CNRS Nantes University UFIP UFIP
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***  PHOTOSYNTHESIS 25-SEP-08 3ENI  ***

elNémo ID: 21021020485394362

Job options:

ID        	=	 21021020485394362
JOBID     	=	 PHOTOSYNTHESIS 25-SEP-08 3ENI
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    PHOTOSYNTHESIS                          25-SEP-08   3ENI              
TITLE     CRYSTAL STRUCTURE OF THE FENNA-MATTHEWS-OLSON PROTEIN FROM            
TITLE    2 CHLOROBACULUM TEPIDUM                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BACTERIOCHLOROPHYLL A PROTEIN;                             
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: BCHL A PROTEIN, BCP, FENNA-MATTHEWS-OLSON PROTEIN,          
COMPND   5 FMO PROTEIN                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLOROBACULUM TEPIDUM;                          
SOURCE   3 ORGANISM_TAXID: 1097;                                                
SOURCE   4 OTHER_DETAILS: THIS SPECIES WAS FORMERLY KNOWN AS                    
SOURCE   5 CHLOROBIUM TEPIDUM                                                   
KEYWDS    BETA SHEET, GAMMA TURN, BACTERIOCHLOROPHYLL, CHLOROPHYLL,             
KEYWDS   2 CHROMOPHORE, ELECTRON TRANSPORT, MAGNESIUM, METAL-BINDING,           
KEYWDS   3 PHOTOSYNTHESIS, REACTION CENTER, TRANSPORT                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.TRONRUD,A.CAMARA-ARTIGAS,R.BLANKENSHIP,J.P.ALLEN                    
REVDAT   2   16-MAR-10 3ENI    1       JRNL                                     
REVDAT   1   12-MAY-09 3ENI    0                                                
SPRSDE     12-MAY-09 3ENI      1M50 1KSA                                        
JRNL        AUTH   D.E.TRONRUD,J.WEN,L.GAY,R.E.BLANKENSHIP                      
JRNL        TITL   THE STRUCTURAL BASIS FOR THE DIFFERENCE IN                   
JRNL        TITL 2 ABSORBANCE SPECTRA FOR THE FMO ANTENNA PROTEIN FROM          
JRNL        TITL 3 VARIOUS GREEN SULFUR BACTERIA.                               
JRNL        REF    PHOTOSYNTH.RES.               V. 100    79 2009              
JRNL        REFN                   ISSN 0166-8595                               
JRNL        PMID   19437128                                                     
JRNL        DOI    10.1007/S11120-009-9430-6                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.CAMARA-ARTIGAS,R.BLANKENSHIP,J.P.ALLEN                     
REMARK   1  TITL   THE STRUCTURE OF THE FMO PROTEIN FROM CHLOROBIUM             
REMARK   1  TITL 2 TEPIDUM AT 2.2 A RESOLUTION                                  
REMARK   1  REF    PHOTOSYNTH.RES.               V.  75    49 2003              
REMARK   1  REFN                   ISSN 0166-8595                               
REMARK   1  PMID   16245093                                                     
REMARK   1  DOI    10.1023/A:1022406703110                                      
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.F.LI,W.L.ZHOU,R.E.BLANKENSHIP,J.P.ALLEN                    
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE BACTERIOCHLOROPHYLL A               
REMARK   1  TITL 2 PROTEIN FROM CHLOROBIUM TEPIDUM                              
REMARK   1  REF    J.MOL.BIOL.                   V. 271   456 1997              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   9268671                                                      
REMARK   1  DOI    10.1006/JMBI.1997.1189                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.1.1                                     
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 36706                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.166                          
REMARK   3   R VALUE            (WORKING SET)  : 0.163                          
REMARK   3   FREE R VALUE                      : 0.207                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1853                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.33                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 86.54                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4147                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2740                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3922                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2705                   
REMARK   3   BIN FREE R VALUE                        : 0.3364                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.43                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 225                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5445                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1122                                    
REMARK   3   SOLVENT ATOMS            : 206                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6865   ; 2.000  ; NULL                
REMARK   3    BOND ANGLES               : 9629   ; 2.000  ; NULL                
REMARK   3    TORSION ANGLES            : 1371   ; 0.000  ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : 257    ; 2.000  ; NULL                
REMARK   3    GENERAL PLANES            : 922    ; 5.000  ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : 6861   ; 20.000 ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : 36     ; 5.000  ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : 36     ; 0.000  ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.011                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.20                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ENI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049543.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : GRAPHITE FILTER                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41641                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.12900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX/PHASER                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% (W/V) POLYETHYLENE GLYCOL 600,        
REMARK 280  50 MM SODIUM CITRATE, 10% (V/V) 2-PROPONAL, PH 5.60, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+1/4,X+3/4,-Z+3/4                                      
REMARK 290      14555   -Y+1/4,-X+1/4,-Z+1/4                                    
REMARK 290      15555   Y+3/4,-X+3/4,Z+1/4                                      
REMARK 290      16555   -Y+3/4,X+1/4,Z+3/4                                      
REMARK 290      17555   X+1/4,Z+3/4,-Y+3/4                                      
REMARK 290      18555   -X+3/4,Z+1/4,Y+3/4                                      
REMARK 290      19555   -X+1/4,-Z+1/4,-Y+1/4                                    
REMARK 290      20555   X+3/4,-Z+3/4,Y+1/4                                      
REMARK 290      21555   Z+1/4,Y+3/4,-X+3/4                                      
REMARK 290      22555   Z+3/4,-Y+3/4,X+1/4                                      
REMARK 290      23555   -Z+3/4,Y+1/4,X+3/4                                      
REMARK 290      24555   -Z+1/4,-Y+1/4,-X+1/4                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       84.55000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       84.55000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       84.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       84.55000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       84.55000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       84.55000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       84.55000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       84.55000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       84.55000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       84.55000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       84.55000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       84.55000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       84.55000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       84.55000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       84.55000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       84.55000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       84.55000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       84.55000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000       42.27500            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000      126.82500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      126.82500            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000       42.27500            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000       42.27500            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       42.27500            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000      126.82500            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000      126.82500            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       42.27500            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000      126.82500            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000       42.27500            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000      126.82500            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000       42.27500            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000      126.82500            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000      126.82500            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000      126.82500            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000       42.27500            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000      126.82500            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000       42.27500            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000       42.27500            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000       42.27500            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000      126.82500            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000      126.82500            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000       42.27500            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000       42.27500            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000      126.82500            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000      126.82500            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000      126.82500            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000      126.82500            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000       42.27500            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000      126.82500            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000       42.27500            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000      126.82500            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000       42.27500            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000       42.27500            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000       42.27500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 51530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -380.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 51530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -374.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 350   BIOMT1   2  0.000000  0.000000 -1.000000       84.55000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000       84.55000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000      -84.55000            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000       84.55000            
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     ALA A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     PHE A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     PHE C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ASN C     6                                                      
REMARK 465     ASP C     7                                                      
REMARK 465     PRO C   213                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   8    CG1  CG2                                            
REMARK 470     SER A  23    CA   C    O    CB   OG                              
REMARK 470     LYS A  30    CD   CE   NZ                                        
REMARK 470     ARG A  32    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  34    CD   CE   NZ                                        
REMARK 470     LYS A  51    CD   CE   NZ                                        
REMARK 470     LYS A  55    CE   NZ                                             
REMARK 470     LYS A  61    CD   CE   NZ                                        
REMARK 470     LYS A  78    CE   NZ                                             
REMARK 470     ARG A 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 130    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 167    CE   NZ                                             
REMARK 470     LYS A 214    CG   CD   CE   NZ                                   
REMARK 470     LYS A 246    CE   NZ                                             
REMARK 470     GLN A 252    CD   OE1  NE2                                       
REMARK 470     GLU A 254    CD   OE1  OE2                                       
REMARK 470     GLN A 262    CD   OE1  NE2                                       
REMARK 470     LYS A 267    CD   CE   NZ                                        
REMARK 470     LYS A 313    CE   NZ                                             
REMARK 470     LYS A 318    CD   CE   NZ                                        
REMARK 470     LYS A 321    CE   NZ                                             
REMARK 470     ARG A 323    NE   CZ   NH1  NH2                                  
REMARK 470     GLN A 365    OE1  NE2                                            
REMARK 470     VAL C   8    CG1  CG2                                            
REMARK 470     GLY C  22    CA   C    O                                         
REMARK 470     SER C  23    OG                                                  
REMARK 470     LYS C  30    CE   NZ                                             
REMARK 470     LYS C  34    CE   NZ                                             
REMARK 470     LYS C  51    CD   CE   NZ                                        
REMARK 470     LYS C  61    CD   CE   NZ                                        
REMARK 470     ARG C 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 130    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C 167    CG   CD   CE   NZ                                   
REMARK 470     GLY C 212    C    O                                              
REMARK 470     LYS C 214    N    CB   CG   CD   CE   NZ                         
REMARK 470     ASP C 245    CG   OD1  OD2                                       
REMARK 470     LYS C 246    CE   NZ                                             
REMARK 470     GLN C 252    CD   OE1  NE2                                       
REMARK 470     LYS C 267    CE   NZ                                             
REMARK 470     LYS C 318    CD   CE   NZ                                        
REMARK 470     LYS C 321    CD   CE   NZ                                        
REMARK 470     GLN C 365    OE1  NE2                                            
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    ALA A  40       45.18    -87.45                                   
REMARK 500    LEU A  57      -66.01   -105.65                                   
REMARK 500    SER A  76       -6.14     78.38                                   
REMARK 500    ILE A 137      -65.95   -108.20                                   
REMARK 500    ASP A 177      -62.03    -96.58                                   
REMARK 500    LEU A 334     -118.35     58.42                                   
REMARK 500    SER A 340      147.98   -170.87                                   
REMARK 500    ALA C  40       45.11    -88.13                                   
REMARK 500    LEU C  57      -66.44   -104.64                                   
REMARK 500    SER C  76       -5.31     78.24                                   
REMARK 500    ILE C 137      -68.04   -108.91                                   
REMARK 500    ASP C 177      -63.30    -93.25                                   
REMARK 500    LEU C 334     -116.67     58.71                                   
REMARK 500    SER C 340      147.01   -171.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1142        DISTANCE =  5.36 ANGSTROMS                       
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     BCL A  378                                                       
REMARK 610     BCL C  378                                                       
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                             BCL A 371  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 110   NE2                                                    
REMARK 620 2 BCL A 371   NA  102.1                                              
REMARK 620 3 BCL A 371   NB   96.3  89.8                                        
REMARK 620 4 BCL A 371   NC   99.9 157.9  89.1                                  
REMARK 620 5 BCL A 371   ND  105.8  87.9 157.9  84.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL A 378  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 123   O                                                      
REMARK 620 2 BCL A 378   NA   94.7                                              
REMARK 620 3 BCL A 378   NB  101.8  90.3                                        
REMARK 620 4 BCL A 378   NC  103.1 161.8  89.9                                  
REMARK 620 5 BCL A 378   ND   97.9  88.7 160.3  85.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL A 376  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 145   NE2                                                    
REMARK 620 2 BCL A 376   NA  100.5                                              
REMARK 620 3 BCL A 376   NB   97.6  89.5                                        
REMARK 620 4 BCL A 376   NC  100.0 159.4  89.5                                  
REMARK 620 5 BCL A 376   NC  100.2 159.3  89.4   0.2                            
REMARK 620 6 BCL A 376   ND  102.8  88.7 159.5  85.1  85.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL A 375  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 241   O                                                      
REMARK 620 2 BCL A 375   NA  102.1                                              
REMARK 620 3 BCL A 375   NB   91.0  89.2                                        
REMARK 620 4 BCL A 375   NC   98.3 159.6  89.6                                  
REMARK 620 5 BCL A 375   ND  112.6  88.3 156.3  84.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL A 374  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 289   NE2                                                    
REMARK 620 2 BCL A 374   NA   94.0                                              
REMARK 620 3 BCL A 374   NB   94.1  89.1                                        
REMARK 620 4 BCL A 374   NC  104.3 161.6  90.3                                  
REMARK 620 5 BCL A 374   ND  108.4  88.7 157.5  84.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL A 377  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 296   ND1                                                    
REMARK 620 2 BCL A 377   NA   94.7                                              
REMARK 620 3 BCL A 377   NB   93.5  89.5                                        
REMARK 620 4 BCL A 377   NC  107.6 157.6  88.9                                  
REMARK 620 5 BCL A 377   ND  110.0  87.9 156.5  84.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL A 373  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 297   NE2                                                    
REMARK 620 2 BCL A 373   NA  102.6                                              
REMARK 620 3 BCL A 373   NB   99.5  89.7                                        
REMARK 620 4 BCL A 373   NC  100.1 157.2  89.1                                  
REMARK 620 5 BCL A 373   ND  103.6  87.2 156.8  85.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL C 371  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 110   NE2                                                    
REMARK 620 2 BCL C 371   NA  100.4                                              
REMARK 620 3 BCL C 371   NB   95.9  89.8                                        
REMARK 620 4 BCL C 371   NC  101.0 158.6  89.3                                  
REMARK 620 5 BCL C 371   ND  106.2  88.2 157.7  84.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL C 378  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 123   O                                                      
REMARK 620 2 BCL C 378   NA   93.5                                              
REMARK 620 3 BCL C 378   NB  101.8  90.3                                        
REMARK 620 4 BCL C 378   NC  103.6 162.5  90.0                                  
REMARK 620 5 BCL C 378   ND   97.8  88.8 160.4  85.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL C 376  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 145   NE2                                                    
REMARK 620 2 BCL C 376   NA  100.5                                              
REMARK 620 3 BCL C 376   NB   98.0  89.3                                        
REMARK 620 4 BCL C 376   NC  100.1 159.3  89.3                                  
REMARK 620 5 BCL C 376   NC  100.3 159.1  89.2   0.2                            
REMARK 620 6 BCL C 376   ND  103.7  88.1 158.2  85.5  85.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL C 375  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU C 241   O                                                      
REMARK 620 2 BCL C 375   NA  101.0                                              
REMARK 620 3 BCL C 375   NB   89.9  89.9                                        
REMARK 620 4 BCL C 375   NC   96.4 162.5  90.5                                  
REMARK 620 5 BCL C 375   ND  110.3  88.3 159.7  85.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL C 374  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 289   NE2                                                    
REMARK 620 2 BCL C 374   NA   95.6                                              
REMARK 620 3 BCL C 374   NB   97.5  89.9                                        
