.00154.86           C  
ATOM   2334  O   PHE B 121     199.509 238.780 189.948  1.00154.86           O  
ATOM   2335  CB  PHE B 121     200.497 238.380 187.179  1.00154.86           C  
ATOM   2336  CG  PHE B 121     201.705 237.532 186.888  1.00154.86           C  
ATOM   2337  CD1 PHE B 121     201.787 236.793 185.723  1.00154.86           C  
ATOM   2338  CD2 PHE B 121     202.744 237.448 187.801  1.00154.86           C  
ATOM   2339  CE1 PHE B 121     202.889 236.004 185.463  1.00154.86           C  
ATOM   2340  CE2 PHE B 121     203.849 236.664 187.542  1.00154.86           C  
ATOM   2341  CZ  PHE B 121     203.920 235.940 186.373  1.00154.86           C  
ATOM   2342  N   VAL B 122     197.510 238.839 188.933  1.00157.06           N  
ATOM   2343  CA  VAL B 122     196.910 239.547 190.059  1.00157.06           C  
ATOM   2344  C   VAL B 122     196.215 238.584 191.010  1.00157.06           C  
ATOM   2345  O   VAL B 122     196.135 238.861 192.211  1.00157.06           O  
ATOM   2346  CB  VAL B 122     195.932 240.647 189.610  1.00157.06           C  
ATOM   2347  CG1 VAL B 122     196.649 241.713 188.788  1.00157.06           C  
ATOM   2348  CG2 VAL B 122     194.729 240.064 188.895  1.00157.06           C  
ATOM   2349  N   LEU B 123     195.699 237.458 190.509  1.00157.61           N  
ATOM   2350  CA  LEU B 123     195.264 236.422 191.436  1.00157.61           C  
ATOM   2351  C   LEU B 123     196.425 235.897 192.267  1.00157.61           C  
ATOM   2352  O   LEU B 123     196.219 235.471 193.409  1.00157.61           O  
ATOM   2353  CB  LEU B 123     194.594 235.271 190.695  1.00157.61           C  
ATOM   2354  CG  LEU B 123     193.817 234.390 191.668  1.00157.61           C  
ATOM   2355  CD1 LEU B 123     192.768 235.217 192.376  1.00157.61           C  
ATOM   2356  CD2 LEU B 123     193.186 233.213 190.970  1.00157.61           C  
ATOM   2357  N   MET B 124     197.639 235.934 191.722  1.00155.28           N  
ATOM   2358  CA  MET B 124     198.818 235.501 192.461  1.00155.28           C  
ATOM   2359  C   MET B 124     198.999 236.339 193.714  1.00155.28           C  
ATOM   2360  O   MET B 124     198.913 235.838 194.840  1.00155.28           O  
ATOM   2361  CB  MET B 124     200.047 235.647 191.572  1.00155.28           C  
ATOM   2362  CG  MET B 124     199.891 234.992 190.242  1.00155.28           C  
ATOM   2363  SD  MET B 124     201.385 234.445 189.435  1.00155.28           S  
ATOM   2364  CE  MET B 124     200.678 234.041 187.841  1.00155.28           C  
ATOM   2365  N   VAL B 125     199.246 237.635 193.527  1.00159.32           N  
ATOM   2366  CA  VAL B 125     199.568 238.508 194.642  1.00159.32           C  
ATOM   2367  C   VAL B 125     198.366 238.722 195.547  1.00159.32           C  
ATOM   2368  O   VAL B 125     198.532 239.156 196.693  1.00159.32           O  
ATOM   2369  CB  VAL B 125     200.117 239.835 194.096  1.00159.32           C  
ATOM   2370  CG1 VAL B 125     199.045 240.574 193.321  1.00159.32           C  
ATOM   2371  CG2 VAL B 125     200.710 240.685 195.194  1.00159.32           C  
ATOM   2372  N   GLU B 126     197.155 238.413 195.078  1.00161.92           N  
ATOM   2373  CA  GLU B 126     195.999 238.487 195.963  1.00161.92           C  
ATOM   2374  C   GLU B 126     196.171 237.552 197.149  1.00161.92           C  
ATOM   2375  O   GLU B 126     196.317 238.002 198.289  1.00161.92           O  
ATOM   2376  CB  GLU B 126     194.713 238.151 195.210  1.00161.92           C  
ATOM   2377  CG  GLU B 126     193.553 237.828 196.146  1.00161.92           C  
ATOM   2378  CD  GLU B 126     192.305 237.365 195.426  1.00161.92           C  
ATOM   2379  OE1 GLU B 126     191.956 236.172 195.544  1.00161.92           O  
ATOM   2380  OE2 GLU B 126     191.660 238.198 194.756  1.00161.92           O  
ATOM   2381  N   ILE B 127     196.219 236.243 196.886  1.00159.21           N  
ATOM   2382  CA  ILE B 127     196.219 235.249 197.954  1.00159.21           C  
ATOM   2383  C   ILE B 127     197.418 235.434 198.871  1.00159.21           C  
ATOM   2384  O   ILE B 127     197.386 235.031 200.040  1.00159.21           O  
ATOM   2385  CB  ILE B 127     196.166 233.833 197.344  1.00159.21           C  
ATOM   2386  CG1 ILE B 127     196.059 232.763 198.432  1.00159.21           C  
ATOM   2387  CG2 ILE B 127     197.371 233.585 196.457  1.00159.21           C  
ATOM   2388  CD1 ILE B 127     194.949 233.005 199.423  1.00159.21           C  
ATOM   2389  N   GLU B 128     198.479 236.065 198.380  1.00161.69           N  
ATOM   2390  CA  GLU B 128     199.632 236.321 199.229  1.00161.69           C  
ATOM   2391  C   GLU B 128     199.394 237.469 200.204  1.00161.69           C  
ATOM   2392  O   GLU B 128     199.905 237.432 201.329  1.00161.69           O  
ATOM   2393  CB  GLU B 128     200.862 236.609 198.364  1.00161.69           C  
ATOM   2394  CG  GLU B 128     202.078 237.057 199.152  1.00161.69           C  
ATOM   2395  CD  GLU B 128     203.367 236.891 198.385  1.00161.69           C  
ATOM   2396  OE1 GLU B 128     203.351 236.197 197.347  1.00161.69           O  
ATOM   2397  OE2 GLU B 128     204.394 237.451 198.825  1.00161.69           O  
ATOM   2398  N   LEU B 129     198.618 238.481 199.817  1.00166.88           N  
ATOM   2399  CA  LEU B 129     198.587 239.737 200.555  1.00166.88           C  
ATOM   2400  C   LEU B 129     197.315 239.939 201.372  1.00166.88           C  
ATOM   2401  O   LEU B 129     196.883 241.081 201.549  1.00166.88           O  
ATOM   2402  CB  LEU B 129     198.786 240.922 199.612  1.00166.88           C  
ATOM   2403  CG  LEU B 129     200.206 241.176 199.099  1.00166.88           C  
ATOM   2404  CD1 LEU B 129     200.223 242.401 198.206  1.00166.88           C  
ATOM   2405  CD2 LEU B 129     201.200 241.320 200.240  1.00166.88           C  
ATOM   2406  N   MET B 130     196.702 238.873 201.876  1.00166.93           N  
ATOM   2407  CA  MET B 130     195.753 239.045 202.978  1.00166.93           C  
ATOM   2408  C   MET B 130     196.433 238.800 204.320  1.00166.93           C  
ATOM   2409  O   MET B 130     196.043 237.938 205.107  1.00166.93           O  
ATOM   2410  CB  MET B 130     194.531 238.151 202.808  1.00166.93           C  
ATOM   2411  CG  MET B 130     193.750 238.382 201.533  1.00166.93           C  
ATOM   2412  SD  MET B 130     194.183 237.269 200.197  1.00166.93           S  
ATOM   2413  CE  MET B 130     193.084 235.900 200.532  1.00166.93           C  
ATOM   2414  N   GLU B 131     197.474 239.580 204.578  1.00168.70           N  
ATOM   2415  CA  GLU B 131     198.257 239.491 205.800  1.00168.70           C  
ATOM   2416  C   GLU B 131     198.007 240.746 206.625  1.00168.70           C  
ATOM   2417  O   GLU B 131     198.170 241.865 206.125  1.00168.70           O  
ATOM   2418  CB  GLU B 131     199.743 239.344 205.480  1.00168.70           C  
ATOM   2419  CG  GLU B 131     200.614 239.162 206.700  1.00168.70           C  
ATOM   2420  CD  GLU B 131     202.083 238.984 206.363  1.00168.70           C  
ATOM   2421  OE1 GLU B 131     202.437 239.028 205.166  1.00168.70           O  
ATOM   2422  OE2 GLU B 131     202.887 238.798 207.300  1.00168.70           O  
ATOM   2423  N   SER B 132     197.616 240.563 207.882  1.00170.33           N  
ATOM   2424  CA  SER B 132     197.333 241.681 208.771  1.00170.33           C  
ATOM   2425  C   SER B 132     198.582 242.254 209.419  1.00170.33           C  
ATOM   2426  O   SER B 132     198.475 242.892 210.471  1.00170.33           O  
ATOM   2427  CB  SER B 132     196.341 241.260 209.855  1.00170.33           C  
ATOM   2428  OG  SER B 132     195.912 242.384 210.606  1.00170.33           O  
ATOM   2429  N   THR B 133     199.754 242.045 208.827  1.00171.16           N  
ATOM   2430  CA  THR B 133     201.017 242.485 209.419  1.00171.16           C  
ATOM   2431  C   THR B 133     201.354 243.912 208.983  1.00171.16           C  
ATOM   2432  O   THR B 133     202.435 244.440 209.250  1.00171.16           O  
ATOM   2433  CB  THR B 133     202.123 241.499 209.043  1.00171.16           C  
ATOM   2434  OG1 THR B 133     201.694 240.170 209.359  1.00171.16           O  
ATOM   2435  CG2 THR B 133     203.411 241.759 209.824  1.00171.16           C  
ATOM   2436  N   ASN B 134     200.391 244.583 208.356  1.00166.14           N  
ATOM   2437  CA  ASN B 134     200.614 245.938 207.868  1.00166.14           C  
ATOM   2438  C   ASN B 134     199.280 246.661 207.767  1.00166.14           C  
ATOM   2439  O   ASN B 134     198.208 246.057 207.854  1.00166.14           O  
ATOM   2440  CB  ASN B 134     201.319 245.951 206.506  1.00166.14           C  
ATOM   2441  CG  ASN B 134     202.720 245.387 206.566  1.00166.14           C  
ATOM   2442  OD1 ASN B 134     203.014 244.352 205.968  1.00166.14           O  
ATOM   2443  ND2 ASN B 134     203.594 246.064 207.299  1.00166.14           N  
ATOM   2444  N   THR B 135     199.372 247.976 207.591  1.00159.16           N  
ATOM   2445  CA  THR B 135     198.248 248.828 207.240  1.00159.16           C  
ATOM   2446  C   THR B 135     198.437 249.508 205.893  1.00159.16           C  
ATOM   2447  O   THR B 135     197.451 249.887 205.256  1.00159.16           O  
ATOM   2448  CB  THR B 135     198.028 249.887 208.332  1.00159.16           C  
ATOM   2449  OG1 THR B 135     197.947 249.235 209.603  1.00159.16           O  
ATOM   2450  CG2 THR B 135     196.731 250.653 208.101  1.00159.16           C  
ATOM   2451  N   ALA B 136     199.679 249.631 205.424  1.00159.51           N  
ATOM   2452  CA  ALA B 136     199.949 250.108 204.075  1.00159.51           C  
ATOM   2453  C   ALA B 136     199.522 249.111 203.007  1.00159.51           C  
ATOM   2454  O   ALA B 136     199.573 249.443 201.819  1.00159.51           O  
ATOM   2455  CB  ALA B 136     201.435 250.425 203.922  1.00159.51           C  
ATOM   2456  N   LEU B 137     199.135 247.896 203.398  1.00158.75           N  
ATOM   2457  CA  LEU B 137     198.628 246.911 202.453  1.00158.75           C  
ATOM   2458  C   LEU B 137     197.150 247.098 202.144  1.00158.75           C  
ATOM   2459  O   LEU B 137     196.669 246.562 201.142  1.00158.75           O  
ATOM   2460  CB  LEU B 137     198.859 245.502 202.995  1.00158.75           C  
ATOM   2461  CG  LEU B 137     200.314 245.052 203.138  1.00158.75           C  
ATOM   2462  CD1 LEU B 137     200.378 243.687 203.819  1.00158.75           C  
ATOM   2463  CD2 LEU B 137     201.022 245.024 201.788  1.00158.75           C  
ATOM   2464  N   TRP B 138     196.483 247.927 202.955  1.00154.33           N  
ATOM   2465  CA  TRP B 138     195.050 248.269 202.751  1.00154.33           C  
ATOM   2466  C   TRP B 138     194.878 249.011 201.417  1.00154.33           C  
ATOM   2467  O   TRP B 138     193.901 248.706 200.705  1.00154.33           O  
ATOM   2468  CB  TRP B 138     194.520 249.095 203.930  1.00154.33           C  
ATOM   2469  CG  TRP B 138     193.269 249.859 203.620  1.00154.33           C  
ATOM   2470  CD1 TRP B 138     191.994 249.532 203.982  1.00154.33           C  
ATOM   2471  CD2 TRP B 138     193.170 251.088 202.877  1.00154.33           C  
ATOM   2472  NE1 TRP B 138     191.112 250.470 203.518  1.00154.33           N  
ATOM   2473  CE2 TRP B 138     191.803 251.436 202.837  1.00154.33           C  
ATOM   2474  CE3 TRP B 138     194.097 251.924 202.246  1.00154.33           C  
ATOM   2475  CZ2 TRP B 138     191.348 252.584 202.190  1.00154.33           C  
ATOM   2476  CZ3 TRP B 138     193.646 253.057 201.607  1.00154.33           C  
ATOM   2477  CH2 TRP B 138     192.289 253.381 201.581  1.00154.33           C  
ATOM   2478  N   PRO B 139     195.788 249.940 201.087  1.00155.77           N  
ATOM   2479  CA  PRO B 139     195.678 250.669 199.812  1.00155.77           C  
ATOM   2480  C   PRO B 139     195.826 249.814 198.563  1.00155.77           C  
ATOM   2481  O   PRO B 139     195.336 250.215 197.501  1.00155.77           O  
ATOM   2482  CB  PRO B 139     196.806 251.701 199.921  1.00155.77           C  
ATOM   2483  CG  PRO B 139     196.856 251.996 201.357  1.00155.77           C  
ATOM   2484  CD  PRO B 139     196.671 250.662 202.022  1.00155.77           C  
ATOM   2485  N   VAL B 140     196.507 248.671 198.626  1.00157.07           N  
ATOM   2486  CA  VAL B 140     196.612 247.836 197.433  1.00157.07           C  
ATOM   2487  C   VAL B 140     195.549 246.742 197.385  1.00157.07           C  
ATOM   2488  O   VAL B 140     195.307 246.176 196.308  1.00157.07           O  
ATOM   2489  CB  VAL B 140     198.011 247.210 197.313  1.00157.07           C  
ATOM   2490  CG1 VAL B 140     199.040 248.280 196.996  1.00157.07           C  
ATOM   2491  CG2 VAL B 140     198.374 246.476 198.578  1.00157.07           C  
ATOM   2492  N   LYS B 141     194.903 246.436 198.513  1.00156.41           N  
ATOM   2493  CA  LYS B 141     193.851 245.425 198.518  1.00156.41           C  
ATOM   2494  C   LYS B 141     192.740 245.796 197.544  1.00156.41           C  
ATOM   2495  O   LYS B 141     192.358 244.996 196.679  1.00156.41           O  
ATOM   2496  CB  LYS B 141     193.305 245.255 199.940  1.00156.41           C  
ATOM   2497  CG  LYS B 141     192.258 244.144 200.126  1.00156.41           C  
ATOM   2498  CD  LYS B 141     190.825 244.606 199.865  1.00156.41           C  
ATOM   2499  CE  LYS B 141     190.255 245.374 201.052  1.00156.41           C  
ATOM   2500  NZ  LYS B 141     188.922 245.981 200.761  1.00156.41           N  
ATOM   2501  N   LEU B 142     192.221 247.019 197.658  1.00157.39           N  
ATOM   2502  CA  LEU B 142     191.153 247.433 196.759  1.00157.39           C  
ATOM   2503  C   LEU B 142     191.648 247.580 195.328  1.00157.39           C  
ATOM   2504  O   LEU B 142     190.895 247.306 194.393  1.00157.39           O  
ATOM   2505  CB  LEU B 142     190.511 248.744 197.220  1.00157.39           C  
ATOM   2506  CG  LEU B 142     191.293 250.046 197.052  1.00157.39           C  
ATOM   2507  CD1 LEU B 142     190.366 251.229 197.199  1.00157.39           C  
ATOM   2508  CD2 LEU B 142     192.382 250.133 198.093  1.00157.39           C  
ATOM   2509  N   ALA B 143     192.893 248.016 195.129  1.00157.08           N  
ATOM   2510  CA  ALA B 143     193.409 248.113 193.769  1.00157.08           C  
ATOM   2511  C   ALA B 143     193.376 246.753 193.089  1.00157.08           C  
ATOM   2512  O   ALA B 143     192.865 246.608 191.970  1.00157.08           O  
ATOM   2513  CB  ALA B 143     194.830 248.679 193.778  1.00157.08           C  
ATOM   2514  N   LEU B 144     193.884 245.731 193.771  1.00157.51           N  
ATOM   2515  CA  LEU B 144     193.894 244.407 193.170  1.00157.51           C  
ATOM   2516  C   LEU B 144     192.477 243.866 193.007  1.00157.51           C  
ATOM   2517  O   LEU B 144     192.177 243.202 192.010  1.00157.51           O  
ATOM   2518  CB  LEU B 144     194.759 243.456 193.997  1.00157.51           C  
ATOM   2519  CG  LEU B 144     196.271 243.471 193.726  1.00157.51           C  
ATOM   2520  CD1 LEU B 144     196.563 243.024 192.305  1.00157.51           C  
ATOM   2521  CD2 LEU B 144     196.927 244.814 194.008  1.00157.51           C  
ATOM   2522  N   GLU B 145     191.585 244.152 193.961  1.00154.41           N  
ATOM   2523  CA  GLU B 145     190.217 243.641 193.868  1.00154.41           C  
ATOM   2524  C   GLU B 145     189.456 244.276 192.706  1.00154.41           C  
ATOM   2525  O   GLU B 145     188.707 243.594 191.988  1.00154.41           O  
ATOM   2526  CB  GLU B 145     189.493 243.881 195.191  1.00154.41           C  
ATOM   2527  CG  GLU B 145     188.095 243.318 195.248  1.00154.41           C  
ATOM   2528  CD  GLU B 145     187.511 243.372 196.647  1.00154.41           C  
ATOM   2529  OE1 GLU B 145     188.213 243.842 197.565  1.00154.41           O  
ATOM   2530  OE2 GLU B 145     186.354 242.943 196.830  1.00154.41           O  
ATOM   2531  N   VAL B 146     189.632 245.581 192.505  1.00156.16           N  
ATOM   2532  CA  VAL B 146     188.964 246.234 191.390  1.00156.16           C  
ATOM   2533  C   VAL B 146     189.582 245.808 190.069  1.00156.16           C  
ATOM   2534  O   VAL B 146     188.873 245.698 189.069  1.00156.16           O  
ATOM   2535  CB  VAL B 146     188.961 247.765 191.549  1.00156.16           C  
ATOM   2536  CG1 VAL B 146     188.309 248.152 192.858  1.00156.16           C  
ATOM   2537  CG2 VAL B 146     190.362 248.342 191.444  1.00156.16           C  
ATOM   2538  N   ALA B 147     190.892 245.547 190.031  1.00156.47           N  
ATOM   2539  CA  ALA B 147     191.466 244.967 188.822  1.00156.47           C  
ATOM   2540  C   ALA B 147     190.863 243.596 188.543  1.00156.47           C  
ATOM   2541  O   ALA B 147     190.571 243.256 187.388  1.00156.47           O  
ATOM   2542  CB  ALA B 147     192.985 244.875 188.950  1.00156.47           C  
ATOM   2543  N   ASP B 148     190.672 242.797 189.594  1.00158.75           N  
ATOM   2544  CA  ASP B 148     189.994 241.514 189.456  1.00158.75           C  
ATOM   2545  C   ASP B 148     188.659 241.679 188.751  1.00158.75           C  
ATOM   2546  O   ASP B 148     188.427 241.099 187.684  1.00158.75           O  
ATOM   2547  CB  ASP B 148     189.786 240.880 190.834  1.00158.75           C  
ATOM   2548  CG  ASP B 148     190.925 239.966 191.238  1.00158.75           C  
ATOM   2549  OD1 ASP B 148     191.855 239.783 190.429  1.00158.75           O  
ATOM   2550  OD2 ASP B 148     190.886 239.419 192.359  1.00158.75           O  
ATOM   2551  N   TRP B 149     187.769 242.478 189.337  1.00156.08           N  
ATOM   2552  CA  TRP B 149     186.430 242.602 188.765  1.00156.08           C  
ATOM   2553  C   TRP B 149     186.448 243.295 187.409  1.00156.08           C  
ATOM   2554  O   TRP B 149     185.585 243.020 186.570  1.00156.08           O  
ATOM   2555  CB  TRP B 149     185.501 243.313 189.744  1.00156.08           C  
ATOM   2556  CG  TRP B 149     185.230 242.468 190.936  1.00156.08           C  
ATOM   2557  CD1 TRP B 149     185.597 241.171 191.105  1.00156.08           C  
ATOM   2558  CD2 TRP B 149     184.554 242.854 192.137  1.00156.08           C  
ATOM   2559  NE1 TRP B 149     185.186 240.718 192.330  1.00156.08           N  
ATOM   2560  CE2 TRP B 149     184.543 241.735 192.984  1.00156.08           C  
ATOM   2561  CE3 TRP B 149     183.954 244.034 192.576  1.00156.08           C  
ATOM   2562  CZ2 TRP B 149     183.956 241.760 194.246  1.00156.08           C  
ATOM   2563  CZ3 TRP B 149     183.372 244.058 193.826  1.00156.08           C  
ATOM   2564  CH2 TRP B 149     183.377 242.930 194.647  1.00156.08           C  
ATOM   2565  N   PHE B 150     187.428 244.168 187.163  1.00155.03           N  
ATOM   2566  CA  PHE B 150     187.582 244.780 185.848  1.00155.03           C  
ATOM   2567  C   PHE B 150     187.839 243.726 184.784  1.00155.03           C  
ATOM   2568  O   PHE B 150     187.146 243.675 183.763  1.00155.03           O  
ATOM   2569  CB  PHE B 150     188.727 245.791 185.883  1.00155.03           C  
ATOM   2570  CG  PHE B 150     189.033 246.414 184.553  1.00155.03           C  
ATOM   2571  CD1 PHE B 150     188.015 246.804 183.696  1.00155.03           C  
ATOM   2572  CD2 PHE B 150     190.345 246.614 184.158  1.00155.03           C  
ATOM   2573  CE1 PHE B 150     188.301 247.381 182.470  1.00155.03           C  
ATOM   2574  CE2 PHE B 150     190.637 247.190 182.934  1.00155.03           C  
ATOM   2575  CZ  PHE B 150     189.613 247.573 182.090  1.00155.03           C  
ATOM   2576  N   ILE B 151     188.831 242.865 185.014  1.00155.77           N  
ATOM   2577  CA  ILE B 151     189.133 241.829 184.032  1.00155.77           C  
ATOM   2578  C   ILE B 151     187.973 240.850 183.919  1.00155.77           C  
ATOM   2579  O   ILE B 151     187.659 240.360 182.828  1.00155.77           O  
ATOM   2580  CB  ILE B 151     190.451 241.117 184.380  1.00155.77           C  
ATOM   2581  CG1 ILE B 151     191.556 242.137 184.666  1.00155.77           C  
ATOM   2582  CG2 ILE B 151     190.871 240.204 183.247  1.00155.77           C  
ATOM   2583  CD1 ILE B 151     191.750 243.162 183.578  1.00155.77           C  
ATOM   2584  N   LEU B 152     187.299 240.575 185.034  1.00155.95           N  
ATOM   2585  CA  LEU B 152     186.145 239.683 185.007  1.00155.95           C  
ATOM   2586  C   LEU B 152     185.045 240.229 184.098  1.00155.95           C  
ATOM   2587  O   LEU B 152     184.664 239.595 183.102  1.00155.95           O  
ATOM   2588  CB  LEU B 152     185.634 239.495 186.434  1.00155.95           C  
ATOM   2589  CG  LEU B 152     184.804 238.274 186.797  1.00155.95           C  
ATOM   2590  CD1 LEU B 152     185.607 237.006 186.570  1.00155.95           C  
ATOM   2591  CD2 LEU B 152     184.383 238.388 188.246  1.00155.95           C  
ATOM   2592  N   LEU B 153     184.539 241.424 184.410  1.00155.75           N  
ATOM   2593  CA  LEU B 153     183.478 242.006 183.597  1.00155.75           C  
ATOM   2594  C   LEU B 153     183.932 242.215 182.162  1.00155.75           C  
ATOM   2595  O   LEU B 153     183.115 242.141 181.240  1.00155.75           O  
ATOM   2596  CB  LEU B 153     182.997 243.324 184.209  1.00155.75           C  
ATOM   2597  CG  LEU B 153     183.934 244.534 184.241  1.00155.75           C  
ATOM   2598  CD1 LEU B 153     183.815 245.390 182.980  1.00155.75           C  
ATOM   2599  CD2 LEU B 153     183.671 245.369 185.475  1.00155.75           C  
ATOM   2600  N   SER B 154     185.223 242.482 181.946  1.00157.92           N  
ATOM   2601  CA  SER B 154     185.719 242.579 180.582  1.00157.92           C  
ATOM   2602  C   SER B 154     185.579 241.245 179.863  1.00157.92           C  
ATOM   2603  O   SER B 154     185.241 241.199 178.674  1.00157.92           O  
ATOM   2604  CB  SER B 154     187.170 243.050 180.583  1.00157.92           C  
ATOM   2605  OG  SER B 154     187.624 243.257 179.259  1.00157.92           O  
ATOM   2606  N   PHE B 155     185.825 240.144 180.568  1.00160.48           N  
ATOM   2607  CA  PHE B 155     185.561 238.844 179.968  1.00160.48           C  
ATOM   2608  C   PHE B 155     184.090 238.701 179.607  1.00160.48           C  
ATOM   2609  O   PHE B 155     183.764 238.198 178.528  1.00160.48           O  
ATOM   2610  CB  PHE B 155     185.999 237.721 180.902  1.00160.48           C  
ATOM   2611  CG  PHE B 155     187.428 237.319 180.723  1.00160.48           C  
ATOM   2612  CD1 PHE B 155     187.846 236.729 179.547  1.00160.48           C  
ATOM   2613  CD2 PHE B 155     188.355 237.539 181.723  1.00160.48           C  
ATOM   2614  CE1 PHE B 155     189.161 236.361 179.374  1.00160.48           C  
ATOM   2615  CE2 PHE B 155     189.668 237.176 181.553  1.00160.48           C  
ATOM   2616  CZ  PHE B 155     190.073 236.586 180.377  1.00160.48           C  
ATOM   2617  N   ILE B 156     183.185 239.137 180.488  1.00162.22           N  
ATOM   2618  CA  ILE B 156     181.760 239.021 180.150  1.00162.22           C  
ATOM   2619  C   ILE B 156     181.425 239.857 178.917  1.00162.22           C  
ATOM   2620  O   ILE B 156     180.673 239.419 178.037  1.00162.22           O  
ATOM   2621  CB  ILE B 156     180.836 239.381 181.334  1.00162.22           C  
ATOM   2622  CG1 ILE B 156     180.938 238.387 182.494  1.00162.22           C  
ATOM   2623  CG2 ILE B 156     179.383 239.443 180.878  1.00162.22           C  
ATOM   2624  CD1 ILE B 156     181.925 238.727 183.530  1.00162.22           C  
ATOM   2625  N   VAL B 157     181.964 241.075 178.836  1.00163.12           N  
ATOM   2626  CA  VAL B 157     181.620 241.920 177.693  1.00163.12           C  
ATOM   2627  C   VAL B 157     182.182 241.326 176.405  1.00163.12           C  
ATOM   2628  O   VAL B 157     181.532 241.385 175.354  1.00163.12           O  
ATOM   2629  CB  VAL B 157     182.073 243.383 177.897  1.00163.12           C  
ATOM   2630  CG1 VAL B 157     183.574 243.534 177.811  1.00163.12           C  
ATOM   2631  CG2 VAL B 157     181.399 244.288 176.884  1.00163.12           C  
ATOM   2632  N   GLU B 158     183.361 240.704 176.459  1.00163.74           N  
ATOM   2633  CA  GLU B 158     183.892 240.068 175.257  1.00163.74           C  
ATOM   2634  C   GLU B 158     183.085 238.836 174.870  1.00163.74           C  
ATOM   2635  O   GLU B 158     182.843 238.594 173.681  1.00163.74           O  
ATOM   2636  CB  GLU B 158     185.360 239.719 175.448  1.00163.74           C  
ATOM   2637  CG  GLU B 158     186.183 240.937 175.738  1.00163.74           C  
ATOM   2638  CD  GLU B 158     186.768 241.524 174.485  1.00163.74           C  
ATOM   2639  OE1 GLU B 158     187.922 241.976 174.529  1.00163.74           O  
ATOM   2640  OE2 GLU B 158     186.072 241.521 173.450  1.00163.74           O  
ATOM   2641  N   ILE B 159     182.660 238.041 175.854  1.00169.40           N  
ATOM   2642  CA  ILE B 159     181.821 236.887 175.542  1.00169.40           C  
ATOM   2643  C   ILE B 159     180.531 237.341 174.878  1.00169.40           C  
ATOM   2644  O   ILE B 159     180.097 236.763 173.876  1.00169.40           O  
ATOM   2645  CB  ILE B 159     181.541 236.049 176.802  1.00169.40           C  
ATOM   2646  CG1 ILE B 159     182.845 235.551 177.423  1.00169.40           C  
ATOM   2647  CG2 ILE B 159     180.648 234.874 176.459  1.00169.40           C  
ATOM   2648  CD1 ILE B 159     183.693 234.716 176.491  1.00169.40           C  
ATOM   2649  N   LEU B 160     179.908 238.393 175.413  1.00167.19           N  
ATOM   2650  CA  LEU B 160     178.714 238.934 174.771  1.00167.19           C  
ATOM   2651  C   LEU B 160     179.034 239.463 173.379  1.00167.19           C  
ATOM   2652  O   LEU B 160     178.182 239.428 172.485  1.00167.19           O  
ATOM   2653  CB  LEU B 160     178.091 240.027 175.641  1.00167.19           C  
ATOM   2654  CG  LEU B 160     177.257 239.519 176.825  1.00167.19           C  
ATOM   2655  CD1 LEU B 160     176.415 240.629 177.447  1.00167.19           C  
ATOM   2656  CD2 LEU B 160     176.379 238.351 176.402  1.00167.19           C  
ATOM   2657  N   LEU B 161     180.255 239.957 173.174  1.00166.58           N  
ATOM   2658  CA  LEU B 161     180.653 240.366 171.833  1.00166.58           C  
ATOM   2659  C   LEU B 161     180.671 239.182 170.873  1.00166.58           C  
ATOM   2660  O   LEU B 161     180.212 239.298 169.731  1.00166.58           O  
ATOM   2661  CB  LEU B 161     182.016 241.052 171.873  1.00166.58           C  
ATOM   2662  CG  LEU B 161     182.002 242.534 172.254  1.00166.58           C  
ATOM   2663  CD1 LEU B 161     183.409 243.083 172.368  1.00166.58           C  
ATOM   2664  CD2 LEU B 161     181.208 243.326 171.236  1.00166.58           C  
ATOM   2665  N   MET B 162     181.198 238.037 171.309  1.00171.17           N  
ATOM   2666  CA  MET B 162     181.134 236.857 170.446  1.00171.17           C  
ATOM   2667  C   MET B 162     179.702 236.363 170.260  1.00171.17           C  
ATOM   2668  O   MET B 162     179.378 235.810 169.204  1.00171.17           O  
ATOM   2669  CB  MET B 162     182.013 235.706 170.950  1.00171.17           C  
ATOM   2670  CG  MET B 162     183.520 235.837 170.691  1.00171.17           C  
ATOM   2671  SD  MET B 162     184.458 237.008 171.681  1.00171.17           S  
ATOM   2672  CE  MET B 162     184.532 236.123 173.236  1.00171.17           C  
ATOM   2673  N   TRP B 163     178.839 236.522 171.268  1.00172.91           N  
ATOM   2674  CA  TRP B 163     177.420 236.244 171.045  1.00172.91           C  
ATOM   2675  C   TRP B 163     176.865 237.117 169.929  1.00172.91           C  
ATOM   2676  O   TRP B 163     176.266 236.619 168.970  1.00172.91           O  
ATOM   2677  CB  TRP B 163     176.589 236.464 172.311  1.00172.91           C  
ATOM   2678  CG  TRP B 163     176.804 235.521 173.442  1.00172.91           C  
ATOM   2679  CD1 TRP B 163     177.589 235.711 174.533  1.00172.91           C  
ATOM   2680  CD2 TRP B 163     176.189 234.240 173.607  1.00172.91           C  
ATOM   2681  NE1 TRP B 163     177.516 234.624 175.367  1.00172.91           N  
ATOM   2682  CE2 TRP B 163     176.661 233.705 174.821  1.00172.91           C  
ATOM   2683  CE3 TRP B 163     175.293 233.490 172.842  1.00172.91           C  
ATOM   2684  CZ2 TRP B 163     176.265 232.454 175.292  1.00172.91           C  
ATOM   2685  CZ3 TRP B 163     174.901 232.249 173.309  1.00172.91           C  
ATOM   2686  CH2 TRP B 163     175.390 231.741 174.522  1.00172.91           C  
ATOM   2687  N   LEU B 164     177.062 238.429 170.045  1.00170.74           N  
ATOM   2688  CA  LEU B 164     176.526 239.369 169.071  1.00170.74           C  
ATOM   2689  C   LEU B 164     177.094 239.114 167.684  1.00170.74           C  
ATOM   2690  O   LEU B 164     176.411 239.349 166.681  1.00170.74           O  
ATOM   2691  CB  LEU B 164     176.827 240.800 169.520  1.00170.74           C  
ATOM   2692  CG  LEU B 164     176.090 241.967 168.859  1.00170.74           C  
ATOM   2693  CD1 LEU B 164     175.873 243.089 169.863  1.00170.74           C  
ATOM   2694  CD2 LEU B 164     176.850 242.481 167.654  1.00170.74           C  
ATOM   2695  N   ALA B 165     178.337 238.644 167.606  1.00172.44           N  
ATOM   2696  CA  ALA B 165     178.948 238.335 166.322  1.00172.44           C  
ATOM   2697  C   ALA B 165     178.200 237.217 165.608  1.00172.44           C  
ATOM   2698  O   ALA B 165     177.582 237.445 164.564  1.00172.44           O  
ATOM   2699  CB  ALA B 165     180.415 237.950 166.510  1.00172.44           C  
ATOM   2700  N   SER B 166     178.277 235.988 166.137  1.00176.51           N  
ATOM   2701  CA  SER B 166     177.614 234.843 165.451  1.00176.51           C  
ATOM   2702  C   SER B 166     176.407 234.285 166.220  1.00176.51           C  
ATOM   2703  O   SER B 166     175.316 234.210 165.620  1.00176.51           O  
ATOM   2704  CB  SER B 166     178.615 233.755 165.153  1.00176.51           C  
ATOM   2705  OG  SER B 166     179.651 234.239 164.311  1.00176.51           O  
ATOM   2706  N   PHE B 167     176.592 233.908 167.490  1.00177.12           N  
ATOM   2707  CA  PHE B 167     175.520 233.325 168.295  1.00177.12           C  
ATOM   2708  C   PHE B 167     175.164 231.928 167.789  1.00177.12           C  
ATOM   2709  O   PHE B 167     174.431 231.189 168.450  1.00177.12           O  
ATOM   2710  CB  PHE B 167     174.301 234.265 168.298  1.00177.12           C  
ATOM   2711  CG  PHE B 167     173.066 233.686 168.929  1.00177.12           C  
ATOM   2712  CD1 PHE B 167     172.852 233.805 170.290  1.00177.12           C  
ATOM   2713  CD2 PHE B 167     172.109 233.045 168.158  1.00177.12           C  
ATOM   2714  CE1 PHE B 167     171.718 233.283 170.873  1.00177.12           C  
ATOM   2715  CE2 PHE B 167     170.974 232.521 168.737  1.00177.12           C  
ATOM   2716  CZ  PHE B 167     170.777 232.641 170.097  1.00177.12           C  
ATOM   2717  N   SER B 168     175.739 231.529 166.655  1.00181.04           N  
ATOM   2718  CA  SER B 168     175.393 230.285 165.981  1.00181.04           C  
ATOM   2719  C   SER B 168     176.540 229.289 165.952  1.00181.04           C  
ATOM   2720  O   SER B 168     176.370 228.137 166.366  1.00181.04           O  
ATOM   2721  CB  SER B 168     174.928 230.582 164.548  1.00181.04           C  
ATOM   2722  OG  SER B 168     175.819 231.470 163.899  1.00181.04           O  
ATOM   2723  N   LEU B 169     177.710 229.698 165.461  1.00182.38           N  
ATOM   2724  CA  LEU B 169     178.911 228.886 165.598  1.00182.38           C  
ATOM   2725  C   LEU B 169     179.564 229.073 166.958  1.00182.38           C  
ATOM   2726  O   LEU B 169     180.587 228.438 167.236  1.00182.38           O  
ATOM   2727  CB  LEU B 169     179.908 229.211 164.478  1.00182.38           C  
ATOM   2728  CG  LEU B 169     180.499 230.620 164.340  1.00182.38           C  
ATOM   2729  CD1 LEU B 169     181.709 230.831 165.250  1.00182.38           C  
ATOM   2730  CD2 LEU B 169     180.854 230.930 162.890  1.00182.38           C  
ATOM   2731  N   PHE B 170     178.989 229.937 167.797  1.00180.36           N  
ATOM   2732  CA  PHE B 170     179.530 230.185 169.127  1.00180.36           C  
ATOM   2733  C   PHE B 170     179.559 228.909 169.954  1.00180.36           C  
ATOM   2734  O   PHE B 170     180.344 228.790 170.901  1.00180.36           O  
ATOM   2735  CB  PHE B 170     178.693 231.263 169.814  1.00180.36           C  
ATOM   2736  CG  PHE B 170     179.179 231.638 171.176  1.00180.36           C  
ATOM   2737  CD1 PHE B 170     180.295 232.439 171.327  1.00180.36           C  
ATOM   2738  CD2 PHE B 170     178.511 231.210 172.303  1.00180.36           C  
ATOM   2739  CE1 PHE B 170     180.742 232.795 172.579  1.00180.36           C  
ATOM   2740  CE2 PHE B 170     178.953 231.558 173.555  1.00180.36           C  
ATOM   2741  CZ  PHE B 170     180.069 232.354 173.695  1.00180.36           C  
ATOM   2742  N   TRP B 171     178.705 227.946 169.615  1.00181.86           N  
ATOM   2743  CA  TRP B 171     178.665 226.654 170.281  1.00181.86           C  
ATOM   2744  C   TRP B 171     179.298 225.543 169.448  1.00181.86           C  
ATOM   2745  O   TRP B 171     178.871 224.386 169.545  1.00181.86           O  
ATOM   2746  CB  TRP B 171     177.223 226.298 170.636  1.00181.86           C  
ATOM   2747  CG  TRP B 171     176.729 227.048 171.821  1.00181.86           C  
ATOM   2748  CD1 TRP B 171     177.270 228.177 172.353  1.00181.86           C  
ATOM   2749  CD2 TRP B 171     175.602 226.718 172.638  1.00181.86           C  
ATOM   2750  NE1 TRP B 171     176.547 228.578 173.449  1.00181.86           N  
ATOM   2751  CE2 TRP B 171     175.517 227.697 173.644  1.00181.86           C  
ATOM   2752  CE3 TRP B 171     174.655 225.691 172.614  1.00181.86           C  
ATOM   2753  CZ2 TRP B 171     174.521 227.681 174.617  1.00181.86           C  
ATOM   2754  CZ3 TRP B 171     173.669 225.677 173.580  1.00181.86           C  
ATOM   2755  CH2 TRP B 171     173.609 226.663 174.567  1.00181.86           C  
ATOM   2756  N   LYS B 172     180.298 225.872 168.625  1.00187.51           N  
ATOM   2757  CA  LYS B 172     181.010 224.892 167.820  1.00187.51           C  
ATOM   2758  C   LYS B 172     182.520 224.932 167.993  1.00187.51           C  
ATOM   2759  O   LYS B 172     183.159 223.877 167.903  1.00187.51           O  
ATOM   2760  CB  LYS B 172     180.680 225.075 166.329  1.00187.51           C  
ATOM   2761  CG  LYS B 172     181.093 223.903 165.450  1.00187.51           C  
ATOM   2762  CD  LYS B 172     180.733 222.559 166.077  1.00187.51           C  
ATOM   2763  CE  LYS B 172     179.255 222.232 165.912  1.00187.51           C  
ATOM   2764  NZ  LYS B 172     178.928 220.859 166.391  1.00187.51           N  
ATOM   2765  N   ASP B 173     183.106 226.101 168.238  1.00188.22           N  
ATOM   2766  CA  ASP B 173     184.534 226.214 168.498  1.00188.22           C  
ATOM   2767  C   ASP B 173     184.804 225.752 169.923  1.00188.22           C  
ATOM   2768  O   ASP B 173     184.217 226.284 170.870  1.00188.22           O  
ATOM   2769  CB  ASP B 173     185.011 227.652 168.299  1.00188.22           C  
ATOM   2770  CG  ASP B 173     186.507 227.803 168.498  1.00188.22           C  
ATOM   2771  OD1 ASP B 173     187.259 227.619 167.517  1.00188.22           O  
ATOM   2772  OD2 ASP B 173     186.933 228.097 169.637  1.00188.22           O  
ATOM   2773  N   ALA B 174     185.694 224.766 170.072  1.00187.74           N  
ATOM   2774  CA  ALA B 174     185.942 224.182 171.388  1.00187.74           C  
ATOM   2775  C   ALA B 174     186.515 225.208 172.352  1.00187.74           C  
ATOM   2776  O   ALA B 174     186.122 225.261 173.524  1.00187.74           O  
ATOM   2777  CB  ALA B 174     186.886 222.986 171.265  1.00187.74           C  
ATOM   2778  N   TRP B 175     187.445 226.034 171.877  1.00182.19           N  
ATOM   2779  CA  TRP B 175     188.115 226.970 172.768  1.00182.19           C  
ATOM   2780  C   TRP B 175     187.151 228.042 173.255  1.00182.19           C  
ATOM   2781  O   TRP B 175     187.117 228.372 174.446  1.00182.19           O  
ATOM   2782  CB  TRP B 175     189.307 227.603 172.056  1.00182.19           C  
ATOM   2783  CG  TRP B 175     190.474 226.676 171.906  1.00182.19           C  
ATOM   2784  CD1 TRP B 175     191.109 226.350 170.747  1.00182.19           C  
ATOM   2785  CD2 TRP B 175     191.097 225.898 172.936  1.00182.19           C  
ATOM   2786  NE1 TRP B 175     192.115 225.451 170.993  1.00182.19           N  
ATOM   2787  CE2 TRP B 175     192.124 225.153 172.329  1.00182.19           C  
ATOM   2788  CE3 TRP B 175     190.897 225.772 174.314  1.00182.19           C  
ATOM   2789  CZ2 TRP B 175     192.947 224.294 173.050  1.00182.19           C  
ATOM   2790  CZ3 TRP B 175     191.708 224.914 175.024  1.00182.19           C  
ATOM   2791  CH2 TRP B 175     192.727 224.192 174.394  1.00182.19           C  
ATOM   2792  N   ASN B 176     186.355 228.597 172.342  1.00182.29           N  
ATOM   2793  CA  ASN B 176     185.424 229.652 172.719  1.00182.29           C  
ATOM   2794  C   ASN B 176     184.355 229.135 173.674  1.00182.29           C  
ATOM   2795  O   ASN B 176     184.017 229.805 174.660  1.00182.29           O  
ATOM   2796  CB  ASN B 176     184.792 230.258 171.468  1.00182.29           C  
ATOM   2797  CG  ASN B 176     185.730 231.212 170.742  1.00182.29           C  
ATOM   2798  OD1 ASN B 176     186.729 231.666 171.300  1.00182.29           O  
ATOM   2799  ND2 ASN B 176     185.405 231.525 169.493  1.00182.29           N  
ATOM   2800  N   VAL B 177     183.818 227.942 173.411  1.00183.44           N  
ATOM   2801  CA  VAL B 177     182.779 227.407 174.285  1.00183.44           C  
ATOM   2802  C   VAL B 177     183.365 227.051 175.646  1.00183.44           C  
ATOM   2803  O   VAL B 177     182.722 227.249 176.684  1.00183.44           O  
ATOM   2804  CB  VAL B 177     182.069 226.207 173.627  1.00183.44           C  
ATOM   2805  CG1 VAL B 177     183.007 225.026 173.438  1.00183.44           C  
ATOM   2806  CG2 VAL B 177     180.846 225.811 174.420  1.00183.44           C  
ATOM   2807  N   PHE B 178     184.598 226.537 175.671  1.00180.72           N  
ATOM   2808  CA  PHE B 178     185.245 226.264 176.948  1.00180.72           C  
ATOM   2809  C   PHE B 178     185.491 227.548 177.730  1.00180.72           C  
ATOM   2810  O   PHE B 178     185.352 227.567 178.957  1.00180.72           O  
ATOM   2811  CB  PHE B 178     186.555 225.517 176.729  1.00180.72           C  
ATOM   2812  CG  PHE B 178     187.251 225.141 178.005  1.00180.72           C  
ATOM   2813  CD1 PHE B 178     186.780 224.099 178.784  1.00180.72           C  
ATOM   2814  CD2 PHE B 178     188.368 225.839 178.431  1.00180.72           C  
ATOM   2815  CE1 PHE B 178     187.415 223.756 179.955  1.00180.72           C  
ATOM   2816  CE2 PHE B 178     189.003 225.498 179.603  1.00180.72           C  
ATOM   2817  CZ  PHE B 178     188.527 224.455 180.365  1.00180.72           C  
ATOM   2818  N   ASP B 179     185.880 228.625 177.042  1.00177.84           N  
ATOM   2819  CA  ASP B 179     186.039 229.909 177.717  1.00177.84           C  
ATOM   2820  C   ASP B 179     184.718 230.393 178.295  1.00177.84           C  
ATOM   2821  O   ASP B 179     184.682 230.955 179.395  1.00177.84           O  
ATOM   2822  CB  ASP B 179     186.614 230.950 176.760  1.00177.84           C  
ATOM   2823  CG  ASP B 179     188.100 230.784 176.543  1.00177.84           C  
ATOM   2824  OD1 ASP B 179     188.771 230.219 177.431  1.00177.84           O  
ATOM   2825  OD2 ASP B 179     188.604 231.247 175.501  1.00177.84           O  
ATOM   2826  N   PHE B 180     183.623 230.206 177.555  1.00177.89           N  
ATOM   2827  CA  PHE B 180     182.310 230.516 178.111  1.00177.89           C  
ATOM   2828  C   PHE B 180     182.046 229.706 179.373  1.00177.89           C  
ATOM   2829  O   PHE B 180     181.576 230.246 180.382  1.00177.89           O  
ATOM   2830  CB  PHE B 180     181.217 230.250 177.079  1.00177.89           C  
ATOM   2831  CG  PHE B 180     179.836 230.189 177.667  1.00177.89           C  
ATOM   2832  CD1 PHE B 180     179.144 231.348 177.959  1.00177.89           C  
ATOM   2833  CD2 PHE B 180     179.232 228.970 177.930  1.00177.89           C  
ATOM   2834  CE1 PHE B 180     177.879 231.294 178.499  1.00177.89           C  
ATOM   2835  CE2 PHE B 180     177.966 228.910 178.472  1.00177.89           C  
ATOM   2836  CZ  PHE B 180     177.289 230.073 178.757  1.00177.89           C  
ATOM   2837  N   PHE B 181     182.341 228.406 179.328  1.00176.23           N  
ATOM   2838  CA  PHE B 181     182.203 227.561 180.510  1.00176.23           C  
ATOM   2839  C   PHE B 181     182.984 228.138 181.683  1.00176.23           C  
ATOM   2840  O   PHE B 181     182.463 228.258 182.800  1.00176.23           O  
ATOM   2841  CB  PHE B 181     182.704 226.148 180.206  1.00176.23           C  
ATOM   2842  CG  PHE B 181     181.898 225.408 179.176  1.00176.23           C  
ATOM   2843  CD1 PHE B 181     180.700 225.911 178.704  1.00176.23           C  
ATOM   2844  CD2 PHE B 181     182.358 224.204 178.670  1.00176.23           C  
ATOM   2845  CE1 PHE B 181     179.974 225.219 177.755  1.00176.23           C  
ATOM   2846  CE2 PHE B 181     181.640 223.513 177.722  1.00176.23           C  
ATOM   2847  CZ  PHE B 181     180.447 224.019 177.266  1.00176.23           C  
ATOM   2848  N   VAL B 182     184.246 228.492 181.439  1.00172.57           N  
ATOM   2849  CA  VAL B 182     185.135 228.933 182.509  1.00172.57           C  
ATOM   2850  C   VAL B 182     184.659 230.250 183.101  1.00172.57           C  
ATOM   2851  O   VAL B 182     184.631 230.420 184.323  1.00172.57           O  
ATOM   2852  CB  VAL B 182     186.583 229.029 181.994  1.00172.57           C  
ATOM   2853  CG1 VAL B 182     187.429 229.858 182.937  1.00172.57           C  
ATOM   2854  CG2 VAL B 182     187.177 227.636 181.852  1.00172.57           C  
ATOM   2855  N   THR B 183     184.277 231.204 182.251  1.00167.84           N  
ATOM   2856  CA  THR B 183     183.788 232.480 182.761  1.00167.84           C  
ATOM   2857  C   THR B 183     182.480 232.300 183.522  1.00167.84           C  
ATOM   2858  O   THR B 183     182.246 232.965 184.537  1.00167.84           O  
ATOM   2859  CB  THR B 183     183.629 233.472 181.613  1.00167.84           C  
ATOM   2860  OG1 THR B 183     184.871 233.574 180.912  1.00167.84           O  
ATOM   2861  CG2 THR B 183     183.259 234.838 182.138  1.00167.84           C  
ATOM   2862  N   LEU B 184     181.621 231.388 183.061  1.00167.31           N  
ATOM   2863  CA  LEU B 184     180.399 231.082 183.795  1.00167.31           C  
ATOM   2864  C   LEU B 184     180.718 230.564 185.192  1.00167.31           C  
ATOM   2865  O   LEU B 184     180.168 231.042 186.195  1.00167.31           O  
ATOM   2866  CB  LEU B 184     179.579 230.060 183.004  1.00167.31           C  
ATOM   2867  CG  LEU B 184     178.164 229.664 183.432  1.00167.31           C  
ATOM   2868  CD1 LEU B 184     177.373 229.208 182.218  1.00167.31           C  
ATOM   2869  CD2 LEU B 184     178.182 228.560 184.481  1.00167.31           C  
ATOM   2870  N   LEU B 185     181.619 229.590 185.277  1.00165.22           N  
ATOM   2871  CA  LEU B 185     181.951 228.998 186.564  1.00165.22           C  
ATOM   2872  C   LEU B 185     182.839 229.888 187.417  1.00165.22           C  
ATOM   2873  O   LEU B 185     183.026 229.592 188.600  1.00165.22           O  
ATOM   2874  CB  LEU B 185     182.596 227.625 186.351  1.00165.22           C  
ATOM   2875  CG  LEU B 185     183.897 227.534 185.549  1.00165.22           C  
ATOM   2876  CD1 LEU B 185     185.124 227.816 186.386  1.00165.22           C  
ATOM   2877  CD2 LEU B 185     184.009 226.167 184.872  1.00165.22           C  
ATOM   2878  N   SER B 186     183.399 230.952 186.846  1.00163.25           N  
ATOM   2879  CA  SER B 186     184.126 231.946 187.623  1.00163.25           C  
ATOM   2880  C   SER B 186     183.234 233.073 188.115  1.00163.25           C  
ATOM   2881  O   SER B 186     183.552 233.697 189.133  1.00163.25           O  
ATOM   2882  CB  SER B 186     185.272 232.533 186.796  1.00163.25           C  
ATOM   2883  OG  SER B 186     184.774 233.269 185.696  1.00163.25           O  
ATOM   2884  N   LEU B 187     182.140 233.359 187.411  1.00161.81           N  
ATOM   2885  CA  LEU B 187     181.145 234.302 187.907  1.00161.81           C  
ATOM   2886  C   LEU B 187     180.139 233.665 188.846  1.00161.81           C  
ATOM   2887  O   LEU B 187     179.425 234.388 189.549  1.00161.81           O  
ATOM   2888  CB  LEU B 187     180.389 234.961 186.753  1.00161.81           C  
ATOM   2889  CG  LEU B 187     181.046 236.185 186.129  1.00161.81           C  
ATOM   2890  CD1 LEU B 187     181.117 237.285 187.171  1.00161.81           C  
ATOM   2891  CD2 LEU B 187     182.414 235.867 185.578  1.00161.81           C  
ATOM   2892  N   LEU B 188     180.046 232.342 188.860  1.00158.07           N  
ATOM   2893  CA  LEU B 188     179.270 231.686 189.907  1.00158.07           C  
ATOM   2894  C   LEU B 188     179.737 232.062 191.315  1.00158.07           C  
ATOM   2895  O   LEU B 188     178.871 232.272 192.182  1.00158.07           O  
ATOM   2896  CB  LEU B 188     179.298 230.167 189.684  1.00158.07           C  
ATOM   2897  CG  LEU B 188     178.804 229.283 190.826  1.00158.07           C  
ATOM   2898  CD1 LEU B 188     177.363 229.610 191.151  1.00158.07           C  
ATOM   2899  CD2 LEU B 188     178.957 227.814 190.464  1.00158.07           C  
ATOM   2900  N   PRO B 189     181.044 232.155 191.615  1.00159.76           N  
ATOM   2901  CA  PRO B 189     181.455 232.625 192.951  1.00159.76           C  
ATOM   2902  C   PRO B 189     180.899 233.982 193.340  1.00159.76           C  
ATOM   2903  O   PRO B 189     180.595 234.199 194.520  1.00159.76           O  
ATOM   2904  CB  PRO B 189     182.983 232.668 192.854  1.00159.76           C  
ATOM   2905  CG  PRO B 189     183.342 231.721 191.783  1.00159.76           C  
ATOM   2906  CD  PRO B 189     182.148 231.470 190.919  1.00159.76           C  
ATOM   2907  N   GLU B 190     180.774 234.914 192.395  1.00158.67           N  
ATOM   2908  CA  GLU B 190     180.186 236.205 192.733  1.00158.67           C  
ATOM   2909  C   GLU B 190     178.757 236.029 193.227  1.00158.67           C  
ATOM   2910  O   GLU B 190     178.335 236.680 194.191  1.00158.67           O  
ATOM   2911  CB  GLU B 190     180.237 237.143 191.528  1.00158.67           C  
ATOM   2912  CG  GLU B 190     181.636 237.634 191.188  1.00158.67           C  
ATOM   2913  CD  GLU B 190     182.098 238.770 192.087  1.00158.67           C  
ATOM   2914  OE1 GLU B 190     181.721 239.932 191.828  1.00158.67           O  
ATOM   2915  OE2 GLU B 190     182.844 238.501 193.053  1.00158.67           O  
ATOM   2916  N   LEU B 191     178.001 235.133 192.590  1.00157.59           N  
ATOM   2917  CA  LEU B 191     176.663 234.834 193.079  1.00157.59           C  
ATOM   2918  C   LEU B 191     176.714 234.197 194.461  1.00157.59           C  
ATOM   2919  O   LEU B 191     176.039 234.658 195.387  1.00157.59           O  
ATOM   2920  CB  LEU B 191     175.936 233.919 192.095  1.00157.59           C  
ATOM   2921  CG  LEU B 191     174.485 233.597 192.451  1.00157.59           C  
ATOM   2922  CD1 LEU B 191     173.649 234.863 192.448  1.00157.59           C  
ATOM   2923  CD2 LEU B 191     173.909 232.564 191.498  1.00157.59           C  
ATOM   2924  N   VAL B 192     177.536 233.157 194.631  1.00156.94           N  
ATOM   2925  CA  VAL B 192     177.534 232.434 195.901  1.00156.94           C  
ATOM   2926  C   VAL B 192     178.012 233.305 197.053  1.00156.94           C  
ATOM   2927  O   VAL B 192     177.722 232.993 198.215  1.00156.94           O  
ATOM   2928  CB  VAL B 192     178.387 231.153 195.848  1.00156.94           C  
ATOM   2929  CG1 VAL B 192     178.037 230.324 194.626  1.00156.94           C  
ATOM   2930  CG2 VAL B 192     179.871 231.465 195.914  1.00156.94           C  
ATOM   2931  N   VAL B 193     178.744 234.381 196.774  1.00156.68           N  
ATOM   2932  CA  VAL B 193     179.097 235.304 197.844  1.00156.68           C  
ATOM   2933  C   VAL B 193     178.020 236.368 198.046  1.00156.68           C  
ATOM   2934  O   VAL B 193     177.755 236.762 199.186  1.00156.68           O  
ATOM   2935  CB  VAL B 193     180.479 235.943 197.609  1.00156.68           C  
ATOM   2936  CG1 VAL B 193     181.552 234.865 197.520  1.00156.68           C  
ATOM   2937  CG2 VAL B 193     180.487 236.817 196.368  1.00156.68           C  
ATOM   2938  N   LEU B 194     177.373 236.836 196.972  1.00155.78           N  
ATOM   2939  CA  LEU B 194     176.251 237.751 197.153  1.00155.78           C  
ATOM   2940  C   LEU B 194     175.042 237.075 197.781  1.00155.78           C  
ATOM   2941  O   LEU B 194     174.145 237.771 198.269  1.00155.78           O  
ATOM   2942  CB  LEU B 194     175.848 238.393 195.824  1.00155.78           C  
ATOM   2943  CG  LEU B 194     176.857 239.344 195.182  1.00155.78           C  
ATOM   2944  CD1 LEU B 194     176.371 239.790 193.811  1.00155.78           C  
ATOM   2945  CD2 LEU B 194     177.095 240.543 196.082  1.00155.78           C  
ATOM   2946  N   LEU B 195     174.992 235.744 197.776  1.00153.08           N  
ATOM   2947  CA  LEU B 195     173.965 234.999 198.494  1.00153.08           C  
ATOM   2948  C   LEU B 195     174.455 234.469 199.833  1.00153.08           C  
ATOM   2949  O   LEU B 195     173.738 234.577 200.830  1.00153.08           O  
ATOM   2950  CB  LEU B 195     173.455 233.834 197.642  1.00153.08           C  
ATOM   2951  CG  LEU B 195     173.062 234.175 196.204  1.00153.08           C  
ATOM   2952  CD1 LEU B 195     172.434 232.973 195.521  1.00153.08           C  
ATOM   2953  CD2 LEU B 195     172.127 235.374 196.158  1.00153.08           C  
ATOM   2954  N   GLY B 196     175.660 233.909 199.877  1.00150.77           N  
ATOM   2955  CA  GLY B 196     176.230 233.423 201.125  1.00150.77           C  
ATOM   2956  C   GLY B 196     175.401 232.358 201.808  1.00150.77           C  
ATOM   2957  O   GLY B 196     175.399 232.271 203.042  1.00150.77           O  
ATOM   2958  N   VAL B 197     174.689 231.546 201.034  1.00155.98           N  
ATOM   2959  CA  VAL B 197     173.809 230.524 201.598  1.00155.98           C  
ATOM   2960  C   VAL B 197     174.582 229.310 202.112  1.00155.98           C  
ATOM   2961  O   VAL B 197     174.484 229.001 203.309  1.00155.98           O  
ATOM   2962  CB  VAL B 197     172.739 230.098 200.579  1.00155.98           C  
ATOM   2963  CG1 VAL B 197     171.968 228.888 201.092  1.00155.98           C  
ATOM   2964  CG2 VAL B 197     171.796 231.258 200.292  1.00155.98           C  
ATOM   2965  N   PRO B 198     175.359 228.581 201.272  1.00163.41           N  
ATOM   2966  CA  PRO B 198     175.841 227.260 201.709  1.00163.41           C  
ATOM   2967  C   PRO B 198     176.783 227.301 202.907  1.00163.41           C  
ATOM   2968  O   PRO B 198     176.478 226.708 203.947  1.00163.41           O  
ATOM   2969  CB  PRO B 198     176.546 226.720 200.461  1.00163.41           C  
ATOM   2970  CG  PRO B 198     177.015 227.941 199.739  1.00163.41           C  
ATOM   2971  CD  PRO B 198     175.995 229.007 200.007  1.00163.41           C  
ATOM   2972  N   ALA B 199     177.916 227.990 202.767  1.00168.83           N  
ATOM   2973  CA  ALA B 199     178.858 228.314 203.835  1.00168.83           C  
ATOM   2974  C   ALA B 199     180.064 228.972 203.178  1.00168.83           C  
ATOM   2975  O   ALA B 199     180.156 229.053 201.950  1.00168.83           O  
ATOM   2976  CB  ALA B 199     179.297 227.099 204.655  1.00168.83           C  
ATOM   2977  N   HIS B 200     180.994 229.439 204.013  1.00168.04           N  
ATOM   2978  CA  HIS B 200     182.309 229.874 203.540  1.00168.04           C  
ATOM   2979  C   HIS B 200     183.289 228.725 203.765  1.00168.04           C  
ATOM   2980  O   HIS B 200     184.141 228.747 204.655  1.00168.04           O  
ATOM   2981  CB  HIS B 200     182.739 231.147 204.256  1.00168.04           C  
ATOM   2982  CG  HIS B 200     183.919 231.820 203.633  1.00168.04           C  
ATOM   2983  ND1 HIS B 200     184.230 231.689 202.297  1.00168.04           N  
ATOM   2984  CD2 HIS B 200     184.855 232.644 204.158  1.00168.04           C  
ATOM   2985  CE1 HIS B 200     185.313 232.395 202.028  1.00168.04           C  
ATOM   2986  NE2 HIS B 200     185.712 232.984 203.140  1.00168.04           N  
ATOM   2987  N   SER B 201     183.169 227.707 202.919  1.00166.91           N  
ATOM   2988  CA  SER B 201     183.774 226.405 203.168  1.00166.91           C  
ATOM   2989  C   SER B 201     184.624 225.969 201.973  1.00166.91           C  
ATOM   2990  O   SER B 201     184.846 226.728 201.028  1.00166.91           O  
ATOM   2991  CB  SER B 201     182.687 225.382 203.499  1.00166.91           C  
ATOM   2992  OG  SER B 201     183.246 224.119 203.797  1.00166.91           O  
ATOM   2993  N   VAL B 202     185.062 224.707 202.014  1.00162.35           N  
ATOM   2994  CA  VAL B 202     186.176 224.252 201.186  1.00162.35           C  
ATOM   2995  C   VAL B 202     185.838 224.322 199.702  1.00162.35           C  
ATOM   2996  O   VAL B 202     186.707 224.616 198.873  1.00162.35           O  
ATOM   2997  CB  VAL B 202     186.600 222.832 201.607  1.00162.35           C  
ATOM   2998  CG1 VAL B 202     187.128 222.847 203.032  1.00162.35           C  
ATOM   2999  CG2 VAL B 202     185.444 221.860 201.474  1.00162.35           C  
ATOM   3000  N   TRP B 203     184.586 224.042 199.335  1.00162.39           N  
ATOM   3001  CA  TRP B 203     184.210 224.104 197.925  1.00162.39           C  
ATOM   3002  C   TRP B 203     184.344 225.520 197.383  1.00162.39           C  
ATOM   3003  O   TRP B 203     184.660 225.712 196.204  1.00162.39           O  
ATOM   3004  CB  TRP B 203     182.783 223.586 197.727  1.00162.39           C  
ATOM   3005  CG  TRP B 203     182.638 222.101 197.912  1.00162.39           C  
ATOM   3006  CD1 TRP B 203     183.644 221.191 198.024  1.00162.39           C  
ATOM   3007  CD2 TRP B 203     181.414 221.356 197.986  1.00162.39           C  
ATOM   3008  NE1 TRP B 203     183.128 219.927 198.175  1.00162.39           N  
ATOM   3009  CE2 TRP B 203     181.761 219.999 198.153  1.00162.39           C  
ATOM   3010  CE3 TRP B 203     180.060 221.703 197.932  1.00162.39           C  
ATOM   3011  CZ2 TRP B 203     180.806 218.990 198.266  1.00162.39           C  
ATOM   3012  CZ3 TRP B 203     179.110 220.695 198.044  1.00162.39           C  
ATOM   3013  CH2 TRP B 203     179.490 219.357 198.209  1.00162.39           C  
ATOM   3014  N   LEU B 204     184.130 226.524 198.236  1.00162.82           N  
ATOM   3015  CA  LEU B 204     184.052 227.903 197.765  1.00162.82           C  
ATOM   3016  C   LEU B 204     185.369 228.373 197.159  1.00162.82           C  
ATOM   3017  O   LEU B 204     185.380 228.973 196.079  1.00162.82           O  
ATOM   3018  CB  LEU B 204     183.639 228.815 198.920  1.00162.82           C  
ATOM   3019  CG  LEU B 204     183.256 230.271 198.646  1.00162.82           C  
ATOM   3020  CD1 LEU B 204     182.252 230.727 199.685  1.00162.82           C  
ATOM   3021  CD2 LEU B 204     184.470 231.191 198.645  1.00162.82           C  
ATOM   3022  N   GLN B 205     186.468 228.146 197.882  1.00161.31           N  
ATOM   3023  CA  GLN B 205     187.811 228.666 197.502  1.00161.31           C  
ATOM   3024  C   GLN B 205     188.269 228.157 196.131  1.00161.31           C  
ATOM   3025  O   GLN B 205     188.842 228.965 195.374  1.00161.31           O  
ATOM   3026  CB  GLN B 205     188.832 228.281 198.575  1.00161.31           C  
ATOM   3027  CG  GLN B 205     188.539 228.887 199.940  1.00161.31           C  
ATOM   3028  CD  GLN B 205     189.572 228.522 200.978  1.00161.31           C  
ATOM   3029  OE1 GLN B 205     189.691 229.169 202.016  1.00161.31           O  
ATOM   3030  NE2 GLN B 205     190.334 227.475 200.704  1.00161.31           N  
ATOM   3031  N   LEU B 206     188.029 226.883 195.820  1.00161.21           N  
ATOM   3032  CA  LEU B 206     188.494 226.326 194.555  1.00161.21           C  
ATOM   3033  C   LEU B 206     187.642 226.799 193.385  1.00161.21           C  
ATOM   3034  O   LEU B 206     188.101 226.766 192.238  1.00161.21           O  
ATOM   3035  CB  LEU B 206     188.531 224.798 194.628  1.00161.21           C  
ATOM   3036  CG  LEU B 206     187.267 223.962 194.829  1.00161.21           C  
ATOM   3037  CD1 LEU B 206     186.629 223.603 193.493  1.00161.21           C  
ATOM   3038  CD2 LEU B 206     187.598 222.710 195.613  1.00161.21           C  
ATOM   3039  N   LEU B 207     186.408 227.240 193.643  1.00163.28           N  
ATOM   3040  CA  LEU B 207     185.616 227.854 192.584  1.00163.28           C  
ATOM   3041  C   LEU B 207     186.173 229.204 192.157  1.00163.28           C  
ATOM   3042  O   LEU B 207     185.977 229.602 191.006  1.00163.28           O  
ATOM   3043  CB  LEU B 207     184.161 228.029 193.020  1.00163.28           C  
ATOM   3044  CG  LEU B 207     183.393 226.868 193.650  1.00163.28           C  
ATOM   3045  CD1 LEU B 207     181.903 227.187 193.697  1.00163.28           C  
ATOM   3046  CD2 LEU B 207     183.638 225.572 192.889  1.00163.28           C  
ATOM   3047  N   ARG B 208     186.854 229.917 193.052  1.00161.67           N  
ATOM   3048  CA  ARG B 208     187.402 231.223 192.709  1.00161.67           C  
ATOM   3049  C   ARG B 208     188.601 231.136 191.781  1.00161.67           C  
ATOM   3050  O   ARG B 208     188.713 231.923 190.835  1.00161.67           O  
ATOM   3051  CB  ARG B 208     187.836 231.975 193.963  1.00161.67           C  
ATOM   3052  CG  ARG B 208     186.769 232.273 194.982  1.00161.67           C  
ATOM   3053  CD  ARG B 208     187.177 233.493 195.814  1.00161.67           C  
ATOM   3054  NE  ARG B 208     188.565 233.437 196.277  1.00161.67           N  
ATOM   3055  CZ  ARG B 208     189.584 234.065 195.693  1.00161.67           C  
ATOM   3056  NH1 ARG B 208     190.808 233.951 196.185  1.00161.67           N  
ATOM   3057  NH2 ARG B 208     189.384 234.798 194.608  1.00161.67           N  
ATOM   3058  N   VAL B 209     189.504 230.196 192.042  1.00163.03           N  
ATOM   3059  CA  VAL B 209     190.848 230.216 191.481  1.00163.03           C  
ATOM   3060  C   VAL B 209     190.810 229.821 190.010  1.00163.03           C  
ATOM   3061  O   VAL B 209     191.785 230.020 189.275  1.00163.03           O  
ATOM   3062  CB  VAL B 209     191.774 229.292 192.293  1.00163.03           C  
ATOM   3063  CG1 VAL B 209     191.237 227.871 192.293  1.00163.03           C  
ATOM   3064  CG2 VAL B 209     193.209 229.361 191.798  1.00163.03           C  
ATOM   3065  N   CYS B 210     189.666 229.304 189.558  1.00166.32           N  
ATOM   3066  CA  CYS B 210     189.556 228.785 188.198  1.00166.32           C  
ATOM   3067  C   CYS B 210     189.923 229.820 187.144  1.00166.32           C  
ATOM   3068  O   CYS B 210     190.322 229.445 186.034  1.00166.32           O  
ATOM   3069  CB  CYS B 210     188.134 228.293 187.952  1.00166.32           C  
ATOM   3070  SG  CYS B 210     187.789 226.632 188.563  1.00166.32           S  
ATOM   3071  N   ARG B 211     189.813 231.105 187.485  1.00166.20           N  
ATOM   3072  CA  ARG B 211     190.089 232.187 186.546  1.00166.20           C  
ATOM   3073  C   ARG B 211     191.364 231.942 185.745  1.00166.20           C  
ATOM   3074  O   ARG B 211     191.327 231.861 184.512  1.00166.20           O  
ATOM   3075  CB  ARG B 211     190.188 233.501 187.315  1.00166.20           C  
ATOM   3076  CG  ARG B 211     190.907 234.595 186.573  1.00166.20           C  
ATOM   3077  CD  ARG B 211     191.410 235.619 187.553  1.00166.20           C  
ATOM   3078  NE  ARG B 211     190.300 236.346 188.153  1.00166.20           N  
ATOM   3079  CZ  ARG B 211     190.444 237.406 188.935  1.00166.20           C  
ATOM   3080  NH1 ARG B 211     189.378 238.010 189.438  1.00166.20           N  
ATOM   3081  NH2 ARG B 211     191.657 237.860 189.209  1.00166.20           N  
ATOM   3082  N   VAL B 212     192.498 231.784 186.432  1.00167.72           N  
ATOM   3083  CA  VAL B 212     193.793 231.748 185.760  1.00167.72           C  
ATOM   3084  C   VAL B 212     193.819 230.743 184.618  1.00167.72           C  
ATOM   3085  O   VAL B 212     194.608 230.897 183.674  1.00167.72           O  
ATOM   3086  CB  VAL B 212     194.901 231.464 186.795  1.00167.72           C  
ATOM   3087  CG1 VAL B 212     196.272 231.532 186.154  1.00167.72           C  
ATOM   3088  CG2 VAL B 212     194.820 232.469 187.926  1.00167.72           C  
ATOM   3089  N   LEU B 213     192.926 229.747 184.649  1.00169.04           N  
ATOM   3090  CA  LEU B 213     192.848 228.769 183.569  1.00169.04           C  
ATOM   3091  C   LEU B 213     192.922 229.415 182.190  1.00169.04           C  
ATOM   3092  O   LEU B 213     193.559 228.864 181.283  1.00169.04           O  
ATOM   3093  CB  LEU B 213     191.557 227.962 183.700  1.00169.04           C  
ATOM   3094  CG  LEU B 213     191.656 226.685 184.528  1.00169.04           C  
ATOM   3095  CD1 LEU B 213     190.277 226.119 184.758  1.00169.04           C  
ATOM   3096  CD2 LEU B 213     192.533 225.680 183.820  1.00169.04           C  
ATOM   3097  N   ARG B 214     192.334 230.607 182.031  1.00171.29           N  
ATOM   3098  CA  ARG B 214     192.259 231.230 180.712  1.00171.29           C  
ATOM   3099  C   ARG B 214     193.616 231.235 180.020  1.00171.29           C  
ATOM   3100  O   ARG B 214     193.718 230.927 178.821  1.00171.29           O  
ATOM   3101  CB  ARG B 214     191.744 232.668 180.826  1.00171.29           C  
ATOM   3102  CG  ARG B 214     190.608 232.895 181.806  1.00171.29           C  
ATOM   3103  CD  ARG B 214     189.266 232.406 181.301  1.00171.29           C  
ATOM   3104  NE  ARG B 214     188.766 233.196 180.179  1.00171.29           N  
ATOM   3105  CZ  ARG B 214     187.562 233.036 179.642  1.00171.29           C  
ATOM   3106  NH1 ARG B 214     187.181 233.790 178.623  1.00171.29           N  
ATOM   3107  NH2 ARG B 214     186.730 232.134 180.142  1.00171.29           N  
ATOM   3108  N   SER B 215     194.681 231.527 180.775  1.00171.09           N  
ATOM   3109  CA  SER B 215     195.988 231.757 180.165  1.00171.09           C  
ATOM   3110  C   SER B 215     196.460 230.588 179.317  1.00171.09           C  
ATOM   3111  O   SER B 215     197.428 230.744 178.564  1.00171.09           O  
ATOM   3112  CB  SER B 215     197.036 232.049 181.233  1.00171.09           C  
ATOM   3113  OG  SER B 215     198.299 232.271 180.636  1.00171.09           O  
ATOM   3114  N   LEU B 216     195.799 229.428 179.412  1.00172.62           N  
ATOM   3115  CA  LEU B 216     196.171 228.315 178.546  1.00172.62           C  
ATOM   3116  C   LEU B 216     196.170 228.735 177.080  1.00172.62           C  
ATOM   3117  O   LEU B 216     197.138 228.472 176.354  1.00172.62           O  
ATOM   3118  CB  LEU B 216     195.245 227.119 178.787  1.00172.62           C  
ATOM   3119  CG  LEU B 216     193.734 227.219 178.564  1.00172.62           C  
ATOM   3120  CD1 LEU B 216     193.377 226.853 177.156  1.00172.62           C  
ATOM   3121  CD2 LEU B 216     193.010 226.287 179.517  1.00172.62           C  
ATOM   3122  N   LYS B 217     195.122 229.439 176.662  1.00172.77           N  
ATOM   3123  CA  LYS B 217     195.015 229.859 175.243  1.00172.77           C  
ATOM   3124  C   LYS B 217     196.251 230.687 174.875  1.00172.77           C  
ATOM   3125  O   LYS B 217     196.712 230.570 173.723  1.00172.77           O  
ATOM   3126  CB  LYS B 217     193.741 230.685 175.043  1.00172.77           C  
ATOM   3127  CG  LYS B 217     192.440 229.968 175.380  1.00172.77           C  
ATOM   3128  CD  LYS B 217     191.210 230.824 175.165  1.00172.77           C  
ATOM   3129  CE  LYS B 217     191.210 232.084 176.003  1.00172.77           C  
ATOM   3130  NZ  LYS B 217     189.995 232.899 175.769  1.00172.77           N  
ATOM   3131  N   LEU B 218     196.763 231.485 175.816  1.00168.81           N  
ATOM   3132  CA  LEU B 218     197.893 232.358 175.522  1.00168.81           C  
ATOM   3133  C   LEU B 218     199.066 231.571 174.961  1.00168.81           C  
ATOM   3134  O   LEU B 218     199.828 232.094 174.140  1.00168.81           O  
ATOM   3135  CB  LEU B 218     198.309 233.123 176.781  1.00168.81           C  
ATOM   3136  CG  LEU B 218     199.365 234.230 176.667  1.00168.81           C  
ATOM   3137  CD1 LEU B 218     199.169 235.256 177.770  1.00168.81           C  
ATOM   3138  CD2 LEU B 218     200.788 233.684 176.727  1.00168.81           C  
ATOM   3139  N   PHE B 219     199.229 230.319 175.382  1.00164.17           N  
ATOM   3140  CA  PHE B 219     200.372 229.554 174.911  1.00164.17           C  
ATOM   3141  C   PHE B 219     200.088 228.812 173.615  1.00164.17           C  
ATOM   3142  O   PHE B 219     201.020 228.265 173.019  1.00164.17           O  
ATOM   3143  CB  PHE B 219     200.831 228.587 176.000  1.00164.17           C  
ATOM   3144  CG  PHE B 219     201.596 229.258 177.106  1.00164.17           C  
ATOM   3145  CD1 PHE B 219     200.927 229.927 178.116  1.00164.17           C  
ATOM   3146  CD2 PHE B 219     202.980 229.221 177.137  1.00164.17           C  
ATOM   3147  CE1 PHE B 219     201.622 230.546 179.132  1.00164.17           C  
ATOM   3148  CE2 PHE B 219     203.680 229.841 178.150  1.00164.17           C  
ATOM   3149  CZ  PHE B 219     202.999 230.503 179.150  1.00164.17           C  
ATOM   3150  N   ALA B 220     198.838 228.797 173.151  1.00165.52           N  
ATOM   3151  CA  ALA B 220     198.573 228.283 171.816  1.00165.52           C  
ATOM   3152  C   ALA B 220     199.259 229.118 170.749  1.00165.52           C  
ATOM   3153  O   ALA B 220     199.479 228.629 169.638  1.00165.52           O  
ATOM   3154  CB  ALA B 220     197.070 228.235 171.554  1.00165.52           C  