REMARK 620 4 BCL C 374   NC  101.8 162.5  89.7                                  
REMARK 620 5 BCL C 374   ND  106.1  88.7 156.3  84.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL C 377  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 296   ND1                                                    
REMARK 620 2 BCL C 377   NA   94.5                                              
REMARK 620 3 BCL C 377   NB   92.0  89.5                                        
REMARK 620 4 BCL C 377   NC  108.1 157.4  89.5                                  
REMARK 620 5 BCL C 377   ND  110.2  87.4 157.8  85.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL C 373  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 297   NE2                                                    
REMARK 620 2 BCL C 373   NA  101.8                                              
REMARK 620 3 BCL C 373   NB  103.0  89.2                                        
REMARK 620 4 BCL C 373   NC   98.1 159.9  88.9                                  
REMARK 620 5 BCL C 373   ND  102.4  87.3 154.5  85.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL A 372  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1043   O                                                      
REMARK 620 2 BCL A 372   NA   93.5                                              
REMARK 620 3 BCL A 372   NB  101.9  89.9                                        
REMARK 620 4 BCL A 372   NC  105.8 160.5  89.0                                  
REMARK 620 5 BCL A 372   ND   99.4  88.9 158.8  85.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BCL C 372  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C1043   O                                                      
REMARK 620 2 BCL C 372   NA   93.0                                              
REMARK 620 3 BCL C 372   NB  101.6  89.4                                        
REMARK 620 4 BCL C 372   NC  106.1 160.6  89.7                                  
REMARK 620 5 BCL C 372   ND  100.7  88.4 157.7  85.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL A 371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL A 372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL A 373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL A 374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL A 375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL A 376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL A 377                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL A 378                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL C 371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL C 372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL C 373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL C 374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL C 375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL C 376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL C 377                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCL C 378                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M50   RELATED DB: PDB                                   
REMARK 900 EARLIER MODEL REFINED AGAINST THE SAME DIFFRACTION DATA SET          
REMARK 900 RELATED ID: 1KSA   RELATED DB: PDB                                   
REMARK 900 EVEN EARLIER MODEL REFINED IN NEARLY CORRECT SPACE GROUP             
REMARK 900 RELATED ID: 3EOJ   RELATED DB: PDB                                   
REMARK 900 FMO PROTEIN FROM PROSTHECOCHLORIS AESTUARII 2K AT 1.3A               
REMARK 900 RESOLUTION                                                           
DBREF  3ENI A    1   365  UNP    Q46393   BCPA_CHLTE       2    366             
DBREF  3ENI C    1   365  UNP    Q46393   BCPA_CHLTE       2    366             
SEQRES   1 A  365  ALA LEU PHE GLY SER ASN ASP VAL THR THR ALA HIS SER          
SEQRES   2 A  365  ASP TYR GLU ILE VAL LEU GLU GLY GLY SER SER SER TRP          
SEQRES   3 A  365  GLY LYS VAL LYS ALA ARG ALA LYS VAL ASN ALA PRO PRO          
SEQRES   4 A  365  ALA SER PRO LEU LEU PRO ALA ASP CYS ASP VAL LYS LEU          
SEQRES   5 A  365  ASN VAL LYS PRO LEU ASP PRO ALA LYS GLY PHE VAL ARG          
SEQRES   6 A  365  ILE SER ALA VAL PHE GLU SER ILE VAL ASP SER THR LYS          
SEQRES   7 A  365  ASN LYS LEU THR ILE GLU ALA ASP ILE ALA ASN GLU THR          
SEQRES   8 A  365  LYS GLU ARG ARG ILE SER VAL GLY GLU GLY MET VAL SER          
SEQRES   9 A  365  VAL GLY ASP PHE SER HIS THR PHE SER PHE GLU GLY SER          
SEQRES  10 A  365  VAL VAL ASN LEU PHE TYR TYR ARG SER ASP ALA VAL ARG          
SEQRES  11 A  365  ARG ASN VAL PRO ASN PRO ILE TYR MET GLN GLY ARG GLN          
SEQRES  12 A  365  PHE HIS ASP ILE LEU MET LYS VAL PRO LEU ASP ASN ASN          
SEQRES  13 A  365  ASP LEU ILE ASP THR TRP GLU GLY THR VAL LYS ALA ILE          
SEQRES  14 A  365  GLY SER THR GLY ALA PHE ASN ASP TRP ILE ARG ASP PHE          
SEQRES  15 A  365  TRP PHE ILE GLY PRO ALA PHE THR ALA LEU ASN GLU GLY          
SEQRES  16 A  365  GLY GLN ARG ILE SER ARG ILE GLU VAL ASN GLY LEU ASN          
SEQRES  17 A  365  THR GLU SER GLY PRO LYS GLY PRO VAL GLY VAL SER ARG          
SEQRES  18 A  365  TRP ARG PHE SER HIS GLY GLY SER GLY MET VAL ASP SER          
SEQRES  19 A  365  ILE SER ARG TRP ALA GLU LEU PHE PRO SER ASP LYS LEU          
SEQRES  20 A  365  ASN ARG PRO ALA GLN VAL GLU ALA GLY PHE ARG SER ASP          
SEQRES  21 A  365  SER GLN GLY ILE GLU VAL LYS VAL ASP GLY GLU PHE PRO          
SEQRES  22 A  365  GLY VAL SER VAL ASP ALA GLY GLY GLY LEU ARG ARG ILE          
SEQRES  23 A  365  LEU ASN HIS PRO LEU ILE PRO LEU VAL HIS HIS GLY MET          
SEQRES  24 A  365  VAL GLY LYS PHE ASN ASN PHE ASN VAL ASP ALA GLN LEU          
SEQRES  25 A  365  LYS VAL VAL LEU PRO LYS GLY TYR LYS ILE ARG TYR ALA          
SEQRES  26 A  365  ALA PRO GLN TYR ARG SER GLN ASN LEU GLU GLU TYR ARG          
SEQRES  27 A  365  TRP SER GLY GLY ALA TYR ALA ARG TRP VAL GLU HIS VAL          
SEQRES  28 A  365  CYS LYS GLY GLY VAL GLY GLN PHE GLU ILE LEU TYR ALA          
SEQRES  29 A  365  GLN                                                          
SEQRES   1 C  365  ALA LEU PHE GLY SER ASN ASP VAL THR THR ALA HIS SER          
SEQRES   2 C  365  ASP TYR GLU ILE VAL LEU GLU GLY GLY SER SER SER TRP          
SEQRES   3 C  365  GLY LYS VAL LYS ALA ARG ALA LYS VAL ASN ALA PRO PRO          
SEQRES   4 C  365  ALA SER PRO LEU LEU PRO ALA ASP CYS ASP VAL LYS LEU          
SEQRES   5 C  365  ASN VAL LYS PRO LEU ASP PRO ALA LYS GLY PHE VAL ARG          
SEQRES   6 C  365  ILE SER ALA VAL PHE GLU SER ILE VAL ASP SER THR LYS          
SEQRES   7 C  365  ASN LYS LEU THR ILE GLU ALA ASP ILE ALA ASN GLU THR          
SEQRES   8 C  365  LYS GLU ARG ARG ILE SER VAL GLY GLU GLY MET VAL SER          
SEQRES   9 C  365  VAL GLY ASP PHE SER HIS THR PHE SER PHE GLU GLY SER          
SEQRES  10 C  365  VAL VAL ASN LEU PHE TYR TYR ARG SER ASP ALA VAL ARG          
SEQRES  11 C  365  ARG ASN VAL PRO ASN PRO ILE TYR MET GLN GLY ARG GLN          
SEQRES  12 C  365  PHE HIS ASP ILE LEU MET LYS VAL PRO LEU ASP ASN ASN          
SEQRES  13 C  365  ASP LEU ILE ASP THR TRP GLU GLY THR VAL LYS ALA ILE          
SEQRES  14 C  365  GLY SER THR GLY ALA PHE ASN ASP TRP ILE ARG ASP PHE          
SEQRES  15 C  365  TRP PHE ILE GLY PRO ALA PHE THR ALA LEU ASN GLU GLY          
SEQRES  16 C  365  GLY GLN ARG ILE SER ARG ILE GLU VAL ASN GLY LEU ASN          
SEQRES  17 C  365  THR GLU SER GLY PRO LYS GLY PRO VAL GLY VAL SER ARG          
SEQRES  18 C  365  TRP ARG PHE SER HIS GLY GLY SER GLY MET VAL ASP SER          
SEQRES  19 C  365  ILE SER ARG TRP ALA GLU LEU PHE PRO SER ASP LYS LEU          
SEQRES  20 C  365  ASN ARG PRO ALA GLN VAL GLU ALA GLY PHE ARG SER ASP          
SEQRES  21 C  365  SER GLN GLY ILE GLU VAL LYS VAL ASP GLY GLU PHE PRO          
SEQRES  22 C  365  GLY VAL SER VAL ASP ALA GLY GLY GLY LEU ARG ARG ILE          
SEQRES  23 C  365  LEU ASN HIS PRO LEU ILE PRO LEU VAL HIS HIS GLY MET          
SEQRES  24 C  365  VAL GLY LYS PHE ASN ASN PHE ASN VAL ASP ALA GLN LEU          
SEQRES  25 C  365  LYS VAL VAL LEU PRO LYS GLY TYR LYS ILE ARG TYR ALA          
SEQRES  26 C  365  ALA PRO GLN TYR ARG SER GLN ASN LEU GLU GLU TYR ARG          
SEQRES  27 C  365  TRP SER GLY GLY ALA TYR ALA ARG TRP VAL GLU HIS VAL          
SEQRES  28 C  365  CYS LYS GLY GLY VAL GLY GLN PHE GLU ILE LEU TYR ALA          
SEQRES  29 C  365  GLN                                                          
HET    BCL  A 374      66                                                       
HET    BCL  A 375      66                                                       
HET    BCL  A 371      71                                                       
HET    BCL  A 376      84                                                       
HET    BCL  A 372      66                                                       
HET    BCL  A 377      83                                                       
HET    BCL  A 373      79                                                       
HET    BCL  A 378      46                                                       
HET    BCL  C 374      66                                                       
HET    BCL  C 375      66                                                       
HET    BCL  C 371      71                                                       
HET    BCL  C 376      84                                                       
HET    BCL  C 372      66                                                       
HET    BCL  C 377      83                                                       
HET    BCL  C 373      79                                                       
HET    BCL  C 378      46                                                       
HETNAM     BCL BACTERIOCHLOROPHYLL A                                            
FORMUL   3  BCL    16(C55 H74 MG N4 O6)                                         
FORMUL  19  HOH   *206(H2 O)                                                    
HELIX    1   1 SER A  126  VAL A  133  1                                   8    
HELIX    2   2 ASN A  155  THR A  172  1                                  18    
HELIX    3   3 ALA A  174  PHE A  184  1                                  11    
HELIX    4   4 PRO A  187  GLY A  195  1                                   9    
HELIX    5   5 VAL A  232  ARG A  237  1                                   6    
HELIX    6   6 PRO A  243  LEU A  247  5                                   5    
HELIX    7   7 LEU A  291  MET A  299  1                                   9    
HELIX    8   8 GLY A  341  LYS A  353  1                                  13    
HELIX    9   9 SER C  126  ARG C  131  1                                   6    
HELIX   10  10 ASN C  155  THR C  172  1                                  18    
HELIX   11  11 ALA C  174  PHE C  184  1                                  11    
HELIX   12  12 PRO C  187  GLY C  195  1                                   9    
HELIX   13  13 VAL C  232  ARG C  237  1                                   6    
HELIX   14  14 PRO C  243  LEU C  247  5                                   5    
HELIX   15  15 LEU C  291  MET C  299  1                                   9    
HELIX   16  16 GLY C  341  LYS C  353  1                                  13    
SHEET    1   A 3 GLN A 197  ILE A 199  0                                        
SHEET    2   A 3 GLY A 215  GLY A 228 -1  O  GLY A 227   N  ARG A 198           
SHEET    3   A 3 GLU A 203  GLY A 212 -1  N  ASN A 208   O  VAL A 219           
SHEET    1   B15 GLN A 197  ILE A 199  0                                        
SHEET    2   B15 GLY A 215  GLY A 228 -1  O  GLY A 227   N  ARG A 198           
SHEET    3   B15 GLY A 141  PRO A 152 -1  N  ILE A 147   O  TRP A 222           
SHEET    4   B15 PHE A 108  PHE A 122 -1  N  VAL A 119   O  PHE A 144           
SHEET    5   B15 ARG A  94  VAL A 105 -1  N  GLY A  99   O  PHE A 114           
SHEET    6   B15 THR A  77  ASN A  89 -1  N  GLU A  84   O  GLU A 100           
SHEET    7   B15 PHE A  63  VAL A  74 -1  N  ILE A  66   O  ALA A  85           
SHEET    8   B15 ALA A  46  ASP A  58 -1  N  ASN A  53   O  SER A  67           
SHEET    9   B15 ALA A 251  ASP A 260 -1  O  ALA A 255   N  VAL A  50           
SHEET   10   B15 GLY A 263  PHE A 272 -1  O  ASP A 269   N  GLU A 254           
SHEET   11   B15 GLY A  27  VAL A  35 -1  N  ALA A  33   O  VAL A 266           
SHEET   12   B15 THR A  10  LEU A  19 -1  N  GLU A  16   O  LYS A  30           
SHEET   13   B15 ASN A 307  VAL A 315  1  O  VAL A 315   N  ILE A  17           
SHEET   14   B15 GLU A 336  SER A 340 -1  O  TYR A 337   N  VAL A 314           
SHEET   15   B15 SER A 331  ASN A 333 -1  N  ASN A 333   O  GLU A 336           
SHEET    1   C 4 SER A 276  GLY A 280  0                                        
SHEET    2   C 4 LEU A 283  ILE A 286 -1  O  LEU A 283   N  ALA A 279           
SHEET    3   C 4 GLU A 360  ALA A 364 -1  O  TYR A 363   N  ARG A 284           
SHEET    4   C 4 LYS A 321  ALA A 326 -1  N  TYR A 324   O  LEU A 362           
SHEET    1   D 3 GLN C 197  ILE C 199  0                                        
SHEET    2   D 3 PRO C 216  GLY C 228 -1  O  GLY C 227   N  ARG C 198           
SHEET    3   D 3 GLU C 203  SER C 211 -1  N  ASN C 208   O  VAL C 219           
SHEET    1   E15 GLN C 197  ILE C 199  0                                        
SHEET    2   E15 PRO C 216  GLY C 228 -1  O  GLY C 227   N  ARG C 198           
SHEET    3   E15 GLY C 141  PRO C 152 -1  N  ILE C 147   O  TRP C 222           
SHEET    4   E15 PHE C 108  PHE C 122 -1  N  VAL C 119   O  PHE C 144           
SHEET    5   E15 ARG C  94  VAL C 105 -1  N  GLY C  99   O  PHE C 114           
SHEET    6   E15 THR C  77  ASN C  89 -1  N  ASP C  86   O  VAL C  98           
SHEET    7   E15 PHE C  63  VAL C  74 -1  N  PHE C  70   O  LEU C  81           
SHEET    8   E15 ALA C  46  ASP C  58 -1  N  ASN C  53   O  SER C  67           
SHEET    9   E15 ALA C 251  ASP C 260 -1  O  ALA C 255   N  VAL C  50           
SHEET   10   E15 GLY C 263  PHE C 272 -1  O  ASP C 269   N  GLU C 254           
SHEET   11   E15 GLY C  27  VAL C  35 -1  N  ALA C  33   O  VAL C 266           
SHEET   12   E15 THR C  10  LEU C  19 -1  N  GLU C  16   O  LYS C  30           
SHEET   13   E15 ASN C 307  VAL C 315  1  O  ASN C 307   N  ALA C  11           
SHEET   14   E15 GLU C 336  SER C 340 -1  O  TYR C 337   N  VAL C 314           
SHEET   15   E15 SER C 331  ASN C 333 -1  N  ASN C 333   O  GLU C 336           
SHEET    1   F 4 SER C 276  GLY C 280  0                                        
SHEET    2   F 4 LEU C 283  ILE C 286 -1  O  LEU C 283   N  ALA C 279           
SHEET    3   F 4 GLU C 360  ALA C 364 -1  O  TYR C 363   N  ARG C 284           
SHEET    4   F 4 LYS C 321  ALA C 326 -1  N  TYR C 324   O  LEU C 362           
LINK         NE2 HIS A 110                MG   BCL A 371     1555   1555  2.26  
LINK         O   TYR A 123                MG  BBCL A 378     1555   1555  2.03  
LINK         NE2 HIS A 145                MG   BCL A 376     1555   1555  2.18  
LINK         O   LEU A 241                MG   BCL A 375     1555   1555  1.99  
LINK         NE2 HIS A 289                MG   BCL A 374     1555   1555  2.15  
LINK         ND1 HIS A 296                MG   BCL A 377     1555   1555  2.22  
LINK         NE2 HIS A 297                MG   BCL A 373     1555   1555  2.18  
LINK         NE2 HIS C 110                MG   BCL C 371     1555   1555  2.27  
LINK         O   TYR C 123                MG  BBCL C 378     1555   1555  2.05  
LINK         NE2 HIS C 145                MG   BCL C 376     1555   1555  2.19  
LINK         O   LEU C 241                MG   BCL C 375     1555   1555  2.01  
LINK         NE2 HIS C 289                MG   BCL C 374     1555   1555  2.19  
LINK         ND1 HIS C 296                MG   BCL C 377     1555   1555  2.22  
LINK         NE2 HIS C 297                MG   BCL C 373     1555   1555  2.17  
LINK        MG   BCL A 372                 O   HOH A1043     1555   1555  2.03  
LINK        MG   BCL C 372                 O   HOH C1043     1555   1555  2.02  
CISPEP   1 LEU A   44    PRO A   45          0        -0.54                     
CISPEP   2 ALA A  326    PRO A  327          0         4.40                     
CISPEP   3 LEU C   44    PRO C   45          0         3.12                     
CISPEP   4 ALA C  326    PRO C  327          0         2.55                     
SITE     1 AC1 18 PHE A 108  HIS A 110  PHE A 112  ALA A 128                    
SITE     2 AC1 18 VAL A 129  MET A 149  VAL A 151  ASP A 157                    
SITE     3 AC1 18 LEU A 158  THR A 161  TRP A 162  THR A 165                    
SITE     4 AC1 18 ILE A 179  TRP A 183  BCL A 372  BCL A 376                    
SITE     5 AC1 18 BCL A 378  HOH A1093                                          
SITE     1 AC2 15 SER A  72  VAL A  74  ASN A  79  LEU A  81                    
SITE     2 AC2 15 VAL A 129  VAL A 133  ILE A 137  TYR A 138                    
SITE     3 AC2 15 GLN A 140  PHE A 182  TRP A 183  BCL A 371                    
SITE     4 AC2 15 BCL A 373  BCL A 377  HOH A1043                               
SITE     1 AC3 16 ALA A  11  TYR A  15  PRO A  38  PRO A  39                    
SITE     2 AC3 16 ALA A  40  PHE A 257  SER A 259  ILE A 264                    
SITE     3 AC3 16 HIS A 297  VAL A 300  ASN A 304  BCL A 372                    
SITE     4 AC3 16 BCL A 374  BCL A 375  BCL A 376  BCL A 377                    
SITE     1 AC4 16 TYR A  15  ILE A  17  VAL A  29  ALA A  31                    
SITE     2 AC4 16 LEU A 287  HIS A 289  PRO A 290  PRO A 293                    
SITE     3 AC4 16 HIS A 297  TYR A 344  TRP A 347  PHE A 359                    
SITE     4 AC4 16 BCL A 373  BCL A 375  BCL A 377  HOH A1081                    
SITE     1 AC5 15 VAL A  54  PHE A  70  SER A 234  ARG A 237                    
SITE     2 AC5 15 GLU A 240  LEU A 241  PHE A 242  PRO A 243                    
SITE     3 AC5 15 ALA A 255  PRO A 290  BCL A 373  BCL A 374                    
SITE     4 AC5 15 BCL A 376  BCL A 377  HOH A1053                               
SITE     1 AC6 18 ILE A  66  ALA A  85  ILE A  87  ARG A  95                    
SITE     2 AC6 18 ILE A  96  SER A  97  VAL A 118  GLN A 143                    
SITE     3 AC6 18 HIS A 145  TRP A 183  HIS A 226  SER A 234                    
SITE     4 AC6 18 TRP A 238  VAL A 253  BCL A 371  BCL A 373                    
SITE     5 AC6 18 BCL A 375  BCL A 377                                          
SITE     1 AC7 14 ALA A  40  TYR A 138  ALA A 188  GLN A 197                    
SITE     2 AC7 14 PRO A 293  HIS A 296  HIS A 297  VAL A 300                    
SITE     3 AC7 14 BCL A 372  BCL A 373  BCL A 374  BCL A 375                    
SITE     4 AC7 14 BCL A 376  HOH A1057                                          
SITE     1 AC8 13 LEU A 121  TYR A 123  ARG A 125  ASP A 160                    
SITE     2 AC8 13 THR A 161  THR A 165  SER A 171  THR A 172                    
SITE     3 AC8 13 PHE A 175  TRP A 178  ILE A 179  PHE A 182                    
SITE     4 AC8 13 BCL A 371                                                     
SITE     1 AC9 16 PHE C 108  HIS C 110  PHE C 112  SER C 126                    
SITE     2 AC9 16 VAL C 129  VAL C 151  LEU C 158  THR C 161                    
SITE     3 AC9 16 TRP C 162  THR C 165  ILE C 179  TRP C 183                    
SITE     4 AC9 16 BCL C 372  BCL C 376  BCL C 378  HOH C1060                    
SITE     1 BC1 18 SER C  72  VAL C  74  ASN C  79  LEU C  81                    
SITE     2 BC1 18 PHE C 114  VAL C 129  VAL C 133  ILE C 137                    
SITE     3 BC1 18 TYR C 138  GLN C 140  PHE C 182  TRP C 183                    
SITE     4 BC1 18 ILE C 185  BCL C 371  BCL C 373  BCL C 377                    
SITE     5 BC1 18 HOH C1043  HOH C1118                                          
SITE     1 BC2 16 ALA C  11  TYR C  15  PRO C  38  PRO C  39                    
SITE     2 BC2 16 ALA C  40  PHE C 257  SER C 259  ILE C 264                    
SITE     3 BC2 16 HIS C 297  VAL C 300  ASN C 304  BCL C 372                    
SITE     4 BC2 16 BCL C 374  BCL C 375  BCL C 376  BCL C 377                    
SITE     1 BC3 16 TYR C  15  ILE C  17  VAL C  29  ALA C  31                    
SITE     2 BC3 16 LEU C 287  HIS C 289  PRO C 293  HIS C 297                    
SITE     3 BC3 16 TYR C 344  TRP C 347  PHE C 359  ILE C 361                    
SITE     4 BC3 16 BCL C 373  BCL C 375  BCL C 377  HOH C1063                    
SITE     1 BC4 13 VAL C  54  PHE C  70  SER C 234  LEU C 241                    
SITE     2 BC4 13 PHE C 242  PRO C 243  ALA C 255  PRO C 290                    
SITE     3 BC4 13 BCL C 373  BCL C 374  BCL C 376  BCL C 377                    
SITE     4 BC4 13 HOH C1050                                                     
SITE     1 BC5 20 ILE C  66  ALA C  85  ILE C  87  ARG C  95                    
SITE     2 BC5 20 ILE C  96  SER C  97  GLY C 116  VAL C 118                    
SITE     3 BC5 20 GLN C 143  HIS C 145  TRP C 183  HIS C 226                    
SITE     4 BC5 20 SER C 234  TRP C 238  GLN C 252  VAL C 253                    
SITE     5 BC5 20 BCL C 371  BCL C 373  BCL C 375  BCL C 377                    
SITE     1 BC6 15 ALA C  40  TYR C 138  ALA C 188  ALA C 191                    
SITE     2 BC6 15 GLN C 197  PRO C 293  HIS C 296  HIS C 297                    
SITE     3 BC6 15 VAL C 300  BCL C 372  BCL C 373  BCL C 374                    
SITE     4 BC6 15 BCL C 375  BCL C 376  HOH C1054                               
SITE     1 BC7 13 LEU C 121  TYR C 123  ARG C 125  ASP C 160                    
SITE     2 BC7 13 THR C 161  THR C 165  SER C 171  THR C 172                    
SITE     3 BC7 13 PHE C 175  TRP C 178  ILE C 179  PHE C 182                    
SITE     4 BC7 13 BCL C 371                                                     
CRYST1  169.100  169.100  169.100  90.00  90.00  90.00 P 43 3 2     48          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005914  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005914  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005914        0.00000                         
ATOM      1  N   VAL A   8     -10.056 -16.507 -24.811  1.00 54.77           N  
ATOM      2  CA  VAL A   8     -10.026 -16.590 -23.348  1.00 53.90           C  
ATOM      3  C   VAL A   8      -8.585 -16.449 -22.873  1.00 53.61           C  
ATOM      4  O   VAL A   8      -7.649 -16.836 -23.593  1.00 56.83           O  
ATOM      5  CB  VAL A   8     -10.623 -17.937 -22.853  1.00 58.09           C  
ATOM      6  N   THR A   9      -8.390 -15.898 -21.677  1.00 41.85           N  
ATOM      7  CA  THR A   9      -7.040 -15.793 -21.145  1.00 38.75           C  
ATOM      8  C   THR A   9      -6.762 -17.088 -20.390  1.00 34.52           C  
ATOM      9  O   THR A   9      -7.473 -17.441 -19.467  1.00 31.00           O  
ATOM     10  CB  THR A   9      -6.825 -14.540 -20.272  1.00 46.73           C  
ATOM     11  OG1 THR A   9      -7.003 -13.377 -21.079  1.00 54.74           O  
ATOM     12  CG2 THR A   9      -5.418 -14.521 -19.717  1.00 39.66           C  
ATOM     13  N   THR A  10      -5.731 -17.798 -20.816  1.00 29.57           N  
ATOM     14  CA  THR A  10      -5.381 -19.047 -20.193  1.00 29.02           C  
ATOM     15  C   THR A  10      -3.937 -19.061 -19.801  1.00 30.37           C  
ATOM     16  O   THR A  10      -3.103 -18.654 -20.559  1.00 32.81           O  
ATOM     17  CB  THR A  10      -5.706 -20.234 -21.114  1.00 38.54           C  
ATOM     18  OG1 THR A  10      -7.120 -20.266 -21.348  1.00 39.19           O  
ATOM     19  CG2 THR A  10      -5.276 -21.558 -20.455  1.00 36.14           C  
ATOM     20  N   ALA A  11      -3.664 -19.510 -18.588  1.00 24.38           N  
ATOM     21  CA  ALA A  11      -2.298 -19.714 -18.114  1.00 22.55           C  
ATOM     22  C   ALA A  11      -2.032 -21.234 -18.184  1.00 27.28           C  
ATOM     23  O   ALA A  11      -2.824 -22.017 -17.663  1.00 26.88           O  
ATOM     24  CB  ALA A  11      -2.189 -19.226 -16.699  1.00 22.11           C  
ATOM     25  N   HIS A  12      -0.979 -21.649 -18.882  1.00 24.28           N  
ATOM     26  CA  HIS A  12      -0.590 -23.079 -18.991  1.00 23.39           C  
ATOM     27  C   HIS A  12       0.735 -23.187 -18.271  1.00 24.01           C  
ATOM     28  O   HIS A  12       1.674 -22.511 -18.653  1.00 22.88           O  
ATOM     29  CB  HIS A  12      -0.287 -23.462 -20.445  1.00 24.57           C  
ATOM     30  CG  HIS A  12      -1.433 -23.259 -21.371  1.00 29.56           C  
ATOM     31  ND1 HIS A  12      -2.452 -24.183 -21.497  1.00 32.46           N  
ATOM     32  CD2 HIS A  12      -1.750 -22.224 -22.189  1.00 32.71           C  
ATOM     33  CE1 HIS A  12      -3.353 -23.725 -22.348  1.00 33.05           C  
ATOM     34  NE2 HIS A  12      -2.941 -22.546 -22.798  1.00 33.69           N  
ATOM     35  N   SER A  13       0.827 -24.044 -17.267  1.00 18.94           N  
ATOM     36  CA  SER A  13       2.082 -24.197 -16.551  1.00 19.01           C  
ATOM     37  C   SER A  13       2.340 -25.637 -16.203  1.00 23.16           C  
ATOM     38  O   SER A  13       1.423 -26.403 -16.013  1.00 23.20           O  
ATOM     39  CB  SER A  13       2.117 -23.352 -15.266  1.00 20.50           C  
ATOM     40  OG  SER A  13       0.954 -23.543 -14.499  1.00 23.85           O  
ATOM     41  N   ASP A  14       3.607 -25.959 -16.027  1.00 22.11           N  
ATOM     42  CA  ASP A  14       4.041 -27.299 -15.693  1.00 23.57           C  
ATOM     43  C   ASP A  14       5.206 -27.172 -14.733  1.00 23.42           C  
ATOM     44  O   ASP A  14       6.166 -26.469 -15.013  1.00 22.57           O  
ATOM     45  CB  ASP A  14       4.539 -27.979 -16.983  1.00 27.46           C  
ATOM     46  CG  ASP A  14       4.003 -29.348 -17.132  1.00 53.89           C  
ATOM     47  OD1 ASP A  14       4.594 -30.252 -16.499  1.00 59.06           O  
ATOM     48  OD2 ASP A  14       2.931 -29.494 -17.764  1.00 66.30           O  
ATOM     49  N   TYR A  15       5.107 -27.820 -13.589  1.00 18.20           N  
ATOM     50  CA  TYR A  15       6.176 -27.756 -12.583  1.00 18.44           C  
ATOM     51  C   TYR A  15       6.604 -29.167 -12.223  1.00 23.43           C  
ATOM     52  O   TYR A  15       5.796 -30.076 -12.108  1.00 22.84           O  
ATOM     53  CB  TYR A  15       5.731 -27.033 -11.300  1.00 19.44           C  
ATOM     54  CG  TYR A  15       4.869 -25.815 -11.534  1.00 22.82           C  
ATOM     55  CD1 TYR A  15       5.419 -24.641 -12.063  1.00 24.71           C  
ATOM     56  CD2 TYR A  15       3.501 -25.851 -11.301  1.00 23.08           C  
ATOM     57  CE1 TYR A  15       4.642 -23.520 -12.301  1.00 23.42           C  
ATOM     58  CE2 TYR A  15       2.707 -24.715 -11.543  1.00 24.32           C  
ATOM     59  CZ  TYR A  15       3.291 -23.558 -12.049  1.00 28.12           C  
ATOM     60  OH  TYR A  15       2.508 -22.449 -12.340  1.00 21.30           O  
ATOM     61  N   GLU A  16       7.880 -29.346 -11.991  1.00 23.17           N  
ATOM     62  CA  GLU A  16       8.366 -30.668 -11.634  1.00 24.40           C  
ATOM     63  C   GLU A  16       9.466 -30.562 -10.606  1.00 27.49           C  
ATOM     64  O   GLU A  16      10.355 -29.725 -10.742  1.00 26.44           O  
ATOM     65  CB  GLU A  16       8.888 -31.380 -12.872  1.00 25.87           C  
ATOM     66  CG  GLU A  16       9.623 -32.659 -12.535  1.00 43.56           C  
ATOM     67  CD  GLU A  16       9.984 -33.461 -13.765  1.00 67.06           C  
ATOM     68  OE1 GLU A  16       9.718 -32.986 -14.885  1.00 70.44           O  
ATOM     69  OE2 GLU A  16      10.473 -34.592 -13.604  1.00 67.65           O  
ATOM     70  N   ILE A  17       9.376 -31.389  -9.572  1.00 23.53           N  
ATOM     71  CA  ILE A  17      10.395 -31.458  -8.539  1.00 24.11           C  
ATOM     72  C   ILE A  17      10.830 -32.931  -8.424  1.00 27.52           C  
ATOM     73  O   ILE A  17       9.994 -33.813  -8.181  1.00 26.81           O  
ATOM     74  CB  ILE A  17       9.819 -31.010  -7.149  1.00 27.84           C  
ATOM     75  CG1 ILE A  17       9.009 -29.723  -7.289  1.00 28.28           C  
ATOM     76  CG2 ILE A  17      10.928 -30.936  -6.087  1.00 27.89           C  
ATOM     77  CD1 ILE A  17       8.391 -29.264  -6.015  1.00 35.62           C  
ATOM     78  N   VAL A  18      12.127 -33.188  -8.554  1.00 22.94           N  
ATOM     79  CA  VAL A  18      12.671 -34.529  -8.362  1.00 21.78           C  
ATOM     80  C   VAL A  18      13.546 -34.430  -7.110  1.00 27.57           C  
ATOM     81  O   VAL A  18      14.512 -33.669  -7.112  1.00 26.23           O  
ATOM     82  CB  VAL A  18      13.541 -34.952  -9.559  1.00 23.61           C  
ATOM     83  CG1 VAL A  18      14.164 -36.365  -9.305  1.00 21.37           C  
ATOM     84  CG2 VAL A  18      12.722 -34.922 -10.869  1.00 22.80           C  
ATOM     85  N   LEU A  19      13.198 -35.134  -6.034  1.00 27.06           N  
ATOM     86  CA  LEU A  19      14.016 -35.067  -4.811  1.00 29.09           C  
ATOM     87  C   LEU A  19      15.132 -36.125  -4.723  1.00 39.22           C  
ATOM     88  O   LEU A  19      14.955 -37.243  -5.206  1.00 38.49           O  
ATOM     89  CB  LEU A  19      13.130 -35.170  -3.571  1.00 28.48           C  
ATOM     90  CG  LEU A  19      12.087 -34.070  -3.454  1.00 33.24           C  
ATOM     91  CD1 LEU A  19      11.107 -34.402  -2.351  1.00 33.33           C  
ATOM     92  CD2 LEU A  19      12.785 -32.761  -3.170  1.00 35.52           C  
ATOM     93  N   GLU A  20      16.238 -35.783  -4.045  1.00 41.54           N  
ATOM     94  CA  GLU A  20      17.338 -36.730  -3.731  1.00 44.55           C  
ATOM     95  C   GLU A  20      17.081 -37.370  -2.351  1.00 56.40           C  
ATOM     96  O   GLU A  20      16.520 -36.722  -1.451  1.00 56.12           O  
ATOM     97  CB  GLU A  20      18.664 -36.001  -3.612  1.00 45.78           C  
ATOM     98  CG  GLU A  20      19.389 -35.836  -4.898  1.00 56.23           C  
ATOM     99  CD  GLU A  20      20.792 -35.276  -4.693  1.00 84.71           C  
ATOM    100  OE1 GLU A  20      21.409 -35.467  -3.602  1.00 48.81           O  
ATOM    101  OE2 GLU A  20      21.264 -34.612  -5.639  1.00 87.49           O  
ATOM    102  N   GLY A  21      17.567 -38.599  -2.160  1.00 57.44           N  
ATOM    103  CA  GLY A  21      17.357 -39.351  -0.909  1.00 58.53           C  
ATOM    104  C   GLY A  21      18.156 -38.926   0.324  1.00 66.00           C  
ATOM    105  O   GLY A  21      19.198 -38.281   0.217  1.00 66.66           O  
ATOM    106  N   GLY A  22      17.667 -39.325   1.499  1.00 63.67           N  
ATOM    107  CA  GLY A  22      18.300 -38.976   2.768  1.00 64.04           C  
ATOM    108  C   GLY A  22      17.858 -37.570   3.206  1.00 69.68           C  
ATOM    109  O   GLY A  22      16.940 -36.987   2.627  1.00 70.27           O  
ATOM    110  N   SER A  23      18.636 -36.959   4.093  1.00 65.59           N  
ATOM    111  N   SER A  24      20.050 -35.512   2.530  1.00 50.99           N  
ATOM    112  CA  SER A  24      20.195 -34.663   1.347  1.00 48.60           C  
ATOM    113  C   SER A  24      18.876 -33.923   1.104  1.00 47.48           C  
ATOM    114  O   SER A  24      17.784 -34.528   0.983  1.00 49.13           O  
ATOM    115  CB  SER A  24      20.576 -35.483   0.103  1.00 49.40           C  
ATOM    116  OG  SER A  24      20.613 -34.679  -1.068  1.00 51.96           O  
ATOM    117  N   SER A  25      18.991 -32.608   1.060  1.00 35.05           N  
ATOM    118  CA  SER A  25      17.865 -31.744   0.843  1.00 31.27           C  
ATOM    119  C   SER A  25      17.881 -31.317  -0.624  1.00 30.42           C  
ATOM    120  O   SER A  25      17.127 -30.457  -1.015  1.00 29.06           O  
ATOM    121  CB  SER A  25      18.061 -30.527   1.725  1.00 30.60           C  
ATOM    122  OG  SER A  25      19.297 -29.941   1.399  1.00 28.87           O  
ATOM    123  N   TRP A  26      18.758 -31.914  -1.435  1.00 26.21           N  
ATOM    124  CA  TRP A  26      18.869 -31.514  -2.845  1.00 25.48           C  
ATOM    125  C   TRP A  26      17.640 -31.835  -3.682  1.00 29.65           C  
ATOM    126  O   TRP A  26      16.946 -32.813  -3.436  1.00 29.09           O  
ATOM    127  CB  TRP A  26      20.083 -32.141  -3.525  1.00 23.06           C  
ATOM    128  CG  TRP A  26      21.422 -31.481  -3.180  1.00 23.16           C  
ATOM    129  CD1 TRP A  26      22.112 -31.581  -2.002  1.00 25.65           C  
ATOM    130  CD2 TRP A  26      22.257 -30.720  -4.070  1.00 22.21           C  
ATOM    131  NE1 TRP A  26      23.306 -30.884  -2.094  1.00 24.34           N  
ATOM    132  CE2 TRP A  26      23.427 -30.372  -3.355  1.00 24.92           C  
ATOM    133  CE3 TRP A  26      22.091 -30.236  -5.368  1.00 23.36           C  
ATOM    134  CZ2 TRP A  26      24.429 -29.600  -3.901  1.00 24.02           C  
ATOM    135  CZ3 TRP A  26      23.110 -29.485  -5.921  1.00 25.19           C  
ATOM    136  CH2 TRP A  26      24.263 -29.167  -5.185  1.00 25.53           C  
ATOM    137  N   GLY A  27      17.380 -31.017  -4.689  1.00 25.40           N  
ATOM    138  CA  GLY A  27      16.261 -31.267  -5.580  1.00 24.37           C  
ATOM    139  C   GLY A  27      16.552 -30.622  -6.922  1.00 27.45           C  
ATOM    140  O   GLY A  27      17.390 -29.711  -7.029  1.00 27.68           O  
ATOM    141  N   LYS A  28      15.923 -31.156  -7.956  1.00 23.79           N  
ATOM    142  CA  LYS A  28      15.965 -30.595  -9.302  1.00 24.29           C  
ATOM    143  C   LYS A  28      14.588 -29.963  -9.501  1.00 28.70           C  
ATOM    144  O   LYS A  28      13.556 -30.594  -9.255  1.00 26.90           O  
ATOM    145  CB  LYS A  28      16.117 -31.681 -10.367  1.00 27.21           C  
ATOM    146  CG  LYS A  28      17.520 -32.249 -10.495  1.00 36.98           C  
ATOM    147  CD  LYS A  28      17.598 -33.179 -11.694  1.00 47.98           C  
ATOM    148  CE  LYS A  28      18.230 -34.510 -11.336  1.00 67.00           C  
ATOM    149  NZ  LYS A  28      19.667 -34.365 -10.966  1.00 86.83           N  
ATOM    150  N   VAL A  29      14.566 -28.728  -9.984  1.00 25.63           N  
ATOM    151  CA  VAL A  29      13.299 -28.036 -10.205  1.00 23.67           C  
ATOM    152  C   VAL A  29      13.217 -27.617 -11.662  1.00 25.91           C  
ATOM    153  O   VAL A  29      14.155 -27.053 -12.213  1.00 25.51           O  
ATOM    154  CB  VAL A  29      13.164 -26.798  -9.249  1.00 26.27           C  
ATOM    155  CG1 VAL A  29      11.862 -26.021  -9.528  1.00 26.53           C  
ATOM    156  CG2 VAL A  29      13.233 -27.228  -7.800  1.00 24.44           C  
ATOM    157  N   LYS A  30      12.089 -27.907 -12.287  1.00 22.58           N  
ATOM    158  CA  LYS A  30      11.849 -27.495 -13.655  1.00 23.36           C  
ATOM    159  C   LYS A  30      10.477 -26.813 -13.659  1.00 27.01           C  
ATOM    160  O   LYS A  30       9.537 -27.306 -13.028  1.00 26.08           O  
ATOM    161  CB  LYS A  30      11.792 -28.703 -14.614  1.00 26.82           C  
ATOM    162  CG  LYS A  30      13.141 -29.261 -15.058  1.00 51.67           C  
ATOM    163  N   ALA A  31      10.352 -25.719 -14.421  1.00 22.83           N  
ATOM    164  CA  ALA A  31       9.085 -24.999 -14.561  1.00 21.35           C  
ATOM    165  C   ALA A  31       8.969 -24.408 -15.943  1.00 24.68           C  
ATOM    166  O   ALA A  31       9.956 -23.844 -16.458  1.00 24.11           O  
ATOM    167  CB  ALA A  31       8.996 -23.881 -13.534  1.00 21.49           C  
ATOM    168  N   ARG A  32       7.768 -24.506 -16.528  1.00 20.52           N  
ATOM    169  CA  ARG A  32       7.441 -23.871 -17.810  1.00 20.76           C  
ATOM    170  C   ARG A  32       6.118 -23.175 -17.623  1.00 24.89           C  
ATOM    171  O   ARG A  32       5.184 -23.724 -17.015  1.00 24.44           O  
ATOM    172  CB  ARG A  32       7.283 -24.885 -18.959  1.00 22.93           C  
ATOM    173  CG  ARG A  32       8.362 -25.967 -19.022  1.00 42.13           C  
ATOM    174  CD  ARG A  32       9.544 -25.604 -19.936  1.00 48.09           C  
ATOM    175  N   ALA A  33       5.984 -21.984 -18.177  1.00 20.47           N  
ATOM    176  CA  ALA A  33       4.706 -21.287 -18.049  1.00 20.12           C  
ATOM    177  C   ALA A  33       4.475 -20.341 -19.190  1.00 25.11           C  
ATOM    178  O   ALA A  33       5.401 -19.666 -19.661  1.00 23.69           O  
ATOM    179  CB  ALA A  33       4.636 -20.506 -16.716  1.00 20.75           C  
ATOM    180  N   LYS A  34       3.223 -20.244 -19.607  1.00 23.79           N  
ATOM    181  CA  LYS A  34       2.894 -19.312 -20.669  1.00 24.71           C  
ATOM    182  C   LYS A  34       1.506 -18.749 -20.471  1.00 27.27           C  
ATOM    183  O   LYS A  34       0.591 -19.471 -20.116  1.00 28.61           O  
ATOM    184  CB  LYS A  34       3.137 -19.922 -22.069  1.00 28.01           C  
ATOM    185  CG  LYS A  34       1.938 -20.420 -22.827  1.00 46.79           C  
ATOM    186  N   VAL A  35       1.378 -17.439 -20.592  1.00 22.00           N  
ATOM    187  CA  VAL A  35       0.078 -16.799 -20.434  1.00 21.71           C  
ATOM    188  C   VAL A  35      -0.083 -15.719 -21.483  1.00 23.29           C  
ATOM    189  O   VAL A  35       0.829 -14.956 -21.740  1.00 22.69           O  
ATOM    190  CB  VAL A  35      -0.195 -16.246 -18.988  1.00 24.44           C  
ATOM    191  CG1 VAL A  35       0.780 -15.183 -18.615  1.00 24.16           C  
ATOM    192  CG2 VAL A  35      -1.616 -15.676 -18.894  1.00 23.53           C  
ATOM    193  N   ASN A  36      -1.240 -15.686 -22.110  1.00 19.05           N  
ATOM    194  CA  ASN A  36      -1.495 -14.693 -23.127  1.00 20.49           C  
ATOM    195  C   ASN A  36      -2.147 -13.435 -22.548  1.00 25.63           C  
ATOM    196  O   ASN A  36      -3.272 -13.093 -22.874  1.00 26.24           O  
ATOM    197  CB  ASN A  36      -2.325 -15.285 -24.278  1.00 22.57           C  
ATOM    198  CG  ASN A  36      -3.671 -15.834 -23.821  1.00 43.60           C  
ATOM    199  OD1 ASN A  36      -3.842 -16.282 -22.674  1.00 39.59           O  
ATOM    200  ND2 ASN A  36      -4.655 -15.767 -24.717  1.00 35.22           N  
ATOM    201  N   ALA A  37      -1.447 -12.761 -21.656  1.00 21.69           N  
ATOM    202  CA  ALA A  37      -1.965 -11.532 -21.064  1.00 20.73           C  
ATOM    203  C   ALA A  37      -0.753 -10.630 -21.081  1.00 23.12           C  
ATOM    204  O   ALA A  37       0.385 -11.125 -21.041  1.00 21.73           O  
ATOM    205  CB  ALA A  37      -2.448 -11.765 -19.624  1.00 21.33           C  
ATOM    206  N   PRO A  38      -0.968  -9.322 -21.229  1.00 18.98           N  
ATOM    207  CA  PRO A  38       0.178  -8.410 -21.300  1.00 19.60           C  
ATOM    208  C   PRO A  38       0.856  -8.194 -19.921  1.00 22.99           C  
ATOM    209  O   PRO A  38       0.215  -8.171 -18.894  1.00 20.36           O  
ATOM    210  CB  PRO A  38      -0.452  -7.100 -21.777  1.00 19.98           C  
ATOM    211  CG  PRO A  38      -1.884  -7.193 -21.379  1.00 23.03           C  
ATOM    212  CD  PRO A  38      -2.248  -8.623 -21.455  1.00 18.63           C  
ATOM    213  N   PRO A  39       2.165  -8.022 -19.930  1.00 20.99           N  
ATOM    214  CA  PRO A  39       2.909  -7.739 -18.710  1.00 19.28           C  
ATOM    215  C   PRO A  39       2.676  -6.278 -18.335  1.00 22.13           C  
ATOM    216  O   PRO A  39       2.330  -5.447 -19.175  1.00 21.37           O  
ATOM    217  CB  PRO A  39       4.361  -7.945 -19.138  1.00 20.83           C  
ATOM    218  CG  PRO A  39       4.346  -7.709 -20.613  1.00 25.47           C  
ATOM    219  CD  PRO A  39       3.037  -8.184 -21.106  1.00 21.54           C  
ATOM    220  N   ALA A  40       2.841  -5.962 -17.060  1.00 18.43           N  
ATOM    221  CA  ALA A  40       2.623  -4.608 -16.581  1.00 17.10           C  
ATOM    222  C   ALA A  40       3.895  -3.774 -16.715  1.00 22.08           C  
ATOM    223  O   ALA A  40       4.295  -3.110 -15.793  1.00 23.16           O  
ATOM    224  CB  ALA A  40       2.190  -4.658 -15.134  1.00 18.08           C  
ATOM    225  N   SER A  41       4.580  -3.846 -17.844  1.00 19.07           N  
ATOM    226  CA  SER A  41       5.791  -3.049 -18.020  1.00 17.34           C  
ATOM    227  C   SER A  41       5.466  -1.919 -18.964  1.00 19.56           C  
ATOM    228  O   SER A  41       4.862  -2.152 -20.001  1.00 19.79           O  
ATOM    229  CB  SER A  41       6.949  -3.871 -18.594  1.00 19.27           C  
ATOM    230  OG  SER A  41       8.029  -2.999 -18.888  1.00 23.03           O  
ATOM    231  N   PRO A  42       5.820  -0.692 -18.590  1.00 15.67           N  
ATOM    232  CA  PRO A  42       5.498   0.451 -19.425  1.00 15.37           C  
ATOM    233  C   PRO A  42       6.413   0.561 -20.650  1.00 19.70           C  
ATOM    234  O   PRO A  42       6.202   1.443 -21.474  1.00 17.11           O  
ATOM    235  CB  PRO A  42       5.663   1.661 -18.488  1.00 16.35           C  
ATOM    236  CG  PRO A  42       6.495   1.196 -17.356  1.00 19.91           C  
ATOM    237  CD  PRO A  42       6.303  -0.296 -17.255  1.00 15.95           C  
ATOM    238  N   LEU A  43       7.404  -0.340 -20.756  1.00 16.58           N  
ATOM    239  CA  LEU A  43       8.273  -0.486 -21.955  1.00 16.34           C  
ATOM    240  C   LEU A  43       8.266  -1.945 -22.407  1.00 21.78           C  
ATOM    241  O   LEU A  43       8.556  -2.853 -21.622  1.00 23.39           O  
ATOM    242  CB  LEU A  43       9.730  -0.044 -21.674  1.00 16.22           C  
ATOM    243  CG  LEU A  43       9.959   1.470 -21.568  1.00 18.75           C  
ATOM    244  CD1 LEU A  43      11.344   1.797 -21.119  1.00 18.15           C  
ATOM    245  CD2 LEU A  43       9.599   2.188 -22.864  1.00 17.77           C  
ATOM    246  N   LEU A  44       7.865  -2.175 -23.643  1.00 19.61           N  
ATOM    247  CA  LEU A  44       7.776  -3.527 -24.207  1.00 20.40           C  
ATOM    248  C   LEU A  44       8.439  -3.420 -25.575  1.00 25.17           C  
ATOM    249  O   LEU A  44       8.475  -2.341 -26.146  1.00 25.83           O  
ATOM    250  CB  LEU A  44       6.287  -3.952 -24.362  1.00 20.37           C  
ATOM    251  CG  LEU A  44       5.571  -4.324 -23.042  1.00 22.94           C  
ATOM    252  CD1 LEU A  44       4.106  -4.640 -23.217  1.00 21.16           C  
ATOM    253  CD2 LEU A  44       6.307  -5.462 -22.317  1.00 21.14           C  
ATOM    254  N   PRO A  45       9.000  -4.510 -26.085  1.00 20.94           N  
ATOM    255  CA  PRO A  45       9.021  -5.806 -25.389  1.00 19.67           C  
ATOM    256  C   PRO A  45      10.134  -5.854 -24.339  1.00 22.95           C  
ATOM    257  O   PRO A  45      10.991  -4.979 -24.291  1.00 21.66           O  
ATOM    258  CB  PRO A  45       9.345  -6.825 -26.512  1.00 21.72           C  
ATOM    259  CG  PRO A  45       9.807  -6.010 -27.702  1.00 24.64           C  
ATOM    260  CD  PRO A  45       9.243  -4.613 -27.541  1.00 19.73           C  
ATOM    261  N   ALA A  46      10.120  -6.909 -23.525  1.00 19.44           N  
ATOM    262  CA  ALA A  46      11.099  -7.125 -22.475  1.00 18.88           C  
ATOM    263  C   ALA A  46      11.385  -8.618 -22.355  1.00 25.01           C  
ATOM    264  O   ALA A  46      10.485  -9.399 -22.047  1.00 25.97           O  
ATOM    265  CB  ALA A  46      10.589  -6.570 -21.119  1.00 19.38           C  
ATOM    266  N   ASP A  47      12.634  -9.000 -22.632  1.00 21.75           N  
ATOM    267  CA  ASP A  47      13.105 -10.381 -22.554  1.00 20.37           C  
ATOM    268  C   ASP A  47      14.250 -10.385 -21.558  1.00 23.56           C  
ATOM    269  O   ASP A  47      15.051  -9.448 -21.522  1.00 23.50           O  
ATOM    270  CB  ASP A  47      13.700 -10.839 -23.914  1.00 21.48           C  
ATOM    271  CG  ASP A  47      12.707 -10.769 -25.056  1.00 29.68           C  
ATOM    272  OD1 ASP A  47      11.494 -10.813 -24.825  1.00 29.64           O  
ATOM    273  OD2 ASP A  47      13.143 -10.608 -26.205  1.00 44.67           O  
ATOM    274  N   CYS A  48      14.403 -11.473 -20.824  1.00 21.16           N  
ATOM    275  CA  CYS A  48      15.525 -11.557 -19.894  1.00 21.68           C  
ATOM    276  C   CYS A  48      15.949 -13.007 -19.712  1.00 26.53           C  
ATOM    277  O   CYS A  48      15.090 -13.890 -19.700  1.00 26.30           O  
ATOM    278  CB  CYS A  48      15.091 -10.980 -18.540  1.00 22.15           C  
ATOM    279  SG  CYS A  48      16.379 -10.885 -17.272  1.00 25.90           S  
ATOM    280  N   ASP A  49      17.259 -13.229 -19.558  1.00 23.17           N  
ATOM    281  CA  ASP A  49      17.863 -14.535 -19.233  1.00 22.38           C  
ATOM    282  C   ASP A  49      18.708 -14.349 -17.990  1.00 25.00           C  
ATOM    283  O   ASP A  49      19.396 -13.321 -17.813  1.00 24.55           O  
ATOM    284  CB  ASP A  49      18.781 -15.024 -20.359  1.00 25.91           C  
ATOM    285  CG  ASP A  49      18.021 -15.375 -21.611  1.00 42.04           C  
ATOM    286  OD1 ASP A  49      18.471 -14.971 -22.705  1.00 46.30           O  
ATOM    287  OD2 ASP A  49      16.963 -16.027 -21.500  1.00 45.74           O  
ATOM    288  N   VAL A  50      18.660 -15.348 -17.121  1.00 20.69           N  
ATOM    289  CA  VAL A  50      19.407 -15.349 -15.882  1.00 19.97           C  