ATOM   3155  N   ARG B 221     199.605 230.364 171.073  1.00162.33           N  
ATOM   3156  CA  ARG B 221     200.284 231.246 170.133  1.00162.33           C  
ATOM   3157  C   ARG B 221     201.759 230.896 169.974  1.00162.33           C  
ATOM   3158  O   ARG B 221     202.396 231.359 169.022  1.00162.33           O  
ATOM   3159  CB  ARG B 221     200.128 232.695 170.593  1.00162.33           C  
ATOM   3160  CG  ARG B 221     200.472 233.720 169.544  1.00162.33           C  
ATOM   3161  CD  ARG B 221     199.708 235.013 169.757  1.00162.33           C  
ATOM   3162  NE  ARG B 221     200.492 236.166 169.328  1.00162.33           N  
ATOM   3163  CZ  ARG B 221     200.767 236.459 168.060  1.00162.33           C  
ATOM   3164  NH1 ARG B 221     200.313 235.691 167.079  1.00162.33           N  
ATOM   3165  NH2 ARG B 221     201.493 237.530 167.775  1.00162.33           N  
ATOM   3166  N   PHE B 222     202.314 230.098 170.879  1.00151.05           N  
ATOM   3167  CA  PHE B 222     203.690 229.654 170.730  1.00151.05           C  
ATOM   3168  C   PHE B 222     203.772 228.535 169.698  1.00151.05           C  
ATOM   3169  O   PHE B 222     202.902 227.665 169.620  1.00151.05           O  
ATOM   3170  CB  PHE B 222     204.248 229.188 172.070  1.00151.05           C  
ATOM   3171  CG  PHE B 222     204.603 230.311 172.998  1.00151.05           C  
ATOM   3172  CD1 PHE B 222     203.649 231.232 173.388  1.00151.05           C  
ATOM   3173  CD2 PHE B 222     205.891 230.443 173.482  1.00151.05           C  
ATOM   3174  CE1 PHE B 222     203.972 232.263 174.241  1.00151.05           C  
ATOM   3175  CE2 PHE B 222     206.220 231.472 174.337  1.00151.05           C  
ATOM   3176  CZ  PHE B 222     205.259 232.385 174.715  1.00151.05           C  
ATOM   3177  N   ARG B 223     204.798 228.650 168.852  1.00136.89           N  
ATOM   3178  CA  ARG B 223     205.108 227.908 167.593  1.00136.89           C  
ATOM   3179  C   ARG B 223     205.381 226.396 167.686  1.00136.89           C  
ATOM   3180  O   ARG B 223     204.771 225.680 166.883  1.00136.89           O  
ATOM   3181  CB  ARG B 223     206.344 228.574 166.972  1.00136.89           C  
ATOM   3182  CG  ARG B 223     206.535 230.051 167.306  1.00136.89           C  
ATOM   3183  CD  ARG B 223     206.889 230.382 168.746  1.00136.89           C  
ATOM   3184  NE  ARG B 223     208.286 230.219 169.119  1.00136.89           N  
ATOM   3185  CZ  ARG B 223     208.948 229.072 169.107  1.00136.89           C  
ATOM   3186  NH1 ARG B 223     210.215 229.032 169.480  1.00136.89           N  
ATOM   3187  NH2 ARG B 223     208.348 227.966 168.716  1.00136.89           N  
ATOM   3188  N   GLN B 224     206.262 225.984 168.595  1.00129.57           N  
ATOM   3189  CA  GLN B 224     206.579 224.546 168.793  1.00129.57           C  
ATOM   3190  C   GLN B 224     205.532 223.918 169.725  1.00129.57           C  
ATOM   3191  O   GLN B 224     205.094 222.779 169.464  1.00129.57           O  
ATOM   3192  CB  GLN B 224     208.012 224.397 169.313  1.00129.57           C  
ATOM   3193  CG  GLN B 224     208.924 225.538 168.882  1.00129.57           C  
ATOM   3194  CD  GLN B 224     210.390 225.203 168.791  1.00129.57           C  
ATOM   3195  OE1 GLN B 224     211.245 226.027 169.102  1.00129.57           O  
ATOM   3196  NE2 GLN B 224     210.691 224.002 168.327  1.00129.57           N  
ATOM   3197  N   ILE B 225     205.119 224.657 170.752  1.00122.77           N  
ATOM   3198  CA  ILE B 225     204.187 224.090 171.719  1.00122.77           C  
ATOM   3199  C   ILE B 225     203.054 223.378 170.999  1.00122.77           C  
ATOM   3200  O   ILE B 225     202.609 222.305 171.416  1.00122.77           O  
ATOM   3201  CB  ILE B 225     203.663 225.188 172.658  1.00122.77           C  
ATOM   3202  CG1 ILE B 225     204.722 225.541 173.693  1.00122.77           C  
ATOM   3203  CG2 ILE B 225     202.385 224.753 173.336  1.00122.77           C  
ATOM   3204  CD1 ILE B 225     204.272 226.578 174.675  1.00122.77           C  
ATOM   3205  N   LYS B 226     202.573 223.960 169.902  1.00117.37           N  
ATOM   3206  CA  LYS B 226     201.523 223.319 169.122  1.00117.37           C  
ATOM   3207  C   LYS B 226     201.983 221.963 168.604  1.00117.37           C  
ATOM   3208  O   LYS B 226     201.239 220.977 168.661  1.00117.37           O  
ATOM   3209  CB  LYS B 226     201.118 224.227 167.962  1.00117.37           C  
ATOM   3210  CG  LYS B 226     199.870 223.798 167.222  1.00117.37           C  
ATOM   3211  CD  LYS B 226     198.632 224.440 167.813  1.00117.37           C  
ATOM   3212  CE  LYS B 226     197.398 224.086 167.001  1.00117.37           C  
ATOM   3213  NZ  LYS B 226     197.518 224.518 165.582  1.00117.37           N  
ATOM   3214  N   VAL B 227     203.215 221.896 168.098  1.00114.55           N  
ATOM   3215  CA  VAL B 227     203.745 220.639 167.582  1.00114.55           C  
ATOM   3216  C   VAL B 227     203.846 219.605 168.691  1.00114.55           C  
ATOM   3217  O   VAL B 227     203.450 218.445 168.518  1.00114.55           O  
ATOM   3218  CB  VAL B 227     205.110 220.870 166.918  1.00114.55           C  
ATOM   3219  CG1 VAL B 227     205.838 219.554 166.756  1.00114.55           C  
ATOM   3220  CG2 VAL B 227     204.936 221.559 165.577  1.00114.55           C  
ATOM   3221  N   ILE B 228     204.458 219.992 169.806  1.00104.52           N  
ATOM   3222  CA  ILE B 228     204.644 218.987 170.885  1.00104.52           C  
ATOM   3223  C   ILE B 228     203.266 218.531 171.339  1.00104.52           C  
ATOM   3224  O   ILE B 228     203.071 217.333 171.456  1.00104.52           O  
ATOM   3225  CB  ILE B 228     205.449 219.596 172.047  1.00104.52           C  
ATOM   3226  CG1 ILE B 228     206.871 219.955 171.620  1.00104.52           C  
ATOM   3227  CG2 ILE B 228     205.450 218.668 173.242  1.00104.52           C  
ATOM   3228  CD1 ILE B 228     207.490 218.960 170.677  1.00104.52           C  
ATOM   3229  N   LEU B 229     202.344 219.465 171.548  1.00102.47           N  
ATOM   3230  CA  LEU B 229     201.012 219.073 172.063  1.00102.47           C  
ATOM   3231  C   LEU B 229     200.240 218.206 171.082  1.00102.47           C  
ATOM   3232  O   LEU B 229     199.724 217.192 171.520  1.00102.47           O  
ATOM   3233  CB  LEU B 229     200.212 220.325 172.397  1.00102.47           C  
ATOM   3234  CG  LEU B 229     200.745 221.116 173.578  1.00102.47           C  
ATOM   3235  CD1 LEU B 229     199.670 222.035 174.111  1.00102.47           C  
ATOM   3236  CD2 LEU B 229     201.227 220.189 174.672  1.00102.47           C  
ATOM   3237  N   LEU B 230     200.187 218.570 169.806  1.00103.50           N  
ATOM   3238  CA  LEU B 230     199.385 217.709 168.906  1.00103.50           C  
ATOM   3239  C   LEU B 230     200.011 216.319 168.926  1.00103.50           C  
ATOM   3240  O   LEU B 230     199.274 215.340 169.085  1.00103.50           O  
ATOM   3241  CB  LEU B 230     199.409 218.270 167.485  1.00103.50           C  
ATOM   3242  CG  LEU B 230     198.966 217.252 166.437  1.00103.50           C  
ATOM   3243  CD1 LEU B 230     197.638 216.631 166.828  1.00103.50           C  
ATOM   3244  CD2 LEU B 230     198.895 217.873 165.050  1.00103.50           C  
ATOM   3245  N   ALA B 231     201.336 216.255 168.821  1.00 97.90           N  
ATOM   3246  CA  ALA B 231     201.998 214.937 168.815  1.00 97.90           C  
ATOM   3247  C   ALA B 231     201.684 214.260 170.142  1.00 97.90           C  
ATOM   3248  O   ALA B 231     201.391 213.074 170.135  1.00 97.90           O  
ATOM   3249  CB  ALA B 231     203.475 215.105 168.608  1.00 97.90           C  
ATOM   3250  N   LEU B 232     201.698 215.016 171.233  1.00 93.98           N  
ATOM   3251  CA  LEU B 232     201.411 214.439 172.568  1.00 93.98           C  
ATOM   3252  C   LEU B 232     199.984 213.889 172.621  1.00 93.98           C  
ATOM   3253  O   LEU B 232     199.812 212.841 173.215  1.00 93.98           O  
ATOM   3254  CB  LEU B 232     201.635 215.506 173.637  1.00 93.98           C  
ATOM   3255  CG  LEU B 232     201.480 215.036 175.081  1.00 93.98           C  
ATOM   3256  CD1 LEU B 232     200.066 215.263 175.574  1.00 93.98           C  
ATOM   3257  CD2 LEU B 232     201.875 213.582 175.242  1.00 93.98           C  
ATOM   3258  N   VAL B 233     199.003 214.569 172.031  1.00 95.36           N  
ATOM   3259  CA  VAL B 233     197.597 214.067 172.032  1.00 95.36           C  
ATOM   3260  C   VAL B 233     197.483 212.882 171.079  1.00 95.36           C  
ATOM   3261  O   VAL B 233     196.791 211.930 171.411  1.00 95.36           O  
ATOM   3262  CB  VAL B 233     196.597 215.171 171.664  1.00 95.36           C  
ATOM   3263  CG1 VAL B 233     196.552 216.248 172.734  1.00 95.36           C  
ATOM   3264  CG2 VAL B 233     196.911 215.773 170.311  1.00 95.36           C  
ATOM   3265  N   ARG B 234     198.138 212.959 169.928  1.00 93.92           N  
ATOM   3266  CA  ARG B 234     198.054 211.845 168.957  1.00 93.92           C  
ATOM   3267  C   ARG B 234     198.688 210.582 169.547  1.00 93.92           C  
ATOM   3268  O   ARG B 234     198.090 209.512 169.435  1.00 93.92           O  
ATOM   3269  CB  ARG B 234     198.726 212.281 167.656  1.00 93.92           C  
ATOM   3270  CG  ARG B 234     199.235 211.136 166.801  1.00 93.92           C  
ATOM   3271  CD  ARG B 234     200.145 211.719 165.754  1.00 93.92           C  
ATOM   3272  NE  ARG B 234     199.885 211.051 164.498  1.00 93.92           N  
ATOM   3273  CZ  ARG B 234     200.548 209.993 164.073  1.00 93.92           C  
ATOM   3274  NH1 ARG B 234     201.529 209.499 164.805  1.00 93.92           N  
ATOM   3275  NH2 ARG B 234     200.233 209.441 162.917  1.00 93.92           N  
ATOM   3276  N   ALA B 235     199.853 210.701 170.170  1.00 93.02           N  
ATOM   3277  CA  ALA B 235     200.489 209.503 170.752  1.00 93.02           C  
ATOM   3278  C   ALA B 235     199.599 208.966 171.867  1.00 93.02           C  
ATOM   3279  O   ALA B 235     199.406 207.768 171.916  1.00 93.02           O  
ATOM   3280  CB  ALA B 235     201.860 209.838 171.268  1.00 93.02           C  
ATOM   3281  N   LEU B 236     199.024 209.839 172.684  1.00 89.35           N  
ATOM   3282  CA  LEU B 236     198.191 209.348 173.800  1.00 89.35           C  
ATOM   3283  C   LEU B 236     197.091 208.473 173.226  1.00 89.35           C  
ATOM   3284  O   LEU B 236     196.762 207.482 173.844  1.00 89.35           O  
ATOM   3285  CB  LEU B 236     197.571 210.546 174.509  1.00 89.35           C  
ATOM   3286  CG  LEU B 236     198.497 211.298 175.453  1.00 89.35           C  
ATOM   3287  CD1 LEU B 236     197.692 212.064 176.483  1.00 89.35           C  
ATOM   3288  CD2 LEU B 236     199.457 210.348 176.142  1.00 89.35           C  
ATOM   3289  N   LYS B 237     196.588 208.849 172.053  1.00 91.01           N  
ATOM   3290  CA  LYS B 237     195.523 208.074 171.373  1.00 91.01           C  
ATOM   3291  C   LYS B 237     196.068 206.675 171.071  1.00 91.01           C  
ATOM   3292  O   LYS B 237     195.283 205.711 171.158  1.00 91.01           O  
ATOM   3293  CB  LYS B 237     195.115 208.782 170.078  1.00 91.01           C  
ATOM   3294  CG  LYS B 237     194.013 208.097 169.280  1.00 91.01           C  
ATOM   3295  CD  LYS B 237     193.639 208.839 168.015  1.00 91.01           C  
ATOM   3296  CE  LYS B 237     192.538 208.156 167.230  1.00 91.01           C  
ATOM   3297  NZ  LYS B 237     192.195 208.907 166.000  1.00 91.01           N  
ATOM   3298  N   SER B 238     197.358 206.571 170.727  1.00 93.15           N  
ATOM   3299  CA  SER B 238     197.894 205.264 170.352  1.00 93.15           C  
ATOM   3300  C   SER B 238     197.799 204.262 171.494  1.00 93.15           C  
ATOM   3301  O   SER B 238     197.335 203.133 171.306  1.00 93.15           O  
ATOM   3302  CB  SER B 238     199.344 205.399 169.917  1.00 93.15           C  
ATOM   3303  OG  SER B 238     200.145 205.791 171.015  1.00 93.15           O  
ATOM   3304  N   MET B 239     198.247 204.650 172.683  1.00 92.12           N  
ATOM   3305  CA  MET B 239     198.335 203.727 173.814  1.00 92.12           C  
ATOM   3306  C   MET B 239     197.051 203.717 174.632  1.00 92.12           C  
ATOM   3307  O   MET B 239     197.051 203.777 175.856  1.00 92.12           O  
ATOM   3308  CB  MET B 239     199.539 204.088 174.674  1.00 92.12           C  
ATOM   3309  CG  MET B 239     199.458 205.442 175.335  1.00 92.12           C  
ATOM   3310  SD  MET B 239     200.949 205.835 176.244  1.00 92.12           S  
ATOM   3311  CE  MET B 239     202.073 206.170 174.899  1.00 92.12           C  
ATOM   3312  N   THR B 240     195.927 203.595 173.940  1.00 93.16           N  
ATOM   3313  CA  THR B 240     194.642 203.670 174.616  1.00 93.16           C  
ATOM   3314  C   THR B 240     194.356 202.412 175.420  1.00 93.16           C  
ATOM   3315  O   THR B 240     193.889 202.497 176.558  1.00 93.16           O  
ATOM   3316  CB  THR B 240     193.541 203.909 173.594  1.00 93.16           C  
ATOM   3317  OG1 THR B 240     193.801 205.137 172.905  1.00 93.16           O  
ATOM   3318  CG2 THR B 240     192.208 204.006 174.286  1.00 93.16           C  
ATOM   3319  N   PHE B 241     194.632 201.241 174.858  1.00 92.98           N  
ATOM   3320  CA  PHE B 241     194.335 199.992 175.541  1.00 92.98           C  
ATOM   3321  C   PHE B 241     195.351 199.637 176.616  1.00 92.98           C  
ATOM   3322  O   PHE B 241     195.013 198.911 177.563  1.00 92.98           O  
ATOM   3323  CB  PHE B 241     194.236 198.871 174.517  1.00 92.98           C  
ATOM   3324  CG  PHE B 241     193.035 198.983 173.643  1.00 92.98           C  
ATOM   3325  CD1 PHE B 241     191.786 198.644 174.123  1.00 92.98           C  
ATOM   3326  CD2 PHE B 241     193.147 199.457 172.352  1.00 92.98           C  
ATOM   3327  CE1 PHE B 241     190.675 198.761 173.332  1.00 92.98           C  
ATOM   3328  CE2 PHE B 241     192.035 199.577 171.554  1.00 92.98           C  
ATOM   3329  CZ  PHE B 241     190.796 199.227 172.047  1.00 92.98           C  
ATOM   3330  N   LEU B 242     196.582 200.137 176.498  1.00 86.69           N  
ATOM   3331  CA  LEU B 242     197.561 199.941 177.558  1.00 86.69           C  
ATOM   3332  C   LEU B 242     197.056 200.511 178.874  1.00 86.69           C  
ATOM   3333  O   LEU B 242     197.209 199.892 179.938  1.00 86.69           O  
ATOM   3334  CB  LEU B 242     198.878 200.590 177.162  1.00 86.69           C  
ATOM   3335  CG  LEU B 242     199.933 200.592 178.253  1.00 86.69           C  
ATOM   3336  CD1 LEU B 242     200.378 199.174 178.538  1.00 86.69           C  
ATOM   3337  CD2 LEU B 242     201.098 201.455 177.832  1.00 86.69           C  
ATOM   3338  N   LEU B 243     196.440 201.686 178.824  1.00 85.96           N  
ATOM   3339  CA  LEU B 243     195.874 202.246 180.037  1.00 85.96           C  
ATOM   3340  C   LEU B 243     194.746 201.378 180.564  1.00 85.96           C  
ATOM   3341  O   LEU B 243     194.498 201.351 181.771  1.00 85.96           O  
ATOM   3342  CB  LEU B 243     195.397 203.668 179.776  1.00 85.96           C  
ATOM   3343  CG  LEU B 243     196.392 204.497 178.962  1.00 85.96           C  
ATOM   3344  CD1 LEU B 243     195.880 205.916 178.753  1.00 85.96           C  
ATOM   3345  CD2 LEU B 243     197.757 204.503 179.622  1.00 85.96           C  
ATOM   3346  N   MET B 244     194.075 200.627 179.695  1.00 85.66           N  
ATOM   3347  CA  MET B 244     193.022 199.758 180.202  1.00 85.66           C  
ATOM   3348  C   MET B 244     193.613 198.531 180.888  1.00 85.66           C  
ATOM   3349  O   MET B 244     193.066 198.051 181.889  1.00 85.66           O  
ATOM   3350  CB  MET B 244     192.062 199.369 179.082  1.00 85.66           C  
ATOM   3351  CG  MET B 244     190.900 198.540 179.577  1.00 85.66           C  
ATOM   3352  SD  MET B 244     189.667 198.118 178.336  1.00 85.66           S  
ATOM   3353  CE  MET B 244     188.580 197.081 179.318  1.00 85.66           C  
ATOM   3354  N   LEU B 245     194.748 198.024 180.393  1.00 79.26           N  
ATOM   3355  CA  LEU B 245     195.472 197.016 181.167  1.00 79.26           C  
ATOM   3356  C   LEU B 245     195.905 197.548 182.525  1.00 79.26           C  
ATOM   3357  O   LEU B 245     195.776 196.849 183.536  1.00 79.26           O  
ATOM   3358  CB  LEU B 245     196.691 196.489 180.417  1.00 79.26           C  
ATOM   3359  CG  LEU B 245     196.463 195.432 179.356  1.00 79.26           C  
ATOM   3360  CD1 LEU B 245     197.763 195.096 178.675  1.00 79.26           C  
ATOM   3361  CD2 LEU B 245     195.917 194.213 180.040  1.00 79.26           C  
ATOM   3362  N   LEU B 246     196.441 198.769 182.577  1.00 72.99           N  
ATOM   3363  CA  LEU B 246     196.797 199.323 183.882  1.00 72.99           C  
ATOM   3364  C   LEU B 246     195.592 199.442 184.799  1.00 72.99           C  
ATOM   3365  O   LEU B 246     195.705 199.199 186.002  1.00 72.99           O  
ATOM   3366  CB  LEU B 246     197.483 200.675 183.755  1.00 72.99           C  
ATOM   3367  CG  LEU B 246     198.854 200.650 183.132  1.00 72.99           C  
ATOM   3368  CD1 LEU B 246     199.354 202.051 182.931  1.00 72.99           C  
ATOM   3369  CD2 LEU B 246     199.708 199.953 184.151  1.00 72.99           C  
ATOM   3370  N   LEU B 247     194.447 199.868 184.278  1.00 73.55           N  
ATOM   3371  CA  LEU B 247     193.277 199.951 185.143  1.00 73.55           C  
ATOM   3372  C   LEU B 247     192.890 198.578 185.662  1.00 73.55           C  
ATOM   3373  O   LEU B 247     192.561 198.421 186.845  1.00 73.55           O  
ATOM   3374  CB  LEU B 247     192.113 200.606 184.412  1.00 73.55           C  
ATOM   3375  CG  LEU B 247     191.968 202.084 184.760  1.00 73.55           C  
ATOM   3376  CD1 LEU B 247     193.146 202.901 184.251  1.00 73.55           C  
ATOM   3377  CD2 LEU B 247     190.671 202.614 184.207  1.00 73.55           C  
ATOM   3378  N   ILE B 248     192.950 197.564 184.802  1.00 72.24           N  
ATOM   3379  CA  ILE B 248     192.676 196.212 185.267  1.00 72.24           C  
ATOM   3380  C   ILE B 248     193.638 195.832 186.381  1.00 72.24           C  
ATOM   3381  O   ILE B 248     193.234 195.259 187.392  1.00 72.24           O  
ATOM   3382  CB  ILE B 248     192.736 195.217 184.100  1.00 72.24           C  
ATOM   3383  CG1 ILE B 248     191.472 195.333 183.261  1.00 72.24           C  
ATOM   3384  CG2 ILE B 248     192.851 193.812 184.614  1.00 72.24           C  
ATOM   3385  CD1 ILE B 248     191.453 194.412 182.076  1.00 72.24           C  
ATOM   3386  N   PHE B 249     194.915 196.166 186.234  1.00 69.00           N  
ATOM   3387  CA  PHE B 249     195.887 195.730 187.231  1.00 69.00           C  
ATOM   3388  C   PHE B 249     195.784 196.513 188.531  1.00 69.00           C  
ATOM   3389  O   PHE B 249     196.066 195.962 189.596  1.00 69.00           O  
ATOM   3390  CB  PHE B 249     197.297 195.807 186.669  1.00 69.00           C  
ATOM   3391  CG  PHE B 249     197.644 194.656 185.790  1.00 69.00           C  
ATOM   3392  CD1 PHE B 249     197.706 193.380 186.307  1.00 69.00           C  
ATOM   3393  CD2 PHE B 249     197.900 194.841 184.451  1.00 69.00           C  
ATOM   3394  CE1 PHE B 249     198.021 192.316 185.508  1.00 69.00           C  
ATOM   3395  CE2 PHE B 249     198.214 193.777 183.646  1.00 69.00           C  
ATOM   3396  CZ  PHE B 249     198.273 192.514 184.174  1.00 69.00           C  
ATOM   3397  N   PHE B 250     195.399 197.784 188.487  1.00 67.73           N  
ATOM   3398  CA  PHE B 250     195.048 198.442 189.740  1.00 67.73           C  
ATOM   3399  C   PHE B 250     193.871 197.759 190.404  1.00 67.73           C  
ATOM   3400  O   PHE B 250     193.885 197.546 191.619  1.00 67.73           O  
ATOM   3401  CB  PHE B 250     194.768 199.930 189.556  1.00 67.73           C  
ATOM   3402  CG  PHE B 250     195.977 200.741 189.228  1.00 67.73           C  
ATOM   3403  CD1 PHE B 250     197.234 200.230 189.406  1.00 67.73           C  
ATOM   3404  CD2 PHE B 250     195.854 202.036 188.796  1.00 67.73           C  
ATOM   3405  CE1 PHE B 250     198.338 200.979 189.131  1.00 67.73           C  
ATOM   3406  CE2 PHE B 250     196.964 202.785 188.521  1.00 67.73           C  
ATOM   3407  CZ  PHE B 250     198.205 202.253 188.692  1.00 67.73           C  
ATOM   3408  N   TYR B 251     192.850 197.392 189.632  1.00 74.94           N  
ATOM   3409  CA  TYR B 251     191.767 196.614 190.219  1.00 74.94           C  
ATOM   3410  C   TYR B 251     192.322 195.379 190.910  1.00 74.94           C  
ATOM   3411  O   TYR B 251     192.063 195.140 192.098  1.00 74.94           O  
ATOM   3412  CB  TYR B 251     190.761 196.217 189.145  1.00 74.94           C  
ATOM   3413  CG  TYR B 251     189.722 195.255 189.633  1.00 74.94           C  
ATOM   3414  CD1 TYR B 251     188.561 195.716 190.219  1.00 74.94           C  
ATOM   3415  CD2 TYR B 251     189.899 193.889 189.522  1.00 74.94           C  
ATOM   3416  CE1 TYR B 251     187.607 194.853 190.676  1.00 74.94           C  
ATOM   3417  CE2 TYR B 251     188.944 193.016 189.982  1.00 74.94           C  
ATOM   3418  CZ  TYR B 251     187.800 193.509 190.556  1.00 74.94           C  
ATOM   3419  OH  TYR B 251     186.834 192.658 191.015  1.00 74.94           O  
ATOM   3420  N   ILE B 252     193.137 194.616 190.182  1.00 72.95           N  
ATOM   3421  CA  ILE B 252     193.695 193.367 190.694  1.00 72.95           C  
ATOM   3422  C   ILE B 252     194.387 193.603 192.022  1.00 72.95           C  
ATOM   3423  O   ILE B 252     193.986 193.074 193.068  1.00 72.95           O  
ATOM   3424  CB  ILE B 252     194.682 192.762 189.685  1.00 72.95           C  
ATOM   3425  CG1 ILE B 252     194.017 192.550 188.339  1.00 72.95           C  
ATOM   3426  CG2 ILE B 252     195.228 191.468 190.207  1.00 72.95           C  
ATOM   3427  CD1 ILE B 252     192.933 191.559 188.370  1.00 72.95           C  
ATOM   3428  N   PHE B 253     195.437 194.417 191.989  1.00 65.47           N  
ATOM   3429  CA  PHE B 253     196.316 194.529 193.135  1.00 65.47           C  
ATOM   3430  C   PHE B 253     195.642 195.239 194.296  1.00 65.47           C  
ATOM   3431  O   PHE B 253     195.895 194.885 195.446  1.00 65.47           O  
ATOM   3432  CB  PHE B 253     197.604 195.228 192.735  1.00 65.47           C  
ATOM   3433  CG  PHE B 253     198.556 194.348 191.975  1.00 65.47           C  
ATOM   3434  CD1 PHE B 253     198.341 194.056 190.650  1.00 65.47           C  
ATOM   3435  CD2 PHE B 253     199.662 193.816 192.588  1.00 65.47           C  
ATOM   3436  CE1 PHE B 253     199.211 193.256 189.957  1.00 65.47           C  
ATOM   3437  CE2 PHE B 253     200.524 193.014 191.898  1.00 65.47           C  
ATOM   3438  CZ  PHE B 253     200.300 192.738 190.582  1.00 65.47           C  
ATOM   3439  N   ALA B 254     194.755 196.199 194.040  1.00 70.20           N  
ATOM   3440  CA  ALA B 254     194.072 196.859 195.145  1.00 70.20           C  
ATOM   3441  C   ALA B 254     193.113 195.913 195.856  1.00 70.20           C  
ATOM   3442  O   ALA B 254     193.128 195.805 197.092  1.00 70.20           O  
ATOM   3443  CB  ALA B 254     193.332 198.092 194.639  1.00 70.20           C  
ATOM   3444  N   VAL B 255     192.263 195.212 195.100  1.00 74.16           N  
ATOM   3445  CA  VAL B 255     191.279 194.384 195.785  1.00 74.16           C  
ATOM   3446  C   VAL B 255     191.883 193.088 196.297  1.00 74.16           C  
ATOM   3447  O   VAL B 255     191.235 192.382 197.076  1.00 74.16           O  
ATOM   3448  CB  VAL B 255     190.058 194.126 194.884  1.00 74.16           C  
ATOM   3449  CG1 VAL B 255     190.384 193.166 193.820  1.00 74.16           C  
ATOM   3450  CG2 VAL B 255     188.879 193.626 195.690  1.00 74.16           C  
ATOM   3451  N   THR B 256     193.117 192.754 195.918  1.00 74.88           N  
ATOM   3452  CA  THR B 256     193.764 191.656 196.623  1.00 74.88           C  
ATOM   3453  C   THR B 256     194.627 192.126 197.779  1.00 74.88           C  
ATOM   3454  O   THR B 256     194.886 191.342 198.696  1.00 74.88           O  
ATOM   3455  CB  THR B 256     194.619 190.808 195.684  1.00 74.88           C  
ATOM   3456  OG1 THR B 256     195.159 189.710 196.421  1.00 74.88           O  
ATOM   3457  CG2 THR B 256     195.758 191.607 195.148  1.00 74.88           C  
ATOM   3458  N   GLY B 257     195.082 193.378 197.764  1.00 77.14           N  
ATOM   3459  CA  GLY B 257     195.762 193.918 198.919  1.00 77.14           C  
ATOM   3460  C   GLY B 257     194.837 194.254 200.057  1.00 77.14           C  
ATOM   3461  O   GLY B 257     195.293 194.389 201.193  1.00 77.14           O  
ATOM   3462  N   VAL B 258     193.546 194.413 199.781  1.00 81.85           N  
ATOM   3463  CA  VAL B 258     192.604 194.498 200.893  1.00 81.85           C  
ATOM   3464  C   VAL B 258     192.589 193.192 201.677  1.00 81.85           C  
ATOM   3465  O   VAL B 258     192.570 193.193 202.911  1.00 81.85           O  
ATOM   3466  CB  VAL B 258     191.199 194.873 200.398  1.00 81.85           C  
ATOM   3467  CG1 VAL B 258     190.267 195.014 201.577  1.00 81.85           C  
ATOM   3468  CG2 VAL B 258     191.248 196.156 199.629  1.00 81.85           C  
ATOM   3469  N   TYR B 259     192.606 192.058 200.978  1.00 87.07           N  
ATOM   3470  CA  TYR B 259     192.493 190.754 201.621  1.00 87.07           C  
ATOM   3471  C   TYR B 259     193.814 190.245 202.182  1.00 87.07           C  
ATOM   3472  O   TYR B 259     193.828 189.640 203.255  1.00 87.07           O  
ATOM   3473  CB  TYR B 259     191.955 189.719 200.638  1.00 87.07           C  
ATOM   3474  CG  TYR B 259     190.462 189.730 200.470  1.00 87.07           C  
ATOM   3475  CD1 TYR B 259     189.766 190.914 200.378  1.00 87.07           C  
ATOM   3476  CD2 TYR B 259     189.748 188.549 200.419  1.00 87.07           C  
ATOM   3477  CE1 TYR B 259     188.403 190.919 200.223  1.00 87.07           C  
ATOM   3478  CE2 TYR B 259     188.391 188.543 200.263  1.00 87.07           C  
ATOM   3479  CZ  TYR B 259     187.719 189.729 200.167  1.00 87.07           C  
ATOM   3480  OH  TYR B 259     186.354 189.725 200.015  1.00 87.07           O  
ATOM   3481  N   PHE B 260     194.923 190.448 201.468  1.00 84.56           N  
ATOM   3482  CA  PHE B 260     196.216 190.023 201.995  1.00 84.56           C  
ATOM   3483  C   PHE B 260     196.509 190.669 203.337  1.00 84.56           C  
ATOM   3484  O   PHE B 260     196.997 190.009 204.258  1.00 84.56           O  
ATOM   3485  CB  PHE B 260     197.347 190.358 201.026  1.00 84.56           C  
ATOM   3486  CG  PHE B 260     197.578 189.328 199.977  1.00 84.56           C  
ATOM   3487  CD1 PHE B 260     196.814 188.189 199.922  1.00 84.56           C  
ATOM   3488  CD2 PHE B 260     198.619 189.462 199.096  1.00 84.56           C  
ATOM   3489  CE1 PHE B 260     197.048 187.237 198.966  1.00 84.56           C  
ATOM   3490  CE2 PHE B 260     198.857 188.506 198.145  1.00 84.56           C  
ATOM   3491  CZ  PHE B 260     198.072 187.393 198.082  1.00 84.56           C  
ATOM   3492  N   PHE B 261     196.240 191.960 203.465  1.00 83.12           N  
ATOM   3493  CA  PHE B 261     196.600 192.705 204.658  1.00 83.12           C  
ATOM   3494  C   PHE B 261     195.317 193.123 205.360  1.00 83.12           C  
ATOM   3495  O   PHE B 261     194.861 194.259 205.249  1.00 83.12           O  
ATOM   3496  CB  PHE B 261     197.426 193.847 204.280  1.00 83.12           C  
ATOM   3497  CG  PHE B 261     198.479 193.501 203.290  1.00 83.12           C  
ATOM   3498  CD1 PHE B 261     199.569 192.750 203.665  1.00 83.12           C  
ATOM   3499  CD2 PHE B 261     198.378 193.908 201.981  1.00 83.12           C  
ATOM   3500  CE1 PHE B 261     200.542 192.422 202.755  1.00 83.12           C  
ATOM   3501  CE2 PHE B 261     199.352 193.581 201.068  1.00 83.12           C  
ATOM   3502  CZ  PHE B 261     200.434 192.837 201.455  1.00 83.12           C  
ATOM   3503  N   ARG B 262     194.748 192.190 206.105  1.00 92.11           N  
ATOM   3504  CA  ARG B 262     193.587 192.454 206.939  1.00 92.11           C  
ATOM   3505  C   ARG B 262     193.913 192.357 208.412  1.00 92.11           C  
ATOM   3506  O   ARG B 262     193.496 193.213 209.187  1.00 92.11           O  
ATOM   3507  CB  ARG B 262     192.451 191.486 206.608  1.00 92.11           C  
ATOM   3508  CG  ARG B 262     191.099 191.992 207.038  1.00 92.11           C  
ATOM   3509  CD  ARG B 262     190.042 190.914 206.943  1.00 92.11           C  
ATOM   3510  NE  ARG B 262     189.624 190.631 205.573  1.00 92.11           N  
ATOM   3511  CZ  ARG B 262     188.814 191.406 204.859  1.00 92.11           C  
ATOM   3512  NH1 ARG B 262     188.484 191.061 203.625  1.00 92.11           N  
ATOM   3513  NH2 ARG B 262     188.341 192.529 205.375  1.00 92.11           N  
ATOM   3514  N   GLU B 263     194.668 191.338 208.815  1.00 95.31           N  
ATOM   3515  CA  GLU B 263     195.180 191.300 210.175  1.00 95.31           C  
ATOM   3516  C   GLU B 263     196.134 192.454 210.435  1.00 95.31           C  
ATOM   3517  O   GLU B 263     196.333 192.849 211.587  1.00 95.31           O  
ATOM   3518  CB  GLU B 263     195.869 189.962 210.430  1.00 95.31           C  
ATOM   3519  CG  GLU B 263     197.106 189.720 209.593  1.00 95.31           C  
ATOM   3520  CD  GLU B 263     196.796 189.305 208.166  1.00 95.31           C  
ATOM   3521  OE1 GLU B 263     195.718 189.663 207.652  1.00 95.31           O  
ATOM   3522  OE2 GLU B 263     197.636 188.618 207.551  1.00 95.31           O  
ATOM   3523  N   TYR B 264     196.730 193.009 209.383  1.00 91.54           N  
ATOM   3524  CA  TYR B 264     197.604 194.159 209.562  1.00 91.54           C  
ATOM   3525  C   TYR B 264     196.804 195.424 209.830  1.00 91.54           C  
ATOM   3526  O   TYR B 264     197.172 196.221 210.697  1.00 91.54           O  
ATOM   3527  CB  TYR B 264     198.487 194.336 208.337  1.00 91.54           C  
ATOM   3528  CG  TYR B 264     199.331 195.580 208.355  1.00 91.54           C  
ATOM   3529  CD1 TYR B 264     199.990 195.976 209.495  1.00 91.54           C  
ATOM   3530  CD2 TYR B 264     199.484 196.343 207.218  1.00 91.54           C  
ATOM   3531  CE1 TYR B 264     200.765 197.104 209.505  1.00 91.54           C  
ATOM   3532  CE2 TYR B 264     200.260 197.472 207.218  1.00 91.54           C  
ATOM   3533  CZ  TYR B 264     200.900 197.848 208.363  1.00 91.54           C  
ATOM   3534  OH  TYR B 264     201.675 198.979 208.367  1.00 91.54           O  
ATOM   3535  N   SER B 265     195.711 195.634 209.098  1.00 95.20           N  
ATOM   3536  CA  SER B 265     194.888 196.809 209.359  1.00 95.20           C  
ATOM   3537  C   SER B 265     194.058 196.638 210.624  1.00 95.20           C  
ATOM   3538  O   SER B 265     193.688 197.629 211.259  1.00 95.20           O  
ATOM   3539  CB  SER B 265     193.997 197.107 208.158  1.00 95.20           C  
ATOM   3540  OG  SER B 265     193.004 196.118 208.003  1.00 95.20           O  
ATOM   3541  N   ARG B 266     193.750 195.380 210.951  1.00 95.09           N  
ATOM   3542  CA  ARG B 266     193.046 195.031 212.211  1.00 95.09           C  
ATOM   3543  C   ARG B 266     194.134 194.650 213.223  1.00 95.09           C  
ATOM   3544  O   ARG B 266     194.145 193.482 213.658  1.00 95.09           O  
ATOM   3545  CB  ARG B 266     192.065 193.878 211.976  1.00 95.09           C  
ATOM   3546  CG  ARG B 266     191.548 193.782 210.548  1.00 95.09           C  
ATOM   3547  CD  ARG B 266     190.139 193.225 210.479  1.00 95.09           C  
ATOM   3548  NE  ARG B 266     189.978 192.022 211.285  1.00 95.09           N  
ATOM   3549  CZ  ARG B 266     189.700 190.820 210.794  1.00 95.09           C  
ATOM   3550  NH1 ARG B 266     189.549 190.655 209.491  1.00 95.09           N  
ATOM   3551  NH2 ARG B 266     189.573 189.787 211.608  1.00 95.09           N  
ATOM   3552  N   SER B 267     195.023 195.590 213.567  1.00106.88           N  
ATOM   3553  CA  SER B 267     196.112 195.277 214.477  1.00106.88           C  
ATOM   3554  C   SER B 267     196.106 196.219 215.669  1.00106.88           C  
ATOM   3555  O   SER B 267     195.589 197.336 215.598  1.00106.88           O  
ATOM   3556  CB  SER B 267     197.466 195.349 213.786  1.00106.88           C  
ATOM   3557  OG  SER B 267     198.442 194.687 214.563  1.00106.88           O  
ATOM   3558  N   THR B 268     196.688 195.747 216.770  1.00122.60           N  
ATOM   3559  CA  THR B 268     196.675 196.464 218.036  1.00122.60           C  
ATOM   3560  C   THR B 268     198.071 196.805 218.534  1.00122.60           C  
ATOM   3561  O   THR B 268     198.212 197.253 219.676  1.00122.60           O  
ATOM   3562  CB  THR B 268     195.954 195.650 219.112  1.00122.60           C  
ATOM   3563  OG1 THR B 268     194.620 196.148 219.267  1.00122.60           O  
ATOM   3564  CG2 THR B 268     196.678 195.745 220.445  1.00122.60           C  
ATOM   3565  N   ILE B 269     199.106 196.587 217.723  1.00122.00           N  
ATOM   3566  CA  ILE B 269     200.460 196.886 218.168  1.00122.00           C  
ATOM   3567  C   ILE B 269     200.565 198.374 218.447  1.00122.00           C  
ATOM   3568  O   ILE B 269     200.242 199.207 217.593  1.00122.00           O  
ATOM   3569  CB  ILE B 269     201.492 196.437 217.128  1.00122.00           C  
ATOM   3570  CG1 ILE B 269     201.399 194.932 216.900  1.00122.00           C  
ATOM   3571  CG2 ILE B 269     202.882 196.803 217.585  1.00122.00           C  
ATOM   3572  CD1 ILE B 269     201.234 194.134 218.153  1.00122.00           C  
ATOM   3573  N   GLU B 270     200.983 198.709 219.669  1.00128.64           N  
ATOM   3574  CA  GLU B 270     200.982 200.115 220.154  1.00128.64           C  
ATOM   3575  C   GLU B 270     201.779 201.011 219.206  1.00128.64           C  
ATOM   3576  O   GLU B 270     201.439 202.205 219.098  1.00128.64           O  
ATOM   3577  CB  GLU B 270     201.509 200.202 221.589  1.00128.64           C  
ATOM   3578  CG  GLU B 270     200.684 199.406 222.584  1.00128.64           C  
ATOM   3579  CD  GLU B 270     201.180 199.479 224.018  1.00128.64           C  
ATOM   3580  OE1 GLU B 270     200.548 198.854 224.893  1.00128.64           O  
ATOM   3581  OE2 GLU B 270     202.196 200.161 224.257  1.00128.64           O  
ATOM   3582  N   GLY B 271     202.817 200.463 218.579  1.00122.04           N  
ATOM   3583  CA  GLY B 271     203.636 201.255 217.689  1.00122.04           C  
ATOM   3584  C   GLY B 271     203.591 200.741 216.268  1.00122.04           C  
ATOM   3585  O   GLY B 271     204.058 199.635 215.991  1.00122.04           O  
ATOM   3586  N   LEU B 272     203.011 201.531 215.367  1.00107.17           N  
ATOM   3587  CA  LEU B 272     203.000 201.251 213.937  1.00107.17           C  
ATOM   3588  C   LEU B 272     202.916 202.578 213.203  1.00107.17           C  
ATOM   3589  O   LEU B 272     202.497 203.587 213.773  1.00107.17           O  
ATOM   3590  CB  LEU B 272     201.833 200.346 213.529  1.00107.17           C  
ATOM   3591  CG  LEU B 272     202.089 198.844 213.547  1.00107.17           C  
ATOM   3592  CD1 LEU B 272     200.812 198.085 213.308  1.00107.17           C  
ATOM   3593  CD2 LEU B 272     203.108 198.494 212.496  1.00107.17           C  
ATOM   3594  N   GLU B 273     203.337 202.580 211.941  1.00 98.89           N  
ATOM   3595  CA  GLU B 273     203.246 203.783 211.124  1.00 98.89           C  
ATOM   3596  C   GLU B 273     202.154 203.673 210.070  1.00 98.89           C  
ATOM   3597  O   GLU B 273     201.205 204.459 210.064  1.00 98.89           O  
ATOM   3598  CB  GLU B 273     204.591 204.073 210.446  1.00 98.89           C  
ATOM   3599  CG  GLU B 273     205.773 204.131 211.390  1.00 98.89           C  
ATOM   3600  CD  GLU B 273     206.236 205.550 211.660  1.00 98.89           C  
ATOM   3601  OE1 GLU B 273     205.501 206.492 211.309  1.00 98.89           O  
ATOM   3602  OE2 GLU B 273     207.334 205.722 212.228  1.00 98.89           O  
ATOM   3603  N   TYR B 274     202.277 202.704 209.176  1.00 90.98           N  
ATOM   3604  CA  TYR B 274     201.396 202.588 208.018  1.00 90.98           C  
ATOM   3605  C   TYR B 274     200.286 201.580 208.286  1.00 90.98           C  
ATOM   3606  O   TYR B 274     200.112 200.597 207.571  1.00 90.98           O  
ATOM   3607  CB  TYR B 274     202.207 202.202 206.793  1.00 90.98           C  
ATOM   3608  CG  TYR B 274     203.407 203.075 206.590  1.00 90.98           C  
ATOM   3609  CD1 TYR B 274     203.347 204.435 206.831  1.00 90.98           C  
ATOM   3610  CD2 TYR B 274     204.604 202.540 206.175  1.00 90.98           C  
ATOM   3611  CE1 TYR B 274     204.446 205.234 206.644  1.00 90.98           C  
ATOM   3612  CE2 TYR B 274     205.708 203.332 205.985  1.00 90.98           C  
ATOM   3613  CZ  TYR B 274     205.626 204.675 206.219  1.00 90.98           C  
ATOM   3614  OH  TYR B 274     206.736 205.458 206.031  1.00 90.98           O  
ATOM   3615  N   ASN B 275     199.533 201.838 209.346  1.00 98.21           N  
ATOM   3616  CA  ASN B 275     198.429 200.963 209.696  1.00 98.21           C  
ATOM   3617  C   ASN B 275     197.168 201.277 208.906  1.00 98.21           C  
ATOM   3618  O   ASN B 275     196.188 200.532 209.010  1.00 98.21           O  
ATOM   3619  CB  ASN B 275     198.152 201.060 211.194  1.00 98.21           C  
ATOM   3620  CG  ASN B 275     197.431 199.849 211.729  1.00 98.21           C  
ATOM   3621  OD1 ASN B 275     197.239 198.868 211.021  1.00 98.21           O  
ATOM   3622  ND2 ASN B 275     197.020 199.916 212.986  1.00 98.21           N  
ATOM   3623  N   MET B 276     197.173 202.343 208.111  1.00 97.14           N  
ATOM   3624  CA  MET B 276     195.995 202.755 207.364  1.00 97.14           C  
ATOM   3625  C   MET B 276     195.983 202.271 205.926  1.00 97.14           C  
ATOM   3626  O   MET B 276     194.917 201.896 205.431  1.00 97.14           O  
ATOM   3627  CB  MET B 276     195.878 204.280 207.365  1.00 97.14           C  
ATOM   3628  CG  MET B 276     197.145 204.985 206.933  1.00 97.14           C  
ATOM   3629  SD  MET B 276     197.167 206.738 207.343  1.00 97.14           S  
ATOM   3630  CE  MET B 276     197.246 206.671 209.129  1.00 97.14           C  
ATOM   3631  N   PHE B 277     197.146 202.229 205.266  1.00 84.57           N  
ATOM   3632  CA  PHE B 277     197.213 202.069 203.813  1.00 84.57           C  
ATOM   3633  C   PHE B 277     196.297 200.993 203.245  1.00 84.57           C  
ATOM   3634  O   PHE B 277     195.883 201.098 202.088  1.00 84.57           O  
ATOM   3635  CB  PHE B 277     198.648 201.795 203.375  1.00 84.57           C  
ATOM   3636  CG  PHE B 277     199.544 202.987 203.461  1.00 84.57           C  
ATOM   3637  CD1 PHE B 277     199.016 204.251 203.614  1.00 84.57           C  
ATOM   3638  CD2 PHE B 277     200.902 202.858 203.288  1.00 84.57           C  
ATOM   3639  CE1 PHE B 277     199.832 205.350 203.660  1.00 84.57           C  
ATOM   3640  CE2 PHE B 277     201.719 203.960 203.327  1.00 84.57           C  
ATOM   3641  CZ  PHE B 277     201.182 205.203 203.516  1.00 84.57           C  
ATOM   3642  N   PHE B 278     195.965 199.963 204.012  1.00 81.08           N  
ATOM   3643  CA  PHE B 278     195.124 198.895 203.490  1.00 81.08           C  
ATOM   3644  C   PHE B 278     193.797 198.809 204.227  1.00 81.08           C  
ATOM   3645  O   PHE B 278     193.169 197.750 204.255  1.00 81.08           O  
ATOM   3646  CB  PHE B 278     195.846 197.557 203.560  1.00 81.08           C  
ATOM   3647  CG  PHE B 278     196.996 197.441 202.613  1.00 81.08           C  
ATOM   3648  CD1 PHE B 278     196.791 197.144 201.287  1.00 81.08           C  
ATOM   3649  CD2 PHE B 278     198.290 197.618 203.059  1.00 81.08           C  
ATOM   3650  CE1 PHE B 278     197.854 197.035 200.428  1.00 81.08           C  
ATOM   3651  CE2 PHE B 278     199.348 197.510 202.206  1.00 81.08           C  
ATOM   3652  CZ  PHE B 278     199.133 197.219 200.889  1.00 81.08           C  
ATOM   3653  N   SER B 279     193.358 199.916 204.829  1.00 86.07           N  
ATOM   3654  CA  SER B 279     192.145 199.897 205.643  1.00 86.07           C  
ATOM   3655  C   SER B 279     190.919 199.539 204.809  1.00 86.07           C  
ATOM   3656  O   SER B 279     190.231 198.550 205.083  1.00 86.07           O  
ATOM   3657  CB  SER B 279     191.957 201.252 206.322  1.00 86.07           C  
ATOM   3658  OG  SER B 279     191.754 202.273 205.363  1.00 86.07           O  
ATOM   3659  N   ASP B 280     190.638 200.335 203.777  1.00 88.39           N  
ATOM   3660  CA  ASP B 280     189.462 200.144 202.937  1.00 88.39           C  
ATOM   3661  C   ASP B 280     189.864 200.027 201.477  1.00 88.39           C  
ATOM   3662  O   ASP B 280     191.048 199.872 201.174  1.00 88.39           O  
ATOM   3663  CB  ASP B 280     188.480 201.296 203.122  1.00 88.39           C  
ATOM   3664  CG  ASP B 280     187.653 201.158 204.383  1.00 88.39           C  
ATOM   3665  OD1 ASP B 280     187.216 200.028 204.686  1.00 88.39           O  
ATOM   3666  OD2 ASP B 280     187.438 202.180 205.068  1.00 88.39           O  
ATOM   3667  N   LEU B 281     188.894 200.087 200.565  1.00 80.21           N  
ATOM   3668  CA  LEU B 281     189.222 199.947 199.151  1.00 80.21           C  
ATOM   3669  C   LEU B 281     189.913 201.185 198.607  1.00 80.21           C  
ATOM   3670  O   LEU B 281     190.881 201.073 197.850  1.00 80.21           O  
ATOM   3671  CB  LEU B 281     187.973 199.659 198.336  1.00 80.21           C  
ATOM   3672  CG  LEU B 281     188.217 199.747 196.832  1.00 80.21           C  
ATOM   3673  CD1 LEU B 281     189.186 198.677 196.383  1.00 80.21           C  
ATOM   3674  CD2 LEU B 281     186.919 199.641 196.068  1.00 80.21           C  
ATOM   3675  N   LEU B 282     189.424 202.374 198.957  1.00 77.50           N  
ATOM   3676  CA  LEU B 282     190.044 203.595 198.451  1.00 77.50           C  
ATOM   3677  C   LEU B 282     191.480 203.720 198.936  1.00 77.50           C  
ATOM   3678  O   LEU B 282     192.384 204.067 198.163  1.00 77.50           O  
ATOM   3679  CB  LEU B 282     189.238 204.819 198.879  1.00 77.50           C  
ATOM   3680  CG  LEU B 282     188.009 205.238 198.070  1.00 77.50           C  
ATOM   3681  CD1 LEU B 282     188.417 205.637 196.674  1.00 77.50           C  
ATOM   3682  CD2 LEU B 282     186.947 204.154 198.034  1.00 77.50           C  
ATOM   3683  N   ASN B 283     191.705 203.456 200.221  1.00 77.55           N  
ATOM   3684  CA  ASN B 283     193.059 203.468 200.748  1.00 77.55           C  
ATOM   3685  C   ASN B 283     193.924 202.434 200.049  1.00 77.55           C  
ATOM   3686  O   ASN B 283     195.101 202.680 199.775  1.00 77.55           O  
ATOM   3687  CB  ASN B 283     193.030 203.218 202.248  1.00 77.55           C  
ATOM   3688  CG  ASN B 283     192.673 204.451 203.027  1.00 77.55           C  
ATOM   3689  OD1 ASN B 283     191.629 204.511 203.670  1.00 77.55           O  
ATOM   3690  ND2 ASN B 283     193.542 205.448 202.981  1.00 77.55           N  
ATOM   3691  N   SER B 284     193.354 201.275 199.736  1.00 73.54           N  
ATOM   3692  CA  SER B 284     194.110 200.266 199.010  1.00 73.54           C  
ATOM   3693  C   SER B 284     194.507 200.760 197.627  1.00 73.54           C  
ATOM   3694  O   SER B 284     195.627 200.511 197.173  1.00 73.54           O  
ATOM   3695  CB  SER B 284     193.297 198.988 198.906  1.00 73.54           C  
ATOM   3696  OG  SER B 284     193.914 198.083 198.025  1.00 73.54           O  
ATOM   3697  N   LEU B 285     193.605 201.458 196.937  1.00 69.45           N  
ATOM   3698  CA  LEU B 285     193.916 201.932 195.592  1.00 69.45           C  
ATOM   3699  C   LEU B 285     194.984 203.016 195.617  1.00 69.45           C  
ATOM   3700  O   LEU B 285     195.914 203.008 194.797  1.00 69.45           O  
ATOM   3701  CB  LEU B 285     192.655 202.449 194.913  1.00 69.45           C  
ATOM   3702  CG  LEU B 285     192.767 202.552 193.396  1.00 69.45           C  
ATOM   3703  CD1 LEU B 285     192.569 201.205 192.752  1.00 69.45           C  
ATOM   3704  CD2 LEU B 285     191.765 203.543 192.861  1.00 69.45           C  
ATOM   3705  N   VAL B 286     194.879 203.957 196.553  1.00 69.38           N  
ATOM   3706  CA  VAL B 286     195.936 204.955 196.640  1.00 69.38           C  
ATOM   3707  C   VAL B 286     197.254 204.298 197.038  1.00 69.38           C  
ATOM   3708  O   VAL B 286     198.323 204.706 196.568  1.00 69.38           O  
ATOM   3709  CB  VAL B 286     195.547 206.100 197.591  1.00 69.38           C  
ATOM   3710  CG1 VAL B 286     195.411 205.614 198.998  1.00 69.38           C  
ATOM   3711  CG2 VAL B 286     196.591 207.166 197.541  1.00 69.38           C  
ATOM   3712  N   THR B 287     197.208 203.263 197.881  1.00 67.51           N  
ATOM   3713  CA  THR B 287     198.423 202.541 198.236  1.00 67.51           C  
ATOM   3714  C   THR B 287     199.047 201.883 197.020  1.00 67.51           C  
ATOM   3715  O   THR B 287     200.271 201.892 196.857  1.00 67.51           O  
ATOM   3716  CB  THR B 287     198.106 201.492 199.287  1.00 67.51           C  
ATOM   3717  OG1 THR B 287     197.899 202.143 200.535  1.00 67.51           O  
ATOM   3718  CG2 THR B 287     199.250 200.526 199.428  1.00 67.51           C  
ATOM   3719  N   VAL B 288     198.223 201.282 196.168  1.00 61.72           N  
ATOM   3720  CA  VAL B 288     198.749 200.673 194.957  1.00 61.72           C  
ATOM   3721  C   VAL B 288     199.408 201.727 194.090  1.00 61.72           C  
ATOM   3722  O   VAL B 288     200.448 201.481 193.475  1.00 61.72           O  
ATOM   3723  CB  VAL B 288     197.642 199.929 194.200  1.00 61.72           C  
ATOM   3724  CG1 VAL B 288     198.149 199.467 192.863  1.00 61.72           C  
ATOM   3725  CG2 VAL B 288     197.186 198.752 195.005  1.00 61.72           C  
ATOM   3726  N   PHE B 289     198.837 202.927 194.045  1.00 63.04           N  
ATOM   3727  CA  PHE B 289     199.502 203.996 193.304  1.00 63.04           C  
ATOM   3728  C   PHE B 289     200.855 204.345 193.915  1.00 63.04           C  
ATOM   3729  O   PHE B 289     201.854 204.501 193.198  1.00 63.04           O  
ATOM   3730  CB  PHE B 289     198.621 205.232 193.251  1.00 63.04           C  
ATOM   3731  CG  PHE B 289     199.064 206.228 192.243  1.00 63.04           C  
ATOM   3732  CD1 PHE B 289     198.900 205.980 190.904  1.00 63.04           C  
ATOM   3733  CD2 PHE B 289     199.652 207.403 192.631  1.00 63.04           C  
ATOM   3734  CE1 PHE B 289     199.302 206.885 189.976  1.00 63.04           C  
ATOM   3735  CE2 PHE B 289     200.063 208.311 191.704  1.00 63.04           C  
ATOM   3736  CZ  PHE B 289     199.887 208.052 190.373  1.00 63.04           C  
ATOM   3737  N   ILE B 290     200.910 204.469 195.239  1.00 62.97           N  
ATOM   3738  CA  ILE B 290     202.168 204.824 195.887  1.00 62.97           C  
ATOM   3739  C   ILE B 290     203.230 203.783 195.580  1.00 62.97           C  
ATOM   3740  O   ILE B 290     204.372 204.119 195.257  1.00 62.97           O  
ATOM   3741  CB  ILE B 290     201.973 204.997 197.399  1.00 62.97           C  
ATOM   3742  CG1 ILE B 290     201.186 206.267 197.686  1.00 62.97           C  
ATOM   3743  CG2 ILE B 290     203.303 205.077 198.088  1.00 62.97           C  
ATOM   3744  CD1 ILE B 290     200.846 206.444 199.133  1.00 62.97           C  
ATOM   3745  N   LEU B 291     202.870 202.506 195.663  1.00 58.61           N  
ATOM   3746  CA  LEU B 291     203.811 201.454 195.294  1.00 58.61           C  
ATOM   3747  C   LEU B 291     204.191 201.548 193.826  1.00 58.61           C  
ATOM   3748  O   LEU B 291     205.329 201.255 193.452  1.00 58.61           O  
ATOM   3749  CB  LEU B 291     203.227 200.078 195.603  1.00 58.61           C  
ATOM   3750  CG  LEU B 291     203.379 199.512 197.011  1.00 58.61           C  
ATOM   3751  CD1 LEU B 291     204.831 199.300 197.253  1.00 58.61           C  
ATOM   3752  CD2 LEU B 291     202.826 200.429 198.059  1.00 58.61           C  
ATOM   3753  N   PHE B 292     203.250 201.951 192.977  1.00 58.02           N  
ATOM   3754  CA  PHE B 292     203.547 202.128 191.563  1.00 58.02           C  
ATOM   3755  C   PHE B 292     204.618 203.180 191.349  1.00 58.02           C  
ATOM   3756  O   PHE B 292     205.388 203.095 190.390  1.00 58.02           O  
ATOM   3757  CB  PHE B 292     202.270 202.509 190.826  1.00 58.02           C  
ATOM   3758  CG  PHE B 292     202.399 202.535 189.343  1.00 58.02           C  
ATOM   3759  CD1 PHE B 292     202.339 201.375 188.614  1.00 58.02           C  
ATOM   3760  CD2 PHE B 292     202.532 203.727 188.671  1.00 58.02           C  
ATOM   3761  CE1 PHE B 292     202.434 201.403 187.250  1.00 58.02           C  
ATOM   3762  CE2 PHE B 292     202.630 203.753 187.306  1.00 58.02           C  
ATOM   3763  CZ  PHE B 292     202.581 202.591 186.597  1.00 58.02           C  
ATOM   3764  N   THR B 293     204.684 204.176 192.219  1.00 61.89           N  
ATOM   3765  CA  THR B 293     205.698 205.211 192.092  1.00 61.89           C  
ATOM   3766  C   THR B 293     206.988 204.898 192.836  1.00 61.89           C  
ATOM   3767  O   THR B 293     207.869 205.758 192.888  1.00 61.89           O  
ATOM   3768  CB  THR B 293     205.153 206.546 192.582  1.00 61.89           C  
ATOM   3769  OG1 THR B 293     204.726 206.411 193.939  1.00 61.89           O  
ATOM   3770  CG2 THR B 293     203.988 206.968 191.734  1.00 61.89           C  
ATOM   3771  N   LEU B 294     207.119 203.706 193.418  1.00 60.18           N  
ATOM   3772  CA  LEU B 294     208.350 203.273 194.080  1.00 60.18           C  
ATOM   3773  C   LEU B 294     208.755 204.225 195.195  1.00 60.18           C  
ATOM   3774  O   LEU B 294     209.913 204.619 195.314  1.00 60.18           O  
ATOM   3775  CB  LEU B 294     209.496 203.128 193.085  1.00 60.18           C  
ATOM   3776  CG  LEU B 294     209.415 201.998 192.091  1.00 60.18           C  
ATOM   3777  CD1 LEU B 294     210.728 201.855 191.382  1.00 60.18           C  
ATOM   3778  CD2 LEU B 294     209.081 200.766 192.839  1.00 60.18           C  
ATOM   3779  N   ASP B 295     207.797 204.604 196.019  1.00 65.26           N  
ATOM   3780  CA  ASP B 295     208.088 205.458 197.154  1.00 65.26           C  
ATOM   3781  C   ASP B 295     207.766 204.690 198.421  1.00 65.26           C  
ATOM   3782  O   ASP B 295     206.614 204.312 198.646  1.00 65.26           O  
ATOM   3783  CB  ASP B 295     207.304 206.764 197.089  1.00 65.26           C  
ATOM   3784  CG  ASP B 295     207.831 207.794 198.047  1.00 65.26           C  
ATOM   3785  OD1 ASP B 295     208.963 208.262 197.845  1.00 65.26           O  
ATOM   3786  OD2 ASP B 295     207.115 208.133 199.006  1.00 65.26           O  
ATOM   3787  N   HIS B 296     208.792 204.444 199.229  1.00 67.22           N  
ATOM   3788  CA  HIS B 296     208.634 203.839 200.544  1.00 67.22           C  
ATOM   3789  C   HIS B 296     208.084 202.428 200.452  1.00 67.22           C  
ATOM   3790  O   HIS B 296     207.333 201.986 201.318  1.00 67.22           O  
ATOM   3791  CB  HIS B 296     207.744 204.697 201.435  1.00 67.22           C  
ATOM   3792  CG  HIS B 296     208.430 205.908 201.965  1.00 67.22           C  
ATOM   3793  ND1 HIS B 296     209.792 206.078 201.881  1.00 67.22           N  
ATOM   3794  CD2 HIS B 296     207.947 207.010 202.579  1.00 67.22           C  
ATOM   3795  CE1 HIS B 296     210.122 207.233 202.428  1.00 67.22           C  
ATOM   3796  NE2 HIS B 296     209.020 207.819 202.858  1.00 67.22           N  
ATOM   3797  N   TRP B 297     208.443 201.706 199.400  1.00 60.95           N  
ATOM   3798  CA  TRP B 297     207.961 200.338 199.327  1.00 60.95           C  
ATOM   3799  C   TRP B 297     208.591 199.491 200.418  1.00 60.95           C  
ATOM   3800  O   TRP B 297     207.903 198.702 201.078  1.00 60.95           O  
ATOM   3801  CB  TRP B 297     208.211 199.751 197.939  1.00 60.95           C  
ATOM   3802  CG  TRP B 297     209.622 199.524 197.543  1.00 60.95           C  
ATOM   3803  CD1 TRP B 297     210.392 200.330 196.767  1.00 60.95           C  
ATOM   3804  CD2 TRP B 297     210.420 198.384 197.851  1.00 60.95           C  
ATOM   3805  NE1 TRP B 297     211.630 199.775 196.590  1.00 60.95           N  
ATOM   3806  CE2 TRP B 297     211.669 198.575 197.247  1.00 60.95           C  
ATOM   3807  CE3 TRP B 297     210.200 197.221 198.584  1.00 60.95           C  
ATOM   3808  CZ2 TRP B 297     212.693 197.654 197.362  1.00 60.95           C  
ATOM   3809  CZ3 TRP B 297     211.215 196.312 198.694  1.00 60.95           C  
ATOM   3810  CH2 TRP B 297     212.444 196.529 198.089  1.00 60.95           C  
ATOM   3811  N   TYR B 298     209.884 199.684 200.668  1.00 63.79           N  
ATOM   3812  CA  TYR B 298     210.562 198.843 201.644  1.00 63.79           C  
ATOM   3813  C   TYR B 298     210.096 199.166 203.054  1.00 63.79           C  
ATOM   3814  O   TYR B 298     209.923 198.263 203.874  1.00 63.79           O  
ATOM   3815  CB  TYR B 298     212.073 198.998 201.514  1.00 63.79           C  
ATOM   3816  CG  TYR B 298     212.853 197.928 202.233  1.00 63.79           C  
ATOM   3817  CD1 TYR B 298     212.432 196.614 202.207  1.00 63.79           C  
ATOM   3818  CD2 TYR B 298     214.018 198.221 202.904  1.00 63.79           C  
ATOM   3819  CE1 TYR B 298     213.134 195.627 202.843  1.00 63.79           C  
ATOM   3820  CE2 TYR B 298     214.727 197.235 203.549  1.00 63.79           C  
ATOM   3821  CZ  TYR B 298     214.279 195.939 203.514  1.00 63.79           C  
ATOM   3822  OH  TYR B 298     214.983 194.949 204.152  1.00 63.79           O  
ATOM   3823  N   ALA B 299     209.870 200.447 203.351  1.00 67.77           N  
ATOM   3824  CA  ALA B 299     209.372 200.830 204.668  1.00 67.77           C  
ATOM   3825  C   ALA B 299     207.998 200.229 204.949  1.00 67.77           C  
ATOM   3826  O   ALA B 299     207.753 199.703 206.040  1.00 67.77           O  
ATOM   3827  CB  ALA B 299     209.322 202.351 204.776  1.00 67.77           C  
ATOM   3828  N   VAL B 300     207.090 200.293 203.976  1.00 70.44           N  
ATOM   3829  CA  VAL B 300     205.770 199.697 204.150  1.00 70.44           C  
ATOM   3830  C   VAL B 300     205.888 198.193 204.334  1.00 70.44           C  
ATOM   3831  O   VAL B 300     205.174 197.591 205.143  1.00 70.44           O  
ATOM   3832  CB  VAL B 300     204.872 200.043 202.952  1.00 70.44           C  
ATOM   3833  CG1 VAL B 300     203.580 199.277 203.024  1.00 70.44           C  
ATOM   3834  CG2 VAL B 300     204.609 201.520 202.899  1.00 70.44           C  
ATOM   3835  N   LEU B 301     206.778 197.559 203.570  1.00 68.11           N  
ATOM   3836  CA  LEU B 301     206.970 196.120 203.694  1.00 68.11           C  
ATOM   3837  C   LEU B 301     207.442 195.743 205.092  1.00 68.11           C  
ATOM   3838  O   LEU B 301     206.928 194.796 205.696  1.00 68.11           O  
ATOM   3839  CB  LEU B 301     207.967 195.658 202.643  1.00 68.11           C  
ATOM   3840  CG  LEU B 301     208.171 194.167 202.503  1.00 68.11           C  
ATOM   3841  CD1 LEU B 301     206.833 193.499 202.418  1.00 68.11           C  
ATOM   3842  CD2 LEU B 301     208.986 193.909 201.266  1.00 68.11           C  
ATOM   3843  N   GLN B 302     208.411 196.479 205.631  1.00 72.22           N  
ATOM   3844  CA  GLN B 302     208.862 196.201 206.989  1.00 72.22           C  
ATOM   3845  C   GLN B 302     207.752 196.444 207.999  1.00 72.22           C  
ATOM   3846  O   GLN B 302     207.618 195.698 208.975  1.00 72.22           O  
ATOM   3847  CB  GLN B 302     210.087 197.039 207.331  1.00 72.22           C  
ATOM   3848  CG  GLN B 302     211.144 197.021 206.271  1.00 72.22           C  
ATOM   3849  CD  GLN B 302     212.534 197.101 206.839  1.00 72.22           C  
ATOM   3850  OE1 GLN B 302     213.012 196.158 207.465  1.00 72.22           O  
ATOM   3851  NE2 GLN B 302     213.200 198.225 206.618  1.00 72.22           N  
ATOM   3852  N   ASP B 303     206.949 197.487 207.793  1.00 80.87           N  
ATOM   3853  CA  ASP B 303     205.825 197.714 208.693  1.00 80.87           C  
ATOM   3854  C   ASP B 303     204.895 196.516 208.706  1.00 80.87           C  
ATOM   3855  O   ASP B 303     204.484 196.050 209.771  1.00 80.87           O  
ATOM   3856  CB  ASP B 303     205.061 198.964 208.283  1.00 80.87           C  
ATOM   3857  CG  ASP B 303     205.511 200.183 209.029  1.00 80.87           C  
ATOM   3858  OD1 ASP B 303     206.587 200.127 209.654  1.00 80.87           O  
ATOM   3859  OD2 ASP B 303     204.789 201.198 208.995  1.00 80.87           O  
ATOM   3860  N   ILE B 304     204.570 195.994 207.527  1.00 78.78           N  
ATOM   3861  CA  ILE B 304     203.750 194.793 207.443  1.00 78.78           C  
ATOM   3862  C   ILE B 304     204.398 193.668 208.222  1.00 78.78           C  
ATOM   3863  O   ILE B 304     203.729 192.922 208.943  1.00 78.78           O  
ATOM   3864  CB  ILE B 304     203.545 194.399 205.975  1.00 78.78           C  
ATOM   3865  CG1 ILE B 304     202.532 195.315 205.315  1.00 78.78           C  
ATOM   3866  CG2 ILE B 304     203.091 192.978 205.877  1.00 78.78           C  
ATOM   3867  CD1 ILE B 304     202.519 195.188 203.826  1.00 78.78           C  
ATOM   3868  N   TRP B 305     205.715 193.531 208.094  1.00 75.58           N  
ATOM   3869  CA  TRP B 305     206.421 192.482 208.819  1.00 75.58           C  
ATOM   3870  C   TRP B 305     206.365 192.680 210.327  1.00 75.58           C  
ATOM   3871  O   TRP B 305     206.541 191.717 211.080  1.00 75.58           O  
ATOM   3872  CB  TRP B 305     207.870 192.431 208.374  1.00 75.58           C  
ATOM   3873  CG  TRP B 305     208.049 191.820 207.058  1.00 75.58           C  
ATOM   3874  CD1 TRP B 305     207.150 191.077 206.372  1.00 75.58           C  
ATOM   3875  CD2 TRP B 305     209.214 191.898 206.251  1.00 75.58           C  
ATOM   3876  NE1 TRP B 305     207.687 190.682 205.178  1.00 75.58           N  
ATOM   3877  CE2 TRP B 305     208.958 191.178 205.083  1.00 75.58           C  
ATOM   3878  CE3 TRP B 305     210.453 192.514 206.406  1.00 75.58           C  
ATOM   3879  CZ2 TRP B 305     209.893 191.053 204.077  1.00 75.58           C  
ATOM   3880  CZ3 TRP B 305     211.373 192.391 205.413  1.00 75.58           C  
ATOM   3881  CH2 TRP B 305     211.095 191.670 204.262  1.00 75.58           C  
ATOM   3882  N   LYS B 306     206.140 193.910 210.791  1.00 83.68           N  
ATOM   3883  CA  LYS B 306     206.170 194.162 212.228  1.00 83.68           C  
ATOM   3884  C   LYS B 306     204.987 193.545 212.956  1.00 83.68           C  
ATOM   3885  O   LYS B 306     204.946 193.579 214.188  1.00 83.68           O  
ATOM   3886  CB  LYS B 306     206.214 195.661 212.513  1.00 83.68           C  
ATOM   3887  CG  LYS B 306     207.614 196.254 212.500  1.00 83.68           C  
ATOM   3888  CD  LYS B 306     207.579 197.760 212.291  1.00 83.68           C  
ATOM   3889  CE  LYS B 306     206.897 198.448 213.456  1.00 83.68           C  
ATOM   3890  NZ  LYS B 306     206.845 199.925 213.305  1.00 83.68           N  
ATOM   3891  N   VAL B 307     204.017 193.003 212.233  1.00 95.50           N  
ATOM   3892  CA  VAL B 307     202.897 192.301 212.849  1.00 95.50           C  
ATOM   3893  C   VAL B 307     203.254 190.820 212.894  1.00 95.50           C  
ATOM   3894  O   VAL B 307     203.752 190.280 211.899  1.00 95.50           O  
ATOM   3895  CB  VAL B 307     201.598 192.569 212.075  1.00 95.50           C  
ATOM   3896  CG1 VAL B 307     200.488 191.663 212.544  1.00 95.50           C  
ATOM   3897  CG2 VAL B 307     201.200 194.020 212.228  1.00 95.50           C  
ATOM   3898  N   PRO B 308     203.048 190.131 214.018  1.00103.80           N  
ATOM   3899  CA  PRO B 308     203.477 188.726 214.104  1.00103.80           C  
ATOM   3900  C   PRO B 308     202.701 187.791 213.197  1.00103.80           C  
ATOM   3901  O   PRO B 308     203.155 186.666 212.961  1.00103.80           O  
ATOM   3902  CB  PRO B 308     203.257 188.391 215.580  1.00103.80           C  
ATOM   3903  CG  PRO B 308     202.145 189.285 215.985  1.00103.80           C  
ATOM   3904  CD  PRO B 308     202.368 190.569 215.246  1.00103.80           C  
ATOM   3905  N   GLU B 309     201.592 188.341 212.684  1.00106.32           N  
ATOM   3906  CA  GLU B 309     200.649 187.749 211.699  1.00106.32           C  
ATOM   3907  C   GLU B 309     200.970 188.394 210.344  1.00106.32           C  
ATOM   3908  O   GLU B 309     201.653 189.437 210.340  1.00106.32           O  
ATOM   3909  CB  GLU B 309     199.202 188.016 212.115  1.00106.32           C  
ATOM   3910  CG  GLU B 309     198.671 187.018 213.129  1.00106.32           C  
ATOM   3911  CD  GLU B 309     197.415 187.464 213.858  1.00106.32           C  
ATOM   3912  OE1 GLU B 309     197.491 188.458 214.607  1.00106.32           O  
ATOM   3913  OE2 GLU B 309     196.366 186.816 213.676  1.00106.32           O  
ATOM   3914  N   SER B 310     200.515 187.789 209.244  1.00102.59           N  
ATOM   3915  CA  SER B 310     200.820 188.271 207.897  1.00102.59           C  
ATOM   3916  C   SER B 310     202.164 187.713 207.418  1.00102.59           C  
ATOM   3917  O   SER B 310     203.167 188.418 207.316  1.00102.59           O  
ATOM   3918  CB  SER B 310     200.793 189.805 207.831  1.00102.59           C  
ATOM   3919  OG  SER B 310     201.753 190.393 208.689  1.00102.59           O  
ATOM   3920  N   SER B 311     202.150 186.402 207.175  1.00 95.21           N  
ATOM   3921  CA  SER B 311     203.348 185.659 206.801  1.00 95.21           C  
ATOM   3922  C   SER B 311     204.177 186.415 205.776  1.00 95.21           C  
ATOM   3923  O   SER B 311     203.655 186.936 204.791  1.00 95.21           O  
ATOM   3924  CB  SER B 311     202.965 184.288 206.241  1.00 95.21           C  
ATOM   3925  OG  SER B 311     204.120 183.543 205.898  1.00 95.21           O  
ATOM   3926  N   ARG B 312     205.471 186.458 206.016  1.00 84.61           N  
ATOM   3927  CA  ARG B 312     206.407 187.195 205.193  1.00 84.61           C  
ATOM   3928  C   ARG B 312     206.642 186.569 203.897  1.00 84.61           C  
ATOM   3929  O   ARG B 312     207.609 186.956 203.254  1.00 84.61           O  
ATOM   3930  CB  ARG B 312     207.734 187.346 205.928  1.00 84.61           C  
ATOM   3931  CG  ARG B 312     207.581 187.848 207.333  1.00 84.61           C  
ATOM   3932  CD  ARG B 312     208.635 187.259 208.216  1.00 84.61           C  
ATOM   3933  NE  ARG B 312     209.883 187.998 208.133  1.00 84.61           N  
ATOM   3934  CZ  ARG B 312     210.310 188.815 209.082  1.00 84.61           C  
ATOM   3935  NH1 ARG B 312     209.580 188.989 210.173  1.00 84.61           N  
ATOM   3936  NH2 ARG B 312     211.459 189.457 208.944  1.00 84.61           N  
ATOM   3937  N   VAL B 313     205.857 185.597 203.450  1.00 82.79           N  
ATOM   3938  CA  VAL B 313     206.026 185.026 202.128  1.00 82.79           C  
ATOM   3939  C   VAL B 313     204.880 185.420 201.207  1.00 82.79           C  
ATOM   3940  O   VAL B 313     204.967 185.265 199.991  1.00 82.79           O  
ATOM   3941  CB  VAL B 313     206.174 183.495 202.237  1.00 82.79           C  
ATOM   3942  CG1 VAL B 313     206.370 182.857 200.884  1.00 82.79           C  
ATOM   3943  CG2 VAL B 313     207.337 183.165 203.134  1.00 82.79           C  
ATOM   3944  N   PHE B 314     203.807 185.968 201.763  1.00 82.26           N  
ATOM   3945  CA  PHE B 314     202.747 186.465 200.902  1.00 82.26           C  
ATOM   3946  C   PHE B 314     202.837 187.970 200.727  1.00 82.26           C  
ATOM   3947  O   PHE B 314     202.681 188.476 199.612  1.00 82.26           O  
ATOM   3948  CB  PHE B 314     201.392 186.061 201.457  1.00 82.26           C  
ATOM   3949  CG  PHE B 314     201.062 184.627 201.217  1.00 82.26           C  
ATOM   3950  CD1 PHE B 314     200.685 184.202 199.963  1.00 82.26           C  
ATOM   3951  CD2 PHE B 314     201.160 183.699 202.236  1.00 82.26           C  
ATOM   3952  CE1 PHE B 314     200.386 182.886 199.732  1.00 82.26           C  
ATOM   3953  CE2 PHE B 314     200.859 182.383 202.013  1.00 82.26           C  
ATOM   3954  CZ  PHE B 314     200.474 181.973 200.756  1.00 82.26           C  
ATOM   3955  N   SER B 315     203.109 188.700 201.805  1.00 75.08           N  
ATOM   3956  CA  SER B 315     203.341 190.130 201.666  1.00 75.08           C  
ATOM   3957  C   SER B 315     204.528 190.397 200.758  1.00 75.08           C  
ATOM   3958  O   SER B 315     204.468 191.265 199.880  1.00 75.08           O  
ATOM   3959  CB  SER B 315     203.580 190.757 203.032  1.00 75.08           C  
ATOM   3960  OG  SER B 315     204.906 190.525 203.458  1.00 75.08           O  
ATOM   3961  N   SER B 316     205.614 189.653 200.951  1.00 70.04           N  
ATOM   3962  CA  SER B 316     206.792 189.844 200.120  1.00 70.04           C  
ATOM   3963  C   SER B 316     206.489 189.551 198.663  1.00 70.04           C  
ATOM   3964  O   SER B 316     206.878 190.319 197.779  1.00 70.04           O  
ATOM   3965  CB  SER B 316     207.929 188.961 200.612  1.00 70.04           C  
ATOM   3966  OG  SER B 316     208.289 189.303 201.934  1.00 70.04           O  
ATOM   3967  N   ILE B 317     205.786 188.452 198.387  1.00 65.89           N  
ATOM   3968  CA  ILE B 317     205.503 188.098 197.000  1.00 65.89           C  
ATOM   3969  C   ILE B 317     204.606 189.140 196.359  1.00 65.89           C  
ATOM   3970  O   ILE B 317     204.845 189.578 195.229  1.00 65.89           O  
ATOM   3971  CB  ILE B 317     204.887 186.696 196.905  1.00 65.89           C  
ATOM   3972  CG1 ILE B 317     205.974 185.647 197.088  1.00 65.89           C  
ATOM   3973  CG2 ILE B 317     204.223 186.517 195.563  1.00 65.89           C  
ATOM   3974  CD1 ILE B 317     207.045 185.702 196.034  1.00 65.89           C  
ATOM   3975  N   TYR B 318     203.568 189.567 197.074  1.00 63.65           N  
ATOM   3976  CA  TYR B 318     202.691 190.599 196.538  1.00 63.65           C  