ATOM    290  C   VAL A  50      20.110 -16.671 -15.728  1.00 25.56           C  
ATOM    291  O   VAL A  50      19.557 -17.747 -16.065  1.00 24.99           O  
ATOM    292  CB  VAL A  50      18.473 -15.172 -14.695  1.00 24.28           C  
ATOM    293  CG1 VAL A  50      19.279 -14.827 -13.417  1.00 22.79           C  
ATOM    294  CG2 VAL A  50      17.439 -14.103 -15.041  1.00 25.15           C  
ATOM    295  N   LYS A  51      21.316 -16.594 -15.186  1.00 22.45           N  
ATOM    296  CA  LYS A  51      22.111 -17.778 -14.957  1.00 23.15           C  
ATOM    297  C   LYS A  51      22.799 -17.538 -13.626  1.00 27.07           C  
ATOM    298  O   LYS A  51      23.366 -16.460 -13.397  1.00 26.25           O  
ATOM    299  CB  LYS A  51      23.116 -17.975 -16.115  1.00 26.43           C  
ATOM    300  CG  LYS A  51      23.623 -19.391 -16.309  1.00 49.10           C  
ATOM    301  N   LEU A  52      22.628 -18.497 -12.721  1.00 24.24           N  
ATOM    302  CA  LEU A  52      23.237 -18.491 -11.392  1.00 24.68           C  
ATOM    303  C   LEU A  52      23.995 -19.791 -11.179  1.00 27.78           C  
ATOM    304  O   LEU A  52      23.495 -20.876 -11.535  1.00 26.83           O  
ATOM    305  CB  LEU A  52      22.174 -18.362 -10.302  1.00 25.23           C  
ATOM    306  CG  LEU A  52      21.272 -17.128 -10.363  1.00 31.62           C  
ATOM    307  CD1 LEU A  52      20.242 -17.258  -9.263  1.00 33.22           C  
ATOM    308  CD2 LEU A  52      22.092 -15.854 -10.145  1.00 34.57           C  
ATOM    309  N   ASN A  53      25.165 -19.693 -10.546  1.00 23.77           N  
ATOM    310  CA  ASN A  53      26.006 -20.857 -10.288  1.00 23.75           C  
ATOM    311  C   ASN A  53      26.645 -20.628  -8.947  1.00 26.92           C  
ATOM    312  O   ASN A  53      27.061 -19.501  -8.640  1.00 26.23           O  
ATOM    313  CB  ASN A  53      27.162 -20.918 -11.313  1.00 26.03           C  
ATOM    314  CG  ASN A  53      26.690 -21.229 -12.723  1.00 62.53           C  
ATOM    315  OD1 ASN A  53      26.465 -20.324 -13.525  1.00 64.69           O  
ATOM    316  ND2 ASN A  53      26.585 -22.514 -13.047  1.00 54.56           N  
ATOM    317  N   VAL A  54      26.815 -21.698  -8.182  1.00 21.82           N  
ATOM    318  CA  VAL A  54      27.549 -21.573  -6.914  1.00 21.56           C  
ATOM    319  C   VAL A  54      28.377 -22.838  -6.689  1.00 28.26           C  
ATOM    320  O   VAL A  54      27.943 -23.950  -7.037  1.00 28.44           O  
ATOM    321  CB  VAL A  54      26.642 -21.245  -5.712  1.00 23.28           C  
ATOM    322  CG1 VAL A  54      25.660 -22.415  -5.404  1.00 21.47           C  
ATOM    323  CG2 VAL A  54      27.495 -20.901  -4.503  1.00 22.99           C  
ATOM    324  N   LYS A  55      29.574 -22.671  -6.135  1.00 26.93           N  
ATOM    325  CA  LYS A  55      30.453 -23.821  -5.893  1.00 27.52           C  
ATOM    326  C   LYS A  55      31.201 -23.688  -4.593  1.00 31.62           C  
ATOM    327  O   LYS A  55      31.516 -22.571  -4.164  1.00 29.41           O  
ATOM    328  CB  LYS A  55      31.438 -24.032  -7.053  1.00 29.66           C  
ATOM    329  CG  LYS A  55      32.544 -23.016  -7.115  1.00 37.79           C  
ATOM    330  CD  LYS A  55      33.094 -22.888  -8.521  1.00 44.80           C  
ATOM    331  N   PRO A  56      31.422 -24.836  -3.944  1.00 29.67           N  
ATOM    332  CA  PRO A  56      32.143 -24.884  -2.670  1.00 29.89           C  
ATOM    333  C   PRO A  56      33.544 -24.351  -2.931  1.00 37.65           C  
ATOM    334  O   PRO A  56      34.166 -24.695  -3.903  1.00 37.24           O  
ATOM    335  CB  PRO A  56      32.198 -26.385  -2.350  1.00 30.94           C  
ATOM    336  CG  PRO A  56      31.174 -27.029  -3.237  1.00 34.43           C  
ATOM    337  CD  PRO A  56      31.122 -26.183  -4.467  1.00 29.89           C  
ATOM    338  N   LEU A  57      33.999 -23.447  -2.095  1.00 39.82           N  
ATOM    339  CA  LEU A  57      35.296 -22.814  -2.268  1.00 42.02           C  
ATOM    340  C   LEU A  57      36.210 -23.424  -1.229  1.00 52.16           C  
ATOM    341  O   LEU A  57      37.133 -24.148  -1.560  1.00 52.45           O  
ATOM    342  CB  LEU A  57      35.177 -21.305  -2.012  1.00 41.90           C  
ATOM    343  CG  LEU A  57      36.143 -20.404  -2.778  1.00 46.63           C  
ATOM    344  CD1 LEU A  57      36.109 -20.743  -4.253  1.00 47.20           C  
ATOM    345  CD2 LEU A  57      35.808 -18.947  -2.544  1.00 47.21           C  
ATOM    346  N   ASP A  58      35.914 -23.160   0.037  1.00 53.79           N  
ATOM    347  CA  ASP A  58      36.699 -23.684   1.152  1.00 55.59           C  
ATOM    348  C   ASP A  58      35.756 -24.059   2.289  1.00 60.93           C  
ATOM    349  O   ASP A  58      35.448 -23.241   3.148  1.00 60.66           O  
ATOM    350  CB  ASP A  58      37.730 -22.641   1.614  1.00 58.29           C  
ATOM    351  CG  ASP A  58      38.336 -22.966   2.973  1.00 73.21           C  
ATOM    352  OD1 ASP A  58      38.292 -24.147   3.384  1.00 73.66           O  
ATOM    353  OD2 ASP A  58      38.865 -22.036   3.626  1.00 81.26           O  
ATOM    354  N   PRO A  59      35.303 -25.306   2.283  1.00 59.45           N  
ATOM    355  CA  PRO A  59      34.368 -25.802   3.290  1.00 59.76           C  
ATOM    356  C   PRO A  59      34.828 -25.652   4.738  1.00 65.24           C  
ATOM    357  O   PRO A  59      33.994 -25.655   5.650  1.00 65.29           O  
ATOM    358  CB  PRO A  59      34.208 -27.270   2.916  1.00 61.36           C  
ATOM    359  CG  PRO A  59      34.426 -27.307   1.438  1.00 65.35           C  
ATOM    360  CD  PRO A  59      35.341 -26.165   1.083  1.00 60.92           C  
ATOM    361  N   ALA A  60      36.138 -25.518   4.951  1.00 62.09           N  
ATOM    362  CA  ALA A  60      36.682 -25.344   6.306  1.00 62.02           C  
ATOM    363  C   ALA A  60      36.254 -24.006   6.919  1.00 64.20           C  
ATOM    364  O   ALA A  60      35.906 -23.927   8.098  1.00 63.93           O  
ATOM    365  CB  ALA A  60      38.215 -25.465   6.305  1.00 62.76           C  
ATOM    366  N   LYS A  61      36.290 -22.955   6.110  1.00 58.40           N  
ATOM    367  CA  LYS A  61      35.886 -21.641   6.583  1.00 57.04           C  
ATOM    368  C   LYS A  61      34.467 -21.268   6.135  1.00 55.74           C  
ATOM    369  O   LYS A  61      34.001 -20.159   6.419  1.00 55.79           O  
ATOM    370  CB  LYS A  61      36.918 -20.569   6.217  1.00 59.95           C  
ATOM    371  CG  LYS A  61      36.988 -20.250   4.739  1.00 80.92           C  
ATOM    372  N   GLY A  62      33.780 -22.217   5.487  1.00 46.76           N  
ATOM    373  CA  GLY A  62      32.402 -22.045   5.015  1.00 44.14           C  
ATOM    374  C   GLY A  62      32.209 -21.147   3.775  1.00 43.69           C  
ATOM    375  O   GLY A  62      31.107 -20.662   3.527  1.00 42.31           O  
ATOM    376  N   PHE A  63      33.269 -20.921   3.004  1.00 36.47           N  
ATOM    377  CA  PHE A  63      33.183 -20.073   1.820  1.00 34.58           C  
ATOM    378  C   PHE A  63      32.620 -20.766   0.585  1.00 35.35           C  
ATOM    379  O   PHE A  63      32.994 -21.899   0.264  1.00 34.83           O  
ATOM    380  CB  PHE A  63      34.549 -19.458   1.465  1.00 36.12           C  
ATOM    381  CG  PHE A  63      34.789 -18.102   2.070  1.00 37.18           C  
ATOM    382  CD1 PHE A  63      34.351 -16.960   1.435  1.00 40.33           C  
ATOM    383  CD2 PHE A  63      35.447 -17.970   3.292  1.00 39.23           C  
ATOM    384  CE1 PHE A  63      34.556 -15.702   2.009  1.00 41.09           C  
ATOM    385  CE2 PHE A  63      35.659 -16.723   3.871  1.00 41.21           C  
ATOM    386  CZ  PHE A  63      35.231 -15.592   3.220  1.00 39.32           C  
ATOM    387  N   VAL A  64      31.778 -20.046  -0.159  1.00 28.27           N  
ATOM    388  CA  VAL A  64      31.256 -20.542  -1.441  1.00 25.34           C  
ATOM    389  C   VAL A  64      31.469 -19.410  -2.442  1.00 28.77           C  
ATOM    390  O   VAL A  64      31.565 -18.227  -2.062  1.00 27.13           O  
ATOM    391  CB  VAL A  64      29.752 -20.975  -1.378  1.00 27.22           C  
ATOM    392  CG1 VAL A  64      29.496 -21.990  -0.254  1.00 25.67           C  
ATOM    393  CG2 VAL A  64      28.823 -19.755  -1.240  1.00 26.94           C  
ATOM    394  N   ARG A  65      31.604 -19.761  -3.715  1.00 26.29           N  
ATOM    395  CA  ARG A  65      31.790 -18.740  -4.722  1.00 27.39           C  
ATOM    396  C   ARG A  65      30.519 -18.699  -5.568  1.00 31.09           C  
ATOM    397  O   ARG A  65      30.144 -19.694  -6.175  1.00 29.54           O  
ATOM    398  CB  ARG A  65      33.006 -19.041  -5.615  1.00 29.78           C  
ATOM    399  CG  ARG A  65      33.033 -18.130  -6.831  1.00 38.16           C  
ATOM    400  CD  ARG A  65      34.425 -17.809  -7.336  1.00 46.04           C  
ATOM    401  NE  ARG A  65      35.316 -17.346  -6.282  1.00 52.86           N  
ATOM    402  CZ  ARG A  65      36.624 -17.588  -6.258  1.00 68.31           C  
ATOM    403  NH1 ARG A  65      37.180 -18.300  -7.228  1.00 60.56           N  
ATOM    404  NH2 ARG A  65      37.373 -17.126  -5.263  1.00 48.30           N  
ATOM    405  N   ILE A  66      29.851 -17.558  -5.613  1.00 28.61           N  
ATOM    406  CA  ILE A  66      28.610 -17.476  -6.380  1.00 28.71           C  
ATOM    407  C   ILE A  66      28.788 -16.582  -7.577  1.00 31.31           C  
ATOM    408  O   ILE A  66      29.487 -15.581  -7.521  1.00 31.75           O  
ATOM    409  CB  ILE A  66      27.415 -17.047  -5.487  1.00 32.68           C  
ATOM    410  CG1 ILE A  66      26.096 -17.069  -6.245  1.00 33.55           C  
ATOM    411  CG2 ILE A  66      27.617 -15.693  -4.889  1.00 35.14           C  
ATOM    412  CD1 ILE A  66      24.887 -17.237  -5.265  1.00 38.70           C  
ATOM    413  N   SER A  67      28.191 -16.956  -8.689  1.00 26.84           N  
ATOM    414  CA  SER A  67      28.276 -16.105  -9.845  1.00 27.32           C  
ATOM    415  C   SER A  67      26.914 -15.957 -10.503  1.00 33.26           C  
ATOM    416  O   SER A  67      26.119 -16.915 -10.577  1.00 33.36           O  
ATOM    417  CB  SER A  67      29.364 -16.554 -10.816  1.00 31.17           C  
ATOM    418  OG  SER A  67      28.935 -17.651 -11.559  1.00 44.38           O  
ATOM    419  N   ALA A  68      26.610 -14.728 -10.918  1.00 28.15           N  
ATOM    420  CA  ALA A  68      25.328 -14.447 -11.529  1.00 26.86           C  
ATOM    421  C   ALA A  68      25.505 -13.639 -12.794  1.00 29.63           C  
ATOM    422  O   ALA A  68      26.320 -12.728 -12.843  1.00 30.26           O  
ATOM    423  CB  ALA A  68      24.433 -13.670 -10.528  1.00 27.48           C  
ATOM    424  N   VAL A  69      24.692 -13.928 -13.795  1.00 24.70           N  
ATOM    425  CA  VAL A  69      24.679 -13.152 -15.020  1.00 24.57           C  
ATOM    426  C   VAL A  69      23.218 -12.840 -15.344  1.00 27.97           C  
ATOM    427  O   VAL A  69      22.394 -13.743 -15.378  1.00 26.83           O  
ATOM    428  CB  VAL A  69      25.279 -13.946 -16.206  1.00 29.46           C  
ATOM    429  CG1 VAL A  69      25.262 -13.089 -17.484  1.00 28.59           C  
ATOM    430  CG2 VAL A  69      26.668 -14.392 -15.888  1.00 29.54           C  
ATOM    431  N   PHE A  70      22.912 -11.568 -15.594  1.00 25.08           N  
ATOM    432  CA  PHE A  70      21.561 -11.152 -15.986  1.00 24.27           C  
ATOM    433  C   PHE A  70      21.685 -10.499 -17.348  1.00 29.64           C  
ATOM    434  O   PHE A  70      22.514  -9.622 -17.533  1.00 30.61           O  
ATOM    435  CB  PHE A  70      21.014 -10.096 -15.020  1.00 25.02           C  
ATOM    436  CG  PHE A  70      20.787 -10.603 -13.636  1.00 26.11           C  
ATOM    437  CD1 PHE A  70      19.517 -11.014 -13.229  1.00 30.69           C  
ATOM    438  CD2 PHE A  70      21.833 -10.713 -12.748  1.00 27.44           C  
ATOM    439  CE1 PHE A  70      19.301 -11.521 -11.937  1.00 30.82           C  
ATOM    440  CE2 PHE A  70      21.618 -11.195 -11.450  1.00 30.12           C  
ATOM    441  CZ  PHE A  70      20.345 -11.584 -11.048  1.00 27.99           C  
ATOM    442  N   GLU A  71      20.877 -10.919 -18.308  1.00 24.15           N  
ATOM    443  CA  GLU A  71      20.945 -10.292 -19.623  1.00 24.48           C  
ATOM    444  C   GLU A  71      19.538 -10.004 -20.105  1.00 25.87           C  
ATOM    445  O   GLU A  71      18.691 -10.893 -20.103  1.00 24.68           O  
ATOM    446  CB  GLU A  71      21.593 -11.221 -20.633  1.00 26.13           C  
ATOM    447  CG  GLU A  71      23.046 -10.999 -20.812  1.00 46.11           C  
ATOM    448  CD  GLU A  71      23.610 -11.913 -21.870  1.00 73.40           C  
ATOM    449  OE1 GLU A  71      23.888 -13.081 -21.536  1.00 58.08           O  
ATOM    450  OE2 GLU A  71      23.667 -11.493 -23.045  1.00 73.61           O  
ATOM    451  N   SER A  72      19.292  -8.796 -20.583  1.00 21.81           N  
ATOM    452  CA  SER A  72      17.951  -8.497 -21.043  1.00 21.95           C  
ATOM    453  C   SER A  72      17.905  -7.553 -22.223  1.00 25.38           C  
ATOM    454  O   SER A  72      18.880  -6.897 -22.537  1.00 24.73           O  
ATOM    455  CB  SER A  72      17.115  -7.927 -19.888  1.00 23.57           C  
ATOM    456  OG  SER A  72      17.662  -6.712 -19.388  1.00 26.84           O  
ATOM    457  N   ILE A  73      16.745  -7.478 -22.863  1.00 21.96           N  
ATOM    458  CA  ILE A  73      16.531  -6.525 -23.952  1.00 22.50           C  
ATOM    459  C   ILE A  73      15.226  -5.831 -23.610  1.00 25.59           C  
ATOM    460  O   ILE A  73      14.202  -6.482 -23.420  1.00 26.37           O  
ATOM    461  CB  ILE A  73      16.469  -7.188 -25.343  1.00 26.13           C  
ATOM    462  CG1 ILE A  73      17.790  -7.894 -25.620  1.00 28.54           C  
ATOM    463  CG2 ILE A  73      16.303  -6.125 -26.412  1.00 26.45           C  
ATOM    464  CD1 ILE A  73      18.016  -8.214 -27.083  1.00 46.52           C  
ATOM    465  N   VAL A  74      15.278  -4.523 -23.424  1.00 20.08           N  
ATOM    466  CA  VAL A  74      14.070  -3.788 -23.083  1.00 20.10           C  
ATOM    467  C   VAL A  74      13.849  -2.681 -24.121  1.00 23.13           C  
ATOM    468  O   VAL A  74      14.653  -1.759 -24.251  1.00 21.65           O  
ATOM    469  CB  VAL A  74      14.150  -3.216 -21.647  1.00 23.31           C  
ATOM    470  CG1 VAL A  74      12.863  -2.429 -21.318  1.00 22.21           C  
ATOM    471  CG2 VAL A  74      14.408  -4.340 -20.666  1.00 23.16           C  
ATOM    472  N   ASP A  75      12.761  -2.776 -24.863  1.00 21.16           N  
ATOM    473  CA  ASP A  75      12.480  -1.791 -25.916  1.00 21.25           C  
ATOM    474  C   ASP A  75      13.700  -1.598 -26.801  1.00 25.19           C  
ATOM    475  O   ASP A  75      14.095  -0.472 -27.057  1.00 24.99           O  
ATOM    476  CB  ASP A  75      12.082  -0.437 -25.316  1.00 22.47           C  
ATOM    477  CG  ASP A  75      11.416   0.491 -26.340  1.00 30.53           C  
ATOM    478  OD1 ASP A  75      10.920  -0.032 -27.352  1.00 32.81           O  
ATOM    479  OD2 ASP A  75      11.370   1.731 -26.130  1.00 28.74           O  
ATOM    480  N   SER A  76      14.353  -2.684 -27.179  1.00 24.73           N  
ATOM    481  CA  SER A  76      15.568  -2.594 -28.012  1.00 27.23           C  
ATOM    482  C   SER A  76      16.905  -2.209 -27.337  1.00 33.37           C  
ATOM    483  O   SER A  76      17.940  -2.306 -27.989  1.00 35.73           O  
ATOM    484  CB  SER A  76      15.356  -1.737 -29.269  1.00 31.85           C  
ATOM    485  OG  SER A  76      15.761  -0.400 -29.001  1.00 43.91           O  
ATOM    486  N   THR A  77      16.904  -1.847 -26.044  1.00 27.52           N  
ATOM    487  CA  THR A  77      18.150  -1.558 -25.315  1.00 26.71           C  
ATOM    488  C   THR A  77      18.678  -2.874 -24.701  1.00 31.71           C  
ATOM    489  O   THR A  77      17.935  -3.571 -24.024  1.00 31.84           O  
ATOM    490  CB  THR A  77      17.909  -0.509 -24.198  1.00 31.78           C  
ATOM    491  OG1 THR A  77      17.382   0.679 -24.765  1.00 30.92           O  
ATOM    492  CG2 THR A  77      19.173  -0.163 -23.438  1.00 25.85           C  
ATOM    493  N   LYS A  78      19.943  -3.212 -24.951  1.00 27.84           N  
ATOM    494  CA  LYS A  78      20.548  -4.411 -24.382  1.00 28.32           C  
ATOM    495  C   LYS A  78      21.205  -4.063 -23.047  1.00 28.62           C  
ATOM    496  O   LYS A  78      21.988  -3.103 -22.967  1.00 25.60           O  
ATOM    497  CB  LYS A  78      21.639  -4.993 -25.310  1.00 32.20           C  
ATOM    498  CG  LYS A  78      21.121  -5.498 -26.647  1.00 51.64           C  
ATOM    499  CD  LYS A  78      22.094  -6.477 -27.279  1.00 70.69           C  
ATOM    500  N   ASN A  79      20.887  -4.840 -22.012  1.00 23.91           N  
ATOM    501  CA  ASN A  79      21.451  -4.587 -20.689  1.00 23.61           C  
ATOM    502  C   ASN A  79      22.097  -5.861 -20.203  1.00 26.93           C  
ATOM    503  O   ASN A  79      21.710  -6.957 -20.621  1.00 26.09           O  
ATOM    504  CB  ASN A  79      20.375  -4.164 -19.685  1.00 21.42           C  
ATOM    505  CG  ASN A  79      19.322  -3.276 -20.290  1.00 32.70           C  
ATOM    506  OD1 ASN A  79      19.512  -2.094 -20.374  1.00 32.49           O  
ATOM    507  ND2 ASN A  79      18.194  -3.847 -20.696  1.00 22.44           N  
ATOM    508  N   LYS A  80      23.072  -5.719 -19.311  1.00 23.84           N  
ATOM    509  CA  LYS A  80      23.772  -6.871 -18.777  1.00 23.39           C  
ATOM    510  C   LYS A  80      24.398  -6.551 -17.434  1.00 29.25           C  
ATOM    511  O   LYS A  80      24.935  -5.463 -17.234  1.00 29.91           O  
ATOM    512  CB  LYS A  80      24.868  -7.315 -19.731  1.00 23.83           C  
ATOM    513  CG  LYS A  80      25.675  -8.476 -19.220  1.00 36.42           C  
ATOM    514  CD  LYS A  80      26.277  -9.265 -20.371  1.00 46.64           C  
ATOM    515  CE  LYS A  80      27.483 -10.058 -19.915  1.00 53.55           C  
ATOM    516  NZ  LYS A  80      27.917 -11.025 -20.953  1.00 54.96           N  
ATOM    517  N   LEU A  81      24.298  -7.498 -16.510  1.00 24.77           N  
ATOM    518  CA  LEU A  81      24.912  -7.357 -15.221  1.00 25.47           C  
ATOM    519  C   LEU A  81      25.531  -8.686 -14.847  1.00 27.30           C  
ATOM    520  O   LEU A  81      24.888  -9.740 -14.966  1.00 26.89           O  
ATOM    521  CB  LEU A  81      23.901  -6.931 -14.151  1.00 27.10           C  
ATOM    522  CG  LEU A  81      24.552  -6.792 -12.759  1.00 33.48           C  
ATOM    523  CD1 LEU A  81      24.755  -5.326 -12.415  1.00 34.21           C  
ATOM    524  CD2 LEU A  81      23.691  -7.476 -11.717  1.00 37.42           C  
ATOM    525  N   THR A  82      26.786  -8.648 -14.414  1.00 22.15           N  
ATOM    526  CA  THR A  82      27.438  -9.873 -13.949  1.00 23.17           C  
ATOM    527  C   THR A  82      27.957  -9.575 -12.577  1.00 28.69           C  
ATOM    528  O   THR A  82      28.349  -8.434 -12.276  1.00 27.82           O  
ATOM    529  CB  THR A  82      28.618 -10.343 -14.855  1.00 28.70           C  
ATOM    530  OG1 THR A  82      29.671  -9.383 -14.772  1.00 37.67           O  
ATOM    531  CG2 THR A  82      28.190 -10.473 -16.292  1.00 21.24           C  
ATOM    532  N   ILE A  83      27.952 -10.589 -11.737  1.00 26.91           N  
ATOM    533  CA  ILE A  83      28.517 -10.433 -10.410  1.00 28.22           C  
ATOM    534  C   ILE A  83      29.126 -11.754  -9.939  1.00 32.35           C  
ATOM    535  O   ILE A  83      28.604 -12.824 -10.265  1.00 30.56           O  
ATOM    536  CB  ILE A  83      27.535  -9.813  -9.412  1.00 32.49           C  
ATOM    537  CG1 ILE A  83      28.000 -10.047  -7.976  1.00 33.17           C  
ATOM    538  CG2 ILE A  83      26.145 -10.295  -9.619  1.00 34.12           C  
ATOM    539  CD1 ILE A  83      27.803  -8.815  -7.092  1.00 47.43           C  
ATOM    540  N   GLU A  84      30.283 -11.665  -9.274  1.00 29.16           N  
ATOM    541  CA  GLU A  84      30.973 -12.836  -8.734  1.00 29.07           C  
ATOM    542  C   GLU A  84      31.359 -12.486  -7.305  1.00 30.19           C  
ATOM    543  O   GLU A  84      31.910 -11.406  -7.040  1.00 28.45           O  
ATOM    544  CB  GLU A  84      32.231 -13.140  -9.545  1.00 30.98           C  
ATOM    545  CG  GLU A  84      31.974 -13.900 -10.829  1.00 48.70           C  
ATOM    546  CD  GLU A  84      33.021 -14.967 -11.082  1.00 84.08           C  
ATOM    547  OE1 GLU A  84      33.827 -15.255 -10.158  1.00 72.82           O  
ATOM    548  OE2 GLU A  84      33.041 -15.505 -12.211  1.00 87.42           O  
ATOM    549  N   ALA A  85      31.022 -13.364  -6.371  1.00 25.89           N  
ATOM    550  CA  ALA A  85      31.266 -13.055  -4.970  1.00 25.19           C  
ATOM    551  C   ALA A  85      31.613 -14.292  -4.161  1.00 27.59           C  
ATOM    552  O   ALA A  85      31.097 -15.391  -4.425  1.00 28.09           O  
ATOM    553  CB  ALA A  85      29.999 -12.369  -4.375  1.00 25.74           C  
ATOM    554  N   ASP A  86      32.415 -14.078  -3.125  1.00 22.08           N  
ATOM    555  CA  ASP A  86      32.771 -15.132  -2.185  1.00 23.29           C  
ATOM    556  C   ASP A  86      32.006 -14.776  -0.906  1.00 26.48           C  
ATOM    557  O   ASP A  86      32.127 -13.654  -0.405  1.00 25.52           O  
ATOM    558  CB  ASP A  86      34.289 -15.125  -1.901  1.00 25.98           C  
ATOM    559  CG  ASP A  86      35.115 -15.641  -3.090  1.00 35.96           C  
ATOM    560  OD1 ASP A  86      34.542 -16.239  -4.016  1.00 35.30           O  
ATOM    561  OD2 ASP A  86      36.330 -15.386  -3.137  1.00 42.61           O  
ATOM    562  N   ILE A  87      31.255 -15.735  -0.366  1.00 22.06           N  
ATOM    563  CA  ILE A  87      30.409 -15.484   0.789  1.00 22.43           C  
ATOM    564  C   ILE A  87      30.583 -16.541   1.863  1.00 27.29           C  
ATOM    565  O   ILE A  87      30.703 -17.733   1.551  1.00 26.53           O  
ATOM    566  CB  ILE A  87      28.903 -15.423   0.356  1.00 25.26           C  
ATOM    567  CG1 ILE A  87      28.691 -14.306  -0.665  1.00 25.50           C  
ATOM    568  CG2 ILE A  87      27.981 -15.205   1.583  1.00 23.46           C  
ATOM    569  CD1 ILE A  87      27.372 -14.375  -1.346  1.00 37.04           C  
ATOM    570  N   ALA A  88      30.515 -16.129   3.131  1.00 23.24           N  
ATOM    571  CA  ALA A  88      30.660 -17.097   4.206  1.00 22.83           C  
ATOM    572  C   ALA A  88      29.960 -16.574   5.418  1.00 25.33           C  
ATOM    573  O   ALA A  88      29.951 -15.364   5.646  1.00 24.82           O  
ATOM    574  CB  ALA A  88      32.172 -17.301   4.543  1.00 22.82           C  
ATOM    575  N   ASN A  89      29.453 -17.480   6.234  1.00 20.51           N  
ATOM    576  CA  ASN A  89      28.925 -17.084   7.529  1.00 22.53           C  
ATOM    577  C   ASN A  89      30.148 -16.912   8.424  1.00 27.95           C  
ATOM    578  O   ASN A  89      31.042 -17.729   8.352  1.00 27.51           O  
ATOM    579  CB  ASN A  89      28.088 -18.230   8.140  1.00 20.26           C  
ATOM    580  CG  ASN A  89      26.710 -18.332   7.549  1.00 34.15           C  
ATOM    581  OD1 ASN A  89      26.059 -17.319   7.287  1.00 31.50           O  
ATOM    582  ND2 ASN A  89      26.240 -19.553   7.361  1.00 21.22           N  
ATOM    583  N   GLU A  90      30.171 -15.888   9.274  1.00 26.97           N  
ATOM    584  CA  GLU A  90      31.228 -15.724  10.297  1.00 28.22           C  
ATOM    585  C   GLU A  90      30.642 -16.275  11.602  1.00 32.99           C  
ATOM    586  O   GLU A  90      31.298 -17.040  12.317  1.00 35.41           O  
ATOM    587  CB  GLU A  90      31.581 -14.261  10.526  1.00 29.52           C  
ATOM    588  CG  GLU A  90      32.683 -13.776   9.652  1.00 44.11           C  
ATOM    589  CD  GLU A  90      33.300 -12.524  10.207  1.00 66.78           C  
ATOM    590  OE1 GLU A  90      32.858 -12.099  11.302  1.00 61.87           O  
ATOM    591  OE2 GLU A  90      34.247 -11.996   9.582  1.00 66.09           O  
ATOM    592  N   THR A  91      29.403 -15.874  11.896  1.00 27.18           N  
ATOM    593  CA  THR A  91      28.652 -16.375  13.044  1.00 26.13           C  
ATOM    594  C   THR A  91      27.292 -16.707  12.504  1.00 29.64           C  
ATOM    595  O   THR A  91      27.075 -16.612  11.288  1.00 28.51           O  
ATOM    596  CB  THR A  91      28.528 -15.348  14.191  1.00 32.49           C  
ATOM    597  OG1 THR A  91      27.646 -14.283  13.803  1.00 32.45           O  
ATOM    598  CG2 THR A  91      29.892 -14.787  14.609  1.00 28.01           C  
ATOM    599  N   LYS A  92      26.356 -17.031  13.397  1.00 28.27           N  
ATOM    600  CA  LYS A  92      24.967 -17.308  12.986  1.00 28.61           C  
ATOM    601  C   LYS A  92      24.218 -16.024  12.572  1.00 31.68           C  
ATOM    602  O   LYS A  92      23.283 -16.087  11.815  1.00 32.29           O  
ATOM    603  CB  LYS A  92      24.199 -18.023  14.090  1.00 30.57           C  
ATOM    604  CG  LYS A  92      24.099 -17.217  15.365  1.00 50.82           C  
ATOM    605  CD  LYS A  92      23.734 -18.102  16.556  1.00 66.81           C  
ATOM    606  CE  LYS A  92      24.145 -17.452  17.866  1.00 80.99           C  
ATOM    607  NZ  LYS A  92      23.044 -16.644  18.450  1.00 90.78           N  
ATOM    608  N   GLU A  93      24.646 -14.870  13.060  1.00 28.53           N  
ATOM    609  CA  GLU A  93      24.004 -13.595  12.715  1.00 28.50           C  
ATOM    610  C   GLU A  93      24.784 -12.761  11.702  1.00 31.77           C  
ATOM    611  O   GLU A  93      24.213 -11.875  11.096  1.00 33.15           O  
ATOM    612  CB  GLU A  93      23.795 -12.719  13.949  1.00 29.81           C  
ATOM    613  CG  GLU A  93      22.862 -13.319  14.967  1.00 49.05           C  
ATOM    614  CD  GLU A  93      23.528 -13.500  16.310  1.00 85.70           C  
ATOM    615  OE1 GLU A  93      24.746 -13.806  16.322  1.00 80.73           O  
ATOM    616  OE2 GLU A  93      22.839 -13.312  17.340  1.00 92.33           O  
ATOM    617  N   ARG A  94      26.085 -13.004  11.568  1.00 25.85           N  
ATOM    618  CA  ARG A  94      26.939 -12.209  10.697  1.00 25.53           C  
ATOM    619  C   ARG A  94      27.499 -12.997   9.505  1.00 31.09           C  
ATOM    620  O   ARG A  94      28.027 -14.107   9.667  1.00 31.14           O  
ATOM    621  CB  ARG A  94      28.098 -11.608  11.501  1.00 22.80           C  
ATOM    622  CG  ARG A  94      28.877 -10.553  10.733  1.00 32.05           C  
ATOM    623  CD  ARG A  94      29.847  -9.807  11.643  1.00 35.03           C  
ATOM    624  NE  ARG A  94      30.928 -10.700  12.052  1.00 52.18           N  
ATOM    625  CZ  ARG A  94      31.196 -11.054  13.311  1.00 64.21           C  
ATOM    626  NH1 ARG A  94      32.210 -11.882  13.562  1.00 41.66           N  
ATOM    627  NH2 ARG A  94      30.466 -10.571  14.317  1.00 44.12           N  
ATOM    628  N   ARG A  95      27.330 -12.427   8.308  1.00 23.49           N  
ATOM    629  CA  ARG A  95      27.779 -13.051   7.081  1.00 22.29           C  
ATOM    630  C   ARG A  95      28.676 -11.996   6.383  1.00 26.43           C  
ATOM    631  O   ARG A  95      28.443 -10.786   6.513  1.00 24.00           O  
ATOM    632  CB  ARG A  95      26.543 -13.381   6.217  1.00 19.08           C  
ATOM    633  CG  ARG A  95      26.778 -14.350   5.075  1.00 17.88           C  
ATOM    634  CD  ARG A  95      25.454 -14.768   4.430  1.00 18.97           C  
ATOM    635  NE  ARG A  95      24.716 -15.681   5.287  1.00 19.95           N  
ATOM    636  CZ  ARG A  95      23.392 -15.826   5.307  1.00 34.22           C  
ATOM    637  NH1 ARG A  95      22.611 -15.131   4.475  1.00 18.62           N  
ATOM    638  NH2 ARG A  95      22.855 -16.701   6.146  1.00 18.57           N  
ATOM    639  N   ILE A  96      29.706 -12.445   5.672  1.00 23.02           N  
ATOM    640  CA  ILE A  96      30.599 -11.509   4.993  1.00 24.44           C  
ATOM    641  C   ILE A  96      30.713 -11.875   3.534  1.00 24.77           C  
ATOM    642  O   ILE A  96      30.435 -13.001   3.148  1.00 22.80           O  
ATOM    643  CB  ILE A  96      32.005 -11.429   5.653  1.00 28.99           C  
ATOM    644  CG1 ILE A  96      32.744 -12.757   5.428  1.00 30.28           C  
ATOM    645  CG2 ILE A  96      31.866 -11.105   7.145  1.00 29.90           C  
ATOM    646  CD1 ILE A  96      33.870 -12.966   6.384  1.00 44.90           C  
ATOM    647  N   SER A  97      31.064 -10.897   2.717  1.00 22.16           N  
ATOM    648  CA  SER A  97      31.171 -11.124   1.279  1.00 22.53           C  
ATOM    649  C   SER A  97      32.201 -10.213   0.664  1.00 26.00           C  
ATOM    650  O   SER A  97      32.422  -9.104   1.136  1.00 24.65           O  
ATOM    651  CB  SER A  97      29.830 -10.858   0.596  1.00 24.00           C  
ATOM    652  OG  SER A  97      29.498  -9.493   0.729  1.00 32.38           O  
ATOM    653  N   VAL A  98      32.770 -10.675  -0.443  1.00 23.68           N  
ATOM    654  CA  VAL A  98      33.761  -9.913  -1.182  1.00 23.57           C  
ATOM    655  C   VAL A  98      33.558 -10.243  -2.646  1.00 24.76           C  
ATOM    656  O   VAL A  98      33.385 -11.380  -3.006  1.00 24.35           O  
ATOM    657  CB  VAL A  98      35.225 -10.233  -0.640  1.00 29.66           C  
ATOM    658  CG1 VAL A  98      35.698 -11.568  -1.131  1.00 29.80           C  
ATOM    659  CG2 VAL A  98      36.206  -9.176  -1.066  1.00 30.05           C  
ATOM    660  N   GLY A  99      33.475  -9.252  -3.516  1.00 22.67           N  
ATOM    661  CA  GLY A  99      33.288  -9.608  -4.913  1.00 21.76           C  
ATOM    662  C   GLY A  99      33.525  -8.492  -5.905  1.00 26.64           C  
ATOM    663  O   GLY A  99      34.065  -7.442  -5.569  1.00 26.64           O  
ATOM    664  N   GLU A 100      33.078  -8.733  -7.137  1.00 23.97           N  
ATOM    665  CA  GLU A 100      33.239  -7.774  -8.223  1.00 24.31           C  
ATOM    666  C   GLU A 100      32.217  -8.100  -9.325  1.00 27.17           C  
ATOM    667  O   GLU A 100      31.635  -9.184  -9.362  1.00 25.06           O  
ATOM    668  CB  GLU A 100      34.638  -7.903  -8.804  1.00 25.02           C  
ATOM    669  CG  GLU A 100      34.775  -9.145  -9.638  1.00 40.50           C  
ATOM    670  CD  GLU A 100      36.216  -9.614  -9.790  1.00 75.07           C  
ATOM    671  OE1 GLU A 100      37.143  -8.826  -9.481  1.00 69.23           O  
ATOM    672  OE2 GLU A 100      36.413 -10.772 -10.237  1.00 77.03           O  
ATOM    673  N   GLY A 101      32.024  -7.162 -10.240  1.00 22.77           N  
ATOM    674  CA  GLY A 101      31.076  -7.368 -11.298  1.00 21.31           C  
ATOM    675  C   GLY A 101      31.109  -6.200 -12.252  1.00 28.62           C  
ATOM    676  O   GLY A 101      32.014  -5.347 -12.209  1.00 29.04           O  
ATOM    677  N   MET A 102      30.094  -6.150 -13.103  1.00 26.40           N  
ATOM    678  CA  MET A 102      30.038  -5.174 -14.144  1.00 28.46           C  
ATOM    679  C   MET A 102      28.597  -4.904 -14.536  1.00 28.22           C  
ATOM    680  O   MET A 102      27.769  -5.808 -14.503  1.00 27.66           O  
ATOM    681  CB  MET A 102      30.753  -5.787 -15.352  1.00 33.55           C  
ATOM    682  CG  MET A 102      31.154  -4.790 -16.413  1.00 42.12           C  
ATOM    683  SD  MET A 102      31.017  -5.572 -18.045  1.00 51.22           S  
ATOM    684  CE  MET A 102      29.211  -6.125 -17.964  1.00 46.96           C  
ATOM    685  N   VAL A 103      28.313  -3.676 -14.970  1.00 23.52           N  
ATOM    686  CA  VAL A 103      26.987  -3.312 -15.486  1.00 23.35           C  
ATOM    687  C   VAL A 103      27.232  -2.741 -16.853  1.00 26.82           C  
ATOM    688  O   VAL A 103      28.161  -1.956 -17.035  1.00 28.13           O  
ATOM    689  CB  VAL A 103      26.272  -2.187 -14.644  1.00 28.41           C  
ATOM    690  CG1 VAL A 103      24.771  -2.132 -15.013  1.00 27.66           C  
ATOM    691  CG2 VAL A 103      26.421  -2.425 -13.191  1.00 29.68           C  
ATOM    692  N   SER A 104      26.356  -3.044 -17.796  1.00 22.93           N  
ATOM    693  CA  SER A 104      26.477  -2.487 -19.138  1.00 23.16           C  
ATOM    694  C   SER A 104      25.092  -2.278 -19.782  1.00 26.06           C  
ATOM    695  O   SER A 104      24.210  -3.131 -19.675  1.00 25.94           O  
ATOM    696  CB  SER A 104      27.387  -3.385 -19.986  1.00 27.71           C  
ATOM    697  OG  SER A 104      26.681  -3.938 -21.058  1.00 37.82           O  
ATOM    698  N   VAL A 105      24.886  -1.098 -20.361  1.00 21.18           N  
ATOM    699  CA  VAL A 105      23.619  -0.711 -20.985  1.00 20.87           C  
ATOM    700  C   VAL A 105      24.013  -0.032 -22.303  1.00 24.08           C  
ATOM    701  O   VAL A 105      24.722   0.959 -22.281  1.00 22.06           O  
ATOM    702  CB  VAL A 105      22.798   0.286 -20.053  1.00 24.13           C  
ATOM    703  CG1 VAL A 105      21.579   0.861 -20.783  1.00 23.42           C  
ATOM    704  CG2 VAL A 105      22.390  -0.390 -18.741  1.00 23.01           C  
ATOM    705  N   GLY A 106      23.593  -0.597 -23.433  1.00 22.05           N  
ATOM    706  CA  GLY A 106      23.949  -0.067 -24.762  1.00 22.35           C  
ATOM    707  C   GLY A 106      25.463   0.195 -24.874  1.00 27.14           C  
ATOM    708  O   GLY A 106      26.265  -0.675 -24.560  1.00 27.54           O  
ATOM    709  N   ASP A 107      25.869   1.408 -25.253  1.00 22.37           N  
ATOM    710  CA  ASP A 107      27.308   1.705 -25.401  1.00 20.66           C  
ATOM    711  C   ASP A 107      28.036   1.962 -24.090  1.00 26.20           C  
ATOM    712  O   ASP A 107      29.206   2.346 -24.090  1.00 25.33           O  
ATOM    713  CB  ASP A 107      27.545   2.894 -26.364  1.00 20.47           C  
ATOM    714  CG  ASP A 107      27.076   4.239 -25.805  1.00 32.54           C  
ATOM    715  OD1 ASP A 107      27.004   4.437 -24.574  1.00 34.94           O  
ATOM    716  OD2 ASP A 107      26.799   5.150 -26.614  1.00 42.65           O  
ATOM    717  N   PHE A 108      27.323   1.892 -22.972  1.00 23.09           N  
ATOM    718  CA  PHE A 108      27.938   2.226 -21.699  1.00 22.12           C  
ATOM    719  C   PHE A 108      28.194   1.049 -20.780  1.00 26.14           C  
ATOM    720  O   PHE A 108      27.405   0.123 -20.696  1.00 25.54           O  
ATOM    721  CB  PHE A 108      27.087   3.256 -20.974  1.00 24.01           C  
ATOM    722  CG  PHE A 108      27.600   3.608 -19.610  1.00 25.57           C  
ATOM    723  CD1 PHE A 108      28.545   4.622 -19.456  1.00 28.34           C  
ATOM    724  CD2 PHE A 108      27.184   2.903 -18.496  1.00 28.30           C  
ATOM    725  CE1 PHE A 108      29.054   4.951 -18.219  1.00 28.38           C  
ATOM    726  CE2 PHE A 108      27.697   3.201 -17.248  1.00 31.80           C  
ATOM    727  CZ  PHE A 108      28.626   4.253 -17.106  1.00 29.98           C  
ATOM    728  N   SER A 109      29.279   1.117 -20.024  1.00 23.42           N  
ATOM    729  CA  SER A 109      29.544   0.082 -19.036  1.00 22.67           C  
ATOM    730  C   SER A 109      30.470   0.611 -17.964  1.00 26.10           C  
ATOM    731  O   SER A 109      31.103   1.636 -18.153  1.00 24.51           O  
ATOM    732  CB  SER A 109      30.134  -1.184 -19.676  1.00 26.46           C  
ATOM    733  OG  SER A 109      31.517  -1.034 -19.881  1.00 36.23           O  
ATOM    734  N   HIS A 110      30.452  -0.050 -16.800  1.00 22.63           N  
ATOM    735  CA  HIS A 110      31.335   0.254 -15.697  1.00 21.53           C  
ATOM    736  C   HIS A 110      31.525  -0.996 -14.843  1.00 24.79           C  
ATOM    737  O   HIS A 110      30.692  -1.914 -14.895  1.00 23.82           O  
ATOM    738  CB  HIS A 110      30.908   1.512 -14.913  1.00 22.70           C  
ATOM    739  CG  HIS A 110      29.863   1.303 -13.844  1.00 25.57           C  
ATOM    740  ND1 HIS A 110      30.150   0.732 -12.618  1.00 27.31           N  
ATOM    741  CD2 HIS A 110      28.604   1.810 -13.727  1.00 26.59           C  
ATOM    742  CE1 HIS A 110      29.096   0.834 -11.816  1.00 25.80           C  
ATOM    743  NE2 HIS A 110      28.146   1.500 -12.460  1.00 25.77           N  
ATOM    744  N   THR A 111      32.646  -1.060 -14.118  1.00 20.79           N  
ATOM    745  CA  THR A 111      32.920  -2.184 -13.244  1.00 20.19           C  
ATOM    746  C   THR A 111      32.800  -1.744 -11.795  1.00 25.33           C  
ATOM    747  O   THR A 111      32.658  -0.574 -11.497  1.00 25.75           O  
ATOM    748  CB  THR A 111      34.308  -2.769 -13.494  1.00 22.01           C  
ATOM    749  OG1 THR A 111      35.273  -1.762 -13.193  1.00 28.11           O  
ATOM    750  CG2 THR A 111      34.477  -3.256 -14.957  1.00 14.27           C  
ATOM    751  N   PHE A 112      32.886  -2.692 -10.881  1.00 22.55           N  
ATOM    752  CA  PHE A 112      32.879  -2.356  -9.479  1.00 22.42           C  
ATOM    753  C   PHE A 112      33.494  -3.499  -8.670  1.00 25.67           C  
ATOM    754  O   PHE A 112      33.514  -4.639  -9.101  1.00 25.96           O  
ATOM    755  CB  PHE A 112      31.434  -2.109  -9.013  1.00 24.64           C  
ATOM    756  CG  PHE A 112      30.484  -3.288  -9.249  1.00 25.30           C  
ATOM    757  CD1 PHE A 112      30.335  -4.276  -8.293  1.00 28.44           C  
ATOM    758  CD2 PHE A 112      29.681  -3.341 -10.394  1.00 26.50           C  
ATOM    759  CE1 PHE A 112      29.439  -5.335  -8.498  1.00 29.93           C  
ATOM    760  CE2 PHE A 112      28.796  -4.374 -10.610  1.00 29.11           C  
ATOM    761  CZ  PHE A 112      28.674  -5.377  -9.668  1.00 27.95           C  
ATOM    762  N   SER A 113      34.006  -3.196  -7.498  1.00 22.31           N  
ATOM    763  CA  SER A 113      34.435  -4.255  -6.600  1.00 23.18           C  
ATOM    764  C   SER A 113      33.875  -3.858  -5.221  1.00 26.48           C  
ATOM    765  O   SER A 113      33.531  -2.687  -5.007  1.00 25.38           O  
ATOM    766  CB  SER A 113      35.956  -4.486  -6.600  1.00 25.75           C  
ATOM    767  OG  SER A 113      36.625  -3.465  -5.871  1.00 38.56           O  
ATOM    768  N   PHE A 114      33.706  -4.823  -4.324  1.00 22.49           N  
ATOM    769  CA  PHE A 114      33.131  -4.488  -3.032  1.00 21.70           C  
ATOM    770  C   PHE A 114      33.449  -5.513  -1.957  1.00 25.05           C  
ATOM    771  O   PHE A 114      33.768  -6.675  -2.219  1.00 23.83           O  
ATOM    772  CB  PHE A 114      31.587  -4.404  -3.160  1.00 22.44           C  
ATOM    773  CG  PHE A 114      30.922  -5.761  -3.298  1.00 22.79           C  
ATOM    774  CD1 PHE A 114      30.474  -6.469  -2.156  1.00 23.63           C  
ATOM    775  CD2 PHE A 114      30.814  -6.374  -4.551  1.00 23.54           C  
ATOM    776  CE1 PHE A 114      29.923  -7.757  -2.276  1.00 23.35           C  
ATOM    777  CE2 PHE A 114      30.235  -7.652  -4.693  1.00 24.79           C  
ATOM    778  CZ  PHE A 114      29.796  -8.351  -3.550  1.00 22.04           C  
ATOM    779  N   GLU A 115      33.253  -5.081  -0.729  1.00 23.57           N  
ATOM    780  CA  GLU A 115      33.264  -5.990   0.392  1.00 26.13           C  
ATOM    781  C   GLU A 115      32.205  -5.491   1.381  1.00 29.03           C  
ATOM    782  O   GLU A 115      31.991  -4.300   1.513  1.00 28.61           O  
ATOM    783  CB  GLU A 115      34.648  -6.120   1.009  1.00 28.46           C  
ATOM    784  CG  GLU A 115      35.089  -4.972   1.865  1.00 44.56           C  
ATOM    785  CD  GLU A 115      36.567  -5.081   2.217  1.00 78.88           C  
ATOM    786  OE1 GLU A 115      37.382  -5.323   1.300  1.00 62.91           O  
ATOM    787  OE2 GLU A 115      36.905  -4.981   3.414  1.00 84.21           O  
ATOM    788  N   GLY A 116      31.446  -6.391   1.982  1.00 24.65           N  
ATOM    789  CA  GLY A 116      30.415  -5.935   2.909  1.00 23.31           C  
ATOM    790  C   GLY A 116      30.032  -7.021   3.901  1.00 25.76           C  
ATOM    791  O   GLY A 116      30.320  -8.208   3.728  1.00 23.71           O  
ATOM    792  N   SER A 117      29.391  -6.610   4.973  1.00 23.03           N  
ATOM    793  CA  SER A 117      28.921  -7.595   5.931  1.00 22.73           C  
ATOM    794  C   SER A 117      27.449  -7.289   6.209  1.00 25.64           C  
ATOM    795  O   SER A 117      26.985  -6.147   6.134  1.00 24.19           O  
ATOM    796  CB  SER A 117      29.728  -7.546   7.232  1.00 23.62           C  
ATOM    797  OG  SER A 117      29.496  -6.308   7.845  1.00 36.71           O  
ATOM    798  N   VAL A 118      26.719  -8.325   6.546  1.00 21.64           N  
ATOM    799  CA  VAL A 118      25.321  -8.157   6.879  1.00 20.89           C  
ATOM    800  C   VAL A 118      25.102  -8.860   8.201  1.00 24.08           C  
ATOM    801  O   VAL A 118      25.519  -9.996   8.354  1.00 26.00           O  
ATOM    802  CB  VAL A 118      24.379  -8.721   5.760  1.00 22.94           C  
ATOM    803  CG1 VAL A 118      22.885  -8.660   6.216  1.00 21.46           C  
ATOM    804  CG2 VAL A 118      24.577  -7.962   4.441  1.00 22.28           C  
ATOM    805  N   VAL A 119      24.498  -8.160   9.158  1.00 18.95           N  
ATOM    806  CA  VAL A 119      24.150  -8.730  10.449  1.00 19.43           C  
ATOM    807  C   VAL A 119      22.622  -8.813  10.543  1.00 24.64           C  
ATOM    808  O   VAL A 119      21.937  -7.803  10.389  1.00 24.58           O  
ATOM    809  CB  VAL A 119      24.724  -7.909  11.606  1.00 24.31           C  
ATOM    810  CG1 VAL A 119      24.215  -8.449  12.944  1.00 23.20           C  
ATOM    811  CG2 VAL A 119      26.273  -7.905  11.539  1.00 23.80           C  
ATOM    812  N   ASN A 120      22.099 -10.022  10.731  1.00 21.56           N  
ATOM    813  CA  ASN A 120      20.660 -10.250  10.842  1.00 21.73           C  
ATOM    814  C   ASN A 120      20.266 -10.471  12.281  1.00 27.31           C  
ATOM    815  O   ASN A 120      20.804 -11.361  12.928  1.00 27.83           O  
ATOM    816  CB  ASN A 120      20.259 -11.507  10.050  1.00 18.38           C  
ATOM    817  CG  ASN A 120      18.764 -11.574   9.803  1.00 32.98           C  
ATOM    818  OD1 ASN A 120      18.238 -10.831   8.990  1.00 24.15           O  
ATOM    819  ND2 ASN A 120      18.070 -12.446  10.528  1.00 18.28           N  
ATOM    820  N   LEU A 121      19.331  -9.672  12.785  1.00 24.79           N  
ATOM    821  CA  LEU A 121      18.873  -9.770  14.181  1.00 24.62           C  
ATOM    822  C   LEU A 121      17.343  -9.930  14.291  1.00 27.95           C  
ATOM    823  O   LEU A 121      16.586  -9.154  13.704  1.00 27.22           O  
ATOM    824  CB  LEU A 121      19.295  -8.520  14.977  1.00 24.95           C  
ATOM    825  CG  LEU A 121      20.811  -8.305  15.157  1.00 32.61           C  
ATOM    826  CD1 LEU A 121      21.144  -6.934  15.773  1.00 33.37           C  
ATOM    827  CD2 LEU A 121      21.503  -9.447  15.957  1.00 34.53           C  
ATOM    828  N   PHE A 122      16.899 -10.882  15.102  1.00 23.97           N  
ATOM    829  CA  PHE A 122      15.486 -11.059  15.388  1.00 24.91           C  
ATOM    830  C   PHE A 122      15.141 -10.172  16.593  1.00 28.66           C  
ATOM    831  O   PHE A 122      15.967  -9.933  17.459  1.00 26.91           O  
ATOM    832  CB  PHE A 122      15.164 -12.527  15.700  1.00 26.91           C  
ATOM    833  CG  PHE A 122      15.311 -13.432  14.524  1.00 28.36           C  
ATOM    834  CD1 PHE A 122      14.683 -13.144  13.329  1.00 30.46           C  
ATOM    835  CD2 PHE A 122      16.108 -14.541  14.588  1.00 31.63           C  
ATOM    836  CE1 PHE A 122      14.859 -13.951  12.212  1.00 31.34           C  
ATOM    837  CE2 PHE A 122      16.276 -15.352  13.474  1.00 34.47           C  
ATOM    838  CZ  PHE A 122      15.645 -15.039  12.282  1.00 31.44           C  
ATOM    839  N   TYR A 123      13.939  -9.610  16.601  1.00 25.49           N  
ATOM    840  CA  TYR A 123      13.559  -8.712  17.707  1.00 24.34           C  
ATOM    841  C   TYR A 123      13.370  -9.427  19.041  1.00 29.50           C  
ATOM    842  O   TYR A 123      13.511  -8.813  20.072  1.00 29.70           O  
ATOM    843  CB  TYR A 123      12.304  -7.912  17.358  1.00 23.28           C  
ATOM    844  CG  TYR A 123      12.552  -6.807  16.352  1.00 23.88           C  
ATOM    845  CD1 TYR A 123      13.506  -5.807  16.593  1.00 26.36           C  
ATOM    846  CD2 TYR A 123      11.813  -6.742  15.166  1.00 22.60           C  
ATOM    847  CE1 TYR A 123      13.697  -4.744  15.663  1.00 26.16           C  
ATOM    848  CE2 TYR A 123      12.010  -5.711  14.238  1.00 22.24           C  
ATOM    849  CZ  TYR A 123      12.931  -4.699  14.504  1.00 27.59           C  
ATOM    850  OH  TYR A 123      13.124  -3.679  13.570  1.00 24.91           O  
ATOM    851  N   TYR A 124      13.046 -10.714  19.016  1.00 26.30           N  
ATOM    852  CA  TYR A 124      12.844 -11.477  20.252  1.00 27.26           C  
ATOM    853  C   TYR A 124      13.209 -12.944  20.033  1.00 32.49           C  
ATOM    854  O   TYR A 124      13.235 -13.412  18.910  1.00 33.02           O  