ATOM   3977  C   TYR B 318     203.468 191.860 196.198  1.00 63.65           C  
ATOM   3978  O   TYR B 318     203.401 192.355 195.068  1.00 63.65           O  
ATOM   3979  CB  TYR B 318     201.588 190.911 197.538  1.00 63.65           C  
ATOM   3980  CG  TYR B 318     200.750 192.103 197.178  1.00 63.65           C  
ATOM   3981  CD1 TYR B 318     199.602 191.963 196.430  1.00 63.65           C  
ATOM   3982  CD2 TYR B 318     201.093 193.364 197.610  1.00 63.65           C  
ATOM   3983  CE1 TYR B 318     198.836 193.044 196.112  1.00 63.65           C  
ATOM   3984  CE2 TYR B 318     200.333 194.447 197.294  1.00 63.65           C  
ATOM   3985  CZ  TYR B 318     199.204 194.284 196.547  1.00 63.65           C  
ATOM   3986  OH  TYR B 318     198.437 195.376 196.233  1.00 63.65           O  
ATOM   3987  N   VAL B 319     204.221 192.392 197.160  1.00 58.93           N  
ATOM   3988  CA  VAL B 319     204.896 193.665 196.932  1.00 58.93           C  
ATOM   3989  C   VAL B 319     205.908 193.533 195.806  1.00 58.93           C  
ATOM   3990  O   VAL B 319     205.976 194.385 194.916  1.00 58.93           O  
ATOM   3991  CB  VAL B 319     205.549 194.178 198.225  1.00 58.93           C  
ATOM   3992  CG1 VAL B 319     206.618 195.178 197.908  1.00 58.93           C  
ATOM   3993  CG2 VAL B 319     204.525 194.835 199.092  1.00 58.93           C  
ATOM   3994  N   ILE B 320     206.704 192.464 195.812  1.00 58.19           N  
ATOM   3995  CA  ILE B 320     207.764 192.357 194.817  1.00 58.19           C  
ATOM   3996  C   ILE B 320     207.183 192.138 193.428  1.00 58.19           C  
ATOM   3997  O   ILE B 320     207.704 192.664 192.442  1.00 58.19           O  
ATOM   3998  CB  ILE B 320     208.762 191.253 195.203  1.00 58.19           C  
ATOM   3999  CG1 ILE B 320     209.378 191.566 196.557  1.00 58.19           C  
ATOM   4000  CG2 ILE B 320     209.859 191.140 194.173  1.00 58.19           C  
ATOM   4001  CD1 ILE B 320     210.073 192.881 196.595  1.00 58.19           C  
ATOM   4002  N   LEU B 321     206.097 191.371 193.316  1.00 53.98           N  
ATOM   4003  CA  LEU B 321     205.516 191.163 191.998  1.00 53.98           C  
ATOM   4004  C   LEU B 321     204.830 192.419 191.495  1.00 53.98           C  
ATOM   4005  O   LEU B 321     204.822 192.670 190.290  1.00 53.98           O  
ATOM   4006  CB  LEU B 321     204.545 189.989 192.022  1.00 53.98           C  
ATOM   4007  CG  LEU B 321     203.999 189.503 190.681  1.00 53.98           C  
ATOM   4008  CD1 LEU B 321     203.663 188.051 190.790  1.00 53.98           C  
ATOM   4009  CD2 LEU B 321     202.771 190.251 190.257  1.00 53.98           C  
ATOM   4010  N   TRP B 322     204.248 193.220 192.384  1.00 56.88           N  
ATOM   4011  CA  TRP B 322     203.726 194.502 191.930  1.00 56.88           C  
ATOM   4012  C   TRP B 322     204.847 195.428 191.491  1.00 56.88           C  
ATOM   4013  O   TRP B 322     204.719 196.126 190.484  1.00 56.88           O  
ATOM   4014  CB  TRP B 322     202.894 195.171 193.017  1.00 56.88           C  
ATOM   4015  CG  TRP B 322     202.460 196.542 192.630  1.00 56.88           C  
ATOM   4016  CD1 TRP B 322     202.734 197.689 193.287  1.00 56.88           C  
ATOM   4017  CD2 TRP B 322     201.680 196.911 191.488  1.00 56.88           C  
ATOM   4018  NE1 TRP B 322     202.179 198.754 192.634  1.00 56.88           N  
ATOM   4019  CE2 TRP B 322     201.522 198.298 191.525  1.00 56.88           C  
ATOM   4020  CE3 TRP B 322     201.097 196.200 190.440  1.00 56.88           C  
ATOM   4021  CZ2 TRP B 322     200.812 198.987 190.562  1.00 56.88           C  
ATOM   4022  CZ3 TRP B 322     200.395 196.892 189.484  1.00 56.88           C  
ATOM   4023  CH2 TRP B 322     200.260 198.265 189.550  1.00 56.88           C  
ATOM   4024  N   LEU B 323     205.951 195.456 192.229  1.00 57.70           N  
ATOM   4025  CA  LEU B 323     207.044 196.343 191.858  1.00 57.70           C  
ATOM   4026  C   LEU B 323     207.663 195.937 190.533  1.00 57.70           C  
ATOM   4027  O   LEU B 323     207.952 196.788 189.690  1.00 57.70           O  
ATOM   4028  CB  LEU B 323     208.111 196.363 192.944  1.00 57.70           C  
ATOM   4029  CG  LEU B 323     207.696 196.862 194.315  1.00 57.70           C  
ATOM   4030  CD1 LEU B 323     208.874 196.774 195.240  1.00 57.70           C  
ATOM   4031  CD2 LEU B 323     207.183 198.260 194.234  1.00 57.70           C  
ATOM   4032  N   LEU B 324     207.891 194.647 190.331  1.00 59.17           N  
ATOM   4033  CA  LEU B 324     208.503 194.222 189.085  1.00 59.17           C  
ATOM   4034  C   LEU B 324     207.549 194.472 187.935  1.00 59.17           C  
ATOM   4035  O   LEU B 324     207.820 195.307 187.072  1.00 59.17           O  
ATOM   4036  CB  LEU B 324     208.886 192.749 189.142  1.00 59.17           C  
ATOM   4037  CG  LEU B 324     210.281 192.505 189.701  1.00 59.17           C  
ATOM   4038  CD1 LEU B 324     210.574 191.027 189.757  1.00 59.17           C  
ATOM   4039  CD2 LEU B 324     211.307 193.227 188.864  1.00 59.17           C  
ATOM   4040  N   LEU B 325     206.402 193.800 187.959  1.00 59.58           N  
ATOM   4041  CA  LEU B 325     205.446 193.905 186.865  1.00 59.58           C  
ATOM   4042  C   LEU B 325     204.935 195.326 186.713  1.00 59.58           C  
ATOM   4043  O   LEU B 325     205.190 195.989 185.706  1.00 59.58           O  
ATOM   4044  CB  LEU B 325     204.290 192.943 187.107  1.00 59.58           C  
ATOM   4045  CG  LEU B 325     203.096 193.036 186.175  1.00 59.58           C  
ATOM   4046  CD1 LEU B 325     203.529 192.928 184.735  1.00 59.58           C  
ATOM   4047  CD2 LEU B 325     202.135 191.929 186.523  1.00 59.58           C  
ATOM   4048  N   GLY B 326     204.217 195.816 187.715  1.00 58.89           N  
ATOM   4049  CA  GLY B 326     203.596 197.117 187.585  1.00 58.89           C  
ATOM   4050  C   GLY B 326     204.592 198.249 187.448  1.00 58.89           C  
ATOM   4051  O   GLY B 326     204.448 199.105 186.577  1.00 58.89           O  
ATOM   4052  N   SER B 327     205.619 198.269 188.280  1.00 59.47           N  
ATOM   4053  CA  SER B 327     206.398 199.492 188.391  1.00 59.47           C  
ATOM   4054  C   SER B 327     207.554 199.607 187.413  1.00 59.47           C  
ATOM   4055  O   SER B 327     207.947 200.728 187.086  1.00 59.47           O  
ATOM   4056  CB  SER B 327     206.953 199.649 189.798  1.00 59.47           C  
ATOM   4057  OG  SER B 327     207.751 200.808 189.842  1.00 59.47           O  
ATOM   4058  N   ILE B 328     208.137 198.508 186.953  1.00 63.07           N  
ATOM   4059  CA  ILE B 328     209.305 198.574 186.082  1.00 63.07           C  
ATOM   4060  C   ILE B 328     208.956 198.236 184.641  1.00 63.07           C  
ATOM   4061  O   ILE B 328     209.349 198.953 183.722  1.00 63.07           O  
ATOM   4062  CB  ILE B 328     210.441 197.678 186.618  1.00 63.07           C  
ATOM   4063  CG1 ILE B 328     211.175 198.398 187.750  1.00 63.07           C  
ATOM   4064  CG2 ILE B 328     211.411 197.340 185.511  1.00 63.07           C  
ATOM   4065  CD1 ILE B 328     212.128 197.530 188.526  1.00 63.07           C  
ATOM   4066  N   ILE B 329     208.222 197.149 184.408  1.00 67.27           N  
ATOM   4067  CA  ILE B 329     207.782 196.861 183.047  1.00 67.27           C  
ATOM   4068  C   ILE B 329     206.811 197.925 182.548  1.00 67.27           C  
ATOM   4069  O   ILE B 329     207.107 198.652 181.592  1.00 67.27           O  
ATOM   4070  CB  ILE B 329     207.185 195.450 182.933  1.00 67.27           C  
ATOM   4071  CG1 ILE B 329     208.254 194.380 183.160  1.00 67.27           C  
ATOM   4072  CG2 ILE B 329     206.517 195.271 181.598  1.00 67.27           C  
ATOM   4073  CD1 ILE B 329     208.447 193.924 184.549  1.00 67.27           C  
ATOM   4074  N   PHE B 330     205.649 198.051 183.193  1.00 71.12           N  
ATOM   4075  CA  PHE B 330     204.612 198.915 182.639  1.00 71.12           C  
ATOM   4076  C   PHE B 330     205.080 200.348 182.490  1.00 71.12           C  
ATOM   4077  O   PHE B 330     204.793 200.983 181.472  1.00 71.12           O  
ATOM   4078  CB  PHE B 330     203.350 198.874 183.486  1.00 71.12           C  
ATOM   4079  CG  PHE B 330     202.387 197.828 183.055  1.00 71.12           C  
ATOM   4080  CD1 PHE B 330     201.563 198.047 181.971  1.00 71.12           C  
ATOM   4081  CD2 PHE B 330     202.290 196.638 183.735  1.00 71.12           C  
ATOM   4082  CE1 PHE B 330     200.673 197.097 181.565  1.00 71.12           C  
ATOM   4083  CE2 PHE B 330     201.400 195.680 183.334  1.00 71.12           C  
ATOM   4084  CZ  PHE B 330     200.590 195.909 182.247  1.00 71.12           C  
ATOM   4085  N   ARG B 331     205.805 200.874 183.470  1.00 75.02           N  
ATOM   4086  CA  ARG B 331     206.343 202.218 183.324  1.00 75.02           C  
ATOM   4087  C   ARG B 331     207.275 202.331 182.125  1.00 75.02           C  
ATOM   4088  O   ARG B 331     207.465 203.432 181.604  1.00 75.02           O  
ATOM   4089  CB  ARG B 331     207.062 202.630 184.609  1.00 75.02           C  
ATOM   4090  CG  ARG B 331     207.468 204.085 184.679  1.00 75.02           C  
ATOM   4091  CD  ARG B 331     208.897 204.254 184.221  1.00 75.02           C  
ATOM   4092  NE  ARG B 331     209.414 205.586 184.491  1.00 75.02           N  
ATOM   4093  CZ  ARG B 331     210.594 206.024 184.073  1.00 75.02           C  
ATOM   4094  NH1 ARG B 331     210.984 207.252 184.372  1.00 75.02           N  
ATOM   4095  NH2 ARG B 331     211.381 205.237 183.354  1.00 75.02           N  
ATOM   4096  N   ASN B 332     207.842 201.221 181.666  1.00 80.06           N  
ATOM   4097  CA  ASN B 332     208.779 201.248 180.552  1.00 80.06           C  
ATOM   4098  C   ASN B 332     208.087 201.063 179.212  1.00 80.06           C  
ATOM   4099  O   ASN B 332     208.563 201.574 178.188  1.00 80.06           O  
ATOM   4100  CB  ASN B 332     209.826 200.159 180.757  1.00 80.06           C  
ATOM   4101  CG  ASN B 332     211.076 200.684 181.404  1.00 80.06           C  
ATOM   4102  OD1 ASN B 332     211.040 201.676 182.126  1.00 80.06           O  
ATOM   4103  ND2 ASN B 332     212.179 199.990 181.201  1.00 80.06           N  
ATOM   4104  N   ILE B 333     206.963 200.352 179.203  1.00 79.76           N  
ATOM   4105  CA  ILE B 333     206.197 200.202 177.975  1.00 79.76           C  
ATOM   4106  C   ILE B 333     205.690 201.554 177.492  1.00 79.76           C  
ATOM   4107  O   ILE B 333     205.644 201.813 176.285  1.00 79.76           O  
ATOM   4108  CB  ILE B 333     205.052 199.198 178.185  1.00 79.76           C  
ATOM   4109  CG1 ILE B 333     205.590 197.776 178.138  1.00 79.76           C  
ATOM   4110  CG2 ILE B 333     203.987 199.360 177.133  1.00 79.76           C  
ATOM   4111  CD1 ILE B 333     204.687 196.791 178.792  1.00 79.76           C  
ATOM   4112  N   ILE B 334     205.306 202.438 178.417  1.00 80.82           N  
ATOM   4113  CA  ILE B 334     204.831 203.768 178.031  1.00 80.82           C  
ATOM   4114  C   ILE B 334     205.908 204.517 177.262  1.00 80.82           C  
ATOM   4115  O   ILE B 334     205.653 205.109 176.206  1.00 80.82           O  
ATOM   4116  CB  ILE B 334     204.399 204.566 179.270  1.00 80.82           C  
ATOM   4117  CG1 ILE B 334     203.351 203.816 180.064  1.00 80.82           C  
ATOM   4118  CG2 ILE B 334     203.853 205.896 178.860  1.00 80.82           C  
ATOM   4119  CD1 ILE B 334     203.031 204.488 181.370  1.00 80.82           C  
ATOM   4120  N   VAL B 335     207.127 204.514 177.794  1.00 88.10           N  
ATOM   4121  CA  VAL B 335     208.236 205.194 177.143  1.00 88.10           C  
ATOM   4122  C   VAL B 335     208.507 204.579 175.783  1.00 88.10           C  
ATOM   4123  O   VAL B 335     208.745 205.290 174.795  1.00 88.10           O  
ATOM   4124  CB  VAL B 335     209.477 205.143 178.044  1.00 88.10           C  
ATOM   4125  CG1 VAL B 335     210.690 205.600 177.283  1.00 88.10           C  
ATOM   4126  CG2 VAL B 335     209.257 205.997 179.258  1.00 88.10           C  
ATOM   4127  N   ALA B 336     208.483 203.248 175.708  1.00 94.94           N  
ATOM   4128  CA  ALA B 336     208.671 202.590 174.420  1.00 94.94           C  
ATOM   4129  C   ALA B 336     207.638 203.070 173.412  1.00 94.94           C  
ATOM   4130  O   ALA B 336     207.977 203.429 172.280  1.00 94.94           O  
ATOM   4131  CB  ALA B 336     208.600 201.074 174.589  1.00 94.94           C  
ATOM   4132  N   MET B 337     206.372 203.117 173.822  1.00 94.10           N  
ATOM   4133  CA  MET B 337     205.310 203.525 172.911  1.00 94.10           C  
ATOM   4134  C   MET B 337     205.499 204.959 172.437  1.00 94.10           C  
ATOM   4135  O   MET B 337     205.301 205.264 171.253  1.00 94.10           O  
ATOM   4136  CB  MET B 337     203.957 203.361 173.589  1.00 94.10           C  
ATOM   4137  CG  MET B 337     203.459 201.941 173.609  1.00 94.10           C  
ATOM   4138  SD  MET B 337     202.363 201.591 172.229  1.00 94.10           S  
ATOM   4139  CE  MET B 337     202.509 199.813 172.137  1.00 94.10           C  
ATOM   4140  N   MET B 338     205.872 205.859 173.343  1.00 94.68           N  
ATOM   4141  CA  MET B 338     205.999 207.252 172.933  1.00 94.68           C  
ATOM   4142  C   MET B 338     207.185 207.448 171.993  1.00 94.68           C  
ATOM   4143  O   MET B 338     207.111 208.243 171.043  1.00 94.68           O  
ATOM   4144  CB  MET B 338     206.094 208.157 174.155  1.00 94.68           C  
ATOM   4145  CG  MET B 338     204.727 208.587 174.628  1.00 94.68           C  
ATOM   4146  SD  MET B 338     204.646 209.038 176.352  1.00 94.68           S  
ATOM   4147  CE  MET B 338     206.059 210.105 176.418  1.00 94.68           C  
ATOM   4148  N   VAL B 339     208.275 206.711 172.215  1.00100.02           N  
ATOM   4149  CA  VAL B 339     209.374 206.755 171.255  1.00100.02           C  
ATOM   4150  C   VAL B 339     208.917 206.222 169.905  1.00100.02           C  
ATOM   4151  O   VAL B 339     209.281 206.763 168.852  1.00100.02           O  
ATOM   4152  CB  VAL B 339     210.590 205.977 171.777  1.00100.02           C  
ATOM   4153  CG1 VAL B 339     211.671 205.944 170.721  1.00100.02           C  
ATOM   4154  CG2 VAL B 339     211.111 206.609 173.024  1.00100.02           C  
ATOM   4155  N   THR B 340     208.116 205.154 169.908  1.00103.57           N  
ATOM   4156  CA  THR B 340     207.614 204.635 168.641  1.00103.57           C  
ATOM   4157  C   THR B 340     206.802 205.683 167.906  1.00103.57           C  
ATOM   4158  O   THR B 340     206.918 205.826 166.685  1.00103.57           O  
ATOM   4159  CB  THR B 340     206.748 203.401 168.851  1.00103.57           C  
ATOM   4160  OG1 THR B 340     205.608 203.760 169.634  1.00103.57           O  
ATOM   4161  CG2 THR B 340     207.518 202.304 169.529  1.00103.57           C  
ATOM   4162  N   ASN B 341     205.955 206.411 168.626  1.00102.32           N  
ATOM   4163  CA  ASN B 341     205.118 207.398 167.957  1.00102.32           C  
ATOM   4164  C   ASN B 341     205.944 208.538 167.387  1.00102.32           C  
ATOM   4165  O   ASN B 341     205.641 209.043 166.299  1.00102.32           O  
ATOM   4166  CB  ASN B 341     204.050 207.918 168.902  1.00102.32           C  
ATOM   4167  CG  ASN B 341     202.978 206.901 169.137  1.00102.32           C  
ATOM   4168  OD1 ASN B 341     203.244 205.701 169.164  1.00102.32           O  
ATOM   4169  ND2 ASN B 341     201.747 207.357 169.221  1.00102.32           N  
ATOM   4170  N   PHE B 342     206.987 208.963 168.100  1.00103.08           N  
ATOM   4171  CA  PHE B 342     207.887 209.947 167.508  1.00103.08           C  
ATOM   4172  C   PHE B 342     208.523 209.406 166.239  1.00103.08           C  
ATOM   4173  O   PHE B 342     208.648 210.125 165.237  1.00103.08           O  
ATOM   4174  CB  PHE B 342     208.958 210.364 168.503  1.00103.08           C  
ATOM   4175  CG  PHE B 342     208.603 211.585 169.269  1.00103.08           C  
ATOM   4176  CD1 PHE B 342     207.506 211.589 170.106  1.00103.08           C  
ATOM   4177  CD2 PHE B 342     209.335 212.738 169.132  1.00103.08           C  
ATOM   4178  CE1 PHE B 342     207.169 212.712 170.812  1.00103.08           C  
ATOM   4179  CE2 PHE B 342     208.996 213.862 169.831  1.00103.08           C  
ATOM   4180  CZ  PHE B 342     207.915 213.850 170.674  1.00103.08           C  
ATOM   4181  N   GLN B 343     208.923 208.137 166.255  1.00116.55           N  
ATOM   4182  CA  GLN B 343     209.476 207.539 165.046  1.00116.55           C  
ATOM   4183  C   GLN B 343     208.471 207.573 163.906  1.00116.55           C  
ATOM   4184  O   GLN B 343     208.826 207.883 162.763  1.00116.55           O  
ATOM   4185  CB  GLN B 343     209.922 206.112 165.335  1.00116.55           C  
ATOM   4186  CG  GLN B 343     211.231 206.058 166.079  1.00116.55           C  
ATOM   4187  CD  GLN B 343     212.391 206.555 165.237  1.00116.55           C  
ATOM   4188  OE1 GLN B 343     212.457 206.298 164.031  1.00116.55           O  
ATOM   4189  NE2 GLN B 343     213.309 207.278 165.867  1.00116.55           N  
ATOM   4190  N   ASN B 344     207.210 207.274 164.202  1.00120.37           N  
ATOM   4191  CA  ASN B 344     206.189 207.331 163.164  1.00120.37           C  
ATOM   4192  C   ASN B 344     206.101 208.727 162.575  1.00120.37           C  
ATOM   4193  O   ASN B 344     206.303 208.908 161.367  1.00120.37           O  
ATOM   4194  CB  ASN B 344     204.842 206.901 163.730  1.00120.37           C  
ATOM   4195  CG  ASN B 344     204.752 205.413 163.916  1.00120.37           C  
ATOM   4196  OD1 ASN B 344     205.600 204.664 163.434  1.00120.37           O  
ATOM   4197  ND2 ASN B 344     203.730 204.966 164.632  1.00120.37           N  
ATOM   4198  N   ILE B 345     205.938 209.736 163.433  1.00120.43           N  
ATOM   4199  CA  ILE B 345     205.796 211.108 162.951  1.00120.43           C  
ATOM   4200  C   ILE B 345     206.964 211.475 162.048  1.00120.43           C  
ATOM   4201  O   ILE B 345     206.784 212.082 160.978  1.00120.43           O  
ATOM   4202  CB  ILE B 345     205.680 212.074 164.139  1.00120.43           C  
ATOM   4203  CG1 ILE B 345     204.269 212.047 164.710  1.00120.43           C  
ATOM   4204  CG2 ILE B 345     206.061 213.476 163.720  1.00120.43           C  
ATOM   4205  CD1 ILE B 345     204.085 213.013 165.848  1.00120.43           C  
ATOM   4206  N   ARG B 346     208.177 211.093 162.455  1.00125.21           N  
ATOM   4207  CA  ARG B 346     209.333 211.258 161.583  1.00125.21           C  
ATOM   4208  C   ARG B 346     209.114 210.582 160.237  1.00125.21           C  
ATOM   4209  O   ARG B 346     209.447 211.150 159.192  1.00125.21           O  
ATOM   4210  CB  ARG B 346     210.587 210.702 162.247  1.00125.21           C  
ATOM   4211  CG  ARG B 346     211.784 210.721 161.331  1.00125.21           C  
ATOM   4212  CD  ARG B 346     213.065 210.633 162.112  1.00125.21           C  
ATOM   4213  NE  ARG B 346     213.156 211.718 163.078  1.00125.21           N  
ATOM   4214  CZ  ARG B 346     213.494 212.962 162.764  1.00125.21           C  
ATOM   4215  NH1 ARG B 346     213.555 213.896 163.706  1.00125.21           N  
ATOM   4216  NH2 ARG B 346     213.790 213.269 161.510  1.00125.21           N  
ATOM   4217  N   SER B 347     208.558 209.369 160.239  1.00134.36           N  
ATOM   4218  CA  SER B 347     208.414 208.638 158.979  1.00134.36           C  
ATOM   4219  C   SER B 347     207.447 209.333 158.022  1.00134.36           C  
ATOM   4220  O   SER B 347     207.745 209.469 156.828  1.00134.36           O  
ATOM   4221  CB  SER B 347     207.969 207.202 159.245  1.00134.36           C  
ATOM   4222  OG  SER B 347     206.585 207.142 159.529  1.00134.36           O  
ATOM   4223  N   GLU B 348     206.284 209.776 158.515  1.00140.32           N  
ATOM   4224  CA  GLU B 348     205.371 210.484 157.607  1.00140.32           C  
ATOM   4225  C   GLU B 348     205.955 211.808 157.121  1.00140.32           C  
ATOM   4226  O   GLU B 348     205.793 212.167 155.946  1.00140.32           O  
ATOM   4227  CB  GLU B 348     203.956 210.700 158.177  1.00140.32           C  
ATOM   4228  CG  GLU B 348     203.078 209.438 158.366  1.00140.32           C  
ATOM   4229  CD  GLU B 348     203.303 208.687 159.634  1.00140.32           C  
ATOM   4230  OE1 GLU B 348     204.095 209.160 160.444  1.00140.32           O  
ATOM   4231  OE2 GLU B 348     202.686 207.622 159.823  1.00140.32           O  
ATOM   4232  N   LEU B 349     206.637 212.554 157.989  1.00144.78           N  
ATOM   4233  CA  LEU B 349     207.232 213.798 157.509  1.00144.78           C  
ATOM   4234  C   LEU B 349     208.295 213.525 156.449  1.00144.78           C  
ATOM   4235  O   LEU B 349     208.369 214.228 155.431  1.00144.78           O  
ATOM   4236  CB  LEU B 349     207.813 214.590 158.675  1.00144.78           C  
ATOM   4237  CG  LEU B 349     206.859 215.657 159.217  1.00144.78           C  
ATOM   4238  CD1 LEU B 349     205.619 215.001 159.831  1.00144.78           C  
ATOM   4239  CD2 LEU B 349     207.535 216.599 160.207  1.00144.78           C  
ATOM   4240  N   SER B 350     209.112 212.490 156.650  1.00150.56           N  
ATOM   4241  CA  SER B 350     210.146 212.181 155.670  1.00150.56           C  
ATOM   4242  C   SER B 350     209.534 211.747 154.345  1.00150.56           C  
ATOM   4243  O   SER B 350     209.993 212.168 153.276  1.00150.56           O  
ATOM   4244  CB  SER B 350     211.086 211.106 156.217  1.00150.56           C  
ATOM   4245  OG  SER B 350     211.862 211.613 157.289  1.00150.56           O  
ATOM   4246  N   GLU B 351     208.486 210.922 154.388  1.00155.68           N  
ATOM   4247  CA  GLU B 351     207.891 210.474 153.133  1.00155.68           C  
ATOM   4248  C   GLU B 351     207.223 211.627 152.392  1.00155.68           C  
ATOM   4249  O   GLU B 351     207.246 211.663 151.158  1.00155.68           O  
ATOM   4250  CB  GLU B 351     206.897 209.337 153.372  1.00155.68           C  
ATOM   4251  CG  GLU B 351     205.708 209.685 154.244  1.00155.68           C  
ATOM   4252  CD  GLU B 351     204.599 210.390 153.485  1.00155.68           C  
ATOM   4253  OE1 GLU B 351     204.545 210.238 152.251  1.00155.68           O  
ATOM   4254  OE2 GLU B 351     203.801 211.119 154.111  1.00155.68           O  
ATOM   4255  N   GLU B 352     206.605 212.572 153.111  1.00160.29           N  
ATOM   4256  CA  GLU B 352     205.983 213.688 152.405  1.00160.29           C  
ATOM   4257  C   GLU B 352     207.037 214.615 151.810  1.00160.29           C  
ATOM   4258  O   GLU B 352     206.838 215.170 150.722  1.00160.29           O  
ATOM   4259  CB  GLU B 352     205.019 214.454 153.313  1.00160.29           C  
ATOM   4260  CG  GLU B 352     205.625 215.094 154.540  1.00160.29           C  
ATOM   4261  CD  GLU B 352     206.196 216.469 154.263  1.00160.29           C  
ATOM   4262  OE1 GLU B 352     205.814 217.086 153.247  1.00160.29           O  
ATOM   4263  OE2 GLU B 352     207.032 216.929 155.064  1.00160.29           O  
ATOM   4264  N   MET B 353     208.168 214.792 152.501  1.00162.13           N  
ATOM   4265  CA  MET B 353     209.288 215.504 151.888  1.00162.13           C  
ATOM   4266  C   MET B 353     209.748 214.810 150.612  1.00162.13           C  
ATOM   4267  O   MET B 353     210.007 215.465 149.593  1.00162.13           O  
ATOM   4268  CB  MET B 353     210.449 215.618 152.878  1.00162.13           C  
ATOM   4269  CG  MET B 353     210.208 216.545 154.059  1.00162.13           C  
ATOM   4270  SD  MET B 353     210.603 218.261 153.661  1.00162.13           S  
ATOM   4271  CE  MET B 353     209.015 219.060 153.858  1.00162.13           C  
ATOM   4272  N   SER B 354     209.848 213.479 150.652  1.00169.54           N  
ATOM   4273  CA  SER B 354     210.220 212.719 149.461  1.00169.54           C  
ATOM   4274  C   SER B 354     209.211 212.915 148.336  1.00169.54           C  
ATOM   4275  O   SER B 354     209.592 213.077 147.173  1.00169.54           O  
ATOM   4276  CB  SER B 354     210.343 211.235 149.806  1.00169.54           C  
ATOM   4277  OG  SER B 354     210.278 210.429 148.642  1.00169.54           O  
ATOM   4278  N   HIS B 355     207.919 212.883 148.663  1.00174.72           N  
ATOM   4279  CA  HIS B 355     206.893 213.055 147.641  1.00174.72           C  
ATOM   4280  C   HIS B 355     206.966 214.438 147.015  1.00174.72           C  
ATOM   4281  O   HIS B 355     206.823 214.582 145.796  1.00174.72           O  
ATOM   4282  CB  HIS B 355     205.509 212.809 148.235  1.00174.72           C  
ATOM   4283  CG  HIS B 355     204.385 213.186 147.322  1.00174.72           C  
ATOM   4284  ND1 HIS B 355     203.946 214.484 147.179  1.00174.72           N  
ATOM   4285  CD2 HIS B 355     203.607 212.435 146.507  1.00174.72           C  
ATOM   4286  CE1 HIS B 355     202.949 214.517 146.314  1.00174.72           C  
ATOM   4287  NE2 HIS B 355     202.723 213.287 145.892  1.00174.72           N  
ATOM   4288  N   LEU B 356     207.181 215.472 147.832  1.00174.72           N  
ATOM   4289  CA  LEU B 356     207.306 216.819 147.282  1.00174.72           C  
ATOM   4290  C   LEU B 356     208.532 216.940 146.388  1.00174.72           C  
ATOM   4291  O   LEU B 356     208.472 217.561 145.321  1.00174.72           O  
ATOM   4292  CB  LEU B 356     207.362 217.851 148.404  1.00174.72           C  
ATOM   4293  CG  LEU B 356     206.020 218.478 148.777  1.00174.72           C  
ATOM   4294  CD1 LEU B 356     205.542 219.374 147.647  1.00174.72           C  
ATOM   4295  CD2 LEU B 356     204.981 217.416 149.100  1.00174.72           C  
ATOM   4296  N   GLU B 357     209.652 216.342 146.798  1.00179.02           N  
ATOM   4297  CA  GLU B 357     210.850 216.408 145.968  1.00179.02           C  
ATOM   4298  C   GLU B 357     210.667 215.640 144.664  1.00179.02           C  
ATOM   4299  O   GLU B 357     211.146 216.070 143.609  1.00179.02           O  
ATOM   4300  CB  GLU B 357     212.054 215.883 146.745  1.00179.02           C  
ATOM   4301  CG  GLU B 357     212.489 216.786 147.893  1.00179.02           C  
ATOM   4302  CD  GLU B 357     213.064 218.111 147.425  1.00179.02           C  
ATOM   4303  OE1 GLU B 357     214.305 218.237 147.389  1.00179.02           O  
ATOM   4304  OE2 GLU B 357     212.280 219.030 147.105  1.00179.02           O  
ATOM   4305  N   VAL B 358     209.971 214.503 144.711  1.00182.99           N  
ATOM   4306  CA  VAL B 358     209.732 213.730 143.495  1.00182.99           C  
ATOM   4307  C   VAL B 358     208.791 214.482 142.562  1.00182.99           C  
ATOM   4308  O   VAL B 358     208.974 214.483 141.337  1.00182.99           O  
ATOM   4309  CB  VAL B 358     209.194 212.331 143.851  1.00182.99           C  
ATOM   4310  CG1 VAL B 358     208.620 211.641 142.623  1.00182.99           C  
ATOM   4311  CG2 VAL B 358     210.299 211.486 144.456  1.00182.99           C  
ATOM   4312  N   GLN B 359     207.776 215.144 143.122  1.00184.90           N  
ATOM   4313  CA  GLN B 359     206.908 215.988 142.309  1.00184.90           C  
ATOM   4314  C   GLN B 359     207.694 217.126 141.670  1.00184.90           C  
ATOM   4315  O   GLN B 359     207.466 217.475 140.506  1.00184.90           O  
ATOM   4316  CB  GLN B 359     205.767 216.538 143.162  1.00184.90           C  
ATOM   4317  CG  GLN B 359     204.643 215.555 143.424  1.00184.90           C  
ATOM   4318  CD  GLN B 359     203.776 215.319 142.202  1.00184.90           C  
ATOM   4319  OE1 GLN B 359     203.690 214.203 141.691  1.00184.90           O  
ATOM   4320  NE2 GLN B 359     203.133 216.376 141.722  1.00184.90           N  
ATOM   4321  N   TYR B 360     208.632 217.714 142.416  1.00189.08           N  
ATOM   4322  CA  TYR B 360     209.463 218.779 141.864  1.00189.08           C  
ATOM   4323  C   TYR B 360     210.372 218.261 140.753  1.00189.08           C  
ATOM   4324  O   TYR B 360     210.626 218.967 139.769  1.00189.08           O  
ATOM   4325  CB  TYR B 360     210.282 219.421 142.980  1.00189.08           C  
ATOM   4326  CG  TYR B 360     210.742 220.828 142.683  1.00189.08           C  
ATOM   4327  CD1 TYR B 360     209.848 221.891 142.721  1.00189.08           C  
ATOM   4328  CD2 TYR B 360     212.070 221.099 142.390  1.00189.08           C  
ATOM   4329  CE1 TYR B 360     210.259 223.181 142.461  1.00189.08           C  
ATOM   4330  CE2 TYR B 360     212.493 222.386 142.133  1.00189.08           C  
ATOM   4331  CZ  TYR B 360     211.583 223.424 142.167  1.00189.08           C  
ATOM   4332  OH  TYR B 360     211.997 224.712 141.906  1.00189.08           O  
ATOM   4333  N   LYS B 361     210.889 217.040 140.901  1.00192.23           N  
ATOM   4334  CA  LYS B 361     211.695 216.447 139.837  1.00192.23           C  
ATOM   4335  C   LYS B 361     210.858 216.192 138.591  1.00192.23           C  
ATOM   4336  O   LYS B 361     211.312 216.432 137.467  1.00192.23           O  
ATOM   4337  CB  LYS B 361     212.344 215.151 140.319  1.00192.23           C  
ATOM   4338  CG  LYS B 361     213.370 215.363 141.409  1.00192.23           C  
ATOM   4339  CD  LYS B 361     214.498 216.248 140.923  1.00192.23           C  
ATOM   4340  CE  LYS B 361     215.302 216.768 142.095  1.00192.23           C  
ATOM   4341  NZ  LYS B 361     214.469 217.670 142.943  1.00192.23           N  
ATOM   4342  N   ALA B 362     209.630 215.701 138.773  1.00196.24           N  
ATOM   4343  CA  ALA B 362     208.727 215.539 137.637  1.00196.24           C  
ATOM   4344  C   ALA B 362     208.432 216.881 136.985  1.00196.24           C  
ATOM   4345  O   ALA B 362     208.308 216.970 135.759  1.00196.24           O  
ATOM   4346  CB  ALA B 362     207.432 214.860 138.080  1.00196.24           C  
ATOM   4347  N   ASP B 363     208.314 217.937 137.796  1.00196.00           N  
ATOM   4348  CA  ASP B 363     208.109 219.277 137.255  1.00196.00           C  
ATOM   4349  C   ASP B 363     209.289 219.716 136.398  1.00196.00           C  
ATOM   4350  O   ASP B 363     209.112 220.121 135.244  1.00196.00           O  
ATOM   4351  CB  ASP B 363     207.877 220.270 138.393  1.00196.00           C  
ATOM   4352  CG  ASP B 363     207.241 221.556 137.920  1.00196.00           C  
ATOM   4353  OD1 ASP B 363     206.012 221.566 137.701  1.00196.00           O  
ATOM   4354  OD2 ASP B 363     207.970 222.557 137.769  1.00196.00           O  
ATOM   4355  N   MET B 364     210.504 219.623 136.940  1.00193.95           N  
ATOM   4356  CA  MET B 364     211.691 219.938 136.151  1.00193.95           C  
ATOM   4357  C   MET B 364     211.811 219.041 134.929  1.00193.95           C  
ATOM   4358  O   MET B 364     212.497 219.397 133.965  1.00193.95           O  
ATOM   4359  CB  MET B 364     212.949 219.840 137.015  1.00193.95           C  
ATOM   4360  CG  MET B 364     212.937 220.771 138.209  1.00193.95           C  
ATOM   4361  SD  MET B 364     213.246 222.460 137.658  1.00193.95           S  
ATOM   4362  CE  MET B 364     212.285 223.406 138.830  1.00193.95           C  
ATOM   4363  N   PHE B 365     211.169 217.873 134.951  1.00196.68           N  
ATOM   4364  CA  PHE B 365     211.091 217.059 133.743  1.00196.68           C  
ATOM   4365  C   PHE B 365     209.905 217.477 132.881  1.00196.68           C  
ATOM   4366  O   PHE B 365     209.954 217.376 131.649  1.00196.68           O  
ATOM   4367  CB  PHE B 365     211.004 215.578 134.109  1.00196.68           C  
ATOM   4368  CG  PHE B 365     212.287 215.009 134.642  1.00196.68           C  
ATOM   4369  CD1 PHE B 365     213.507 215.408 134.118  1.00196.68           C  
ATOM   4370  CD2 PHE B 365     212.274 214.063 135.656  1.00196.68           C  
ATOM   4371  CE1 PHE B 365     214.691 214.883 134.604  1.00196.68           C  
ATOM   4372  CE2 PHE B 365     213.454 213.532 136.144  1.00196.68           C  
ATOM   4373  CZ  PHE B 365     214.663 213.942 135.619  1.00196.68           C  
ATOM   4374  N   LYS B 366     208.825 217.947 133.513  1.00198.30           N  
ATOM   4375  CA  LYS B 366     207.642 218.350 132.756  1.00198.30           C  
ATOM   4376  C   LYS B 366     207.825 219.724 132.122  1.00198.30           C  
ATOM   4377  O   LYS B 366     207.191 220.031 131.106  1.00198.30           O  
ATOM   4378  CB  LYS B 366     206.406 218.338 133.657  1.00198.30           C  
ATOM   4379  CG  LYS B 366     206.093 219.667 134.335  1.00198.30           C  
ATOM   4380  CD  LYS B 366     204.734 219.632 135.017  1.00198.30           C  
ATOM   4381  CE  LYS B 366     204.648 218.475 136.004  1.00198.30           C  
ATOM   4382  NZ  LYS B 366     203.413 218.530 136.829  1.00198.30           N  
ATOM   4383  N   GLN B 367     208.674 220.569 132.711  1.00198.16           N  
ATOM   4384  CA  GLN B 367     208.847 221.916 132.180  1.00198.16           C  
ATOM   4385  C   GLN B 367     209.634 221.897 130.878  1.00198.16           C  
ATOM   4386  O   GLN B 367     209.376 222.702 129.975  1.00198.16           O  
ATOM   4387  CB  GLN B 367     209.532 222.812 133.213  1.00198.16           C  
ATOM   4388  CG  GLN B 367     208.701 223.132 134.465  1.00198.16           C  
ATOM   4389  CD  GLN B 367     207.453 223.971 134.203  1.00198.16           C  
ATOM   4390  OE1 GLN B 367     207.037 224.171 133.062  1.00198.16           O  
ATOM   4391  NE2 GLN B 367     206.850 224.464 135.276  1.00198.16           N  
ATOM   4392  N   GLN B 368     210.601 220.982 130.760  1.00198.94           N  
ATOM   4393  CA  GLN B 368     211.374 220.882 129.525  1.00198.94           C  
ATOM   4394  C   GLN B 368     210.499 220.436 128.363  1.00198.94           C  
ATOM   4395  O   GLN B 368     210.783 220.758 127.203  1.00198.94           O  
ATOM   4396  CB  GLN B 368     212.542 219.914 129.710  1.00198.94           C  
ATOM   4397  CG  GLN B 368     213.273 220.068 131.029  1.00198.94           C  
ATOM   4398  CD  GLN B 368     214.195 218.902 131.319  1.00198.94           C  
ATOM   4399  OE1 GLN B 368     214.110 217.854 130.679  1.00198.94           O  
ATOM   4400  NE2 GLN B 368     215.075 219.074 132.298  1.00198.94           N  
ATOM   4401  N   ILE B 369     209.433 219.688 128.655  1.00202.91           N  
ATOM   4402  CA  ILE B 369     208.575 219.160 127.598  1.00202.91           C  
ATOM   4403  C   ILE B 369     207.950 220.299 126.805  1.00202.91           C  
ATOM   4404  O   ILE B 369     208.050 220.353 125.574  1.00202.91           O  
ATOM   4405  CB  ILE B 369     207.501 218.234 128.197  1.00202.91           C  
ATOM   4406  CG1 ILE B 369     208.141 216.952 128.732  1.00202.91           C  
ATOM   4407  CG2 ILE B 369     206.433 217.911 127.164  1.00202.91           C  
ATOM   4408  CD1 ILE B 369     207.247 216.158 129.656  1.00202.91           C  
ATOM   4409  N   ILE B 370     207.325 221.247 127.504  1.00201.83           N  
ATOM   4410  CA  ILE B 370     206.686 222.366 126.818  1.00201.83           C  
ATOM   4411  C   ILE B 370     207.733 223.266 126.177  1.00201.83           C  
ATOM   4412  O   ILE B 370     207.512 223.820 125.094  1.00201.83           O  
ATOM   4413  CB  ILE B 370     205.774 223.137 127.788  1.00201.83           C  
ATOM   4414  CG1 ILE B 370     204.594 222.253 128.208  1.00201.83           C  
ATOM   4415  CG2 ILE B 370     205.278 224.429 127.152  1.00201.83           C  
ATOM   4416  CD1 ILE B 370     203.782 222.813 129.351  1.00201.83           C  
ATOM   4417  N   GLN B 371     208.890 223.422 126.826  1.00201.34           N  
ATOM   4418  CA  GLN B 371     209.983 224.168 126.207  1.00201.34           C  
ATOM   4419  C   GLN B 371     210.389 223.535 124.884  1.00201.34           C  
ATOM   4420  O   GLN B 371     210.588 224.235 123.884  1.00201.34           O  
ATOM   4421  CB  GLN B 371     211.183 224.234 127.151  1.00201.34           C  
ATOM   4422  CG  GLN B 371     210.961 225.069 128.398  1.00201.34           C  
ATOM   4423  CD  GLN B 371     212.047 224.859 129.434  1.00201.34           C  
ATOM   4424  OE1 GLN B 371     212.729 223.834 129.436  1.00201.34           O  
ATOM   4425  NE2 GLN B 371     212.208 225.826 130.328  1.00201.34           N  
ATOM   4426  N   ARG B 372     210.516 222.207 124.861  1.00201.07           N  
ATOM   4427  CA  ARG B 372     210.810 221.518 123.610  1.00201.07           C  
ATOM   4428  C   ARG B 372     209.612 221.552 122.668  1.00201.07           C  
ATOM   4429  O   ARG B 372     209.774 221.752 121.459  1.00201.07           O  
ATOM   4430  CB  ARG B 372     211.244 220.080 123.895  1.00201.07           C  
ATOM   4431  CG  ARG B 372     212.647 219.970 124.480  1.00201.07           C  
ATOM   4432  CD  ARG B 372     213.002 218.532 124.806  1.00201.07           C  
ATOM   4433  NE  ARG B 372     214.338 218.402 125.379  1.00201.07           N  
ATOM   4434  CZ  ARG B 372     214.793 217.296 125.961  1.00201.07           C  
ATOM   4435  NH1 ARG B 372     214.017 216.225 126.044  1.00201.07           N  
ATOM   4436  NH2 ARG B 372     216.021 217.259 126.459  1.00201.07           N  
ATOM   4437  N   ARG B 373     208.400 221.373 123.204  1.00200.35           N  
ATOM   4438  CA  ARG B 373     207.207 221.399 122.362  1.00200.35           C  
ATOM   4439  C   ARG B 373     206.974 222.773 121.748  1.00200.35           C  
ATOM   4440  O   ARG B 373     206.227 222.896 120.770  1.00200.35           O  
ATOM   4441  CB  ARG B 373     205.979 220.962 123.161  1.00200.35           C  
ATOM   4442  CG  ARG B 373     205.951 219.485 123.505  1.00200.35           C  
ATOM   4443  CD  ARG B 373     204.646 219.095 124.181  1.00200.35           C  
ATOM   4444  NE  ARG B 373     204.530 217.647 124.338  1.00200.35           N  
ATOM   4445  CZ  ARG B 373     203.431 217.025 124.750  1.00200.35           C  
ATOM   4446  NH1 ARG B 373     202.343 217.722 125.042  1.00200.35           N  
ATOM   4447  NH2 ARG B 373     203.417 215.705 124.858  1.00200.35           N  
ATOM   4448  N   GLN B 374     207.580 223.814 122.307  1.00201.02           N  
ATOM   4449  CA  GLN B 374     207.512 225.138 121.704  1.00201.02           C  
ATOM   4450  C   GLN B 374     208.613 225.300 120.662  1.00201.02           C  
ATOM   4451  O   GLN B 374     209.112 224.316 120.115  1.00201.02           O  
ATOM   4452  CB  GLN B 374     207.626 226.230 122.768  1.00201.02           C  
ATOM   4453  CG  GLN B 374     206.393 226.391 123.638  1.00201.02           C  
ATOM   4454  CD  GLN B 374     206.624 227.348 124.790  1.00201.02           C  
ATOM   4455  OE1 GLN B 374     207.758 227.546 125.226  1.00201.02           O  
ATOM   4456  NE2 GLN B 374     205.549 227.950 125.288  1.00201.02           N  
TER    4457      GLN B 374                                                      
ATOM   4458  N   GLU C  38     175.630 166.609 163.930  1.00177.55           N  
ATOM   4459  CA  GLU C  38     174.274 167.144 163.925  1.00177.55           C  
ATOM   4460  C   GLU C  38     174.003 167.987 165.167  1.00177.55           C  
ATOM   4461  O   GLU C  38     173.533 169.116 165.062  1.00177.55           O  
ATOM   4462  CB  GLU C  38     173.250 166.008 163.802  1.00177.55           C  
ATOM   4463  CG  GLU C  38     173.444 164.855 164.777  1.00177.55           C  
ATOM   4464  CD  GLU C  38     174.303 163.749 164.197  1.00177.55           C  
ATOM   4465  OE1 GLU C  38     174.812 163.921 163.070  1.00177.55           O  
ATOM   4466  OE2 GLU C  38     174.475 162.712 164.870  1.00177.55           O  
ATOM   4467  N   CYS C  39     174.296 167.433 166.343  1.00175.78           N  
ATOM   4468  CA  CYS C  39     174.239 168.197 167.581  1.00175.78           C  
ATOM   4469  C   CYS C  39     175.449 169.100 167.759  1.00175.78           C  
ATOM   4470  O   CYS C  39     175.320 170.195 168.315  1.00175.78           O  
ATOM   4471  CB  CYS C  39     174.135 167.256 168.781  1.00175.78           C  
ATOM   4472  SG  CYS C  39     175.613 166.268 169.064  1.00175.78           S  
ATOM   4473  N   GLN C  40     176.608 168.632 167.289  1.00174.49           N  
ATOM   4474  CA  GLN C  40     177.883 169.391 167.402  1.00174.49           C  
ATOM   4475  C   GLN C  40     177.789 170.706 166.619  1.00174.49           C  
ATOM   4476  O   GLN C  40     178.274 171.732 167.137  1.00174.49           O  
ATOM   4477  CB  GLN C  40     179.040 168.539 166.876  1.00174.49           C  
ATOM   4478  CG  GLN C  40     179.231 167.234 167.636  1.00174.49           C  
ATOM   4479  CD  GLN C  40     180.383 166.423 167.096  1.00174.49           C  
ATOM   4480  OE1 GLN C  40     181.054 166.818 166.145  1.00174.49           O  
ATOM   4481  NE2 GLN C  40     180.623 165.274 167.706  1.00174.49           N  
ATOM   4482  N   ALA C  41     177.184 170.677 165.427  1.00174.65           N  
ATOM   4483  CA  ALA C  41     177.085 171.875 164.599  1.00174.65           C  
ATOM   4484  C   ALA C  41     176.237 172.943 165.279  1.00174.65           C  
ATOM   4485  O   ALA C  41     176.666 174.092 165.440  1.00174.65           O  
ATOM   4486  CB  ALA C  41     176.502 171.515 163.234  1.00174.65           C  
ATOM   4487  N   TYR C  42     175.027 172.572 165.698  1.00172.94           N  
ATOM   4488  CA  TYR C  42     174.186 173.492 166.451  1.00172.94           C  
ATOM   4489  C   TYR C  42     174.846 173.909 167.755  1.00172.94           C  
ATOM   4490  O   TYR C  42     174.620 175.020 168.238  1.00172.94           O  
ATOM   4491  CB  TYR C  42     172.831 172.843 166.723  1.00172.94           C  
ATOM   4492  CG  TYR C  42     172.077 173.432 167.890  1.00172.94           C  
ATOM   4493  CD1 TYR C  42     171.398 174.635 167.766  1.00172.94           C  
ATOM   4494  CD2 TYR C  42     172.046 172.784 169.118  1.00172.94           C  
ATOM   4495  CE1 TYR C  42     170.709 175.176 168.829  1.00172.94           C  
ATOM   4496  CE2 TYR C  42     171.357 173.318 170.187  1.00172.94           C  
ATOM   4497  CZ  TYR C  42     170.691 174.514 170.036  1.00172.94           C  
ATOM   4498  OH  TYR C  42     170.003 175.054 171.095  1.00172.94           O  
ATOM   4499  N   PHE C  43     175.678 173.046 168.327  1.00168.20           N  
ATOM   4500  CA  PHE C  43     176.272 173.357 169.618  1.00168.20           C  
ATOM   4501  C   PHE C  43     177.367 174.407 169.463  1.00168.20           C  
ATOM   4502  O   PHE C  43     177.494 175.317 170.288  1.00168.20           O  
ATOM   4503  CB  PHE C  43     176.803 172.065 170.232  1.00168.20           C  
ATOM   4504  CG  PHE C  43     177.071 172.148 171.698  1.00168.20           C  
ATOM   4505  CD1 PHE C  43     176.016 172.090 172.595  1.00168.20           C  
ATOM   4506  CD2 PHE C  43     178.359 172.229 172.185  1.00168.20           C  
ATOM   4507  CE1 PHE C  43     176.235 172.140 173.946  1.00168.20           C  
ATOM   4508  CE2 PHE C  43     178.585 172.280 173.541  1.00168.20           C  
ATOM   4509  CZ  PHE C  43     177.519 172.232 174.422  1.00168.20           C  
ATOM   4510  N   ARG C  44     178.149 174.314 168.387  1.00166.11           N  
ATOM   4511  CA  ARG C  44     179.075 175.388 168.042  1.00166.11           C  
ATOM   4512  C   ARG C  44     178.331 176.659 167.644  1.00166.11           C  
ATOM   4513  O   ARG C  44     178.813 177.771 167.902  1.00166.11           O  
ATOM   4514  CB  ARG C  44     180.003 174.929 166.919  1.00166.11           C  
ATOM   4515  CG  ARG C  44     180.919 176.004 166.370  1.00166.11           C  
ATOM   4516  CD  ARG C  44     181.811 175.500 165.236  1.00166.11           C  
ATOM   4517  NE  ARG C  44     182.684 174.391 165.625  1.00166.11           N  
ATOM   4518  CZ  ARG C  44     182.374 173.100 165.519  1.00166.11           C  
ATOM   4519  NH1 ARG C  44     183.243 172.177 165.905  1.00166.11           N  
ATOM   4520  NH2 ARG C  44     181.207 172.728 165.009  1.00166.11           N  
ATOM   4521  N   LYS C  45     177.163 176.518 167.014  1.00164.18           N  
ATOM   4522  CA  LYS C  45     176.329 177.686 166.750  1.00164.18           C  
ATOM   4523  C   LYS C  45     175.864 178.333 168.047  1.00164.18           C  
ATOM   4524  O   LYS C  45     175.666 179.551 168.101  1.00164.18           O  
ATOM   4525  CB  LYS C  45     175.131 177.290 165.891  1.00164.18           C  
ATOM   4526  CG  LYS C  45     174.493 178.443 165.138  1.00164.18           C  
ATOM   4527  CD  LYS C  45     172.981 178.287 165.083  1.00164.18           C  
ATOM   4528  CE  LYS C  45     172.574 176.947 164.483  1.00164.18           C  
ATOM   4529  NZ  LYS C  45     171.156 176.954 164.029  1.00164.18           N  
ATOM   4530  N   VAL C  46     175.666 177.530 169.091  1.00162.01           N  
ATOM   4531  CA  VAL C  46     175.403 178.072 170.421  1.00162.01           C  
ATOM   4532  C   VAL C  46     176.652 178.748 170.975  1.00162.01           C  
ATOM   4533  O   VAL C  46     176.571 179.795 171.626  1.00162.01           O  
ATOM   4534  CB  VAL C  46     174.894 176.959 171.355  1.00162.01           C  
ATOM   4535  CG1 VAL C  46     174.849 177.439 172.798  1.00162.01           C  
ATOM   4536  CG2 VAL C  46     173.521 176.483 170.907  1.00162.01           C  
ATOM   4537  N   ILE C  47     177.824 178.159 170.722  1.00160.21           N  
ATOM   4538  CA  ILE C  47     179.084 178.780 171.139  1.00160.21           C  
ATOM   4539  C   ILE C  47     179.175 180.195 170.598  1.00160.21           C  
ATOM   4540  O   ILE C  47     179.470 181.145 171.330  1.00160.21           O  
ATOM   4541  CB  ILE C  47     180.290 177.951 170.662  1.00160.21           C  
ATOM   4542  CG1 ILE C  47     180.254 176.535 171.218  1.00160.21           C  
ATOM   4543  CG2 ILE C  47     181.588 178.640 171.047  1.00160.21           C  
ATOM   4544  CD1 ILE C  47     180.307 176.503 172.689  1.00160.21           C  
ATOM   4545  N   LYS C  48     178.909 180.358 169.310  1.00153.71           N  
ATOM   4546  CA  LYS C  48     179.116 181.656 168.688  1.00153.71           C  
ATOM   4547  C   LYS C  48     177.988 182.634 168.975  1.00153.71           C  
ATOM   4548  O   LYS C  48     178.036 183.770 168.489  1.00153.71           O  
ATOM   4549  CB  LYS C  48     179.300 181.486 167.177  1.00153.71           C  
ATOM   4550  CG  LYS C  48     180.077 182.618 166.516  1.00153.71           C  
ATOM   4551  CD  LYS C  48     181.454 182.806 167.150  1.00153.71           C  
ATOM   4552  CE  LYS C  48     182.222 181.491 167.275  1.00153.71           C  
ATOM   4553  NZ  LYS C  48     183.459 181.642 168.090  1.00153.71           N  
ATOM   4554  N   SER C  49     176.994 182.230 169.760  1.00144.76           N  
ATOM   4555  CA  SER C  49     175.842 183.079 170.013  1.00144.76           C  
ATOM   4556  C   SER C  49     176.276 184.425 170.572  1.00144.76           C  
ATOM   4557  O   SER C  49     176.978 184.493 171.583  1.00144.76           O  
ATOM   4558  CB  SER C  49     174.896 182.390 170.990  1.00144.76           C  
ATOM   4559  OG  SER C  49     174.505 181.123 170.502  1.00144.76           O  
ATOM   4560  N   THR C  50     175.855 185.500 169.905  1.00131.96           N  
ATOM   4561  CA  THR C  50     176.058 186.832 170.457  1.00131.96           C  
ATOM   4562  C   THR C  50     175.401 186.956 171.823  1.00131.96           C  
ATOM   4563  O   THR C  50     175.941 187.615 172.725  1.00131.96           O  
ATOM   4564  CB  THR C  50     175.502 187.876 169.494  1.00131.96           C  
ATOM   4565  OG1 THR C  50     176.180 187.766 168.238  1.00131.96           O  
ATOM   4566  CG2 THR C  50     175.695 189.275 170.044  1.00131.96           C  
ATOM   4567  N   PHE C  51     174.242 186.320 171.990  1.00129.23           N  
ATOM   4568  CA  PHE C  51     173.629 186.209 173.305  1.00129.23           C  
ATOM   4569  C   PHE C  51     174.610 185.613 174.304  1.00129.23           C  
ATOM   4570  O   PHE C  51     174.744 186.107 175.426  1.00129.23           O  
ATOM   4571  CB  PHE C  51     172.360 185.361 173.203  1.00129.23           C  
ATOM   4572  CG  PHE C  51     171.822 184.895 174.524  1.00129.23           C  
ATOM   4573  CD1 PHE C  51     170.982 185.704 175.266  1.00129.23           C  
ATOM   4574  CD2 PHE C  51     172.139 183.639 175.015  1.00129.23           C  
ATOM   4575  CE1 PHE C  51     170.478 185.277 176.479  1.00129.23           C  
ATOM   4576  CE2 PHE C  51     171.641 183.208 176.227  1.00129.23           C  
ATOM   4577  CZ  PHE C  51     170.809 184.028 176.959  1.00129.23           C  
ATOM   4578  N   PHE C  52     175.320 184.557 173.906  1.00129.73           N  
ATOM   4579  CA  PHE C  52     176.289 183.939 174.803  1.00129.73           C  
ATOM   4580  C   PHE C  52     177.440 184.885 175.115  1.00129.73           C  
ATOM   4581  O   PHE C  52     177.928 184.928 176.251  1.00129.73           O  
ATOM   4582  CB  PHE C  52     176.815 182.645 174.193  1.00129.73           C  
ATOM   4583  CG  PHE C  52     177.882 181.987 175.006  1.00129.73           C  
ATOM   4584  CD1 PHE C  52     177.671 181.697 176.339  1.00129.73           C  
ATOM   4585  CD2 PHE C  52     179.101 181.667 174.441  1.00129.73           C  
ATOM   4586  CE1 PHE C  52     178.649 181.094 177.088  1.00129.73           C  
ATOM   4587  CE2 PHE C  52     180.085 181.064 175.188  1.00129.73           C  
ATOM   4588  CZ  PHE C  52     179.857 180.778 176.513  1.00129.73           C  
ATOM   4589  N   GLN C  53     177.897 185.640 174.116  1.00124.24           N  
ATOM   4590  CA  GLN C  53     178.937 186.634 174.357  1.00124.24           C  
ATOM   4591  C   GLN C  53     178.513 187.605 175.445  1.00124.24           C  
ATOM   4592  O   GLN C  53     179.231 187.807 176.434  1.00124.24           O  
ATOM   4593  CB  GLN C  53     179.249 187.397 173.068  1.00124.24           C  
ATOM   4594  CG  GLN C  53     179.859 186.561 171.971  1.00124.24           C  
ATOM   4595  CD  GLN C  53     181.185 185.968 172.372  1.00124.24           C  
ATOM   4596  OE1 GLN C  53     182.191 186.668 172.443  1.00124.24           O  
ATOM   4597  NE2 GLN C  53     181.194 184.672 172.650  1.00124.24           N  
ATOM   4598  N   ILE C  54     177.334 188.208 175.287  1.00120.74           N  
ATOM   4599  CA  ILE C  54     176.932 189.215 176.259  1.00120.74           C  
ATOM   4600  C   ILE C  54     176.621 188.565 177.600  1.00120.74           C  
ATOM   4601  O   ILE C  54     176.803 189.188 178.651  1.00120.74           O  
ATOM   4602  CB  ILE C  54     175.759 190.052 175.721  1.00120.74           C  
ATOM   4603  CG1 ILE C  54     175.524 191.271 176.613  1.00120.74           C  
ATOM   4604  CG2 ILE C  54     174.501 189.222 175.624  1.00120.74           C  
ATOM   4605  CD1 ILE C  54     174.625 192.307 175.991  1.00120.74           C  
ATOM   4606  N   VAL C  55     176.193 187.302 177.598  1.00118.93           N  
ATOM   4607  CA  VAL C  55     175.983 186.588 178.855  1.00118.93           C  
ATOM   4608  C   VAL C  55     177.289 186.472 179.622  1.00118.93           C  
ATOM   4609  O   VAL C  55     177.351 186.754 180.824  1.00118.93           O  
ATOM   4610  CB  VAL C  55     175.368 185.203 178.595  1.00118.93           C  
ATOM   4611  CG1 VAL C  55     175.573 184.313 179.792  1.00118.93           C  
ATOM   4612  CG2 VAL C  55     173.895 185.335 178.319  1.00118.93           C  
ATOM   4613  N   MET C  56     178.357 186.060 178.939  1.00117.31           N  
ATOM   4614  CA  MET C  56     179.630 185.923 179.634  1.00117.31           C  
ATOM   4615  C   MET C  56     180.148 187.275 180.099  1.00117.31           C  
ATOM   4616  O   MET C  56     180.663 187.396 181.218  1.00117.31           O  
ATOM   4617  CB  MET C  56     180.660 185.234 178.749  1.00117.31           C  
ATOM   4618  CG  MET C  56     180.493 183.735 178.677  1.00117.31           C  
ATOM   4619  SD  MET C  56     179.914 182.961 180.197  1.00117.31           S  
ATOM   4620  CE  MET C  56     181.244 183.338 181.332  1.00117.31           C  
ATOM   4621  N   ILE C  57     180.015 188.305 179.264  1.00113.26           N  
ATOM   4622  CA  ILE C  57     180.522 189.620 179.646  1.00113.26           C  
ATOM   4623  C   ILE C  57     179.802 190.129 180.888  1.00113.26           C  
ATOM   4624  O   ILE C  57     180.431 190.608 181.840  1.00113.26           O  
ATOM   4625  CB  ILE C  57     180.401 190.609 178.476  1.00113.26           C  
ATOM   4626  CG1 ILE C  57     181.183 190.098 177.271  1.00113.26           C  
ATOM   4627  CG2 ILE C  57     180.925 191.971 178.875  1.00113.26           C  
ATOM   4628  CD1 ILE C  57     180.987 190.932 176.028  1.00113.26           C  
ATOM   4629  N   THR C  58     178.473 190.017 180.911  1.00111.94           N  
ATOM   4630  CA  THR C  58     177.726 190.486 182.073  1.00111.94           C  
ATOM   4631  C   THR C  58     178.005 189.629 183.303  1.00111.94           C  
ATOM   4632  O   THR C  58     178.090 190.152 184.420  1.00111.94           O  
ATOM   4633  CB  THR C  58     176.234 190.527 181.757  1.00111.94           C  
ATOM   4634  OG1 THR C  58     175.967 191.652 180.912  1.00111.94           O  
ATOM   4635  CG2 THR C  58     175.412 190.652 183.026  1.00111.94           C  
ATOM   4636  N   THR C  59     178.175 188.319 183.125  1.00112.64           N  
ATOM   4637  CA  THR C  59     178.526 187.473 184.259  1.00112.64           C  
ATOM   4638  C   THR C  59     179.825 187.936 184.902  1.00112.64           C  
ATOM   4639  O   THR C  59     179.891 188.145 186.119  1.00112.64           O  
ATOM   4640  CB  THR C  59     178.649 186.022 183.811  1.00112.64           C  
ATOM   4641  OG1 THR C  59     177.517 185.675 183.008  1.00112.64           O  
ATOM   4642  CG2 THR C  59     178.704 185.111 185.011  1.00112.64           C  
ATOM   4643  N   VAL C  60     180.865 188.130 184.092  1.00108.83           N  
ATOM   4644  CA  VAL C  60     182.155 188.520 184.647  1.00108.83           C  
ATOM   4645  C   VAL C  60     182.078 189.905 185.275  1.00108.83           C  
ATOM   4646  O   VAL C  60     182.655 190.148 186.343  1.00108.83           O  
ATOM   4647  CB  VAL C  60     183.252 188.442 183.574  1.00108.83           C  
ATOM   4648  CG1 VAL C  60     184.588 188.726 184.195  1.00108.83           C  
ATOM   4649  CG2 VAL C  60     183.277 187.072 182.950  1.00108.83           C  
ATOM   4650  N   THR C  61     181.378 190.840 184.633  1.00104.04           N  
ATOM   4651  CA  THR C  61     181.303 192.183 185.195  1.00104.04           C  
ATOM   4652  C   THR C  61     180.576 192.185 186.535  1.00104.04           C  
ATOM   4653  O   THR C  61     181.008 192.853 187.484  1.00104.04           O  
ATOM   4654  CB  THR C  61     180.624 193.126 184.211  1.00104.04           C  
ATOM   4655  OG1 THR C  61     181.327 193.088 182.968  1.00104.04           O  
ATOM   4656  CG2 THR C  61     180.648 194.537 184.734  1.00104.04           C  
ATOM   4657  N   THR C  62     179.476 191.441 186.642  1.00106.43           N  
ATOM   4658  CA  THR C  62     178.777 191.381 187.920  1.00106.43           C  
ATOM   4659  C   THR C  62     179.629 190.700 188.978  1.00106.43           C  
ATOM   4660  O   THR C  62     179.593 191.085 190.153  1.00106.43           O  
ATOM   4661  CB  THR C  62     177.441 190.660 187.763  1.00106.43           C  
ATOM   4662  OG1 THR C  62     177.662 189.362 187.200  1.00106.43           O  
ATOM   4663  CG2 THR C  62     176.507 191.453 186.863  1.00106.43           C  
ATOM   4664  N   ASN C  63     180.404 189.688 188.586  1.00106.14           N  
ATOM   4665  CA  ASN C  63     181.283 189.045 189.552  1.00106.14           C  
ATOM   4666  C   ASN C  63     182.305 190.025 190.096  1.00106.14           C  
ATOM   4667  O   ASN C  63     182.559 190.062 191.305  1.00106.14           O  
ATOM   4668  CB  ASN C  63     181.989 187.855 188.920  1.00106.14           C  
ATOM   4669  CG  ASN C  63     182.955 187.200 189.868  1.00106.14           C  
ATOM   4670  OD1 ASN C  63     184.041 186.777 189.482  1.00106.14           O  
ATOM   4671  ND2 ASN C  63     182.571 187.134 191.132  1.00106.14           N  
ATOM   4672  N   SER C  64     182.900 190.828 189.218  1.00 98.13           N  
ATOM   4673  CA  SER C  64     183.865 191.819 189.675  1.00 98.13           C  
ATOM   4674  C   SER C  64     183.208 192.856 190.577  1.00 98.13           C  
ATOM   4675  O   SER C  64     183.796 193.283 191.578  1.00 98.13           O  
ATOM   4676  CB  SER C  64     184.534 192.489 188.481  1.00 98.13           C  
ATOM   4677  OG  SER C  64     185.225 191.538 187.699  1.00 98.13           O  
ATOM   4678  N   PHE C  65     181.992 193.280 190.239  1.00100.10           N  
ATOM   4679  CA  PHE C  65     181.316 194.261 191.081  1.00100.10           C  
ATOM   4680  C   PHE C  65     181.048 193.712 192.475  1.00100.10           C  
ATOM   4681  O   PHE C  65     181.272 194.399 193.481  1.00100.10           O  
ATOM   4682  CB  PHE C  65     180.013 194.707 190.430  1.00100.10           C  
ATOM   4683  CG  PHE C  65     179.573 196.064 190.863  1.00100.10           C  
ATOM   4684  CD1 PHE C  65     178.836 196.226 192.022  1.00100.10           C  
ATOM   4685  CD2 PHE C  65     179.916 197.183 190.125  1.00100.10           C  
ATOM   4686  CE1 PHE C  65     178.438 197.479 192.430  1.00100.10           C  
ATOM   4687  CE2 PHE C  65     179.523 198.439 190.526  1.00100.10           C  
ATOM   4688  CZ  PHE C  65     178.782 198.589 191.680  1.00100.10           C  
ATOM   4689  N   LEU C  66     180.567 192.476 192.560  1.00103.43           N  
ATOM   4690  CA  LEU C  66     180.318 191.894 193.871  1.00103.43           C  
ATOM   4691  C   LEU C  66     181.617 191.695 194.633  1.00103.43           C  
ATOM   4692  O   LEU C  66     181.664 191.885 195.852  1.00103.43           O  
ATOM   4693  CB  LEU C  66     179.562 190.583 193.725  1.00103.43           C  
ATOM   4694  CG  LEU C  66     178.174 190.812 193.138  1.00103.43           C  
ATOM   4695  CD1 LEU C  66     177.472 189.502 192.953  1.00103.43           C  
ATOM   4696  CD2 LEU C  66     177.364 191.738 194.027  1.00103.43           C  
ATOM   4697  N   LEU C  67     182.688 191.329 193.933  1.00 98.32           N  
ATOM   4698  CA  LEU C  67     183.981 191.226 194.595  1.00 98.32           C  
ATOM   4699  C   LEU C  67     184.382 192.556 195.214  1.00 98.32           C  
ATOM   4700  O   LEU C  67     184.849 192.598 196.356  1.00 98.32           O  
ATOM   4701  CB  LEU C  67     185.042 190.760 193.603  1.00 98.32           C  
ATOM   4702  CG  LEU C  67     186.104 189.880 194.235  1.00 98.32           C  
ATOM   4703  CD1 LEU C  67     185.443 188.622 194.759  1.00 98.32           C  
ATOM   4704  CD2 LEU C  67     187.177 189.550 193.233  1.00 98.32           C  
ATOM   4705  N   VAL C  68     184.194 193.654 194.479  1.00 98.93           N  
ATOM   4706  CA  VAL C  68     184.508 194.972 195.024  1.00 98.93           C  
ATOM   4707  C   VAL C  68     183.678 195.249 196.266  1.00 98.93           C  
ATOM   4708  O   VAL C  68     184.195 195.714 197.288  1.00 98.93           O  
ATOM   4709  CB  VAL C  68     184.286 196.063 193.969  1.00 98.93           C  
ATOM   4710  CG1 VAL C  68     184.511 197.416 194.590  1.00 98.93           C  
ATOM   4711  CG2 VAL C  68     185.228 195.863 192.833  1.00 98.93           C  
ATOM   4712  N   LEU C  69     182.375 194.978 196.196  1.00107.21           N  
ATOM   4713  CA  LEU C  69     181.541 195.218 197.369  1.00107.21           C  
ATOM   4714  C   LEU C  69     181.855 194.266 198.511  1.00107.21           C  
ATOM   4715  O   LEU C  69     181.363 194.478 199.622  1.00107.21           O  
ATOM   4716  CB  LEU C  69     180.062 195.114 197.019  1.00107.21           C  
ATOM   4717  CG  LEU C  69     179.515 196.217 196.118  1.00107.21           C  
ATOM   4718  CD1 LEU C  69     178.019 196.052 195.934  1.00107.21           C  
ATOM   4719  CD2 LEU C  69     179.841 197.586 196.681  1.00107.21           C  
ATOM   4720  N   GLY C  70     182.636 193.223 198.261  1.00111.13           N  
ATOM   4721  CA  GLY C  70     182.964 192.286 199.314  1.00111.13           C  
ATOM   4722  C   GLY C  70     184.054 192.713 200.269  1.00111.13           C  
ATOM   4723  O   GLY C  70     184.296 192.015 201.256  1.00111.13           O  
ATOM   4724  N   THR C  71     184.723 193.832 200.015  1.00111.30           N  
ATOM   4725  CA  THR C  71     185.788 194.292 200.892  1.00111.30           C  
ATOM   4726  C   THR C  71     185.282 195.229 201.971  1.00111.30           C  
ATOM   4727  O   THR C  71     186.069 195.993 202.539  1.00111.30           O  
ATOM   4728  CB  THR C  71     186.891 194.974 200.085  1.00111.30           C  
ATOM   4729  OG1 THR C  71     186.359 196.120 199.413  1.00111.30           O  
ATOM   4730  CG2 THR C  71     187.450 194.016 199.061  1.00111.30           C  
ATOM   4731  N   ASN C  72     183.986 195.195 202.259  1.00126.76           N  
ATOM   4732  CA  ASN C  72     183.395 195.987 203.325  1.00126.76           C  
ATOM   4733  C   ASN C  72     182.553 195.048 204.168  1.00126.76           C  
ATOM   4734  O   ASN C  72     181.573 194.484 203.675  1.00126.76           O  
ATOM   4735  CB  ASN C  72     182.555 197.128 202.756  1.00126.76           C  
ATOM   4736  CG  ASN C  72     181.975 198.016 203.826  1.00126.76           C  
ATOM   4737  OD1 ASN C  72     181.452 197.545 204.833  1.00126.76           O  
ATOM   4738  ND2 ASN C  72     182.062 199.321 203.610  1.00126.76           N  
ATOM   4739  N   TYR C  73     182.932 194.881 205.434  1.00129.16           N  
ATOM   4740  CA  TYR C  73     182.248 193.912 206.281  1.00129.16           C  
ATOM   4741  C   TYR C  73     180.796 194.289 206.531  1.00129.16           C  
ATOM   4742  O   TYR C  73     179.959 193.407 206.740  1.00129.16           O  
ATOM   4743  CB  TYR C  73     182.975 193.757 207.610  1.00129.16           C  
ATOM   4744  CG  TYR C  73     182.206 192.914 208.593  1.00129.16           C  
ATOM   4745  CD1 TYR C  73     182.063 191.553 208.405  1.00129.16           C  
ATOM   4746  CD2 TYR C  73     181.598 193.489 209.693  1.00129.16           C  
ATOM   4747  CE1 TYR C  73     181.358 190.791 209.293  1.00129.16           C  
ATOM   4748  CE2 TYR C  73     180.889 192.734 210.584  1.00129.16           C  
ATOM   4749  CZ  TYR C  73     180.772 191.388 210.381  1.00129.16           C  
ATOM   4750  OH  TYR C  73     180.060 190.632 211.279  1.00129.16           O  
ATOM   4751  N   ASP C  74     180.475 195.581 206.524  1.00137.65           N  
ATOM   4752  CA  ASP C  74     179.088 195.987 206.714  1.00137.65           C  
ATOM   4753  C   ASP C  74     178.208 195.457 205.588  1.00137.65           C  
ATOM   4754  O   ASP C  74     177.188 194.802 205.832  1.00137.65           O  
ATOM   4755  CB  ASP C  74     179.006 197.510 206.799  1.00137.65           C  
ATOM   4756  CG  ASP C  74     179.841 198.070 207.930  1.00137.65           C  
ATOM   4757  OD1 ASP C  74     180.066 197.334 208.915  1.00137.65           O  
ATOM   4758  OD2 ASP C  74     180.273 199.240 207.838  1.00137.65           O  
ATOM   4759  N   ILE C  75     178.604 195.717 204.341  1.00139.95           N  
ATOM   4760  CA  ILE C  75     177.847 195.230 203.196  1.00139.95           C  
ATOM   4761  C   ILE C  75     178.061 193.737 203.010  1.00139.95           C  
ATOM   4762  O   ILE C  75     177.224 193.051 202.420  1.00139.95           O  
ATOM   4763  CB  ILE C  75     178.233 196.029 201.940  1.00139.95           C  
ATOM   4764  CG1 ILE C  75     177.918 197.501 202.157  1.00139.95           C  
ATOM   4765  CG2 ILE C  75     177.466 195.547 200.729  1.00139.95           C  
ATOM   4766  CD1 ILE C  75     176.461 197.756 202.413  1.00139.95           C  
ATOM   4767  N   GLN C  76     179.180 193.202 203.483  1.00137.81           N  
ATOM   4768  CA  GLN C  76     179.310 191.753 203.498  1.00137.81           C  
ATOM   4769  C   GLN C  76     178.313 191.120 204.450  1.00137.81           C  
ATOM   4770  O   GLN C  76     177.925 189.963 204.264  1.00137.81           O  
ATOM   4771  CB  GLN C  76     180.731 191.353 203.869  1.00137.81           C  
ATOM   4772  CG  GLN C  76     181.024 189.898 203.617  1.00137.81           C  
ATOM   4773  CD  GLN C  76     181.412 189.620 202.198  1.00137.81           C  
ATOM   4774  OE1 GLN C  76     181.984 190.470 201.525  1.00137.81           O  
ATOM   4775  NE2 GLN C  76     181.109 188.415 201.728  1.00137.81           N  
ATOM   4776  N   PHE C  77     177.926 191.842 205.518  1.00143.08           N  
ATOM   4777  CA  PHE C  77     176.979 191.276 206.526  1.00143.08           C  
ATOM   4778  C   PHE C  77     175.534 191.414 206.031  1.00143.08           C  
ATOM   4779  O   PHE C  77     174.892 190.374 205.783  1.00143.08           O  
ATOM   4780  CB  PHE C  77     177.171 191.957 207.884  1.00143.08           C  
ATOM   4781  CG  PHE C  77     176.265 191.450 208.978  1.00143.08           C  
ATOM   4782  CD1 PHE C  77     176.657 190.402 209.795  1.00143.08           C  
ATOM   4783  CD2 PHE C  77     175.020 192.019 209.191  1.00143.08           C  
ATOM   4784  CE1 PHE C  77     175.825 189.936 210.801  1.00143.08           C  
ATOM   4785  CE2 PHE C  77     174.189 191.552 210.196  1.00143.08           C  
ATOM   4786  CZ  PHE C  77     174.592 190.512 211.000  1.00143.08           C  
ATOM   4787  N   GLU C  78     175.057 192.650 205.847  1.00149.48           N  
ATOM   4788  CA  GLU C  78     173.763 192.873 205.227  1.00149.48           C  
ATOM   4789  C   GLU C  78     173.858 192.465 203.767  1.00149.48           C  
ATOM   4790  O   GLU C  78     174.758 192.917 203.061  1.00149.48           O  
ATOM   4791  CB  GLU C  78     173.374 194.343 205.355  1.00149.48           C  
ATOM   4792  CG  GLU C  78     172.066 194.728 204.701  1.00149.48           C  
ATOM   4793  CD  GLU C  78     171.751 196.202 204.893  1.00149.48           C  
ATOM   4794  OE1 GLU C  78     172.627 196.927 205.409  1.00149.48           O  
ATOM   4795  OE2 GLU C  78     170.630 196.635 204.548  1.00149.48           O  
ATOM   4796  N   PHE C  79     172.934 191.613 203.323  1.00149.90           N  
ATOM   4797  CA  PHE C  79     172.934 191.032 201.981  1.00149.90           C  