ATOM    855  CB  TYR A 124      11.370 -11.403  20.696  1.00 29.09           C  
ATOM    856  CG  TYR A 124      10.485 -12.404  19.977  1.00 31.85           C  
ATOM    857  CD1 TYR A 124      10.001 -12.136  18.707  1.00 34.15           C  
ATOM    858  CD2 TYR A 124      10.183 -13.639  20.534  1.00 32.94           C  
ATOM    859  CE1 TYR A 124       9.204 -13.054  18.025  1.00 34.54           C  
ATOM    860  CE2 TYR A 124       9.416 -14.583  19.841  1.00 33.56           C  
ATOM    861  CZ  TYR A 124       8.931 -14.279  18.590  1.00 40.38           C  
ATOM    862  OH  TYR A 124       8.166 -15.182  17.887  1.00 39.41           O  
ATOM    863  N   ARG A 125      13.500 -13.668  21.094  1.00 30.10           N  
ATOM    864  CA  ARG A 125      13.747 -15.112  20.982  1.00 31.82           C  
ATOM    865  C   ARG A 125      13.015 -15.666  22.190  1.00 33.44           C  
ATOM    866  O   ARG A 125      13.203 -15.180  23.296  1.00 33.46           O  
ATOM    867  CB  ARG A 125      15.250 -15.477  21.074  1.00 36.19           C  
ATOM    868  N   SER A 126      12.084 -16.580  21.979  1.00 27.65           N  
ATOM    869  CA  SER A 126      11.348 -17.106  23.113  1.00 26.03           C  
ATOM    870  C   SER A 126      11.166 -18.611  23.054  1.00 28.36           C  
ATOM    871  O   SER A 126      10.688 -19.152  22.073  1.00 28.62           O  
ATOM    872  CB  SER A 126       9.989 -16.436  23.215  1.00 28.64           C  
ATOM    873  OG  SER A 126       9.233 -16.998  24.269  1.00 33.36           O  
ATOM    874  N   ASP A 127      11.484 -19.286  24.139  1.00 24.52           N  
ATOM    875  CA  ASP A 127      11.302 -20.724  24.185  1.00 25.25           C  
ATOM    876  C   ASP A 127       9.821 -21.100  24.232  1.00 26.28           C  
ATOM    877  O   ASP A 127       9.421 -22.179  23.823  1.00 25.99           O  
ATOM    878  CB  ASP A 127      12.058 -21.346  25.378  1.00 28.68           C  
ATOM    879  CG  ASP A 127      12.129 -22.863  25.285  1.00 47.53           C  
ATOM    880  OD1 ASP A 127      12.572 -23.353  24.208  1.00 50.48           O  
ATOM    881  OD2 ASP A 127      11.663 -23.567  26.230  1.00 53.28           O  
ATOM    882  N   ALA A 128       9.001 -20.210  24.754  1.00 23.83           N  
ATOM    883  CA  ALA A 128       7.558 -20.458  24.831  1.00 23.64           C  
ATOM    884  C   ALA A 128       6.967 -20.569  23.408  1.00 28.15           C  
ATOM    885  O   ALA A 128       6.046 -21.356  23.148  1.00 25.77           O  
ATOM    886  CB  ALA A 128       6.887 -19.327  25.598  1.00 23.48           C  
ATOM    887  N   VAL A 129       7.510 -19.789  22.476  1.00 23.80           N  
ATOM    888  CA  VAL A 129       7.036 -19.858  21.095  1.00 22.29           C  
ATOM    889  C   VAL A 129       7.611 -21.113  20.442  1.00 26.31           C  
ATOM    890  O   VAL A 129       6.886 -21.937  19.879  1.00 25.11           O  
ATOM    891  CB  VAL A 129       7.368 -18.554  20.303  1.00 25.66           C  
ATOM    892  CG1 VAL A 129       7.126 -18.741  18.822  1.00 25.16           C  
ATOM    893  CG2 VAL A 129       6.533 -17.372  20.827  1.00 25.12           C  
ATOM    894  N   ARG A 130       8.920 -21.273  20.581  1.00 26.45           N  
ATOM    895  CA  ARG A 130       9.657 -22.394  20.005  1.00 27.37           C  
ATOM    896  C   ARG A 130       9.088 -23.777  20.305  1.00 31.80           C  
ATOM    897  O   ARG A 130       8.953 -24.593  19.398  1.00 31.85           O  
ATOM    898  CB  ARG A 130      11.122 -22.334  20.448  1.00 31.33           C  
ATOM    899  CG  ARG A 130      12.056 -23.246  19.642  1.00 47.82           C  
ATOM    900  N   ARG A 131       8.746 -24.062  21.559  1.00 27.42           N  
ATOM    901  CA  ARG A 131       8.239 -25.395  21.841  1.00 27.71           C  
ATOM    902  C   ARG A 131       6.784 -25.608  21.535  1.00 31.23           C  
ATOM    903  O   ARG A 131       6.320 -26.735  21.539  1.00 31.70           O  
ATOM    904  CB  ARG A 131       8.537 -25.874  23.284  1.00 27.72           C  
ATOM    905  CG  ARG A 131       8.347 -24.875  24.347  1.00 30.11           C  
ATOM    906  CD  ARG A 131       8.442 -25.499  25.774  1.00 33.43           C  
ATOM    907  NE  ARG A 131       7.531 -24.770  26.645  1.00 28.62           N  
ATOM    908  CZ  ARG A 131       7.830 -23.608  27.201  1.00 32.42           C  
ATOM    909  NH1 ARG A 131       9.041 -23.123  27.056  1.00 22.33           N  
ATOM    910  NH2 ARG A 131       6.920 -22.938  27.898  1.00 28.30           N  
ATOM    911  N   ASN A 132       6.039 -24.527  21.346  1.00 25.44           N  
ATOM    912  CA  ASN A 132       4.613 -24.637  21.121  1.00 23.39           C  
ATOM    913  C   ASN A 132       4.200 -24.481  19.654  1.00 27.23           C  
ATOM    914  O   ASN A 132       3.104 -24.870  19.265  1.00 25.70           O  
ATOM    915  CB  ASN A 132       3.865 -23.647  22.021  1.00 22.49           C  
ATOM    916  CG  ASN A 132       3.851 -24.089  23.461  1.00 27.96           C  
ATOM    917  OD1 ASN A 132       3.282 -25.113  23.779  1.00 25.12           O  
ATOM    918  ND2 ASN A 132       4.560 -23.380  24.311  1.00 17.16           N  
ATOM    919  N   VAL A 133       5.068 -23.914  18.820  1.00 23.47           N  
ATOM    920  CA  VAL A 133       4.700 -23.739  17.414  1.00 20.34           C  
ATOM    921  C   VAL A 133       5.614 -24.625  16.580  1.00 26.07           C  
ATOM    922  O   VAL A 133       6.811 -24.390  16.508  1.00 28.47           O  
ATOM    923  CB  VAL A 133       4.816 -22.257  17.034  1.00 22.04           C  
ATOM    924  CG1 VAL A 133       4.535 -22.073  15.552  1.00 20.96           C  
ATOM    925  CG2 VAL A 133       3.860 -21.383  17.934  1.00 20.97           C  
ATOM    926  N   PRO A 134       5.083 -25.698  16.015  1.00 22.82           N  
ATOM    927  CA  PRO A 134       5.940 -26.615  15.265  1.00 22.11           C  
ATOM    928  C   PRO A 134       6.490 -26.080  13.963  1.00 27.45           C  
ATOM    929  O   PRO A 134       7.567 -26.496  13.555  1.00 27.79           O  
ATOM    930  CB  PRO A 134       5.058 -27.853  15.025  1.00 22.31           C  
ATOM    931  CG  PRO A 134       3.685 -27.436  15.262  1.00 27.65           C  
ATOM    932  CD  PRO A 134       3.660 -26.096  15.968  1.00 24.46           C  
ATOM    933  N   ASN A 135       5.753 -25.204  13.279  1.00 22.54           N  
ATOM    934  CA  ASN A 135       6.237 -24.701  11.985  1.00 22.19           C  
ATOM    935  C   ASN A 135       6.024 -23.202  11.905  1.00 25.05           C  
ATOM    936  O   ASN A 135       5.067 -22.732  11.288  1.00 23.49           O  
ATOM    937  CB  ASN A 135       5.547 -25.446  10.816  1.00 20.03           C  
ATOM    938  CG  ASN A 135       6.110 -25.062   9.441  1.00 28.69           C  
ATOM    939  OD1 ASN A 135       7.254 -24.641   9.314  1.00 22.04           O  
ATOM    940  ND2 ASN A 135       5.338 -25.315   8.402  1.00 23.40           N  
ATOM    941  N   PRO A 136       6.856 -22.465  12.637  1.00 23.79           N  
ATOM    942  CA  PRO A 136       6.739 -20.998  12.739  1.00 23.50           C  
ATOM    943  C   PRO A 136       6.987 -20.301  11.394  1.00 25.72           C  
ATOM    944  O   PRO A 136       7.921 -20.654  10.658  1.00 25.13           O  
ATOM    945  CB  PRO A 136       7.856 -20.625  13.745  1.00 24.85           C  
ATOM    946  CG  PRO A 136       8.842 -21.754  13.675  1.00 28.16           C  
ATOM    947  CD  PRO A 136       8.030 -22.990  13.374  1.00 24.56           C  
ATOM    948  N   ILE A 137       6.152 -19.316  11.072  1.00 21.41           N  
ATOM    949  CA  ILE A 137       6.297 -18.581   9.809  1.00 20.38           C  
ATOM    950  C   ILE A 137       6.811 -17.157   9.993  1.00 23.95           C  
ATOM    951  O   ILE A 137       7.894 -16.821   9.507  1.00 24.20           O  
ATOM    952  CB  ILE A 137       4.991 -18.581   8.976  1.00 22.66           C  
ATOM    953  CG1 ILE A 137       4.472 -20.004   8.778  1.00 21.79           C  
ATOM    954  CG2 ILE A 137       5.224 -17.861   7.615  1.00 20.78           C  
ATOM    955  CD1 ILE A 137       5.375 -20.891   7.870  1.00 17.92           C  
ATOM    956  N   TYR A 138       6.017 -16.298  10.635  1.00 21.62           N  
ATOM    957  CA  TYR A 138       6.443 -14.889  10.811  1.00 21.65           C  
ATOM    958  C   TYR A 138       7.546 -14.700  11.841  1.00 25.87           C  
ATOM    959  O   TYR A 138       7.362 -15.077  12.980  1.00 26.96           O  
ATOM    960  CB  TYR A 138       5.269 -13.983  11.198  1.00 19.70           C  
ATOM    961  CG  TYR A 138       4.095 -14.066  10.260  1.00 18.79           C  
ATOM    962  CD1 TYR A 138       4.260 -13.982   8.882  1.00 18.87           C  
ATOM    963  CD2 TYR A 138       2.791 -14.127  10.777  1.00 19.07           C  
ATOM    964  CE1 TYR A 138       3.148 -13.994   8.039  1.00 21.23           C  
ATOM    965  CE2 TYR A 138       1.692 -14.157   9.959  1.00 18.37           C  
ATOM    966  CZ  TYR A 138       1.862 -14.097   8.600  1.00 24.35           C  
ATOM    967  OH  TYR A 138       0.733 -14.138   7.822  1.00 18.97           O  
ATOM    968  N   MET A 139       8.657 -14.084  11.447  1.00 22.18           N  
ATOM    969  CA  MET A 139       9.721 -13.762  12.405  1.00 25.09           C  
ATOM    970  C   MET A 139      10.128 -12.323  12.133  1.00 24.14           C  
ATOM    971  O   MET A 139      10.698 -12.029  11.078  1.00 22.71           O  
ATOM    972  CB  MET A 139      10.945 -14.691  12.302  1.00 29.90           C  
ATOM    973  CG  MET A 139      10.829 -15.939  13.190  1.00 39.61           C  
ATOM    974  SD  MET A 139      10.803 -15.505  14.992  1.00 48.90           S  
ATOM    975  CE  MET A 139      11.724 -13.999  14.941  1.00 45.65           C  
ATOM    976  N   GLN A 140       9.753 -11.424  13.036  1.00 17.67           N  
ATOM    977  CA  GLN A 140      10.055 -10.003  12.873  1.00 16.83           C  
ATOM    978  C   GLN A 140      11.524  -9.771  13.197  1.00 22.67           C  
ATOM    979  O   GLN A 140      12.048 -10.350  14.159  1.00 22.67           O  
ATOM    980  CB  GLN A 140       9.199  -9.158  13.816  1.00 17.63           C  
ATOM    981  CG  GLN A 140       7.679  -9.502  13.837  1.00 11.99           C  
ATOM    982  CD  GLN A 140       7.321 -10.476  14.966  1.00 21.60           C  
ATOM    983  OE1 GLN A 140       7.891 -11.553  15.085  1.00 18.49           O  
ATOM    984  NE2 GLN A 140       6.407 -10.070  15.812  1.00 14.01           N  
ATOM    985  N   GLY A 141      12.179  -8.890  12.439  1.00 18.59           N  
ATOM    986  CA  GLY A 141      13.583  -8.609  12.722  1.00 18.02           C  
ATOM    987  C   GLY A 141      14.116  -7.454  11.918  1.00 20.66           C  
ATOM    988  O   GLY A 141      13.371  -6.798  11.183  1.00 20.41           O  
ATOM    989  N   ARG A 142      15.408  -7.195  12.089  1.00 17.39           N  
ATOM    990  CA  ARG A 142      16.093  -6.130  11.369  1.00 17.95           C  
ATOM    991  C   ARG A 142      17.470  -6.634  10.910  1.00 21.95           C  
ATOM    992  O   ARG A 142      18.135  -7.385  11.610  1.00 22.20           O  
ATOM    993  CB  ARG A 142      16.214  -4.874  12.248  1.00 18.36           C  
ATOM    994  CG  ARG A 142      16.635  -3.611  11.487  1.00 16.24           C  
ATOM    995  CD  ARG A 142      16.189  -2.348  12.237  1.00 23.43           C  
ATOM    996  NE  ARG A 142      14.805  -1.981  11.922  1.00 20.26           N  
ATOM    997  CZ  ARG A 142      14.452  -1.036  11.052  1.00 25.97           C  
ATOM    998  NH1 ARG A 142      15.372  -0.344  10.392  1.00 17.26           N  
ATOM    999  NH2 ARG A 142      13.169  -0.777  10.847  1.00 16.59           N  
ATOM   1000  N   GLN A 143      17.901  -6.164   9.756  1.00 19.13           N  
ATOM   1001  CA  GLN A 143      19.147  -6.596   9.094  1.00 20.38           C  
ATOM   1002  C   GLN A 143      20.056  -5.385   8.793  1.00 24.96           C  
ATOM   1003  O   GLN A 143      19.606  -4.424   8.183  1.00 26.10           O  
ATOM   1004  CB  GLN A 143      18.736  -7.227   7.762  1.00 21.54           C  
ATOM   1005  CG  GLN A 143      19.529  -8.379   7.390  1.00 31.05           C  
ATOM   1006  CD  GLN A 143      19.020  -9.010   6.106  1.00 34.74           C  
ATOM   1007  OE1 GLN A 143      18.969  -8.369   5.058  1.00 25.39           O  
ATOM   1008  NE2 GLN A 143      18.656 -10.281   6.186  1.00 23.35           N  
ATOM   1009  N   PHE A 144      21.331  -5.444   9.185  1.00 20.46           N  
ATOM   1010  CA  PHE A 144      22.247  -4.305   8.975  1.00 18.71           C  
ATOM   1011  C   PHE A 144      23.320  -4.574   7.903  1.00 24.00           C  
ATOM   1012  O   PHE A 144      24.039  -5.577   7.962  1.00 24.06           O  
ATOM   1013  CB  PHE A 144      22.898  -3.911  10.312  1.00 19.15           C  
ATOM   1014  CG  PHE A 144      21.898  -3.589  11.394  1.00 19.08           C  
ATOM   1015  CD1 PHE A 144      21.535  -2.258  11.652  1.00 20.07           C  
ATOM   1016  CD2 PHE A 144      21.243  -4.620  12.094  1.00 19.61           C  
ATOM   1017  CE1 PHE A 144      20.597  -1.942  12.641  1.00 20.91           C  
ATOM   1018  CE2 PHE A 144      20.279  -4.323  13.075  1.00 22.44           C  
ATOM   1019  CZ  PHE A 144      19.928  -2.984  13.332  1.00 20.25           C  
ATOM   1020  N   HIS A 145      23.432  -3.656   6.943  1.00 19.31           N  
ATOM   1021  CA  HIS A 145      24.396  -3.769   5.859  1.00 18.54           C  
ATOM   1022  C   HIS A 145      25.511  -2.752   6.117  1.00 23.47           C  
ATOM   1023  O   HIS A 145      25.246  -1.617   6.484  1.00 21.64           O  
ATOM   1024  CB  HIS A 145      23.747  -3.437   4.486  1.00 17.89           C  
ATOM   1025  CG  HIS A 145      22.988  -4.570   3.846  1.00 20.31           C  
ATOM   1026  ND1 HIS A 145      21.849  -5.131   4.397  1.00 20.53           N  
ATOM   1027  CD2 HIS A 145      23.164  -5.188   2.649  1.00 21.54           C  
ATOM   1028  CE1 HIS A 145      21.411  -6.101   3.609  1.00 20.06           C  
ATOM   1029  NE2 HIS A 145      22.171  -6.134   2.524  1.00 20.82           N  
ATOM   1030  N   ASP A 146      26.754  -3.157   5.869  1.00 20.64           N  
ATOM   1031  CA  ASP A 146      27.909  -2.273   5.980  1.00 20.42           C  
ATOM   1032  C   ASP A 146      28.677  -2.559   4.689  1.00 25.22           C  
ATOM   1033  O   ASP A 146      29.051  -3.710   4.407  1.00 23.31           O  
ATOM   1034  CB  ASP A 146      28.723  -2.650   7.206  1.00 23.46           C  
ATOM   1035  CG  ASP A 146      29.925  -1.759   7.407  1.00 33.81           C  
ATOM   1036  OD1 ASP A 146      30.085  -0.779   6.662  1.00 31.87           O  
ATOM   1037  OD2 ASP A 146      30.713  -2.061   8.309  1.00 47.66           O  
ATOM   1038  N   ILE A 147      28.737  -1.563   3.817  1.00 22.87           N  
ATOM   1039  CA  ILE A 147      29.291  -1.791   2.494  1.00 23.67           C  
ATOM   1040  C   ILE A 147      30.470  -0.900   2.128  1.00 27.16           C  
ATOM   1041  O   ILE A 147      30.453   0.309   2.357  1.00 26.40           O  
ATOM   1042  CB  ILE A 147      28.163  -1.633   1.421  1.00 27.19           C  
ATOM   1043  CG1 ILE A 147      27.068  -2.703   1.602  1.00 27.49           C  
ATOM   1044  CG2 ILE A 147      28.750  -1.667  -0.021  1.00 25.77           C  
ATOM   1045  CD1 ILE A 147      25.687  -2.171   1.374  1.00 25.74           C  
ATOM   1046  N   LEU A 148      31.482  -1.501   1.524  1.00 24.46           N  
ATOM   1047  CA  LEU A 148      32.585  -0.721   0.975  1.00 24.76           C  
ATOM   1048  C   LEU A 148      32.604  -1.056  -0.515  1.00 28.72           C  
ATOM   1049  O   LEU A 148      32.735  -2.220  -0.881  1.00 29.30           O  
ATOM   1050  CB  LEU A 148      33.918  -1.083   1.613  1.00 25.52           C  
ATOM   1051  CG  LEU A 148      35.168  -0.443   0.950  1.00 31.19           C  
ATOM   1052  CD1 LEU A 148      35.237   1.045   1.192  1.00 30.54           C  
ATOM   1053  CD2 LEU A 148      36.444  -1.085   1.447  1.00 36.61           C  
ATOM   1054  N   MET A 149      32.431  -0.057  -1.378  1.00 23.90           N  
ATOM   1055  CA  MET A 149      32.486  -0.317  -2.811  1.00 22.41           C  
ATOM   1056  C   MET A 149      33.435   0.621  -3.574  1.00 26.79           C  
ATOM   1057  O   MET A 149      33.630   1.800  -3.203  1.00 26.01           O  
ATOM   1058  CB  MET A 149      31.092  -0.341  -3.444  1.00 23.89           C  
ATOM   1059  CG  MET A 149      30.292   0.902  -3.198  1.00 25.97           C  
ATOM   1060  SD  MET A 149      28.610   0.753  -3.759  1.00 28.63           S  
ATOM   1061  CE  MET A 149      28.267   2.579  -4.115  1.00 24.64           C  
ATOM   1062  N   LYS A 150      33.992   0.097  -4.671  1.00 23.76           N  
ATOM   1063  CA  LYS A 150      34.955   0.836  -5.483  1.00 22.65           C  
ATOM   1064  C   LYS A 150      34.618   0.711  -6.935  1.00 27.55           C  
ATOM   1065  O   LYS A 150      34.444  -0.408  -7.437  1.00 27.71           O  
ATOM   1066  CB  LYS A 150      36.378   0.307  -5.256  1.00 23.48           C  
ATOM   1067  CG  LYS A 150      36.763   0.245  -3.796  1.00 34.86           C  
ATOM   1068  CD  LYS A 150      38.104  -0.416  -3.581  1.00 43.86           C  
ATOM   1069  CE  LYS A 150      38.821   0.214  -2.392  1.00 57.78           C  
ATOM   1070  NZ  LYS A 150      40.276  -0.116  -2.340  1.00 66.38           N  
ATOM   1071  N   VAL A 151      34.585   1.847  -7.622  1.00 24.56           N  
ATOM   1072  CA  VAL A 151      34.301   1.875  -9.048  1.00 24.38           C  
ATOM   1073  C   VAL A 151      35.367   2.753  -9.721  1.00 29.04           C  
ATOM   1074  O   VAL A 151      35.538   3.906  -9.353  1.00 28.36           O  
ATOM   1075  CB  VAL A 151      32.893   2.493  -9.306  1.00 27.38           C  
ATOM   1076  CG1 VAL A 151      32.668   2.709 -10.801  1.00 25.96           C  
ATOM   1077  CG2 VAL A 151      31.778   1.611  -8.676  1.00 27.00           C  
ATOM   1078  N   PRO A 152      36.078   2.207 -10.701  1.00 26.22           N  
ATOM   1079  CA  PRO A 152      37.058   2.987 -11.433  1.00 25.86           C  
ATOM   1080  C   PRO A 152      36.312   4.050 -12.242  1.00 29.91           C  
ATOM   1081  O   PRO A 152      35.385   3.752 -12.971  1.00 30.09           O  
ATOM   1082  CB  PRO A 152      37.709   1.959 -12.365  1.00 27.45           C  
ATOM   1083  CG  PRO A 152      37.356   0.634 -11.813  1.00 31.68           C  
ATOM   1084  CD  PRO A 152      36.027   0.809 -11.154  1.00 27.70           C  
ATOM   1085  N   LEU A 153      36.708   5.302 -12.077  1.00 26.70           N  
ATOM   1086  CA  LEU A 153      36.092   6.404 -12.801  1.00 27.16           C  
ATOM   1087  C   LEU A 153      36.798   6.529 -14.151  1.00 33.15           C  
ATOM   1088  O   LEU A 153      37.577   7.454 -14.356  1.00 34.46           O  
ATOM   1089  CB  LEU A 153      36.269   7.703 -11.991  1.00 26.49           C  
ATOM   1090  CG  LEU A 153      35.765   7.564 -10.558  1.00 29.54           C  
ATOM   1091  CD1 LEU A 153      36.028   8.797  -9.725  1.00 27.31           C  
ATOM   1092  CD2 LEU A 153      34.267   7.227 -10.594  1.00 29.49           C  
ATOM   1093  N   ASP A 154      36.556   5.573 -15.044  1.00 30.05           N  
ATOM   1094  CA  ASP A 154      37.262   5.548 -16.326  1.00 30.21           C  
ATOM   1095  C   ASP A 154      36.541   6.067 -17.544  1.00 33.46           C  
ATOM   1096  O   ASP A 154      36.914   5.750 -18.666  1.00 32.85           O  
ATOM   1097  CB  ASP A 154      37.898   4.182 -16.609  1.00 32.07           C  
ATOM   1098  CG  ASP A 154      36.912   3.033 -16.472  1.00 46.40           C  
ATOM   1099  OD1 ASP A 154      35.681   3.270 -16.491  1.00 46.49           O  
ATOM   1100  OD2 ASP A 154      37.376   1.883 -16.354  1.00 56.15           O  
ATOM   1101  N   ASN A 155      35.543   6.909 -17.338  1.00 28.84           N  
ATOM   1102  CA  ASN A 155      34.863   7.521 -18.476  1.00 27.70           C  
ATOM   1103  C   ASN A 155      34.165   8.755 -17.960  1.00 30.28           C  
ATOM   1104  O   ASN A 155      34.091   8.945 -16.749  1.00 30.64           O  
ATOM   1105  CB  ASN A 155      33.988   6.531 -19.298  1.00 29.98           C  
ATOM   1106  CG  ASN A 155      32.702   6.139 -18.595  1.00 39.34           C  
ATOM   1107  OD1 ASN A 155      31.946   7.004 -18.166  1.00 32.25           O  
ATOM   1108  ND2 ASN A 155      32.386   4.837 -18.590  1.00 28.02           N  
ATOM   1109  N   ASN A 156      33.792   9.658 -18.859  1.00 25.36           N  
ATOM   1110  CA  ASN A 156      33.222  10.925 -18.455  1.00 25.57           C  
ATOM   1111  C   ASN A 156      31.903  10.823 -17.736  1.00 29.94           C  
ATOM   1112  O   ASN A 156      31.583  11.654 -16.891  1.00 29.37           O  
ATOM   1113  CB  ASN A 156      33.123  11.870 -19.652  1.00 31.32           C  
ATOM   1114  CG  ASN A 156      34.491  12.328 -20.140  1.00 73.19           C  
ATOM   1115  OD1 ASN A 156      35.262  12.933 -19.386  1.00 66.58           O  
ATOM   1116  ND2 ASN A 156      34.832  11.970 -21.380  1.00 68.76           N  
ATOM   1117  N   ASP A 157      31.121   9.811 -18.096  1.00 27.66           N  
ATOM   1118  CA  ASP A 157      29.808   9.617 -17.486  1.00 26.94           C  
ATOM   1119  C   ASP A 157      29.996   9.291 -15.999  1.00 27.08           C  
ATOM   1120  O   ASP A 157      29.337   9.854 -15.133  1.00 25.51           O  
ATOM   1121  CB  ASP A 157      29.048   8.541 -18.259  1.00 29.28           C  
ATOM   1122  CG  ASP A 157      28.700   8.987 -19.668  1.00 34.47           C  
ATOM   1123  OD1 ASP A 157      28.170  10.107 -19.791  1.00 37.78           O  
ATOM   1124  OD2 ASP A 157      28.967   8.258 -20.655  1.00 38.12           O  
ATOM   1125  N   LEU A 158      30.981   8.459 -15.699  1.00 22.68           N  
ATOM   1126  CA  LEU A 158      31.256   8.094 -14.315  1.00 22.65           C  
ATOM   1127  C   LEU A 158      31.712   9.301 -13.510  1.00 29.28           C  
ATOM   1128  O   LEU A 158      31.294   9.504 -12.339  1.00 29.07           O  
ATOM   1129  CB  LEU A 158      32.319   6.983 -14.255  1.00 22.25           C  
ATOM   1130  CG  LEU A 158      31.825   5.623 -14.766  1.00 25.30           C  
ATOM   1131  CD1 LEU A 158      32.998   4.691 -15.034  1.00 24.51           C  
ATOM   1132  CD2 LEU A 158      30.845   4.996 -13.743  1.00 22.98           C  
ATOM   1133  N   ILE A 159      32.581  10.097 -14.131  1.00 28.83           N  
ATOM   1134  CA  ILE A 159      33.118  11.304 -13.493  1.00 28.80           C  
ATOM   1135  C   ILE A 159      31.995  12.281 -13.197  1.00 31.71           C  
ATOM   1136  O   ILE A 159      31.903  12.795 -12.089  1.00 30.93           O  
ATOM   1137  CB  ILE A 159      34.293  11.956 -14.317  1.00 31.52           C  
ATOM   1138  CG1 ILE A 159      35.551  11.080 -14.202  1.00 32.63           C  
ATOM   1139  CG2 ILE A 159      34.622  13.358 -13.772  1.00 28.89           C  
ATOM   1140  CD1 ILE A 159      36.474  11.182 -15.372  1.00 41.53           C  
ATOM   1141  N   ASP A 160      31.123  12.500 -14.179  1.00 28.65           N  
ATOM   1142  CA  ASP A 160      29.987  13.391 -13.983  1.00 29.23           C  
ATOM   1143  C   ASP A 160      29.118  12.942 -12.824  1.00 31.62           C  
ATOM   1144  O   ASP A 160      28.716  13.757 -11.976  1.00 32.02           O  
ATOM   1145  CB  ASP A 160      29.120  13.446 -15.239  1.00 32.85           C  
ATOM   1146  CG  ASP A 160      29.775  14.225 -16.350  1.00 55.06           C  
ATOM   1147  OD1 ASP A 160      30.708  15.023 -16.046  1.00 57.14           O  
ATOM   1148  OD2 ASP A 160      29.382  14.017 -17.521  1.00 64.17           O  
ATOM   1149  N   THR A 161      28.777  11.652 -12.815  1.00 26.19           N  
ATOM   1150  CA  THR A 161      27.921  11.134 -11.753  1.00 25.50           C  
ATOM   1151  C   THR A 161      28.587  11.234 -10.387  1.00 29.08           C  
ATOM   1152  O   THR A 161      27.950  11.572  -9.397  1.00 27.30           O  
ATOM   1153  CB  THR A 161      27.421   9.700 -12.073  1.00 33.02           C  
ATOM   1154  OG1 THR A 161      26.629   9.728 -13.275  1.00 31.25           O  
ATOM   1155  CG2 THR A 161      26.582   9.155 -10.916  1.00 29.22           C  
ATOM   1156  N   TRP A 162      29.885  10.945 -10.333  1.00 28.00           N  
ATOM   1157  CA  TRP A 162      30.621  11.010  -9.069  1.00 28.32           C  
ATOM   1158  C   TRP A 162      30.642  12.436  -8.518  1.00 33.73           C  
ATOM   1159  O   TRP A 162      30.325  12.682  -7.336  1.00 32.12           O  
ATOM   1160  CB  TRP A 162      32.040  10.540  -9.308  1.00 27.97           C  
ATOM   1161  CG  TRP A 162      32.936  10.637  -8.103  1.00 29.54           C  
ATOM   1162  CD1 TRP A 162      34.019  11.470  -7.939  1.00 32.22           C  
ATOM   1163  CD2 TRP A 162      32.882   9.815  -6.927  1.00 29.13           C  
ATOM   1164  NE1 TRP A 162      34.619  11.229  -6.730  1.00 31.46           N  
ATOM   1165  CE2 TRP A 162      33.951  10.215  -6.090  1.00 33.46           C  
ATOM   1166  CE3 TRP A 162      32.017   8.807  -6.483  1.00 29.31           C  
ATOM   1167  CZ2 TRP A 162      34.193   9.611  -4.839  1.00 32.25           C  
ATOM   1168  CZ3 TRP A 162      32.275   8.195  -5.261  1.00 30.15           C  
ATOM   1169  CH2 TRP A 162      33.359   8.593  -4.461  1.00 30.97           C  
ATOM   1170  N   GLU A 163      31.007  13.388  -9.372  1.00 31.97           N  
ATOM   1171  CA  GLU A 163      31.045  14.783  -8.944  1.00 32.14           C  
ATOM   1172  C   GLU A 163      29.667  15.319  -8.566  1.00 34.24           C  
ATOM   1173  O   GLU A 163      29.531  16.055  -7.607  1.00 33.87           O  
ATOM   1174  CB  GLU A 163      31.705  15.658 -10.019  1.00 33.87           C  
ATOM   1175  CG  GLU A 163      33.207  15.500 -10.026  1.00 46.39           C  
ATOM   1176  CD  GLU A 163      33.853  16.095 -11.252  1.00 75.35           C  
ATOM   1177  OE1 GLU A 163      33.114  16.645 -12.104  1.00 60.02           O  
ATOM   1178  OE2 GLU A 163      35.097  16.006 -11.357  1.00 75.66           O  
ATOM   1179  N   GLY A 164      28.639  14.943  -9.315  1.00 30.73           N  
ATOM   1180  CA  GLY A 164      27.278  15.361  -8.987  1.00 30.46           C  
ATOM   1181  C   GLY A 164      26.870  14.848  -7.591  1.00 34.93           C  
ATOM   1182  O   GLY A 164      26.241  15.549  -6.810  1.00 34.62           O  
ATOM   1183  N   THR A 165      27.247  13.615  -7.286  1.00 30.63           N  
ATOM   1184  CA  THR A 165      26.884  12.990  -6.034  1.00 29.23           C  
ATOM   1185  C   THR A 165      27.576  13.652  -4.849  1.00 32.27           C  
ATOM   1186  O   THR A 165      26.952  13.913  -3.803  1.00 29.40           O  
ATOM   1187  CB  THR A 165      27.135  11.460  -6.086  1.00 27.17           C  
ATOM   1188  OG1 THR A 165      26.331  10.882  -7.113  1.00 25.72           O  
ATOM   1189  CG2 THR A 165      26.778  10.790  -4.742  1.00 24.30           C  
ATOM   1190  N   VAL A 166      28.880  13.858  -4.997  1.00 30.23           N  
ATOM   1191  CA  VAL A 166      29.693  14.496  -3.957  1.00 30.73           C  
ATOM   1192  C   VAL A 166      29.150  15.919  -3.698  1.00 34.89           C  
ATOM   1193  O   VAL A 166      29.036  16.348  -2.556  1.00 33.51           O  
ATOM   1194  CB  VAL A 166      31.215  14.474  -4.329  1.00 35.09           C  
ATOM   1195  CG1 VAL A 166      32.026  15.320  -3.343  1.00 34.69           C  
ATOM   1196  CG2 VAL A 166      31.731  13.041  -4.359  1.00 34.46           C  
ATOM   1197  N   LYS A 167      28.732  16.602  -4.761  1.00 32.48           N  
ATOM   1198  CA  LYS A 167      28.097  17.911  -4.626  1.00 32.77           C  
ATOM   1199  C   LYS A 167      26.784  17.821  -3.834  1.00 35.62           C  
ATOM   1200  O   LYS A 167      26.560  18.608  -2.917  1.00 35.24           O  
ATOM   1201  CB  LYS A 167      27.815  18.512  -6.007  1.00 35.86           C  
ATOM   1202  CG  LYS A 167      28.036  20.016  -6.084  1.00 54.91           C  
ATOM   1203  CD  LYS A 167      26.908  20.703  -6.843  1.00 65.37           C  
ATOM   1204  N   ALA A 168      25.926  16.863  -4.186  1.00 31.93           N  
ATOM   1205  CA  ALA A 168      24.634  16.671  -3.505  1.00 31.21           C  
ATOM   1206  C   ALA A 168      24.790  16.331  -2.032  1.00 34.75           C  
ATOM   1207  O   ALA A 168      24.115  16.903  -1.175  1.00 33.40           O  
ATOM   1208  CB  ALA A 168      23.790  15.585  -4.225  1.00 31.56           C  
ATOM   1209  N   ILE A 169      25.678  15.396  -1.730  1.00 33.48           N  
ATOM   1210  CA  ILE A 169      25.892  14.989  -0.346  1.00 35.21           C  
ATOM   1211  C   ILE A 169      26.305  16.173   0.535  1.00 44.07           C  
ATOM   1212  O   ILE A 169      25.827  16.326   1.672  1.00 43.80           O  
ATOM   1213  CB  ILE A 169      26.926  13.848  -0.246  1.00 38.58           C  
ATOM   1214  CG1 ILE A 169      26.330  12.546  -0.763  1.00 39.14           C  
ATOM   1215  CG2 ILE A 169      27.342  13.629   1.193  1.00 39.91           C  
ATOM   1216  CD1 ILE A 169      27.358  11.512  -1.137  1.00 51.78           C  
ATOM   1217  N   GLY A 170      27.195  17.009   0.011  1.00 43.54           N  
ATOM   1218  CA  GLY A 170      27.716  18.143   0.768  1.00 44.16           C  
ATOM   1219  C   GLY A 170      26.811  19.367   0.830  1.00 49.58           C  
ATOM   1220  O   GLY A 170      27.034  20.269   1.628  1.00 50.81           O  
ATOM   1221  N   SER A 171      25.792  19.402  -0.009  1.00 46.05           N  
ATOM   1222  CA  SER A 171      24.890  20.550  -0.056  1.00 45.96           C  
ATOM   1223  C   SER A 171      23.474  20.280   0.494  1.00 50.43           C  
ATOM   1224  O   SER A 171      22.793  21.200   0.943  1.00 49.39           O  
ATOM   1225  CB  SER A 171      24.769  21.028  -1.508  1.00 49.53           C  
ATOM   1226  OG  SER A 171      23.652  20.415  -2.149  1.00 60.31           O  
ATOM   1227  N   THR A 172      23.011  19.035   0.378  1.00 47.84           N  
ATOM   1228  CA  THR A 172      21.654  18.642   0.798  1.00 46.25           C  
ATOM   1229  C   THR A 172      21.682  17.829   2.083  1.00 46.90           C  
ATOM   1230  O   THR A 172      22.192  16.699   2.110  1.00 45.11           O  
ATOM   1231  CB  THR A 172      20.936  17.824  -0.341  1.00 54.13           C  
ATOM   1232  OG1 THR A 172      21.318  18.320  -1.637  1.00 55.09           O  
ATOM   1233  CG2 THR A 172      19.419  17.886  -0.194  1.00 49.79           C  
ATOM   1234  N   GLY A 173      21.092  18.371   3.141  1.00 42.01           N  
ATOM   1235  CA  GLY A 173      21.023  17.637   4.403  1.00 40.69           C  
ATOM   1236  C   GLY A 173      20.062  16.431   4.324  1.00 43.50           C  
ATOM   1237  O   GLY A 173      20.194  15.466   5.088  1.00 44.20           O  
ATOM   1238  N   ALA A 174      19.107  16.474   3.389  1.00 35.55           N  
ATOM   1239  CA  ALA A 174      18.099  15.419   3.292  1.00 31.96           C  
ATOM   1240  C   ALA A 174      18.520  14.300   2.358  1.00 31.29           C  
ATOM   1241  O   ALA A 174      17.752  13.372   2.125  1.00 29.20           O  
ATOM   1242  CB  ALA A 174      16.751  16.011   2.862  1.00 32.32           C  
ATOM   1243  N   PHE A 175      19.756  14.377   1.860  1.00 25.31           N  
ATOM   1244  CA  PHE A 175      20.266  13.367   0.931  1.00 24.36           C  
ATOM   1245  C   PHE A 175      20.078  11.903   1.386  1.00 27.55           C  
ATOM   1246  O   PHE A 175      19.723  11.050   0.594  1.00 29.17           O  
ATOM   1247  CB  PHE A 175      21.735  13.655   0.591  1.00 25.66           C  
ATOM   1248  CG  PHE A 175      22.366  12.631  -0.313  1.00 26.32           C  
ATOM   1249  CD1 PHE A 175      22.951  11.487   0.211  1.00 28.30           C  
ATOM   1250  CD2 PHE A 175      22.436  12.845  -1.676  1.00 27.37           C  
ATOM   1251  CE1 PHE A 175      23.518  10.532  -0.629  1.00 28.92           C  
ATOM   1252  CE2 PHE A 175      22.988  11.895  -2.525  1.00 29.78           C  
ATOM   1253  CZ  PHE A 175      23.544  10.741  -1.996  1.00 27.85           C  
ATOM   1254  N   ASN A 176      20.327  11.640   2.657  1.00 23.53           N  
ATOM   1255  CA  ASN A 176      20.257  10.314   3.270  1.00 24.54           C  
ATOM   1256  C   ASN A 176      18.829   9.809   3.337  1.00 27.07           C  
ATOM   1257  O   ASN A 176      18.585   8.622   3.529  1.00 25.04           O  
ATOM   1258  CB  ASN A 176      20.839  10.367   4.697  1.00 26.14           C  
ATOM   1259  CG  ASN A 176      22.345  10.577   4.706  1.00 62.30           C  
ATOM   1260  OD1 ASN A 176      23.000  10.388   3.700  1.00 62.86           O  
ATOM   1261  ND2 ASN A 176      22.899  10.940   5.853  1.00 59.20           N  
ATOM   1262  N   ASP A 177      17.892  10.739   3.196  1.00 23.23           N  
ATOM   1263  CA  ASP A 177      16.468  10.439   3.215  1.00 21.79           C  
ATOM   1264  C   ASP A 177      15.968  10.303   1.777  1.00 23.05           C  
ATOM   1265  O   ASP A 177      15.538   9.223   1.366  1.00 21.20           O  
ATOM   1266  CB  ASP A 177      15.756  11.563   3.961  1.00 23.73           C  
ATOM   1267  CG  ASP A 177      14.244  11.482   3.883  1.00 27.17           C  
ATOM   1268  OD1 ASP A 177      13.661  10.547   3.272  1.00 25.37           O  
ATOM   1269  OD2 ASP A 177      13.641  12.413   4.422  1.00 32.86           O  
ATOM   1270  N   TRP A 178      16.073  11.386   1.009  1.00 19.61           N  
ATOM   1271  CA  TRP A 178      15.648  11.424  -0.400  1.00 18.64           C  
ATOM   1272  C   TRP A 178      16.296  10.397  -1.322  1.00 23.22           C  
ATOM   1273  O   TRP A 178      15.723  10.046  -2.358  1.00 23.62           O  
ATOM   1274  CB  TRP A 178      15.814  12.830  -0.987  1.00 16.61           C  
ATOM   1275  CG  TRP A 178      14.996  13.857  -0.268  1.00 17.59           C  
ATOM   1276  CD1 TRP A 178      13.988  13.633   0.666  1.00 20.10           C  
ATOM   1277  CD2 TRP A 178      15.102  15.287  -0.404  1.00 18.08           C  
ATOM   1278  NE1 TRP A 178      13.536  14.843   1.171  1.00 19.56           N  
ATOM   1279  CE2 TRP A 178      14.210  15.866   0.539  1.00 21.91           C  
ATOM   1280  CE3 TRP A 178      15.967  16.134  -1.121  1.00 19.46           C  
ATOM   1281  CZ2 TRP A 178      14.114  17.250   0.711  1.00 21.27           C  
ATOM   1282  CZ3 TRP A 178      15.850  17.503  -0.953  1.00 20.62           C  
ATOM   1283  CH2 TRP A 178      14.899  18.046  -0.084  1.00 20.95           C  
ATOM   1284  N   ILE A 179      17.475   9.906  -0.961  1.00 19.02           N  
ATOM   1285  CA  ILE A 179      18.147   8.925  -1.835  1.00 19.02           C  
ATOM   1286  C   ILE A 179      17.239   7.701  -2.055  1.00 22.39           C  
ATOM   1287  O   ILE A 179      17.324   6.999  -3.093  1.00 19.30           O  
ATOM   1288  CB  ILE A 179      19.544   8.544  -1.287  1.00 21.73           C  
ATOM   1289  CG1 ILE A 179      20.353   7.756  -2.324  1.00 22.45           C  
ATOM   1290  CG2 ILE A 179      19.407   7.735   0.007  1.00 20.33           C  
ATOM   1291  CD1 ILE A 179      20.789   8.558  -3.487  1.00 30.56           C  
ATOM   1292  N   ARG A 180      16.353   7.460  -1.079  1.00 19.43           N  
ATOM   1293  CA  ARG A 180      15.452   6.313  -1.154  1.00 19.24           C  
ATOM   1294  C   ARG A 180      14.443   6.442  -2.298  1.00 23.70           C  
ATOM   1295  O   ARG A 180      14.038   5.430  -2.849  1.00 24.16           O  
ATOM   1296  CB  ARG A 180      14.799   6.014   0.198  1.00 18.41           C  
ATOM   1297  CG  ARG A 180      15.761   5.440   1.233  1.00 19.10           C  
ATOM   1298  CD  ARG A 180      15.140   5.367   2.636  1.00 21.39           C  
ATOM   1299  NE  ARG A 180      14.645   6.686   3.068  1.00 21.00           N  
ATOM   1300  CZ  ARG A 180      14.051   6.945   4.224  1.00 26.94           C  
ATOM   1301  NH1 ARG A 180      13.867   5.992   5.120  1.00 20.79           N  
ATOM   1302  NH2 ARG A 180      13.667   8.169   4.494  1.00 17.61           N  
ATOM   1303  N   ASP A 181      14.099   7.686  -2.694  1.00 18.39           N  
ATOM   1304  CA  ASP A 181      13.179   7.920  -3.813  1.00 17.20           C  
ATOM   1305  C   ASP A 181      13.864   7.516  -5.098  1.00 20.90           C  
ATOM   1306  O   ASP A 181      13.236   7.016  -6.007  1.00 21.35           O  
ATOM   1307  CB  ASP A 181      12.793   9.413  -3.953  1.00 19.27           C  
ATOM   1308  CG  ASP A 181      12.208  10.004  -2.683  1.00 25.05           C  
ATOM   1309  OD1 ASP A 181      11.820   9.216  -1.782  1.00 27.76           O  
ATOM   1310  OD2 ASP A 181      12.134  11.261  -2.600  1.00 24.86           O  
ATOM   1311  N   PHE A 182      15.164   7.771  -5.176  1.00 17.55           N  
ATOM   1312  CA  PHE A 182      15.943   7.416  -6.347  1.00 18.47           C  
ATOM   1313  C   PHE A 182      16.203   5.901  -6.451  1.00 21.76           C  
ATOM   1314  O   PHE A 182      16.089   5.304  -7.513  1.00 22.88           O  
ATOM   1315  CB  PHE A 182      17.288   8.163  -6.296  1.00 20.37           C  
ATOM   1316  CG  PHE A 182      18.296   7.653  -7.284  1.00 22.20           C  
ATOM   1317  CD1 PHE A 182      18.249   8.061  -8.613  1.00 24.26           C  
ATOM   1318  CD2 PHE A 182      19.324   6.812  -6.878  1.00 24.54           C  
ATOM   1319  CE1 PHE A 182      19.188   7.615  -9.515  1.00 25.46           C  
ATOM   1320  CE2 PHE A 182      20.241   6.353  -7.792  1.00 27.07           C  
ATOM   1321  CZ  PHE A 182      20.183   6.772  -9.105  1.00 24.33           C  
ATOM   1322  N   TRP A 183      16.558   5.306  -5.325  1.00 17.69           N  
ATOM   1323  CA  TRP A 183      16.958   3.901  -5.199  1.00 17.86           C  
ATOM   1324  C   TRP A 183      15.825   2.909  -5.582  1.00 21.54           C  
ATOM   1325  O   TRP A 183      16.015   1.970  -6.383  1.00 22.14           O  
ATOM   1326  CB  TRP A 183      17.367   3.760  -3.718  1.00 16.81           C  
ATOM   1327  CG  TRP A 183      17.836   2.444  -3.214  1.00 18.19           C  
ATOM   1328  CD1 TRP A 183      17.945   1.251  -3.912  1.00 21.00           C  
ATOM   1329  CD2 TRP A 183      18.318   2.179  -1.887  1.00 18.01           C  
ATOM   1330  NE1 TRP A 183      18.393   0.258  -3.068  1.00 20.31           N  
ATOM   1331  CE2 TRP A 183      18.678   0.807  -1.838  1.00 22.04           C  
ATOM   1332  CE3 TRP A 183      18.497   2.974  -0.738  1.00 18.78           C  
ATOM   1333  CZ2 TRP A 183      19.148   0.195  -0.657  1.00 21.29           C  
ATOM   1334  CZ3 TRP A 183      18.991   2.377   0.423  1.00 20.44           C  
ATOM   1335  CH2 TRP A 183      19.320   1.001   0.449  1.00 21.27           C  
ATOM   1336  N   PHE A 184      14.644   3.115  -5.016  1.00 17.20           N  
ATOM   1337  CA  PHE A 184      13.514   2.243  -5.292  1.00 16.99           C  
ATOM   1338  C   PHE A 184      12.660   2.730  -6.459  1.00 20.68           C  
ATOM   1339  O   PHE A 184      11.498   3.103  -6.320  1.00 19.94           O  
ATOM   1340  CB  PHE A 184      12.732   1.971  -4.014  1.00 18.86           C  
ATOM   1341  CG  PHE A 184      13.583   1.367  -2.945  1.00 19.53           C  
ATOM   1342  CD1 PHE A 184      14.047   0.056  -3.093  1.00 20.36           C  
ATOM   1343  CD2 PHE A 184      14.105   2.167  -1.915  1.00 21.09           C  
ATOM   1344  CE1 PHE A 184      14.933  -0.503  -2.151  1.00 21.10           C  
ATOM   1345  CE2 PHE A 184      15.001   1.629  -0.992  1.00 22.97           C  
ATOM   1346  CZ  PHE A 184      15.395   0.281  -1.091  1.00 19.91           C  
ATOM   1347  N   ILE A 185      13.296   2.732  -7.619  1.00 17.86           N  
ATOM   1348  CA  ILE A 185      12.687   3.209  -8.862  1.00 18.33           C  
ATOM   1349  C   ILE A 185      11.264   2.682  -9.157  1.00 21.29           C  
ATOM   1350  O   ILE A 185      10.953   1.482  -9.009  1.00 19.10           O  
ATOM   1351  CB  ILE A 185      13.679   2.966 -10.058  1.00 20.46           C  
ATOM   1352  CG1 ILE A 185      13.199   3.689 -11.308  1.00 22.37           C  
ATOM   1353  CG2 ILE A 185      13.888   1.482 -10.294  1.00 18.57           C  
ATOM   1354  CD1 ILE A 185      14.303   3.969 -12.361  1.00 26.38           C  
ATOM   1355  N   GLY A 186      10.433   3.568  -9.694  1.00 17.19           N  
ATOM   1356  CA  GLY A 186       9.094   3.156 -10.106  1.00 17.29           C  
ATOM   1357  C   GLY A 186       8.313   2.446  -8.978  1.00 21.45           C  
ATOM   1358  O   GLY A 186       8.251   2.927  -7.829  1.00 19.51           O  
ATOM   1359  N   PRO A 187       7.709   1.312  -9.328  1.00 19.53           N  
ATOM   1360  CA  PRO A 187       6.893   0.552  -8.373  1.00 18.54           C  
ATOM   1361  C   PRO A 187       7.670  -0.279  -7.345  1.00 20.22           C  
ATOM   1362  O   PRO A 187       7.068  -0.933  -6.487  1.00 19.35           O  
ATOM   1363  CB  PRO A 187       5.985  -0.279  -9.279  1.00 18.73           C  
ATOM   1364  CG  PRO A 187       6.815  -0.485 -10.510  1.00 22.43           C  
ATOM   1365  CD  PRO A 187       7.602   0.759 -10.702  1.00 19.67           C  
ATOM   1366  N   ALA A 188       9.000  -0.198  -7.386  1.00 16.59           N  
ATOM   1367  CA  ALA A 188       9.826  -0.874  -6.383  1.00 16.65           C  
ATOM   1368  C   ALA A 188       9.548  -0.206  -5.036  1.00 20.58           C  
ATOM   1369  O   ALA A 188       9.412  -0.862  -4.018  1.00 21.06           O  
ATOM   1370  CB  ALA A 188      11.306  -0.793  -6.744  1.00 17.23           C  
ATOM   1371  N   PHE A 189       9.363   1.103  -5.051  1.00 17.71           N  
ATOM   1372  CA  PHE A 189       9.007   1.844  -3.851  1.00 18.59           C  
ATOM   1373  C   PHE A 189       7.747   1.257  -3.178  1.00 19.94           C  
ATOM   1374  O   PHE A 189       7.695   0.993  -1.981  1.00 18.67           O  
ATOM   1375  CB  PHE A 189       8.708   3.297  -4.259  1.00 21.90           C  
ATOM   1376  CG  PHE A 189       8.533   4.207  -3.106  1.00 24.98           C  
ATOM   1377  CD1 PHE A 189       9.609   4.898  -2.595  1.00 30.40           C  
ATOM   1378  CD2 PHE A 189       7.296   4.327  -2.495  1.00 29.40           C  
ATOM   1379  CE1 PHE A 189       9.439   5.730  -1.502  1.00 33.54           C  
ATOM   1380  CE2 PHE A 189       7.106   5.147  -1.405  1.00 33.49           C  
ATOM   1381  CZ  PHE A 189       8.171   5.862  -0.914  1.00 32.40           C  
ATOM   1382  N   THR A 190       6.698   1.141  -3.964  1.00 16.40           N  
ATOM   1383  CA  THR A 190       5.419   0.644  -3.506  1.00 15.96           C  
ATOM   1384  C   THR A 190       5.524  -0.741  -2.876  1.00 19.18           C  
ATOM   1385  O   THR A 190       4.837  -1.034  -1.927  1.00 19.79           O  
ATOM   1386  CB  THR A 190       4.426   0.596  -4.704  1.00 19.30           C  
ATOM   1387  OG1 THR A 190       4.454   1.857  -5.390  1.00 16.25           O  
ATOM   1388  CG2 THR A 190       2.994   0.281  -4.242  1.00 14.91           C  
ATOM   1389  N   ALA A 191       6.320  -1.615  -3.477  1.00 17.05           N  
ATOM   1390  CA  ALA A 191       6.461  -2.997  -3.032  1.00 16.65           C  
ATOM   1391  C   ALA A 191       7.000  -3.105  -1.606  1.00 20.41           C  
ATOM   1392  O   ALA A 191       6.726  -4.076  -0.915  1.00 21.20           O  
ATOM   1393  CB  ALA A 191       7.335  -3.822  -4.043  1.00 16.69           C  
ATOM   1394  N   LEU A 192       7.783  -2.121  -1.177  1.00 15.73           N  
ATOM   1395  CA  LEU A 192       8.300  -2.116   0.202  1.00 14.19           C  
ATOM   1396  C   LEU A 192       7.164  -2.296   1.226  1.00 19.49           C  
ATOM   1397  O   LEU A 192       7.171  -3.221   2.000  1.00 21.12           O  
ATOM   1398  CB  LEU A 192       9.102  -0.842   0.487  1.00 12.41           C  
ATOM   1399  CG  LEU A 192      10.426  -0.665  -0.249  1.00 15.41           C  
ATOM   1400  CD1 LEU A 192      10.989   0.749  -0.017  1.00 14.95           C  
ATOM   1401  CD2 LEU A 192      11.421  -1.741   0.237  1.00 15.66           C  
ATOM   1402  N   ASN A 193       6.203  -1.386   1.252  1.00 15.98           N  
ATOM   1403  CA  ASN A 193       5.088  -1.489   2.206  1.00 16.08           C  
ATOM   1404  C   ASN A 193       4.278  -2.792   2.061  1.00 18.83           C  
ATOM   1405  O   ASN A 193       3.831  -3.377   3.033  1.00 18.47           O  
ATOM   1406  CB  ASN A 193       4.127  -0.311   2.009  1.00 17.44           C  
ATOM   1407  CG  ASN A 193       3.003  -0.321   3.012  1.00 32.96           C  
ATOM   1408  OD1 ASN A 193       3.205  -0.002   4.184  1.00 32.38           O  
ATOM   1409  ND2 ASN A 193       1.825  -0.754   2.582  1.00 27.37           N  
ATOM   1410  N   GLU A 194       4.062  -3.205   0.821  1.00 14.09           N  
ATOM   1411  CA  GLU A 194       3.302  -4.394   0.519  1.00 14.45           C  
ATOM   1412  C   GLU A 194       3.859  -5.613   1.227  1.00 20.07           C  
ATOM   1413  O   GLU A 194       3.098  -6.525   1.597  1.00 18.02           O  
ATOM   1414  CB  GLU A 194       3.322  -4.616  -0.997  1.00 15.99           C  
ATOM   1415  CG  GLU A 194       2.185  -5.455  -1.521  1.00 26.98           C  
ATOM   1416  CD  GLU A 194       0.837  -4.746  -1.443  1.00 47.69           C  
ATOM   1417  OE1 GLU A 194       0.792  -3.500  -1.387  1.00 40.07           O  
ATOM   1418  OE2 GLU A 194      -0.179  -5.449  -1.390  1.00 48.49           O  
ATOM   1419  N   GLY A 195       5.189  -5.662   1.392  1.00 14.96           N  