ATOM   4798  C   PHE C  79     173.965 189.924 201.832  1.00149.90           C  
ATOM   4799  O   PHE C  79     174.534 189.758 200.752  1.00149.90           O  
ATOM   4800  CB  PHE C  79     173.198 192.091 200.907  1.00149.90           C  
ATOM   4801  CG  PHE C  79     172.098 193.087 200.749  1.00149.90           C  
ATOM   4802  CD1 PHE C  79     170.847 192.857 201.294  1.00149.90           C  
ATOM   4803  CD2 PHE C  79     172.321 194.267 200.067  1.00149.90           C  
ATOM   4804  CE1 PHE C  79     169.837 193.780 201.148  1.00149.90           C  
ATOM   4805  CE2 PHE C  79     171.317 195.192 199.919  1.00149.90           C  
ATOM   4806  CZ  PHE C  79     170.072 194.950 200.459  1.00149.90           C  
ATOM   4807  N   PHE C  80     174.234 189.168 202.895  1.00148.59           N  
ATOM   4808  CA  PHE C  80     175.188 188.070 202.773  1.00148.59           C  
ATOM   4809  C   PHE C  80     174.641 186.953 201.893  1.00148.59           C  
ATOM   4810  O   PHE C  80     175.385 186.341 201.114  1.00148.59           O  
ATOM   4811  CB  PHE C  80     175.556 187.532 204.151  1.00148.59           C  
ATOM   4812  CG  PHE C  80     176.334 186.257 204.105  1.00148.59           C  
ATOM   4813  CD1 PHE C  80     177.581 186.217 203.519  1.00148.59           C  
ATOM   4814  CD2 PHE C  80     175.825 185.099 204.653  1.00148.59           C  
ATOM   4815  CE1 PHE C  80     178.299 185.048 203.474  1.00148.59           C  
ATOM   4816  CE2 PHE C  80     176.544 183.928 204.609  1.00148.59           C  
ATOM   4817  CZ  PHE C  80     177.781 183.904 204.020  1.00148.59           C  
ATOM   4818  N   ARG C  81     173.343 186.666 202.009  1.00150.36           N  
ATOM   4819  CA  ARG C  81     172.739 185.623 201.188  1.00150.36           C  
ATOM   4820  C   ARG C  81     172.844 185.969 199.710  1.00150.36           C  
ATOM   4821  O   ARG C  81     173.020 185.082 198.863  1.00150.36           O  
ATOM   4822  CB  ARG C  81     171.282 185.425 201.597  1.00150.36           C  
ATOM   4823  CG  ARG C  81     171.077 185.357 203.099  1.00150.36           C  
ATOM   4824  CD  ARG C  81     171.435 183.990 203.651  1.00150.36           C  
ATOM   4825  NE  ARG C  81     170.302 183.071 203.660  1.00150.36           N  
ATOM   4826  CZ  ARG C  81     170.343 181.834 203.176  1.00150.36           C  
ATOM   4827  NH1 ARG C  81     169.267 181.061 203.227  1.00150.36           N  
ATOM   4828  NH2 ARG C  81     171.460 181.368 202.638  1.00150.36           N  
ATOM   4829  N   THR C  82     172.733 187.259 199.385  1.00148.66           N  
ATOM   4830  CA  THR C  82     172.986 187.721 198.025  1.00148.66           C  
ATOM   4831  C   THR C  82     174.370 187.299 197.558  1.00148.66           C  
ATOM   4832  O   THR C  82     174.524 186.716 196.478  1.00148.66           O  
ATOM   4833  CB  THR C  82     172.843 189.243 197.962  1.00148.66           C  
ATOM   4834  OG1 THR C  82     171.513 189.621 198.338  1.00148.66           O  
ATOM   4835  CG2 THR C  82     173.147 189.760 196.575  1.00148.66           C  
ATOM   4836  N   PHE C  83     175.387 187.564 198.380  1.00141.54           N  
ATOM   4837  CA  PHE C  83     176.756 187.218 198.020  1.00141.54           C  
ATOM   4838  C   PHE C  83     176.906 185.718 197.812  1.00141.54           C  
ATOM   4839  O   PHE C  83     177.546 185.274 196.853  1.00141.54           O  
ATOM   4840  CB  PHE C  83     177.718 187.702 199.102  1.00141.54           C  
ATOM   4841  CG  PHE C  83     178.124 189.131 198.954  1.00141.54           C  
ATOM   4842  CD1 PHE C  83     177.321 190.144 199.435  1.00141.54           C  
ATOM   4843  CD2 PHE C  83     179.316 189.464 198.340  1.00141.54           C  
ATOM   4844  CE1 PHE C  83     177.697 191.459 199.301  1.00141.54           C  
ATOM   4845  CE2 PHE C  83     179.696 190.776 198.207  1.00141.54           C  
ATOM   4846  CZ  PHE C  83     178.887 191.775 198.685  1.00141.54           C  
ATOM   4847  N   GLU C  84     176.317 184.919 198.700  1.00150.38           N  
ATOM   4848  CA  GLU C  84     176.467 183.472 198.585  1.00150.38           C  
ATOM   4849  C   GLU C  84     175.823 182.942 197.309  1.00150.38           C  
ATOM   4850  O   GLU C  84     176.452 182.204 196.530  1.00150.38           O  
ATOM   4851  CB  GLU C  84     175.866 182.782 199.804  1.00150.38           C  
ATOM   4852  CG  GLU C  84     175.651 181.309 199.568  1.00150.38           C  
ATOM   4853  CD  GLU C  84     175.599 180.513 200.841  1.00150.38           C  
ATOM   4854  OE1 GLU C  84     175.633 179.271 200.747  1.00150.38           O  
ATOM   4855  OE2 GLU C  84     175.523 181.121 201.927  1.00150.38           O  
ATOM   4856  N   VAL C  85     174.556 183.297 197.086  1.00146.66           N  
ATOM   4857  CA  VAL C  85     173.853 182.808 195.908  1.00146.66           C  
ATOM   4858  C   VAL C  85     174.568 183.259 194.645  1.00146.66           C  
ATOM   4859  O   VAL C  85     174.720 182.488 193.690  1.00146.66           O  
ATOM   4860  CB  VAL C  85     172.387 183.276 195.931  1.00146.66           C  
ATOM   4861  CG1 VAL C  85     171.782 183.205 194.542  1.00146.66           C  
ATOM   4862  CG2 VAL C  85     171.588 182.437 196.908  1.00146.66           C  
ATOM   4863  N   SER C  86     175.036 184.506 194.626  1.00140.78           N  
ATOM   4864  CA  SER C  86     175.710 185.016 193.442  1.00140.78           C  
ATOM   4865  C   SER C  86     177.029 184.302 193.193  1.00140.78           C  
ATOM   4866  O   SER C  86     177.360 183.998 192.044  1.00140.78           O  
ATOM   4867  CB  SER C  86     175.922 186.514 193.586  1.00140.78           C  
ATOM   4868  OG  SER C  86     174.733 187.136 194.037  1.00140.78           O  
ATOM   4869  N   GLU C  87     177.803 184.030 194.243  1.00138.45           N  
ATOM   4870  CA  GLU C  87     179.066 183.333 194.034  1.00138.45           C  
ATOM   4871  C   GLU C  87     178.830 181.941 193.462  1.00138.45           C  
ATOM   4872  O   GLU C  87     179.532 181.513 192.533  1.00138.45           O  
ATOM   4873  CB  GLU C  87     179.865 183.264 195.340  1.00138.45           C  
ATOM   4874  CG  GLU C  87     180.719 184.510 195.618  1.00138.45           C  
ATOM   4875  CD  GLU C  87     181.868 184.258 196.593  1.00138.45           C  
ATOM   4876  OE1 GLU C  87     182.033 185.048 197.548  1.00138.45           O  
ATOM   4877  OE2 GLU C  87     182.615 183.277 196.399  1.00138.45           O  
ATOM   4878  N   LEU C  88     177.833 181.225 193.986  1.00139.74           N  
ATOM   4879  CA  LEU C  88     177.576 179.887 193.457  1.00139.74           C  
ATOM   4880  C   LEU C  88     177.041 179.949 192.026  1.00139.74           C  
ATOM   4881  O   LEU C  88     177.404 179.119 191.180  1.00139.74           O  
ATOM   4882  CB  LEU C  88     176.638 179.124 194.393  1.00139.74           C  
ATOM   4883  CG  LEU C  88     175.222 179.609 194.700  1.00139.74           C  
ATOM   4884  CD1 LEU C  88     174.224 179.185 193.627  1.00139.74           C  
ATOM   4885  CD2 LEU C  88     174.789 179.110 196.069  1.00139.74           C  
ATOM   4886  N   PHE C  89     176.211 180.947 191.725  1.00135.67           N  
ATOM   4887  CA  PHE C  89     175.747 181.144 190.357  1.00135.67           C  
ATOM   4888  C   PHE C  89     176.923 181.370 189.410  1.00135.67           C  
ATOM   4889  O   PHE C  89     176.997 180.762 188.333  1.00135.67           O  
ATOM   4890  CB  PHE C  89     174.778 182.329 190.334  1.00135.67           C  
ATOM   4891  CG  PHE C  89     174.530 182.912 188.973  1.00135.67           C  
ATOM   4892  CD1 PHE C  89     174.216 182.106 187.893  1.00135.67           C  
ATOM   4893  CD2 PHE C  89     174.619 184.281 188.775  1.00135.67           C  
ATOM   4894  CE1 PHE C  89     173.978 182.661 186.648  1.00135.67           C  
ATOM   4895  CE2 PHE C  89     174.392 184.838 187.530  1.00135.67           C  
ATOM   4896  CZ  PHE C  89     174.075 184.026 186.465  1.00135.67           C  
ATOM   4897  N   PHE C  90     177.868 182.218 189.812  1.00127.00           N  
ATOM   4898  CA  PHE C  90     178.994 182.534 188.945  1.00127.00           C  
ATOM   4899  C   PHE C  90     179.882 181.320 188.712  1.00127.00           C  
ATOM   4900  O   PHE C  90     180.312 181.066 187.577  1.00127.00           O  
ATOM   4901  CB  PHE C  90     179.802 183.680 189.546  1.00127.00           C  
ATOM   4902  CG  PHE C  90     179.071 184.983 189.568  1.00127.00           C  
ATOM   4903  CD1 PHE C  90     178.153 185.288 188.589  1.00127.00           C  
ATOM   4904  CD2 PHE C  90     179.302 185.901 190.567  1.00127.00           C  
ATOM   4905  CE1 PHE C  90     177.482 186.478 188.606  1.00127.00           C  
ATOM   4906  CE2 PHE C  90     178.629 187.087 190.588  1.00127.00           C  
ATOM   4907  CZ  PHE C  90     177.720 187.379 189.605  1.00127.00           C  
ATOM   4908  N   VAL C  91     180.195 180.569 189.772  1.00133.77           N  
ATOM   4909  CA  VAL C  91     181.040 179.394 189.576  1.00133.77           C  
ATOM   4910  C   VAL C  91     180.343 178.396 188.665  1.00133.77           C  
ATOM   4911  O   VAL C  91     180.975 177.783 187.790  1.00133.77           O  
ATOM   4912  CB  VAL C  91     181.447 178.761 190.923  1.00133.77           C  
ATOM   4913  CG1 VAL C  91     180.248 178.346 191.727  1.00133.77           C  
ATOM   4914  CG2 VAL C  91     182.320 177.544 190.683  1.00133.77           C  
ATOM   4915  N   SER C  92     179.024 178.242 188.826  1.00136.76           N  
ATOM   4916  CA  SER C  92     178.288 177.352 187.940  1.00136.76           C  
ATOM   4917  C   SER C  92     178.413 177.798 186.490  1.00136.76           C  
ATOM   4918  O   SER C  92     178.639 176.974 185.595  1.00136.76           O  
ATOM   4919  CB  SER C  92     176.825 177.291 188.369  1.00136.76           C  
ATOM   4920  OG  SER C  92     176.257 178.584 188.382  1.00136.76           O  
ATOM   4921  N   VAL C  93     178.292 179.102 186.238  1.00130.92           N  
ATOM   4922  CA  VAL C  93     178.352 179.584 184.860  1.00130.92           C  
ATOM   4923  C   VAL C  93     179.721 179.313 184.253  1.00130.92           C  
ATOM   4924  O   VAL C  93     179.832 178.803 183.133  1.00130.92           O  
ATOM   4925  CB  VAL C  93     177.996 181.076 184.790  1.00130.92           C  
ATOM   4926  CG1 VAL C  93     178.248 181.594 183.401  1.00130.92           C  
ATOM   4927  CG2 VAL C  93     176.565 181.262 185.143  1.00130.92           C  
ATOM   4928  N   TYR C  94     180.785 179.659 184.976  1.00128.45           N  
ATOM   4929  CA  TYR C  94     182.120 179.480 184.408  1.00128.45           C  
ATOM   4930  C   TYR C  94     182.412 178.011 184.144  1.00128.45           C  
ATOM   4931  O   TYR C  94     182.988 177.662 183.104  1.00128.45           O  
ATOM   4932  CB  TYR C  94     183.189 180.069 185.324  1.00128.45           C  
ATOM   4933  CG  TYR C  94     182.888 181.450 185.836  1.00128.45           C  
ATOM   4934  CD1 TYR C  94     182.219 182.372 185.055  1.00128.45           C  
ATOM   4935  CD2 TYR C  94     183.264 181.823 187.113  1.00128.45           C  
ATOM   4936  CE1 TYR C  94     181.944 183.628 185.532  1.00128.45           C  
ATOM   4937  CE2 TYR C  94     182.993 183.074 187.598  1.00128.45           C  
ATOM   4938  CZ  TYR C  94     182.331 183.972 186.808  1.00128.45           C  
ATOM   4939  OH  TYR C  94     182.062 185.223 187.301  1.00128.45           O  
ATOM   4940  N   VAL C  95     182.018 177.129 185.068  1.00139.43           N  
ATOM   4941  CA  VAL C  95     182.327 175.717 184.871  1.00139.43           C  
ATOM   4942  C   VAL C  95     181.506 175.143 183.727  1.00139.43           C  
ATOM   4943  O   VAL C  95     182.002 174.317 182.953  1.00139.43           O  
ATOM   4944  CB  VAL C  95     182.139 174.914 186.170  1.00139.43           C  
ATOM   4945  CG1 VAL C  95     180.692 174.900 186.605  1.00139.43           C  
ATOM   4946  CG2 VAL C  95     182.653 173.498 185.979  1.00139.43           C  
ATOM   4947  N   CYS C  96     180.244 175.563 183.589  1.00142.89           N  
ATOM   4948  CA  CYS C  96     179.457 175.057 182.471  1.00142.89           C  
ATOM   4949  C   CYS C  96     180.034 175.540 181.151  1.00142.89           C  
ATOM   4950  O   CYS C  96     180.104 174.775 180.182  1.00142.89           O  
ATOM   4951  CB  CYS C  96     177.992 175.468 182.609  1.00142.89           C  
ATOM   4952  SG  CYS C  96     177.598 177.120 182.031  1.00142.89           S  
ATOM   4953  N   GLU C  97     180.475 176.799 181.104  1.00140.95           N  
ATOM   4954  CA  GLU C  97     181.128 177.306 179.904  1.00140.95           C  
ATOM   4955  C   GLU C  97     182.337 176.457 179.548  1.00140.95           C  
ATOM   4956  O   GLU C  97     182.495 176.040 178.397  1.00140.95           O  
ATOM   4957  CB  GLU C  97     181.548 178.762 180.095  1.00140.95           C  
ATOM   4958  CG  GLU C  97     182.062 179.416 178.831  1.00140.95           C  
ATOM   4959  CD  GLU C  97     182.903 180.650 179.100  1.00140.95           C  
ATOM   4960  OE1 GLU C  97     183.315 180.850 180.259  1.00140.95           O  
ATOM   4961  OE2 GLU C  97     183.150 181.425 178.156  1.00140.95           O  
ATOM   4962  N   PHE C  98     183.196 176.175 180.529  1.00148.94           N  
ATOM   4963  CA  PHE C  98     184.383 175.375 180.241  1.00148.94           C  
ATOM   4964  C   PHE C  98     184.008 173.984 179.752  1.00148.94           C  
ATOM   4965  O   PHE C  98     184.542 173.498 178.746  1.00148.94           O  
ATOM   4966  CB  PHE C  98     185.274 175.262 181.474  1.00148.94           C  
ATOM   4967  CG  PHE C  98     186.317 174.188 181.358  1.00148.94           C  
ATOM   4968  CD1 PHE C  98     187.253 174.222 180.340  1.00148.94           C  
ATOM   4969  CD2 PHE C  98     186.350 173.135 182.253  1.00148.94           C  
ATOM   4970  CE1 PHE C  98     188.212 173.233 180.226  1.00148.94           C  
ATOM   4971  CE2 PHE C  98     187.307 172.144 182.143  1.00148.94           C  
ATOM   4972  CZ  PHE C  98     188.238 172.192 181.129  1.00148.94           C  
ATOM   4973  N   LEU C  99     183.088 173.326 180.459  1.00153.76           N  
ATOM   4974  CA  LEU C  99     182.761 171.941 180.141  1.00153.76           C  
ATOM   4975  C   LEU C  99     182.156 171.825 178.752  1.00153.76           C  
ATOM   4976  O   LEU C  99     182.564 170.979 177.953  1.00153.76           O  
ATOM   4977  CB  LEU C  99     181.810 171.371 181.191  1.00153.76           C  
ATOM   4978  CG  LEU C  99     182.479 170.955 182.498  1.00153.76           C  
ATOM   4979  CD1 LEU C  99     181.527 170.120 183.329  1.00153.76           C  
ATOM   4980  CD2 LEU C  99     183.766 170.203 182.229  1.00153.76           C  
ATOM   4981  N   MET C 100     181.200 172.685 178.430  1.00155.15           N  
ATOM   4982  CA  MET C 100     180.575 172.580 177.122  1.00155.15           C  
ATOM   4983  C   MET C 100     181.481 173.093 176.003  1.00155.15           C  
ATOM   4984  O   MET C 100     181.429 172.570 174.880  1.00155.15           O  
ATOM   4985  CB  MET C 100     179.216 173.281 177.171  1.00155.15           C  
ATOM   4986  CG  MET C 100     179.243 174.785 177.266  1.00155.15           C  
ATOM   4987  SD  MET C 100     179.375 175.596 175.686  1.00155.15           S  
ATOM   4988  CE  MET C 100     177.648 175.714 175.247  1.00155.15           C  
ATOM   4989  N   LYS C 101     182.353 174.063 176.285  1.00153.55           N  
ATOM   4990  CA  LYS C 101     183.245 174.554 175.246  1.00153.55           C  
ATOM   4991  C   LYS C 101     184.368 173.568 174.960  1.00153.55           C  
ATOM   4992  O   LYS C 101     184.974 173.619 173.886  1.00153.55           O  
ATOM   4993  CB  LYS C 101     183.810 175.914 175.647  1.00153.55           C  
ATOM   4994  CG  LYS C 101     184.393 176.704 174.494  1.00153.55           C  
ATOM   4995  CD  LYS C 101     184.887 178.050 174.968  1.00153.55           C  
ATOM   4996  CE  LYS C 101     183.741 178.875 175.514  1.00153.55           C  
ATOM   4997  NZ  LYS C 101     182.733 179.209 174.476  1.00153.55           N  
ATOM   4998  N   VAL C 102     184.684 172.684 175.905  1.00157.66           N  
ATOM   4999  CA  VAL C 102     185.573 171.583 175.550  1.00157.66           C  
ATOM   5000  C   VAL C 102     184.775 170.399 175.019  1.00157.66           C  
ATOM   5001  O   VAL C 102     185.336 169.530 174.339  1.00157.66           O  
ATOM   5002  CB  VAL C 102     186.462 171.163 176.733  1.00157.66           C  
ATOM   5003  CG1 VAL C 102     185.645 170.490 177.826  1.00157.66           C  
ATOM   5004  CG2 VAL C 102     187.614 170.274 176.260  1.00157.66           C  
ATOM   5005  N   TYR C 103     183.474 170.342 175.308  1.00160.23           N  
ATOM   5006  CA  TYR C 103     182.629 169.329 174.690  1.00160.23           C  
ATOM   5007  C   TYR C 103     182.576 169.513 173.182  1.00160.23           C  
ATOM   5008  O   TYR C 103     182.651 168.534 172.432  1.00160.23           O  
ATOM   5009  CB  TYR C 103     181.221 169.380 175.286  1.00160.23           C  
ATOM   5010  CG  TYR C 103     180.195 168.549 174.543  1.00160.23           C  
ATOM   5011  CD1 TYR C 103     179.510 169.060 173.449  1.00160.23           C  
ATOM   5012  CD2 TYR C 103     179.907 167.254 174.946  1.00160.23           C  
ATOM   5013  CE1 TYR C 103     178.582 168.304 172.773  1.00160.23           C  
ATOM   5014  CE2 TYR C 103     178.974 166.490 174.276  1.00160.23           C  
ATOM   5015  CZ  TYR C 103     178.315 167.019 173.191  1.00160.23           C  
ATOM   5016  OH  TYR C 103     177.384 166.259 172.522  1.00160.23           O  
ATOM   5017  N   VAL C 104     182.439 170.758 172.717  1.00160.92           N  
ATOM   5018  CA  VAL C 104     182.369 170.979 171.276  1.00160.92           C  
ATOM   5019  C   VAL C 104     183.650 170.535 170.583  1.00160.92           C  
ATOM   5020  O   VAL C 104     183.640 170.258 169.379  1.00160.92           O  
ATOM   5021  CB  VAL C 104     182.084 172.458 170.952  1.00160.92           C  
ATOM   5022  CG1 VAL C 104     183.247 173.326 171.366  1.00160.92           C  
ATOM   5023  CG2 VAL C 104     181.765 172.647 169.474  1.00160.92           C  
ATOM   5024  N   ASP C 105     184.749 170.430 171.315  1.00160.50           N  
ATOM   5025  CA  ASP C 105     186.047 170.209 170.698  1.00160.50           C  
ATOM   5026  C   ASP C 105     187.003 169.474 171.629  1.00160.50           C  
ATOM   5027  O   ASP C 105     187.406 170.011 172.667  1.00160.50           O  
ATOM   5028  CB  ASP C 105     186.648 171.545 170.276  1.00160.50           C  
ATOM   5029  CG  ASP C 105     187.924 171.380 169.519  1.00160.50           C  
ATOM   5030  OD1 ASP C 105     187.886 170.980 168.340  1.00160.50           O  
ATOM   5031  OD2 ASP C 105     188.974 171.624 170.131  1.00160.50           O  
ATOM   5032  N   PRO C 106     187.405 168.264 171.279  1.00158.19           N  
ATOM   5033  CA  PRO C 106     188.253 167.474 172.178  1.00158.19           C  
ATOM   5034  C   PRO C 106     189.666 168.009 172.341  1.00158.19           C  
ATOM   5035  O   PRO C 106     190.131 168.188 173.469  1.00158.19           O  
ATOM   5036  CB  PRO C 106     188.261 166.093 171.515  1.00158.19           C  
ATOM   5037  CG  PRO C 106     188.026 166.371 170.075  1.00158.19           C  
ATOM   5038  CD  PRO C 106     187.102 167.550 170.028  1.00158.19           C  
ATOM   5039  N   ILE C 107     190.359 168.265 171.233  1.00159.82           N  
ATOM   5040  CA  ILE C 107     191.792 168.505 171.247  1.00159.82           C  
ATOM   5041  C   ILE C 107     192.135 169.970 171.006  1.00159.82           C  
ATOM   5042  O   ILE C 107     192.915 170.552 171.762  1.00159.82           O  
ATOM   5043  CB  ILE C 107     192.513 167.593 170.230  1.00159.82           C  
ATOM   5044  CG1 ILE C 107     194.028 167.789 170.310  1.00159.82           C  
ATOM   5045  CG2 ILE C 107     191.981 167.802 168.820  1.00159.82           C  
ATOM   5046  CD1 ILE C 107     194.634 167.323 171.615  1.00159.82           C  
ATOM   5047  N   THR C 108     191.561 170.590 169.973  1.00158.35           N  
ATOM   5048  CA  THR C 108     191.947 171.948 169.607  1.00158.35           C  
ATOM   5049  C   THR C 108     191.593 172.962 170.687  1.00158.35           C  
ATOM   5050  O   THR C 108     192.083 174.094 170.635  1.00158.35           O  
ATOM   5051  CB  THR C 108     191.290 172.335 168.281  1.00158.35           C  
ATOM   5052  OG1 THR C 108     191.371 171.228 167.378  1.00158.35           O  
ATOM   5053  CG2 THR C 108     191.990 173.521 167.652  1.00158.35           C  
ATOM   5054  N   TYR C 109     190.764 172.585 171.662  1.00152.71           N  
ATOM   5055  CA  TYR C 109     190.468 173.493 172.763  1.00152.71           C  
ATOM   5056  C   TYR C 109     191.742 173.970 173.445  1.00152.71           C  
ATOM   5057  O   TYR C 109     191.839 175.134 173.847  1.00152.71           O  
ATOM   5058  CB  TYR C 109     189.556 172.815 173.779  1.00152.71           C  
ATOM   5059  CG  TYR C 109     189.189 173.726 174.919  1.00152.71           C  
ATOM   5060  CD1 TYR C 109     188.252 174.729 174.752  1.00152.71           C  
ATOM   5061  CD2 TYR C 109     189.804 173.603 176.154  1.00152.71           C  
ATOM   5062  CE1 TYR C 109     187.922 175.572 175.785  1.00152.71           C  
ATOM   5063  CE2 TYR C 109     189.483 174.442 177.194  1.00152.71           C  
ATOM   5064  CZ  TYR C 109     188.540 175.425 177.005  1.00152.71           C  
ATOM   5065  OH  TYR C 109     188.214 176.268 178.043  1.00152.71           O  
ATOM   5066  N   TRP C 110     192.731 173.093 173.576  1.00150.11           N  
ATOM   5067  CA  TRP C 110     193.988 173.461 174.212  1.00150.11           C  
ATOM   5068  C   TRP C 110     194.886 174.297 173.314  1.00150.11           C  
ATOM   5069  O   TRP C 110     195.924 174.776 173.783  1.00150.11           O  
ATOM   5070  CB  TRP C 110     194.751 172.215 174.668  1.00150.11           C  
ATOM   5071  CG  TRP C 110     193.991 171.290 175.570  1.00150.11           C  
ATOM   5072  CD1 TRP C 110     192.656 171.315 175.846  1.00150.11           C  
ATOM   5073  CD2 TRP C 110     194.533 170.194 176.314  1.00150.11           C  
ATOM   5074  NE1 TRP C 110     192.334 170.305 176.718  1.00150.11           N  
ATOM   5075  CE2 TRP C 110     193.469 169.602 177.020  1.00150.11           C  
ATOM   5076  CE3 TRP C 110     195.816 169.656 176.451  1.00150.11           C  
ATOM   5077  CZ2 TRP C 110     193.649 168.498 177.850  1.00150.11           C  
ATOM   5078  CZ3 TRP C 110     195.993 168.561 177.276  1.00150.11           C  
ATOM   5079  CH2 TRP C 110     194.916 167.994 177.966  1.00150.11           C  
ATOM   5080  N   LYS C 111     194.535 174.472 172.040  1.00152.42           N  
ATOM   5081  CA  LYS C 111     195.331 175.344 171.182  1.00152.42           C  
ATOM   5082  C   LYS C 111     195.271 176.784 171.671  1.00152.42           C  
ATOM   5083  O   LYS C 111     196.304 177.449 171.807  1.00152.42           O  
ATOM   5084  CB  LYS C 111     194.852 175.250 169.733  1.00152.42           C  
ATOM   5085  CG  LYS C 111     195.586 174.220 168.893  1.00152.42           C  
ATOM   5086  CD  LYS C 111     197.064 174.539 168.805  1.00152.42           C  
ATOM   5087  CE  LYS C 111     197.845 173.392 168.196  1.00152.42           C  
ATOM   5088  NZ  LYS C 111     199.306 173.519 168.451  1.00152.42           N  
ATOM   5089  N   ASP C 112     194.071 177.273 171.957  1.00148.12           N  
ATOM   5090  CA  ASP C 112     193.893 178.666 172.336  1.00148.12           C  
ATOM   5091  C   ASP C 112     194.586 178.967 173.656  1.00148.12           C  
ATOM   5092  O   ASP C 112     194.489 178.195 174.614  1.00148.12           O  
ATOM   5093  CB  ASP C 112     192.406 178.989 172.434  1.00148.12           C  
ATOM   5094  CG  ASP C 112     192.145 180.452 172.691  1.00148.12           C  
ATOM   5095  OD1 ASP C 112     192.304 181.264 171.760  1.00148.12           O  
ATOM   5096  OD2 ASP C 112     191.771 180.788 173.829  1.00148.12           O  
ATOM   5097  N   GLY C 113     195.302 180.092 173.699  1.00144.00           N  
ATOM   5098  CA  GLY C 113     195.906 180.523 174.949  1.00144.00           C  
ATOM   5099  C   GLY C 113     194.875 180.967 175.966  1.00144.00           C  
ATOM   5100  O   GLY C 113     195.000 180.679 177.160  1.00144.00           O  
ATOM   5101  N   TYR C 114     193.839 181.667 175.511  1.00131.50           N  
ATOM   5102  CA  TYR C 114     192.845 182.171 176.445  1.00131.50           C  
ATOM   5103  C   TYR C 114     192.033 181.036 177.050  1.00131.50           C  
ATOM   5104  O   TYR C 114     191.559 181.155 178.182  1.00131.50           O  
ATOM   5105  CB  TYR C 114     191.943 183.191 175.755  1.00131.50           C  
ATOM   5106  CG  TYR C 114     192.650 184.480 175.398  1.00131.50           C  
ATOM   5107  CD1 TYR C 114     194.007 184.638 175.622  1.00131.50           C  
ATOM   5108  CD2 TYR C 114     191.959 185.541 174.842  1.00131.50           C  
ATOM   5109  CE1 TYR C 114     194.655 185.808 175.297  1.00131.50           C  
ATOM   5110  CE2 TYR C 114     192.599 186.715 174.521  1.00131.50           C  
ATOM   5111  CZ  TYR C 114     193.947 186.841 174.747  1.00131.50           C  
ATOM   5112  OH  TYR C 114     194.593 188.006 174.427  1.00131.50           O  
ATOM   5113  N   ASN C 115     191.885 179.922 176.335  1.00141.10           N  
ATOM   5114  CA  ASN C 115     191.260 178.753 176.941  1.00141.10           C  
ATOM   5115  C   ASN C 115     192.078 178.253 178.123  1.00141.10           C  
ATOM   5116  O   ASN C 115     191.525 177.892 179.171  1.00141.10           O  
ATOM   5117  CB  ASN C 115     191.093 177.645 175.905  1.00141.10           C  
ATOM   5118  CG  ASN C 115     190.048 177.973 174.867  1.00141.10           C  
ATOM   5119  OD1 ASN C 115     189.260 178.900 175.034  1.00141.10           O  
ATOM   5120  ND2 ASN C 115     190.026 177.203 173.789  1.00141.10           N  
ATOM   5121  N   ILE C 116     193.402 178.221 177.968  1.00136.69           N  
ATOM   5122  CA  ILE C 116     194.273 177.833 179.071  1.00136.69           C  
ATOM   5123  C   ILE C 116     194.137 178.816 180.221  1.00136.69           C  
ATOM   5124  O   ILE C 116     194.037 178.422 181.390  1.00136.69           O  
ATOM   5125  CB  ILE C 116     195.726 177.730 178.584  1.00136.69           C  
ATOM   5126  CG1 ILE C 116     195.812 176.700 177.463  1.00136.69           C  
ATOM   5127  CG2 ILE C 116     196.640 177.363 179.726  1.00136.69           C  
ATOM   5128  CD1 ILE C 116     195.398 175.310 177.892  1.00136.69           C  
ATOM   5129  N   LEU C 117     194.122 180.112 179.907  1.00129.37           N  
ATOM   5130  CA  LEU C 117     193.923 181.117 180.943  1.00129.37           C  
ATOM   5131  C   LEU C 117     192.621 180.879 181.692  1.00129.37           C  
ATOM   5132  O   LEU C 117     192.559 181.033 182.915  1.00129.37           O  
ATOM   5133  CB  LEU C 117     193.938 182.509 180.318  1.00129.37           C  
ATOM   5134  CG  LEU C 117     193.921 183.738 181.221  1.00129.37           C  
ATOM   5135  CD1 LEU C 117     194.584 184.884 180.488  1.00129.37           C  
ATOM   5136  CD2 LEU C 117     192.509 184.134 181.617  1.00129.37           C  
ATOM   5137  N   ASP C 118     191.573 180.487 180.977  1.00129.94           N  
ATOM   5138  CA  ASP C 118     190.264 180.394 181.603  1.00129.94           C  
ATOM   5139  C   ASP C 118     190.153 179.141 182.464  1.00129.94           C  
ATOM   5140  O   ASP C 118     189.548 179.168 183.546  1.00129.94           O  
ATOM   5141  CB  ASP C 118     189.189 180.430 180.523  1.00129.94           C  
ATOM   5142  CG  ASP C 118     189.106 181.788 179.842  1.00129.94           C  
ATOM   5143  OD1 ASP C 118     189.425 182.802 180.494  1.00129.94           O  
ATOM   5144  OD2 ASP C 118     188.728 181.846 178.655  1.00129.94           O  
ATOM   5145  N   VAL C 119     190.748 178.035 182.018  1.00129.08           N  
ATOM   5146  CA  VAL C 119     190.758 176.860 182.884  1.00129.08           C  
ATOM   5147  C   VAL C 119     191.641 177.111 184.104  1.00129.08           C  
ATOM   5148  O   VAL C 119     191.353 176.621 185.202  1.00129.08           O  
ATOM   5149  CB  VAL C 119     191.178 175.600 182.103  1.00129.08           C  
ATOM   5150  CG1 VAL C 119     192.506 175.797 181.434  1.00129.08           C  
ATOM   5151  CG2 VAL C 119     191.234 174.399 183.024  1.00129.08           C  
ATOM   5152  N   ILE C 120     192.707 177.900 183.949  1.00126.01           N  
ATOM   5153  CA  ILE C 120     193.503 178.300 185.105  1.00126.01           C  
ATOM   5154  C   ILE C 120     192.662 179.123 186.071  1.00126.01           C  
ATOM   5155  O   ILE C 120     192.757 178.967 187.295  1.00126.01           O  
ATOM   5156  CB  ILE C 120     194.751 179.071 184.643  1.00126.01           C  
ATOM   5157  CG1 ILE C 120     195.801 178.112 184.098  1.00126.01           C  
ATOM   5158  CG2 ILE C 120     195.326 179.880 185.776  1.00126.01           C  
ATOM   5159  CD1 ILE C 120     196.959 178.816 183.444  1.00126.01           C  
ATOM   5160  N   ILE C 121     191.840 180.025 185.537  1.00122.04           N  
ATOM   5161  CA  ILE C 121     190.962 180.823 186.386  1.00122.04           C  
ATOM   5162  C   ILE C 121     190.029 179.919 187.172  1.00122.04           C  
ATOM   5163  O   ILE C 121     189.821 180.110 188.375  1.00122.04           O  
ATOM   5164  CB  ILE C 121     190.173 181.836 185.543  1.00122.04           C  
ATOM   5165  CG1 ILE C 121     191.056 183.021 185.186  1.00122.04           C  
ATOM   5166  CG2 ILE C 121     188.963 182.309 186.304  1.00122.04           C  
ATOM   5167  CD1 ILE C 121     191.444 183.851 186.370  1.00122.04           C  
ATOM   5168  N   LEU C 122     189.455 178.918 186.506  1.00128.32           N  
ATOM   5169  CA  LEU C 122     188.569 177.991 187.204  1.00128.32           C  
ATOM   5170  C   LEU C 122     189.322 177.191 188.267  1.00128.32           C  
ATOM   5171  O   LEU C 122     188.776 176.894 189.336  1.00128.32           O  
ATOM   5172  CB  LEU C 122     187.888 177.068 186.197  1.00128.32           C  
ATOM   5173  CG  LEU C 122     186.830 176.135 186.781  1.00128.32           C  
ATOM   5174  CD1 LEU C 122     185.739 176.936 187.450  1.00128.32           C  
ATOM   5175  CD2 LEU C 122     186.247 175.282 185.683  1.00128.32           C  
ATOM   5176  N   ILE C 123     190.578 176.838 187.997  1.00128.58           N  
ATOM   5177  CA  ILE C 123     191.390 176.142 188.995  1.00128.58           C  
ATOM   5178  C   ILE C 123     191.578 177.013 190.232  1.00128.58           C  
ATOM   5179  O   ILE C 123     191.431 176.554 191.376  1.00128.58           O  
ATOM   5180  CB  ILE C 123     192.745 175.740 188.390  1.00128.58           C  
ATOM   5181  CG1 ILE C 123     192.581 174.563 187.435  1.00128.58           C  
ATOM   5182  CG2 ILE C 123     193.752 175.425 189.479  1.00128.58           C  
ATOM   5183  CD1 ILE C 123     193.851 174.210 186.718  1.00128.58           C  
ATOM   5184  N   ILE C 124     191.935 178.281 190.016  1.00125.08           N  
ATOM   5185  CA  ILE C 124     192.128 179.202 191.132  1.00125.08           C  
ATOM   5186  C   ILE C 124     190.820 179.394 191.881  1.00125.08           C  
ATOM   5187  O   ILE C 124     190.803 179.582 193.101  1.00125.08           O  
ATOM   5188  CB  ILE C 124     192.698 180.541 190.633  1.00125.08           C  
ATOM   5189  CG1 ILE C 124     194.072 180.334 189.991  1.00125.08           C  
ATOM   5190  CG2 ILE C 124     192.792 181.534 191.774  1.00125.08           C  
ATOM   5191  CD1 ILE C 124     195.196 180.111 190.981  1.00125.08           C  
ATOM   5192  N   LEU C 125     189.706 179.362 191.157  1.00127.05           N  
ATOM   5193  CA  LEU C 125     188.401 179.423 191.800  1.00127.05           C  
ATOM   5194  C   LEU C 125     188.168 178.217 192.698  1.00127.05           C  
ATOM   5195  O   LEU C 125     187.613 178.344 193.795  1.00127.05           O  
ATOM   5196  CB  LEU C 125     187.317 179.522 190.732  1.00127.05           C  
ATOM   5197  CG  LEU C 125     185.866 179.397 191.172  1.00127.05           C  
ATOM   5198  CD1 LEU C 125     185.559 180.364 192.298  1.00127.05           C  
ATOM   5199  CD2 LEU C 125     184.989 179.676 189.975  1.00127.05           C  
ATOM   5200  N   THR C 126     188.570 177.035 192.243  1.00133.37           N  
ATOM   5201  CA  THR C 126     188.304 175.832 193.023  1.00133.37           C  
ATOM   5202  C   THR C 126     189.179 175.758 194.269  1.00133.37           C  
ATOM   5203  O   THR C 126     188.724 175.290 195.319  1.00133.37           O  
ATOM   5204  CB  THR C 126     188.505 174.587 192.162  1.00133.37           C  
ATOM   5205  OG1 THR C 126     189.769 174.663 191.491  1.00133.37           O  
ATOM   5206  CG2 THR C 126     187.396 174.477 191.136  1.00133.37           C  
ATOM   5207  N   ILE C 127     190.434 176.214 194.178  1.00136.55           N  
ATOM   5208  CA  ILE C 127     191.413 175.888 195.224  1.00136.55           C  
ATOM   5209  C   ILE C 127     190.986 176.348 196.619  1.00136.55           C  
ATOM   5210  O   ILE C 127     190.967 175.511 197.540  1.00136.55           O  
ATOM   5211  CB  ILE C 127     192.814 176.378 194.814  1.00136.55           C  
ATOM   5212  CG1 ILE C 127     193.880 175.848 195.766  1.00136.55           C  
ATOM   5213  CG2 ILE C 127     192.942 177.882 194.756  1.00136.55           C  
ATOM   5214  CD1 ILE C 127     195.284 176.035 195.244  1.00136.55           C  
ATOM   5215  N   PRO C 128     190.593 177.612 196.849  1.00137.51           N  
ATOM   5216  CA  PRO C 128     190.326 178.010 198.231  1.00137.51           C  
ATOM   5217  C   PRO C 128     189.054 177.403 198.769  1.00137.51           C  
ATOM   5218  O   PRO C 128     188.936 177.235 199.987  1.00137.51           O  
ATOM   5219  CB  PRO C 128     190.222 179.531 198.138  1.00137.51           C  
ATOM   5220  CG  PRO C 128     189.539 179.724 196.871  1.00137.51           C  
ATOM   5221  CD  PRO C 128     190.014 178.617 195.937  1.00137.51           C  
ATOM   5222  N   TYR C 129     188.106 177.047 197.901  1.00149.02           N  
ATOM   5223  CA  TYR C 129     186.931 176.325 198.364  1.00149.02           C  
ATOM   5224  C   TYR C 129     187.315 175.033 199.061  1.00149.02           C  
ATOM   5225  O   TYR C 129     186.871 174.770 200.183  1.00149.02           O  
ATOM   5226  CB  TYR C 129     185.988 176.010 197.210  1.00149.02           C  
ATOM   5227  CG  TYR C 129     184.851 175.167 197.707  1.00149.02           C  
ATOM   5228  CD1 TYR C 129     183.796 175.726 198.413  1.00149.02           C  
ATOM   5229  CD2 TYR C 129     184.883 173.788 197.557  1.00149.02           C  
ATOM   5230  CE1 TYR C 129     182.771 174.930 198.900  1.00149.02           C  
ATOM   5231  CE2 TYR C 129     183.875 172.992 198.043  1.00149.02           C  
ATOM   5232  CZ  TYR C 129     182.822 173.563 198.708  1.00149.02           C  
ATOM   5233  OH  TYR C 129     181.828 172.747 199.181  1.00149.02           O  
ATOM   5234  N   LEU C 130     188.102 174.189 198.395  1.00147.50           N  
ATOM   5235  CA  LEU C 130     188.455 172.922 199.019  1.00147.50           C  
ATOM   5236  C   LEU C 130     189.354 173.150 200.218  1.00147.50           C  
ATOM   5237  O   LEU C 130     189.194 172.476 201.241  1.00147.50           O  
ATOM   5238  CB  LEU C 130     189.100 171.975 198.004  1.00147.50           C  
ATOM   5239  CG  LEU C 130     190.405 172.292 197.277  1.00147.50           C  
ATOM   5240  CD1 LEU C 130     191.615 171.940 198.120  1.00147.50           C  
ATOM   5241  CD2 LEU C 130     190.446 171.544 195.960  1.00147.50           C  
ATOM   5242  N   LEU C 131     190.258 174.132 200.131  1.00148.26           N  
ATOM   5243  CA  LEU C 131     191.077 174.482 201.289  1.00148.26           C  
ATOM   5244  C   LEU C 131     190.208 174.762 202.510  1.00148.26           C  
ATOM   5245  O   LEU C 131     190.442 174.216 203.593  1.00148.26           O  
ATOM   5246  CB  LEU C 131     191.949 175.693 200.956  1.00148.26           C  
ATOM   5247  CG  LEU C 131     192.866 176.276 202.031  1.00148.26           C  
ATOM   5248  CD1 LEU C 131     194.126 176.830 201.394  1.00148.26           C  
ATOM   5249  CD2 LEU C 131     192.169 177.366 202.814  1.00148.26           C  
ATOM   5250  N   ARG C 132     189.188 175.603 202.349  1.00150.17           N  
ATOM   5251  CA  ARG C 132     188.363 175.997 203.482  1.00150.17           C  
ATOM   5252  C   ARG C 132     187.426 174.887 203.928  1.00150.17           C  
ATOM   5253  O   ARG C 132     187.228 174.699 205.132  1.00150.17           O  
ATOM   5254  CB  ARG C 132     187.560 177.250 203.135  1.00150.17           C  
ATOM   5255  CG  ARG C 132     186.701 177.777 204.270  1.00150.17           C  
ATOM   5256  CD  ARG C 132     185.242 177.433 204.064  1.00150.17           C  
ATOM   5257  NE  ARG C 132     184.778 177.846 202.746  1.00150.17           N  
ATOM   5258  CZ  ARG C 132     184.208 179.019 202.496  1.00150.17           C  
ATOM   5259  NH1 ARG C 132     183.815 179.323 201.268  1.00150.17           N  
ATOM   5260  NH2 ARG C 132     184.024 179.888 203.480  1.00150.17           N  
ATOM   5261  N   LYS C 133     186.828 174.155 202.992  1.00152.08           N  
ATOM   5262  CA  LYS C 133     185.850 173.148 203.384  1.00152.08           C  
ATOM   5263  C   LYS C 133     186.529 171.887 203.901  1.00152.08           C  
ATOM   5264  O   LYS C 133     186.392 171.534 205.077  1.00152.08           O  
ATOM   5265  CB  LYS C 133     184.930 172.822 202.208  1.00152.08           C  
ATOM   5266  CG  LYS C 133     183.874 171.779 202.524  1.00152.08           C  
ATOM   5267  CD  LYS C 133     182.857 172.294 203.527  1.00152.08           C  
ATOM   5268  CE  LYS C 133     181.715 171.303 203.718  1.00152.08           C  
ATOM   5269  NZ  LYS C 133     182.159 170.036 204.355  1.00152.08           N  
ATOM   5270  N   ILE C 134     187.293 171.208 203.045  1.00152.62           N  
ATOM   5271  CA  ILE C 134     187.792 169.890 203.412  1.00152.62           C  
ATOM   5272  C   ILE C 134     188.903 170.011 204.446  1.00152.62           C  
ATOM   5273  O   ILE C 134     188.769 169.538 205.580  1.00152.62           O  
ATOM   5274  CB  ILE C 134     188.252 169.126 202.160  1.00152.62           C  
ATOM   5275  CG1 ILE C 134     187.036 168.698 201.340  1.00152.62           C  
ATOM   5276  CG2 ILE C 134     189.065 167.899 202.547  1.00152.62           C  
ATOM   5277  CD1 ILE C 134     185.940 168.070 202.168  1.00152.62           C  
ATOM   5278  N   LYS C 135     190.009 170.656 204.081  1.00149.08           N  
ATOM   5279  CA  LYS C 135     191.102 170.805 205.032  1.00149.08           C  
ATOM   5280  C   LYS C 135     190.722 171.729 206.180  1.00149.08           C  
ATOM   5281  O   LYS C 135     191.182 171.529 207.308  1.00149.08           O  
ATOM   5282  CB  LYS C 135     192.351 171.315 204.317  1.00149.08           C  
ATOM   5283  CG  LYS C 135     193.643 171.109 205.081  1.00149.08           C  
ATOM   5284  CD  LYS C 135     194.820 171.631 204.276  1.00149.08           C  
ATOM   5285  CE  LYS C 135     195.029 170.793 203.028  1.00149.08           C  
ATOM   5286  NZ  LYS C 135     196.139 171.290 202.179  1.00149.08           N  
ATOM   5287  N   GLY C 136     189.884 172.726 205.916  1.00152.28           N  
ATOM   5288  CA  GLY C 136     189.343 173.547 206.984  1.00152.28           C  
ATOM   5289  C   GLY C 136     190.385 174.419 207.651  1.00152.28           C  
ATOM   5290  O   GLY C 136     191.267 174.995 207.003  1.00152.28           O  
ATOM   5291  N   ASN C 137     190.244 174.548 208.972  1.00148.79           N  
ATOM   5292  CA  ASN C 137     191.157 175.251 209.871  1.00148.79           C  
ATOM   5293  C   ASN C 137     191.035 176.769 209.776  1.00148.79           C  
ATOM   5294  O   ASN C 137     191.578 177.478 210.629  1.00148.79           O  
ATOM   5295  CB  ASN C 137     192.611 174.841 209.598  1.00148.79           C  
ATOM   5296  CG  ASN C 137     192.864 173.370 209.860  1.00148.79           C  
ATOM   5297  OD1 ASN C 137     193.164 172.611 208.940  1.00148.79           O  
ATOM   5298  ND2 ASN C 137     192.744 172.961 211.117  1.00148.79           N  
ATOM   5299  N   HIS C 138     190.290 177.263 208.786  1.00140.99           N  
ATOM   5300  CA  HIS C 138     190.225 178.689 208.445  1.00140.99           C  
ATOM   5301  C   HIS C 138     191.577 179.351 208.707  1.00140.99           C  
ATOM   5302  O   HIS C 138     191.720 180.277 209.505  1.00140.99           O  
ATOM   5303  CB  HIS C 138     189.075 179.412 209.157  1.00140.99           C  
ATOM   5304  CG  HIS C 138     188.998 179.179 210.634  1.00140.99           C  
ATOM   5305  ND1 HIS C 138     189.620 179.998 211.550  1.00140.99           N  
ATOM   5306  CD2 HIS C 138     188.321 178.255 211.356  1.00140.99           C  
ATOM   5307  CE1 HIS C 138     189.353 179.572 212.772  1.00140.99           C  
ATOM   5308  NE2 HIS C 138     188.568 178.514 212.682  1.00140.99           N  
ATOM   5309  N   SER C 139     192.576 178.831 208.004  1.00137.45           N  
ATOM   5310  CA  SER C 139     193.976 178.953 208.384  1.00137.45           C  
ATOM   5311  C   SER C 139     194.490 180.374 208.174  1.00137.45           C  
ATOM   5312  O   SER C 139     193.737 181.314 207.906  1.00137.45           O  
ATOM   5313  CB  SER C 139     194.809 177.947 207.598  1.00137.45           C  
ATOM   5314  OG  SER C 139     195.039 178.416 206.282  1.00137.45           O  
ATOM   5315  N   ALA C 140     195.807 180.530 208.317  1.00132.33           N  
ATOM   5316  CA  ALA C 140     196.440 181.826 208.118  1.00132.33           C  
ATOM   5317  C   ALA C 140     196.272 182.310 206.686  1.00132.33           C  
ATOM   5318  O   ALA C 140     196.004 183.494 206.449  1.00132.33           O  
ATOM   5319  CB  ALA C 140     197.921 181.739 208.480  1.00132.33           C  
ATOM   5320  N   TYR C 141     196.436 181.412 205.717  1.00123.48           N  
ATOM   5321  CA  TYR C 141     196.306 181.753 204.309  1.00123.48           C  
ATOM   5322  C   TYR C 141     194.992 181.268 203.718  1.00123.48           C  
ATOM   5323  O   TYR C 141     194.955 180.780 202.584  1.00123.48           O  
ATOM   5324  CB  TYR C 141     197.499 181.229 203.514  1.00123.48           C  
ATOM   5325  CG  TYR C 141     197.960 179.829 203.841  1.00123.48           C  
ATOM   5326  CD1 TYR C 141     198.751 179.585 204.952  1.00123.48           C  
ATOM   5327  CD2 TYR C 141     197.656 178.766 203.011  1.00123.48           C  
ATOM   5328  CE1 TYR C 141     199.197 178.324 205.247  1.00123.48           C  
ATOM   5329  CE2 TYR C 141     198.104 177.495 203.296  1.00123.48           C  
ATOM   5330  CZ  TYR C 141     198.874 177.281 204.417  1.00123.48           C  
ATOM   5331  OH  TYR C 141     199.325 176.017 204.715  1.00123.48           O  
ATOM   5332  N   LEU C 142     193.908 181.383 204.479  1.00119.18           N  
ATOM   5333  CA  LEU C 142     192.588 181.285 203.879  1.00119.18           C  
ATOM   5334  C   LEU C 142     192.283 182.532 203.068  1.00119.18           C  
ATOM   5335  O   LEU C 142     192.119 182.469 201.846  1.00119.18           O  
ATOM   5336  CB  LEU C 142     191.529 181.071 204.957  1.00119.18           C  
ATOM   5337  CG  LEU C 142     190.091 181.105 204.438  1.00119.18           C  
ATOM   5338  CD1 LEU C 142     189.863 180.000 203.432  1.00119.18           C  
ATOM   5339  CD2 LEU C 142     189.097 180.998 205.581  1.00119.18           C  
ATOM   5340  N   HIS C 143     192.234 183.690 203.729  1.00105.73           N  
ATOM   5341  CA  HIS C 143     191.793 184.894 203.039  1.00105.73           C  
ATOM   5342  C   HIS C 143     192.795 185.376 202.000  1.00105.73           C  
ATOM   5343  O   HIS C 143     192.432 186.192 201.153  1.00105.73           O  
ATOM   5344  CB  HIS C 143     191.445 186.010 204.034  1.00105.73           C  
ATOM   5345  CG  HIS C 143     192.537 186.359 204.995  1.00105.73           C  
ATOM   5346  ND1 HIS C 143     193.274 185.412 205.670  1.00105.73           N  
ATOM   5347  CD2 HIS C 143     192.980 187.561 205.432  1.00105.73           C  
ATOM   5348  CE1 HIS C 143     194.144 186.015 206.459  1.00105.73           C  
ATOM   5349  NE2 HIS C 143     193.986 187.320 206.334  1.00105.73           N  
ATOM   5350  N   PHE C 144     194.012 184.840 201.984  1.00101.39           N  
ATOM   5351  CA  PHE C 144     194.927 185.138 200.888  1.00101.39           C  
ATOM   5352  C   PHE C 144     194.391 184.584 199.574  1.00101.39           C  
ATOM   5353  O   PHE C 144     194.138 185.327 198.616  1.00101.39           O  
ATOM   5354  CB  PHE C 144     196.304 184.561 201.194  1.00101.39           C  
ATOM   5355  CG  PHE C 144     196.989 185.224 202.347  1.00101.39           C  
ATOM   5356  CD1 PHE C 144     196.488 186.384 202.892  1.00101.39           C  
ATOM   5357  CD2 PHE C 144     198.124 184.678 202.895  1.00101.39           C  
ATOM   5358  CE1 PHE C 144     197.112 186.985 203.951  1.00101.39           C  
ATOM   5359  CE2 PHE C 144     198.750 185.279 203.958  1.00101.39           C  
ATOM   5360  CZ  PHE C 144     198.242 186.432 204.485  1.00101.39           C  
ATOM   5361  N   ALA C 145     194.195 183.270 199.514  1.00105.25           N  
ATOM   5362  CA  ALA C 145     193.587 182.680 198.332  1.00105.25           C  
ATOM   5363  C   ALA C 145     192.134 183.103 198.161  1.00105.25           C  
ATOM   5364  O   ALA C 145     191.607 183.018 197.052  1.00105.25           O  
ATOM   5365  CB  ALA C 145     193.697 181.160 198.393  1.00105.25           C  
ATOM   5366  N   ASP C 146     191.472 183.540 199.232  1.00100.67           N  
ATOM   5367  CA  ASP C 146     190.146 184.129 199.082  1.00100.67           C  
ATOM   5368  C   ASP C 146     190.210 185.436 198.294  1.00100.67           C  
ATOM   5369  O   ASP C 146     189.343 185.708 197.455  1.00100.67           O  
ATOM   5370  CB  ASP C 146     189.523 184.359 200.456  1.00100.67           C  
ATOM   5371  CG  ASP C 146     188.078 184.799 200.384  1.00100.67           C  
ATOM   5372  OD1 ASP C 146     187.522 184.887 199.273  1.00100.67           O  
ATOM   5373  OD2 ASP C 146     187.497 185.085 201.448  1.00100.67           O  
ATOM   5374  N   GLY C 147     191.219 186.261 198.555  1.00 94.36           N  
ATOM   5375  CA  GLY C 147     191.381 187.497 197.827  1.00 94.36           C  
ATOM   5376  C   GLY C 147     192.114 187.383 196.528  1.00 94.36           C  
ATOM   5377  O   GLY C 147     192.261 188.379 195.818  1.00 94.36           O  
ATOM   5378  N   ILE C 148     192.618 186.192 196.201  1.00 97.83           N  
ATOM   5379  CA  ILE C 148     193.331 186.048 194.935  1.00 97.83           C  
ATOM   5380  C   ILE C 148     192.393 185.921 193.740  1.00 97.83           C  
ATOM   5381  O   ILE C 148     192.847 186.078 192.602  1.00 97.83           O  
ATOM   5382  CB  ILE C 148     194.296 184.849 194.996  1.00 97.83           C  
ATOM   5383  CG1 ILE C 148     195.302 184.910 193.860  1.00 97.83           C  
ATOM   5384  CG2 ILE C 148     193.533 183.567 194.807  1.00 97.83           C  
ATOM   5385  CD1 ILE C 148     196.462 183.978 194.048  1.00 97.83           C  
ATOM   5386  N   GLN C 149     191.093 185.670 193.940  1.00101.15           N  
ATOM   5387  CA  GLN C 149     190.146 185.827 192.836  1.00101.15           C  
ATOM   5388  C   GLN C 149     189.913 187.279 192.473  1.00101.15           C  
ATOM   5389  O   GLN C 149     189.029 187.575 191.665  1.00101.15           O  
ATOM   5390  CB  GLN C 149     188.799 185.158 193.111  1.00101.15           C  
ATOM   5391  CG  GLN C 149     188.828 183.660 193.185  1.00101.15           C  
ATOM   5392  CD  GLN C 149     189.256 183.159 194.516  1.00101.15           C  
ATOM   5393  OE1 GLN C 149     189.237 183.894 195.496  1.00101.15           O  
ATOM   5394  NE2 GLN C 149     189.644 181.895 194.572  1.00101.15           N  
ATOM   5395  N   SER C 150     190.675 188.185 193.072  1.00 92.83           N  
ATOM   5396  CA  SER C 150     190.895 189.499 192.495  1.00 92.83           C  
ATOM   5397  C   SER C 150     191.129 189.442 190.996  1.00 92.83           C  
ATOM   5398  O   SER C 150     190.779 190.392 190.291  1.00 92.83           O  
ATOM   5399  CB  SER C 150     192.105 190.134 193.171  1.00 92.83           C  
ATOM   5400  OG  SER C 150     192.422 191.381 192.609  1.00 92.83           O  
ATOM   5401  N   LEU C 151     191.705 188.350 190.494  1.00 95.94           N  
ATOM   5402  CA  LEU C 151     192.159 188.256 189.115  1.00 95.94           C  
ATOM   5403  C   LEU C 151     191.312 187.310 188.280  1.00 95.94           C  
ATOM   5404  O   LEU C 151     191.756 186.853 187.232  1.00 95.94           O  
ATOM   5405  CB  LEU C 151     193.630 187.847 189.061  1.00 95.94           C  
ATOM   5406  CG  LEU C 151     194.106 186.582 189.776  1.00 95.94           C  
ATOM   5407  CD1 LEU C 151     193.858 185.314 188.990  1.00 95.94           C  
ATOM   5408  CD2 LEU C 151     195.580 186.717 190.099  1.00 95.94           C  
ATOM   5409  N   ARG C 152     190.096 187.002 188.714  1.00100.27           N  
ATOM   5410  CA  ARG C 152     189.180 186.311 187.818  1.00100.27           C  
ATOM   5411  C   ARG C 152     188.312 187.284 187.040  1.00100.27           C  
ATOM   5412  O   ARG C 152     187.415 186.853 186.312  1.00100.27           O  
ATOM   5413  CB  ARG C 152     188.326 185.295 188.578  1.00100.27           C  
ATOM   5414  CG  ARG C 152     187.057 185.798 189.209  1.00100.27           C  
ATOM   5415  CD  ARG C 152     186.501 184.698 190.098  1.00100.27           C  
ATOM   5416  NE  ARG C 152     185.213 185.019 190.700  1.00100.27           N  
ATOM   5417  CZ  ARG C 152     184.741 184.418 191.787  1.00100.27           C  
ATOM   5418  NH1 ARG C 152     183.560 184.751 192.281  1.00100.27           N  
ATOM   5419  NH2 ARG C 152     185.465 183.494 192.394  1.00100.27           N  
ATOM   5420  N   ILE C 153     188.564 188.588 187.181  1.00 93.97           N  
ATOM   5421  CA  ILE C 153     188.152 189.547 186.170  1.00 93.97           C  
ATOM   5422  C   ILE C 153     188.940 189.337 184.896  1.00 93.97           C  
ATOM   5423  O   ILE C 153     188.527 189.787 183.825  1.00 93.97           O  
ATOM   5424  CB  ILE C 153     188.359 190.985 186.664  1.00 93.97           C  
ATOM   5425  CG1 ILE C 153     187.699 191.985 185.724  1.00 93.97           C  
ATOM   5426  CG2 ILE C 153     189.821 191.303 186.723  1.00 93.97           C  
ATOM   5427  CD1 ILE C 153     187.591 193.372 186.300  1.00 93.97           C  
ATOM   5428  N   LEU C 154     190.060 188.629 184.980  1.00 98.56           N  
ATOM   5429  CA  LEU C 154     190.996 188.546 183.875  1.00 98.56           C  
ATOM   5430  C   LEU C 154     190.442 187.738 182.711  1.00 98.56           C  
ATOM   5431  O   LEU C 154     191.074 187.695 181.652  1.00 98.56           O  
ATOM   5432  CB  LEU C 154     192.307 187.957 184.385  1.00 98.56           C  
ATOM   5433  CG  LEU C 154     193.605 188.341 183.695  1.00 98.56           C  
ATOM   5434  CD1 LEU C 154     193.946 189.777 184.053  1.00 98.56           C  
ATOM   5435  CD2 LEU C 154     194.704 187.412 184.141  1.00 98.56           C  
ATOM   5436  N   LYS C 155     189.293 187.081 182.890  1.00104.31           N  
ATOM   5437  CA  LYS C 155     188.547 186.540 181.762  1.00104.31           C  
ATOM   5438  C   LYS C 155     188.009 187.632 180.856  1.00104.31           C  
ATOM   5439  O   LYS C 155     187.711 187.363 179.692  1.00104.31           O  
ATOM   5440  CB  LYS C 155     187.372 185.694 182.246  1.00104.31           C  
ATOM   5441  CG  LYS C 155     187.703 184.276 182.655  1.00104.31           C  
ATOM   5442  CD  LYS C 155     186.472 183.593 183.218  1.00104.31           C  
ATOM   5443  CE  LYS C 155     185.356 183.515 182.180  1.00104.31           C  
ATOM   5444  NZ  LYS C 155     185.584 182.482 181.138  1.00104.31           N  
ATOM   5445  N   LEU C 156     187.868 188.852 181.365  1.00102.10           N  
ATOM   5446  CA  LEU C 156     187.284 189.926 180.577  1.00102.10           C  
ATOM   5447  C   LEU C 156     188.221 190.418 179.489  1.00102.10           C  
ATOM   5448  O   LEU C 156     187.796 191.194 178.631  1.00102.10           O  
ATOM   5449  CB  LEU C 156     186.896 191.085 181.491  1.00102.10           C  
ATOM   5450  CG  LEU C 156     185.847 192.061 180.978  1.00102.10           C  
ATOM   5451  CD1 LEU C 156     184.630 191.298 180.516  1.00102.10           C  
ATOM   5452  CD2 LEU C 156     185.482 193.043 182.069  1.00102.10           C  
ATOM   5453  N   ILE C 157     189.484 189.993 179.505  1.00105.26           N  
ATOM   5454  CA  ILE C 157     190.422 190.434 178.485  1.00105.26           C  
ATOM   5455  C   ILE C 157     190.185 189.728 177.162  1.00105.26           C  
ATOM   5456  O   ILE C 157     190.631 190.210 176.118  1.00105.26           O  
ATOM   5457  CB  ILE C 157     191.870 190.213 178.951  1.00105.26           C  
ATOM   5458  CG1 ILE C 157     192.789 191.224 178.292  1.00105.26           C  
ATOM   5459  CG2 ILE C 157     192.339 188.827 178.586  1.00105.26           C  
ATOM   5460  CD1 ILE C 157     194.171 191.222 178.854  1.00105.26           C  
ATOM   5461  N   SER C 158     189.475 188.604 177.174  1.00107.86           N  
ATOM   5462  CA  SER C 158     189.317 187.808 175.969  1.00107.86           C  
ATOM   5463  C   SER C 158     188.383 188.438 174.955  1.00107.86           C  
ATOM   5464  O   SER C 158     188.116 187.817 173.924  1.00107.86           O  
ATOM   5465  CB  SER C 158     188.800 186.419 176.332  1.00107.86           C  
ATOM   5466  OG  SER C 158     188.302 185.752 175.188  1.00107.86           O  
ATOM   5467  N   TYR C 159     187.875 189.638 175.209  1.00110.38           N  
ATOM   5468  CA  TYR C 159     186.795 190.161 174.389  1.00110.38           C  
ATOM   5469  C   TYR C 159     187.181 191.417 173.621  1.00110.38           C  
ATOM   5470  O   TYR C 159     186.935 191.504 172.417  1.00110.38           O  
ATOM   5471  CB  TYR C 159     185.573 190.419 175.271  1.00110.38           C  
ATOM   5472  CG  TYR C 159     184.891 189.132 175.644  1.00110.38           C  
ATOM   5473  CD1 TYR C 159     184.202 188.393 174.702  1.00110.38           C  
ATOM   5474  CD2 TYR C 159     184.964 188.637 176.933  1.00110.38           C  
ATOM   5475  CE1 TYR C 159     183.595 187.209 175.039  1.00110.38           C  
ATOM   5476  CE2 TYR C 159     184.359 187.453 177.276  1.00110.38           C  
ATOM   5477  CZ  TYR C 159     183.678 186.744 176.325  1.00110.38           C  
ATOM   5478  OH  TYR C 159     183.071 185.563 176.660  1.00110.38           O  
ATOM   5479  N   SER C 160     187.779 192.393 174.288  1.00113.17           N  
ATOM   5480  CA  SER C 160     188.187 193.610 173.604  1.00113.17           C  
ATOM   5481  C   SER C 160     189.271 193.281 172.589  1.00113.17           C  
ATOM   5482  O   SER C 160     190.349 192.805 172.953  1.00113.17           O  
ATOM   5483  CB  SER C 160     188.678 194.643 174.609  1.00113.17           C  
ATOM   5484  OG  SER C 160     187.589 195.307 175.224  1.00113.17           O  
ATOM   5485  N   ARG C 161     188.976 193.524 171.312  1.00115.35           N  
ATOM   5486  CA  ARG C 161     189.919 193.190 170.252  1.00115.35           C  
ATOM   5487  C   ARG C 161     191.184 194.030 170.355  1.00115.35           C  
ATOM   5488  O   ARG C 161     192.296 193.526 170.141  1.00115.35           O  
ATOM   5489  CB  ARG C 161     189.255 193.376 168.888  1.00115.35           C  
ATOM   5490  CG  ARG C 161     188.480 192.155 168.404  1.00115.35           C  
ATOM   5491  CD  ARG C 161     187.155 191.982 169.147  1.00115.35           C  
ATOM   5492  NE  ARG C 161     186.452 190.767 168.739  1.00115.35           N  
ATOM   5493  CZ  ARG C 161     185.295 190.356 169.250  1.00115.35           C  
ATOM   5494  NH1 ARG C 161     184.693 191.067 170.191  1.00115.35           N  
ATOM   5495  NH2 ARG C 161     184.736 189.236 168.815  1.00115.35           N  
ATOM   5496  N   GLY C 162     191.034 195.312 170.686  1.00110.91           N  
ATOM   5497  CA  GLY C 162     192.194 196.179 170.788  1.00110.91           C  
ATOM   5498  C   GLY C 162     193.196 195.689 171.811  1.00110.91           C  
ATOM   5499  O   GLY C 162     194.403 195.687 171.559  1.00110.91           O  
ATOM   5500  N   ILE C 163     192.712 195.253 172.976  1.00105.61           N  
ATOM   5501  CA  ILE C 163     193.631 194.701 173.958  1.00105.61           C  
ATOM   5502  C   ILE C 163     194.280 193.432 173.432  1.00105.61           C  
ATOM   5503  O   ILE C 163     195.433 193.153 173.753  1.00105.61           O  
ATOM   5504  CB  ILE C 163     192.938 194.453 175.304  1.00105.61           C  
ATOM   5505  CG1 ILE C 163     192.480 195.760 175.921  1.00105.61           C  
ATOM   5506  CG2 ILE C 163     193.900 193.843 176.269  1.00105.61           C  
ATOM   5507  CD1 ILE C 163     192.013 195.596 177.344  1.00105.61           C  
ATOM   5508  N   ARG C 164     193.571 192.631 172.639  1.00110.54           N  
ATOM   5509  CA  ARG C 164     194.202 191.436 172.086  1.00110.54           C  
ATOM   5510  C   ARG C 164     195.364 191.798 171.173  1.00110.54           C  
ATOM   5511  O   ARG C 164     196.438 191.183 171.241  1.00110.54           O  
ATOM   5512  CB  ARG C 164     193.176 190.590 171.337  1.00110.54           C  
ATOM   5513  CG  ARG C 164     192.099 189.995 172.220  1.00110.54           C  
ATOM   5514  CD  ARG C 164     191.105 189.214 171.389  1.00110.54           C  
ATOM   5515  NE  ARG C 164     191.617 187.906 170.995  1.00110.54           N  
ATOM   5516  CZ  ARG C 164     191.190 186.755 171.498  1.00110.54           C  
ATOM   5517  NH1 ARG C 164     190.237 186.746 172.415  1.00110.54           N  
ATOM   5518  NH2 ARG C 164     191.713 185.612 171.081  1.00110.54           N  
ATOM   5519  N   THR C 165     195.177 192.804 170.318  1.00112.06           N  
ATOM   5520  CA  THR C 165     196.283 193.254 169.476  1.00112.06           C  
ATOM   5521  C   THR C 165     197.420 193.814 170.321  1.00112.06           C  
ATOM   5522  O   THR C 165     198.603 193.618 170.005  1.00112.06           O  
ATOM   5523  CB  THR C 165     195.803 194.303 168.482  1.00112.06           C  
ATOM   5524  OG1 THR C 165     195.673 195.560 169.154  1.00112.06           O  
ATOM   5525  CG2 THR C 165     194.467 193.904 167.907  1.00112.06           C  
ATOM   5526  N   LEU C 166     197.079 194.530 171.392  1.00108.20           N  
ATOM   5527  CA  LEU C 166     198.107 195.008 172.304  1.00108.20           C  
ATOM   5528  C   LEU C 166     198.877 193.853 172.917  1.00108.20           C  
ATOM   5529  O   LEU C 166     200.101 193.916 173.046  1.00108.20           O  
ATOM   5530  CB  LEU C 166     197.488 195.859 173.404  1.00108.20           C  
ATOM   5531  CG  LEU C 166     198.569 196.415 174.322  1.00108.20           C  
ATOM   5532  CD1 LEU C 166     199.455 197.369 173.553  1.00108.20           C  
ATOM   5533  CD2 LEU C 166     197.955 197.088 175.520  1.00108.20           C  
ATOM   5534  N   ILE C 167     198.172 192.803 173.330  1.00110.80           N  
ATOM   5535  CA  ILE C 167     198.836 191.625 173.869  1.00110.80           C  
ATOM   5536  C   ILE C 167     199.820 191.079 172.856  1.00110.80           C  
ATOM   5537  O   ILE C 167     200.963 190.765 173.190  1.00110.80           O  
ATOM   5538  CB  ILE C 167     197.812 190.556 174.277  1.00110.80           C  
ATOM   5539  CG1 ILE C 167     197.135 190.926 175.586  1.00110.80           C  
ATOM   5540  CG2 ILE C 167     198.497 189.234 174.435  1.00110.80           C  
ATOM   5541  CD1 ILE C 167     198.062 190.884 176.760  1.00110.80           C  
ATOM   5542  N   ILE C 168     199.402 190.976 171.596  1.00115.32           N  
ATOM   5543  CA  ILE C 168     200.337 190.542 170.560  1.00115.32           C  
ATOM   5544  C   ILE C 168     201.585 191.415 170.592  1.00115.32           C  
ATOM   5545  O   ILE C 168     202.689 190.955 170.921  1.00115.32           O  
ATOM   5546  CB  ILE C 168     199.668 190.575 169.177  1.00115.32           C  
ATOM   5547  CG1 ILE C 168     198.481 189.610 169.137  1.00115.32           C  
ATOM   5548  CG2 ILE C 168     200.682 190.246 168.096  1.00115.32           C  
ATOM   5549  CD1 ILE C 168     198.839 188.185 169.457  1.00115.32           C  
ATOM   5550  N   ALA C 169     201.398 192.713 170.332  1.00119.21           N  
ATOM   5551  CA  ALA C 169     202.531 193.616 170.125  1.00119.21           C  
ATOM   5552  C   ALA C 169     203.455 193.660 171.334  1.00119.21           C  
ATOM   5553  O   ALA C 169     204.673 193.801 171.187  1.00119.21           O  
ATOM   5554  CB  ALA C 169     202.033 195.022 169.797  1.00119.21           C  
ATOM   5555  N   VAL C 170     202.900 193.549 172.534  1.00113.49           N  
ATOM   5556  CA  VAL C 170     203.706 193.669 173.741  1.00113.49           C  
ATOM   5557  C   VAL C 170     204.286 192.319 174.138  1.00113.49           C  
ATOM   5558  O   VAL C 170     205.508 192.133 174.169  1.00113.49           O  
ATOM   5559  CB  VAL C 170     202.868 194.275 174.879  1.00113.49           C  
ATOM   5560  CG1 VAL C 170     203.606 194.173 176.193  1.00113.49           C  
ATOM   5561  CG2 VAL C 170     202.535 195.711 174.559  1.00113.49           C  
ATOM   5562  N   GLY C 171     203.419 191.354 174.435  1.00111.55           N  
ATOM   5563  CA  GLY C 171     203.849 190.065 174.917  1.00111.55           C  
ATOM   5564  C   GLY C 171     204.650 189.260 173.929  1.00111.55           C  
ATOM   5565  O   GLY C 171     205.154 188.196 174.302  1.00111.55           O  
ATOM   5566  N   GLU C 172     204.786 189.716 172.686  1.00114.39           N  
ATOM   5567  CA  GLU C 172     205.753 189.030 171.843  1.00114.39           C  
ATOM   5568  C   GLU C 172     207.187 189.416 172.186  1.00114.39           C  
ATOM   5569  O   GLU C 172     208.115 188.948 171.520  1.00114.39           O  
ATOM   5570  CB  GLU C 172     205.461 189.297 170.363  1.00114.39           C  
ATOM   5571  CG  GLU C 172     205.667 190.720 169.905  1.00114.39           C  
ATOM   5572  CD  GLU C 172     207.054 190.931 169.343  1.00114.39           C  
ATOM   5573  OE1 GLU C 172     207.686 189.929 168.949  1.00114.39           O  
ATOM   5574  OE2 GLU C 172     207.514 192.087 169.293  1.00114.39           O  
ATOM   5575  N   THR C 173     207.388 190.238 173.216  1.00104.48           N  
ATOM   5576  CA  THR C 173     208.716 190.628 173.672  1.00104.48           C  
ATOM   5577  C   THR C 173     208.936 190.166 175.101  1.00104.48           C  
ATOM   5578  O   THR C 173     209.328 190.957 175.961  1.00104.48           O  
ATOM   5579  CB  THR C 173     208.897 192.138 173.606  1.00104.48           C  
ATOM   5580  OG1 THR C 173     207.983 192.758 174.516  1.00104.48           O  
ATOM   5581  CG2 THR C 173     208.617 192.633 172.211  1.00104.48           C  
ATOM   5582  N   VAL C 174     208.644 188.901 175.374  1.00 90.26           N  
ATOM   5583  CA  VAL C 174     208.788 188.384 176.725  1.00 90.26           C  
ATOM   5584  C   VAL C 174     210.114 187.660 176.914  1.00 90.26           C  
ATOM   5585  O   VAL C 174     210.659 187.644 178.022  1.00 90.26           O  
ATOM   5586  CB  VAL C 174     207.592 187.484 177.059  1.00 90.26           C  
ATOM   5587  CG1 VAL C 174     207.887 186.602 178.248  1.00 90.26           C  
ATOM   5588  CG2 VAL C 174     206.394 188.351 177.349  1.00 90.26           C  
ATOM   5589  N   TYR C 175     210.672 187.089 175.853  1.00 84.84           N  
ATOM   5590  CA  TYR C 175     211.972 186.451 175.989  1.00 84.84           C  
ATOM   5591  C   TYR C 175     213.042 187.475 176.340  1.00 84.84           C  
ATOM   5592  O   TYR C 175     213.947 187.189 177.131  1.00 84.84           O  
ATOM   5593  CB  TYR C 175     212.331 185.694 174.713  1.00 84.84           C  
ATOM   5594  CG  TYR C 175     211.322 184.638 174.311  1.00 84.84           C  
ATOM   5595  CD1 TYR C 175     210.070 184.989 173.831  1.00 84.84           C  
ATOM   5596  CD2 TYR C 175     211.625 183.290 174.418  1.00 84.84           C  
ATOM   5597  CE1 TYR C 175     209.153 184.031 173.465  1.00 84.84           C  
ATOM   5598  CE2 TYR C 175     210.713 182.324 174.056  1.00 84.84           C  
ATOM   5599  CZ  TYR C 175     209.478 182.700 173.580  1.00 84.84           C  
ATOM   5600  OH  TYR C 175     208.561 181.741 173.216  1.00 84.84           O  
ATOM   5601  N   THR C 176     212.953 188.680 175.774  1.00 81.59           N  
ATOM   5602  CA  THR C 176     213.888 189.730 176.163  1.00 81.59           C  
ATOM   5603  C   THR C 176     213.700 190.121 177.623  1.00 81.59           C  
ATOM   5604  O   THR C 176     214.682 190.314 178.350  1.00 81.59           O  
ATOM   5605  CB  THR C 176     213.737 190.946 175.247  1.00 81.59           C  
ATOM   5606  OG1 THR C 176     214.677 191.953 175.623  1.00 81.59           O  
ATOM   5607  CG2 THR C 176     212.356 191.528 175.334  1.00 81.59           C  
ATOM   5608  N   VAL C 177     212.451 190.216 178.078  1.00 73.07           N  
ATOM   5609  CA  VAL C 177     212.190 190.565 179.469  1.00 73.07           C  
ATOM   5610  C   VAL C 177     212.732 189.491 180.393  1.00 73.07           C  
ATOM   5611  O   VAL C 177     213.396 189.784 181.393  1.00 73.07           O  
ATOM   5612  CB  VAL C 177     210.687 190.778 179.689  1.00 73.07           C  
ATOM   5613  CG1 VAL C 177     210.385 190.844 181.162  1.00 73.07           C  
ATOM   5614  CG2 VAL C 177     210.242 192.030 178.993  1.00 73.07           C  
ATOM   5615  N   ALA C 178     212.454 188.228 180.077  1.00 69.07           N  
ATOM   5616  CA  ALA C 178     212.925 187.143 180.926  1.00 69.07           C  
ATOM   5617  C   ALA C 178     214.444 187.071 180.930  1.00 69.07           C  
ATOM   5618  O   ALA C 178     215.054 186.751 181.955  1.00 69.07           O  
ATOM   5619  CB  ALA C 178     212.319 185.824 180.468  1.00 69.07           C  
ATOM   5620  N   SER C 179     215.077 187.391 179.802  1.00 69.83           N  
ATOM   5621  CA  SER C 179     216.534 187.437 179.769  1.00 69.83           C  
ATOM   5622  C   SER C 179     217.068 188.515 180.697  1.00 69.83           C  
ATOM   5623  O   SER C 179     217.959 188.263 181.516  1.00 69.83           O  
ATOM   5624  CB  SER C 179     217.025 187.691 178.349  1.00 69.83           C  
ATOM   5625  OG  SER C 179     216.493 188.899 177.850  1.00 69.83           O  
ATOM   5626  N   VAL C 180     216.547 189.733 180.574  1.00 63.79           N  
ATOM   5627  CA  VAL C 180     217.072 190.809 181.403  1.00 63.79           C  
ATOM   5628  C   VAL C 180     216.805 190.519 182.870  1.00 63.79           C  
ATOM   5629  O   VAL C 180     217.615 190.859 183.738  1.00 63.79           O  
ATOM   5630  CB  VAL C 180     216.497 192.169 180.978  1.00 63.79           C  
ATOM   5631  CG1 VAL C 180     217.227 193.264 181.694  1.00 63.79           C  
ATOM   5632  CG2 VAL C 180     216.641 192.358 179.500  1.00 63.79           C  
ATOM   5633  N   LEU C 181     215.681 189.873 183.174  1.00 59.55           N  
ATOM   5634  CA  LEU C 181     215.384 189.575 184.571  1.00 59.55           C  
ATOM   5635  C   LEU C 181     216.312 188.498 185.117  1.00 59.55           C  
ATOM   5636  O   LEU C 181     216.732 188.564 186.279  1.00 59.55           O  
ATOM   5637  CB  LEU C 181     213.925 189.170 184.726  1.00 59.55           C  
ATOM   5638  CG  LEU C 181     212.970 190.353 184.851  1.00 59.55           C  
ATOM   5639  CD1 LEU C 181     211.595 189.868 185.229  1.00 59.55           C  
ATOM   5640  CD2 LEU C 181     213.473 191.343 185.871  1.00 59.55           C  
ATOM   5641  N   THR C 182     216.667 187.515 184.291  1.00 55.41           N  
ATOM   5642  CA  THR C 182     217.657 186.533 184.713  1.00 55.41           C  
ATOM   5643  C   THR C 182     219.003 187.185 184.983  1.00 55.41           C  
ATOM   5644  O   THR C 182     219.664 186.880 185.981  1.00 55.41           O  
ATOM   5645  CB  THR C 182     217.800 185.457 183.649  1.00 55.41           C  
ATOM   5646  OG1 THR C 182     216.534 184.819 183.455  1.00 55.41           O  
ATOM   5647  CG2 THR C 182     218.818 184.433 184.075  1.00 55.41           C  
ATOM   5648  N   LEU C 183     219.429 188.087 184.103  1.00 57.27           N  
ATOM   5649  CA  LEU C 183     220.715 188.743 184.318  1.00 57.27           C  
ATOM   5650  C   LEU C 183     220.693 189.614 185.563  1.00 57.27           C  
ATOM   5651  O   LEU C 183     221.672 189.654 186.318  1.00 57.27           O  
ATOM   5652  CB  LEU C 183     221.121 189.569 183.100  1.00 57.27           C  
ATOM   5653  CG  LEU C 183     221.850 188.837 181.976  1.00 57.27           C  
ATOM   5654  CD1 LEU C 183     223.161 188.342 182.503  1.00 57.27           C  
ATOM   5655  CD2 LEU C 183     221.068 187.699 181.412  1.00 57.27           C  
ATOM   5656  N   LEU C 184     219.596 190.332 185.792  1.00 54.95           N  
ATOM   5657  CA  LEU C 184     219.503 191.136 187.002  1.00 54.95           C  
ATOM   5658  C   LEU C 184     219.573 190.259 188.235  1.00 54.95           C  
ATOM   5659  O   LEU C 184     220.239 190.609 189.213  1.00 54.95           O  
ATOM   5660  CB  LEU C 184     218.214 191.946 187.020  1.00 54.95           C  
ATOM   5661  CG  LEU C 184     218.117 192.920 188.197  1.00 54.95           C  
ATOM   5662  CD1 LEU C 184     219.004 194.116 187.976  1.00 54.95           C  
ATOM   5663  CD2 LEU C 184     216.690 193.347 188.466  1.00 54.95           C  
ATOM   5664  N   PHE C 185     218.884 189.119 188.216  1.00 54.64           N  
ATOM   5665  CA  PHE C 185     218.945 188.227 189.364  1.00 54.64           C  
ATOM   5666  C   PHE C 185     220.359 187.720 189.594  1.00 54.64           C  
ATOM   5667  O   PHE C 185     220.796 187.584 190.739  1.00 54.64           O  
ATOM   5668  CB  PHE C 185     218.002 187.050 189.181  1.00 54.64           C  
ATOM   5669  CG  PHE C 185     218.139 186.024 190.248  1.00 54.64           C  
ATOM   5670  CD1 PHE C 185     217.492 186.186 191.455  1.00 54.64           C  
ATOM   5671  CD2 PHE C 185     218.928 184.915 190.061  1.00 54.64           C  
ATOM   5672  CE1 PHE C 185     217.615 185.256 192.451  1.00 54.64           C  
ATOM   5673  CE2 PHE C 185     219.059 183.982 191.056  1.00 54.64           C  
ATOM   5674  CZ  PHE C 185     218.398 184.154 192.256  1.00 54.64           C  
ATOM   5675  N   LEU C 186     221.082 187.406 188.521  1.00 54.12           N  
ATOM   5676  CA  LEU C 186     222.449 186.929 188.685  1.00 54.12           C  
ATOM   5677  C   LEU C 186     223.331 188.007 189.293  1.00 54.12           C  
ATOM   5678  O   LEU C 186     224.154 187.729 190.175  1.00 54.12           O  
ATOM   5679  CB  LEU C 186     222.999 186.467 187.342  1.00 54.12           C  
ATOM   5680  CG  LEU C 186     224.313 185.693 187.290  1.00 54.12           C  
ATOM   5681  CD1 LEU C 186     224.289 184.791 186.092  1.00 54.12           C  
ATOM   5682  CD2 LEU C 186     225.511 186.612 187.199  1.00 54.12           C  
ATOM   5683  N   LEU C 187     223.179 189.246 188.833  1.00 51.30           N  
ATOM   5684  CA  LEU C 187     223.966 190.337 189.395  1.00 51.30           C  
ATOM   5685  C   LEU C 187     223.642 190.549 190.867  1.00 51.30           C  
ATOM   5686  O   LEU C 187     224.546 190.720 191.698  1.00 51.30           O  
ATOM   5687  CB  LEU C 187     223.715 191.611 188.603  1.00 51.30           C  
ATOM   5688  CG  LEU C 187     224.532 192.833 189.000  1.00 51.30           C  
ATOM   5689  CD1 LEU C 187     226.013 192.563 188.848  1.00 51.30           C  
ATOM   5690  CD2 LEU C 187     224.105 194.018 188.169  1.00 51.30           C  
ATOM   5691  N   MET C 188     222.355 190.534 191.212  1.00 59.01           N  
ATOM   5692  CA  MET C 188     221.980 190.656 192.614  1.00 59.01           C  
ATOM   5693  C   MET C 188     222.515 189.500 193.433  1.00 59.01           C  
ATOM   5694  O   MET C 188     222.873 189.688 194.590  1.00 59.01           O  
ATOM   5695  CB  MET C 188     220.465 190.747 192.779  1.00 59.01           C  
ATOM   5696  CG  MET C 188     219.840 191.908 192.054  1.00 59.01           C  
ATOM   5697  SD  MET C 188     218.460 192.601 192.960  1.00 59.01           S  
ATOM   5698  CE  MET C 188     217.662 191.103 193.511  1.00 59.01           C  
ATOM   5699  N   PHE C 189     222.586 188.303 192.864  1.00 51.85           N  
ATOM   5700  CA  PHE C 189     223.135 187.185 193.617  1.00 51.85           C  
ATOM   5701  C   PHE C 189     224.613 187.393 193.914  1.00 51.85           C  
ATOM   5702  O   PHE C 189     225.065 187.199 195.050  1.00 51.85           O  
ATOM   5703  CB  PHE C 189     222.922 185.888 192.853  1.00 51.85           C  
ATOM   5704  CG  PHE C 189     223.381 184.693 193.593  1.00 51.85           C  
ATOM   5705  CD1 PHE C 189     222.593 184.128 194.557  1.00 51.85           C  
ATOM   5706  CD2 PHE C 189     224.610 184.145 193.338  1.00 51.85           C  
ATOM   5707  CE1 PHE C 189     223.015 183.034 195.246  1.00 51.85           C  
ATOM   5708  CE2 PHE C 189     225.036 183.052 194.024  1.00 51.85           C  
ATOM   5709  CZ  PHE C 189     224.237 182.496 194.982  1.00 51.85           C  
ATOM   5710  N   VAL C 190     225.384 187.777 192.896  1.00 51.88           N  
ATOM   5711  CA  VAL C 190     226.811 188.018 193.098  1.00 51.88           C  
ATOM   5712  C   VAL C 190     227.018 189.053 194.188  1.00 51.88           C  
ATOM   5713  O   VAL C 190     227.838 188.885 195.104  1.00 51.88           O  
ATOM   5714  CB  VAL C 190     227.469 188.475 191.790  1.00 51.88           C  
ATOM   5715  CG1 VAL C 190     228.911 188.765 192.031  1.00 51.88           C  
ATOM   5716  CG2 VAL C 190     227.310 187.439 190.724  1.00 51.88           C  
ATOM   5717  N   PHE C 191     226.264 190.141 194.116  1.00 55.00           N  
ATOM   5718  CA  PHE C 191     226.473 191.180 195.102  1.00 55.00           C  
ATOM   5719  C   PHE C 191     225.877 190.833 196.451  1.00 55.00           C  
ATOM   5720  O   PHE C 191     226.337 191.361 197.458  1.00 55.00           O  
ATOM   5721  CB  PHE C 191     225.926 192.495 194.593  1.00 55.00           C  
ATOM   5722  CG  PHE C 191     226.919 193.273 193.821  1.00 55.00           C  
ATOM   5723  CD1 PHE C 191     227.764 194.143 194.458  1.00 55.00           C  
ATOM   5724  CD2 PHE C 191     227.031 193.110 192.464  1.00 55.00           C  
ATOM   5725  CE1 PHE C 191     228.678 194.853 193.759  1.00 55.00           C  
ATOM   5726  CE2 PHE C 191     227.950 193.820 191.761  1.00 55.00           C  
ATOM   5727  CZ  PHE C 191     228.776 194.692 192.409  1.00 55.00           C  
ATOM   5728  N   ALA C 192     224.890 189.947 196.512  1.00 54.48           N  
ATOM   5729  CA  ALA C 192     224.416 189.497 197.811  1.00 54.48           C  
ATOM   5730  C   ALA C 192     225.469 188.661 198.505  1.00 54.48           C  
ATOM   5731  O   ALA C 192     225.655 188.769 199.720  1.00 54.48           O  
ATOM   5732  CB  ALA C 192     223.130 188.698 197.664  1.00 54.48           C  
ATOM   5733  N   ILE C 193     226.168 187.818 197.750  1.00 54.52           N  
ATOM   5734  CA  ILE C 193     227.261 187.058 198.344  1.00 54.52           C  
ATOM   5735  C   ILE C 193     228.350 187.997 198.846  1.00 54.52           C  
ATOM   5736  O   ILE C 193     228.857 187.835 199.962  1.00 54.52           O  
ATOM   5737  CB  ILE C 193     227.809 186.025 197.352  1.00 54.52           C  
ATOM   5738  CG1 ILE C 193     226.711 185.052 196.973  1.00 54.52           C  
ATOM   5739  CG2 ILE C 193     228.912 185.252 197.993  1.00 54.52           C  
ATOM   5740  CD1 ILE C 193     226.164 184.324 198.144  1.00 54.52           C  
ATOM   5741  N   LEU C 194     228.717 189.003 198.052  1.00 58.75           N  
ATOM   5742  CA  LEU C 194     229.684 189.979 198.558  1.00 58.75           C  
ATOM   5743  C   LEU C 194     229.181 190.679 199.813  1.00 58.75           C  
ATOM   5744  O   LEU C 194     229.903 190.786 200.809  1.00 58.75           O  
ATOM   5745  CB  LEU C 194     230.026 191.019 197.500  1.00 58.75           C  
ATOM   5746  CG  LEU C 194     231.234 190.725 196.640  1.00 58.75           C  
ATOM   5747  CD1 LEU C 194     231.340 191.753 195.555  1.00 58.75           C  
ATOM   5748  CD2 LEU C 194     232.422 190.816 197.544  1.00 58.75           C  
ATOM   5749  N   GLY C 195     227.954 191.186 199.776  1.00 62.19           N  
ATOM   5750  CA  GLY C 195     227.450 191.967 200.885  1.00 62.19           C  
ATOM   5751  C   GLY C 195     227.301 191.162 202.150  1.00 62.19           C  
ATOM   5752  O   GLY C 195     227.421 191.702 203.249  1.00 62.19           O  
ATOM   5753  N   PHE C 196     227.010 189.875 202.020  1.00 66.93           N  
ATOM   5754  CA  PHE C 196     227.017 189.012 203.188  1.00 66.93           C  
ATOM   5755  C   PHE C 196     228.431 188.816 203.701  1.00 66.93           C  
ATOM   5756  O   PHE C 196     228.690 188.956 204.898  1.00 66.93           O  
ATOM   5757  CB  PHE C 196     226.377 187.672 202.855  1.00 66.93           C  
ATOM   5758  CG  PHE C 196     226.522 186.664 203.937  1.00 66.93           C  
ATOM   5759  CD1 PHE C 196     225.579 186.570 204.939  1.00 66.93           C  
ATOM   5760  CD2 PHE C 196     227.607 185.810 203.960  1.00 66.93           C  
ATOM   5761  CE1 PHE C 196     225.717 185.644 205.940  1.00 66.93           C  
ATOM   5762  CE2 PHE C 196     227.750 184.887 204.958  1.00 66.93           C  
ATOM   5763  CZ  PHE C 196     226.802 184.802 205.949  1.00 66.93           C  
ATOM   5764  N   CYS C 197     229.367 188.498 202.808  1.00 66.71           N  
ATOM   5765  CA  CYS C 197     230.717 188.191 203.258  1.00 66.71           C  
ATOM   5766  C   CYS C 197     231.391 189.392 203.898  1.00 66.71           C  
ATOM   5767  O   CYS C 197     232.265 189.223 204.752  1.00 66.71           O  
ATOM   5768  CB  CYS C 197     231.551 187.674 202.094  1.00 66.71           C  
ATOM   5769  SG  CYS C 197     231.016 186.068 201.486  1.00 66.71           S  
ATOM   5770  N   LEU C 198     231.002 190.603 203.514  1.00 68.33           N  
ATOM   5771  CA  LEU C 198     231.670 191.800 204.007  1.00 68.33           C  
ATOM   5772  C   LEU C 198     230.968 192.441 205.188  1.00 68.33           C  
ATOM   5773  O   LEU C 198     231.628 192.835 206.149  1.00 68.33           O  
ATOM   5774  CB  LEU C 198     231.807 192.836 202.894  1.00 68.33           C  
ATOM   5775  CG  LEU C 198     232.726 192.466 201.738  1.00 68.33           C  
ATOM   5776  CD1 LEU C 198     233.038 193.686 200.909  1.00 68.33           C  
ATOM   5777  CD2 LEU C 198     233.988 191.839 202.266  1.00 68.33           C  
ATOM   5778  N   PHE C 199     229.647 192.563 205.142  1.00 71.98           N  
ATOM   5779  CA  PHE C 199     228.905 193.269 206.174  1.00 71.98           C  
ATOM   5780  C   PHE C 199     227.968 192.352 206.940  1.00 71.98           C  
ATOM   5781  O   PHE C 199     227.090 192.838 207.650  1.00 71.98           O  
ATOM   5782  CB  PHE C 199     228.111 194.418 205.551  1.00 71.98           C  
ATOM   5783  CG  PHE C 199     228.827 195.111 204.431  1.00 71.98           C  
ATOM   5784  CD1 PHE C 199     229.944 195.875 204.671  1.00 71.98           C  
ATOM   5785  CD2 PHE C 199     228.387 194.985 203.135  1.00 71.98           C  
ATOM   5786  CE1 PHE C 199     230.595 196.498 203.641  1.00 71.98           C  
ATOM   5787  CE2 PHE C 199     229.034 195.608 202.112  1.00 71.98           C  
ATOM   5788  CZ  PHE C 199     230.137 196.361 202.362  1.00 71.98           C  
ATOM   5789  N   GLY C 200     228.122 191.048 206.807  1.00 78.98           N  
ATOM   5790  CA  GLY C 200     227.178 190.095 207.352  1.00 78.98           C  
ATOM   5791  C   GLY C 200     227.740 189.258 208.476  1.00 78.98           C  
ATOM   5792  O   GLY C 200     227.639 189.605 209.653  1.00 78.98           O  
ATOM   5793  N   VAL C 201     228.303 188.111 208.097  1.00 86.57           N  
ATOM   5794  CA  VAL C 201     228.817 187.118 209.024  1.00 86.57           C  
ATOM   5795  C   VAL C 201     229.939 187.646 209.909  1.00 86.57           C  
ATOM   5796  O   VAL C 201     230.384 186.943 210.816  1.00 86.57           O  
ATOM   5797  CB  VAL C 201     229.304 185.893 208.219  1.00 86.57           C  
ATOM   5798  CG1 VAL C 201     230.529 186.262 207.376  1.00 86.57           C  
ATOM   5799  CG2 VAL C 201     229.534 184.669 209.113  1.00 86.57           C  
ATOM   5800  N   THR C 202     230.415 188.867 209.672  1.00 95.98           N  
ATOM   5801  CA  THR C 202     231.527 189.395 210.457  1.00 95.98           C  
ATOM   5802  C   THR C 202     231.205 189.529 211.945  1.00 95.98           C  
ATOM   5803  O   THR C 202     232.134 189.608 212.754  1.00 95.98           O  
ATOM   5804  CB  THR C 202     231.960 190.751 209.896  1.00 95.98           C  
ATOM   5805  OG1 THR C 202     233.096 191.232 210.623  1.00 95.98           O  
ATOM   5806  CG2 THR C 202     230.834 191.757 210.007  1.00 95.98           C  
ATOM   5807  N   ASP C 203     229.922 189.604 212.314  1.00 98.61           N  
ATOM   5808  CA  ASP C 203     229.459 189.675 213.701  1.00 98.61           C  
ATOM   5809  C   ASP C 203     229.876 190.961 214.405  1.00 98.61           C  
ATOM   5810  O   ASP C 203     229.416 191.240 215.515  1.00 98.61           O  
ATOM   5811  CB  ASP C 203     229.952 188.479 214.516  1.00 98.61           C  
ATOM   5812  CG  ASP C 203     229.765 187.168 213.801  1.00 98.61           C  
ATOM   5813  OD1 ASP C 203     228.798 187.051 213.022  1.00 98.61           O  
ATOM   5814  OD2 ASP C 203     230.587 186.253 214.023  1.00 98.61           O  
ATOM   5815  N   ARG C 204     230.730 191.756 213.775  1.00101.09           N  
ATOM   5816  CA  ARG C 204     231.041 193.085 214.268  1.00101.09           C  
ATOM   5817  C   ARG C 204     230.350 194.172 213.463  1.00101.09           C  
ATOM   5818  O   ARG C 204     230.515 195.355 213.775  1.00101.09           O  
ATOM   5819  CB  ARG C 204     232.553 193.332 214.239  1.00101.09           C  
ATOM   5820  CG  ARG C 204     233.135 193.414 212.835  1.00101.09           C  
ATOM   5821  CD  ARG C 204     234.425 194.223 212.817  1.00101.09           C  
ATOM   5822  NE  ARG C 204     234.755 194.701 211.476  1.00101.09           N  
ATOM   5823  CZ  ARG C 204     234.621 195.963 211.076  1.00101.09           C  
ATOM   5824  NH1 ARG C 204     234.152 196.881 211.911  1.00101.09           N  
ATOM   5825  NH2 ARG C 204     234.949 196.308 209.837  1.00101.09           N  
ATOM   5826  N   GLY C 205     229.599 193.801 212.433  1.00 96.60           N  
ATOM   5827  CA  GLY C 205     228.949 194.782 211.598  1.00 96.60           C  
ATOM   5828  C   GLY C 205     227.675 194.311 210.934  1.00 96.60           C  
ATOM   5829  O   GLY C 205     227.650 193.276 210.270  1.00 96.60           O  
ATOM   5830  N   ASP C 206     226.612 195.080 211.150  1.00 87.54           N  
ATOM   5831  CA  ASP C 206     225.352 195.050 210.405  1.00 87.54           C  
ATOM   5832  C   ASP C 206     224.871 193.641 210.071  1.00 87.54           C  
ATOM   5833  O   ASP C 206     224.705 193.268 208.912  1.00 87.54           O  
ATOM   5834  CB  ASP C 206     225.443 195.879 209.130  1.00 87.54           C  
ATOM   5835  CG  ASP C 206     224.085 196.325 208.652  1.00 87.54           C  
ATOM   5836  OD1 ASP C 206     223.088 195.712 209.072  1.00 87.54           O  
ATOM   5837  OD2 ASP C 206     224.004 197.314 207.901  1.00 87.54           O  
ATOM   5838  N   LEU C 207     224.589 192.876 211.110  1.00 86.24           N  
ATOM   5839  CA  LEU C 207     223.735 191.723 210.923  1.00 86.24           C  
ATOM   5840  C   LEU C 207     222.337 192.218 210.539  1.00 86.24           C  
ATOM   5841  O   LEU C 207     222.099 193.418 210.384  1.00 86.24           O  
ATOM   5842  CB  LEU C 207     223.765 190.866 212.189  1.00 86.24           C  
ATOM   5843  CG  LEU C 207     223.109 189.490 212.312  1.00 86.24           C  
ATOM   5844  CD1 LEU C 207     223.972 188.615 213.190  1.00 86.24           C  
ATOM   5845  CD2 LEU C 207     221.728 189.607 212.928  1.00 86.24           C  
ATOM   5846  N   GLU C 208     221.422 191.282 210.287  1.00 83.38           N  
ATOM   5847  CA  GLU C 208     219.978 191.508 210.159  1.00 83.38           C  
ATOM   5848  C   GLU C 208     219.609 192.505 209.064  1.00 83.38           C  
ATOM   5849  O   GLU C 208     218.428 192.774 208.832  1.00 83.38           O  
ATOM   5850  CB  GLU C 208     219.356 191.940 211.499  1.00 83.38           C  
ATOM   5851  CG  GLU C 208     219.728 193.309 212.039  1.00 83.38           C  
ATOM   5852  CD  GLU C 208     218.903 194.416 211.433  1.00 83.38           C  
ATOM   5853  OE1 GLU C 208     217.798 194.123 210.937  1.00 83.38           O  
ATOM   5854  OE2 GLU C 208     219.364 195.576 211.437  1.00 83.38           O  
ATOM   5855  N   ASN C 209     220.577 193.031 208.386  1.00 74.88           N  
ATOM   5856  CA  ASN C 209     220.330 193.738 207.140  1.00 74.88           C  
ATOM   5857  C   ASN C 209     221.108 193.109 206.006  1.00 74.88           C  
ATOM   5858  O   ASN C 209     220.617 193.057 204.880  1.00 74.88           O  
ATOM   5859  CB  ASN C 209     220.695 195.211 207.282  1.00 74.88           C  
ATOM   5860  CG  ASN C 209     219.763 196.108 206.529  1.00 74.88           C  
ATOM   5861  OD1 ASN C 209     218.924 195.646 205.764  1.00 74.88           O  
ATOM   5862  ND2 ASN C 209     219.880 197.402 206.761  1.00 74.88           N  
ATOM   5863  N   TRP C 210     222.309 192.623 206.289  1.00 67.18           N  
ATOM   5864  CA  TRP C 210     223.030 191.701 205.430  1.00 67.18           C  
ATOM   5865  C   TRP C 210     223.205 190.344 206.095  1.00 67.18           C  
ATOM   5866  O   TRP C 210     224.110 189.594 205.733  1.00 67.18           O  
ATOM   5867  CB  TRP C 210     224.384 192.290 205.064  1.00 67.18           C  
ATOM   5868  CG  TRP C 210     224.276 193.659 204.539  1.00 67.18           C  
ATOM   5869  CD1 TRP C 210     224.213 194.802 205.256  1.00 67.18           C  
ATOM   5870  CD2 TRP C 210     224.224 194.037 203.171  1.00 67.18           C  
ATOM   5871  NE1 TRP C 210     224.120 195.878 204.419  1.00 67.18           N  
ATOM   5872  CE2 TRP C 210     224.125 195.428 203.129  1.00 67.18           C  
ATOM   5873  CE3 TRP C 210     224.247 193.330 201.974  1.00 67.18           C  
ATOM   5874  CZ2 TRP C 210     224.057 196.126 201.944  1.00 67.18           C  
ATOM   5875  CZ3 TRP C 210     224.176 194.022 200.806  1.00 67.18           C  
ATOM   5876  CH2 TRP C 210     224.082 195.405 200.793  1.00 67.18           C  
ATOM   5877  N   GLY C 211     222.358 190.024 207.074  1.00 66.11           N  
ATOM   5878  CA  GLY C 211     222.544 188.799 207.828  1.00 66.11           C  
ATOM   5879  C   GLY C 211     222.428 187.554 206.974  1.00 66.11           C  
ATOM   5880  O   GLY C 211     223.157 186.584 207.178  1.00 66.11           O  
ATOM   5881  N   ASN C 212     221.519 187.561 206.006  1.00 58.40           N  
ATOM   5882  CA  ASN C 212     221.239 186.381 205.204  1.00 58.40           C  
ATOM   5883  C   ASN C 212     220.703 186.817 203.853  1.00 58.40           C  
ATOM   5884  O   ASN C 212     220.273 187.957 203.681  1.00 58.40           O  
ATOM   5885  CB  ASN C 212     220.256 185.471 205.922  1.00 58.40           C  
ATOM   5886  CG  ASN C 212     219.117 186.238 206.521  1.00 58.40           C  
ATOM   5887  OD1 ASN C 212     219.108 187.462 206.484  1.00 58.40           O  
ATOM   5888  ND2 ASN C 212     218.133 185.532 207.048  1.00 58.40           N  
ATOM   5889  N   LEU C 213     220.728 185.896 202.882  1.00 55.03           N  
ATOM   5890  CA  LEU C 213     220.285 186.246 201.534  1.00 55.03           C  
ATOM   5891  C   LEU C 213     218.840 186.714 201.493  1.00 55.03           C  
ATOM   5892  O   LEU C 213     218.501 187.586 200.687  1.00 55.03           O  
ATOM   5893  CB  LEU C 213     220.472 185.082 200.569  1.00 55.03           C  
ATOM   5894  CG  LEU C 213     221.779 185.093 199.779  1.00 55.03           C  
ATOM   5895  CD1 LEU C 213     222.947 184.790 200.649  1.00 55.03           C  
ATOM   5896  CD2 LEU C 213     221.714 184.123 198.617  1.00 55.03           C  
ATOM   5897  N   ALA C 214     217.977 186.178 202.351  1.00 53.10           N  
ATOM   5898  CA  ALA C 214     216.602 186.658 202.370  1.00 53.10           C  
ATOM   5899  C   ALA C 214     216.542 188.134 202.709  1.00 53.10           C  
ATOM   5900  O   ALA C 214     215.545 188.797 202.419  1.00 53.10           O  
ATOM   5901  CB  ALA C 214     215.775 185.852 203.362  1.00 53.10           C  
ATOM   5902  N   SER C 215     217.591 188.663 203.328  1.00 53.24           N  
ATOM   5903  CA  SER C 215     217.709 190.081 203.610  1.00 53.24           C  
ATOM   5904  C   SER C 215     218.692 190.789 202.704  1.00 53.24           C  
ATOM   5905  O   SER C 215     218.525 191.983 202.442  1.00 53.24           O  
ATOM   5906  CB  SER C 215     218.138 190.295 205.061  1.00 53.24           C  
ATOM   5907  OG  SER C 215     218.299 191.669 205.336  1.00 53.24           O  
ATOM   5908  N   ALA C 216     219.710 190.084 202.220  1.00 53.02           N  
ATOM   5909  CA  ALA C 216     220.642 190.694 201.285  1.00 53.02           C  
ATOM   5910  C   ALA C 216     219.953 191.051 199.978  1.00 53.02           C  
ATOM   5911  O   ALA C 216     220.165 192.138 199.442  1.00 53.02           O  
ATOM   5912  CB  ALA C 216     221.825 189.768 201.037  1.00 53.02           C  
ATOM   5913  N   PHE C 217     219.110 190.161 199.454  1.00 52.26           N  
ATOM   5914  CA  PHE C 217     218.352 190.511 198.257  1.00 52.26           C  
ATOM   5915  C   PHE C 217     217.450 191.709 198.478  1.00 52.26           C  
ATOM   5916  O   PHE C 217     217.325 192.556 197.598  1.00 52.26           O  
ATOM   5917  CB  PHE C 217     217.536 189.327 197.764  1.00 52.26           C  
ATOM   5918  CG  PHE C 217     218.352 188.250 197.143  1.00 52.26           C  
ATOM   5919  CD1 PHE C 217     219.648 188.492 196.752  1.00 52.26           C  
ATOM   5920  CD2 PHE C 217     217.819 186.995 196.940  1.00 52.26           C  
ATOM   5921  CE1 PHE C 217     220.388 187.509 196.159  1.00 52.26           C  
ATOM   5922  CE2 PHE C 217     218.566 186.006 196.358  1.00 52.26           C  
ATOM   5923  CZ  PHE C 217     219.854 186.267 195.970  1.00 52.26           C  
ATOM   5924  N   PHE C 218     216.792 191.796 199.625  1.00 52.65           N  
ATOM   5925  CA  PHE C 218     215.885 192.918 199.825  1.00 52.65           C  
ATOM   5926  C   PHE C 218     216.645 194.231 199.904  1.00 52.65           C  
ATOM   5927  O   PHE C 218     216.267 195.213 199.259  1.00 52.65           O  
ATOM   5928  CB  PHE C 218     215.031 192.706 201.064  1.00 52.65           C  
ATOM   5929  CG  PHE C 218     213.851 191.839 200.820  1.00 52.65           C  
ATOM   5930  CD1 PHE C 218     213.993 190.609 200.228  1.00 52.65           C  
ATOM   5931  CD2 PHE C 218     212.590 192.272 201.137  1.00 52.65           C  
ATOM   5932  CE1 PHE C 218     212.899 189.815 199.988  1.00 52.65           C  
ATOM   5933  CE2 PHE C 218     211.495 191.481 200.897  1.00 52.65           C  
ATOM   5934  CZ  PHE C 218     211.649 190.256 200.323  1.00 52.65           C  
ATOM   5935  N   THR C 219     217.729 194.273 200.671  1.00 54.85           N  
ATOM   5936  CA  THR C 219     218.501 195.507 200.712  1.00 54.85           C  
ATOM   5937  C   THR C 219     219.085 195.833 199.343  1.00 54.85           C  
ATOM   5938  O   THR C 219     219.129 196.998 198.929  1.00 54.85           O  
ATOM   5939  CB  THR C 219     219.587 195.415 201.780  1.00 54.85           C  
ATOM   5940  OG1 THR C 219     220.244 196.676 201.897  1.00 54.85           O  
ATOM   5941  CG2 THR C 219     220.591 194.369 201.455  1.00 54.85           C  
ATOM   5942  N   LEU C 220     219.462 194.813 198.589  1.00 50.28           N  
ATOM   5943  CA  LEU C 220     220.116 195.034 197.313  1.00 50.28           C  
ATOM   5944  C   LEU C 220     219.116 195.455 196.245  1.00 50.28           C  
ATOM   5945  O   LEU C 220     219.465 196.174 195.307  1.00 50.28           O  
ATOM   5946  CB  LEU C 220     220.843 193.754 196.949  1.00 50.28           C  
ATOM   5947  CG  LEU C 220     222.146 193.861 196.219  1.00 50.28           C  
ATOM   5948  CD1 LEU C 220     223.092 194.543 197.147  1.00 50.28           C  
ATOM   5949  CD2 LEU C 220     222.602 192.475 195.993  1.00 50.28           C  
ATOM   5950  N   PHE C 221     217.865 195.035 196.392  1.00 54.06           N  
ATOM   5951  CA  PHE C 221     216.791 195.487 195.523  1.00 54.06           C  
ATOM   5952  C   PHE C 221     216.388 196.907 195.864  1.00 54.06           C  
ATOM   5953  O   PHE C 221     216.104 197.706 194.969  1.00 54.06           O  
ATOM   5954  CB  PHE C 221     215.596 194.544 195.642  1.00 54.06           C  
ATOM   5955  CG  PHE C 221     214.612 194.677 194.532  1.00 54.06           C  
ATOM   5956  CD1 PHE C 221     215.039 194.872 193.235  1.00 54.06           C  
ATOM   5957  CD2 PHE C 221     213.259 194.575 194.774  1.00 54.06           C  
ATOM   5958  CE1 PHE C 221     214.131 194.991 192.203  1.00 54.06           C  
ATOM   5959  CE2 PHE C 221     212.347 194.694 193.745  1.00 54.06           C  
ATOM   5960  CZ  PHE C 221     212.785 194.902 192.459  1.00 54.06           C  
ATOM   5961  N   SER C 222     216.367 197.245 197.151  1.00 54.00           N  
ATOM   5962  CA  SER C 222     216.138 198.631 197.528  1.00 54.00           C  
ATOM   5963  C   SER C 222     217.240 199.530 197.000  1.00 54.00           C  
ATOM   5964  O   SER C 222     217.019 200.723 196.797  1.00 54.00           O  
ATOM   5965  CB  SER C 222     216.029 198.750 199.041  1.00 54.00           C  
ATOM   5966  OG  SER C 222     216.299 200.067 199.457  1.00 54.00           O  
ATOM   5967  N   LEU C 223     218.433 198.988 196.784  1.00 54.39           N  
ATOM   5968  CA  LEU C 223     219.452 199.756 196.072  1.00 54.39           C  
ATOM   5969  C   LEU C 223     219.249 199.753 194.562  1.00 54.39           C  
ATOM   5970  O   LEU C 223     219.619 200.722 193.897  1.00 54.39           O  
ATOM   5971  CB  LEU C 223     220.847 199.240 196.396  1.00 54.39           C  
ATOM   5972  CG  LEU C 223     221.570 199.941 197.536  1.00 54.39           C  
ATOM   5973  CD1 LEU C 223     220.890 199.685 198.852  1.00 54.39           C  
ATOM   5974  CD2 LEU C 223     222.997 199.462 197.573  1.00 54.39           C  
ATOM   5975  N   ALA C 224     218.703 198.679 193.990  1.00 56.56           N  
ATOM   5976  CA  ALA C 224     218.433 198.677 192.554  1.00 56.56           C  
ATOM   5977  C   ALA C 224     217.415 199.749 192.193  1.00 56.56           C  
ATOM   5978  O   ALA C 224     217.737 200.727 191.515  1.00 56.56           O  
ATOM   5979  CB  ALA C 224     217.944 197.301 192.111  1.00 56.56           C  
ATOM   5980  N   THR C 225     216.179 199.585 192.654  1.00 57.47           N  
ATOM   5981  CA  THR C 225     215.161 200.628 192.580  1.00 57.47           C  
ATOM   5982  C   THR C 225     215.484 201.623 193.677  1.00 57.47           C  
ATOM   5983  O   THR C 225     215.113 201.418 194.832  1.00 57.47           O  
ATOM   5984  CB  THR C 225     213.774 200.042 192.790  1.00 57.47           C  
ATOM   5985  OG1 THR C 225     213.697 199.478 194.100  1.00 57.47           O  
ATOM   5986  CG2 THR C 225     213.512 198.950 191.798  1.00 57.47           C  
ATOM   5987  N   VAL C 226     216.120 202.735 193.324  1.00 59.85           N  
ATOM   5988  CA  VAL C 226     216.985 203.459 194.250  1.00 59.85           C  
ATOM   5989  C   VAL C 226     216.266 203.973 195.487  1.00 59.85           C  
ATOM   5990  O   VAL C 226     216.863 204.683 196.300  1.00 59.85           O  
ATOM   5991  CB  VAL C 226     217.682 204.623 193.541  1.00 59.85           C  
ATOM   5992  CG1 VAL C 226     218.571 204.098 192.448  1.00 59.85           C  
ATOM   5993  CG2 VAL C 226     216.650 205.559 192.978  1.00 59.85           C  
ATOM   5994  N   ASP C 227     214.983 203.665 195.627  1.00 64.22           N  
ATOM   5995  CA  ASP C 227     214.244 204.059 196.818  1.00 64.22           C  
ATOM   5996  C   ASP C 227     214.935 203.726 198.133  1.00 64.22           C  
ATOM   5997  O   ASP C 227     214.997 202.560 198.529  1.00 64.22           O  
ATOM   5998  CB  ASP C 227     212.878 203.390 196.832  1.00 64.22           C  
ATOM   5999  CG  ASP C 227     212.029 203.865 197.972  1.00 64.22           C  
ATOM   6000  OD1 ASP C 227     211.519 205.002 197.916  1.00 64.22           O  
ATOM   6001  OD2 ASP C 227     211.913 203.111 198.955  1.00 64.22           O  
ATOM   6002  N   GLY C 228     215.395 204.751 198.847  1.00 64.33           N  
ATOM   6003  CA  GLY C 228     215.816 204.583 200.224  1.00 64.33           C  
ATOM   6004  C   GLY C 228     217.188 204.002 200.436  1.00 64.33           C  
ATOM   6005  O   GLY C 228     217.479 203.528 201.533  1.00 64.33           O  
ATOM   6006  N   TRP C 229     218.053 204.034 199.431  1.00 65.13           N  
ATOM   6007  CA  TRP C 229     219.359 203.423 199.594  1.00 65.13           C  
ATOM   6008  C   TRP C 229     220.232 204.155 200.592  1.00 65.13           C  
ATOM   6009  O   TRP C 229     221.127 203.536 201.176  1.00 65.13           O  
ATOM   6010  CB  TRP C 229     220.070 203.356 198.255  1.00 65.13           C  
ATOM   6011  CG  TRP C 229     220.445 204.673 197.716  1.00 65.13           C  
ATOM   6012  CD1 TRP C 229     219.649 205.531 197.032  1.00 65.13           C  
ATOM   6013  CD2 TRP C 229     221.731 205.287 197.785  1.00 65.13           C  
ATOM   6014  NE1 TRP C 229     220.356 206.649 196.674  1.00 65.13           N  
ATOM   6015  CE2 TRP C 229     221.640 206.518 197.126  1.00 65.13           C  
ATOM   6016  CE3 TRP C 229     222.952 204.915 198.345  1.00 65.13           C  
ATOM   6017  CZ2 TRP C 229     222.718 207.368 197.007  1.00 65.13           C  
ATOM   6018  CZ3 TRP C 229     224.017 205.764 198.225  1.00 65.13           C  
ATOM   6019  CH2 TRP C 229     223.896 206.973 197.568  1.00 65.13           C  
ATOM   6020  N   THR C 230     219.995 205.440 200.817  1.00 72.75           N  
ATOM   6021  CA  THR C 230     220.852 206.208 201.702  1.00 72.75           C  
ATOM   6022  C   THR C 230     220.626 205.895 203.171  1.00 72.75           C  
ATOM   6023  O   THR C 230     221.551 206.039 203.967  1.00 72.75           O  
ATOM   6024  CB  THR C 230     220.673 207.708 201.454  1.00 72.75           C  
ATOM   6025  OG1 THR C 230     221.470 208.441 202.384  1.00 72.75           O  
ATOM   6026  CG2 THR C 230     219.238 208.112 201.610  1.00 72.75           C  
ATOM   6027  N   ASP C 231     219.446 205.420 203.553  1.00 77.23           N  
ATOM   6028  CA  ASP C 231     219.244 205.026 204.942  1.00 77.23           C  
ATOM   6029  C   ASP C 231     220.040 203.765 205.266  1.00 77.23           C  
ATOM   6030  O   ASP C 231     220.726 203.690 206.294  1.00 77.23           O  
ATOM   6031  CB  ASP C 231     217.752 204.825 205.205  1.00 77.23           C  
ATOM   6032  CG  ASP C 231     217.442 204.490 206.653  1.00 77.23           C  
ATOM   6033  OD1 ASP C 231     218.155 203.676 207.277  1.00 77.23           O  
ATOM   6034  OD2 ASP C 231     216.455 205.048 207.174  1.00 77.23           O  
ATOM   6035  N   LEU C 232     219.959 202.761 204.398  1.00 71.68           N  
ATOM   6036  CA  LEU C 232     220.782 201.574 204.577  1.00 71.68           C  
ATOM   6037  C   LEU C 232     222.260 201.927 204.520  1.00 71.68           C  
ATOM   6038  O   LEU C 232     223.058 201.420 205.312  1.00 71.68           O  
ATOM   6039  CB  LEU C 232     220.430 200.536 203.516  1.00 71.68           C  
ATOM   6040  CG  LEU C 232     218.937 200.315 203.330  1.00 71.68           C  
ATOM   6041  CD1 LEU C 232     218.683 199.338 202.226  1.00 71.68           C  
ATOM   6042  CD2 LEU C 232     218.348 199.807 204.610  1.00 71.68           C  
ATOM   6043  N   GLN C 233     222.642 202.809 203.600  1.00 74.48           N  
ATOM   6044  CA  GLN C 233     224.042 203.199 203.510  1.00 74.48           C  
ATOM   6045  C   GLN C 233     224.518 203.866 204.789  1.00 74.48           C  
ATOM   6046  O   GLN C 233     225.632 203.609 205.246  1.00 74.48           O  
ATOM   6047  CB  GLN C 233     224.259 204.129 202.325  1.00 74.48           C  
ATOM   6048  CG  GLN C 233     225.644 204.696 202.265  1.00 74.48           C  
ATOM   6049  CD  GLN C 233     226.688 203.621 202.356  1.00 74.48           C  
ATOM   6050  OE1 GLN C 233     226.809 202.794 201.466  1.00 74.48           O  
ATOM   6051  NE2 GLN C 233     227.454 203.624 203.433  1.00 74.48           N  
ATOM   6052  N   GLU C 234     223.702 204.733 205.385  1.00 81.30           N  
ATOM   6053  CA  GLU C 234     224.163 205.406 206.594  1.00 81.30           C  
ATOM   6054  C   GLU C 234     224.226 204.443 207.771  1.00 81.30           C  
ATOM   6055  O   GLU C 234     225.165 204.505 208.573  1.00 81.30           O  
ATOM   6056  CB  GLU C 234     223.292 206.630 206.899  1.00 81.30           C  
ATOM   6057  CG  GLU C 234     221.817 206.399 207.165  1.00 81.30           C  
ATOM   6058  CD  GLU C 234     221.513 205.837 208.543  1.00 81.30           C  
ATOM   6059  OE1 GLU C 234     220.353 205.441 208.779  1.00 81.30           O  
ATOM   6060  OE2 GLU C 234     222.411 205.830 209.407  1.00 81.30           O  
ATOM   6061  N   GLU C 235     223.254 203.537 207.897  1.00 82.03           N  
ATOM   6062  CA  GLU C 235     223.321 202.601 209.013  1.00 82.03           C  
ATOM   6063  C   GLU C 235     224.420 201.573 208.822  1.00 82.03           C  
ATOM   6064  O   GLU C 235     224.829 200.930 209.790  1.00 82.03           O  
ATOM   6065  CB  GLU C 235     221.974 201.913 209.229  1.00 82.03           C  
ATOM   6066  CG  GLU C 235     221.498 201.042 208.092  1.00 82.03           C  
ATOM   6067  CD  GLU C 235     221.953 199.614 208.231  1.00 82.03           C  
ATOM   6068  OE1 GLU C 235     222.479 199.268 209.307  1.00 82.03           O  
ATOM   6069  OE2 GLU C 235     221.780 198.836 207.270  1.00 82.03           O  
ATOM   6070  N   LEU C 236     224.897 201.401 207.597  1.00 78.40           N  
ATOM   6071  CA  LEU C 236     226.076 200.596 207.318  1.00 78.40           C  
ATOM   6072  C   LEU C 236     227.366 201.399 207.387  1.00 78.40           C  
ATOM   6073  O   LEU C 236     228.451 200.814 207.392  1.00 78.40           O  
ATOM   6074  CB  LEU C 236     225.938 199.976 205.931  1.00 78.40           C  
ATOM   6075  CG  LEU C 236     226.924 198.932 205.453  1.00 78.40           C  
ATOM   6076  CD1 LEU C 236     226.713 197.668 206.231  1.00 78.40           C  
ATOM   6077  CD2 LEU C 236     226.722 198.708 203.977  1.00 78.40           C  
ATOM   6078  N   ASP C 237     227.272 202.722 207.404  1.00 82.07           N  
ATOM   6079  CA  ASP C 237     228.446 203.569 207.512  1.00 82.07           C  
ATOM   6080  C   ASP C 237     228.742 203.983 208.942  1.00 82.07           C  
ATOM   6081  O   ASP C 237     229.881 204.348 209.242  1.00 82.07           O  
ATOM   6082  CB  ASP C 237     228.269 204.820 206.647  1.00 82.07           C  
ATOM   6083  CG  ASP C 237     229.575 205.318 206.056  1.00 82.07           C  
ATOM   6084  OD1 ASP C 237     230.599 205.334 206.771  1.00 82.07           O  
ATOM   6085  OD2 ASP C 237     229.575 205.686 204.862  1.00 82.07           O  
ATOM   6086  N   LYS C 238     227.749 203.948 209.828  1.00 87.53           N  
ATOM   6087  CA  LYS C 238     228.025 204.217 211.232  1.00 87.53           C  
ATOM   6088  C   LYS C 238     228.890 203.137 211.859  1.00 87.53           C  
ATOM   6089  O   LYS C 238     229.494 203.374 212.909  1.00 87.53           O  
ATOM   6090  CB  LYS C 238     226.727 204.344 212.021  1.00 87.53           C  
ATOM   6091  CG  LYS C 238     226.068 203.019 212.334  1.00 87.53           C  
ATOM   6092  CD  LYS C 238     224.742 203.221 213.027  1.00 87.53           C  
ATOM   6093  CE  LYS C 238     224.000 201.911 213.160  1.00 87.53           C  
ATOM   6094  NZ  LYS C 238     222.704 202.085 213.860  1.00 87.53           N  
ATOM   6095  N   ARG C 239     228.964 201.958 211.247  1.00 87.99           N  
ATOM   6096  CA  ARG C 239     229.750 200.856 211.774  1.00 87.99           C  
ATOM   6097  C   ARG C 239     231.173 200.851 211.240  1.00 87.99           C  
ATOM   6098  O   ARG C 239     231.836 199.811 211.273  1.00 87.99           O  
ATOM   6099  CB  ARG C 239     229.053 199.530 211.476  1.00 87.99           C  
ATOM   6100  CG  ARG C 239     227.749 199.378 212.224  1.00 87.99           C  
ATOM   6101  CD  ARG C 239     227.066 198.098 211.866  1.00 87.99           C  
ATOM   6102  NE  ARG C 239     225.629 198.273 211.690  1.00 87.99           N  
ATOM   6103  CZ  ARG C 239     224.721 198.046 212.634  1.00 87.99           C  
ATOM   6104  NH1 ARG C 239     223.434 198.232 212.380  1.00 87.99           N  
ATOM   6105  NH2 ARG C 239     225.096 197.623 213.832  1.00 87.99           N  
ATOM   6106  N   LYS C 240     231.648 201.993 210.755  1.00 91.48           N  
ATOM   6107  CA  LYS C 240     233.047 202.189 210.385  1.00 91.48           C  
ATOM   6108  C   LYS C 240     233.522 201.147 209.375  1.00 91.48           C  
ATOM   6109  O   LYS C 240     234.600 200.566 209.505  1.00 91.48           O  
ATOM   6110  CB  LYS C 240     233.937 202.193 211.628  1.00 91.48           C  
ATOM   6111  CG  LYS C 240     233.695 203.365 212.567  1.00 91.48           C  
ATOM   6112  CD  LYS C 240     233.329 202.881 213.959  1.00 91.48           C  
ATOM   6113  CE  LYS C 240     233.058 204.045 214.901  1.00 91.48           C  
ATOM   6114  NZ  LYS C 240     232.533 203.608 216.227  1.00 91.48           N  
ATOM   6115  N   PHE C 241     232.705 200.912 208.358  1.00 86.44           N  
ATOM   6116  CA  PHE C 241     233.100 200.102 207.216  1.00 86.44           C  
ATOM   6117  C   PHE C 241     233.682 201.023 206.153  1.00 86.44           C  
ATOM   6118  O   PHE C 241     233.008 201.949 205.691  1.00 86.44           O  
ATOM   6119  CB  PHE C 241     231.918 199.318 206.659  1.00 86.44           C  
ATOM   6120  CG  PHE C 241     231.566 198.112 207.458  1.00 86.44           C  
ATOM   6121  CD1 PHE C 241     232.453 197.070 207.583  1.00 86.44           C  
ATOM   6122  CD2 PHE C 241     230.339 198.008 208.064  1.00 86.44           C  
ATOM   6123  CE1 PHE C 241     232.127 195.958 208.311  1.00 86.44           C  
ATOM   6124  CE2 PHE C 241     230.008 196.898 208.788  1.00 86.44           C  
ATOM   6125  CZ  PHE C 241     230.905 195.873 208.912  1.00 86.44           C  
ATOM   6126  N   THR C 242     234.931 200.776 205.774  1.00 87.54           N  
ATOM   6127  CA  THR C 242     235.599 201.676 204.844  1.00 87.54           C  
ATOM   6128  C   THR C 242     235.087 201.493 203.421  1.00 87.54           C  
ATOM   6129  O   THR C 242     234.858 202.475 202.706  1.00 87.54           O  
ATOM   6130  CB  THR C 242     237.108 201.450 204.903  1.00 87.54           C  
ATOM   6131  OG1 THR C 242     237.541 201.458 206.269  1.00 87.54           O  
ATOM   6132  CG2 THR C 242     237.839 202.539 204.138  1.00 87.54           C  
ATOM   6133  N   VAL C 243     234.885 200.242 202.998  1.00 80.93           N  
ATOM   6134  CA  VAL C 243     234.598 199.939 201.598  1.00 80.93           C  
ATOM   6135  C   VAL C 243     233.125 200.072 201.250  1.00 80.93           C  
ATOM   6136  O   VAL C 243     232.766 199.972 200.070  1.00 80.93           O  
ATOM   6137  CB  VAL C 243     235.104 198.516 201.287  1.00 80.93           C  
ATOM   6138  CG1 VAL C 243     234.223 197.483 201.958  1.00 80.93           C  
ATOM   6139  CG2 VAL C 243     235.213 198.270 199.792  1.00 80.93           C  
ATOM   6140  N   SER C 244     232.258 200.322 202.232  1.00 73.11           N  
ATOM   6141  CA  SER C 244     230.822 200.269 201.984  1.00 73.11           C  
ATOM   6142  C   SER C 244     230.387 201.297 200.949  1.00 73.11           C  
ATOM   6143  O   SER C 244     229.549 201.001 200.088  1.00 73.11           O  
ATOM   6144  CB  SER C 244     230.071 200.468 203.292  1.00 73.11           C  
ATOM   6145  OG  SER C 244     230.471 201.677 203.895  1.00 73.11           O  
ATOM   6146  N   ARG C 245     230.936 202.512 201.014  1.00 68.11           N  
ATOM   6147  CA  ARG C 245     230.570 203.537 200.041  1.00 68.11           C  
ATOM   6148  C   ARG C 245     230.885 203.083 198.625  1.00 68.11           C  
ATOM   6149  O   ARG C 245     230.065 203.242 197.718  1.00 68.11           O  
ATOM   6150  CB  ARG C 245     231.292 204.846 200.342  1.00 68.11           C  
ATOM   6151  CG  ARG C 245     230.837 205.534 201.597  1.00 68.11           C  
ATOM   6152  CD  ARG C 245     229.591 206.328 201.345  1.00 68.11           C  
ATOM   6153  NE  ARG C 245     229.147 207.045 202.533  1.00 68.11           N  
ATOM   6154  CZ  ARG C 245     229.612 208.230 202.898  1.00 68.11           C  
ATOM   6155  NH1 ARG C 245     229.148 208.820 203.985  1.00 68.11           N  
ATOM   6156  NH2 ARG C 245     230.542 208.824 202.173  1.00 68.11           N  
ATOM   6157  N   ALA C 246     232.069 202.511 198.415  1.00 64.43           N  
ATOM   6158  CA  ALA C 246     232.427 202.040 197.084  1.00 64.43           C  
ATOM   6159  C   ALA C 246     231.495 200.929 196.620  1.00 64.43           C  
ATOM   6160  O   ALA C 246     231.037 200.931 195.472  1.00 64.43           O  
ATOM   6161  CB  ALA C 246     233.875 201.562 197.072  1.00 64.43           C  
ATOM   6162  N   PHE C 247     231.196 199.980 197.505  1.00 61.57           N  
ATOM   6163  CA  PHE C 247     230.296 198.882 197.169  1.00 61.57           C  
ATOM   6164  C   PHE C 247     228.939 199.404 196.719  1.00 61.57           C  
ATOM   6165  O   PHE C 247     228.449 199.051 195.640  1.00 61.57           O  
ATOM   6166  CB  PHE C 247     230.158 197.966 198.386  1.00 61.57           C  
ATOM   6167  CG  PHE C 247     229.162 196.856 198.226  1.00 61.57           C  
ATOM   6168  CD1 PHE C 247     227.832 197.053 198.522  1.00 61.57           C  
ATOM   6169  CD2 PHE C 247     229.568 195.602 197.839  1.00 61.57           C  
ATOM   6170  CE1 PHE C 247     226.929 196.031 198.394  1.00 61.57           C  
ATOM   6171  CE2 PHE C 247     228.667 194.583 197.715  1.00 61.57           C  
ATOM   6172  CZ  PHE C 247     227.349 194.796 197.993  1.00 61.57           C  
ATOM   6173  N   THR C 248     228.322 200.264 197.526  1.00 63.24           N  
ATOM   6174  CA  THR C 248     226.995 200.744 197.169  1.00 63.24           C  
ATOM   6175  C   THR C 248     227.029 201.622 195.933  1.00 63.24           C  
ATOM   6176  O   THR C 248     226.134 201.531 195.092  1.00 63.24           O  
ATOM   6177  CB  THR C 248     226.361 201.502 198.322  1.00 63.24           C  
ATOM   6178  OG1 THR C 248     227.205 202.595 198.685  1.00 63.24           O  
ATOM   6179  CG2 THR C 248     226.153 200.584 199.498  1.00 63.24           C  
ATOM   6180  N   ILE C 249     228.035 202.487 195.801  1.00 59.03           N  
ATOM   6181  CA  ILE C 249     228.081 203.377 194.647  1.00 59.03           C  
ATOM   6182  C   ILE C 249     228.220 202.576 193.362  1.00 59.03           C  
ATOM   6183  O   ILE C 249     227.505 202.819 192.384  1.00 59.03           O  
ATOM   6184  CB  ILE C 249     229.215 204.402 194.811  1.00 59.03           C  
ATOM   6185  CG1 ILE C 249     228.800 205.479 195.805  1.00 59.03           C  
ATOM   6186  CG2 ILE C 249     229.559 205.029 193.488  1.00 59.03           C  
ATOM   6187  CD1 ILE C 249     229.853 206.497 196.060  1.00 59.03           C  
ATOM   6188  N   LEU C 250     229.112 201.587 193.350  1.00 58.66           N  
ATOM   6189  CA  LEU C 250     229.300 200.803 192.138  1.00 58.66           C  
ATOM   6190  C   LEU C 250     228.092 199.915 191.861  1.00 58.66           C  
ATOM   6191  O   LEU C 250     227.759 199.653 190.698  1.00 58.66           O  
ATOM   6192  CB  LEU C 250     230.576 199.981 192.249  1.00 58.66           C  
ATOM   6193  CG  LEU C 250     230.955 199.156 191.030  1.00 58.66           C  
ATOM   6194  CD1 LEU C 250     231.215 200.073 189.855  1.00 58.66           C  
ATOM   6195  CD2 LEU C 250     232.188 198.340 191.334  1.00 58.66           C  
ATOM   6196  N   PHE C 251     227.398 199.463 192.906  1.00 54.76           N  
ATOM   6197  CA  PHE C 251     226.160 198.743 192.648  1.00 54.76           C  
ATOM   6198  C   PHE C 251     225.099 199.656 192.054  1.00 54.76           C  
ATOM   6199  O   PHE C 251     224.363 199.246 191.154  1.00 54.76           O  
ATOM   6200  CB  PHE C 251     225.626 198.083 193.911  1.00 54.76           C  
ATOM   6201  CG  PHE C 251     224.495 197.146 193.644  1.00 54.76           C  
ATOM   6202  CD1 PHE C 251     224.715 195.947 193.017  1.00 54.76           C  
ATOM   6203  CD2 PHE C 251     223.209 197.487 193.966  1.00 54.76           C  
ATOM   6204  CE1 PHE C 251     223.678 195.093 192.757  1.00 54.76           C  
ATOM   6205  CE2 PHE C 251     222.176 196.636 193.699  1.00 54.76           C  
ATOM   6206  CZ  PHE C 251     222.412 195.440 193.089  1.00 54.76           C  
ATOM   6207  N   ILE C 252     224.988 200.888 192.548  1.00 60.64           N  
ATOM   6208  CA  ILE C 252     223.998 201.809 191.996  1.00 60.64           C  
ATOM   6209  C   ILE C 252     224.297 202.081 190.533  1.00 60.64           C  
ATOM   6210  O   ILE C 252     223.387 202.145 189.703  1.00 60.64           O  
ATOM   6211  CB  ILE C 252     223.942 203.118 192.802  1.00 60.64           C  
ATOM   6212  CG1 ILE C 252     223.567 202.865 194.258  1.00 60.64           C  
ATOM   6213  CG2 ILE C 252     222.927 204.044 192.202  1.00 60.64           C  
ATOM   6214  CD1 ILE C 252     222.350 202.082 194.431  1.00 60.64           C  
ATOM   6215  N   LEU C 253     225.574 202.254 190.194  1.00 62.94           N  
ATOM   6216  CA  LEU C 253     225.934 202.355 188.783  1.00 62.94           C  
ATOM   6217  C   LEU C 253     225.449 201.145 188.005  1.00 62.94           C  
ATOM   6218  O   LEU C 253     224.614 201.273 187.106  1.00 62.94           O  
ATOM   6219  CB  LEU C 253     227.440 202.525 188.602  1.00 62.94           C  
ATOM   6220  CG  LEU C 253     228.021 203.937 188.600  1.00 62.94           C  
ATOM   6221  CD1 LEU C 253     227.997 204.574 189.958  1.00 62.94           C  
ATOM   6222  CD2 LEU C 253     229.431 203.910 188.061  1.00 62.94           C  
ATOM   6223  N   LEU C 254     225.941 199.954 188.347  1.00 62.97           N  
ATOM   6224  CA  LEU C 254     225.711 198.800 187.479  1.00 62.97           C  
ATOM   6225  C   LEU C 254     224.233 198.428 187.395  1.00 62.97           C  
ATOM   6226  O   LEU C 254     223.746 198.044 186.328  1.00 62.97           O  
ATOM   6227  CB  LEU C 254     226.531 197.609 187.957  1.00 62.97           C  
ATOM   6228  CG  LEU C 254     228.043 197.775 187.911  1.00 62.97           C  
ATOM   6229  CD1 LEU C 254     228.717 196.572 188.528  1.00 62.97           C  
ATOM   6230  CD2 LEU C 254     228.496 197.975 186.490  1.00 62.97           C  
ATOM   6231  N   ALA C 255     223.500 198.533 188.500  1.00 63.17           N  
ATOM   6232  CA  ALA C 255     222.175 197.926 188.549  1.00 63.17           C  
ATOM   6233  C   ALA C 255     221.057 198.918 188.272  1.00 63.17           C  
ATOM   6234  O   ALA C 255     219.974 198.518 187.833  1.00 63.17           O  
ATOM   6235  CB  ALA C 255     221.953 197.273 189.904  1.00 63.17           C  
ATOM   6236  N   SER C 256     221.281 200.197 188.609  1.00 70.61           N  
ATOM   6237  CA  SER C 256     220.225 201.235 188.440  1.00 70.61           C  
ATOM   6238  C   SER C 256     220.444 202.083 187.181  1.00 70.61           C  
ATOM   6239  O   SER C 256     219.503 202.174 186.368  1.00 70.61           O  
ATOM   6240  CB  SER C 256     220.134 202.102 189.670  1.00 70.61           C  
ATOM   6241  OG  SER C 256     219.129 203.093 189.515  1.00 70.61           O  
ATOM   6242  N   PHE C 257     221.638 202.663 187.015  1.00 75.07           N  
ATOM   6243  CA  PHE C 257     221.922 203.458 185.829  1.00 75.07           C  
ATOM   6244  C   PHE C 257     221.994 202.572 184.597  1.00 75.07           C  
ATOM   6245  O   PHE C 257     221.185 202.706 183.678  1.00 75.07           O  
ATOM   6246  CB  PHE C 257     223.233 204.228 185.994  1.00 75.07           C  
ATOM   6247  CG  PHE C 257     223.223 205.234 187.103  1.00 75.07           C  
ATOM   6248  CD1 PHE C 257     222.052 205.566 187.755  1.00 75.07           C  
ATOM   6249  CD2 PHE C 257     224.398 205.840 187.501  1.00 75.07           C  
ATOM   6250  CE1 PHE C 257     222.056 206.480 188.775  1.00 75.07           C  
ATOM   6251  CE2 PHE C 257     224.403 206.759 188.520  1.00 75.07           C  
ATOM   6252  CZ  PHE C 257     223.232 207.077 189.159  1.00 75.07           C  
ATOM   6253  N   ILE C 258     222.936 201.634 184.579  1.00 71.70           N  
ATOM   6254  CA  ILE C 258     223.276 200.921 183.354  1.00 71.70           C  
ATOM   6255  C   ILE C 258     222.301 199.791 183.033  1.00 71.70           C  
ATOM   6256  O   ILE C 258     222.185 199.387 181.873  1.00 71.70           O  
ATOM   6257  CB  ILE C 258     224.711 200.394 183.469  1.00 71.70           C  
ATOM   6258  CG1 ILE C 258     225.652 201.538 183.799  1.00 71.70           C  
ATOM   6259  CG2 ILE C 258     225.156 199.727 182.202  1.00 71.70           C  
ATOM   6260  CD1 ILE C 258     226.970 201.078 184.327  1.00 71.70           C  
ATOM   6261  N   PHE C 259     221.574 199.276 184.018  1.00 73.02           N  
ATOM   6262  CA  PHE C 259     220.856 198.034 183.772  1.00 73.02           C  
ATOM   6263  C   PHE C 259     219.379 198.263 183.461  1.00 73.02           C  
ATOM   6264  O   PHE C 259     218.872 197.781 182.446  1.00 73.02           O  
ATOM   6265  CB  PHE C 259     221.010 197.102 184.968  1.00 73.02           C  
ATOM   6266  CG  PHE C 259     220.882 195.666 184.612  1.00 73.02           C  
ATOM   6267  CD1 PHE C 259     221.994 194.943 184.250  1.00 73.02           C  
ATOM   6268  CD2 PHE C 259     219.655 195.049 184.598  1.00 73.02           C  
ATOM   6269  CE1 PHE C 259     221.889 193.623 183.914  1.00 73.02           C  
ATOM   6270  CE2 PHE C 259     219.544 193.731 184.260  1.00 73.02           C  
ATOM   6271  CZ  PHE C 259     220.664 193.016 183.915  1.00 73.02           C  
ATOM   6272  N   LEU C 260     218.667 198.973 184.331  1.00 79.96           N  
ATOM   6273  CA  LEU C 260     217.262 199.243 184.049  1.00 79.96           C  
ATOM   6274  C   LEU C 260     217.114 200.214 182.886  1.00 79.96           C  
ATOM   6275  O   LEU C 260     216.159 200.121 182.104  1.00 79.96           O  
ATOM   6276  CB  LEU C 260     216.583 199.780 185.303  1.00 79.96           C  
ATOM   6277  CG  LEU C 260     216.633 198.802 186.471  1.00 79.96           C  
ATOM   6278  CD1 LEU C 260     215.800 199.309 187.617  1.00 79.96           C  
ATOM   6279  CD2 LEU C 260     216.154 197.432 186.030  1.00 79.96           C  
ATOM   6280  N   ASN C 261     218.054 201.139 182.748  1.00 87.18           N  
ATOM   6281  CA  ASN C 261     218.083 201.994 181.579  1.00 87.18           C  
ATOM   6282  C   ASN C 261     218.577 201.262 180.341  1.00 87.18           C  
ATOM   6283  O   ASN C 261     218.691 201.879 179.280  1.00 87.18           O  
ATOM   6284  CB  ASN C 261     218.946 203.220 181.854  1.00 87.18           C  
ATOM   6285  CG  ASN C 261     218.282 204.191 182.809  1.00 87.18           C  
ATOM   6286  OD1 ASN C 261     217.068 204.166 182.984  1.00 87.18           O  
ATOM   6287  ND2 ASN C 261     219.075 205.047 183.434  1.00 87.18           N  
ATOM   6288  N   MET C 262     218.898 199.976 180.461  1.00 89.97           N  
ATOM   6289  CA  MET C 262     219.056 199.091 179.316  1.00 89.97           C  
ATOM   6290  C   MET C 262     217.798 198.271 179.082  1.00 89.97           C  
ATOM   6291  O   MET C 262     217.462 197.954 177.934  1.00 89.97           O  
ATOM   6292  CB  MET C 262     220.256 198.165 179.535  1.00 89.97           C  
ATOM   6293  CG  MET C 262     220.419 197.066 178.503  1.00 89.97           C  
ATOM   6294  SD  MET C 262     219.692 195.493 178.981  1.00 89.97           S  
ATOM   6295  CE  MET C 262     220.786 194.991 180.295  1.00 89.97           C  
ATOM   6296  N   PHE C 263     217.101 197.927 180.160  1.00 87.70           N  
ATOM   6297  CA  PHE C 263     215.769 197.354 180.049  1.00 87.70           C  
ATOM   6298  C   PHE C 263     214.884 198.247 179.197  1.00 87.70           C  
ATOM   6299  O   PHE C 263     214.171 197.783 178.301  1.00 87.70           O  
ATOM   6300  CB  PHE C 263     215.177 197.197 181.449  1.00 87.70           C  
ATOM   6301  CG  PHE C 263     214.101 196.172 181.550  1.00 87.70           C  
ATOM   6302  CD1 PHE C 263     212.901 196.344 180.908  1.00 87.70           C  
ATOM   6303  CD2 PHE C 263     214.280 195.056 182.326  1.00 87.70           C  
ATOM   6304  CE1 PHE C 263     211.922 195.409 181.009  1.00 87.70           C  
ATOM   6305  CE2 PHE C 263     213.305 194.123 182.436  1.00 87.70           C  
ATOM   6306  CZ  PHE C 263     212.122 194.297 181.778  1.00 87.70           C  
ATOM   6307  N   VAL C 264     214.918 199.547 179.474  1.00 97.02           N  
ATOM   6308  CA  VAL C 264     214.062 200.469 178.735  1.00 97.02           C  
ATOM   6309  C   VAL C 264     214.460 200.528 177.265  1.00 97.02           C  
ATOM   6310  O   VAL C 264     213.597 200.570 176.383  1.00 97.02           O  
ATOM   6311  CB  VAL C 264     214.061 201.854 179.404  1.00 97.02           C  
ATOM   6312  CG1 VAL C 264     215.409 202.461 179.345  1.00 97.02           C  
ATOM   6313  CG2 VAL C 264     213.057 202.757 178.721  1.00 97.02           C  
ATOM   6314  N   GLY C 265     215.760 200.503 176.970  1.00108.31           N  
ATOM   6315  CA  GLY C 265     216.185 200.503 175.579  1.00108.31           C  
ATOM   6316  C   GLY C 265     215.719 199.273 174.823  1.00108.31           C  
ATOM   6317  O   GLY C 265     215.188 199.374 173.708  1.00108.31           O  
ATOM   6318  N   VAL C 266     215.914 198.090 175.416  1.00109.42           N  
ATOM   6319  CA  VAL C 266     215.508 196.865 174.731  1.00109.42           C  
ATOM   6320  C   VAL C 266     214.003 196.874 174.508  1.00109.42           C  
ATOM   6321  O   VAL C 266     213.516 196.486 173.436  1.00109.42           O  
ATOM   6322  CB  VAL C 266     215.963 195.603 175.497  1.00109.42           C  
ATOM   6323  CG1 VAL C 266     217.465 195.557 175.637  1.00109.42           C  
ATOM   6324  CG2 VAL C 266     215.298 195.461 176.842  1.00109.42           C  
ATOM   6325  N   MET C 267     213.244 197.336 175.505  1.00110.57           N  
ATOM   6326  CA  MET C 267     211.802 197.429 175.337  1.00110.57           C  
ATOM   6327  C   MET C 267     211.448 198.365 174.195  1.00110.57           C  
ATOM   6328  O   MET C 267     210.600 198.040 173.352  1.00110.57           O  
ATOM   6329  CB  MET C 267     211.155 197.906 176.636  1.00110.57           C  
ATOM   6330  CG  MET C 267     211.221 196.910 177.780  1.00110.57           C  
ATOM   6331  SD  MET C 267     210.191 195.443 177.588  1.00110.57           S  
ATOM   6332  CE  MET C 267     208.831 196.057 176.606  1.00110.57           C  
ATOM   6333  N   ILE C 268     212.111 199.520 174.135  1.00115.95           N  
ATOM   6334  CA  ILE C 268     211.808 200.497 173.096  1.00115.95           C  
ATOM   6335  C   ILE C 268     211.995 199.880 171.724  1.00115.95           C  
ATOM   6336  O   ILE C 268     211.099 199.933 170.877  1.00115.95           O  
ATOM   6337  CB  ILE C 268     212.678 201.755 173.258  1.00115.95           C  
ATOM   6338  CG1 ILE C 268     212.274 202.532 174.508  1.00115.95           C  
ATOM   6339  CG2 ILE C 268     212.544 202.624 172.040  1.00115.95           C  
ATOM   6340  CD1 ILE C 268     213.211 203.650 174.853  1.00115.95           C  
ATOM   6341  N   MET C 269     213.145 199.256 171.492  1.00126.67           N  
ATOM   6342  CA  MET C 269     213.383 198.827 170.118  1.00126.67           C  
ATOM   6343  C   MET C 269     212.619 197.561 169.750  1.00126.67           C  
ATOM   6344  O   MET C 269     212.181 197.425 168.603  1.00126.67           O  
ATOM   6345  CB  MET C 269     214.861 198.652 169.832  1.00126.67           C  
ATOM   6346  CG  MET C 269     215.697 199.855 170.154  1.00126.67           C  
ATOM   6347  SD  MET C 269     217.371 199.274 170.093  1.00126.67           S  
ATOM   6348  CE  MET C 269     217.185 198.337 168.573  1.00126.67           C  
ATOM   6349  N   HIS C 270     212.442 196.620 170.678  1.00127.60           N  
ATOM   6350  CA  HIS C 270     211.597 195.477 170.356  1.00127.60           C  
ATOM   6351  C   HIS C 270     210.175 195.916 170.025  1.00127.60           C  
ATOM   6352  O   HIS C 270     209.612 195.496 169.003  1.00127.60           O  
ATOM   6353  CB  HIS C 270     211.610 194.473 171.505  1.00127.60           C  
ATOM   6354  CG  HIS C 270     212.759 193.521 171.449  1.00127.60           C  
ATOM   6355  ND1 HIS C 270     214.045 193.888 171.777  1.00127.60           N  
ATOM   6356  CD2 HIS C 270     212.816 192.211 171.116  1.00127.60           C  
ATOM   6357  CE1 HIS C 270     214.848 192.849 171.635  1.00127.60           C  
ATOM   6358  NE2 HIS C 270     214.127 191.818 171.236  1.00127.60           N  
ATOM   6359  N   THR C 271     209.584 196.784 170.855  1.00131.42           N  
ATOM   6360  CA  THR C 271     208.235 197.250 170.562  1.00131.42           C  
ATOM   6361  C   THR C 271     208.194 198.041 169.265  1.00131.42           C  
ATOM   6362  O   THR C 271     207.235 197.930 168.496  1.00131.42           O  
ATOM   6363  CB  THR C 271     207.697 198.093 171.714  1.00131.42           C  
ATOM   6364  OG1 THR C 271     208.552 199.224 171.911  1.00131.42           O  
ATOM   6365  CG2 THR C 271     207.598 197.269 172.992  1.00131.42           C  
ATOM   6366  N   GLU C 272     209.224 198.849 169.006  1.00136.99           N  
ATOM   6367  CA  GLU C 272     209.262 199.643 167.785  1.00136.99           C  
ATOM   6368  C   GLU C 272     209.287 198.763 166.546  1.00136.99           C  
ATOM   6369  O   GLU C 272     208.525 198.984 165.598  1.00136.99           O  
ATOM   6370  CB  GLU C 272     210.476 200.565 167.806  1.00136.99           C  
ATOM   6371  CG  GLU C 272     210.781 201.165 166.459  1.00136.99           C  
ATOM   6372  CD  GLU C 272     211.395 202.535 166.549  1.00136.99           C  
ATOM   6373  OE1 GLU C 272     211.669 203.001 167.673  1.00136.99           O  
ATOM   6374  OE2 GLU C 272     211.626 203.134 165.481  1.00136.99           O  
ATOM   6375  N   ASP C 273     210.171 197.767 166.529  1.00145.46           N  
ATOM   6376  CA  ASP C 273     210.244 196.883 165.376  1.00145.46           C  
ATOM   6377  C   ASP C 273     208.936 196.126 165.185  1.00145.46           C  
ATOM   6378  O   ASP C 273     208.430 196.021 164.059  1.00145.46           O  
ATOM   6379  CB  ASP C 273     211.424 195.925 165.530  1.00145.46           C  
ATOM   6380  CG  ASP C 273     212.768 196.635 165.426  1.00145.46           C  
ATOM   6381  OD1 ASP C 273     212.844 197.665 164.725  1.00145.46           O  
ATOM   6382  OD2 ASP C 273     213.749 196.168 166.040  1.00145.46           O  
ATOM   6383  N   SER C 274     208.351 195.624 166.275  1.00149.81           N  
ATOM   6384  CA  SER C 274     207.067 194.938 166.160  1.00149.81           C  
ATOM   6385  C   SER C 274     206.002 195.854 165.571  1.00149.81           C  
ATOM   6386  O   SER C 274     205.287 195.480 164.629  1.00149.81           O  
ATOM   6387  CB  SER C 274     206.625 194.435 167.531  1.00149.81           C  
ATOM   6388  OG  SER C 274     206.439 195.519 168.424  1.00149.81           O  
ATOM   6389  N   MET C 275     205.887 197.064 166.116  1.00152.47           N  
ATOM   6390  CA  MET C 275     204.827 197.971 165.706  1.00152.47           C  
ATOM   6391  C   MET C 275     204.999 198.389 164.256  1.00152.47           C  
ATOM   6392  O   MET C 275     204.017 198.494 163.512  1.00152.47           O  
ATOM   6393  CB  MET C 275     204.806 199.187 166.631  1.00152.47           C  
ATOM   6394  CG  MET C 275     203.488 199.933 166.659  1.00152.47           C  
ATOM   6395  SD  MET C 275     203.155 200.592 168.304  1.00152.47           S  
ATOM   6396  CE  MET C 275     201.610 201.462 168.047  1.00152.47           C  
ATOM   6397  N   LYS C 276     206.241 198.616 163.826  1.00158.39           N  
ATOM   6398  CA  LYS C 276     206.457 198.996 162.436  1.00158.39           C  
ATOM   6399  C   LYS C 276     206.156 197.835 161.497  1.00158.39           C  
ATOM   6400  O   LYS C 276     205.637 198.045 160.395  1.00158.39           O  
ATOM   6401  CB  LYS C 276     207.881 199.513 162.229  1.00158.39           C  
ATOM   6402  CG  LYS C 276     208.956 198.455 162.267  1.00158.39           C  
ATOM   6403  CD  LYS C 276     210.273 199.019 161.809  1.00158.39           C  
ATOM   6404  CE  LYS C 276     210.210 199.389 160.340  1.00158.39           C  
ATOM   6405  NZ  LYS C 276     210.048 198.200 159.470  1.00158.39           N  
ATOM   6406  N   LYS C 277     206.451 196.601 161.913  1.00162.60           N  
ATOM   6407  CA  LYS C 277     206.070 195.464 161.083  1.00162.60           C  
ATOM   6408  C   LYS C 277     204.555 195.380 160.923  1.00162.60           C  
ATOM   6409  O   LYS C 277     204.050 195.191 159.806  1.00162.60           O  
ATOM   6410  CB  LYS C 277     206.624 194.169 161.672  1.00162.60           C  
ATOM   6411  CG  LYS C 277     208.134 194.058 161.587  1.00162.60           C  
ATOM   6412  CD  LYS C 277     208.624 192.802 162.280  1.00162.60           C  
ATOM   6413  CE  LYS C 277     208.057 191.563 161.614  1.00162.60           C  
ATOM   6414  NZ  LYS C 277     209.040 190.451 161.593  1.00162.60           N  
ATOM   6415  N   PHE C 278     203.813 195.537 162.024  1.00162.54           N  
ATOM   6416  CA  PHE C 278     202.354 195.503 161.924  1.00162.54           C  
ATOM   6417  C   PHE C 278     201.834 196.615 161.020  1.00162.54           C  
ATOM   6418  O   PHE C 278     200.944 196.389 160.185  1.00162.54           O  
ATOM   6419  CB  PHE C 278     201.706 195.608 163.304  1.00162.54           C  
ATOM   6420  CG  PHE C 278     202.313 194.709 164.336  1.00162.54           C  
ATOM   6421  CD1 PHE C 278     202.701 193.419 164.013  1.00162.54           C  
ATOM   6422  CD2 PHE C 278     202.478 195.147 165.641  1.00162.54           C  
ATOM   6423  CE1 PHE C 278     203.257 192.590 164.968  1.00162.54           C  
ATOM   6424  CE2 PHE C 278     203.037 194.325 166.598  1.00162.54           C  
ATOM   6425  CZ  PHE C 278     203.425 193.045 166.263  1.00162.54           C  
ATOM   6426  N   GLU C 279     202.375 197.825 161.172  1.00167.90           N  
ATOM   6427  CA  GLU C 279     201.904 198.938 160.357  1.00167.90           C  
ATOM   6428  C   GLU C 279     202.195 198.704 158.880  1.00167.90           C  
ATOM   6429  O   GLU C 279     201.343 198.972 158.025  1.00167.90           O  
ATOM   6430  CB  GLU C 279     202.533 200.246 160.835  1.00167.90           C  
ATOM   6431  CG  GLU C 279     202.186 200.626 162.268  1.00167.90           C  
ATOM   6432  CD  GLU C 279     200.844 201.317 162.400  1.00167.90           C  
ATOM   6433  OE1 GLU C 279     200.724 202.205 163.269  1.00167.90           O  
ATOM   6434  OE2 GLU C 279     199.907 200.979 161.647  1.00167.90           O  
ATOM   6435  N   ARG C 280     203.390 198.200 158.559  1.00172.97           N  
ATOM   6436  CA  ARG C 280     203.723 197.934 157.162  1.00172.97           C  
ATOM   6437  C   ARG C 280     202.798 196.882 156.570  1.00172.97           C  
ATOM   6438  O   ARG C 280     202.336 197.015 155.426  1.00172.97           O  
ATOM   6439  CB  ARG C 280     205.179 197.488 157.040  1.00172.97           C  
ATOM   6440  CG  ARG C 280     206.158 198.628 156.845  1.00172.97           C  
ATOM   6441  CD  ARG C 280     207.563 198.115 156.588  1.00172.97           C  
ATOM   6442  NE  ARG C 280     208.412 199.159 156.025  1.00172.97           N  
ATOM   6443  CZ  ARG C 280     209.708 199.017 155.777  1.00172.97           C  
ATOM   6444  NH1 ARG C 280     210.315 197.869 156.039  1.00172.97           N  
ATOM   6445  NH2 ARG C 280     210.399 200.024 155.263  1.00172.97           N  
ATOM   6446  N   ASP C 281     202.520 195.826 157.336  1.00175.33           N  
ATOM   6447  CA  ASP C 281     201.639 194.775 156.844  1.00175.33           C  
ATOM   6448  C   ASP C 281     200.246 195.324 156.551  1.00175.33           C  
ATOM   6449  O   ASP C 281     199.671 195.058 155.488  1.00175.33           O  
ATOM   6450  CB  ASP C 281     201.585 193.638 157.860  1.00175.33           C  
ATOM   6451  CG  ASP C 281     202.900 192.889 157.957  1.00175.33           C  
ATOM   6452  OD1 ASP C 281     203.630 192.837 156.947  1.00175.33           O  
ATOM   6453  OD2 ASP C 281     203.203 192.350 159.041  1.00175.33           O  
ATOM   6454  N   LEU C 282     199.704 196.127 157.469  1.00178.85           N  
ATOM   6455  CA  LEU C 282     198.384 196.708 157.240  1.00178.85           C  
ATOM   6456  C   LEU C 282     198.381 197.628 156.022  1.00178.85           C  
ATOM   6457  O   LEU C 282     197.446 197.596 155.206  1.00178.85           O  
ATOM   6458  CB  LEU C 282     197.926 197.456 158.488  1.00178.85           C  
ATOM   6459  CG  LEU C 282     197.807 196.550 159.715  1.00178.85           C  
ATOM   6460  CD1 LEU C 282     197.880 197.345 161.010  1.00178.85           C  
ATOM   6461  CD2 LEU C 282     196.521 195.743 159.647  1.00178.85           C  
ATOM   6462  N   THR C 283     199.426 198.450 155.876  1.00181.99           N  
ATOM   6463  CA  THR C 283     199.489 199.362 154.737  1.00181.99           C  
ATOM   6464  C   THR C 283     199.498 198.598 153.423  1.00181.99           C  
ATOM   6465  O   THR C 283     198.822 198.990 152.464  1.00181.99           O  
ATOM   6466  CB  THR C 283     200.725 200.257 154.826  1.00181.99           C  
ATOM   6467  OG1 THR C 283     201.890 199.448 155.014  1.00181.99           O  
ATOM   6468  CG2 THR C 283     200.601 201.245 155.973  1.00181.99           C  
ATOM   6469  N   LEU C 284     200.268 197.505 153.402  1.00184.67           N  
ATOM   6470  CA  LEU C 284     200.368 196.672 152.178  1.00184.67           C  
ATOM   6471  C   LEU C 284     198.983 196.114 151.868  1.00184.67           C  
ATOM   6472  O   LEU C 284     198.533 196.264 150.715  1.00184.67           O  
ATOM   6473  CB  LEU C 284     201.321 195.511 152.472  1.00184.67           C  
ATOM   6474  CG  LEU C 284     201.688 194.602 151.298  1.00184.67           C  
ATOM   6475  CD1 LEU C 284     201.689 193.146 151.735  1.00184.67           C  
ATOM   6476  CD2 LEU C 284     200.774 194.785 150.093  1.00184.67           C  
ATOM   6477  N   GLU C 285     198.320 195.548 152.881  1.00184.33           N  
ATOM   6478  CA  GLU C 285     196.974 195.012 152.653  1.00184.33           C  
ATOM   6479  C   GLU C 285     196.071 196.055 152.005  1.00184.33           C  
ATOM   6480  O   GLU C 285     195.317 195.752 151.067  1.00184.33           O  
ATOM   6481  CB  GLU C 285     196.330 194.516 153.949  1.00184.33           C  
ATOM   6482  CG  GLU C 285     197.142 193.594 154.826  1.00184.33           C  
ATOM   6483  CD  GLU C 285     198.031 192.661 154.043  1.00184.33           C  
ATOM   6484  OE1 GLU C 285     199.259 192.718 154.229  1.00184.33           O  
ATOM   6485  OE2 GLU C 285     197.498 191.867 153.242  1.00184.33           O  
ATOM   6486  N   ARG C 286     196.120 197.291 152.510  1.00186.09           N  
ATOM   6487  CA  ARG C 286     195.330 198.356 151.895  1.00186.09           C  
ATOM   6488  C   ARG C 286     195.744 198.575 150.444  1.00186.09           C  
ATOM   6489  O   ARG C 286     194.894 198.783 149.568  1.00186.09           O  
ATOM   6490  CB  ARG C 286     195.475 199.649 152.692  1.00186.09           C  
ATOM   6491  CG  ARG C 286     194.994 199.561 154.123  1.00186.09           C  
ATOM   6492  CD  ARG C 286     195.233 200.878 154.831  1.00186.09           C  
ATOM   6493  NE  ARG C 286     194.897 200.820 156.248  1.00186.09           N  
ATOM   6494  CZ  ARG C 286     195.188 201.780 157.118  1.00186.09           C  
ATOM   6495  NH1 ARG C 286     195.825 202.872 156.715  1.00186.09           N  
ATOM   6496  NH2 ARG C 286     194.845 201.649 158.391  1.00186.09           N  
ATOM   6497  N   ASN C 287     197.052 198.534 150.177  1.00191.93           N  
ATOM   6498  CA  ASN C 287     197.542 198.631 148.805  1.00191.93           C  
ATOM   6499  C   ASN C 287     196.958 197.527 147.930  1.00191.93           C  
ATOM   6500  O   ASN C 287     196.521 197.782 146.803  1.00191.93           O  
ATOM   6501  CB  ASN C 287     199.071 198.573 148.785  1.00191.93           C  
ATOM   6502  CG  ASN C 287     199.712 199.949 148.739  1.00191.93           C  
ATOM   6503  OD1 ASN C 287     199.157 200.887 148.169  1.00191.93           O  
ATOM   6504  ND2 ASN C 287     200.889 200.074 149.343  1.00191.93           N  
ATOM   6505  N   LEU C 288     196.954 196.288 148.431  1.00191.70           N  
ATOM   6506  CA  LEU C 288     196.417 195.171 147.655  1.00191.70           C  
ATOM   6507  C   LEU C 288     194.947 195.387 147.324  1.00191.70           C  
ATOM   6508  O   LEU C 288     194.514 195.155 146.186  1.00191.70           O  
ATOM   6509  CB  LEU C 288     196.592 193.858 148.420  1.00191.70           C  
ATOM   6510  CG  LEU C 288     198.005 193.364 148.740  1.00191.70           C  
ATOM   6511  CD1 LEU C 288     197.960 191.924 149.231  1.00191.70           C  
ATOM   6512  CD2 LEU C 288     198.937 193.509 147.543  1.00191.70           C  
ATOM   6513  N   ALA C 289     194.164 195.831 148.310  1.00196.69           N  
ATOM   6514  CA  ALA C 289     192.748 196.092 148.060  1.00196.69           C  
ATOM   6515  C   ALA C 289     192.562 197.180 147.007  1.00196.69           C  
ATOM   6516  O   ALA C 289     191.727 197.046 146.102  1.00196.69           O  
ATOM   6517  CB  ALA C 289     192.045 196.478 149.361  1.00196.69           C  
ATOM   6518  N   ILE C 290     193.340 198.261 147.105  1.00197.53           N  
ATOM   6519  CA  ILE C 290     193.191 199.370 146.165  1.00197.53           C  
ATOM   6520  C   ILE C 290     193.547 198.926 144.750  1.00197.53           C  
ATOM   6521  O   ILE C 290     192.866 199.282 143.779  1.00197.53           O  
ATOM   6522  CB  ILE C 290     194.036 200.575 146.612  1.00197.53           C  
ATOM   6523  CG1 ILE C 290     193.509 201.134 147.931  1.00197.53           C  
ATOM   6524  CG2 ILE C 290     193.996 201.663 145.568  1.00197.53           C  
ATOM   6525  CD1 ILE C 290     194.329 202.283 148.472  1.00197.53           C  
ATOM   6526  N   MET C 291     194.624 198.150 144.607  1.00197.82           N  
ATOM   6527  CA  MET C 291     194.990 197.678 143.274  1.00197.82           C  
ATOM   6528  C   MET C 291     193.969 196.693 142.712  1.00197.82           C  
ATOM   6529  O   MET C 291     193.707 196.713 141.502  1.00197.82           O  
ATOM   6530  CB  MET C 291     196.389 197.060 143.274  1.00197.82           C  
ATOM   6531  CG  MET C 291     197.439 197.886 143.987  1.00197.82           C  
ATOM   6532  SD  MET C 291     197.309 199.644 143.607  1.00197.82           S  
ATOM   6533  CE  MET C 291     198.790 200.274 144.389  1.00197.82           C  
ATOM   6534  N   GLU C 292     193.379 195.831 143.549  1.00196.84           N  
ATOM   6535  CA  GLU C 292     192.313 194.969 143.042  1.00196.84           C  
ATOM   6536  C   GLU C 292     191.129 195.794 142.557  1.00196.84           C  
ATOM   6537  O   GLU C 292     190.536 195.496 141.514  1.00196.84           O  
ATOM   6538  CB  GLU C 292     191.848 193.964 144.096  1.00196.84           C  
ATOM   6539  CG  GLU C 292     192.847 192.895 144.470  1.00196.84           C  
ATOM   6540  CD  GLU C 292     192.287 191.949 145.514  1.00196.84           C  
ATOM   6541  OE1 GLU C 292     191.176 192.215 146.016  1.00196.84           O  
ATOM   6542  OE2 GLU C 292     192.953 190.942 145.832  1.00196.84           O  
ATOM   6543  N   GLU C 293     190.757 196.830 143.312  1.00198.18           N  
ATOM   6544  CA  GLU C 293     189.633 197.660 142.889  1.00198.18           C  
ATOM   6545  C   GLU C 293     189.942 198.387 141.584  1.00198.18           C  
ATOM   6546  O   GLU C 293     189.078 198.498 140.705  1.00198.18           O  
ATOM   6547  CB  GLU C 293     189.258 198.648 143.993  1.00198.18           C  
ATOM   6548  CG  GLU C 293     188.565 197.995 145.182  1.00198.18           C  
ATOM   6549  CD  GLU C 293     187.792 198.989 146.026  1.00198.18           C  
ATOM   6550  OE1 GLU C 293     187.919 200.207 145.780  1.00198.18           O  
ATOM   6551  OE2 GLU C 293     187.054 198.551 146.933  1.00198.18           O  
ATOM   6552  N   LYS C 294     191.173 198.881 141.435  1.00198.33           N  
ATOM   6553  CA  LYS C 294     191.561 199.530 140.185  1.00198.33           C  
ATOM   6554  C   LYS C 294     191.508 198.554 139.015  1.00198.33           C  
ATOM   6555  O   LYS C 294     191.027 198.898 137.924  1.00198.33           O  
ATOM   6556  CB  LYS C 294     192.959 200.131 140.320  1.00198.33           C  
ATOM   6557  CG  LYS C 294     193.019 201.350 141.219  1.00198.33           C  
ATOM   6558  CD  LYS C 294     194.394 201.520 141.839  1.00198.33           C  
ATOM   6559  CE  LYS C 294     194.616 202.958 142.284  1.00198.33           C  
ATOM   6560  NZ  LYS C 294     195.779 203.089 143.204  1.00198.33           N  
ATOM   6561  N   GLN C 295     192.002 197.331 139.220  1.00200.89           N  
ATOM   6562  CA  GLN C 295     191.956 196.334 138.157  1.00200.89           C  
ATOM   6563  C   GLN C 295     190.519 195.989 137.789  1.00200.89           C  
ATOM   6564  O   GLN C 295     190.209 195.777 136.613  1.00200.89           O  
ATOM   6565  CB  GLN C 295     192.725 195.082 138.575  1.00200.89           C  
ATOM   6566  CG  GLN C 295     192.818 194.017 137.492  1.00200.89           C  
ATOM   6567  CD  GLN C 295     193.473 194.525 136.218  1.00200.89           C  
ATOM   6568  OE1 GLN C 295     193.038 194.201 135.112  1.00200.89           O  
ATOM   6569  NE2 GLN C 295     194.525 195.321 136.367  1.00200.89           N  
ATOM   6570  N   ILE C 296     189.625 195.932 138.778  1.00201.38           N  
ATOM   6571  CA  ILE C 296     188.221 195.652 138.484  1.00201.38           C  
ATOM   6572  C   ILE C 296     187.590 196.810 137.713  1.00201.38           C  
ATOM   6573  O   ILE C 296     186.756 196.599 136.823  1.00201.38           O  
ATOM   6574  CB  ILE C 296     187.459 195.334 139.785  1.00201.38           C  
ATOM   6575  CG1 ILE C 296     188.011 194.051 140.410  1.00201.38           C  
ATOM   6576  CG2 ILE C 296     185.970 195.174 139.514  1.00201.38           C  
ATOM   6577  CD1 ILE C 296     187.579 193.823 141.838  1.00201.38           C  
ATOM   6578  N   ILE C 297     187.981 198.047 138.033  1.00201.67           N  
ATOM   6579  CA  ILE C 297     187.519 199.193 137.248  1.00201.67           C  
ATOM   6580  C   ILE C 297     187.959 199.058 135.795  1.00201.67           C  
ATOM   6581  O   ILE C 297     187.165 199.266 134.865  1.00201.67           O  
ATOM   6582  CB  ILE C 297     188.026 200.514 137.860  1.00201.67           C  
ATOM   6583  CG1 ILE C 297     187.129 200.967 139.010  1.00201.67           C  
ATOM   6584  CG2 ILE C 297     188.116 201.599 136.795  1.00201.67           C  
ATOM   6585  CD1 ILE C 297     187.609 202.239 139.676  1.00201.67           C  
ATOM   6586  N   LEU C 298     189.231 198.715 135.578  1.00201.20           N  
ATOM   6587  CA  LEU C 298     189.720 198.526 134.214  1.00201.20           C  
ATOM   6588  C   LEU C 298     188.975 197.393 133.513  1.00201.20           C  
ATOM   6589  O   LEU C 298     188.646 197.495 132.324  1.00201.20           O  
ATOM   6590  CB  LEU C 298     191.227 198.261 134.232  1.00201.20           C  
ATOM   6591  CG  LEU C 298     192.129 199.457 134.566  1.00201.20           C  
ATOM   6592  CD1 LEU C 298     193.566 199.017 134.803  1.00201.20           C  
ATOM   6593  CD2 LEU C 298     192.072 200.518 133.471  1.00201.20           C  
ATOM   6594  N   LYS C 299     188.694 196.307 134.241  1.00199.34           N  
ATOM   6595  CA  LYS C 299     187.955 195.183 133.673  1.00199.34           C  
ATOM   6596  C   LYS C 299     186.564 195.606 133.222  1.00199.34           C  
ATOM   6597  O   LYS C 299     186.115 195.238 132.128  1.00199.34           O  
ATOM   6598  CB  LYS C 299     187.843 194.055 134.699  1.00199.34           C  
ATOM   6599  CG  LYS C 299     189.126 193.297 134.983  1.00199.34           C  
ATOM   6600  CD  LYS C 299     188.894 192.259 136.071  1.00199.34           C  
ATOM   6601  CE  LYS C 299     190.149 191.460 136.371  1.00199.34           C  
ATOM   6602  NZ  LYS C 299     189.895 190.417 137.407  1.00199.34           N  
ATOM   6603  N   ARG C 300     185.862 196.372 134.060  1.00199.04           N  
ATOM   6604  CA  ARG C 300     184.521 196.819 133.697  1.00199.04           C  
ATOM   6605  C   ARG C 300     184.559 197.789 132.521  1.00199.04           C  
ATOM   6606  O   ARG C 300     183.680 197.754 131.654  1.00199.04           O  
ATOM   6607  CB  ARG C 300     183.829 197.454 134.901  1.00199.04           C  
ATOM   6608  CG  ARG C 300     183.493 196.464 135.997  1.00199.04           C  
ATOM   6609  CD  ARG C 300     182.783 197.143 137.152  1.00199.04           C  
ATOM   6610  NE  ARG C 300     182.792 196.312 138.350  1.00199.04           N  
ATOM   6611  CZ  ARG C 300     182.431 196.738 139.553  1.00199.04           C  
ATOM   6612  NH1 ARG C 300     182.024 197.988 139.721  1.00199.04           N  
ATOM   6613  NH2 ARG C 300     182.475 195.912 140.589  1.00199.04           N  
ATOM   6614  N   GLN C 301     185.565 198.667 132.478  1.00199.83           N  
ATOM   6615  CA  GLN C 301     185.698 199.568 131.336  1.00199.83           C  
ATOM   6616  C   GLN C 301     185.894 198.786 130.043  1.00199.83           C  
ATOM   6617  O   GLN C 301     185.257 199.081 129.021  1.00199.83           O  
ATOM   6618  CB  GLN C 301     186.867 200.529 131.556  1.00199.83           C  
ATOM   6619  CG  GLN C 301     186.986 201.624 130.506  1.00199.83           C  
ATOM   6620  CD  GLN C 301     187.817 201.202 129.308  1.00199.83           C  
ATOM   6621  OE1 GLN C 301     188.616 200.270 129.388  1.00199.83           O  
ATOM   6622  NE2 GLN C 301     187.632 201.892 128.189  1.00199.83           N  
ATOM   6623  N   GLN C 302     186.775 197.782 130.072  1.00198.71           N  
ATOM   6624  CA  GLN C 302     187.004 196.967 128.885  1.00198.71           C  
ATOM   6625  C   GLN C 302     185.742 196.219 128.483  1.00198.71           C  
ATOM   6626  O   GLN C 302     185.414 196.133 127.294  1.00198.71           O  
ATOM   6627  CB  GLN C 302     188.151 195.989 129.135  1.00198.71           C  
ATOM   6628  CG  GLN C 302     189.499 196.657 129.304  1.00198.71           C  
ATOM   6629  CD  GLN C 302     190.622 195.660 129.485  1.00198.71           C  
ATOM   6630  OE1 GLN C 302     190.403 194.533 129.928  1.00198.71           O  
ATOM   6631  NE2 GLN C 302     191.837 196.071 129.146  1.00198.71           N  
ATOM   6632  N   GLU C 303     185.017 195.676 129.464  1.00197.38           N  
ATOM   6633  CA  GLU C 303     183.779 194.965 129.169  1.00197.38           C  
ATOM   6634  C   GLU C 303     182.753 195.884 128.516  1.00197.38           C  
ATOM   6635  O   GLU C 303     182.105 195.507 127.531  1.00197.38           O  
ATOM   6636  CB  GLU C 303     183.214 194.358 130.454  1.00197.38           C  
ATOM   6637  CG  GLU C 303     183.857 193.043 130.876  1.00197.38           C  
ATOM   6638  CD  GLU C 303     183.339 192.547 132.210  1.00197.38           C  
ATOM   6639  OE1 GLU C 303     182.820 193.376 132.985  1.00197.38           O  
ATOM   6640  OE2 GLU C 303     183.437 191.332 132.480  1.00197.38           O  
ATOM   6641  N   GLU C 304     182.591 197.094 129.058  1.00195.20           N  
ATOM   6642  CA  GLU C 304     181.623 198.038 128.509  1.00195.20           C  
ATOM   6643  C   GLU C 304     181.993 198.446 127.089  1.00195.20           C  
ATOM   6644  O   GLU C 304     181.127 198.504 126.206  1.00195.20           O  
ATOM   6645  CB  GLU C 304     181.522 199.268 129.411  1.00195.20           C  
ATOM   6646  CG  GLU C 304     180.878 198.998 130.759  1.00195.20           C  
ATOM   6647  CD  GLU C 304     180.855 200.227 131.647  1.00195.20           C  
ATOM   6648  OE1 GLU C 304     181.381 201.277 131.222  1.00195.20           O  
ATOM   6649  OE2 GLU C 304     180.314 200.144 132.771  1.00195.20           O  
ATOM   6650  N   VAL C 305     183.276 198.730 126.847  1.00195.26           N  
ATOM   6651  CA  VAL C 305     183.698 199.105 125.501  1.00195.26           C  
ATOM   6652  C   VAL C 305     183.497 197.944 124.533  1.00195.26           C  
ATOM   6653  O   VAL C 305     183.068 198.141 123.390  1.00195.26           O  
ATOM   6654  CB  VAL C 305     185.155 199.601 125.510  1.00195.26           C  
ATOM   6655  CG1 VAL C 305     185.732 199.584 124.109  1.00195.26           C  
ATOM   6656  CG2 VAL C 305     185.220 201.006 126.083  1.00195.26           C  
ATOM   6657  N   ASN C 306     183.793 196.716 124.972  1.00195.35           N  
ATOM   6658  CA  ASN C 306     183.596 195.558 124.104  1.00195.35           C  
ATOM   6659  C   ASN C 306     182.128 195.379 123.739  1.00195.35           C  
ATOM   6660  O   ASN C 306     181.796 195.134 122.571  1.00195.35           O  
ATOM   6661  CB  ASN C 306     184.137 194.297 124.776  1.00195.35           C  
ATOM   6662  CG  ASN C 306     185.497 193.895 124.247  1.00195.35           C  
ATOM   6663  OD1 ASN C 306     185.885 194.280 123.145  1.00195.35           O  
ATOM   6664  ND2 ASN C 306     186.227 193.110 125.028  1.00195.35           N  
ATOM   6665  N   ARG C 307     181.232 195.500 124.720  1.00192.30           N  
ATOM   6666  CA  ARG C 307     179.807 195.375 124.424  1.00192.30           C  
ATOM   6667  C   ARG C 307     179.335 196.492 123.503  1.00192.30           C  
ATOM   6668  O   ARG C 307     178.508 196.263 122.612  1.00192.30           O  
ATOM   6669  CB  ARG C 307     178.994 195.363 125.716  1.00192.30           C  
ATOM   6670  CG  ARG C 307     179.215 194.127 126.558  1.00192.30           C  
ATOM   6671  CD  ARG C 307     179.043 194.434 128.028  1.00192.30           C  
ATOM   6672  NE  ARG C 307     179.576 193.370 128.868  1.00192.30           N  
ATOM   6673  CZ  ARG C 307     179.983 193.547 130.119  1.00192.30           C  
ATOM   6674  NH1 ARG C 307     179.918 194.751 130.671  1.00192.30           N  
ATOM   6675  NH2 ARG C 307     180.457 192.522 130.814  1.00192.30           N  
ATOM   6676  N   LEU C 308     179.845 197.710 123.704  1.00188.56           N  
ATOM   6677  CA  LEU C 308     179.461 198.812 122.831  1.00188.56           C  
ATOM   6678  C   LEU C 308     179.927 198.572 121.399  1.00188.56           C  
ATOM   6679  O   LEU C 308     179.188 198.846 120.446  1.00188.56           O  
ATOM   6680  CB  LEU C 308     180.017 200.128 123.374  1.00188.56           C  
ATOM   6681  CG  LEU C 308     179.249 200.698 124.568  1.00188.56           C  
ATOM   6682  CD1 LEU C 308     180.026 201.829 125.232  1.00188.56           C  
ATOM   6683  CD2 LEU C 308     177.866 201.166 124.133  1.00188.56           C  
ATOM   6684  N   MET C 309     181.148 198.057 121.227  1.00182.87           N  
ATOM   6685  CA  MET C 309     181.630 197.734 119.886  1.00182.87           C  
ATOM   6686  C   MET C 309     180.797 196.628 119.254  1.00182.87           C  
ATOM   6687  O   MET C 309     180.512 196.665 118.051  1.00182.87           O  
ATOM   6688  CB  MET C 309     183.107 197.337 119.928  1.00182.87           C  
ATOM   6689  CG  MET C 309     184.031 198.405 120.490  1.00182.87           C  
ATOM   6690  SD  MET C 309     185.640 198.431 119.676  1.00182.87           S  
ATOM   6691  CE  MET C 309     185.241 199.276 118.149  1.00182.87           C  
ATOM   6692  N   ASN C 310     180.406 195.629 120.050  1.00181.34           N  
ATOM   6693  CA  ASN C 310     179.546 194.567 119.535  1.00181.34           C  
ATOM   6694  C   ASN C 310     178.210 195.126 119.060  1.00181.34           C  
ATOM   6695  O   ASN C 310     177.713 194.747 117.992  1.00181.34           O  
ATOM   6696  CB  ASN C 310     179.332 193.503 120.611  1.00181.34           C  
ATOM   6697  CG  ASN C 310     180.622 192.816 121.016  1.00181.34           C  
ATOM   6698  OD1 ASN C 310     181.583 192.773 120.248  1.00181.34           O  
ATOM   6699  ND2 ASN C 310     180.652 192.283 122.231  1.00181.34           N  
ATOM   6700  N   THR C 311     177.618 196.032 119.842  1.00178.12           N  
ATOM   6701  CA  THR C 311     176.355 196.648 119.446  1.00178.12           C  
ATOM   6702  C   THR C 311     176.521 197.503 118.195  1.00178.12           C  
ATOM   6703  O   THR C 311     175.641 197.520 117.325  1.00178.12           O  
ATOM   6704  CB  THR C 311     175.797 197.490 120.592  1.00178.12           C  
ATOM   6705  OG1 THR C 311     176.807 198.397 121.051  1.00178.12           O  
ATOM   6706  CG2 THR C 311     175.357 196.599 121.747  1.00178.12           C  
ATOM   6707  N   GLN C 312     177.636 198.231 118.096  1.00175.74           N  
ATOM   6708  CA  GLN C 312     177.891 199.058 116.921  1.00175.74           C  
ATOM   6709  C   GLN C 312     178.008 198.205 115.666  1.00175.74           C  
ATOM   6710  O   GLN C 312     177.385 198.497 114.639  1.00175.74           O  
ATOM   6711  CB  GLN C 312     179.167 199.875 117.123  1.00175.74           C  
ATOM   6712  CG  GLN C 312     179.030 201.059 118.055  1.00175.74           C  
ATOM   6713  CD  GLN C 312     180.377 201.609 118.476  1.00175.74           C  
ATOM   6714  OE1 GLN C 312     181.356 200.869 118.573  1.00175.74           O  
ATOM   6715  NE2 GLN C 312     180.435 202.914 118.726  1.00175.74           N  
ATOM   6716  N   LYS C 313     178.811 197.140 115.734  1.00172.24           N  
ATOM   6717  CA  LYS C 313     179.022 196.293 114.565  1.00172.24           C  
ATOM   6718  C   LYS C 313     177.744 195.562 114.178  1.00172.24           C  
ATOM   6719  O   LYS C 313     177.336 195.578 113.011  1.00172.24           O  
ATOM   6720  CB  LYS C 313     180.151 195.300 114.841  1.00172.24           C  
ATOM   6721  CG  LYS C 313     181.491 195.964 115.119  1.00172.24           C  
ATOM   6722  CD  LYS C 313     182.484 195.001 115.743  1.00172.24           C  
ATOM   6723  CE  LYS C 313     183.718 195.745 116.221  1.00172.24           C  
ATOM   6724  NZ  LYS C 313     184.721 194.843 116.854  1.00172.24           N  
ATOM   6725  N   SER C 314     177.088 194.928 115.152  1.00170.06           N  
ATOM   6726  CA  SER C 314     175.891 194.146 114.871  1.00170.06           C  
ATOM   6727  C   SER C 314     174.687 195.019 114.542  1.00170.06           C  
ATOM   6728  O   SER C 314     173.658 194.490 114.109  1.00170.06           O  
ATOM   6729  CB  SER C 314     175.576 193.238 116.059  1.00170.06           C  
ATOM   6730  OG  SER C 314     175.524 193.981 117.265  1.00170.06           O  
ATOM   6731  N   GLY C 315     174.789 196.330 114.738  1.00164.60           N  
ATOM   6732  CA  GLY C 315     173.702 197.237 114.414  1.00164.60           C  
ATOM   6733  C   GLY C 315     174.049 198.227 113.318  1.00164.60           C  
ATOM   6734  O   GLY C 315     173.445 198.223 112.246  1.00164.60           O  
TER    6735      GLY C 315                                                      
ATOM   6736  N   ASP D  51     252.349 165.778 159.957  1.00153.15           N  
ATOM   6737  CA  ASP D  51     251.369 166.840 160.138  1.00153.15           C  
ATOM   6738  C   ASP D  51     249.956 166.295 159.969  1.00153.15           C  
ATOM   6739  O   ASP D  51     248.999 166.851 160.494  1.00153.15           O  
ATOM   6740  CB  ASP D  51     251.624 167.973 159.144  1.00153.15           C  
ATOM   6741  CG  ASP D  51     251.312 169.340 159.718  1.00153.15           C  
ATOM   6742  OD1 ASP D  51     250.335 169.464 160.475  1.00153.15           O  
ATOM   6743  OD2 ASP D  51     252.049 170.297 159.413  1.00153.15           O  
ATOM   6744  N   VAL D  52     249.849 165.180 159.245  1.00154.56           N  
ATOM   6745  CA  VAL D  52     248.547 164.639 158.865  1.00154.56           C  
ATOM   6746  C   VAL D  52     247.739 164.231 160.088  1.00154.56           C  
ATOM   6747  O   VAL D  52     246.507 164.338 160.095  1.00154.56           O  
ATOM   6748  CB  VAL D  52     248.742 163.454 157.896  1.00154.56           C  
ATOM   6749  CG1 VAL D  52     247.405 162.844 157.502  1.00154.56           C  
ATOM   6750  CG2 VAL D  52     249.509 163.894 156.668  1.00154.56           C  
ATOM   6751  N   GLN D  53     248.409 163.779 161.142  1.00155.73           N  
ATOM   6752  CA  GLN D  53     247.706 163.116 162.231  1.00155.73           C  
ATOM   6753  C   GLN D  53     247.061 164.111 163.190  1.00155.73           C  
ATOM   6754  O   GLN D  53     245.861 164.018 163.474  1.00155.73           O  
ATOM   6755  CB  GLN D  53     248.663 162.188 162.984  1.00155.73           C  
ATOM   6756  CG  GLN D  53     249.978 162.813 163.438  1.00155.73           C  
ATOM   6757  CD  GLN D  53     250.977 163.001 162.314  1.00155.73           C  
ATOM   6758  OE1 GLN D  53     251.246 162.081 161.541  1.00155.73           O  
ATOM   6759  NE2 GLN D  53     251.534 164.202 162.217  1.00155.73           N  
ATOM   6760  N   GLU D  54     247.835 165.075 163.692  1.00155.42           N  
ATOM   6761  CA  GLU D  54     247.389 165.836 164.853  1.00155.42           C  
ATOM   6762  C   GLU D  54     246.152 166.669 164.567  1.00155.42           C  
ATOM   6763  O   GLU D  54     245.438 167.037 165.506  1.00155.42           O  
ATOM   6764  CB  GLU D  54     248.511 166.726 165.371  1.00155.42           C  
ATOM   6765  CG  GLU D  54     248.873 167.858 164.459  1.00155.42           C  
ATOM   6766  CD  GLU D  54     249.856 167.422 163.406  1.00155.42           C  
ATOM   6767  OE1 GLU D  54     250.014 166.199 163.205  1.00155.42           O  
ATOM   6768  OE2 GLU D  54     250.500 168.299 162.805  1.00155.42           O  
ATOM   6769  N   PHE D  55     245.873 166.978 163.300  1.00155.83           N  
ATOM   6770  CA  PHE D  55     244.623 167.666 163.004  1.00155.83           C  
ATOM   6771  C   PHE D  55     243.437 166.847 163.484  1.00155.83           C  
ATOM   6772  O   PHE D  55     242.472 167.399 164.026  1.00155.83           O  
ATOM   6773  CB  PHE D  55     244.493 167.955 161.513  1.00155.83           C  
ATOM   6774  CG  PHE D  55     245.491 168.945 160.997  1.00155.83           C  
ATOM   6775  CD1 PHE D  55     245.295 170.305 161.174  1.00155.83           C  
ATOM   6776  CD2 PHE D  55     246.591 168.520 160.279  1.00155.83           C  
ATOM   6777  CE1 PHE D  55     246.209 171.218 160.684  1.00155.83           C  
ATOM   6778  CE2 PHE D  55     247.500 169.426 159.780  1.00155.83           C  
ATOM   6779  CZ  PHE D  55     247.314 170.775 159.984  1.00155.83           C  
ATOM   6780  N   ILE D  56     243.495 165.527 163.303  1.00153.55           N  
ATOM   6781  CA  ILE D  56     242.444 164.667 163.837  1.00153.55           C  
ATOM   6782  C   ILE D  56     242.398 164.779 165.354  1.00153.55           C  
ATOM   6783  O   ILE D  56     241.321 164.887 165.952  1.00153.55           O  
ATOM   6784  CB  ILE D  56     242.657 163.214 163.376  1.00153.55           C  
ATOM   6785  CG1 ILE D  56     242.374 163.085 161.881  1.00153.55           C  
ATOM   6786  CG2 ILE D  56     241.751 162.279 164.145  1.00153.55           C  
ATOM   6787  CD1 ILE D  56     242.623 161.702 161.333  1.00153.55           C  
ATOM   6788  N   THR D  57     243.567 164.773 165.999  1.00153.10           N  
ATOM   6789  CA  THR D  57     243.614 165.034 167.434  1.00153.10           C  
ATOM   6790  C   THR D  57     243.097 166.430 167.744  1.00153.10           C  
ATOM   6791  O   THR D  57     242.404 166.635 168.745  1.00153.10           O  
ATOM   6792  CB  THR D  57     245.036 164.876 167.963  1.00153.10           C  
ATOM   6793  OG1 THR D  57     245.794 166.049 167.642  1.00153.10           O  
ATOM   6794  CG2 THR D  57     245.702 163.668 167.338  1.00153.10           C  
ATOM   6795  N   GLN D  58     243.438 167.409 166.904  1.00150.39           N  
ATOM   6796  CA  GLN D  58     242.831 168.725 167.040  1.00150.39           C  
ATOM   6797  C   GLN D  58     241.342 168.665 166.737  1.00150.39           C  
ATOM   6798  O   GLN D  58     240.538 169.342 167.388  1.00150.39           O  
ATOM   6799  CB  GLN D  58     243.520 169.723 166.117  1.00150.39           C  
ATOM   6800  CG  GLN D  58     244.963 169.992 166.470  1.00150.39           C  
ATOM   6801  CD  GLN D  58     245.114 170.603 167.836  1.00150.39           C  
ATOM   6802  OE1 GLN D  58     245.603 169.958 168.761  1.00150.39           O  
ATOM   6803  NE2 GLN D  58     244.675 171.848 167.982  1.00150.39           N  
ATOM   6804  N   MET D  59     240.984 167.806 165.773  1.00151.64           N  
ATOM   6805  CA  MET D  59     239.561 167.580 165.404  1.00151.64           C  
ATOM   6806  C   MET D  59     238.863 166.993 166.636  1.00151.64           C  
ATOM   6807  O   MET D  59     237.738 167.434 166.946  1.00151.64           O  
ATOM   6808  CB  MET D  59     239.446 166.596 164.236  1.00151.64           C  
ATOM   6809  CG  MET D  59     238.014 166.267 163.861  1.00151.64           C  
ATOM   6810  SD  MET D  59     237.696 166.463 162.089  1.00151.64           S  
ATOM   6811  CE  MET D  59     236.705 165.005 161.768  1.00151.64           C  
ATOM   6812  N   TYR D  60     239.528 166.051 167.316  1.00151.28           N  
ATOM   6813  CA  TYR D  60     239.005 165.478 168.550  1.00151.28           C  
ATOM   6814  C   TYR D  60     238.864 166.519 169.656  1.00151.28           C  
ATOM   6815  O   TYR D  60     237.846 166.556 170.359  1.00151.28           O  
ATOM   6816  CB  TYR D  60     239.892 164.328 169.006  1.00151.28           C  
ATOM   6817  CG  TYR D  60     239.849 163.097 168.137  1.00151.28           C  
ATOM   6818  CD1 TYR D  60     238.846 162.920 167.196  1.00151.28           C  
ATOM   6819  CD2 TYR D  60     240.779 162.081 168.302  1.00151.28           C  
ATOM   6820  CE1 TYR D  60     238.793 161.781 166.419  1.00151.28           C  
ATOM   6821  CE2 TYR D  60     240.736 160.942 167.531  1.00151.28           C  
ATOM   6822  CZ  TYR D  60     239.742 160.795 166.591  1.00151.28           C  
ATOM   6823  OH  TYR D  60     239.701 159.655 165.821  1.00151.28           O  
ATOM   6824  N   ILE D  61     239.876 167.367 169.832  1.00145.15           N  
ATOM   6825  CA  ILE D  61     239.814 168.386 170.873  1.00145.15           C  
ATOM   6826  C   ILE D  61     238.638 169.314 170.628  1.00145.15           C  
ATOM   6827  O   ILE D  61     237.917 169.684 171.558  1.00145.15           O  
ATOM   6828  CB  ILE D  61     241.140 169.164 170.943  1.00145.15           C  
ATOM   6829  CG1 ILE D  61     242.248 168.276 171.501  1.00145.15           C  
ATOM   6830  CG2 ILE D  61     240.991 170.400 171.799  1.00145.15           C  
ATOM   6831  CD1 ILE D  61     243.614 168.905 171.432  1.00145.15           C  
ATOM   6832  N   LYS D  62     238.435 169.714 169.375  1.00145.56           N  
ATOM   6833  CA  LYS D  62     237.302 170.575 169.061  1.00145.56           C  
ATOM   6834  C   LYS D  62     235.983 169.871 169.338  1.00145.56           C  
ATOM   6835  O   LYS D  62     235.119 170.413 170.037  1.00145.56           O  
ATOM   6836  CB  LYS D  62     237.377 171.031 167.606  1.00145.56           C  
ATOM   6837  CG  LYS D  62     238.554 171.946 167.322  1.00145.56           C  
ATOM   6838  CD  LYS D  62     238.655 172.304 165.853  1.00145.56           C  
ATOM   6839  CE  LYS D  62     239.866 173.188 165.598  1.00145.56           C  
ATOM   6840  NZ  LYS D  62     239.982 173.576 164.167  1.00145.56           N  
ATOM   6841  N   GLN D  63     235.818 168.650 168.826  1.00145.99           N  
ATOM   6842  CA  GLN D  63     234.550 167.951 168.992  1.00145.99           C  
ATOM   6843  C   GLN D  63     234.282 167.585 170.441  1.00145.99           C  
ATOM   6844  O   GLN D  63     233.156 167.206 170.769  1.00145.99           O  
ATOM   6845  CB  GLN D  63     234.503 166.698 168.112  1.00145.99           C  
ATOM   6846  CG  GLN D  63     235.559 165.640 168.404  1.00145.99           C  
ATOM   6847  CD  GLN D  63     235.302 164.835 169.667  1.00145.99           C  
ATOM   6848  OE1 GLN D  63     234.164 164.699 170.112  1.00145.99           O  
ATOM   6849  NE2 GLN D  63     236.369 164.314 170.260  1.00145.99           N  
ATOM   6850  N   LEU D  64     235.293 167.646 171.304  1.00140.73           N  
ATOM   6851  CA  LEU D  64     235.051 167.488 172.732  1.00140.73           C  
ATOM   6852  C   LEU D  64     234.746 168.810 173.421  1.00140.73           C  
ATOM   6853  O   LEU D  64     233.708 168.952 174.071  1.00140.73           O  
ATOM   6854  CB  LEU D  64     236.254 166.843 173.412  1.00140.73           C  
ATOM   6855  CG  LEU D  64     236.008 166.611 174.900  1.00140.73           C  
ATOM   6856  CD1 LEU D  64     234.862 165.647 175.118  1.00140.73           C  
ATOM   6857  CD2 LEU D  64     237.265 166.114 175.570  1.00140.73           C  
ATOM   6858  N   LEU D  65     235.652 169.774 173.308  1.00129.67           N  
ATOM   6859  CA  LEU D  65     235.522 171.014 174.055  1.00129.67           C  
ATOM   6860  C   LEU D  65     234.294 171.799 173.616  1.00129.67           C  
ATOM   6861  O   LEU D  65     233.541 172.307 174.453  1.00129.67           O  
ATOM   6862  CB  LEU D  65     236.790 171.843 173.888  1.00129.67           C  
ATOM   6863  CG  LEU D  65     236.890 173.060 174.790  1.00129.67           C  
ATOM   6864  CD1 LEU D  65     236.744 172.627 176.229  1.00129.67           C  
ATOM   6865  CD2 LEU D  65     238.220 173.740 174.570  1.00129.67           C  
ATOM   6866  N   ARG D  66     234.064 171.893 172.309  1.00129.06           N  
ATOM   6867  CA  ARG D  66     232.882 172.577 171.810  1.00129.06           C  
ATOM   6868  C   ARG D  66     231.629 171.712 171.921  1.00129.06           C  
ATOM   6869  O   ARG D  66     230.531 172.193 171.621  1.00129.06           O  
ATOM   6870  CB  ARG D  66     233.135 173.003 170.359  1.00129.06           C  
ATOM   6871  CG  ARG D  66     232.104 173.938 169.734  1.00129.06           C  
ATOM   6872  CD  ARG D  66     232.172 175.365 170.284  1.00129.06           C  
ATOM   6873  NE  ARG D  66     233.417 176.052 169.938  1.00129.06           N  
ATOM   6874  CZ  ARG D  66     233.702 177.303 170.293  1.00129.06           C  
ATOM   6875  NH1 ARG D  66     232.828 178.008 170.996  1.00129.06           N  
ATOM   6876  NH2 ARG D  66     234.854 177.854 169.942  1.00129.06           N  
ATOM   6877  N   HIS D  67     231.764 170.464 172.364  1.00122.44           N  
ATOM   6878  CA  HIS D  67     230.632 169.551 172.405  1.00122.44           C  
ATOM   6879  C   HIS D  67     229.620 170.020 173.447  1.00122.44           C  
ATOM   6880  O   HIS D  67     230.009 170.531 174.502  1.00122.44           O  
ATOM   6881  CB  HIS D  67     231.112 168.140 172.736  1.00122.44           C  
ATOM   6882  CG  HIS D  67     230.113 167.072 172.434  1.00122.44           C  
ATOM   6883  ND1 HIS D  67     229.156 166.669 173.338  1.00122.44           N  
ATOM   6884  CD2 HIS D  67     229.918 166.327 171.322  1.00122.44           C  
ATOM   6885  CE1 HIS D  67     228.416 165.719 172.797  1.00122.44           C  
ATOM   6886  NE2 HIS D  67     228.858 165.493 171.574  1.00122.44           N  
ATOM   6887  N   PRO D  68     228.317 169.857 173.193  1.00117.97           N  
ATOM   6888  CA  PRO D  68     227.319 170.414 174.117  1.00117.97           C  
ATOM   6889  C   PRO D  68     227.089 169.599 175.373  1.00117.97           C  
ATOM   6890  O   PRO D  68     226.674 170.176 176.385  1.00117.97           O  
ATOM   6891  CB  PRO D  68     226.038 170.468 173.272  1.00117.97           C  
ATOM   6892  CG  PRO D  68     226.292 169.633 172.071  1.00117.97           C  
ATOM   6893  CD  PRO D  68     227.697 169.150 172.063  1.00117.97           C  
ATOM   6894  N   ALA D  69     227.314 168.287 175.352  1.00113.80           N  
ATOM   6895  CA  ALA D  69     227.170 167.515 176.580  1.00113.80           C  
ATOM   6896  C   ALA D  69     228.180 167.973 177.620  1.00113.80           C  
ATOM   6897  O   ALA D  69     227.851 168.123 178.804  1.00113.80           O  
ATOM   6898  CB  ALA D  69     227.332 166.026 176.286  1.00113.80           C  
ATOM   6899  N   PHE D  70     229.417 168.205 177.184  1.00109.47           N  
ATOM   6900  CA  PHE D  70     230.445 168.737 178.068  1.00109.47           C  
ATOM   6901  C   PHE D  70     230.040 170.080 178.657  1.00109.47           C  
ATOM   6902  O   PHE D  70     230.179 170.305 179.866  1.00109.47           O  
ATOM   6903  CB  PHE D  70     231.752 168.863 177.296  1.00109.47           C  
ATOM   6904  CG  PHE D  70     232.763 169.716 177.971  1.00109.47           C  
ATOM   6905  CD1 PHE D  70     233.622 169.185 178.904  1.00109.47           C  
ATOM   6906  CD2 PHE D  70     232.858 171.062 177.664  1.00109.47           C  
ATOM   6907  CE1 PHE D  70     234.546 169.985 179.520  1.00109.47           C  
ATOM   6908  CE2 PHE D  70     233.777 171.861 178.282  1.00109.47           C  
ATOM   6909  CZ  PHE D  70     234.617 171.327 179.206  1.00109.47           C  
ATOM   6910  N   GLN D  71     229.561 170.993 177.814  1.00104.36           N  
ATOM   6911  CA  GLN D  71     229.148 172.299 178.306  1.00104.36           C  
ATOM   6912  C   GLN D  71     228.024 172.164 179.315  1.00104.36           C  
ATOM   6913  O   GLN D  71     228.010 172.852 180.339  1.00104.36           O  
ATOM   6914  CB  GLN D  71     228.713 173.184 177.141  1.00104.36           C  
ATOM   6915  CG  GLN D  71     229.838 173.614 176.220  1.00104.36           C  
ATOM   6916  CD  GLN D  71     230.879 174.439 176.936  1.00104.36           C  
ATOM   6917  OE1 GLN D  71     232.003 173.995 177.142  1.00104.36           O  
ATOM   6918  NE2 GLN D  71     230.505 175.649 177.329  1.00104.36           N  
ATOM   6919  N   LEU D  72     227.071 171.279 179.039  1.00102.34           N  
ATOM   6920  CA  LEU D  72     225.950 171.094 179.949  1.00102.34           C  
ATOM   6921  C   LEU D  72     226.422 170.551 181.290  1.00102.34           C  
ATOM   6922  O   LEU D  72     225.952 170.988 182.345  1.00102.34           O  
ATOM   6923  CB  LEU D  72     224.919 170.170 179.303  1.00102.34           C  
ATOM   6924  CG  LEU D  72     223.563 169.946 179.968  1.00102.34           C  
ATOM   6925  CD1 LEU D  72     222.553 169.592 178.903  1.00102.34           C  
ATOM   6926  CD2 LEU D  72     223.625 168.839 181.006  1.00102.34           C  
ATOM   6927  N   LEU D  73     227.361 169.605 181.270  1.00 95.58           N  
ATOM   6928  CA  LEU D  73     227.908 169.088 182.521  1.00 95.58           C  
ATOM   6929  C   LEU D  73     228.622 170.173 183.314  1.00 95.58           C  
ATOM   6930  O   LEU D  73     228.438 170.286 184.532  1.00 95.58           O  
ATOM   6931  CB  LEU D  73     228.858 167.928 182.241  1.00 95.58           C  
ATOM   6932  CG  LEU D  73     229.592 167.382 183.459  1.00 95.58           C  
ATOM   6933  CD1 LEU D  73     229.601 165.880 183.447  1.00 95.58           C  
ATOM   6934  CD2 LEU D  73     231.014 167.907 183.438  1.00 95.58           C  
ATOM   6935  N   LEU D  74     229.463 170.963 182.647  1.00 90.55           N  
ATOM   6936  CA  LEU D  74     230.197 172.004 183.355  1.00 90.55           C  
ATOM   6937  C   LEU D  74     229.243 173.038 183.937  1.00 90.55           C  
ATOM   6938  O   LEU D  74     229.432 173.504 185.067  1.00 90.55           O  
ATOM   6939  CB  LEU D  74     231.217 172.639 182.415  1.00 90.55           C  
ATOM   6940  CG  LEU D  74     232.240 173.628 182.965  1.00 90.55           C  
ATOM   6941  CD1 LEU D  74     233.477 173.578 182.111  1.00 90.55           C  
ATOM   6942  CD2 LEU D  74     231.696 175.037 182.953  1.00 90.55           C  
ATOM   6943  N   ALA D  75     228.200 173.389 183.186  1.00 87.57           N  
ATOM   6944  CA  ALA D  75     227.171 174.280 183.707  1.00 87.57           C  
ATOM   6945  C   ALA D  75     226.491 173.684 184.923  1.00 87.57           C  
ATOM   6946  O   ALA D  75     226.233 174.388 185.902  1.00 87.57           O  
ATOM   6947  CB  ALA D  75     226.135 174.564 182.627  1.00 87.57           C  
ATOM   6948  N   PHE D  76     226.170 172.391 184.869  1.00 86.19           N  
ATOM   6949  CA  PHE D  76     225.519 171.731 185.994  1.00 86.19           C  
ATOM   6950  C   PHE D  76     226.397 171.781 187.232  1.00 86.19           C  
ATOM   6951  O   PHE D  76     225.915 172.039 188.341  1.00 86.19           O  
ATOM   6952  CB  PHE D  76     225.200 170.288 185.621  1.00 86.19           C  
ATOM   6953  CG  PHE D  76     224.890 169.409 186.791  1.00 86.19           C  
ATOM   6954  CD1 PHE D  76     223.924 169.769 187.711  1.00 86.19           C  
ATOM   6955  CD2 PHE D  76     225.534 168.195 186.943  1.00 86.19           C  
ATOM   6956  CE1 PHE D  76     223.629 168.948 188.779  1.00 86.19           C  
ATOM   6957  CE2 PHE D  76     225.248 167.374 188.009  1.00 86.19           C  
ATOM   6958  CZ  PHE D  76     224.293 167.747 188.927  1.00 86.19           C  
ATOM   6959  N   LEU D  77     227.693 171.546 187.059  1.00 81.87           N  
ATOM   6960  CA  LEU D  77     228.603 171.594 188.194  1.00 81.87           C  
ATOM   6961  C   LEU D  77     228.677 172.992 188.786  1.00 81.87           C  
ATOM   6962  O   LEU D  77     228.560 173.163 190.003  1.00 81.87           O  
ATOM   6963  CB  LEU D  77     229.985 171.115 187.775  1.00 81.87           C  
ATOM   6964  CG  LEU D  77     230.157 169.616 187.922  1.00 81.87           C  
ATOM   6965  CD1 LEU D  77     231.215 169.166 186.984  1.00 81.87           C  
ATOM   6966  CD2 LEU D  77     230.540 169.297 189.340  1.00 81.87           C  
ATOM   6967  N   LEU D  78     228.884 174.007 187.941  1.00 78.63           N  
ATOM   6968  CA  LEU D  78     229.003 175.370 188.455  1.00 78.63           C  
ATOM   6969  C   LEU D  78     227.711 175.828 189.113  1.00 78.63           C  
ATOM   6970  O   LEU D  78     227.739 176.536 190.124  1.00 78.63           O  
ATOM   6971  CB  LEU D  78     229.398 176.325 187.337  1.00 78.63           C  
ATOM   6972  CG  LEU D  78     230.890 176.569 187.146  1.00 78.63           C  
ATOM   6973  CD1 LEU D  78     231.141 177.249 185.832  1.00 78.63           C  
ATOM   6974  CD2 LEU D  78     231.415 177.425 188.271  1.00 78.63           C  
ATOM   6975  N   LEU D  79     226.569 175.430 188.559  1.00 77.29           N  
ATOM   6976  CA  LEU D  79     225.286 175.765 189.160  1.00 77.29           C  
ATOM   6977  C   LEU D  79     225.112 175.091 190.516  1.00 77.29           C  
ATOM   6978  O   LEU D  79     224.637 175.715 191.477  1.00 77.29           O  
ATOM   6979  CB  LEU D  79     224.174 175.364 188.197  1.00 77.29           C  
ATOM   6980  CG  LEU D  79     222.724 175.738 188.461  1.00 77.29           C  
ATOM   6981  CD1 LEU D  79     222.015 175.816 187.127  1.00 77.29           C  
ATOM   6982  CD2 LEU D  79     222.039 174.721 189.355  1.00 77.29           C  
ATOM   6983  N   SER D  80     225.492 173.818 190.620  1.00 73.80           N  
ATOM   6984  CA  SER D  80     225.417 173.148 191.910  1.00 73.80           C  
ATOM   6985  C   SER D  80     226.338 173.813 192.916  1.00 73.80           C  
ATOM   6986  O   SER D  80     225.995 173.947 194.096  1.00 73.80           O  
ATOM   6987  CB  SER D  80     225.765 171.672 191.761  1.00 73.80           C  
ATOM   6988  OG  SER D  80     225.334 170.947 192.897  1.00 73.80           O  
ATOM   6989  N   ASN D  81     227.514 174.242 192.468  1.00 73.59           N  
ATOM   6990  CA  ASN D  81     228.431 174.914 193.375  1.00 73.59           C  
ATOM   6991  C   ASN D  81     227.844 176.231 193.855  1.00 73.59           C  
ATOM   6992  O   ASN D  81     228.014 176.606 195.018  1.00 73.59           O  
ATOM   6993  CB  ASN D  81     229.771 175.151 192.695  1.00 73.59           C  
ATOM   6994  CG  ASN D  81     230.821 175.651 193.652  1.00 73.59           C  
ATOM   6995  OD1 ASN D  81     231.968 175.875 193.276  1.00 73.59           O  
ATOM   6996  ND2 ASN D  81     230.443 175.799 194.910  1.00 73.59           N  
ATOM   6997  N   ALA D  82     227.159 176.955 192.971  1.00 68.51           N  
ATOM   6998  CA  ALA D  82     226.510 178.189 193.395  1.00 68.51           C  
ATOM   6999  C   ALA D  82     225.432 177.913 194.434  1.00 68.51           C  
ATOM   7000  O   ALA D  82     225.273 178.675 195.395  1.00 68.51           O  
ATOM   7001  CB  ALA D  82     225.927 178.916 192.191  1.00 68.51           C  
ATOM   7002  N   ILE D  83     224.680 176.828 194.263  1.00 68.47           N  
ATOM   7003  CA  ILE D  83     223.704 176.468 195.289  1.00 68.47           C  
ATOM   7004  C   ILE D  83     224.404 176.171 196.608  1.00 68.47           C  
ATOM   7005  O   ILE D  83     223.916 176.536 197.685  1.00 68.47           O  
ATOM   7006  CB  ILE D  83     222.847 175.277 194.838  1.00 68.47           C  
ATOM   7007  CG1 ILE D  83     222.036 175.639 193.610  1.00 68.47           C  
ATOM   7008  CG2 ILE D  83     221.894 174.895 195.921  1.00 68.47           C  
ATOM   7009  CD1 ILE D  83     221.382 174.448 192.980  1.00 68.47           C  
ATOM   7010  N   THR D  84     225.547 175.487 196.549  1.00 69.73           N  
ATOM   7011  CA  THR D  84     226.287 175.202 197.775  1.00 69.73           C  
ATOM   7012  C   THR D  84     226.751 176.482 198.444  1.00 69.73           C  
ATOM   7013  O   THR D  84     226.746 176.587 199.672  1.00 69.73           O  
ATOM   7014  CB  THR D  84     227.488 174.311 197.487  1.00 69.73           C  
ATOM   7015  OG1 THR D  84     228.339 174.960 196.541  1.00 69.73           O  
ATOM   7016  CG2 THR D  84     227.046 172.976 196.941  1.00 69.73           C  
ATOM   7017  N   ILE D  85     227.181 177.457 197.650  1.00 65.37           N  
ATOM   7018  CA  ILE D  85     227.585 178.744 198.205  1.00 65.37           C  
ATOM   7019  C   ILE D  85     226.407 179.414 198.888  1.00 65.37           C  
ATOM   7020  O   ILE D  85     226.540 179.980 199.976  1.00 65.37           O  
ATOM   7021  CB  ILE D  85     228.173 179.637 197.104  1.00 65.37           C  
ATOM   7022  CG1 ILE D  85     229.465 179.036 196.576  1.00 65.37           C  
ATOM   7023  CG2 ILE D  85     228.422 181.014 197.633  1.00 65.37           C  
ATOM   7024  CD1 ILE D  85     230.100 179.863 195.514  1.00 65.37           C  
ATOM   7025  N   ALA D  86     225.237 179.367 198.258  1.00 64.18           N  
ATOM   7026  CA  ALA D  86     224.059 179.975 198.864  1.00 64.18           C  
ATOM   7027  C   ALA D  86     223.705 179.300 200.179  1.00 64.18           C  
ATOM   7028  O   ALA D  86     223.280 179.961 201.131  1.00 64.18           O  
ATOM   7029  CB  ALA D  86     222.879 179.909 197.901  1.00 64.18           C  
ATOM   7030  N   LEU D  87     223.851 177.981 200.244  1.00 68.27           N  
ATOM   7031  CA  LEU D  87     223.495 177.270 201.466  1.00 68.27           C  
ATOM   7032  C   LEU D  87     224.527 177.476 202.564  1.00 68.27           C  
ATOM   7033  O   LEU D  87     224.166 177.559 203.740  1.00 68.27           O  
ATOM   7034  CB  LEU D  87     223.307 175.794 201.161  1.00 68.27           C  
ATOM   7035  CG  LEU D  87     222.036 175.595 200.350  1.00 68.27           C  
ATOM   7036  CD1 LEU D  87     222.114 174.338 199.529  1.00 68.27           C  
ATOM   7037  CD2 LEU D  87     220.852 175.550 201.281  1.00 68.27           C  
ATOM   7038  N   ARG D  88     225.806 177.576 202.204  1.00 71.71           N  
ATOM   7039  CA  ARG D  88     226.839 177.909 203.176  1.00 71.71           C  
ATOM   7040  C   ARG D  88     226.608 179.270 203.799  1.00 71.71           C  
ATOM   7041  O   ARG D  88     227.186 179.568 204.846  1.00 71.71           O  
ATOM   7042  CB  ARG D  88     228.214 177.903 202.519  1.00 71.71           C  
ATOM   7043  CG  ARG D  88     228.798 176.545 202.285  1.00 71.71           C  
ATOM   7044  CD  ARG D  88     230.242 176.672 201.840  1.00 71.71           C  
ATOM   7045  NE  ARG D  88     230.405 176.378 200.420  1.00 71.71           N  
ATOM   7046  CZ  ARG D  88     231.570 176.387 199.784  1.00 71.71           C  
ATOM   7047  NH1 ARG D  88     231.621 176.104 198.491  1.00 71.71           N  
ATOM   7048  NH2 ARG D  88     232.682 176.677 200.439  1.00 71.71           N  
ATOM   7049  N   THR D  89     225.783 180.106 203.181  1.00 73.31           N  
ATOM   7050  CA  THR D  89     225.465 181.404 203.752  1.00 73.31           C  
ATOM   7051  C   THR D  89     224.415 181.189 204.829  1.00 73.31           C  
ATOM   7052  O   THR D  89     223.373 181.850 204.861  1.00 73.31           O  
ATOM   7053  CB  THR D  89     224.982 182.361 202.666  1.00 73.31           C  
ATOM   7054  OG1 THR D  89     225.885 182.311 201.556  1.00 73.31           O  
ATOM   7055  CG2 THR D  89     224.977 183.751 203.177  1.00 73.31           C  
ATOM   7056  N   ASN D  90     224.702 180.237 205.708  1.00 83.97           N  
ATOM   7057  CA  ASN D  90     223.805 179.826 206.779  1.00 83.97           C  
ATOM   7058  C   ASN D  90     224.640 179.012 207.747  1.00 83.97           C  
ATOM   7059  O   ASN D  90     225.167 177.962 207.371  1.00 83.97           O  
ATOM   7060  CB  ASN D  90     222.649 179.011 206.237  1.00 83.97           C  
ATOM   7061  CG  ASN D  90     221.827 178.396 207.321  1.00 83.97           C  
ATOM   7062  OD1 ASN D  90     221.841 178.848 208.460  1.00 83.97           O  
ATOM   7063  ND2 ASN D  90     221.090 177.359 206.976  1.00 83.97           N  
ATOM   7064  N   SER D  91     224.765 179.493 208.983  1.00 93.29           N  
ATOM   7065  CA  SER D  91     225.701 178.880 209.915  1.00 93.29           C  
ATOM   7066  C   SER D  91     225.343 177.429 210.189  1.00 93.29           C  
ATOM   7067  O   SER D  91     226.227 176.570 210.235  1.00 93.29           O  
ATOM   7068  CB  SER D  91     225.749 179.678 211.214  1.00 93.29           C  
ATOM   7069  OG  SER D  91     226.255 180.979 210.983  1.00 93.29           O  
ATOM   7070  N   TYR D  92     224.055 177.131 210.360  1.00 94.40           N  
ATOM   7071  CA  TYR D  92     223.655 175.770 210.697  1.00 94.40           C  
ATOM   7072  C   TYR D  92     224.053 174.785 209.608  1.00 94.40           C  
ATOM   7073  O   TYR D  92     224.807 173.840 209.856  1.00 94.40           O  
ATOM   7074  CB  TYR D  92     222.152 175.704 210.935  1.00 94.40           C  
ATOM   7075  CG  TYR D  92     221.702 174.323 211.322  1.00 94.40           C  
ATOM   7076  CD1 TYR D  92     221.927 173.834 212.595  1.00 94.40           C  
ATOM   7077  CD2 TYR D  92     221.092 173.493 210.403  1.00 94.40           C  
ATOM   7078  CE1 TYR D  92     221.533 172.570 212.946  1.00 94.40           C  
ATOM   7079  CE2 TYR D  92     220.696 172.229 210.745  1.00 94.40           C  
ATOM   7080  CZ  TYR D  92     220.918 171.772 212.018  1.00 94.40           C  
ATOM   7081  OH  TYR D  92     220.523 170.504 212.371  1.00 94.40           O  
ATOM   7082  N   LEU D  93     223.555 174.987 208.391  1.00 90.58           N  
ATOM   7083  CA  LEU D  93     223.904 174.094 207.296  1.00 90.58           C  
ATOM   7084  C   LEU D  93     225.358 174.213 206.882  1.00 90.58           C  
ATOM   7085  O   LEU D  93     225.821 173.406 206.072  1.00 90.58           O  
ATOM   7086  CB  LEU D  93     223.011 174.348 206.086  1.00 90.58           C  
ATOM   7087  CG  LEU D  93     221.689 173.588 206.070  1.00 90.58           C  
ATOM   7088  CD1 LEU D  93     220.689 174.215 207.005  1.00 90.58           C  
ATOM   7089  CD2 LEU D  93     221.135 173.520 204.668  1.00 90.58           C  
ATOM   7090  N   GLY D  94     226.084 175.196 207.399  1.00 92.13           N  
ATOM   7091  CA  GLY D  94     227.505 175.262 207.124  1.00 92.13           C  
ATOM   7092  C   GLY D  94     228.247 174.036 207.613  1.00 92.13           C  
ATOM   7093  O   GLY D  94     229.222 173.606 206.995  1.00 92.13           O  
ATOM   7094  N   GLN D  95     227.800 173.450 208.728  1.00 92.85           N  
ATOM   7095  CA  GLN D  95     228.525 172.310 209.278  1.00 92.85           C  
ATOM   7096  C   GLN D  95     227.992 170.994 208.739  1.00 92.85           C  
ATOM   7097  O   GLN D  95     228.758 170.183 208.210  1.00 92.85           O  
ATOM   7098  CB  GLN D  95     228.452 172.288 210.802  1.00 92.85           C  
ATOM   7099  CG  GLN D  95     229.110 173.445 211.469  1.00 92.85           C  
ATOM   7100  CD  GLN D  95     228.166 174.595 211.567  1.00 92.85           C  
ATOM   7101  OE1 GLN D  95     226.958 174.405 211.474  1.00 92.85           O  
ATOM   7102  NE2 GLN D  95     228.695 175.797 211.739  1.00 92.85           N  
ATOM   7103  N   LYS D  96     226.678 170.777 208.857  1.00 91.18           N  
ATOM   7104  CA  LYS D  96     226.130 169.432 208.725  1.00 91.18           C  
ATOM   7105  C   LYS D  96     226.620 168.749 207.459  1.00 91.18           C  
ATOM   7106  O   LYS D  96     226.982 167.570 207.482  1.00 91.18           O  
ATOM   7107  CB  LYS D  96     224.606 169.478 208.746  1.00 91.18           C  
ATOM   7108  CG  LYS D  96     223.970 168.105 208.608  1.00 91.18           C  
ATOM   7109  CD  LYS D  96     222.478 168.126 208.852  1.00 91.18           C  
ATOM   7110  CE  LYS D  96     222.102 169.037 210.000  1.00 91.18           C  
ATOM   7111  NZ  LYS D  96     220.624 169.176 210.105  1.00 91.18           N  
ATOM   7112  N   HIS D  97     226.675 169.478 206.354  1.00 90.45           N  
ATOM   7113  CA  HIS D  97     227.151 168.932 205.093  1.00 90.45           C  
ATOM   7114  C   HIS D  97     228.477 169.554 204.672  1.00 90.45           C  
ATOM   7115  O   HIS D  97     228.757 169.691 203.480  1.00 90.45           O  
ATOM   7116  CB  HIS D  97     226.095 169.119 204.012  1.00 90.45           C  
ATOM   7117  CG  HIS D  97     224.699 168.912 204.499  1.00 90.45           C  
ATOM   7118  ND1 HIS D  97     224.057 169.811 205.321  1.00 90.45           N  
ATOM   7119  CD2 HIS D  97     223.822 167.905 204.285  1.00 90.45           C  
ATOM   7120  CE1 HIS D  97     222.843 169.368 205.590  1.00 90.45           C  
ATOM   7121  NE2 HIS D  97     222.674 168.214 204.972  1.00 90.45           N  
ATOM   7122  N   TYR D  98     229.307 169.917 205.650  1.00 85.28           N  
ATOM   7123  CA  TYR D  98     230.601 170.515 205.351  1.00 85.28           C  
ATOM   7124  C   TYR D  98     231.449 169.610 204.473  1.00 85.28           C  
ATOM   7125  O   TYR D  98     232.148 170.084 203.570  1.00 85.28           O  
ATOM   7126  CB  TYR D  98     231.328 170.826 206.649  1.00 85.28           C  
ATOM   7127  CG  TYR D  98     232.757 171.215 206.456  1.00 85.28           C  
ATOM   7128  CD1 TYR D  98     233.093 172.433 205.905  1.00 85.28           C  
ATOM   7129  CD2 TYR D  98     233.775 170.363 206.829  1.00 85.28           C  
ATOM   7130  CE1 TYR D  98     234.404 172.792 205.728  1.00 85.28           C  
ATOM   7131  CE2 TYR D  98     235.086 170.712 206.658  1.00 85.28           C  
ATOM   7132  CZ  TYR D  98     235.398 171.928 206.105  1.00 85.28           C  
ATOM   7133  OH  TYR D  98     236.714 172.280 205.929  1.00 85.28           O  
ATOM   7134  N   GLU D  99     231.360 168.299 204.723  1.00 87.29           N  
ATOM   7135  CA  GLU D  99     232.129 167.289 203.945  1.00 87.29           C  
ATOM   7136  C   GLU D  99     231.700 167.324 202.472  1.00 87.29           C  
ATOM   7137  O   GLU D  99     232.591 167.267 201.602  1.00 87.29           O  
ATOM   7138  CB  GLU D  99     231.900 165.896 204.536  1.00 87.29           C  
ATOM   7139  CG  GLU D  99     232.647 164.798 203.801  1.00 87.29           C  
ATOM   7140  CD  GLU D  99     232.442 163.404 204.368  1.00 87.29           C  
ATOM   7141  OE1 GLU D  99     233.025 162.451 203.813  1.00 87.29           O  
ATOM   7142  OE2 GLU D  99     231.701 163.275 205.362  1.00 87.29           O  
ATOM   7143  N   LEU D 100     230.393 167.433 202.208  1.00 84.03           N  
ATOM   7144  CA  LEU D 100     229.888 167.473 200.843  1.00 84.03           C  
ATOM   7145  C   LEU D 100     230.258 168.778 200.151  1.00 84.03           C  
ATOM   7146  O   LEU D 100     230.673 168.775 198.983  1.00 84.03           O  
ATOM   7147  CB  LEU D 100     228.377 167.287 200.853  1.00 84.03           C  
ATOM   7148  CG  LEU D 100     227.777 166.778 199.553  1.00 84.03           C  
ATOM   7149  CD1 LEU D 100     228.261 165.370 199.284  1.00 84.03           C  
ATOM   7150  CD2 LEU D 100     226.273 166.823 199.636  1.00 84.03           C  
ATOM   7151  N   PHE D 101     230.103 169.902 200.852  1.00 80.52           N  
ATOM   7152  CA  PHE D 101     230.413 171.188 200.247  1.00 80.52           C  
ATOM   7153  C   PHE D 101     231.886 171.286 199.906  1.00 80.52           C  
ATOM   7154  O   PHE D 101     232.244 171.760 198.827  1.00 80.52           O  
ATOM   7155  CB  PHE D 101     229.992 172.327 201.169  1.00 80.52           C  
ATOM   7156  CG  PHE D 101     228.521 172.358 201.453  1.00 80.52           C  
ATOM   7157  CD1 PHE D 101     227.624 171.810 200.563  1.00 80.52           C  
ATOM   7158  CD2 PHE D 101     228.036 172.937 202.608  1.00 80.52           C  
ATOM   7159  CE1 PHE D 101     226.278 171.833 200.820  1.00 80.52           C  
ATOM   7160  CE2 PHE D 101     226.684 172.962 202.866  1.00 80.52           C  
ATOM   7161  CZ  PHE D 101     225.807 172.407 201.973  1.00 80.52           C  
ATOM   7162  N   SER D 102     232.757 170.821 200.798  1.00 81.11           N  
ATOM   7163  CA  SER D 102     234.185 170.847 200.506  1.00 81.11           C  
ATOM   7164  C   SER D 102     234.531 169.974 199.303  1.00 81.11           C  
ATOM   7165  O   SER D 102     235.308 170.384 198.426  1.00 81.11           O  
ATOM   7166  CB  SER D 102     234.960 170.395 201.732  1.00 81.11           C  
ATOM   7167  OG  SER D 102     234.683 169.038 202.006  1.00 81.11           O  
ATOM   7168  N   THR D 103     233.970 168.763 199.243  1.00 81.86           N  
ATOM   7169  CA  THR D 103     234.220 167.906 198.088  1.00 81.86           C  
ATOM   7170  C   THR D 103     233.816 168.588 196.791  1.00 81.86           C  
ATOM   7171  O   THR D 103     234.595 168.629 195.832  1.00 81.86           O  
ATOM   7172  CB  THR D 103     233.474 166.584 198.233  1.00 81.86           C  
ATOM   7173  OG1 THR D 103     232.070 166.844 198.337  1.00 81.86           O  
ATOM   7174  CG2 THR D 103     233.955 165.814 199.430  1.00 81.86           C  
ATOM   7175  N   ILE D 104     232.590 169.110 196.733  1.00 78.58           N  
ATOM   7176  CA  ILE D 104     232.120 169.749 195.506  1.00 78.58           C  
ATOM   7177  C   ILE D 104     233.000 170.939 195.165  1.00 78.58           C  
ATOM   7178  O   ILE D 104     233.358 171.165 193.999  1.00 78.58           O  
ATOM   7179  CB  ILE D 104     230.648 170.160 195.658  1.00 78.58           C  
ATOM   7180  CG1 ILE D 104     229.772 168.921 195.844  1.00 78.58           C  
ATOM   7181  CG2 ILE D 104     230.202 170.972 194.469  1.00 78.58           C  
ATOM   7182  CD1 ILE D 104     228.462 169.196 196.532  1.00 78.58           C  
ATOM   7183  N   ASP D 105     233.358 171.715 196.187  1.00 79.23           N  
ATOM   7184  CA  ASP D 105     234.245 172.858 196.042  1.00 79.23           C  
ATOM   7185  C   ASP D 105     235.529 172.491 195.324  1.00 79.23           C  
ATOM   7186  O   ASP D 105     236.010 173.242 194.472  1.00 79.23           O  
ATOM   7187  CB  ASP D 105     234.556 173.404 197.433  1.00 79.23           C  
ATOM   7188  CG  ASP D 105     234.865 174.860 197.427  1.00 79.23           C  
ATOM   7189  OD1 ASP D 105     235.120 175.380 196.332  1.00 79.23           O  
ATOM   7190  OD2 ASP D 105     234.851 175.483 198.508  1.00 79.23           O  
ATOM   7191  N   ASP D 106     236.114 171.350 195.675  1.00 80.86           N  
ATOM   7192  CA  ASP D 106     237.373 170.966 195.043  1.00 80.86           C  
ATOM   7193  C   ASP D 106     237.163 170.318 193.679  1.00 80.86           C  
ATOM   7194  O   ASP D 106     237.993 170.484 192.776  1.00 80.86           O  
ATOM   7195  CB  ASP D 106     238.149 170.036 195.964  1.00 80.86           C  
ATOM   7196  CG  ASP D 106     238.653 170.744 197.190  1.00 80.86           C  
ATOM   7197  OD1 ASP D 106     238.907 171.960 197.100  1.00 80.86           O  
ATOM   7198  OD2 ASP D 106     238.787 170.101 198.248  1.00 80.86           O  
ATOM   7199  N   ILE D 107     236.070 169.574 193.512  1.00 79.69           N  
ATOM   7200  CA  ILE D 107     235.814 168.917 192.234  1.00 79.69           C  
ATOM   7201  C   ILE D 107     235.657 169.948 191.130  1.00 79.69           C  
ATOM   7202  O   ILE D 107     236.237 169.820 190.039  1.00 79.69           O  
ATOM   7203  CB  ILE D 107     234.568 168.022 192.336  1.00 79.69           C  
ATOM   7204  CG1 ILE D 107     234.849 166.807 193.215  1.00 79.69           C  
ATOM   7205  CG2 ILE D 107     234.107 167.597 190.958  1.00 79.69           C  
ATOM   7206  CD1 ILE D 107     233.643 165.947 193.448  1.00 79.69           C  
ATOM   7207  N   VAL D 108     234.875 170.992 191.394  1.00 82.12           N  
ATOM   7208  CA  VAL D 108     234.662 171.995 190.363  1.00 82.12           C  
ATOM   7209  C   VAL D 108     235.968 172.703 190.028  1.00 82.12           C  
ATOM   7210  O   VAL D 108     236.240 173.006 188.861  1.00 82.12           O  
ATOM   7211  CB  VAL D 108     233.566 172.984 190.788  1.00 82.12           C  
ATOM   7212  CG1 VAL D 108     232.247 172.268 190.928  1.00 82.12           C  
ATOM   7213  CG2 VAL D 108     233.937 173.644 192.082  1.00 82.12           C  
ATOM   7214  N   LEU D 109     236.801 172.975 191.032  1.00 85.50           N  
ATOM   7215  CA  LEU D 109     238.057 173.655 190.747  1.00 85.50           C  
ATOM   7216  C   LEU D 109     238.966 172.796 189.886  1.00 85.50           C  
ATOM   7217  O   LEU D 109     239.573 173.294 188.932  1.00 85.50           O  
ATOM   7218  CB  LEU D 109     238.766 174.040 192.036  1.00 85.50           C  
ATOM   7219  CG  LEU D 109     239.982 174.919 191.760  1.00 85.50           C  
ATOM   7220  CD1 LEU D 109     239.566 176.119 190.948  1.00 85.50           C  
ATOM   7221  CD2 LEU D 109     240.646 175.357 193.043  1.00 85.50           C  
ATOM   7222  N   THR D 110     239.072 171.505 190.200  1.00 86.90           N  
ATOM   7223  CA  THR D 110     239.912 170.638 189.381  1.00 86.90           C  
ATOM   7224  C   THR D 110     239.408 170.583 187.948  1.00 86.90           C  
ATOM   7225  O   THR D 110     240.204 170.588 187.003  1.00 86.90           O  
ATOM   7226  CB  THR D 110     239.991 169.236 189.979  1.00 86.90           C  
ATOM   7227  OG1 THR D 110     238.680 168.666 190.051  1.00 86.90           O  
ATOM   7228  CG2 THR D 110     240.612 169.282 191.355  1.00 86.90           C  
ATOM   7229  N   ILE D 111     238.091 170.548 187.759  1.00 87.99           N  
ATOM   7230  CA  ILE D 111     237.580 170.509 186.393  1.00 87.99           C  
ATOM   7231  C   ILE D 111     237.869 171.815 185.666  1.00 87.99           C  
ATOM   7232  O   ILE D 111     238.226 171.814 184.482  1.00 87.99           O  
ATOM   7233  CB  ILE D 111     236.087 170.165 186.395  1.00 87.99           C  
ATOM   7234  CG1 ILE D 111     235.927 168.727 186.856  1.00 87.99           C  
ATOM   7235  CG2 ILE D 111     235.506 170.340 185.020  1.00 87.99           C  
ATOM   7236  CD1 ILE D 111     234.536 168.334 187.120  1.00 87.99           C  
ATOM   7237  N   LEU D 112     237.731 172.947 186.355  1.00 91.45           N  
ATOM   7238  CA  LEU D 112     238.076 174.224 185.736  1.00 91.45           C  
ATOM   7239  C   LEU D 112     239.534 174.247 185.294  1.00 91.45           C  
ATOM   7240  O   LEU D 112     239.854 174.709 184.189  1.00 91.45           O  
ATOM   7241  CB  LEU D 112     237.807 175.369 186.709  1.00 91.45           C  
ATOM   7242  CG  LEU D 112     236.464 176.086 186.663  1.00 91.45           C  
ATOM   7243  CD1 LEU D 112     236.375 176.889 185.397  1.00 91.45           C  
ATOM   7244  CD2 LEU D 112     235.327 175.096 186.743  1.00 91.45           C  
ATOM   7245  N   ILE D 113     240.433 173.759 186.147  1.00 96.00           N  
ATOM   7246  CA  ILE D 113     241.842 173.721 185.769  1.00 96.00           C  
ATOM   7247  C   ILE D 113     242.044 172.806 184.574  1.00 96.00           C  
ATOM   7248  O   ILE D 113     242.835 173.106 183.671  1.00 96.00           O  
ATOM   7249  CB  ILE D 113     242.724 173.300 186.958  1.00 96.00           C  
ATOM   7250  CG1 ILE D 113     242.438 174.168 188.178  1.00 96.00           C  
ATOM   7251  CG2 ILE D 113     244.186 173.390 186.587  1.00 96.00           C  
ATOM   7252  CD1 ILE D 113     242.528 173.433 189.480  1.00 96.00           C  
ATOM   7253  N   CYS D 114     241.341 171.677 184.545  1.00101.86           N  
ATOM   7254  CA  CYS D 114     241.459 170.796 183.393  1.00101.86           C  
ATOM   7255  C   CYS D 114     241.046 171.517 182.120  1.00101.86           C  
ATOM   7256  O   CYS D 114     241.661 171.338 181.061  1.00101.86           O  
ATOM   7257  CB  CYS D 114     240.615 169.542 183.598  1.00101.86           C  
ATOM   7258  SG  CYS D 114     241.029 168.210 182.459  1.00101.86           S  
ATOM   7259  N   GLU D 115     240.015 172.352 182.207  1.00105.08           N  
ATOM   7260  CA  GLU D 115     239.527 173.011 181.005  1.00105.08           C  
ATOM   7261  C   GLU D 115     240.515 174.060 180.527  1.00105.08           C  
ATOM   7262  O   GLU D 115     240.745 174.212 179.321  1.00105.08           O  
ATOM   7263  CB  GLU D 115     238.164 173.634 181.270  1.00105.08           C  
ATOM   7264  CG  GLU D 115     237.095 172.612 181.575  1.00105.08           C  
ATOM   7265  CD  GLU D 115     237.238 171.293 180.825  1.00105.08           C  
ATOM   7266  OE1 GLU D 115     237.703 171.264 179.666  1.00105.08           O  
ATOM   7267  OE2 GLU D 115     236.886 170.252 181.415  1.00105.08           O  
ATOM   7268  N   VAL D 116     241.109 174.795 181.461  1.00108.03           N  
ATOM   7269  CA  VAL D 116     242.146 175.746 181.075  1.00108.03           C  
ATOM   7270  C   VAL D 116     243.321 175.014 180.440  1.00108.03           C  
ATOM   7271  O   VAL D 116     243.936 175.504 179.485  1.00108.03           O  
ATOM   7272  CB  VAL D 116     242.572 176.587 182.287  1.00108.03           C  
ATOM   7273  CG1 VAL D 116     243.778 177.426 181.951  1.00108.03           C  
ATOM   7274  CG2 VAL D 116     241.425 177.469 182.725  1.00108.03           C  
ATOM   7275  N   LEU D 117     243.647 173.825 180.952  1.00111.18           N  
ATOM   7276  CA  LEU D 117     244.719 173.040 180.346  1.00111.18           C  
ATOM   7277  C   LEU D 117     244.378 172.645 178.920  1.00111.18           C  
ATOM   7278  O   LEU D 117     245.229 172.718 178.029  1.00111.18           O  
ATOM   7279  CB  LEU D 117     245.007 171.793 181.171  1.00111.18           C  
ATOM   7280  CG  LEU D 117     245.762 172.031 182.468  1.00111.18           C  
ATOM   7281  CD1 LEU D 117     246.138 170.697 183.086  1.00111.18           C  
ATOM   7282  CD2 LEU D 117     246.985 172.884 182.204  1.00111.18           C  
ATOM   7283  N   LEU D 118     243.142 172.205 178.687  1.00116.02           N  
ATOM   7284  CA  LEU D 118     242.746 171.864 177.326  1.00116.02           C  
ATOM   7285  C   LEU D 118     242.850 173.073 176.416  1.00116.02           C  
ATOM   7286  O   LEU D 118     243.353 172.974 175.294  1.00116.02           O  
ATOM   7287  CB  LEU D 118     241.328 171.304 177.303  1.00116.02           C  
ATOM   7288  CG  LEU D 118     241.131 170.065 178.164  1.00116.02           C  
ATOM   7289  CD1 LEU D 118     239.746 169.487 177.957  1.00116.02           C  
ATOM   7290  CD2 LEU D 118     242.202 169.042 177.841  1.00116.02           C  
ATOM   7291  N   GLY D 119     242.394 174.229 176.890  1.00124.21           N  
ATOM   7292  CA  GLY D 119     242.507 175.433 176.085  1.00124.21           C  
ATOM   7293  C   GLY D 119     243.945 175.755 175.729  1.00124.21           C  
ATOM   7294  O   GLY D 119     244.255 176.061 174.577  1.00124.21           O  
ATOM   7295  N   TRP D 120     244.844 175.675 176.712  1.00127.98           N  
ATOM   7296  CA  TRP D 120     246.260 175.909 176.444  1.00127.98           C  
ATOM   7297  C   TRP D 120     246.838 174.860 175.507  1.00127.98           C  
ATOM   7298  O   TRP D 120     247.782 175.146 174.762  1.00127.98           O  
ATOM   7299  CB  TRP D 120     247.045 175.932 177.750  1.00127.98           C  
ATOM   7300  CG  TRP D 120     247.222 177.296 178.299  1.00127.98           C  
ATOM   7301  CD1 TRP D 120     246.660 178.443 177.832  1.00127.98           C  
ATOM   7302  CD2 TRP D 120     248.032 177.671 179.415  1.00127.98           C  
ATOM   7303  NE1 TRP D 120     247.064 179.512 178.592  1.00127.98           N  
ATOM   7304  CE2 TRP D 120     247.907 179.063 179.572  1.00127.98           C  
ATOM   7305  CE3 TRP D 120     248.851 176.964 180.299  1.00127.98           C  
ATOM   7306  CZ2 TRP D 120     248.568 179.761 180.577  1.00127.98           C  
ATOM   7307  CZ3 TRP D 120     249.508 177.658 181.292  1.00127.98           C  
ATOM   7308  CH2 TRP D 120     249.364 179.042 181.424  1.00127.98           C  
ATOM   7309  N   LEU D 121     246.284 173.647 175.529  1.00129.34           N  
ATOM   7310  CA  LEU D 121     246.769 172.576 174.670  1.00129.34           C  
ATOM   7311  C   LEU D 121     246.585 172.899 173.197  1.00129.34           C  
ATOM   7312  O   LEU D 121     247.219 172.266 172.348  1.00129.34           O  
ATOM   7313  CB  LEU D 121     246.043 171.278 175.017  1.00129.34           C  
ATOM   7314  CG  LEU D 121     246.594 169.979 174.440  1.00129.34           C  
ATOM   7315  CD1 LEU D 121     248.007 169.756 174.941  1.00129.34           C  
ATOM   7316  CD2 LEU D 121     245.697 168.813 174.817  1.00129.34           C  
ATOM   7317  N   ASN D 122     245.738 173.865 172.875  1.00134.77           N  
ATOM   7318  CA  ASN D 122     245.494 174.251 171.497  1.00134.77           C  
ATOM   7319  C   ASN D 122     246.412 175.371 171.032  1.00134.77           C  
ATOM   7320  O   ASN D 122     246.319 175.793 169.876  1.00134.77           O  
ATOM   7321  CB  ASN D 122     244.034 174.666 171.339  1.00134.77           C  
ATOM   7322  CG  ASN D 122     243.091 173.493 171.465  1.00134.77           C  
ATOM   7323  OD1 ASN D 122     243.357 172.415 170.939  1.00134.77           O  
ATOM   7324  ND2 ASN D 122     241.991 173.690 172.180  1.00134.77           N  
ATOM   7325  N   GLY D 123     247.305 175.845 171.892  1.00139.23           N  
ATOM   7326  CA  GLY D 123     248.189 176.932 171.533  1.00139.23           C  
ATOM   7327  C   GLY D 123     248.042 178.098 172.480  1.00139.23           C  
ATOM   7328  O   GLY D 123     246.960 178.679 172.585  1.00139.23           O  
ATOM   7329  N   PHE D 124     249.128 178.444 173.173  1.00140.44           N  
ATOM   7330  CA  PHE D 124     249.069 179.489 174.188  1.00140.44           C  
ATOM   7331  C   PHE D 124     248.443 180.762 173.641  1.00140.44           C  
ATOM   7332  O   PHE D 124     247.642 181.413 174.321  1.00140.44           O  
ATOM   7333  CB  PHE D 124     250.471 179.790 174.715  1.00140.44           C  
ATOM   7334  CG  PHE D 124     251.278 178.570 175.042  1.00140.44           C  
ATOM   7335  CD1 PHE D 124     250.787 177.605 175.902  1.00140.44           C  
ATOM   7336  CD2 PHE D 124     252.537 178.392 174.490  1.00140.44           C  
ATOM   7337  CE1 PHE D 124     251.538 176.481 176.204  1.00140.44           C  
ATOM   7338  CE2 PHE D 124     253.292 177.270 174.785  1.00140.44           C  
ATOM   7339  CZ  PHE D 124     252.792 176.314 175.642  1.00140.44           C  
ATOM   7340  N   TRP D 125     248.791 181.128 172.410  1.00137.52           N  
ATOM   7341  CA  TRP D 125     248.441 182.449 171.905  1.00137.52           C  
ATOM   7342  C   TRP D 125     246.961 182.554 171.560  1.00137.52           C  
ATOM   7343  O   TRP D 125     246.317 183.558 171.886  1.00137.52           O  
ATOM   7344  CB  TRP D 125     249.317 182.770 170.700  1.00137.52           C  
ATOM   7345  CG  TRP D 125     250.719 182.316 170.908  1.00137.52           C  
ATOM   7346  CD1 TRP D 125     251.336 181.262 170.307  1.00137.52           C  
ATOM   7347  CD2 TRP D 125     251.684 182.899 171.785  1.00137.52           C  
ATOM   7348  NE1 TRP D 125     252.628 181.150 170.755  1.00137.52           N  
ATOM   7349  CE2 TRP D 125     252.866 182.147 171.663  1.00137.52           C  
ATOM   7350  CE3 TRP D 125     251.666 183.987 172.658  1.00137.52           C  
ATOM   7351  CZ2 TRP D 125     254.017 182.447 172.382  1.00137.52           C  
ATOM   7352  CZ3 TRP D 125     252.808 184.283 173.371  1.00137.52           C  
ATOM   7353  CH2 TRP D 125     253.967 183.517 173.230  1.00137.52           C  
ATOM   7354  N   ILE D 126     246.398 181.536 170.909  1.00137.23           N  
ATOM   7355  CA  ILE D 126     244.997 181.624 170.510  1.00137.23           C  
ATOM   7356  C   ILE D 126     244.089 181.582 171.732  1.00137.23           C  
ATOM   7357  O   ILE D 126     243.056 182.261 171.775  1.00137.23           O  
ATOM   7358  CB  ILE D 126     244.647 180.521 169.500  1.00137.23           C  
ATOM   7359  CG1 ILE D 126     244.829 179.136 170.113  1.00137.23           C  
ATOM   7360  CG2 ILE D 126     245.512 180.659 168.267  1.00137.23           C  
ATOM   7361  CD1 ILE D 126     244.279 178.033 169.251  1.00137.23           C  
ATOM   7362  N   PHE D 127     244.449 180.782 172.737  1.00129.90           N  
ATOM   7363  CA  PHE D 127     243.737 180.829 174.005  1.00129.90           C  
ATOM   7364  C   PHE D 127     243.755 182.231 174.583  1.00129.90           C  
ATOM   7365  O   PHE D 127     242.778 182.660 175.201  1.00129.90           O  
ATOM   7366  CB  PHE D 127     244.365 179.846 174.985  1.00129.90           C  
ATOM   7367  CG  PHE D 127     243.714 179.826 176.339  1.00129.90           C  
ATOM   7368  CD1 PHE D 127     244.119 180.697 177.338  1.00129.90           C  
ATOM   7369  CD2 PHE D 127     242.709 178.918 176.621  1.00129.90           C  
ATOM   7370  CE1 PHE D 127     243.523 180.669 178.579  1.00129.90           C  
ATOM   7371  CE2 PHE D 127     242.116 178.886 177.863  1.00129.90           C  
ATOM   7372  CZ  PHE D 127     242.522 179.762 178.840  1.00129.90           C  
ATOM   7373  N   TRP D 128     244.854 182.955 174.393  1.00131.50           N  
ATOM   7374  CA  TRP D 128     244.981 184.329 174.853  1.00131.50           C  
ATOM   7375  C   TRP D 128     244.563 185.350 173.809  1.00131.50           C  
ATOM   7376  O   TRP D 128     244.613 186.551 174.086  1.00131.50           O  
ATOM   7377  CB  TRP D 128     246.416 184.600 175.294  1.00131.50           C  
ATOM   7378  CG  TRP D 128     246.645 184.308 176.729  1.00131.50           C  
ATOM   7379  CD1 TRP D 128     245.863 183.549 177.549  1.00131.50           C  
ATOM   7380  CD2 TRP D 128     247.734 184.771 177.528  1.00131.50           C  
ATOM   7381  NE1 TRP D 128     246.396 183.513 178.812  1.00131.50           N  
ATOM   7382  CE2 TRP D 128     247.547 184.256 178.825  1.00131.50           C  
ATOM   7383  CE3 TRP D 128     248.849 185.577 177.274  1.00131.50           C  
ATOM   7384  CZ2 TRP D 128     248.435 184.518 179.864  1.00131.50           C  
ATOM   7385  CZ3 TRP D 128     249.730 185.836 178.307  1.00131.50           C  
ATOM   7386  CH2 TRP D 128     249.520 185.308 179.585  1.00131.50           C  
ATOM   7387  N   LYS D 129     244.140 184.912 172.628  1.00133.96           N  
ATOM   7388  CA  LYS D 129     243.583 185.810 171.631  1.00133.96           C  
ATOM   7389  C   LYS D 129     242.085 186.004 171.825  1.00133.96           C  
ATOM   7390  O   LYS D 129     241.354 186.215 170.851  1.00133.96           O  
ATOM   7391  CB  LYS D 129     243.888 185.292 170.225  1.00133.96           C  
ATOM   7392  CG  LYS D 129     243.897 186.363 169.142  1.00133.96           C  
ATOM   7393  CD  LYS D 129     244.981 187.404 169.385  1.00133.96           C  
ATOM   7394  CE  LYS D 129     244.560 188.770 168.855  1.00133.96           C  
ATOM   7395  NZ  LYS D 129     245.514 189.854 169.217  1.00133.96           N  
ATOM   7396  N   ASP D 130     241.617 185.916 173.067  1.00127.83           N  
ATOM   7397  CA  ASP D 130     240.213 186.044 173.411  1.00127.83           C  
ATOM   7398  C   ASP D 130     240.106 186.853 174.692  1.00127.83           C  
ATOM   7399  O   ASP D 130     241.116 187.204 175.305  1.00127.83           O  
ATOM   7400  CB  ASP D 130     239.553 184.672 173.601  1.00127.83           C  
ATOM   7401  CG  ASP D 130     238.044 184.735 173.541  1.00127.83           C  
ATOM   7402  OD1 ASP D 130     237.476 185.809 173.829  1.00127.83           O  
ATOM   7403  OD2 ASP D 130     237.423 183.701 173.227  1.00127.83           O  
ATOM   7404  N   GLY D 131     238.870 187.167 175.080  1.00120.26           N  
ATOM   7405  CA  GLY D 131     238.645 187.765 176.381  1.00120.26           C  
ATOM   7406  C   GLY D 131     238.006 186.817 177.366  1.00120.26           C  
ATOM   7407  O   GLY D 131     238.343 186.828 178.553  1.00120.26           O  
ATOM   7408  N   TRP D 132     237.075 185.990 176.905  1.00109.13           N  
ATOM   7409  CA  TRP D 132     236.415 185.081 177.827  1.00109.13           C  
ATOM   7410  C   TRP D 132     237.404 184.092 178.412  1.00109.13           C  
ATOM   7411  O   TRP D 132     237.311 183.733 179.592  1.00109.13           O  
ATOM   7412  CB  TRP D 132     235.265 184.375 177.119  1.00109.13           C  
ATOM   7413  CG  TRP D 132     234.201 185.342 176.817  1.00109.13           C  
ATOM   7414  CD1 TRP D 132     233.829 185.795 175.592  1.00109.13           C  
ATOM   7415  CD2 TRP D 132     233.400 186.040 177.767  1.00109.13           C  
ATOM   7416  NE1 TRP D 132     232.824 186.718 175.718  1.00109.13           N  
ATOM   7417  CE2 TRP D 132     232.545 186.886 177.048  1.00109.13           C  
ATOM   7418  CE3 TRP D 132     233.314 186.021 179.157  1.00109.13           C  
ATOM   7419  CZ2 TRP D 132     231.617 187.706 177.672  1.00109.13           C  
ATOM   7420  CZ3 TRP D 132     232.392 186.832 179.771  1.00109.13           C  
ATOM   7421  CH2 TRP D 132     231.555 187.660 179.033  1.00109.13           C  
ATOM   7422  N   ASN D 133     238.377 183.665 177.613  1.00115.18           N  
ATOM   7423  CA  ASN D 133     239.379 182.742 178.121  1.00115.18           C  
ATOM   7424  C   ASN D 133     240.237 183.396 179.189  1.00115.18           C  
ATOM   7425  O   ASN D 133     240.536 182.774 180.211  1.00115.18           O  
ATOM   7426  CB  ASN D 133     240.239 182.220 176.980  1.00115.18           C  
ATOM   7427  CG  ASN D 133     239.463 181.348 176.032  1.00115.18           C  
ATOM   7428  OD1 ASN D 133     239.150 181.753 174.914  1.00115.18           O  
ATOM   7429  ND2 ASN D 133     239.122 180.150 176.479  1.00115.18           N  
ATOM   7430  N   ILE D 134     240.641 184.649 178.984  1.00111.72           N  
ATOM   7431  CA  ILE D 134     241.466 185.278 180.007  1.00111.72           C  
ATOM   7432  C   ILE D 134     240.648 185.523 181.264  1.00111.72           C  
ATOM   7433  O   ILE D 134     241.180 185.464 182.376  1.00111.72           O  
ATOM   7434  CB  ILE D 134     242.119 186.570 179.490  1.00111.72           C  
ATOM   7435  CG1 ILE D 134     241.093 187.668 179.294  1.00111.72           C  
ATOM   7436  CG2 ILE D 134     242.773 186.318 178.173  1.00111.72           C  
ATOM   7437  CD1 ILE D 134     241.694 188.988 178.929  1.00111.72           C  
ATOM   7438  N   LEU D 135     239.346 185.769 181.126  1.00107.78           N  
ATOM   7439  CA  LEU D 135     238.512 185.912 182.313  1.00107.78           C  
ATOM   7440  C   LEU D 135     238.450 184.611 183.100  1.00107.78           C  
ATOM   7441  O   LEU D 135     238.655 184.593 184.322  1.00107.78           O  
ATOM   7442  CB  LEU D 135     237.110 186.358 181.920  1.00107.78           C  
ATOM   7443  CG  LEU D 135     236.249 186.565 183.154  1.00107.78           C  
ATOM   7444  CD1 LEU D 135     236.879 187.638 184.014  1.00107.78           C  
ATOM   7445  CD2 LEU D 135     234.840 186.939 182.768  1.00107.78           C  
ATOM   7446  N   ASN D 136     238.155 183.507 182.412  1.00102.46           N  
ATOM   7447  CA  ASN D 136     238.078 182.221 183.095  1.00102.46           C  
ATOM   7448  C   ASN D 136     239.420 181.854 183.704  1.00102.46           C  
ATOM   7449  O   ASN D 136     239.485 181.286 184.803  1.00102.46           O  
ATOM   7450  CB  ASN D 136     237.608 181.142 182.124  1.00102.46           C  
ATOM   7451  CG  ASN D 136     236.386 181.565 181.339  1.00102.46           C  
ATOM   7452  OD1 ASN D 136     236.287 181.320 180.141  1.00102.46           O  
ATOM   7453  ND2 ASN D 136     235.451 182.218 182.013  1.00102.46           N  
ATOM   7454  N   PHE D 137     240.506 182.189 183.009  1.00102.93           N  
ATOM   7455  CA  PHE D 137     241.834 181.929 183.541  1.00102.93           C  
ATOM   7456  C   PHE D 137     242.095 182.742 184.797  1.00102.93           C  
ATOM   7457  O   PHE D 137     242.663 182.230 185.763  1.00102.93           O  
ATOM   7458  CB  PHE D 137     242.893 182.235 182.490  1.00102.93           C  
ATOM   7459  CG  PHE D 137     244.276 182.240 183.036  1.00102.93           C  
ATOM   7460  CD1 PHE D 137     244.933 181.055 183.284  1.00102.93           C  
ATOM   7461  CD2 PHE D 137     244.911 183.429 183.328  1.00102.93           C  
ATOM   7462  CE1 PHE D 137     246.201 181.055 183.800  1.00102.93           C  
ATOM   7463  CE2 PHE D 137     246.181 183.436 183.845  1.00102.93           C  
ATOM   7464  CZ  PHE D 137     246.827 182.248 184.083  1.00102.93           C  
ATOM   7465  N   ALA D 138     241.708 184.015 184.799  1.00100.76           N  
ATOM   7466  CA  ALA D 138     241.916 184.834 185.984  1.00100.76           C  
ATOM   7467  C   ALA D 138     241.156 184.269 187.169  1.00100.76           C  
ATOM   7468  O   ALA D 138     241.689 184.192 188.283  1.00100.76           O  
ATOM   7469  CB  ALA D 138     241.490 186.270 185.709  1.00100.76           C  
ATOM   7470  N   ILE D 139     239.916 183.846 186.944  1.00 96.86           N  
ATOM   7471  CA  ILE D 139     239.127 183.274 188.031  1.00 96.86           C  
ATOM   7472  C   ILE D 139     239.795 182.018 188.572  1.00 96.86           C  
ATOM   7473  O   ILE D 139     239.990 181.868 189.785  1.00 96.86           O  
ATOM   7474  CB  ILE D 139     237.696 182.984 187.557  1.00 96.86           C  
ATOM   7475  CG1 ILE D 139     236.946 184.293 187.342  1.00 96.86           C  
ATOM   7476  CG2 ILE D 139     236.990 182.098 188.552  1.00 96.86           C  
ATOM   7477  CD1 ILE D 139     235.808 184.174 186.383  1.00 96.86           C  
ATOM   7478  N   VAL D 140     240.163 181.096 187.682  1.00 97.64           N  
ATOM   7479  CA  VAL D 140     240.725 179.838 188.158  1.00 97.64           C  
ATOM   7480  C   VAL D 140     242.079 180.062 188.808  1.00 97.64           C  
ATOM   7481  O   VAL D 140     242.446 179.356 189.747  1.00 97.64           O  
ATOM   7482  CB  VAL D 140     240.807 178.811 187.017  1.00 97.64           C  
ATOM   7483  CG1 VAL D 140     241.791 179.253 185.977  1.00 97.64           C  
ATOM   7484  CG2 VAL D 140     241.202 177.466 187.561  1.00 97.64           C  
ATOM   7485  N   PHE D 141     242.832 181.058 188.356  1.00101.66           N  
ATOM   7486  CA  PHE D 141     244.141 181.307 188.940  1.00101.66           C  
ATOM   7487  C   PHE D 141     244.011 181.902 190.330  1.00101.66           C  
ATOM   7488  O   PHE D 141     244.732 181.503 191.255  1.00101.66           O  
ATOM   7489  CB  PHE D 141     244.934 182.214 188.003  1.00101.66           C  
ATOM   7490  CG  PHE D 141     246.339 182.481 188.440  1.00101.66           C  
ATOM   7491  CD1 PHE D 141     246.617 183.269 189.536  1.00101.66           C  
ATOM   7492  CD2 PHE D 141     247.388 181.893 187.762  1.00101.66           C  
ATOM   7493  CE1 PHE D 141     247.910 183.503 189.913  1.00101.66           C  
ATOM   7494  CE2 PHE D 141     248.679 182.111 188.145  1.00101.66           C  
ATOM   7495  CZ  PHE D 141     248.944 182.914 189.224  1.00101.66           C  
ATOM   7496  N   ILE D 142     243.105 182.862 190.502  1.00 99.27           N  
ATOM   7497  CA  ILE D 142     242.880 183.407 191.833  1.00 99.27           C  
ATOM   7498  C   ILE D 142     242.380 182.317 192.769  1.00 99.27           C  
ATOM   7499  O   ILE D 142     242.772 182.257 193.938  1.00 99.27           O  
ATOM   7500  CB  ILE D 142     241.913 184.599 191.771  1.00 99.27           C  
ATOM   7501  CG1 ILE D 142     242.492 185.687 190.880  1.00 99.27           C  
ATOM   7502  CG2 ILE D 142     241.675 185.152 193.151  1.00 99.27           C  
ATOM   7503  CD1 ILE D 142     243.904 186.059 191.235  1.00 99.27           C  
ATOM   7504  N   LEU D 143     241.520 181.428 192.271  1.00 97.01           N  
ATOM   7505  CA  LEU D 143     241.089 180.308 193.099  1.00 97.01           C  
ATOM   7506  C   LEU D 143     242.257 179.399 193.444  1.00 97.01           C  
ATOM   7507  O   LEU D 143     242.346 178.886 194.565  1.00 97.01           O  
ATOM   7508  CB  LEU D 143     239.997 179.514 192.392  1.00 97.01           C  
ATOM   7509  CG  LEU D 143     238.555 179.919 192.667  1.00 97.01           C  
ATOM   7510  CD1 LEU D 143     237.603 179.006 191.920  1.00 97.01           C  
ATOM   7511  CD2 LEU D 143     238.275 179.879 194.149  1.00 97.01           C  
ATOM   7512  N   PHE D 144     243.159 179.178 192.489  1.00110.05           N  
ATOM   7513  CA  PHE D 144     244.231 178.212 192.684  1.00110.05           C  
ATOM   7514  C   PHE D 144     245.233 178.689 193.716  1.00110.05           C  
ATOM   7515  O   PHE D 144     245.698 177.902 194.546  1.00110.05           O  
ATOM   7516  CB  PHE D 144     244.935 177.933 191.362  1.00110.05           C  
ATOM   7517  CG  PHE D 144     246.081 176.986 191.487  1.00110.05           C  
ATOM   7518  CD1 PHE D 144     245.910 175.749 192.087  1.00110.05           C  
ATOM   7519  CD2 PHE D 144     247.328 177.323 191.003  1.00110.05           C  
ATOM   7520  CE1 PHE D 144     246.969 174.874 192.204  1.00110.05           C  
ATOM   7521  CE2 PHE D 144     248.387 176.449 191.114  1.00110.05           C  
ATOM   7522  CZ  PHE D 144     248.207 175.226 191.715  1.00110.05           C  
ATOM   7523  N   MET D 145     245.574 179.974 193.690  1.00116.34           N  
ATOM   7524  CA  MET D 145     246.608 180.433 194.608  1.00116.34           C  
ATOM   7525  C   MET D 145     246.183 180.351 196.061  1.00116.34           C  
ATOM   7526  O   MET D 145     247.037 180.490 196.940  1.00116.34           O  
ATOM   7527  CB  MET D 145     247.036 181.856 194.279  1.00116.34           C  
ATOM   7528  CG  MET D 145     247.348 182.076 192.822  1.00116.34           C  
ATOM   7529  SD  MET D 145     248.578 180.995 192.052  1.00116.34           S  
ATOM   7530  CE  MET D 145     249.723 180.653 193.386  1.00116.34           C  
ATOM   7531  N   GLY D 146     244.904 180.112 196.339  1.00122.31           N  
ATOM   7532  CA  GLY D 146     244.485 179.939 197.717  1.00122.31           C  
ATOM   7533  C   GLY D 146     245.150 178.761 198.397  1.00122.31           C  
ATOM   7534  O   GLY D 146     245.389 178.792 199.605  1.00122.31           O  
ATOM   7535  N   PHE D 147     245.454 177.706 197.638  1.00126.35           N  
ATOM   7536  CA  PHE D 147     246.121 176.553 198.229  1.00126.35           C  
ATOM   7537  C   PHE D 147     247.489 176.939 198.766  1.00126.35           C  
ATOM   7538  O   PHE D 147     247.877 176.515 199.860  1.00126.35           O  
ATOM   7539  CB  PHE D 147     246.241 175.429 197.201  1.00126.35           C  
ATOM   7540  CG  PHE D 147     246.883 174.171 197.735  1.00126.35           C  
ATOM   7541  CD1 PHE D 147     246.822 173.847 199.081  1.00126.35           C  
ATOM   7542  CD2 PHE D 147     247.564 173.317 196.884  1.00126.35           C  
ATOM   7543  CE1 PHE D 147     247.422 172.701 199.560  1.00126.35           C  
ATOM   7544  CE2 PHE D 147     248.163 172.172 197.361  1.00126.35           C  
ATOM   7545  CZ  PHE D 147     248.092 171.864 198.700  1.00126.35           C  
ATOM   7546  N   PHE D 148     248.226 177.761 198.024  1.00127.07           N  
ATOM   7547  CA  PHE D 148     249.572 178.145 198.438  1.00127.07           C  
ATOM   7548  C   PHE D 148     249.552 179.326 199.403  1.00127.07           C  
ATOM   7549  O   PHE D 148     250.002 179.205 200.545  1.00127.07           O  
ATOM   7550  CB  PHE D 148     250.434 178.460 197.210  1.00127.07           C  
ATOM   7551  CG  PHE D 148     250.432 177.379 196.166  1.00127.07           C  
ATOM   7552  CD1 PHE D 148     250.043 176.086 196.476  1.00127.07           C  
ATOM   7553  CD2 PHE D 148     250.880 177.644 194.887  1.00127.07           C  
ATOM   7554  CE1 PHE D 148     250.057 175.096 195.520  1.00127.07           C  
ATOM   7555  CE2 PHE D 148     250.895 176.653 193.926  1.00127.07           C  
ATOM   7556  CZ  PHE D 148     250.485 175.378 194.245  1.00127.07           C  
ATOM   7557  N   ILE D 149     249.021 180.460 198.971  1.00127.11           N  
ATOM   7558  CA  ILE D 149     249.012 181.640 199.824  1.00127.11           C  
ATOM   7559  C   ILE D 149     247.879 181.497 200.832  1.00127.11           C  
ATOM   7560  O   ILE D 149     246.983 180.664 200.674  1.00127.11           O  
ATOM   7561  CB  ILE D 149     248.882 182.923 198.981  1.00127.11           C  
ATOM   7562  CG1 ILE D 149     249.203 184.158 199.814  1.00127.11           C  
ATOM   7563  CG2 ILE D 149     247.474 183.078 198.485  1.00127.11           C  
ATOM   7564  CD1 ILE D 149     249.419 185.396 198.989  1.00127.11           C  
ATOM   7565  N   LYS D 150     247.924 182.294 201.893  1.00128.87           N  
ATOM   7566  CA  LYS D 150     246.984 182.143 202.992  1.00128.87           C  
ATOM   7567  C   LYS D 150     246.033 183.316 203.139  1.00128.87           C  
ATOM   7568  O   LYS D 150     244.922 183.134 203.644  1.00128.87           O  
ATOM   7569  CB  LYS D 150     247.743 181.951 204.306  1.00128.87           C  
ATOM   7570  CG  LYS D 150     246.895 181.450 205.456  1.00128.87           C  
ATOM   7571  CD  LYS D 150     247.533 181.800 206.789  1.00128.87           C  
ATOM   7572  CE  LYS D 150     247.037 183.141 207.294  1.00128.87           C  
ATOM   7573  NZ  LYS D 150     245.555 183.182 207.320  1.00128.87           N  
ATOM   7574  N   GLN D 151     246.435 184.509 202.718  1.00127.05           N  
ATOM   7575  CA  GLN D 151     245.607 185.692 202.900  1.00127.05           C  
ATOM   7576  C   GLN D 151     244.634 185.916 201.755  1.00127.05           C  
ATOM   7577  O   GLN D 151     243.926 186.925 201.759  1.00127.05           O  
ATOM   7578  CB  GLN D 151     246.482 186.933 203.090  1.00127.05           C  
ATOM   7579  CG  GLN D 151     247.588 186.768 204.122  1.00127.05           C  
ATOM   7580  CD  GLN D 151     248.854 186.188 203.531  1.00127.05           C  
ATOM   7581  OE1 GLN D 151     248.855 185.069 203.021  1.00127.05           O  
ATOM   7582  NE2 GLN D 151     249.941 186.947 203.590  1.00127.05           N  
ATOM   7583  N   LEU D 152     244.586 185.010 200.778  1.00122.51           N  
ATOM   7584  CA  LEU D 152     243.586 185.059 199.721  1.00122.51           C  
ATOM   7585  C   LEU D 152     242.527 183.977 199.832  1.00122.51           C  
ATOM   7586  O   LEU D 152     241.440 184.147 199.274  1.00122.51           O  
ATOM   7587  CB  LEU D 152     244.241 184.949 198.333  1.00122.51           C  
ATOM   7588  CG  LEU D 152     244.905 186.182 197.723  1.00122.51           C  
ATOM   7589  CD1 LEU D 152     246.080 186.660 198.547  1.00122.51           C  
ATOM   7590  CD2 LEU D 152     245.340 185.885 196.299  1.00122.51           C  
ATOM   7591  N   ASP D 153     242.799 182.889 200.547  1.00118.78           N  
ATOM   7592  CA  ASP D 153     241.874 181.764 200.639  1.00118.78           C  
ATOM   7593  C   ASP D 153     240.771 182.057 201.658  1.00118.78           C  
ATOM   7594  O   ASP D 153     240.499 181.285 202.577  1.00118.78           O  
ATOM   7595  CB  ASP D 153     242.644 180.502 200.995  1.00118.78           C  
ATOM   7596  CG  ASP D 153     241.821 179.246 200.827  1.00118.78           C  
ATOM   7597  OD1 ASP D 153     241.633 178.810 199.672  1.00118.78           O  
ATOM   7598  OD2 ASP D 153     241.368 178.694 201.850  1.00118.78           O  
ATOM   7599  N   MET D 154     240.122 183.204 201.471  1.00101.99           N  
ATOM   7600  CA  MET D 154     239.059 183.663 202.349  1.00101.99           C  
ATOM   7601  C   MET D 154     237.790 183.888 201.545  1.00101.99           C  
ATOM   7602  O   MET D 154     237.833 184.189 200.353  1.00101.99           O  
ATOM   7603  CB  MET D 154     239.465 184.936 203.084  1.00101.99           C  
ATOM   7604  CG  MET D 154     239.672 186.141 202.197  1.00101.99           C  
ATOM   7605  SD  MET D 154     240.200 187.559 203.172  1.00101.99           S  
ATOM   7606  CE  MET D 154     240.384 188.810 201.907  1.00101.99           C  
ATOM   7607  N   VAL D 155     236.653 183.741 202.220  1.00 84.67           N  
ATOM   7608  CA  VAL D 155     235.382 183.607 201.523  1.00 84.67           C  
ATOM   7609  C   VAL D 155     235.034 184.864 200.744  1.00 84.67           C  
ATOM   7610  O   VAL D 155     234.439 184.787 199.664  1.00 84.67           O  
ATOM   7611  CB  VAL D 155     234.283 183.231 202.527  1.00 84.67           C  
ATOM   7612  CG1 VAL D 155     234.636 181.931 203.191  1.00 84.67           C  
ATOM   7613  CG2 VAL D 155     234.130 184.311 203.567  1.00 84.67           C  
ATOM   7614  N   ALA D 156     235.402 186.034 201.258  1.00 82.37           N  
ATOM   7615  CA  ALA D 156     235.075 187.272 200.566  1.00 82.37           C  
ATOM   7616  C   ALA D 156     235.761 187.375 199.217  1.00 82.37           C  
ATOM   7617  O   ALA D 156     235.370 188.211 198.400  1.00 82.37           O  
ATOM   7618  CB  ALA D 156     235.453 188.472 201.428  1.00 82.37           C  
ATOM   7619  N   ILE D 157     236.775 186.555 198.968  1.00 83.85           N  
ATOM   7620  CA  ILE D 157     237.490 186.565 197.699  1.00 83.85           C  
ATOM   7621  C   ILE D 157     237.280 185.289 196.907  1.00 83.85           C  
ATOM   7622  O   ILE D 157     237.513 185.288 195.693  1.00 83.85           O  
ATOM   7623  CB  ILE D 157     238.994 186.823 197.918  1.00 83.85           C  
ATOM   7624  CG1 ILE D 157     239.177 188.159 198.625  1.00 83.85           C  
ATOM   7625  CG2 ILE D 157     239.743 186.896 196.614  1.00 83.85           C  
ATOM   7626  CD1 ILE D 157     238.645 189.343 197.845  1.00 83.85           C  
ATOM   7627  N   THR D 158     236.845 184.205 197.539  1.00 80.31           N  
ATOM   7628  CA  THR D 158     236.682 182.947 196.832  1.00 80.31           C  
ATOM   7629  C   THR D 158     235.253 182.617 196.461  1.00 80.31           C  
ATOM   7630  O   THR D 158     235.046 181.888 195.498  1.00 80.31           O  
ATOM   7631  CB  THR D 158     237.251 181.796 197.659  1.00 80.31           C  
ATOM   7632  OG1 THR D 158     236.797 181.911 199.013  1.00 80.31           O  
ATOM   7633  CG2 THR D 158     238.762 181.827 197.617  1.00 80.31           C  
ATOM   7634  N   TYR D 159     234.270 183.122 197.184  1.00 74.82           N  
ATOM   7635  CA  TYR D 159     232.913 182.721 196.840  1.00 74.82           C  
ATOM   7636  C   TYR D 159     232.417 183.448 195.598  1.00 74.82           C  
ATOM   7637  O   TYR D 159     232.058 182.787 194.619  1.00 74.82           O  
ATOM   7638  CB  TYR D 159     231.947 182.935 198.008  1.00 74.82           C  
ATOM   7639  CG  TYR D 159     232.084 181.913 199.094  1.00 74.82           C  
ATOM   7640  CD1 TYR D 159     232.968 180.865 198.970  1.00 74.82           C  
ATOM   7641  CD2 TYR D 159     231.323 181.992 200.239  1.00 74.82           C  
ATOM   7642  CE1 TYR D 159     233.099 179.932 199.955  1.00 74.82           C  
ATOM   7643  CE2 TYR D 159     231.444 181.060 201.230  1.00 74.82           C  
ATOM   7644  CZ  TYR D 159     232.333 180.033 201.083  1.00 74.82           C  
ATOM   7645  OH  TYR D 159     232.461 179.095 202.074  1.00 74.82           O  
ATOM   7646  N   PRO D 160     232.364 184.781 195.576  1.00 72.79           N  
ATOM   7647  CA  PRO D 160     231.735 185.437 194.426  1.00 72.79           C  
ATOM   7648  C   PRO D 160     232.445 185.206 193.108  1.00 72.79           C  
ATOM   7649  O   PRO D 160     231.805 185.310 192.059  1.00 72.79           O  
ATOM   7650  CB  PRO D 160     231.736 186.913 194.832  1.00 72.79           C  
ATOM   7651  CG  PRO D 160     232.802 187.028 195.815  1.00 72.79           C  
ATOM   7652  CD  PRO D 160     232.777 185.771 196.582  1.00 72.79           C  
ATOM   7653  N   LEU D 161     233.741 184.899 193.114  1.00 75.44           N  
ATOM   7654  CA  LEU D 161     234.410 184.546 191.866  1.00 75.44           C  
ATOM   7655  C   LEU D 161     233.845 183.275 191.254  1.00 75.44           C  
ATOM   7656  O   LEU D 161     233.767 183.165 190.026  1.00 75.44           O  
ATOM   7657  CB  LEU D 161     235.916 184.437 192.076  1.00 75.44           C  
ATOM   7658  CG  LEU D 161     236.584 185.813 192.124  1.00 75.44           C  
ATOM   7659  CD1 LEU D 161     236.278 186.599 193.372  1.00 75.44           C  
ATOM   7660  CD2 LEU D 161     238.080 185.667 191.952  1.00 75.44           C  
ATOM   7661  N   ARG D 162     233.424 182.317 192.071  1.00 74.62           N  
ATOM   7662  CA  ARG D 162     232.789 181.148 191.492  1.00 74.62           C  
ATOM   7663  C   ARG D 162     231.426 181.460 190.904  1.00 74.62           C  
ATOM   7664  O   ARG D 162     230.855 180.604 190.224  1.00 74.62           O  
ATOM   7665  CB  ARG D 162     232.664 180.041 192.520  1.00 74.62           C  
ATOM   7666  CG  ARG D 162     233.865 179.903 193.374  1.00 74.62           C  
ATOM   7667  CD  ARG D 162     233.500 179.265 194.678  1.00 74.62           C  
ATOM   7668  NE  ARG D 162     234.686 178.840 195.401  1.00 74.62           N  
ATOM   7669  CZ  ARG D 162     235.470 177.836 195.031  1.00 74.62           C  
ATOM   7670  NH1 ARG D 162     236.530 177.533 195.765  1.00 74.62           N  
ATOM   7671  NH2 ARG D 162     235.192 177.116 193.954  1.00 74.62           N  
ATOM   7672  N   VAL D 163     230.884 182.646 191.157  1.00 71.41           N  
ATOM   7673  CA  VAL D 163     229.655 183.043 190.488  1.00 71.41           C  
ATOM   7674  C   VAL D 163     229.939 183.916 189.269  1.00 71.41           C  
ATOM   7675  O   VAL D 163     229.236 183.816 188.262  1.00 71.41           O  
ATOM   7676  CB  VAL D 163     228.707 183.741 191.470  1.00 71.41           C  
ATOM   7677  CG1 VAL D 163     227.364 183.941 190.828  1.00 71.41           C  
ATOM   7678  CG2 VAL D 163     228.551 182.902 192.717  1.00 71.41           C  
ATOM   7679  N   LEU D 164     230.965 184.762 189.325  1.00 75.81           N  
ATOM   7680  CA  LEU D 164     231.435 185.397 188.099  1.00 75.81           C  
ATOM   7681  C   LEU D 164     231.929 184.384 187.088  1.00 75.81           C  
ATOM   7682  O   LEU D 164     232.049 184.713 185.905  1.00 75.81           O  
ATOM   7683  CB  LEU D 164     232.554 186.397 188.351  1.00 75.81           C  
ATOM   7684  CG  LEU D 164     232.228 187.798 188.842  1.00 75.81           C  
ATOM   7685  CD1 LEU D 164     231.789 187.811 190.277  1.00 75.81           C  
ATOM   7686  CD2 LEU D 164     233.437 188.701 188.623  1.00 75.81           C  
ATOM   7687  N   ARG D 165     232.258 183.174 187.523  1.00 82.14           N  
ATOM   7688  CA  ARG D 165     232.560 182.135 186.557  1.00 82.14           C  
ATOM   7689  C   ARG D 165     231.328 181.712 185.770  1.00 82.14           C  
ATOM   7690  O   ARG D 165     231.466 181.122 184.696  1.00 82.14           O  
ATOM   7691  CB  ARG D 165     233.172 180.934 187.264  1.00 82.14           C  
ATOM   7692  CG  ARG D 165     233.787 179.933 186.324  1.00 82.14           C  
ATOM   7693  CD  ARG D 165     234.653 180.627 185.302  1.00 82.14           C  
ATOM   7694  NE  ARG D 165     235.058 179.734 184.228  1.00 82.14           N  
ATOM   7695  CZ  ARG D 165     234.243 179.276 183.288  1.00 82.14           C  
ATOM   7696  NH1 ARG D 165     232.969 179.631 183.279  1.00 82.14           N  
ATOM   7697  NH2 ARG D 165     234.706 178.470 182.350  1.00 82.14           N  
ATOM   7698  N   LEU D 166     230.132 182.014 186.265  1.00 80.17           N  
ATOM   7699  CA  LEU D 166     228.908 181.510 185.658  1.00 80.17           C  
ATOM   7700  C   LEU D 166     228.476 182.271 184.414  1.00 80.17           C  
ATOM   7701  O   LEU D 166     227.662 181.750 183.646  1.00 80.17           O  
ATOM   7702  CB  LEU D 166     227.776 181.544 186.678  1.00 80.17           C  
ATOM   7703  CG  LEU D 166     227.453 180.209 187.324  1.00 80.17           C  
ATOM   7704  CD1 LEU D 166     226.348 180.363 188.339  1.00 80.17           C  
ATOM   7705  CD2 LEU D 166     227.048 179.250 186.240  1.00 80.17           C  
ATOM   7706  N   VAL D 167     228.970 183.488 184.199  1.00 83.93           N  
ATOM   7707  CA  VAL D 167     228.452 184.281 183.093  1.00 83.93           C  
ATOM   7708  C   VAL D 167     228.879 183.690 181.760  1.00 83.93           C  
ATOM   7709  O   VAL D 167     228.082 183.616 180.816  1.00 83.93           O  
ATOM   7710  CB  VAL D 167     228.887 185.747 183.237  1.00 83.93           C  
ATOM   7711  CG1 VAL D 167     228.211 186.356 184.430  1.00 83.93           C  
ATOM   7712  CG2 VAL D 167     230.379 185.849 183.386  1.00 83.93           C  
ATOM   7713  N   HIS D 168     230.135 183.264 181.649  1.00 92.30           N  
ATOM   7714  CA  HIS D 168     230.560 182.639 180.407  1.00 92.30           C  
ATOM   7715  C   HIS D 168     229.815 181.338 180.164  1.00 92.30           C  
ATOM   7716  O   HIS D 168     229.685 180.901 179.017  1.00 92.30           O  
ATOM   7717  CB  HIS D 168     232.057 182.388 180.411  1.00 92.30           C  
ATOM   7718  CG  HIS D 168     232.533 181.711 179.171  1.00 92.30           C  
ATOM   7719  ND1 HIS D 168     232.672 182.373 177.971  1.00 92.30           N  
ATOM   7720  CD2 HIS D 168     232.860 180.421 178.930  1.00 92.30           C  
ATOM   7721  CE1 HIS D 168     233.085 181.524 177.048  1.00 92.30           C  
ATOM   7722  NE2 HIS D 168     233.207 180.333 177.604  1.00 92.30           N  
ATOM   7723  N   VAL D 169     229.334 180.699 181.227  1.00 88.56           N  
ATOM   7724  CA  VAL D 169     228.455 179.551 181.064  1.00 88.56           C  
ATOM   7725  C   VAL D 169     227.122 179.986 180.484  1.00 88.56           C  
ATOM   7726  O   VAL D 169     226.611 179.385 179.534  1.00 88.56           O  
ATOM   7727  CB  VAL D 169     228.273 178.834 182.408  1.00 88.56           C  
ATOM   7728  CG1 VAL D 169     227.136 177.866 182.317  1.00 88.56           C  
ATOM   7729  CG2 VAL D 169     229.543 178.113 182.774  1.00 88.56           C  
ATOM   7730  N   CYS D 170     226.543 181.044 181.042  1.00 91.57           N  
ATOM   7731  CA  CYS D 170     225.262 181.530 180.548  1.00 91.57           C  
ATOM   7732  C   CYS D 170     225.346 182.015 179.111  1.00 91.57           C  
ATOM   7733  O   CYS D 170     224.320 182.063 178.428  1.00 91.57           O  
ATOM   7734  CB  CYS D 170     224.739 182.647 181.445  1.00 91.57           C  
ATOM   7735  SG  CYS D 170     224.032 182.064 183.000  1.00 91.57           S  
ATOM   7736  N   MET D 171     226.544 182.363 178.639  1.00 93.00           N  
ATOM   7737  CA  MET D 171     226.693 182.823 177.261  1.00 93.00           C  
ATOM   7738  C   MET D 171     226.176 181.814 176.248  1.00 93.00           C  
ATOM   7739  O   MET D 171     225.701 182.201 175.177  1.00 93.00           O  
ATOM   7740  CB  MET D 171     228.150 183.126 176.955  1.00 93.00           C  
ATOM   7741  CG  MET D 171     228.706 184.269 177.720  1.00 93.00           C  
ATOM   7742  SD  MET D 171     229.789 185.180 176.628  1.00 93.00           S  
ATOM   7743  CE  MET D 171     228.593 185.941 175.537  1.00 93.00           C  
ATOM   7744  N   ALA D 172     226.244 180.543 176.553  1.00 95.59           N  
ATOM   7745  CA  ALA D 172     225.802 179.543 175.587  1.00 95.59           C  
ATOM   7746  C   ALA D 172     224.289 179.530 175.371  1.00 95.59           C  
ATOM   7747  O   ALA D 172     223.777 178.632 174.692  1.00 95.59           O  
ATOM   7748  CB  ALA D 172     226.268 178.160 176.037  1.00 95.59           C  
ATOM   7749  N   VAL D 173     223.575 180.505 175.924  1.00 94.23           N  
ATOM   7750  CA  VAL D 173     222.122 180.484 176.025  1.00 94.23           C  
ATOM   7751  C   VAL D 173     221.650 181.706 175.238  1.00 94.23           C  
ATOM   7752  O   VAL D 173     220.932 182.571 175.749  1.00 94.23           O  
ATOM   7753  CB  VAL D 173     221.662 180.432 177.498  1.00 94.23           C  
ATOM   7754  CG1 VAL D 173     220.193 180.789 177.688  1.00 94.23           C  
ATOM   7755  CG2 VAL D 173     221.935 179.063 178.070  1.00 94.23           C  
ATOM   7756  N   GLU D 174     222.154 181.838 174.012  1.00 93.91           N  
ATOM   7757  CA  GLU D 174     222.199 183.049 173.197  1.00 93.91           C  
ATOM   7758  C   GLU D 174     220.967 183.957 173.250  1.00 93.91           C  
ATOM   7759  O   GLU D 174     221.120 185.161 173.012  1.00 93.91           O  
ATOM   7760  CB  GLU D 174     222.536 182.675 171.747  1.00 93.91           C  
ATOM   7761  CG  GLU D 174     221.461 181.995 170.928  1.00 93.91           C  
ATOM   7762  CD  GLU D 174     221.332 180.513 171.237  1.00 93.91           C  
ATOM   7763  OE1 GLU D 174     221.427 180.139 172.423  1.00 93.91           O  
ATOM   7764  OE2 GLU D 174     221.132 179.721 170.292  1.00 93.91           O  
ATOM   7765  N   PRO D 175     219.742 183.479 173.526  1.00 89.28           N  
ATOM   7766  CA  PRO D 175     218.715 184.437 173.961  1.00 89.28           C  
ATOM   7767  C   PRO D 175     219.172 185.298 175.131  1.00 89.28           C  
ATOM   7768  O   PRO D 175     218.633 186.384 175.354  1.00 89.28           O  
ATOM   7769  CB  PRO D 175     217.541 183.538 174.351  1.00 89.28           C  
ATOM   7770  CG  PRO D 175     217.675 182.385 173.463  1.00 89.28           C  
ATOM   7771  CD  PRO D 175     219.144 182.156 173.274  1.00 89.28           C  
ATOM   7772  N   LEU D 176     220.158 184.818 175.889  1.00 84.86           N  
ATOM   7773  CA  LEU D 176     220.813 185.616 176.917  1.00 84.86           C  
ATOM   7774  C   LEU D 176     222.027 186.351 176.373  1.00 84.86           C  
ATOM   7775  O   LEU D 176     222.233 187.528 176.677  1.00 84.86           O  
ATOM   7776  CB  LEU D 176     221.257 184.735 178.080  1.00 84.86           C  
ATOM   7777  CG  LEU D 176     220.208 184.145 179.001  1.00 84.86           C  
ATOM   7778  CD1 LEU D 176     220.896 183.363 180.085  1.00 84.86           C  
ATOM   7779  CD2 LEU D 176     219.386 185.241 179.587  1.00 84.86           C  
ATOM   7780  N   ALA D 177     222.837 185.664 175.570  1.00 84.87           N  
ATOM   7781  CA  ALA D 177     224.131 186.206 175.185  1.00 84.87           C  
ATOM   7782  C   ALA D 177     224.003 187.530 174.454  1.00 84.87           C  
ATOM   7783  O   ALA D 177     224.896 188.375 174.556  1.00 84.87           O  
ATOM   7784  CB  ALA D 177     224.889 185.204 174.322  1.00 84.87           C  
ATOM   7785  N   ARG D 178     222.917 187.740 173.714  1.00 83.65           N  
ATOM   7786  CA  ARG D 178     222.801 188.999 172.996  1.00 83.65           C  
ATOM   7787  C   ARG D 178     222.696 190.180 173.945  1.00 83.65           C  
ATOM   7788  O   ARG D 178     223.203 191.256 173.626  1.00 83.65           O  
ATOM   7789  CB  ARG D 178     221.612 188.977 172.043  1.00 83.65           C  
ATOM   7790  CG  ARG D 178     220.268 189.089 172.705  1.00 83.65           C  
ATOM   7791  CD  ARG D 178     219.176 188.562 171.802  1.00 83.65           C  
ATOM   7792  NE  ARG D 178     219.494 187.236 171.287  1.00 83.65           N  
ATOM   7793  CZ  ARG D 178     218.708 186.553 170.465  1.00 83.65           C  
ATOM   7794  NH1 ARG D 178     219.072 185.352 170.042  1.00 83.65           N  
ATOM   7795  NH2 ARG D 178     217.557 187.074 170.069  1.00 83.65           N  
ATOM   7796  N   ILE D 179     222.083 190.004 175.113  1.00 78.74           N  
ATOM   7797  CA  ILE D 179     222.040 191.091 176.084  1.00 78.74           C  
ATOM   7798  C   ILE D 179     223.443 191.466 176.535  1.00 78.74           C  
ATOM   7799  O   ILE D 179     223.805 192.648 176.569  1.00 78.74           O  
ATOM   7800  CB  ILE D 179     221.154 190.694 177.271  1.00 78.74           C  
ATOM   7801  CG1 ILE D 179     219.728 190.502 176.801  1.00 78.74           C  
ATOM   7802  CG2 ILE D 179     221.184 191.759 178.316  1.00 78.74           C  
ATOM   7803  CD1 ILE D 179     219.133 191.747 176.259  1.00 78.74           C  
ATOM   7804  N   ILE D 180     224.254 190.469 176.879  1.00 80.12           N  
ATOM   7805  CA  ILE D 180     225.611 190.738 177.328  1.00 80.12           C  
ATOM   7806  C   ILE D 180     226.420 191.372 176.212  1.00 80.12           C  
ATOM   7807  O   ILE D 180     227.235 192.271 176.448  1.00 80.12           O  
ATOM   7808  CB  ILE D 180     226.266 189.445 177.832  1.00 80.12           C  
ATOM   7809  CG1 ILE D 180     225.441 188.843 178.963  1.00 80.12           C  
ATOM   7810  CG2 ILE D 180     227.681 189.715 178.287  1.00 80.12           C  
ATOM   7811  CD1 ILE D 180     225.864 187.453 179.334  1.00 80.12           C  
ATOM   7812  N   LYS D 181     226.225 190.906 174.981  1.00 81.96           N  
ATOM   7813  CA  LYS D 181     226.964 191.479 173.867  1.00 81.96           C  
ATOM   7814  C   LYS D 181     226.572 192.931 173.640  1.00 81.96           C  
ATOM   7815  O   LYS D 181     227.426 193.768 173.336  1.00 81.96           O  
ATOM   7816  CB  LYS D 181     226.745 190.651 172.609  1.00 81.96           C  
ATOM   7817  CG  LYS D 181     227.320 189.253 172.704  1.00 81.96           C  
ATOM   7818  CD  LYS D 181     228.571 189.092 171.846  1.00 81.96           C  
ATOM   7819  CE  LYS D 181     228.983 187.626 171.735  1.00 81.96           C  
ATOM   7820  NZ  LYS D 181     230.425 187.457 171.401  1.00 81.96           N  
ATOM   7821  N   VAL D 182     225.287 193.252 173.792  1.00 89.08           N  
ATOM   7822  CA  VAL D 182     224.860 194.643 173.686  1.00 89.08           C  
ATOM   7823  C   VAL D 182     225.517 195.486 174.760  1.00 89.08           C  
ATOM   7824  O   VAL D 182     226.003 196.590 174.493  1.00 89.08           O  
ATOM   7825  CB  VAL D 182     223.332 194.750 173.773  1.00 89.08           C  
ATOM   7826  CG1 VAL D 182     222.934 196.199 173.775  1.00 89.08           C  
ATOM   7827  CG2 VAL D 182     222.692 194.056 172.605  1.00 89.08           C  
ATOM   7828  N   ILE D 183     225.520 194.993 175.995  1.00 85.88           N  
ATOM   7829  CA  ILE D 183     226.125 195.748 177.086  1.00 85.88           C  
ATOM   7830  C   ILE D 183     227.591 196.017 176.790  1.00 85.88           C  
ATOM   7831  O   ILE D 183     228.075 197.151 176.897  1.00 85.88           O  
ATOM   7832  CB  ILE D 183     225.954 194.991 178.410  1.00 85.88           C  
ATOM   7833  CG1 ILE D 183     224.491 195.003 178.830  1.00 85.88           C  
ATOM   7834  CG2 ILE D 183     226.830 195.592 179.476  1.00 85.88           C  
ATOM   7835  CD1 ILE D 183     224.131 193.886 179.773  1.00 85.88           C  
ATOM   7836  N   LEU D 184     228.319 194.974 176.405  1.00 88.14           N  
ATOM   7837  CA  LEU D 184     229.743 195.130 176.154  1.00 88.14           C  
ATOM   7838  C   LEU D 184     230.000 196.077 174.995  1.00 88.14           C  
ATOM   7839  O   LEU D 184     230.891 196.929 175.070  1.00 88.14           O  
ATOM   7840  CB  LEU D 184     230.373 193.771 175.889  1.00 88.14           C  
ATOM   7841  CG  LEU D 184     230.456 192.899 177.131  1.00 88.14           C  
ATOM   7842  CD1 LEU D 184     230.636 191.453 176.732  1.00 88.14           C  
ATOM   7843  CD2 LEU D 184     231.599 193.366 177.998  1.00 88.14           C  
ATOM   7844  N   GLN D 185     229.230 195.954 173.917  1.00 96.39           N  
ATOM   7845  CA  GLN D 185     229.430 196.840 172.780  1.00 96.39           C  
ATOM   7846  C   GLN D 185     229.138 198.288 173.146  1.00 96.39           C  
ATOM   7847  O   GLN D 185     229.876 199.195 172.746  1.00 96.39           O  
ATOM   7848  CB  GLN D 185     228.556 196.400 171.609  1.00 96.39           C  
ATOM   7849  CG  GLN D 185     228.658 197.286 170.366  1.00 96.39           C  
ATOM   7850  CD  GLN D 185     230.080 197.606 169.911  1.00 96.39           C  
ATOM   7851  OE1 GLN D 185     231.050 196.961 170.310  1.00 96.39           O  
ATOM   7852  NE2 GLN D 185     230.201 198.625 169.068  1.00 96.39           N  
ATOM   7853  N   SER D 186     228.075 198.528 173.907  1.00 95.46           N  
ATOM   7854  CA  SER D 186     227.695 199.884 174.267  1.00 95.46           C  
ATOM   7855  C   SER D 186     228.544 200.468 175.379  1.00 95.46           C  
ATOM   7856  O   SER D 186     228.413 201.659 175.664  1.00 95.46           O  
ATOM   7857  CB  SER D 186     226.231 199.913 174.689  1.00 95.46           C  
ATOM   7858  OG  SER D 186     226.018 199.099 175.824  1.00 95.46           O  
ATOM   7859  N   MET D 187     229.384 199.664 176.023  1.00 93.46           N  
ATOM   7860  CA  MET D 187     230.182 200.164 177.142  1.00 93.46           C  
ATOM   7861  C   MET D 187     230.990 201.418 176.833  1.00 93.46           C  
ATOM   7862  O   MET D 187     230.970 202.339 177.661  1.00 93.46           O  
ATOM   7863  CB  MET D 187     231.101 199.050 177.657  1.00 93.46           C  
ATOM   7864  CG  MET D 187     231.636 199.305 179.045  1.00 93.46           C  
ATOM   7865  SD  MET D 187     230.346 199.259 180.299  1.00 93.46           S  
ATOM   7866  CE  MET D 187     231.115 200.181 181.630  1.00 93.46           C  
ATOM   7867  N   PRO D 188     231.730 201.527 175.722  1.00 94.22           N  
ATOM   7868  CA  PRO D 188     232.508 202.763 175.509  1.00 94.22           C  
ATOM   7869  C   PRO D 188     231.662 204.022 175.423  1.00 94.22           C  
ATOM   7870  O   PRO D 188     232.073 205.084 175.917  1.00 94.22           O  
ATOM   7871  CB  PRO D 188     233.252 202.487 174.196  1.00 94.22           C  
ATOM   7872  CG  PRO D 188     232.589 201.320 173.595  1.00 94.22           C  
ATOM   7873  CD  PRO D 188     232.068 200.507 174.720  1.00 94.22           C  
ATOM   7874  N   ASP D 189     230.483 203.941 174.812  1.00 98.48           N  
ATOM   7875  CA  ASP D 189     229.605 205.104 174.790  1.00 98.48           C  
ATOM   7876  C   ASP D 189     229.163 205.479 176.196  1.00 98.48           C  
ATOM   7877  O   ASP D 189     229.094 206.667 176.540  1.00 98.48           O  
ATOM   7878  CB  ASP D 189     228.399 204.830 173.906  1.00 98.48           C  
ATOM   7879  CG  ASP D 189     228.624 205.240 172.478  1.00 98.48           C  
ATOM   7880  OD1 ASP D 189     229.545 206.047 172.237  1.00 98.48           O  
ATOM   7881  OD2 ASP D 189     227.871 204.768 171.598  1.00 98.48           O  
ATOM   7882  N   LEU D 190     228.863 204.477 177.025  1.00 95.21           N  
ATOM   7883  CA  LEU D 190     228.545 204.740 178.420  1.00 95.21           C  
ATOM   7884  C   LEU D 190     229.730 205.344 179.149  1.00 95.21           C  
ATOM   7885  O   LEU D 190     229.548 206.159 180.054  1.00 95.21           O  
ATOM   7886  CB  LEU D 190     228.094 203.458 179.105  1.00 95.21           C  
ATOM   7887  CG  LEU D 190     226.687 203.051 178.696  1.00 95.21           C  
ATOM   7888  CD1 LEU D 190     226.239 201.797 179.412  1.00 95.21           C  
ATOM   7889  CD2 LEU D 190     225.736 204.193 178.959  1.00 95.21           C  
ATOM   7890  N   ALA D 191     230.947 204.962 178.774  1.00 95.00           N  
ATOM   7891  CA  ALA D 191     232.122 205.596 179.355  1.00 95.00           C  
ATOM   7892  C   ALA D 191     232.160 207.076 179.018  1.00 95.00           C  
ATOM   7893  O   ALA D 191     232.467 207.910 179.876  1.00 95.00           O  
ATOM   7894  CB  ALA D 191     233.391 204.904 178.865  1.00 95.00           C  
ATOM   7895  N   ASN D 192     231.847 207.423 177.771  1.00100.38           N  
ATOM   7896  CA  ASN D 192     231.822 208.835 177.399  1.00100.38           C  
ATOM   7897  C   ASN D 192     230.746 209.595 178.167  1.00100.38           C  
ATOM   7898  O   ASN D 192     230.973 210.719 178.628  1.00100.38           O  
ATOM   7899  CB  ASN D 192     231.614 208.981 175.897  1.00100.38           C  
ATOM   7900  CG  ASN D 192     232.916 208.986 175.134  1.00100.38           C  
ATOM   7901  OD1 ASN D 192     233.988 208.843 175.716  1.00100.38           O  
ATOM   7902  ND2 ASN D 192     232.830 209.148 173.823  1.00100.38           N  
ATOM   7903  N   VAL D 193     229.566 208.996 178.317  1.00 93.65           N  
ATOM   7904  CA  VAL D 193     228.488 209.672 179.035  1.00 93.65           C  
ATOM   7905  C   VAL D 193     228.834 209.828 180.511  1.00 93.65           C  
ATOM   7906  O   VAL D 193     228.519 210.850 181.135  1.00 93.65           O  
ATOM   7907  CB  VAL D 193     227.163 208.919 178.836  1.00 93.65           C  
ATOM   7908  CG1 VAL D 193     226.087 209.503 179.716  1.00 93.65           C  
ATOM   7909  CG2 VAL D 193     226.748 208.997 177.400  1.00 93.65           C  
ATOM   7910  N   MET D 194     229.511 208.809 181.052  1.00 94.24           N  
ATOM   7911  CA  MET D 194     229.965 208.820 182.468  1.00 94.24           C  
ATOM   7912  C   MET D 194     230.966 209.969 182.637  1.00 94.24           C  
ATOM   7913  O   MET D 194     230.869 210.694 183.647  1.00 94.24           O  
ATOM   7914  CB  MET D 194     230.652 207.497 182.823  1.00 94.24           C  
ATOM   7915  CG  MET D 194     231.145 207.438 184.257  1.00 94.24           C  
ATOM   7916  SD  MET D 194     231.960 205.869 184.648  1.00 94.24           S  
ATOM   7917  CE  MET D 194     230.624 204.717 184.335  1.00 94.24           C  
ATOM   7918  N   ALA D 195     231.870 210.136 181.664  1.00 91.01           N  
ATOM   7919  CA  ALA D 195     232.847 211.217 181.701  1.00 91.01           C  
ATOM   7920  C   ALA D 195     232.163 212.573 181.663  1.00 91.01           C  
ATOM   7921  O   ALA D 195     232.530 213.483 182.414  1.00 91.01           O  
ATOM   7922  CB  ALA D 195     233.826 211.080 180.539  1.00 91.01           C  
ATOM   7923  N   LEU D 196     231.167 212.726 180.790  1.00 94.38           N  
ATOM   7924  CA  LEU D 196     230.358 213.943 180.780  1.00 94.38           C  
ATOM   7925  C   LEU D 196     229.764 214.235 182.151  1.00 94.38           C  
ATOM   7926  O   LEU D 196     229.876 215.353 182.665  1.00 94.38           O  
ATOM   7927  CB  LEU D 196     229.245 213.819 179.746  1.00 94.38           C  
ATOM   7928  CG  LEU D 196     228.318 215.024 179.652  1.00 94.38           C  
ATOM   7929  CD1 LEU D 196     229.076 216.231 179.243  1.00 94.38           C  
ATOM   7930  CD2 LEU D 196     227.201 214.757 178.680  1.00 94.38           C  
ATOM   7931  N   ILE D 197     229.121 213.240 182.758  1.00 90.92           N  
ATOM   7932  CA  ILE D 197     228.418 213.485 184.015  1.00 90.92           C  
ATOM   7933  C   ILE D 197     229.399 213.838 185.125  1.00 90.92           C  
ATOM   7934  O   ILE D 197     229.145 214.735 185.931  1.00 90.92           O  
ATOM   7935  CB  ILE D 197     227.540 212.283 184.388  1.00 90.92           C  
ATOM   7936  CG1 ILE D 197     226.460 212.140 183.343  1.00 90.92           C  
ATOM   7937  CG2 ILE D 197     226.880 212.506 185.711  1.00 90.92           C  
ATOM   7938  CD1 ILE D 197     225.637 213.382 183.231  1.00 90.92           C  
ATOM   7939  N   LEU D 198     230.526 213.133 185.194  1.00 88.41           N  
ATOM   7940  CA  LEU D 198     231.515 213.440 186.221  1.00 88.41           C  
ATOM   7941  C   LEU D 198     232.109 214.826 186.019  1.00 88.41           C  
ATOM   7942  O   LEU D 198     232.314 215.570 186.988  1.00 88.41           O  
ATOM   7943  CB  LEU D 198     232.618 212.389 186.212  1.00 88.41           C  
ATOM   7944  CG  LEU D 198     233.676 212.569 187.295  1.00 88.41           C  
ATOM   7945  CD1 LEU D 198     233.052 212.432 188.662  1.00 88.41           C  
ATOM   7946  CD2 LEU D 198     234.828 211.607 187.111  1.00 88.41           C  
ATOM   7947  N   PHE D 199     232.411 215.187 184.771  1.00 92.49           N  
ATOM   7948  CA  PHE D 199     232.997 216.493 184.507  1.00 92.49           C  
ATOM   7949  C   PHE D 199     232.002 217.599 184.812  1.00 92.49           C  
ATOM   7950  O   PHE D 199     232.388 218.725 185.135  1.00 92.49           O  
ATOM   7951  CB  PHE D 199     233.467 216.561 183.057  1.00 92.49           C  
ATOM   7952  CG  PHE D 199     234.518 217.593 182.816  1.00 92.49           C  
ATOM   7953  CD1 PHE D 199     235.710 217.554 183.508  1.00 92.49           C  
ATOM   7954  CD2 PHE D 199     234.310 218.607 181.906  1.00 92.49           C  
ATOM   7955  CE1 PHE D 199     236.668 218.504 183.296  1.00 92.49           C  
ATOM   7956  CE2 PHE D 199     235.267 219.561 181.690  1.00 92.49           C  
ATOM   7957  CZ  PHE D 199     236.446 219.512 182.385  1.00 92.49           C  
ATOM   7958  N   PHE D 200     230.714 217.296 184.698  1.00 87.95           N  
ATOM   7959  CA  PHE D 200     229.687 218.235 185.124  1.00 87.95           C  
ATOM   7960  C   PHE D 200     229.612 218.322 186.641  1.00 87.95           C  
ATOM   7961  O   PHE D 200     229.527 219.417 187.201  1.00 87.95           O  
ATOM   7962  CB  PHE D 200     228.351 217.807 184.531  1.00 87.95           C  
ATOM   7963  CG  PHE D 200     227.176 218.524 185.090  1.00 87.95           C  
ATOM   7964  CD1 PHE D 200     226.963 219.849 184.797  1.00 87.95           C  
ATOM   7965  CD2 PHE D 200     226.253 217.856 185.870  1.00 87.95           C  
ATOM   7966  CE1 PHE D 200     225.873 220.503 185.296  1.00 87.95           C  
ATOM   7967  CE2 PHE D 200     225.156 218.507 186.374  1.00 87.95           C  
ATOM   7968  CZ  PHE D 200     224.966 219.829 186.087  1.00 87.95           C  
ATOM   7969  N   MET D 201     229.652 217.177 187.322  1.00 83.93           N  
ATOM   7970  CA  MET D 201     229.543 217.137 188.775  1.00 83.93           C  
ATOM   7971  C   MET D 201     230.688 217.837 189.477  1.00 83.93           C  
ATOM   7972  O   MET D 201     230.468 218.427 190.534  1.00 83.93           O  
ATOM   7973  CB  MET D 201     229.493 215.700 189.290  1.00 83.93           C  
ATOM   7974  CG  MET D 201     228.265 214.917 188.917  1.00 83.93           C  
ATOM   7975  SD  MET D 201     228.365 213.222 189.503  1.00 83.93           S  
ATOM   7976  CE  MET D 201     228.196 213.468 191.254  1.00 83.93           C  
ATOM   7977  N   LEU D 202     231.904 217.758 188.943  1.00 82.68           N  
ATOM   7978  CA  LEU D 202     233.033 218.368 189.641  1.00 82.68           C  
ATOM   7979  C   LEU D 202     232.868 219.876 189.764  1.00 82.68           C  
ATOM   7980  O   LEU D 202     233.136 220.453 190.824  1.00 82.68           O  
ATOM   7981  CB  LEU D 202     234.334 218.028 188.930  1.00 82.68           C  
ATOM   7982  CG  LEU D 202     234.735 216.567 189.081  1.00 82.68           C  
ATOM   7983  CD1 LEU D 202     236.123 216.354 188.532  1.00 82.68           C  
ATOM   7984  CD2 LEU D 202     234.657 216.146 190.531  1.00 82.68           C  
ATOM   7985  N   VAL D 203     232.425 220.533 188.696  1.00 84.18           N  
ATOM   7986  CA  VAL D 203     232.273 221.984 188.731  1.00 84.18           C  
ATOM   7987  C   VAL D 203     231.226 222.387 189.764  1.00 84.18           C  
ATOM   7988  O   VAL D 203     231.453 223.280 190.593  1.00 84.18           O  
ATOM   7989  CB  VAL D 203     231.922 222.510 187.330  1.00 84.18           C  
ATOM   7990  CG1 VAL D 203     231.603 223.978 187.383  1.00 84.18           C  
ATOM   7991  CG2 VAL D 203     233.056 222.239 186.379  1.00 84.18           C  
ATOM   7992  N   PHE D 204     230.064 221.735 189.738  1.00 83.23           N  
ATOM   7993  CA  PHE D 204     229.064 222.067 190.741  1.00 83.23           C  
ATOM   7994  C   PHE D 204     229.523 221.710 192.140  1.00 83.23           C  
ATOM   7995  O   PHE D 204     229.109 222.359 193.100  1.00 83.23           O  
ATOM   7996  CB  PHE D 204     227.731 221.391 190.464  1.00 83.23           C  
ATOM   7997  CG  PHE D 204     226.840 222.174 189.569  1.00 83.23           C  
ATOM   7998  CD1 PHE D 204     227.306 223.296 188.922  1.00 83.23           C  
ATOM   7999  CD2 PHE D 204     225.504 221.867 189.476  1.00 83.23           C  
ATOM   8000  CE1 PHE D 204     226.476 224.037 188.122  1.00 83.23           C  
ATOM   8001  CE2 PHE D 204     224.671 222.607 188.686  1.00 83.23           C  
ATOM   8002  CZ  PHE D 204     225.156 223.695 188.009  1.00 83.23           C  
ATOM   8003  N   SER D 205     230.363 220.691 192.288  1.00 80.75           N  
ATOM   8004  CA  SER D 205     230.908 220.394 193.604  1.00 80.75           C  
ATOM   8005  C   SER D 205     231.764 221.547 194.100  1.00 80.75           C  
ATOM   8006  O   SER D 205     231.659 221.957 195.260  1.00 80.75           O  
ATOM   8007  CB  SER D 205     231.710 219.101 193.557  1.00 80.75           C  
ATOM   8008  OG  SER D 205     232.261 218.826 194.823  1.00 80.75           O  
ATOM   8009  N   VAL D 206     232.607 222.096 193.225  1.00 82.46           N  
ATOM   8010  CA  VAL D 206     233.412 223.256 193.602  1.00 82.46           C  
ATOM   8011  C   VAL D 206     232.511 224.392 194.063  1.00 82.46           C  
ATOM   8012  O   VAL D 206     232.717 224.991 195.129  1.00 82.46           O  
ATOM   8013  CB  VAL D 206     234.297 223.707 192.428  1.00 82.46           C  
ATOM   8014  CG1 VAL D 206     234.773 225.127 192.652  1.00 82.46           C  
ATOM   8015  CG2 VAL D 206     235.466 222.789 192.254  1.00 82.46           C  
ATOM   8016  N   PHE D 207     231.501 224.708 193.257  1.00 91.12           N  
ATOM   8017  CA  PHE D 207     230.660 225.856 193.571  1.00 91.12           C  
ATOM   8018  C   PHE D 207     229.898 225.624 194.866  1.00 91.12           C  
ATOM   8019  O   PHE D 207     229.782 226.527 195.704  1.00 91.12           O  
ATOM   8020  CB  PHE D 207     229.690 226.139 192.424  1.00 91.12           C  
ATOM   8021  CG  PHE D 207     230.356 226.542 191.125  1.00 91.12           C  
ATOM   8022  CD1 PHE D 207     231.729 226.516 190.978  1.00 91.12           C  
ATOM   8023  CD2 PHE D 207     229.591 226.945 190.046  1.00 91.12           C  
ATOM   8024  CE1 PHE D 207     232.320 226.878 189.788  1.00 91.12           C  
ATOM   8025  CE2 PHE D 207     230.182 227.308 188.857  1.00 91.12           C  
ATOM   8026  CZ  PHE D 207     231.545 227.276 188.731  1.00 91.12           C  
ATOM   8027  N   GLY D 208     229.392 224.407 195.058  1.00 88.18           N  
ATOM   8028  CA  GLY D 208     228.630 224.107 196.254  1.00 88.18           C  
ATOM   8029  C   GLY D 208     229.469 224.153 197.512  1.00 88.18           C  
ATOM   8030  O   GLY D 208     229.003 224.611 198.553  1.00 88.18           O  
ATOM   8031  N   VAL D 209     230.710 223.672 197.444  1.00 88.10           N  
ATOM   8032  CA  VAL D 209     231.582 223.767 198.609  1.00 88.10           C  
ATOM   8033  C   VAL D 209     231.860 225.221 198.938  1.00 88.10           C  
ATOM   8034  O   VAL D 209     231.690 225.660 200.080  1.00 88.10           O  
ATOM   8035  CB  VAL D 209     232.888 223.000 198.379  1.00 88.10           C  
ATOM   8036  CG1 VAL D 209     233.868 223.383 199.430  1.00 88.10           C  
ATOM   8037  CG2 VAL D 209     232.639 221.535 198.436  1.00 88.10           C  
ATOM   8038  N   THR D 210     232.273 226.000 197.934  1.00 91.43           N  
ATOM   8039  CA  THR D 210     232.645 227.383 198.207  1.00 91.43           C  
ATOM   8040  C   THR D 210     231.451 228.258 198.563  1.00 91.43           C  
ATOM   8041  O   THR D 210     231.653 229.389 199.011  1.00 91.43           O  
ATOM   8042  CB  THR D 210     233.379 227.982 197.018  1.00 91.43           C  
ATOM   8043  OG1 THR D 210     234.019 229.189 197.428  1.00 91.43           O  
ATOM   8044  CG2 THR D 210     232.407 228.320 195.933  1.00 91.43           C  
ATOM   8045  N   LEU D 211     230.222 227.779 198.364  1.00 94.61           N  
ATOM   8046  CA  LEU D 211     229.056 228.414 198.974  1.00 94.61           C  
ATOM   8047  C   LEU D 211     228.779 227.894 200.378  1.00 94.61           C  
ATOM   8048  O   LEU D 211     228.867 228.645 201.348  1.00 94.61           O  
ATOM   8049  CB  LEU D 211     227.817 228.210 198.104  1.00 94.61           C  
ATOM   8050  CG  LEU D 211     227.802 228.973 196.798  1.00 94.61           C  
ATOM   8051  CD1 LEU D 211     226.636 228.566 195.938  1.00 94.61           C  
ATOM   8052  CD2 LEU D 211     227.630 230.400 197.225  1.00 94.61           C  
ATOM   8053  N   PHE D 212     228.455 226.613 200.506  1.00 92.36           N  
ATOM   8054  CA  PHE D 212     228.009 226.048 201.771  1.00 92.36           C  
ATOM   8055  C   PHE D 212     229.142 225.401 202.555  1.00 92.36           C  
ATOM   8056  O   PHE D 212     228.931 224.401 203.243  1.00 92.36           O  
ATOM   8057  CB  PHE D 212     226.879 225.055 201.526  1.00 92.36           C  
ATOM   8058  CG  PHE D 212     225.948 225.476 200.441  1.00 92.36           C  
ATOM   8059  CD1 PHE D 212     225.108 226.554 200.617  1.00 92.36           C  
ATOM   8060  CD2 PHE D 212     225.929 224.816 199.232  1.00 92.36           C  
ATOM   8061  CE1 PHE D 212     224.256 226.953 199.615  1.00 92.36           C  
ATOM   8062  CE2 PHE D 212     225.082 225.212 198.229  1.00 92.36           C  
ATOM   8063  CZ  PHE D 212     224.245 226.281 198.421  1.00 92.36           C  
ATOM   8064  N   GLY D 213     230.352 225.931 202.442  1.00101.67           N  
ATOM   8065  CA  GLY D 213     231.361 225.662 203.440  1.00101.67           C  
ATOM   8066  C   GLY D 213     231.199 226.595 204.625  1.00101.67           C  
ATOM   8067  O   GLY D 213     230.694 227.711 204.503  1.00101.67           O  
ATOM   8068  N   ALA D 214     231.619 226.121 205.796  1.00107.68           N  
ATOM   8069  CA  ALA D 214     231.399 226.835 207.053  1.00107.68           C  
ATOM   8070  C   ALA D 214     229.914 227.082 207.299  1.00107.68           C  
ATOM   8071  O   ALA D 214     229.530 228.036 207.980  1.00107.68           O  
ATOM   8072  CB  ALA D 214     232.178 228.151 207.097  1.00107.68           C  
ATOM   8073  N   PHE D 215     229.079 226.222 206.727  1.00103.59           N  
ATOM   8074  CA  PHE D 215     227.635 226.254 206.921  1.00103.59           C  
ATOM   8075  C   PHE D 215     227.116 224.943 206.370  1.00103.59           C  
ATOM   8076  O   PHE D 215     227.311 224.665 205.187  1.00103.59           O  
ATOM   8077  CB  PHE D 215     227.016 227.438 206.195  1.00103.59           C  
ATOM   8078  CG  PHE D 215     225.525 227.487 206.271  1.00103.59           C  
ATOM   8079  CD1 PHE D 215     224.873 227.245 207.457  1.00103.59           C  
ATOM   8080  CD2 PHE D 215     224.777 227.796 205.158  1.00103.59           C  
ATOM   8081  CE1 PHE D 215     223.514 227.300 207.526  1.00103.59           C  
ATOM   8082  CE2 PHE D 215     223.418 227.847 205.229  1.00103.59           C  
ATOM   8083  CZ  PHE D 215     222.786 227.599 206.414  1.00103.59           C  
ATOM   8084  N   VAL D 216     226.453 224.154 207.203  1.00 97.69           N  
ATOM   8085  CA  VAL D 216     226.109 222.776 206.856  1.00 97.69           C  
ATOM   8086  C   VAL D 216     227.374 222.047 206.416  1.00 97.69           C  
ATOM   8087  O   VAL D 216     227.503 221.699 205.235  1.00 97.69           O  
ATOM   8088  CB  VAL D 216     225.037 222.726 205.754  1.00 97.69           C  
ATOM   8089  CG1 VAL D 216     224.571 221.299 205.514  1.00 97.69           C  
ATOM   8090  CG2 VAL D 216     223.881 223.631 206.096  1.00 97.69           C  
ATOM   8091  N   PRO D 217     228.353 221.824 207.298  1.00 93.43           N  
ATOM   8092  CA  PRO D 217     229.561 221.083 206.916  1.00 93.43           C  
ATOM   8093  C   PRO D 217     229.397 219.571 207.029  1.00 93.43           C  
ATOM   8094  O   PRO D 217     230.347 218.811 206.885  1.00 93.43           O  
ATOM   8095  CB  PRO D 217     230.611 221.614 207.897  1.00 93.43           C  
ATOM   8096  CG  PRO D 217     229.995 222.805 208.539  1.00 93.43           C  
ATOM   8097  CD  PRO D 217     228.551 222.482 208.591  1.00 93.43           C  
ATOM   8098  N   LYS D 218     228.175 219.124 207.283  1.00 88.92           N  
ATOM   8099  CA  LYS D 218     227.929 217.698 207.228  1.00 88.92           C  
ATOM   8100  C   LYS D 218     227.945 217.181 205.801  1.00 88.92           C  
ATOM   8101  O   LYS D 218     228.153 215.983 205.595  1.00 88.92           O  
ATOM   8102  CB  LYS D 218     226.587 217.358 207.893  1.00 88.92           C  
ATOM   8103  CG  LYS D 218     226.296 215.875 207.978  1.00 88.92           C  
ATOM   8104  CD  LYS D 218     225.212 215.572 208.993  1.00 88.92           C  
ATOM   8105  CE  LYS D 218     224.280 214.466 208.503  1.00 88.92           C  
ATOM   8106  NZ  LYS D 218     225.007 213.334 207.864  1.00 88.92           N  
ATOM   8107  N   HIS D 219     227.782 218.066 204.816  1.00 83.21           N  
ATOM   8108  CA  HIS D 219     227.720 217.678 203.419  1.00 83.21           C  
ATOM   8109  C   HIS D 219     228.626 218.472 202.493  1.00 83.21           C  
ATOM   8110  O   HIS D 219     228.785 218.064 201.341  1.00 83.21           O  
ATOM   8111  CB  HIS D 219     226.286 217.804 202.895  1.00 83.21           C  
ATOM   8112  CG  HIS D 219     225.251 217.241 203.814  1.00 83.21           C  
ATOM   8113  ND1 HIS D 219     224.982 215.893 203.893  1.00 83.21           N  
ATOM   8114  CD2 HIS D 219     224.411 217.844 204.687  1.00 83.21           C  
ATOM   8115  CE1 HIS D 219     224.022 215.689 204.775  1.00 83.21           C  
ATOM   8116  NE2 HIS D 219     223.658 216.857 205.272  1.00 83.21           N  
ATOM   8117  N   PHE D 220     229.223 219.576 202.936  1.00 87.54           N  
ATOM   8118  CA  PHE D 220     229.884 220.498 202.017  1.00 87.54           C  
ATOM   8119  C   PHE D 220     231.200 221.039 202.574  1.00 87.54           C  
ATOM   8120  O   PHE D 220     231.451 222.244 202.550  1.00 87.54           O  
ATOM   8121  CB  PHE D 220     228.966 221.666 201.678  1.00 87.54           C  
ATOM   8122  CG  PHE D 220     227.902 221.346 200.678  1.00 87.54           C  
ATOM   8123  CD1 PHE D 220     228.187 221.327 199.333  1.00 87.54           C  
ATOM   8124  CD2 PHE D 220     226.606 221.113 201.085  1.00 87.54           C  
ATOM   8125  CE1 PHE D 220     227.212 221.051 198.425  1.00 87.54           C  
ATOM   8126  CE2 PHE D 220     225.627 220.844 200.177  1.00 87.54           C  
ATOM   8127  CZ  PHE D 220     225.928 220.811 198.848  1.00 87.54           C  
ATOM   8128  N   GLN D 221     232.073 220.174 203.089  1.00 91.15           N  
ATOM   8129  CA  GLN D 221     233.381 220.667 203.521  1.00 91.15           C  
ATOM   8130  C   GLN D 221     234.415 220.571 202.411  1.00 91.15           C  
ATOM   8131  O   GLN D 221     234.948 221.582 201.952  1.00 91.15           O  
ATOM   8132  CB  GLN D 221     233.896 219.882 204.728  1.00 91.15           C  
ATOM   8133  CG  GLN D 221     232.892 219.652 205.798  1.00 91.15           C  
ATOM   8134  CD  GLN D 221     233.279 218.510 206.712  1.00 91.15           C  
ATOM   8135  OE1 GLN D 221     233.774 217.479 206.257  1.00 91.15           O  
ATOM   8136  NE2 GLN D 221     233.057 218.687 208.008  1.00 91.15           N  
ATOM   8137  N   ASN D 222     234.707 219.361 201.982  1.00 87.16           N  
ATOM   8138  CA  ASN D 222     235.734 219.108 200.992  1.00 87.16           C  
ATOM   8139  C   ASN D 222     235.097 218.626 199.699  1.00 87.16           C  
ATOM   8140  O   ASN D 222     233.879 218.493 199.587  1.00 87.16           O  
ATOM   8141  CB  ASN D 222     236.753 218.106 201.545  1.00 87.16           C  
ATOM   8142  CG  ASN D 222     236.150 216.747 201.829  1.00 87.16           C  
ATOM   8143  OD1 ASN D 222     235.000 216.483 201.504  1.00 87.16           O  
ATOM   8144  ND2 ASN D 222     236.915 215.894 202.490  1.00 87.16           N  
ATOM   8145  N   MET D 223     235.944 218.371 198.709  1.00 85.98           N  
ATOM   8146  CA  MET D 223     235.445 217.905 197.425  1.00 85.98           C  
ATOM   8147  C   MET D 223     234.724 216.572 197.562  1.00 85.98           C  
ATOM   8148  O   MET D 223     233.664 216.373 196.969  1.00 85.98           O  
ATOM   8149  CB  MET D 223     236.590 217.782 196.433  1.00 85.98           C  
ATOM   8150  CG  MET D 223     236.126 217.558 195.020  1.00 85.98           C  
ATOM   8151  SD  MET D 223     237.202 218.339 193.826  1.00 85.98           S  
ATOM   8152  CE  MET D 223     236.566 219.992 193.902  1.00 85.98           C  
ATOM   8153  N   GLY D 224     235.279 215.643 198.337  1.00 79.30           N  
ATOM   8154  CA  GLY D 224     234.718 214.300 198.372  1.00 79.30           C  
ATOM   8155  C   GLY D 224     233.324 214.238 198.969  1.00 79.30           C  
ATOM   8156  O   GLY D 224     232.436 213.561 198.437  1.00 79.30           O  
ATOM   8157  N   VAL D 225     233.110 214.936 200.080  1.00 75.97           N  
ATOM   8158  CA  VAL D 225     231.790 214.940 200.691  1.00 75.97           C  
ATOM   8159  C   VAL D 225     230.779 215.568 199.746  1.00 75.97           C  
ATOM   8160  O   VAL D 225     229.643 215.095 199.620  1.00 75.97           O  
ATOM   8161  CB  VAL D 225     231.831 215.661 202.047  1.00 75.97           C  
ATOM   8162  CG1 VAL D 225     230.481 215.652 202.669  1.00 75.97           C  
ATOM   8163  CG2 VAL D 225     232.798 214.973 202.968  1.00 75.97           C  
ATOM   8164  N   ALA D 226     231.176 216.635 199.056  1.00 74.00           N  
ATOM   8165  CA  ALA D 226     230.265 217.258 198.107  1.00 74.00           C  
ATOM   8166  C   ALA D 226     229.948 216.328 196.946  1.00 74.00           C  
ATOM   8167  O   ALA D 226     228.798 216.260 196.509  1.00 74.00           O  
ATOM   8168  CB  ALA D 226     230.840 218.571 197.601  1.00 74.00           C  
ATOM   8169  N   LEU D 227     230.945 215.621 196.410  1.00 70.67           N  
ATOM   8170  CA  LEU D 227     230.649 214.631 195.380  1.00 70.67           C  
ATOM   8171  C   LEU D 227     229.638 213.616 195.866  1.00 70.67           C  
ATOM   8172  O   LEU D 227     228.706 213.271 195.139  1.00 70.67           O  
ATOM   8173  CB  LEU D 227     231.910 213.910 194.918  1.00 70.67           C  
ATOM   8174  CG  LEU D 227     232.783 214.444 193.791  1.00 70.67           C  
ATOM   8175  CD1 LEU D 227     231.989 214.402 192.517  1.00 70.67           C  
ATOM   8176  CD2 LEU D 227     233.217 215.837 194.051  1.00 70.67           C  
ATOM   8177  N   TYR D 228     229.803 213.115 197.085  1.00 67.20           N  
ATOM   8178  CA  TYR D 228     228.852 212.119 197.560  1.00 67.20           C  
ATOM   8179  C   TYR D 228     227.459 212.722 197.689  1.00 67.20           C  
ATOM   8180  O   TYR D 228     226.459 212.070 197.375  1.00 67.20           O  
ATOM   8181  CB  TYR D 228     229.314 211.527 198.884  1.00 67.20           C  
ATOM   8182  CG  TYR D 228     228.358 210.509 199.419  1.00 67.20           C  
ATOM   8183  CD1 TYR D 228     228.121 209.343 198.729  1.00 67.20           C  
ATOM   8184  CD2 TYR D 228     227.682 210.716 200.603  1.00 67.20           C  
ATOM   8185  CE1 TYR D 228     227.249 208.409 199.202  1.00 67.20           C  
ATOM   8186  CE2 TYR D 228     226.804 209.788 201.085  1.00 67.20           C  
ATOM   8187  CZ  TYR D 228     226.590 208.634 200.378  1.00 67.20           C  
ATOM   8188  OH  TYR D 228     225.712 207.692 200.850  1.00 67.20           O  
ATOM   8189  N   THR D 229     227.372 213.978 198.128  1.00 68.32           N  
ATOM   8190  CA  THR D 229     226.070 214.634 198.241  1.00 68.32           C  
ATOM   8191  C   THR D 229     225.406 214.805 196.878  1.00 68.32           C  
ATOM   8192  O   THR D 229     224.234 214.457 196.692  1.00 68.32           O  
ATOM   8193  CB  THR D 229     226.233 215.984 198.931  1.00 68.32           C  
ATOM   8194  OG1 THR D 229     226.648 215.773 200.283  1.00 68.32           O  
ATOM   8195  CG2 THR D 229     224.934 216.733 198.929  1.00 68.32           C  
ATOM   8196  N   LEU D 230     226.142 215.338 195.909  1.00 69.36           N  
ATOM   8197  CA  LEU D 230     225.596 215.462 194.563  1.00 69.36           C  
ATOM   8198  C   LEU D 230     225.261 214.114 193.941  1.00 69.36           C  
ATOM   8199  O   LEU D 230     224.381 214.036 193.082  1.00 69.36           O  
ATOM   8200  CB  LEU D 230     226.552 216.243 193.668  1.00 69.36           C  
ATOM   8201  CG  LEU D 230     226.621 217.765 193.751  1.00 69.36           C  
ATOM   8202  CD1 LEU D 230     227.253 218.316 194.990  1.00 69.36           C  
ATOM   8203  CD2 LEU D 230     227.409 218.193 192.549  1.00 69.36           C  
ATOM   8204  N   PHE D 231     225.952 213.048 194.333  1.00 65.19           N  
ATOM   8205  CA  PHE D 231     225.553 211.737 193.847  1.00 65.19           C  
ATOM   8206  C   PHE D 231     224.275 211.262 194.525  1.00 65.19           C  
ATOM   8207  O   PHE D 231     223.502 210.511 193.925  1.00 65.19           O  
ATOM   8208  CB  PHE D 231     226.677 210.730 194.044  1.00 65.19           C  
ATOM   8209  CG  PHE D 231     226.328 209.354 193.591  1.00 65.19           C  
ATOM   8210  CD1 PHE D 231     226.549 208.973 192.293  1.00 65.19           C  
ATOM   8211  CD2 PHE D 231     225.780 208.441 194.465  1.00 65.19           C  
ATOM   8212  CE1 PHE D 231     226.230 207.721 191.875  1.00 65.19           C  
ATOM   8213  CE2 PHE D 231     225.450 207.189 194.046  1.00 65.19           C  
ATOM   8214  CZ  PHE D 231     225.674 206.827 192.752  1.00 65.19           C  
ATOM   8215  N   ILE D 232     224.038 211.666 195.771  1.00 63.94           N  
ATOM   8216  CA  ILE D 232     222.718 211.448 196.355  1.00 63.94           C  
ATOM   8217  C   ILE D 232     221.664 212.131 195.500  1.00 63.94           C  
ATOM   8218  O   ILE D 232     220.636 211.542 195.156  1.00 63.94           O  
ATOM   8219  CB  ILE D 232     222.654 211.971 197.799  1.00 63.94           C  
ATOM   8220  CG1 ILE D 232     223.591 211.214 198.724  1.00 63.94           C  
ATOM   8221  CG2 ILE D 232     221.243 211.854 198.310  1.00 63.94           C  
ATOM   8222  CD1 ILE D 232     223.068 209.917 199.161  1.00 63.94           C  
ATOM   8223  N   CYS D 233     221.914 213.389 195.144  1.00 69.23           N  
ATOM   8224  CA  CYS D 233     220.912 214.164 194.416  1.00 69.23           C  
ATOM   8225  C   CYS D 233     220.653 213.581 193.034  1.00 69.23           C  
ATOM   8226  O   CYS D 233     219.500 213.357 192.653  1.00 69.23           O  
ATOM   8227  CB  CYS D 233     221.347 215.620 194.304  1.00 69.23           C  
ATOM   8228  SG  CYS D 233     221.349 216.496 195.861  1.00 69.23           S  
ATOM   8229  N   ILE D 234     221.715 213.307 192.272  1.00 67.94           N  
ATOM   8230  CA  ILE D 234     221.557 212.819 190.904  1.00 67.94           C  
ATOM   8231  C   ILE D 234     220.846 211.475 190.889  1.00 67.94           C  
ATOM   8232  O   ILE D 234     220.305 211.060 189.862  1.00 67.94           O  
ATOM   8233  CB  ILE D 234     222.929 212.746 190.216  1.00 67.94           C  
ATOM   8234  CG1 ILE D 234     222.781 212.824 188.705  1.00 67.94           C  
ATOM   8235  CG2 ILE D 234     223.613 211.462 190.555  1.00 67.94           C  
ATOM   8236  CD1 ILE D 234     224.062 213.159 188.001  1.00 67.94           C  
ATOM   8237  N   THR D 235     220.840 210.772 192.018  1.00 68.77           N  
ATOM   8238  CA  THR D 235     220.046 209.563 192.159  1.00 68.77           C  
ATOM   8239  C   THR D 235     218.608 209.878 192.543  1.00 68.77           C  
ATOM   8240  O   THR D 235     217.753 208.991 192.490  1.00 68.77           O  
ATOM   8241  CB  THR D 235     220.693 208.656 193.201  1.00 68.77           C  
ATOM   8242  OG1 THR D 235     222.093 208.567 192.930  1.00 68.77           O  
ATOM   8243  CG2 THR D 235     220.123 207.270 193.130  1.00 68.77           C  
ATOM   8244  N   GLN D 236     218.327 211.120 192.925  1.00 70.74           N  
ATOM   8245  CA  GLN D 236     216.978 211.607 193.183  1.00 70.74           C  
ATOM   8246  C   GLN D 236     216.285 210.892 194.322  1.00 70.74           C  
ATOM   8247  O   GLN D 236     215.056 210.812 194.332  1.00 70.74           O  
ATOM   8248  CB  GLN D 236     216.093 211.501 191.947  1.00 70.74           C  
ATOM   8249  CG  GLN D 236     216.402 212.467 190.862  1.00 70.74           C  
ATOM   8250  CD  GLN D 236     215.589 212.165 189.645  1.00 70.74           C  
ATOM   8251  OE1 GLN D 236     214.937 211.127 189.568  1.00 70.74           O  
ATOM   8252  NE2 GLN D 236     215.613 213.062 188.684  1.00 70.74           N  
ATOM   8253  N   ASP D 237     217.017 210.355 195.288  1.00 70.71           N  
ATOM   8254  CA  ASP D 237     216.363 209.752 196.439  1.00 70.71           C  
ATOM   8255  C   ASP D 237     217.144 210.086 197.693  1.00 70.71           C  
ATOM   8256  O   ASP D 237     218.267 209.612 197.873  1.00 70.71           O  
ATOM   8257  CB  ASP D 237     216.229 208.242 196.279  1.00 70.71           C  
ATOM   8258  CG  ASP D 237     215.313 207.640 197.310  1.00 70.71           C  
ATOM   8259  OD1 ASP D 237     214.082 207.791 197.162  1.00 70.71           O  
ATOM   8260  OD2 ASP D 237     215.817 207.030 198.270  1.00 70.71           O  
ATOM   8261  N   GLY D 238     216.545 210.884 198.562  1.00 75.76           N  
ATOM   8262  CA  GLY D 238     217.169 211.235 199.810  1.00 75.76           C  
ATOM   8263  C   GLY D 238     217.897 212.551 199.825  1.00 75.76           C  
ATOM   8264  O   GLY D 238     218.700 212.774 200.732  1.00 75.76           O  
ATOM   8265  N   TRP D 239     217.669 213.423 198.849  1.00 75.52           N  
ATOM   8266  CA  TRP D 239     218.206 214.770 198.938  1.00 75.52           C  
ATOM   8267  C   TRP D 239     217.252 215.728 199.625  1.00 75.52           C  
ATOM   8268  O   TRP D 239     217.671 216.810 200.041  1.00 75.52           O  
ATOM   8269  CB  TRP D 239     218.553 215.312 197.554  1.00 75.52           C  
ATOM   8270  CG  TRP D 239     217.392 215.470 196.659  1.00 75.52           C  
ATOM   8271  CD1 TRP D 239     216.839 214.521 195.862  1.00 75.52           C  
ATOM   8272  CD2 TRP D 239     216.632 216.661 196.453  1.00 75.52           C  
ATOM   8273  NE1 TRP D 239     215.777 215.045 195.174  1.00 75.52           N  
ATOM   8274  CE2 TRP D 239     215.629 216.360 195.524  1.00 75.52           C  
ATOM   8275  CE3 TRP D 239     216.700 217.953 196.972  1.00 75.52           C  
ATOM   8276  CZ2 TRP D 239     214.706 217.303 195.098  1.00 75.52           C  
ATOM   8277  CZ3 TRP D 239     215.782 218.882 196.552  1.00 75.52           C  
ATOM   8278  CH2 TRP D 239     214.801 218.557 195.624  1.00 75.52           C  
ATOM   8279  N   LEU D 240     215.982 215.357 199.760  1.00 79.60           N  
ATOM   8280  CA  LEU D 240     215.073 216.161 200.562  1.00 79.60           C  
ATOM   8281  C   LEU D 240     215.533 216.197 202.012  1.00 79.60           C  
ATOM   8282  O   LEU D 240     215.487 217.245 202.674  1.00 79.60           O  
ATOM   8283  CB  LEU D 240     213.662 215.596 200.450  1.00 79.60           C  
ATOM   8284  CG  LEU D 240     212.558 216.597 200.754  1.00 79.60           C  
ATOM   8285  CD1 LEU D 240     212.619 217.705 199.735  1.00 79.60           C  
ATOM   8286  CD2 LEU D 240     211.192 215.931 200.746  1.00 79.60           C  
ATOM   8287  N   ASP D 241     216.002 215.057 202.512  1.00 84.43           N  
ATOM   8288  CA  ASP D 241     216.567 215.004 203.851  1.00 84.43           C  
ATOM   8289  C   ASP D 241     217.797 215.887 203.950  1.00 84.43           C  
ATOM   8290  O   ASP D 241     218.030 216.529 204.978  1.00 84.43           O  
ATOM   8291  CB  ASP D 241     216.919 213.562 204.200  1.00 84.43           C  
ATOM   8292  CG  ASP D 241     215.699 212.695 204.369  1.00 84.43           C  
ATOM   8293  OD1 ASP D 241     214.643 213.226 204.763  1.00 84.43           O  
ATOM   8294  OD2 ASP D 241     215.793 211.482 204.100  1.00 84.43           O  
ATOM   8295  N   ILE D 242     218.599 215.926 202.889  1.00 82.28           N  
ATOM   8296  CA  ILE D 242     219.776 216.783 202.870  1.00 82.28           C  
ATOM   8297  C   ILE D 242     219.370 218.242 202.964  1.00 82.28           C  
ATOM   8298  O   ILE D 242     219.966 219.019 203.715  1.00 82.28           O  
ATOM   8299  CB  ILE D 242     220.601 216.511 201.604  1.00 82.28           C  
ATOM   8300  CG1 ILE D 242     221.130 215.086 201.620  1.00 82.28           C  
ATOM   8301  CG2 ILE D 242     221.736 217.500 201.476  1.00 82.28           C  
ATOM   8302  CD1 ILE D 242     221.966 214.768 200.426  1.00 82.28           C  
ATOM   8303  N   TYR D 243     218.350 218.641 202.206  1.00 87.21           N  
ATOM   8304  CA  TYR D 243     217.949 220.043 202.200  1.00 87.21           C  
ATOM   8305  C   TYR D 243     217.307 220.451 203.515  1.00 87.21           C  
ATOM   8306  O   TYR D 243     217.350 221.629 203.891  1.00 87.21           O  
ATOM   8307  CB  TYR D 243     217.000 220.316 201.036  1.00 87.21           C  
ATOM   8308  CG  TYR D 243     216.631 221.770 200.892  1.00 87.21           C  
ATOM   8309  CD1 TYR D 243     217.405 222.628 200.136  1.00 87.21           C  
ATOM   8310  CD2 TYR D 243     215.511 222.284 201.524  1.00 87.21           C  
ATOM   8311  CE1 TYR D 243     217.073 223.946 200.012  1.00 87.21           C  
ATOM   8312  CE2 TYR D 243     215.175 223.602 201.407  1.00 87.21           C  
ATOM   8313  CZ  TYR D 243     215.955 224.429 200.647  1.00 87.21           C  
ATOM   8314  OH  TYR D 243     215.608 225.750 200.532  1.00 87.21           O  
ATOM   8315  N   THR D 244     216.704 219.503 204.229  1.00 93.61           N  
ATOM   8316  CA  THR D 244     216.214 219.835 205.561  1.00 93.61           C  
ATOM   8317  C   THR D 244     217.344 220.298 206.474  1.00 93.61           C  
ATOM   8318  O   THR D 244     217.102 221.041 207.429  1.00 93.61           O  
ATOM   8319  CB  THR D 244     215.486 218.646 206.171  1.00 93.61           C  
ATOM   8320  OG1 THR D 244     216.291 217.472 206.032  1.00 93.61           O  
ATOM   8321  CG2 THR D 244     214.171 218.431 205.466  1.00 93.61           C  
ATOM   8322  N   ASP D 245     218.582 219.889 206.194  1.00 96.32           N  
ATOM   8323  CA  ASP D 245     219.712 220.404 206.959  1.00 96.32           C  
ATOM   8324  C   ASP D 245     219.931 221.890 206.701  1.00 96.32           C  
ATOM   8325  O   ASP D 245     220.253 222.639 207.627  1.00 96.32           O  
ATOM   8326  CB  ASP D 245     220.972 219.607 206.639  1.00 96.32           C  
ATOM   8327  CG  ASP D 245     220.883 218.174 207.115  1.00 96.32           C  
ATOM   8328  OD1 ASP D 245     219.908 217.853 207.821  1.00 96.32           O  
ATOM   8329  OD2 ASP D 245     221.783 217.372 206.792  1.00 96.32           O  
ATOM   8330  N   PHE D 246     219.783 222.336 205.450  1.00 95.84           N  
ATOM   8331  CA  PHE D 246     219.737 223.772 205.188  1.00 95.84           C  
ATOM   8332  C   PHE D 246     218.613 224.418 205.975  1.00 95.84           C  
ATOM   8333  O   PHE D 246     218.785 225.494 206.558  1.00 95.84           O  
ATOM   8334  CB  PHE D 246     219.509 224.051 203.705  1.00 95.84           C  
ATOM   8335  CG  PHE D 246     220.684 223.783 202.837  1.00 95.84           C  
ATOM   8336  CD1 PHE D 246     221.162 222.502 202.671  1.00 95.84           C  
ATOM   8337  CD2 PHE D 246     221.290 224.813 202.154  1.00 95.84           C  
ATOM   8338  CE1 PHE D 246     222.233 222.261 201.860  1.00 95.84           C  
ATOM   8339  CE2 PHE D 246     222.360 224.577 201.344  1.00 95.84           C  
ATOM   8340  CZ  PHE D 246     222.833 223.301 201.197  1.00 95.84           C  
ATOM   8341  N   GLN D 247     217.444 223.772 205.987  1.00110.94           N  
ATOM   8342  CA  GLN D 247     216.278 224.352 206.643  1.00110.94           C  
ATOM   8343  C   GLN D 247     216.405 224.298 208.160  1.00110.94           C  
ATOM   8344  O   GLN D 247     215.910 225.186 208.861  1.00110.94           O  
ATOM   8345  CB  GLN D 247     215.013 223.633 206.180  1.00110.94           C  
ATOM   8346  CG  GLN D 247     213.731 224.427 206.333  1.00110.94           C  
ATOM   8347  CD  GLN D 247     213.161 224.357 207.733  1.00110.94           C  
ATOM   8348  OE1 GLN D 247     213.509 223.473 208.512  1.00110.94           O  
ATOM   8349  NE2 GLN D 247     212.268 225.284 208.056  1.00110.94           N  
ATOM   8350  N   MET D 248     217.057 223.269 208.687  1.00126.38           N  
ATOM   8351  CA  MET D 248     217.158 223.102 210.132  1.00126.38           C  
ATOM   8352  C   MET D 248     218.211 224.056 210.671  1.00126.38           C  
ATOM   8353  O   MET D 248     219.401 223.732 210.694  1.00126.38           O  
ATOM   8354  CB  MET D 248     217.488 221.658 210.495  1.00126.38           C  
ATOM   8355  CG  MET D 248     216.273 220.835 210.907  1.00126.38           C  
ATOM   8356  SD  MET D 248     215.496 221.416 212.429  1.00126.38           S  
ATOM   8357  CE  MET D 248     216.537 220.643 213.665  1.00126.38           C  
ATOM   8358  N   ASP D 249     217.770 225.226 211.113  1.00140.04           N  
ATOM   8359  CA  ASP D 249     218.644 226.207 211.735  1.00140.04           C  
ATOM   8360  C   ASP D 249     217.827 226.952 212.774  1.00140.04           C  
ATOM   8361  O   ASP D 249     216.603 226.823 212.836  1.00140.04           O  
ATOM   8362  CB  ASP D 249     219.230 227.171 210.704  1.00140.04           C  
ATOM   8363  CG  ASP D 249     220.533 226.683 210.129  1.00140.04           C  
ATOM   8364  OD1 ASP D 249     221.146 225.772 210.719  1.00140.04           O  
ATOM   8365  OD2 ASP D 249     220.949 227.219 209.088  1.00140.04           O  
ATOM   8366  N   GLU D 250     218.519 227.727 213.605  1.00156.64           N  
ATOM   8367  CA  GLU D 250     217.801 228.548 214.570  1.00156.64           C  
ATOM   8368  C   GLU D 250     216.948 229.596 213.868  1.00156.64           C  
ATOM   8369  O   GLU D 250     215.751 229.719 214.150  1.00156.64           O  
ATOM   8370  CB  GLU D 250     218.782 229.205 215.537  1.00156.64           C  
ATOM   8371  CG  GLU D 250     219.183 228.303 216.693  1.00156.64           C  
ATOM   8372  CD  GLU D 250     217.985 227.691 217.395  1.00156.64           C  
ATOM   8373  OE1 GLU D 250     216.992 228.413 217.624  1.00156.64           O  
ATOM   8374  OE2 GLU D 250     218.031 226.483 217.710  1.00156.64           O  
ATOM   8375  N   ARG D 251     217.539 230.342 212.940  1.00142.57           N  
ATOM   8376  CA  ARG D 251     216.803 231.342 212.172  1.00142.57           C  
ATOM   8377  C   ARG D 251     217.617 231.667 210.934  1.00142.57           C  
ATOM   8378  O   ARG D 251     218.737 232.169 211.052  1.00142.57           O  
ATOM   8379  CB  ARG D 251     216.552 232.599 213.006  1.00142.57           C  
ATOM   8380  CG  ARG D 251     215.973 233.775 212.226  1.00142.57           C  
ATOM   8381  CD  ARG D 251     217.041 234.829 211.943  1.00142.57           C  
ATOM   8382  NE  ARG D 251     216.491 236.039 211.337  1.00142.57           N  
ATOM   8383  CZ  ARG D 251     216.331 236.219 210.030  1.00142.57           C  
ATOM   8384  NH1 ARG D 251     216.676 235.263 209.176  1.00142.57           N  
ATOM   8385  NH2 ARG D 251     215.823 237.359 209.577  1.00142.57           N  
ATOM   8386  N   GLU D 252     217.068 231.392 209.756  1.00125.88           N  
ATOM   8387  CA  GLU D 252     217.814 231.644 208.532  1.00125.88           C  
ATOM   8388  C   GLU D 252     216.849 231.736 207.364  1.00125.88           C  
ATOM   8389  O   GLU D 252     215.872 230.986 207.319  1.00125.88           O  
ATOM   8390  CB  GLU D 252     218.839 230.538 208.290  1.00125.88           C  
ATOM   8391  CG  GLU D 252     219.433 230.560 206.910  1.00125.88           C  
ATOM   8392  CD  GLU D 252     220.019 231.905 206.566  1.00125.88           C  
ATOM   8393  OE1 GLU D 252     220.620 232.540 207.456  1.00125.88           O  
ATOM   8394  OE2 GLU D 252     219.852 232.337 205.411  1.00125.88           O  
ATOM   8395  N   TYR D 253     217.116 232.659 206.433  1.00120.59           N  
ATOM   8396  CA  TYR D 253     216.352 232.763 205.195  1.00120.59           C  
ATOM   8397  C   TYR D 253     217.197 232.980 203.951  1.00120.59           C  
ATOM   8398  O   TYR D 253     216.732 232.653 202.856  1.00120.59           O  
ATOM   8399  CB  TYR D 253     215.342 233.914 205.281  1.00120.59           C  
ATOM   8400  CG  TYR D 253     214.092 233.600 206.057  1.00120.59           C  
ATOM   8401  CD1 TYR D 253     213.595 232.310 206.123  1.00120.59           C  
ATOM   8402  CD2 TYR D 253     213.410 234.598 206.732  1.00120.59           C  
ATOM   8403  CE1 TYR D 253     212.455 232.022 206.842  1.00120.59           C  
ATOM   8404  CE2 TYR D 253     212.269 234.320 207.449  1.00120.59           C  
ATOM   8405  CZ  TYR D 253     211.797 233.033 207.500  1.00120.59           C  
ATOM   8406  OH  TYR D 253     210.658 232.765 208.216  1.00120.59           O  
ATOM   8407  N   ALA D 254     218.403 233.527 204.068  1.00115.10           N  
ATOM   8408  CA  ALA D 254     219.115 233.973 202.877  1.00115.10           C  
ATOM   8409  C   ALA D 254     219.717 232.814 202.104  1.00115.10           C  
ATOM   8410  O   ALA D 254     219.847 232.890 200.880  1.00115.10           O  
ATOM   8411  CB  ALA D 254     220.209 234.971 203.254  1.00115.10           C  
ATOM   8412  N   MET D 255     220.117 231.747 202.792  1.00110.77           N  
ATOM   8413  CA  MET D 255     220.806 230.649 202.129  1.00110.77           C  
ATOM   8414  C   MET D 255     219.944 229.419 201.919  1.00110.77           C  
ATOM   8415  O   MET D 255     220.348 228.530 201.166  1.00110.77           O  
ATOM   8416  CB  MET D 255     222.068 230.262 202.897  1.00110.77           C  
ATOM   8417  CG  MET D 255     223.221 231.125 202.500  1.00110.77           C  
ATOM   8418  SD  MET D 255     224.802 230.298 202.556  1.00110.77           S  
ATOM   8419  CE  MET D 255     225.847 231.740 202.523  1.00110.77           C  
ATOM   8420  N   GLU D 256     218.771 229.344 202.541  1.00102.96           N  
ATOM   8421  CA  GLU D 256     217.840 228.290 202.166  1.00102.96           C  
ATOM   8422  C   GLU D 256     217.415 228.449 200.715  1.00102.96           C  
ATOM   8423  O   GLU D 256     217.406 227.479 199.951  1.00102.96           O  
ATOM   8424  CB  GLU D 256     216.636 228.304 203.098  1.00102.96           C  
ATOM   8425  CG  GLU D 256     217.033 228.344 204.548  1.00102.96           C  
ATOM   8426  CD  GLU D 256     215.853 228.344 205.480  1.00102.96           C  
ATOM   8427  OE1 GLU D 256     214.705 228.353 204.995  1.00102.96           O  
ATOM   8428  OE2 GLU D 256     216.075 228.327 206.705  1.00102.96           O  
ATOM   8429  N   VAL D 257     217.107 229.677 200.305  1.00 95.65           N  
ATOM   8430  CA  VAL D 257     216.729 229.927 198.922  1.00 95.65           C  
ATOM   8431  C   VAL D 257     217.902 229.674 197.980  1.00 95.65           C  
ATOM   8432  O   VAL D 257     217.726 229.112 196.894  1.00 95.65           O  
ATOM   8433  CB  VAL D 257     216.164 231.351 198.778  1.00 95.65           C  
ATOM   8434  CG1 VAL D 257     217.160 232.371 199.256  1.00 95.65           C  
ATOM   8435  CG2 VAL D 257     215.807 231.630 197.338  1.00 95.65           C  
ATOM   8436  N   GLY D 258     219.113 230.075 198.370  1.00 91.90           N  
ATOM   8437  CA  GLY D 258     220.268 229.825 197.520  1.00 91.90           C  
ATOM   8438  C   GLY D 258     220.544 228.346 197.330  1.00 91.90           C  
ATOM   8439  O   GLY D 258     220.769 227.877 196.210  1.00 91.90           O  
ATOM   8440  N   GLY D 259     220.518 227.586 198.424  1.00 86.80           N  
ATOM   8441  CA  GLY D 259     220.692 226.150 198.315  1.00 86.80           C  
ATOM   8442  C   GLY D 259     219.590 225.493 197.509  1.00 86.80           C  
ATOM   8443  O   GLY D 259     219.838 224.548 196.756  1.00 86.80           O  
ATOM   8444  N   ALA D 260     218.357 225.979 197.657  1.00 83.18           N  
ATOM   8445  CA  ALA D 260     217.264 225.441 196.860  1.00 83.18           C  
ATOM   8446  C   ALA D 260     217.500 225.688 195.383  1.00 83.18           C  
ATOM   8447  O   ALA D 260     217.275 224.799 194.559  1.00 83.18           O  
ATOM   8448  CB  ALA D 260     215.938 226.052 197.302  1.00 83.18           C  
ATOM   8449  N   ILE D 261     217.953 226.889 195.030  1.00 78.87           N  
ATOM   8450  CA  ILE D 261     218.252 227.186 193.634  1.00 78.87           C  
ATOM   8451  C   ILE D 261     219.319 226.237 193.120  1.00 78.87           C  
ATOM   8452  O   ILE D 261     219.215 225.688 192.016  1.00 78.87           O  
ATOM   8453  CB  ILE D 261     218.692 228.652 193.486  1.00 78.87           C  
ATOM   8454  CG1 ILE D 261     217.508 229.590 193.686  1.00 78.87           C  
ATOM   8455  CG2 ILE D 261     219.310 228.883 192.133  1.00 78.87           C  
ATOM   8456  CD1 ILE D 261     216.392 229.356 192.720  1.00 78.87           C  
ATOM   8457  N   TYR D 262     220.359 226.028 193.922  1.00 79.36           N  
ATOM   8458  CA  TYR D 262     221.457 225.149 193.537  1.00 79.36           C  
ATOM   8459  C   TYR D 262     220.955 223.736 193.259  1.00 79.36           C  
ATOM   8460  O   TYR D 262     221.232 223.155 192.201  1.00 79.36           O  
ATOM   8461  CB  TYR D 262     222.498 225.172 194.656  1.00 79.36           C  
ATOM   8462  CG  TYR D 262     223.702 224.301 194.485  1.00 79.36           C  
ATOM   8463  CD1 TYR D 262     224.820 224.766 193.832  1.00 79.36           C  
ATOM   8464  CD2 TYR D 262     223.742 223.029 195.026  1.00 79.36           C  
ATOM   8465  CE1 TYR D 262     225.932 223.981 193.694  1.00 79.36           C  
ATOM   8466  CE2 TYR D 262     224.846 222.240 194.892  1.00 79.36           C  
ATOM   8467  CZ  TYR D 262     225.937 222.720 194.224  1.00 79.36           C  
ATOM   8468  OH  TYR D 262     227.051 221.937 194.085  1.00 79.36           O  
ATOM   8469  N   PHE D 263     220.189 223.180 194.195  1.00 77.93           N  
ATOM   8470  CA  PHE D 263     219.685 221.823 194.031  1.00 77.93           C  
ATOM   8471  C   PHE D 263     218.741 221.721 192.845  1.00 77.93           C  
ATOM   8472  O   PHE D 263     218.775 220.738 192.100  1.00 77.93           O  
ATOM   8473  CB  PHE D 263     218.983 221.366 195.305  1.00 77.93           C  
ATOM   8474  CG  PHE D 263     219.917 220.910 196.373  1.00 77.93           C  
ATOM   8475  CD1 PHE D 263     221.210 220.553 196.065  1.00 77.93           C  
ATOM   8476  CD2 PHE D 263     219.507 220.847 197.685  1.00 77.93           C  
ATOM   8477  CE1 PHE D 263     222.071 220.138 197.040  1.00 77.93           C  
ATOM   8478  CE2 PHE D 263     220.366 220.431 198.664  1.00 77.93           C  
ATOM   8479  CZ  PHE D 263     221.651 220.076 198.339  1.00 77.93           C  
ATOM   8480  N   ALA D 264     217.882 222.724 192.656  1.00 77.01           N  
ATOM   8481  CA  ALA D 264     216.948 222.695 191.541  1.00 77.01           C  
ATOM   8482  C   ALA D 264     217.676 222.692 190.210  1.00 77.01           C  
ATOM   8483  O   ALA D 264     217.327 221.924 189.311  1.00 77.01           O  
ATOM   8484  CB  ALA D 264     216.000 223.886 191.620  1.00 77.01           C  
ATOM   8485  N   VAL D 265     218.695 223.534 190.060  1.00 73.14           N  
ATOM   8486  CA  VAL D 265     219.406 223.575 188.789  1.00 73.14           C  
ATOM   8487  C   VAL D 265     220.171 222.281 188.556  1.00 73.14           C  
ATOM   8488  O   VAL D 265     220.171 221.738 187.442  1.00 73.14           O  
ATOM   8489  CB  VAL D 265     220.326 224.799 188.730  1.00 73.14           C  
ATOM   8490  CG1 VAL D 265     221.073 224.818 187.422  1.00 73.14           C  
ATOM   8491  CG2 VAL D 265     219.512 226.052 188.883  1.00 73.14           C  
ATOM   8492  N   PHE D 266     220.825 221.750 189.595  1.00 74.76           N  
ATOM   8493  CA  PHE D 266     221.535 220.486 189.415  1.00 74.76           C  
ATOM   8494  C   PHE D 266     220.580 219.365 189.044  1.00 74.76           C  
ATOM   8495  O   PHE D 266     220.884 218.547 188.172  1.00 74.76           O  
ATOM   8496  CB  PHE D 266     222.313 220.104 190.673  1.00 74.76           C  
ATOM   8497  CG  PHE D 266     223.109 218.839 190.520  1.00 74.76           C  
ATOM   8498  CD1 PHE D 266     224.368 218.863 189.951  1.00 74.76           C  
ATOM   8499  CD2 PHE D 266     222.591 217.629 190.916  1.00 74.76           C  
ATOM   8500  CE1 PHE D 266     225.097 217.712 189.792  1.00 74.76           C  
ATOM   8501  CE2 PHE D 266     223.315 216.477 190.758  1.00 74.76           C  
ATOM   8502  CZ  PHE D 266     224.570 216.521 190.196  1.00 74.76           C  
ATOM   8503  N   ILE D 267     219.426 219.302 189.696  1.00 72.73           N  
ATOM   8504  CA  ILE D 267     218.502 218.207 189.452  1.00 72.73           C  
ATOM   8505  C   ILE D 267     217.852 218.334 188.082  1.00 72.73           C  
ATOM   8506  O   ILE D 267     217.602 217.331 187.410  1.00 72.73           O  
ATOM   8507  CB  ILE D 267     217.477 218.142 190.591  1.00 72.73           C  
ATOM   8508  CG1 ILE D 267     218.156 217.565 191.819  1.00 72.73           C  
ATOM   8509  CG2 ILE D 267     216.295 217.318 190.209  1.00 72.73           C  
ATOM   8510  CD1 ILE D 267     217.366 217.694 193.046  1.00 72.73           C  
ATOM   8511  N   THR D 268     217.571 219.558 187.636  1.00 75.18           N  
ATOM   8512  CA  THR D 268     217.010 219.718 186.301  1.00 75.18           C  
ATOM   8513  C   THR D 268     218.018 219.339 185.231  1.00 75.18           C  
ATOM   8514  O   THR D 268     217.712 218.548 184.336  1.00 75.18           O  
ATOM   8515  CB  THR D 268     216.542 221.150 186.082  1.00 75.18           C  
ATOM   8516  OG1 THR D 268     217.586 222.045 186.458  1.00 75.18           O  
ATOM   8517  CG2 THR D 268     215.330 221.438 186.915  1.00 75.18           C  
ATOM   8518  N   LEU D 269     219.228 219.878 185.305  1.00 78.30           N  
ATOM   8519  CA  LEU D 269     220.148 219.668 184.198  1.00 78.30           C  
ATOM   8520  C   LEU D 269     220.845 218.319 184.240  1.00 78.30           C  
ATOM   8521  O   LEU D 269     221.292 217.832 183.199  1.00 78.30           O  
ATOM   8522  CB  LEU D 269     221.201 220.774 184.167  1.00 78.30           C  
ATOM   8523  CG  LEU D 269     220.666 222.196 184.032  1.00 78.30           C  
ATOM   8524  CD1 LEU D 269     221.783 223.192 184.218  1.00 78.30           C  
ATOM   8525  CD2 LEU D 269     219.985 222.390 182.697  1.00 78.30           C  
ATOM   8526  N   GLY D 270     220.951 217.701 185.408  1.00 74.42           N  
ATOM   8527  CA  GLY D 270     221.778 216.521 185.533  1.00 74.42           C  
ATOM   8528  C   GLY D 270     221.003 215.257 185.808  1.00 74.42           C  
ATOM   8529  O   GLY D 270     221.437 214.164 185.444  1.00 74.42           O  
ATOM   8530  N   ALA D 271     219.860 215.386 186.464  1.00 73.89           N  
ATOM   8531  CA  ALA D 271     219.061 214.208 186.758  1.00 73.89           C  
ATOM   8532  C   ALA D 271     218.042 213.944 185.659  1.00 73.89           C  
ATOM   8533  O   ALA D 271     217.828 212.795 185.267  1.00 73.89           O  
ATOM   8534  CB  ALA D 271     218.377 214.370 188.110  1.00 73.89           C  
ATOM   8535  N   PHE D 272     217.404 214.993 185.146  1.00 76.57           N  
ATOM   8536  CA  PHE D 272     216.401 214.824 184.106  1.00 76.57           C  
ATOM   8537  C   PHE D 272     216.996 214.725 182.713  1.00 76.57           C  
ATOM   8538  O   PHE D 272     216.270 214.389 181.776  1.00 76.57           O  
ATOM   8539  CB  PHE D 272     215.406 215.980 184.127  1.00 76.57           C  
ATOM   8540  CG  PHE D 272     214.642 216.104 185.411  1.00 76.57           C  
ATOM   8541  CD1 PHE D 272     214.526 215.034 186.276  1.00 76.57           C  
ATOM   8542  CD2 PHE D 272     214.039 217.300 185.751  1.00 76.57           C  
ATOM   8543  CE1 PHE D 272     213.825 215.162 187.451  1.00 76.57           C  
ATOM   8544  CE2 PHE D 272     213.342 217.425 186.925  1.00 76.57           C  
ATOM   8545  CZ  PHE D 272     213.241 216.356 187.778  1.00 76.57           C  
ATOM   8546  N   ILE D 273     218.266 215.111 182.558  1.00 78.84           N  
ATOM   8547  CA  ILE D 273     218.892 215.103 181.200  1.00 78.84           C  
ATOM   8548  C   ILE D 273     220.119 214.185 181.163  1.00 78.84           C  
ATOM   8549  O   ILE D 273     220.189 213.337 180.251  1.00 78.84           O  
ATOM   8550  CB  ILE D 273     219.242 216.537 180.754  1.00 78.84           C  
ATOM   8551  CG1 ILE D 273     218.023 217.462 180.809  1.00 78.84           C  
ATOM   8552  CG2 ILE D 273     219.885 216.532 179.375  1.00 78.84           C  
ATOM   8553  CD1 ILE D 273     218.311 218.882 180.381  1.00 78.84           C  
ATOM   8554  N   GLY D 274     221.046 214.354 182.110  1.00 80.30           N  
ATOM   8555  CA  GLY D 274     222.259 213.557 182.111  1.00 80.30           C  
ATOM   8556  C   GLY D 274     222.022 212.107 182.476  1.00 80.30           C  
ATOM   8557  O   GLY D 274     222.566 211.203 181.842  1.00 80.30           O  
ATOM   8558  N   LEU D 275     221.224 211.859 183.501  1.00 79.39           N  
ATOM   8559  CA  LEU D 275     220.992 210.485 183.909  1.00 79.39           C  
ATOM   8560  C   LEU D 275     219.946 209.790 183.055  1.00 79.39           C  
ATOM   8561  O   LEU D 275     219.739 208.585 183.217  1.00 79.39           O  
ATOM   8562  CB  LEU D 275     220.588 210.440 185.376  1.00 79.39           C  
ATOM   8563  CG  LEU D 275     220.851 209.108 186.060  1.00 79.39           C  
ATOM   8564  CD1 LEU D 275     222.311 209.006 186.405  1.00 79.39           C  
ATOM   8565  CD2 LEU D 275     220.001 208.995 187.301  1.00 79.39           C  
ATOM   8566  N   ASN D 276     219.277 210.517 182.162  1.00 83.47           N  
ATOM   8567  CA  ASN D 276     218.436 209.923 181.133  1.00 83.47           C  
ATOM   8568  C   ASN D 276     219.165 209.829 179.804  1.00 83.47           C  
ATOM   8569  O   ASN D 276     218.551 209.962 178.745  1.00 83.47           O  
ATOM   8570  CB  ASN D 276     217.135 210.705 180.970  1.00 83.47           C  
ATOM   8571  CG  ASN D 276     216.012 210.145 181.814  1.00 83.47           C  
ATOM   8572  OD1 ASN D 276     215.981 208.957 182.113  1.00 83.47           O  
ATOM   8573  ND2 ASN D 276     215.071 210.998 182.185  1.00 83.47           N  
ATOM   8574  N   LEU D 277     220.477 209.616 179.848  1.00 88.37           N  
ATOM   8575  CA  LEU D 277     221.291 209.461 178.657  1.00 88.37           C  
ATOM   8576  C   LEU D 277     221.829 208.047 178.494  1.00 88.37           C  
ATOM   8577  O   LEU D 277     222.179 207.654 177.376  1.00 88.37           O  
ATOM   8578  CB  LEU D 277     222.452 210.463 178.703  1.00 88.37           C  
ATOM   8579  CG  LEU D 277     222.967 211.126 177.427  1.00 88.37           C  
ATOM   8580  CD1 LEU D 277     221.852 211.853 176.729  1.00 88.37           C  
ATOM   8581  CD2 LEU D 277     224.056 212.100 177.774  1.00 88.37           C  
ATOM   8582  N   PHE D 278     221.872 207.271 179.578  1.00 90.17           N  
ATOM   8583  CA  PHE D 278     222.215 205.856 179.490  1.00 90.17           C  
ATOM   8584  C   PHE D 278     221.198 205.100 178.646  1.00 90.17           C  
ATOM   8585  O   PHE D 278     221.563 204.236 177.836  1.00 90.17           O  
ATOM   8586  CB  PHE D 278     222.283 205.258 180.893  1.00 90.17           C  
ATOM   8587  CG  PHE D 278     223.436 205.754 181.708  1.00 90.17           C  
ATOM   8588  CD1 PHE D 278     223.524 207.079 182.074  1.00 90.17           C  
ATOM   8589  CD2 PHE D 278     224.430 204.895 182.109  1.00 90.17           C  
ATOM   8590  CE1 PHE D 278     224.582 207.534 182.814  1.00 90.17           C  
ATOM   8591  CE2 PHE D 278     225.491 205.348 182.850  1.00 90.17           C  
ATOM   8592  CZ  PHE D 278     225.567 206.668 183.202  1.00 90.17           C  
ATOM   8593  N   VAL D 279     219.914 205.399 178.849  1.00 93.88           N  
ATOM   8594  CA  VAL D 279     218.852 204.883 177.994  1.00 93.88           C  
ATOM   8595  C   VAL D 279     219.217 205.057 176.531  1.00 93.88           C  
ATOM   8596  O   VAL D 279     219.206 204.107 175.737  1.00 93.88           O  
ATOM   8597  CB  VAL D 279     217.543 205.619 178.304  1.00 93.88           C  
ATOM   8598  CG1 VAL D 279     216.420 205.077 177.460  1.00 93.88           C  
ATOM   8599  CG2 VAL D 279     217.237 205.548 179.771  1.00 93.88           C  
ATOM   8600  N   VAL D 280     219.535 206.289 176.162  1.00 97.89           N  
ATOM   8601  CA  VAL D 280     219.715 206.642 174.769  1.00 97.89           C  
ATOM   8602  C   VAL D 280     220.957 205.973 174.205  1.00 97.89           C  
ATOM   8603  O   VAL D 280     220.976 205.550 173.046  1.00 97.89           O  
ATOM   8604  CB  VAL D 280     219.769 208.170 174.654  1.00 97.89           C  
ATOM   8605  CG1 VAL D 280     219.855 208.575 173.236  1.00 97.89           C  
ATOM   8606  CG2 VAL D 280     218.546 208.766 175.314  1.00 97.89           C  
ATOM   8607  N   VAL D 281     222.013 205.864 175.008  1.00101.41           N  
ATOM   8608  CA  VAL D 281     223.222 205.178 174.553  1.00101.41           C  
ATOM   8609  C   VAL D 281     222.943 203.705 174.284  1.00101.41           C  
ATOM   8610  O   VAL D 281     223.373 203.146 173.263  1.00101.41           O  
ATOM   8611  CB  VAL D 281     224.349 205.359 175.579  1.00101.41           C  
ATOM   8612  CG1 VAL D 281     225.377 204.301 175.389  1.00101.41           C  
ATOM   8613  CG2 VAL D 281     224.977 206.706 175.388  1.00101.41           C  
ATOM   8614  N   VAL D 282     222.229 203.051 175.201  1.00104.04           N  
ATOM   8615  CA  VAL D 282     221.902 201.641 175.009  1.00104.04           C  
ATOM   8616  C   VAL D 282     221.081 201.455 173.744  1.00104.04           C  
ATOM   8617  O   VAL D 282     221.345 200.552 172.942  1.00104.04           O  
ATOM   8618  CB  VAL D 282     221.165 201.088 176.241  1.00104.04           C  
ATOM   8619  CG1 VAL D 282     220.601 199.727 175.940  1.00104.04           C  
ATOM   8620  CG2 VAL D 282     222.102 201.018 177.423  1.00104.04           C  
ATOM   8621  N   THR D 283     220.077 202.309 173.542  1.00109.83           N  
ATOM   8622  CA  THR D 283     219.236 202.195 172.355  1.00109.83           C  
ATOM   8623  C   THR D 283     220.042 202.416 171.080  1.00109.83           C  
ATOM   8624  O   THR D 283     219.914 201.658 170.113  1.00109.83           O  
ATOM   8625  CB  THR D 283     218.081 203.184 172.448  1.00109.83           C  
ATOM   8626  OG1 THR D 283     217.109 202.684 173.371  1.00109.83           O  
ATOM   8627  CG2 THR D 283     217.439 203.376 171.100  1.00109.83           C  
ATOM   8628  N   THR D 284     220.878 203.453 171.064  1.00117.21           N  
ATOM   8629  CA  THR D 284     221.815 203.677 169.969  1.00117.21           C  
ATOM   8630  C   THR D 284     222.554 202.404 169.586  1.00117.21           C  
ATOM   8631  O   THR D 284     222.450 201.912 168.453  1.00117.21           O  
ATOM   8632  CB  THR D 284     222.820 204.758 170.384  1.00117.21           C  
ATOM   8633  OG1 THR D 284     222.169 206.030 170.501  1.00117.21           O  
ATOM   8634  CG2 THR D 284     223.989 204.830 169.422  1.00117.21           C  
ATOM   8635  N   ASN D 285     223.315 201.855 170.531  1.00119.91           N  
ATOM   8636  CA  ASN D 285     224.170 200.722 170.195  1.00119.91           C  
ATOM   8637  C   ASN D 285     223.351 199.499 169.818  1.00119.91           C  
ATOM   8638  O   ASN D 285     223.733 198.741 168.916  1.00119.91           O  
ATOM   8639  CB  ASN D 285     225.103 200.407 171.354  1.00119.91           C  
ATOM   8640  CG  ASN D 285     226.175 201.450 171.524  1.00119.91           C  
ATOM   8641  OD1 ASN D 285     226.152 202.227 172.474  1.00119.91           O  
ATOM   8642  ND2 ASN D 285     227.127 201.476 170.600  1.00119.91           N  
ATOM   8643  N   LEU D 286     222.222 199.285 170.487  1.00127.59           N  
ATOM   8644  CA  LEU D 286     221.511 198.041 170.259  1.00127.59           C  
ATOM   8645  C   LEU D 286     220.811 198.084 168.906  1.00127.59           C  
ATOM   8646  O   LEU D 286     220.708 197.058 168.222  1.00127.59           O  
ATOM   8647  CB  LEU D 286     220.546 197.798 171.416  1.00127.59           C  
ATOM   8648  CG  LEU D 286     219.809 196.471 171.568  1.00127.59           C  
ATOM   8649  CD1 LEU D 286     219.508 196.313 173.036  1.00127.59           C  
ATOM   8650  CD2 LEU D 286     218.572 196.261 170.766  1.00127.59           C  
ATOM   8651  N   GLU D 287     220.387 199.277 168.475  1.00135.51           N  
ATOM   8652  CA  GLU D 287     219.940 199.441 167.097  1.00135.51           C  
ATOM   8653  C   GLU D 287     221.080 199.222 166.122  1.00135.51           C  
ATOM   8654  O   GLU D 287     220.876 198.647 165.049  1.00135.51           O  
ATOM   8655  CB  GLU D 287     219.325 200.822 166.895  1.00135.51           C  
ATOM   8656  CG  GLU D 287     219.152 201.198 165.437  1.00135.51           C  
ATOM   8657  CD  GLU D 287     217.867 200.668 164.853  1.00135.51           C  
ATOM   8658  OE1 GLU D 287     217.792 200.522 163.617  1.00135.51           O  
ATOM   8659  OE2 GLU D 287     216.931 200.395 165.630  1.00135.51           O  
ATOM   8660  N   GLN D 288     222.284 199.678 166.465  1.00139.07           N  
ATOM   8661  CA  GLN D 288     223.407 199.440 165.564  1.00139.07           C  
ATOM   8662  C   GLN D 288     223.618 197.947 165.344  1.00139.07           C  
ATOM   8663  O   GLN D 288     223.834 197.503 164.210  1.00139.07           O  
ATOM   8664  CB  GLN D 288     224.679 200.084 166.107  1.00139.07           C  
ATOM   8665  CG  GLN D 288     225.949 199.545 165.468  1.00139.07           C  
ATOM   8666  CD  GLN D 288     226.723 198.633 166.395  1.00139.07           C  
ATOM   8667  OE1 GLN D 288     226.858 198.911 167.585  1.00139.07           O  
ATOM   8668  NE2 GLN D 288     227.226 197.532 165.856  1.00139.07           N  
ATOM   8669  N   MET D 289     223.550 197.156 166.417  1.00142.97           N  
ATOM   8670  CA  MET D 289     223.671 195.706 166.263  1.00142.97           C  
ATOM   8671  C   MET D 289     222.523 195.138 165.440  1.00142.97           C  
ATOM   8672  O   MET D 289     222.745 194.357 164.507  1.00142.97           O  
ATOM   8673  CB  MET D 289     223.738 195.007 167.620  1.00142.97           C  
ATOM   8674  CG  MET D 289     225.139 194.860 168.164  1.00142.97           C  
ATOM   8675  SD  MET D 289     225.709 196.299 169.066  1.00142.97           S  
ATOM   8676  CE  MET D 289     224.634 196.231 170.485  1.00142.97           C  
ATOM   8677  N   MET D 290     221.287 195.523 165.767  1.00149.48           N  
ATOM   8678  CA  MET D 290     220.139 195.013 165.024  1.00149.48           C  
ATOM   8679  C   MET D 290     220.250 195.348 163.540  1.00149.48           C  
ATOM   8680  O   MET D 290     219.753 194.604 162.687  1.00149.48           O  
ATOM   8681  CB  MET D 290     218.849 195.580 165.614  1.00149.48           C  
ATOM   8682  CG  MET D 290     218.508 195.043 166.989  1.00149.48           C  
ATOM   8683  SD  MET D 290     217.669 193.450 166.949  1.00149.48           S  
ATOM   8684  CE  MET D 290     216.658 193.573 168.419  1.00149.48           C  
ATOM   8685  N   LYS D 291     220.909 196.461 163.213  1.00161.48           N  
ATOM   8686  CA  LYS D 291     221.057 196.868 161.818  1.00161.48           C  
ATOM   8687  C   LYS D 291     222.229 196.155 161.153  1.00161.48           C  
ATOM   8688  O   LYS D 291     222.073 195.533 160.096  1.00161.48           O  
ATOM   8689  CB  LYS D 291     221.236 198.386 161.736  1.00161.48           C  
ATOM   8690  CG  LYS D 291     221.554 198.906 160.344  1.00161.48           C  
ATOM   8691  CD  LYS D 291     220.434 198.599 159.368  1.00161.48           C  
ATOM   8692  CE  LYS D 291     219.120 199.210 159.826  1.00161.48           C  
ATOM   8693  NZ  LYS D 291     219.193 200.692 159.918  1.00161.48           N  
ATOM   8694  N   THR D 292     223.412 196.242 161.754  1.00165.00           N  
ATOM   8695  CA  THR D 292     224.599 195.583 161.223  1.00165.00           C  
ATOM   8696  C   THR D 292     224.874 194.267 161.944  1.00165.00           C  
ATOM   8697  O   THR D 292     224.402 193.210 161.526  1.00165.00           O  
ATOM   8698  CB  THR D 292     225.838 196.491 161.333  1.00165.00           C  
ATOM   8699  OG1 THR D 292     225.769 197.521 160.338  1.00165.00           O  
ATOM   8700  CG2 THR D 292     227.114 195.690 161.151  1.00165.00           C  
TER    8701      THR D 292                                                      
ATOM   8702  N   VAL E  22     229.844 192.060 270.190  1.00 70.93           N  
ATOM   8703  CA  VAL E  22     230.536 191.202 271.140  1.00 70.93           C  
ATOM   8704  C   VAL E  22     231.356 192.047 272.096  1.00 70.93           C  
ATOM   8705  O   VAL E  22     232.317 192.690 271.690  1.00 70.93           O  
ATOM   8706  CB  VAL E  22     231.435 190.185 270.424  1.00 70.93           C  
ATOM   8707  CG1 VAL E  22     232.083 189.253 271.431  1.00 70.93           C  
ATOM   8708  CG2 VAL E  22     230.637 189.400 269.399  1.00 70.93           C  
ATOM   8709  N   ILE E  23     230.976 192.047 273.369  1.00 67.11           N  
ATOM   8710  CA  ILE E  23     231.713 192.747 274.415  1.00 67.11           C  
ATOM   8711  C   ILE E  23     232.471 191.695 275.206  1.00 67.11           C  
ATOM   8712  O   ILE E  23     231.857 190.837 275.853  1.00 67.11           O  
ATOM   8713  CB  ILE E  23     230.780 193.558 275.323  1.00 67.11           C  
ATOM   8714  CG1 ILE E  23     229.872 194.466 274.498  1.00 67.11           C  
ATOM   8715  CG2 ILE E  23     231.590 194.400 276.283  1.00 67.11           C  
ATOM   8716  CD1 ILE E  23     230.559 195.683 273.952  1.00 67.11           C  
ATOM   8717  N   HIS E  24     233.801 191.751 275.154  1.00 67.70           N  
ATOM   8718  CA  HIS E  24     234.599 190.654 275.691  1.00 67.70           C  
ATOM   8719  C   HIS E  24     234.596 190.644 277.215  1.00 67.70           C  
ATOM   8720  O   HIS E  24     234.426 189.589 277.835  1.00 67.70           O  
ATOM   8721  CB  HIS E  24     236.022 190.724 275.144  1.00 67.70           C  
ATOM   8722  CG  HIS E  24     236.116 190.435 273.678  1.00 67.70           C  
ATOM   8723  ND1 HIS E  24     237.243 189.897 273.097  1.00 67.70           N  
ATOM   8724  CD2 HIS E  24     235.221 190.601 272.678  1.00 67.70           C  
ATOM   8725  CE1 HIS E  24     237.041 189.751 271.799  1.00 67.70           C  
ATOM   8726  NE2 HIS E  24     235.820 190.170 271.519  1.00 67.70           N  
ATOM   8727  N   ASN E  25     234.773 191.806 277.842  1.00 60.12           N  
ATOM   8728  CA  ASN E  25     234.816 191.888 279.296  1.00 60.12           C  
ATOM   8729  C   ASN E  25     233.485 192.322 279.893  1.00 60.12           C  
ATOM   8730  O   ASN E  25     233.461 192.872 280.997  1.00 60.12           O  
ATOM   8731  CB  ASN E  25     235.918 192.841 279.747  1.00 60.12           C  
ATOM   8732  CG  ASN E  25     237.298 192.340 279.406  1.00 60.12           C  
ATOM   8733  OD1 ASN E  25     237.556 191.138 279.417  1.00 60.12           O  
ATOM   8734  ND2 ASN E  25     238.204 193.263 279.106  1.00 60.12           N  
ATOM   8735  N   LYS E  26     232.390 192.081 279.165  1.00 67.13           N  
ATOM   8736  CA  LYS E  26     231.030 192.479 279.624  1.00 67.13           C  
ATOM   8737  C   LYS E  26     230.679 191.779 280.943  1.00 67.13           C  
ATOM   8738  O   LYS E  26     229.952 192.384 281.756  1.00 67.13           O  
ATOM   8739  CB  LYS E  26     229.990 192.162 278.544  1.00 67.13           C  
ATOM   8740  CG  LYS E  26     229.293 193.371 277.935  1.00 67.13           C  
ATOM   8741  CD  LYS E  26     227.789 193.217 277.852  1.00 67.13           C  
ATOM   8742  CE  LYS E  26     227.067 194.534 277.666  1.00 67.13           C  
ATOM   8743  NZ  LYS E  26     225.619 194.337 277.421  1.00 67.13           N  
ATOM   8744  N   GLY E  27     231.172 190.552 281.137  1.00 80.64           N  
ATOM   8745  CA  GLY E  27     230.898 189.778 282.325  1.00 80.64           C  
ATOM   8746  C   GLY E  27     229.835 188.720 282.086  1.00 80.64           C  
ATOM   8747  O   GLY E  27     228.765 188.976 281.527  1.00 80.64           O  
ATOM   8748  N   LYS E  28     230.178 187.491 282.481  1.00 89.67           N  
ATOM   8749  CA  LYS E  28     229.297 186.299 282.361  1.00 89.67           C  
ATOM   8750  C   LYS E  28     229.384 185.573 283.703  1.00 89.67           C  
ATOM   8751  O   LYS E  28     230.376 184.849 283.920  1.00 89.67           O  
ATOM   8752  CB  LYS E  28     229.760 185.403 281.209  1.00 89.67           C  
ATOM   8753  CG  LYS E  28     229.045 185.625 279.883  1.00 89.67           C  
ATOM   8754  CD  LYS E  28     229.731 184.955 278.711  1.00 89.67           C  
ATOM   8755  CE  LYS E  28     229.611 183.446 278.738  1.00 89.67           C  
ATOM   8756  NZ  LYS E  28     229.601 182.872 277.372  1.00 89.67           N  
ATOM   8757  N   GLU E  29     228.397 185.786 284.576  1.00 96.36           N  
ATOM   8758  CA  GLU E  29     228.456 185.204 285.910  1.00 96.36           C  
ATOM   8759  C   GLU E  29     227.564 183.981 286.063  1.00 96.36           C  
ATOM   8760  O   GLU E  29     227.357 183.509 287.188  1.00 96.36           O  
ATOM   8761  CB  GLU E  29     228.087 186.263 286.950  1.00 96.36           C  
ATOM   8762  CG  GLU E  29     228.974 187.502 286.926  1.00 96.36           C  
ATOM   8763  CD  GLU E  29     230.317 187.273 287.592  1.00 96.36           C  
ATOM   8764  OE1 GLU E  29     230.359 186.529 288.595  1.00 96.36           O  
ATOM   8765  OE2 GLU E  29     231.326 187.835 287.115  1.00 96.36           O  
ATOM   8766  N   ARG E  30     227.025 183.451 284.967  1.00 90.84           N  
ATOM   8767  CA  ARG E  30     226.080 182.350 285.067  1.00 90.84           C  
ATOM   8768  C   ARG E  30     226.127 181.521 283.792  1.00 90.84           C  
ATOM   8769  O   ARG E  30     226.454 182.019 282.712  1.00 90.84           O  
ATOM   8770  CB  ARG E  30     224.664 182.877 285.328  1.00 90.84           C  
ATOM   8771  CG  ARG E  30     223.600 181.816 285.543  1.00 90.84           C  
ATOM   8772  CD  ARG E  30     222.270 182.463 285.872  1.00 90.84           C  
ATOM   8773  NE  ARG E  30     221.207 181.484 286.051  1.00 90.84           N  
ATOM   8774  CZ  ARG E  30     219.954 181.791 286.359  1.00 90.84           C  
ATOM   8775  NH1 ARG E  30     219.571 183.046 286.531  1.00 90.84           N  
ATOM   8776  NH2 ARG E  30     219.061 180.815 286.491  1.00 90.84           N  
ATOM   8777  N   THR E  31     225.790 180.241 283.936  1.00 85.86           N  
ATOM   8778  CA  THR E  31     225.645 179.319 282.818  1.00 85.86           C  
ATOM   8779  C   THR E  31     224.191 178.885 282.737  1.00 85.86           C  
ATOM   8780  O   THR E  31     223.519 178.753 283.765  1.00 85.86           O  
ATOM   8781  CB  THR E  31     226.561 178.104 282.976  1.00 85.86           C  
ATOM   8782  OG1 THR E  31     226.406 177.238 281.846  1.00 85.86           O  
ATOM   8783  CG2 THR E  31     226.230 177.338 284.244  1.00 85.86           C  
ATOM   8784  N   TYR E  32     223.698 178.679 281.515  1.00 80.67           N  
ATOM   8785  CA  TYR E  32     222.272 178.485 281.300  1.00 80.67           C  
ATOM   8786  C   TYR E  32     221.900 177.166 280.640  1.00 80.67           C  
ATOM   8787  O   TYR E  32     220.747 176.745 280.760  1.00 80.67           O  
ATOM   8788  CB  TYR E  32     221.707 179.634 280.458  1.00 80.67           C  
ATOM   8789  CG  TYR E  32     221.866 180.991 281.095  1.00 80.67           C  
ATOM   8790  CD1 TYR E  32     220.929 181.465 282.001  1.00 80.67           C  
ATOM   8791  CD2 TYR E  32     222.948 181.801 280.787  1.00 80.67           C  
ATOM   8792  CE1 TYR E  32     221.066 182.705 282.583  1.00 80.67           C  
ATOM   8793  CE2 TYR E  32     223.095 183.043 281.364  1.00 80.67           C  
ATOM   8794  CZ  TYR E  32     222.151 183.490 282.263  1.00 80.67           C  
ATOM   8795  OH  TYR E  32     222.290 184.727 282.845  1.00 80.67           O  
ATOM   8796  N   PHE E  33     222.827 176.493 279.967  1.00 74.35           N  
ATOM   8797  CA  PHE E  33     222.510 175.267 279.252  1.00 74.35           C  
ATOM   8798  C   PHE E  33     223.303 174.110 279.830  1.00 74.35           C  
ATOM   8799  O   PHE E  33     224.350 174.300 280.454  1.00 74.35           O  
ATOM   8800  CB  PHE E  33     222.817 175.372 277.754  1.00 74.35           C  
ATOM   8801  CG  PHE E  33     221.840 176.207 276.987  1.00 74.35           C  
ATOM   8802  CD1 PHE E  33     220.606 175.700 276.626  1.00 74.35           C  
ATOM   8803  CD2 PHE E  33     222.164 177.496 276.610  1.00 74.35           C  
ATOM   8804  CE1 PHE E  33     219.714 176.464 275.916  1.00 74.35           C  
ATOM   8805  CE2 PHE E  33     221.275 178.265 275.900  1.00 74.35           C  
ATOM   8806  CZ  PHE E  33     220.049 177.747 275.553  1.00 74.35           C  
ATOM   8807  N   SER E  34     222.785 172.904 279.621  1.00 80.11           N  
ATOM   8808  CA  SER E  34     223.505 171.677 279.948  1.00 80.11           C  
ATOM   8809  C   SER E  34     223.404 170.765 278.737  1.00 80.11           C  
ATOM   8810  O   SER E  34     222.317 170.265 278.426  1.00 80.11           O  
ATOM   8811  CB  SER E  34     222.926 171.004 281.189  1.00 80.11           C  
ATOM   8812  OG  SER E  34     223.580 169.778 281.453  1.00 80.11           O  
ATOM   8813  N   CYS E  35     224.522 170.571 278.042  1.00 83.56           N  
ATOM   8814  CA  CYS E  35     224.580 169.758 276.838  1.00 83.56           C  
ATOM   8815  C   CYS E  35     225.322 168.465 277.140  1.00 83.56           C  
ATOM   8816  O   CYS E  35     226.245 168.443 277.958  1.00 83.56           O  
ATOM   8817  CB  CYS E  35     225.288 170.499 275.699  1.00 83.56           C  
ATOM   8818  SG  CYS E  35     224.343 171.778 274.822  1.00 83.56           S  
ATOM   8819  N   SER E  36     225.030 167.377 276.461  1.00 88.76           N  
ATOM   8820  CA  SER E  36     225.856 166.189 276.756  1.00 88.76           C  
ATOM   8821  C   SER E  36     226.017 165.368 275.484  1.00 88.76           C  
ATOM   8822  O   SER E  36     225.055 165.259 274.746  1.00 88.76           O  
ATOM   8823  CB  SER E  36     225.249 165.383 277.844  1.00 88.76           C  
ATOM   8824  OG  SER E  36     225.867 164.107 277.886  1.00 88.76           O  
ATOM   8825  N   GLY E  37     227.183 164.779 275.259  1.00 97.32           N  
ATOM   8826  CA  GLY E  37     227.373 163.970 274.043  1.00 97.32           C  
ATOM   8827  C   GLY E  37     227.058 162.519 274.315  1.00 97.32           C  
ATOM   8828  O   GLY E  37     227.187 161.685 273.401  1.00 97.32           O  
ATOM   8829  N   GLU E  38     226.730 162.203 275.563  1.00101.85           N  
ATOM   8830  CA  GLU E  38     226.416 160.792 275.889  1.00101.85           C  
ATOM   8831  C   GLU E  38     227.707 159.994 275.757  1.00101.85           C  
ATOM   8832  O   GLU E  38     228.067 159.285 276.709  1.00101.85           O  
ATOM   8833  CB  GLU E  38     225.411 160.257 274.883  1.00101.85           C  
ATOM   8834  CG  GLU E  38     224.605 159.107 275.421  1.00101.85           C  
ATOM   8835  CD  GLU E  38     224.033 158.292 274.286  1.00101.85           C  
ATOM   8836  OE1 GLU E  38     223.902 157.068 274.446  1.00101.85           O  
ATOM   8837  OE2 GLU E  38     223.756 158.891 273.232  1.00101.85           O  
ATOM   8838  N   GLY E  39     228.367 160.160 274.604  1.00 97.95           N  
ATOM   8839  CA  GLY E  39     229.608 159.440 274.270  1.00 97.95           C  
ATOM   8840  C   GLY E  39     230.671 159.701 275.311  1.00 97.95           C  
ATOM   8841  O   GLY E  39     231.329 158.742 275.705  1.00 97.95           O  
ATOM   8842  N   ILE E  40     230.821 160.948 275.754  1.00 89.30           N  
ATOM   8843  CA  ILE E  40     231.789 161.291 276.838  1.00 89.30           C  
ATOM   8844  C   ILE E  40     231.425 162.676 277.387  1.00 89.30           C  
ATOM   8845  O   ILE E  40     230.549 163.337 276.811  1.00 89.30           O  
ATOM   8846  CB  ILE E  40     233.268 161.136 276.425  1.00 89.30           C  
ATOM   8847  CG1 ILE E  40     233.447 160.327 275.139  1.00 89.30           C  
ATOM   8848  CG2 ILE E  40     234.094 160.567 277.571  1.00 89.30           C  
ATOM   8849  CD1 ILE E  40     234.870 159.901 274.863  1.00 89.30           C  
ATOM   8850  N   LEU E  41     232.049 163.085 278.486  1.00 93.31           N  
ATOM   8851  CA  LEU E  41     231.677 164.380 279.091  1.00 93.31           C  
ATOM   8852  C   LEU E  41     232.657 164.711 280.209  1.00 93.31           C  
ATOM   8853  O   LEU E  41     233.667 163.991 280.344  1.00 93.31           O  
ATOM   8854  CB  LEU E  41     230.275 164.195 279.665  1.00 93.31           C  
ATOM   8855  CG  LEU E  41     230.018 162.928 280.493  1.00 93.31           C  
ATOM   8856  CD1 LEU E  41     230.092 161.646 279.686  1.00 93.31           C  
ATOM   8857  CD2 LEU E  41     230.889 162.844 281.729  1.00 93.31           C  
ATOM   8858  N   THR E  42     232.359 165.774 280.957  1.00 87.91           N  
ATOM   8859  CA  THR E  42     233.170 166.172 282.132  1.00 87.91           C  
ATOM   8860  C   THR E  42     232.239 166.839 283.122  1.00 87.91           C  
ATOM   8861  O   THR E  42     231.064 167.045 282.771  1.00 87.91           O  
ATOM   8862  CB  THR E  42     234.310 167.145 281.871  1.00 87.91           C  
ATOM   8863  OG1 THR E  42     234.913 167.211 283.160  1.00 87.91           O  
ATOM   8864  CG2 THR E  42     233.833 168.526 281.494  1.00 87.91           C  
ATOM   8865  N   GLY E  43     232.739 167.152 284.309  1.00 87.36           N  
ATOM   8866  CA  GLY E  43     231.746 167.717 285.242  1.00 87.36           C  
ATOM   8867  C   GLY E  43     230.835 168.620 284.442  1.00 87.36           C  
ATOM   8868  O   GLY E  43     231.353 169.521 283.765  1.00 87.36           O  
ATOM   8869  N   LEU E  44     229.525 168.430 284.544  1.00 90.81           N  
ATOM   8870  CA  LEU E  44     228.608 169.164 283.645  1.00 90.81           C  
ATOM   8871  C   LEU E  44     228.801 170.667 283.842  1.00 90.81           C  
ATOM   8872  O   LEU E  44     228.181 171.457 283.129  1.00 90.81           O  
ATOM   8873  CB  LEU E  44     227.164 168.682 283.802  1.00 90.81           C  
ATOM   8874  CG  LEU E  44     226.441 168.378 282.486  1.00 90.81           C  
ATOM   8875  CD1 LEU E  44     225.934 169.644 281.823  1.00 90.81           C  
ATOM   8876  CD2 LEU E  44     227.329 167.603 281.529  1.00 90.81           C  
ATOM   8877  N   HIS E  45     229.691 171.053 284.741  1.00 91.92           N  
ATOM   8878  CA  HIS E  45     229.948 172.496 284.909  1.00 91.92           C  
ATOM   8879  C   HIS E  45     230.332 173.036 283.533  1.00 91.92           C  
ATOM   8880  O   HIS E  45     229.851 174.122 283.205  1.00 91.92           O  
ATOM   8881  CB  HIS E  45     231.052 172.659 285.945  1.00 91.92           C  
ATOM   8882  CG  HIS E  45     230.773 171.810 287.127  1.00 91.92           C  
ATOM   8883  ND1 HIS E  45     230.465 172.337 288.352  1.00 91.92           N  
ATOM   8884  CD2 HIS E  45     230.662 170.472 287.247  1.00 91.92           C  
ATOM   8885  CE1 HIS E  45     230.231 171.357 289.203  1.00 91.92           C  
ATOM   8886  NE2 HIS E  45     230.346 170.199 288.547  1.00 91.92           N  
ATOM   8887  N   THR E  46     231.174 172.329 282.764  1.00 80.58           N  
ATOM   8888  CA  THR E  46     231.638 172.799 281.420  1.00 80.58           C  
ATOM   8889  C   THR E  46     231.093 171.864 280.332  1.00 80.58           C  
ATOM   8890  O   THR E  46     230.660 170.757 280.709  1.00 80.58           O  
ATOM   8891  CB  THR E  46     233.167 172.917 281.365  1.00 80.58           C  
ATOM   8892  OG1 THR E  46     233.721 171.621 281.593  1.00 80.58           O  
ATOM   8893  CG2 THR E  46     233.718 173.895 282.380  1.00 80.58           C  
ATOM   8894  N   ILE E  47     231.064 172.268 279.049  1.00 71.37           N  
ATOM   8895  CA  ILE E  47     230.466 171.305 278.135  1.00 71.37           C  
ATOM   8896  C   ILE E  47     231.500 170.990 277.068  1.00 71.37           C  
ATOM   8897  O   ILE E  47     231.743 171.817 276.184  1.00 71.37           O  
ATOM   8898  CB  ILE E  47     229.189 171.840 277.481  1.00 71.37           C  
ATOM   8899  CG1 ILE E  47     228.110 172.110 278.527  1.00 71.37           C  
ATOM   8900  CG2 ILE E  47     228.701 170.867 276.433  1.00 71.37           C  
ATOM   8901  CD1 ILE E  47     226.926 172.880 277.985  1.00 71.37           C  
ATOM   8902  N   LYS E  48     232.095 169.807 277.128  1.00 61.42           N  
ATOM   8903  CA  LYS E  48     233.082 169.414 276.134  1.00 61.42           C  
ATOM   8904  C   LYS E  48     232.613 168.190 275.363  1.00 61.42           C  
ATOM   8905  O   LYS E  48     232.110 167.227 275.950  1.00 61.42           O  
ATOM   8906  CB  LYS E  48