ATOM   1420  CA  GLY A 195       5.777  -6.839   2.036  1.00 14.74           C  
ATOM   1421  C   GLY A 195       6.078  -6.598   3.527  1.00 19.65           C  
ATOM   1422  O   GLY A 195       6.749  -7.403   4.160  1.00 19.79           O  
ATOM   1423  N   GLY A 196       5.599  -5.486   4.092  1.00 14.78           N  
ATOM   1424  CA  GLY A 196       5.885  -5.202   5.504  1.00 14.05           C  
ATOM   1425  C   GLY A 196       7.396  -4.910   5.691  1.00 20.31           C  
ATOM   1426  O   GLY A 196       8.019  -5.281   6.693  1.00 19.28           O  
ATOM   1427  N   GLN A 197       7.976  -4.241   4.702  1.00 17.88           N  
ATOM   1428  CA  GLN A 197       9.380  -3.980   4.713  1.00 17.66           C  
ATOM   1429  C   GLN A 197       9.695  -2.477   4.806  1.00 20.89           C  
ATOM   1430  O   GLN A 197       9.010  -1.663   4.191  1.00 20.10           O  
ATOM   1431  CB  GLN A 197       9.963  -4.629   3.469  1.00 19.45           C  
ATOM   1432  CG  GLN A 197      11.476  -4.639   3.397  1.00 24.83           C  
ATOM   1433  CD  GLN A 197      11.988  -5.459   2.237  1.00 32.39           C  
ATOM   1434  OE1 GLN A 197      11.239  -5.841   1.344  1.00 25.15           O  
ATOM   1435  NE2 GLN A 197      13.272  -5.741   2.251  1.00 25.49           N  
ATOM   1436  N   ARG A 198      10.719  -2.128   5.591  1.00 17.81           N  
ATOM   1437  CA  ARG A 198      11.153  -0.739   5.777  1.00 18.33           C  
ATOM   1438  C   ARG A 198      12.658  -0.608   5.526  1.00 21.14           C  
ATOM   1439  O   ARG A 198      13.444  -1.408   6.015  1.00 21.62           O  
ATOM   1440  CB  ARG A 198      10.904  -0.267   7.256  1.00 19.92           C  
ATOM   1441  CG  ARG A 198       9.480  -0.231   7.723  1.00 29.55           C  
ATOM   1442  CD  ARG A 198       9.407  -0.090   9.255  1.00 36.35           C  
ATOM   1443  NE  ARG A 198       9.733   1.269   9.620  1.00 30.08           N  
ATOM   1444  CZ  ARG A 198       9.992   1.717  10.836  1.00 29.77           C  
ATOM   1445  NH1 ARG A 198       9.940   0.956  11.909  1.00 18.53           N  
ATOM   1446  NH2 ARG A 198      10.271   2.976  10.970  1.00 22.14           N  
ATOM   1447  N   ILE A 199      13.055   0.484   4.887  1.00 18.64           N  
ATOM   1448  CA  ILE A 199      14.467   0.801   4.655  1.00 18.65           C  
ATOM   1449  C   ILE A 199      14.798   2.070   5.445  1.00 22.85           C  
ATOM   1450  O   ILE A 199      14.113   3.076   5.279  1.00 22.66           O  
ATOM   1451  CB  ILE A 199      14.738   1.067   3.177  1.00 20.92           C  
ATOM   1452  CG1 ILE A 199      14.259  -0.108   2.318  1.00 21.42           C  
ATOM   1453  CG2 ILE A 199      16.228   1.299   2.974  1.00 21.85           C  
ATOM   1454  CD1 ILE A 199      15.035  -1.386   2.516  1.00 25.45           C  
ATOM   1455  N   SER A 200      15.849   2.055   6.275  1.00 18.98           N  
ATOM   1456  CA  SER A 200      16.216   3.260   7.049  1.00 17.92           C  
ATOM   1457  C   SER A 200      16.898   4.304   6.160  1.00 22.39           C  
ATOM   1458  O   SER A 200      17.278   4.019   5.033  1.00 20.46           O  
ATOM   1459  CB  SER A 200      17.220   2.889   8.132  1.00 20.05           C  
ATOM   1460  OG  SER A 200      18.452   2.536   7.529  1.00 21.76           O  
ATOM   1461  N   ARG A 201      17.167   5.484   6.712  1.00 22.02           N  
ATOM   1462  CA  ARG A 201      17.973   6.457   5.987  1.00 21.61           C  
ATOM   1463  C   ARG A 201      19.335   5.818   5.886  1.00 24.72           C  
ATOM   1464  O   ARG A 201      19.655   4.949   6.687  1.00 22.33           O  
ATOM   1465  CB  ARG A 201      18.105   7.719   6.803  1.00 20.70           C  
ATOM   1466  CG  ARG A 201      16.802   8.483   6.887  1.00 28.60           C  
ATOM   1467  CD  ARG A 201      16.874   9.536   7.964  1.00 35.12           C  
ATOM   1468  NE  ARG A 201      15.591  10.224   8.088  1.00 53.61           N  
ATOM   1469  CZ  ARG A 201      15.422  11.537   7.945  1.00 70.46           C  
ATOM   1470  NH1 ARG A 201      16.462  12.324   7.647  1.00 51.38           N  
ATOM   1471  NH2 ARG A 201      14.208  12.057   8.109  1.00 57.77           N  
ATOM   1472  N   ILE A 202      20.127   6.186   4.886  1.00 23.16           N  
ATOM   1473  CA  ILE A 202      21.460   5.616   4.808  1.00 23.50           C  
ATOM   1474  C   ILE A 202      22.414   6.434   5.658  1.00 28.49           C  
ATOM   1475  O   ILE A 202      22.126   7.569   6.014  1.00 27.80           O  
ATOM   1476  CB  ILE A 202      21.987   5.489   3.363  1.00 26.57           C  
ATOM   1477  CG1 ILE A 202      22.310   6.860   2.786  1.00 26.92           C  
ATOM   1478  CG2 ILE A 202      21.009   4.679   2.475  1.00 26.30           C  
ATOM   1479  CD1 ILE A 202      23.215   6.791   1.591  1.00 32.14           C  
ATOM   1480  N   GLU A 203      23.550   5.840   5.990  1.00 25.89           N  
ATOM   1481  CA  GLU A 203      24.605   6.534   6.695  1.00 25.39           C  
ATOM   1482  C   GLU A 203      25.830   6.481   5.780  1.00 28.81           C  
ATOM   1483  O   GLU A 203      26.222   5.416   5.272  1.00 27.17           O  
ATOM   1484  CB  GLU A 203      24.853   5.913   8.079  1.00 26.63           C  
ATOM   1485  CG  GLU A 203      26.308   6.025   8.568  1.00 46.71           C  
ATOM   1486  CD  GLU A 203      26.493   5.631  10.049  1.00 78.10           C  
ATOM   1487  OE1 GLU A 203      26.925   6.496  10.846  1.00 89.72           O  
ATOM   1488  OE2 GLU A 203      26.260   4.451  10.410  1.00 64.25           O  
ATOM   1489  N   VAL A 204      26.355   7.653   5.454  1.00 27.55           N  
ATOM   1490  CA  VAL A 204      27.541   7.741   4.594  1.00 26.98           C  
ATOM   1491  C   VAL A 204      28.787   7.890   5.484  1.00 31.65           C  
ATOM   1492  O   VAL A 204      28.999   8.942   6.058  1.00 33.16           O  
ATOM   1493  CB  VAL A 204      27.413   8.913   3.603  1.00 29.08           C  
ATOM   1494  CG1 VAL A 204      28.638   8.988   2.734  1.00 28.73           C  
ATOM   1495  CG2 VAL A 204      26.174   8.752   2.729  1.00 28.56           C  
ATOM   1496  N   ASN A 205      29.589   6.842   5.617  1.00 28.41           N  
ATOM   1497  CA  ASN A 205      30.772   6.874   6.467  1.00 29.28           C  
ATOM   1498  C   ASN A 205      32.033   7.370   5.802  1.00 35.97           C  
ATOM   1499  O   ASN A 205      32.969   7.782   6.476  1.00 36.15           O  
ATOM   1500  CB  ASN A 205      31.034   5.515   7.142  1.00 31.23           C  
ATOM   1501  CG  ASN A 205      29.792   4.957   7.861  1.00 59.95           C  
ATOM   1502  OD1 ASN A 205      29.402   3.812   7.650  1.00 65.26           O  
ATOM   1503  ND2 ASN A 205      29.160   5.779   8.682  1.00 45.45           N  
ATOM   1504  N   GLY A 206      32.056   7.370   4.480  1.00 34.06           N  
ATOM   1505  CA  GLY A 206      33.223   7.868   3.749  1.00 33.35           C  
ATOM   1506  C   GLY A 206      33.026   7.842   2.243  1.00 35.33           C  
ATOM   1507  O   GLY A 206      32.455   6.903   1.698  1.00 35.34           O  
ATOM   1508  N   LEU A 207      33.519   8.884   1.591  1.00 31.39           N  
ATOM   1509  CA  LEU A 207      33.484   9.049   0.140  1.00 32.00           C  
ATOM   1510  C   LEU A 207      34.878   9.566  -0.250  1.00 35.35           C  
ATOM   1511  O   LEU A 207      35.252  10.644   0.138  1.00 35.02           O  
ATOM   1512  CB  LEU A 207      32.449  10.115  -0.237  1.00 32.96           C  
ATOM   1513  CG  LEU A 207      31.078   9.816  -0.830  1.00 39.48           C  
ATOM   1514  CD1 LEU A 207      30.950  10.591  -2.124  1.00 41.12           C  
ATOM   1515  CD2 LEU A 207      30.902   8.343  -1.092  1.00 43.03           C  
ATOM   1516  N   ASN A 208      35.645   8.790  -1.013  1.00 30.86           N  
ATOM   1517  CA  ASN A 208      36.997   9.189  -1.410  1.00 29.78           C  
ATOM   1518  C   ASN A 208      37.336   8.818  -2.837  1.00 33.53           C  
ATOM   1519  O   ASN A 208      36.875   7.812  -3.348  1.00 32.13           O  
ATOM   1520  CB  ASN A 208      38.042   8.504  -0.514  1.00 26.35           C  
ATOM   1521  CG  ASN A 208      38.031   9.037   0.893  1.00 42.67           C  
ATOM   1522  OD1 ASN A 208      38.420  10.171   1.140  1.00 45.37           O  
ATOM   1523  ND2 ASN A 208      37.535   8.242   1.817  1.00 29.24           N  
ATOM   1524  N   THR A 209      38.200   9.616  -3.447  1.00 32.02           N  
ATOM   1525  CA  THR A 209      38.763   9.314  -4.747  1.00 33.38           C  
ATOM   1526  C   THR A 209      40.174   8.815  -4.432  1.00 41.90           C  
ATOM   1527  O   THR A 209      40.953   9.524  -3.800  1.00 42.56           O  
ATOM   1528  CB  THR A 209      38.823  10.551  -5.637  1.00 38.75           C  
ATOM   1529  OG1 THR A 209      37.531  11.147  -5.678  1.00 38.47           O  
ATOM   1530  CG2 THR A 209      39.171  10.152  -7.034  1.00 39.55           C  
ATOM   1531  N   GLU A 210      40.450   7.560  -4.767  1.00 40.36           N  
ATOM   1532  CA  GLU A 210      41.758   6.953  -4.550  1.00 41.02           C  
ATOM   1533  C   GLU A 210      42.521   6.967  -5.864  1.00 50.41           C  
ATOM   1534  O   GLU A 210      41.936   7.078  -6.935  1.00 48.32           O  
ATOM   1535  CB  GLU A 210      41.600   5.486  -4.156  1.00 41.77           C  
ATOM   1536  CG  GLU A 210      41.479   5.212  -2.681  1.00 48.84           C  
ATOM   1537  CD  GLU A 210      41.491   3.731  -2.367  1.00 68.93           C  
ATOM   1538  OE1 GLU A 210      41.223   3.377  -1.202  1.00 59.30           O  
ATOM   1539  OE2 GLU A 210      41.768   2.920  -3.282  1.00 62.94           O  
ATOM   1540  N   SER A 211      43.831   6.795  -5.789  1.00 54.43           N  
ATOM   1541  CA  SER A 211      44.613   6.706  -7.011  1.00 57.17           C  
ATOM   1542  C   SER A 211      44.905   5.243  -7.262  1.00 66.32           C  
ATOM   1543  O   SER A 211      45.669   4.618  -6.526  1.00 67.66           O  
ATOM   1544  CB  SER A 211      45.881   7.548  -6.939  1.00 61.80           C  
ATOM   1545  OG  SER A 211      45.630   8.825  -7.519  1.00 74.82           O  
ATOM   1546  N   GLY A 212      44.201   4.672  -8.235  1.00 63.68           N  
ATOM   1547  CA  GLY A 212      44.346   3.262  -8.548  1.00 63.50           C  
ATOM   1548  C   GLY A 212      45.516   3.023  -9.492  1.00 66.66           C  
ATOM   1549  O   GLY A 212      46.095   3.966 -10.056  1.00 66.36           O  
ATOM   1550  N   PRO A 213      45.854   1.749  -9.658  1.00 61.63           N  
ATOM   1551  CA  PRO A 213      46.941   1.355 -10.549  1.00 61.34           C  
ATOM   1552  C   PRO A 213      46.714   1.989 -11.906  1.00 65.50           C  
ATOM   1553  O   PRO A 213      47.623   2.558 -12.507  1.00 66.57           O  
ATOM   1554  CB  PRO A 213      46.769  -0.164 -10.657  1.00 62.77           C  
ATOM   1555  CG  PRO A 213      45.316  -0.395 -10.388  1.00 66.87           C  
ATOM   1556  CD  PRO A 213      44.950   0.626  -9.352  1.00 62.34           C  
ATOM   1557  N   LYS A 214      45.476   1.911 -12.367  1.00 60.56           N  
ATOM   1558  CA  LYS A 214      45.124   2.443 -13.665  1.00 59.32           C  
ATOM   1559  C   LYS A 214      44.349   3.771 -13.717  1.00 59.92           C  
ATOM   1560  O   LYS A 214      43.870   4.145 -14.786  1.00 60.56           O  
ATOM   1561  CB  LYS A 214      44.382   1.377 -14.480  1.00 62.28           C  
ATOM   1562  N   GLY A 215      44.215   4.484 -12.599  1.00 50.77           N  
ATOM   1563  CA  GLY A 215      43.457   5.746 -12.620  1.00 47.35           C  
ATOM   1564  C   GLY A 215      42.650   5.992 -11.339  1.00 43.06           C  
ATOM   1565  O   GLY A 215      42.682   5.177 -10.407  1.00 42.27           O  
ATOM   1566  N   PRO A 216      41.956   7.127 -11.285  1.00 35.27           N  
ATOM   1567  CA  PRO A 216      41.132   7.474 -10.114  1.00 34.38           C  
ATOM   1568  C   PRO A 216      40.010   6.457  -9.871  1.00 37.47           C  
ATOM   1569  O   PRO A 216      39.423   5.915 -10.805  1.00 36.84           O  
ATOM   1570  CB  PRO A 216      40.543   8.835 -10.475  1.00 36.16           C  
ATOM   1571  CG  PRO A 216      40.579   8.868 -12.001  1.00 40.81           C  
ATOM   1572  CD  PRO A 216      41.729   8.016 -12.443  1.00 35.82           C  
ATOM   1573  N   VAL A 217      39.744   6.173  -8.599  1.00 32.84           N  
ATOM   1574  CA  VAL A 217      38.704   5.228  -8.216  1.00 30.54           C  
ATOM   1575  C   VAL A 217      37.816   5.935  -7.217  1.00 33.12           C  
ATOM   1576  O   VAL A 217      38.332   6.588  -6.290  1.00 31.25           O  
ATOM   1577  CB  VAL A 217      39.305   3.992  -7.573  1.00 33.68           C  
ATOM   1578  CG1 VAL A 217      38.193   3.004  -7.195  1.00 32.88           C  
ATOM   1579  CG2 VAL A 217      40.349   3.364  -8.489  1.00 33.23           C  
ATOM   1580  N   GLY A 218      36.496   5.822  -7.404  1.00 28.41           N  
ATOM   1581  CA  GLY A 218      35.541   6.418  -6.456  1.00 27.72           C  
ATOM   1582  C   GLY A 218      35.257   5.353  -5.406  1.00 29.58           C  
ATOM   1583  O   GLY A 218      34.820   4.279  -5.741  1.00 30.43           O  
ATOM   1584  N   VAL A 219      35.585   5.632  -4.154  1.00 24.91           N  
ATOM   1585  CA  VAL A 219      35.425   4.696  -3.050  1.00 24.30           C  
ATOM   1586  C   VAL A 219      34.382   5.210  -2.082  1.00 27.46           C  
ATOM   1587  O   VAL A 219      34.474   6.346  -1.638  1.00 25.89           O  
ATOM   1588  CB  VAL A 219      36.783   4.514  -2.269  1.00 27.66           C  
ATOM   1589  CG1 VAL A 219      36.651   3.401  -1.179  1.00 26.32           C  
ATOM   1590  CG2 VAL A 219      37.888   4.183  -3.247  1.00 27.62           C  
ATOM   1591  N   SER A 220      33.438   4.347  -1.691  1.00 25.37           N  
ATOM   1592  CA  SER A 220      32.403   4.754  -0.734  1.00 25.60           C  
ATOM   1593  C   SER A 220      32.131   3.686   0.286  1.00 28.15           C  
ATOM   1594  O   SER A 220      32.240   2.481   0.009  1.00 26.45           O  
ATOM   1595  CB  SER A 220      31.112   5.199  -1.443  1.00 29.88           C  
ATOM   1596  OG  SER A 220      30.581   4.157  -2.225  1.00 35.61           O  
ATOM   1597  N   ARG A 221      31.844   4.145   1.493  1.00 25.28           N  
ATOM   1598  CA  ARG A 221      31.600   3.268   2.621  1.00 25.50           C  
ATOM   1599  C   ARG A 221      30.288   3.753   3.252  1.00 28.10           C  
ATOM   1600  O   ARG A 221      30.180   4.896   3.677  1.00 25.33           O  
ATOM   1601  CB  ARG A 221      32.744   3.377   3.643  1.00 25.47           C  
ATOM   1602  CG  ARG A 221      32.476   2.595   4.923  1.00 28.73           C  
ATOM   1603  CD  ARG A 221      32.611   1.096   4.676  1.00 41.58           C  
ATOM   1604  NE  ARG A 221      32.527   0.324   5.907  1.00 58.81           N  
ATOM   1605  CZ  ARG A 221      33.544   0.121   6.735  1.00 76.34           C  
ATOM   1606  NH1 ARG A 221      34.741   0.614   6.445  1.00 66.76           N  
ATOM   1607  NH2 ARG A 221      33.364  -0.574   7.853  1.00 55.45           N  
ATOM   1608  N   TRP A 222      29.273   2.903   3.239  1.00 23.84           N  
ATOM   1609  CA  TRP A 222      27.963   3.321   3.722  1.00 22.92           C  
ATOM   1610  C   TRP A 222      27.207   2.164   4.335  1.00 24.19           C  
ATOM   1611  O   TRP A 222      27.529   0.995   4.132  1.00 21.24           O  
ATOM   1612  CB  TRP A 222      27.124   3.914   2.577  1.00 21.10           C  
ATOM   1613  CG  TRP A 222      26.952   3.003   1.379  1.00 21.78           C  
ATOM   1614  CD1 TRP A 222      27.913   2.619   0.501  1.00 24.33           C  
ATOM   1615  CD2 TRP A 222      25.717   2.405   0.914  1.00 21.44           C  
ATOM   1616  NE1 TRP A 222      27.361   1.816  -0.478  1.00 23.65           N  
ATOM   1617  CE2 TRP A 222      26.009   1.718  -0.279  1.00 24.85           C  
ATOM   1618  CE3 TRP A 222      24.406   2.384   1.398  1.00 22.01           C  
ATOM   1619  CZ2 TRP A 222      25.041   0.978  -0.979  1.00 23.89           C  
ATOM   1620  CZ3 TRP A 222      23.444   1.695   0.673  1.00 23.44           C  
ATOM   1621  CH2 TRP A 222      23.773   0.979  -0.487  1.00 23.82           C  
ATOM   1622  N   ARG A 223      26.187   2.512   5.089  1.00 21.80           N  
ATOM   1623  CA  ARG A 223      25.374   1.503   5.753  1.00 22.99           C  
ATOM   1624  C   ARG A 223      23.883   1.851   5.684  1.00 23.73           C  
ATOM   1625  O   ARG A 223      23.501   3.015   5.562  1.00 22.29           O  
ATOM   1626  CB  ARG A 223      25.746   1.392   7.236  1.00 23.57           C  
ATOM   1627  CG  ARG A 223      27.192   1.554   7.565  1.00 37.55           C  
ATOM   1628  CD  ARG A 223      27.330   1.715   9.058  1.00 53.09           C  
ATOM   1629  NE  ARG A 223      28.531   1.054   9.554  1.00 79.51           N  
ATOM   1630  CZ  ARG A 223      28.974   1.162  10.803  1.00103.40           C  
ATOM   1631  NH1 ARG A 223      28.301   1.896  11.683  1.00 89.94           N  
ATOM   1632  NH2 ARG A 223      30.086   0.536  11.173  1.00 94.61           N  
ATOM   1633  N   PHE A 224      23.062   0.829   5.871  1.00 18.38           N  
ATOM   1634  CA  PHE A 224      21.621   1.006   6.016  1.00 17.92           C  
ATOM   1635  C   PHE A 224      21.086  -0.218   6.753  1.00 23.07           C  
ATOM   1636  O   PHE A 224      21.763  -1.267   6.801  1.00 22.35           O  
ATOM   1637  CB  PHE A 224      20.932   1.184   4.644  1.00 18.19           C  
ATOM   1638  CG  PHE A 224      20.794  -0.094   3.833  1.00 19.12           C  
ATOM   1639  CD1 PHE A 224      19.647  -0.870   3.934  1.00 20.92           C  
ATOM   1640  CD2 PHE A 224      21.789  -0.463   2.904  1.00 20.48           C  
ATOM   1641  CE1 PHE A 224      19.504  -2.032   3.160  1.00 21.98           C  
ATOM   1642  CE2 PHE A 224      21.676  -1.593   2.132  1.00 23.24           C  
ATOM   1643  CZ  PHE A 224      20.511  -2.392   2.233  1.00 22.03           C  
ATOM   1644  N   SER A 225      19.904  -0.088   7.355  1.00 19.13           N  
ATOM   1645  CA  SER A 225      19.226  -1.251   7.965  1.00 18.29           C  
ATOM   1646  C   SER A 225      17.866  -1.447   7.267  1.00 23.96           C  
ATOM   1647  O   SER A 225      17.324  -0.548   6.636  1.00 22.11           O  
ATOM   1648  CB  SER A 225      19.042  -1.108   9.478  1.00 19.90           C  
ATOM   1649  OG  SER A 225      18.114  -0.084   9.812  1.00 25.03           O  
ATOM   1650  N   HIS A 226      17.357  -2.661   7.325  1.00 23.10           N  
ATOM   1651  CA  HIS A 226      16.061  -2.951   6.784  1.00 22.82           C  
ATOM   1652  C   HIS A 226      15.251  -3.822   7.747  1.00 24.77           C  
ATOM   1653  O   HIS A 226      15.737  -4.840   8.231  1.00 24.25           O  
ATOM   1654  CB  HIS A 226      16.110  -3.360   5.296  1.00 23.73           C  
ATOM   1655  CG  HIS A 226      16.132  -4.832   5.027  1.00 26.69           C  
ATOM   1656  ND1 HIS A 226      15.034  -5.500   4.524  1.00 27.83           N  
ATOM   1657  CD2 HIS A 226      17.166  -5.702   4.950  1.00 28.65           C  
ATOM   1658  CE1 HIS A 226      15.368  -6.751   4.263  1.00 27.23           C  
ATOM   1659  NE2 HIS A 226      16.660  -6.897   4.499  1.00 27.82           N  
ATOM   1660  N   GLY A 227      14.080  -3.311   8.132  1.00 18.21           N  
ATOM   1661  CA  GLY A 227      13.178  -3.994   9.059  1.00 17.37           C  
ATOM   1662  C   GLY A 227      12.118  -4.815   8.296  1.00 21.89           C  
ATOM   1663  O   GLY A 227      11.789  -4.532   7.134  1.00 20.56           O  
ATOM   1664  N   GLY A 228      11.568  -5.832   8.965  1.00 17.35           N  
ATOM   1665  CA  GLY A 228      10.566  -6.686   8.346  1.00 16.15           C  
ATOM   1666  C   GLY A 228       9.621  -7.116   9.460  1.00 20.74           C  
ATOM   1667  O   GLY A 228      10.033  -7.432  10.579  1.00 19.93           O  
ATOM   1668  N   SER A 229       8.338  -7.097   9.163  1.00 16.75           N  
ATOM   1669  CA  SER A 229       7.319  -7.455  10.154  1.00 15.07           C  
ATOM   1670  C   SER A 229       7.076  -8.979  10.191  1.00 18.08           C  
ATOM   1671  O   SER A 229       6.262  -9.459  10.936  1.00 18.92           O  
ATOM   1672  CB  SER A 229       6.031  -6.649   9.896  1.00 15.88           C  
ATOM   1673  OG  SER A 229       5.391  -7.043   8.683  1.00 17.38           O  
ATOM   1674  N   GLY A 230       7.804  -9.757   9.393  1.00 15.09           N  
ATOM   1675  CA  GLY A 230       7.637 -11.207   9.481  1.00 13.71           C  
ATOM   1676  C   GLY A 230       7.462 -11.951   8.168  1.00 20.89           C  
ATOM   1677  O   GLY A 230       7.607 -13.175   8.136  1.00 22.06           O  
ATOM   1678  N   MET A 231       7.093 -11.238   7.101  1.00 17.81           N  
ATOM   1679  CA  MET A 231       6.956 -11.852   5.763  1.00 17.02           C  
ATOM   1680  C   MET A 231       8.252 -11.717   4.959  1.00 20.59           C  
ATOM   1681  O   MET A 231       8.402 -12.350   3.925  1.00 20.95           O  
ATOM   1682  CB  MET A 231       5.830 -11.192   4.952  1.00 18.75           C  
ATOM   1683  CG  MET A 231       4.493 -11.178   5.635  1.00 22.02           C  
ATOM   1684  SD  MET A 231       3.170 -10.646   4.494  1.00 25.81           S  
ATOM   1685  CE  MET A 231       3.513  -8.932   4.367  1.00 20.75           C  
ATOM   1686  N   VAL A 232       9.180 -10.873   5.405  1.00 17.15           N  
ATOM   1687  CA  VAL A 232      10.444 -10.679   4.650  1.00 16.83           C  
ATOM   1688  C   VAL A 232      11.358 -11.910   4.848  1.00 21.25           C  
ATOM   1689  O   VAL A 232      12.007 -12.052   5.890  1.00 21.95           O  
ATOM   1690  CB  VAL A 232      11.153  -9.354   5.050  1.00 18.98           C  
ATOM   1691  CG1 VAL A 232      12.309  -9.081   4.146  1.00 17.75           C  
ATOM   1692  CG2 VAL A 232      10.161  -8.188   4.998  1.00 19.78           C  
ATOM   1693  N   ASP A 233      11.359 -12.826   3.880  1.00 15.61           N  
ATOM   1694  CA  ASP A 233      12.135 -14.054   4.031  1.00 14.39           C  
ATOM   1695  C   ASP A 233      13.625 -13.816   4.246  1.00 19.30           C  
ATOM   1696  O   ASP A 233      14.299 -14.601   4.901  1.00 18.39           O  
ATOM   1697  CB  ASP A 233      11.906 -15.017   2.863  1.00 14.75           C  
ATOM   1698  CG  ASP A 233      10.478 -14.980   2.351  1.00 16.64           C  
ATOM   1699  OD1 ASP A 233       9.584 -15.663   2.906  1.00 20.85           O  
ATOM   1700  OD2 ASP A 233      10.227 -14.179   1.452  1.00 18.10           O  
ATOM   1701  N   SER A 234      14.136 -12.737   3.675  1.00 15.59           N  
ATOM   1702  CA  SER A 234      15.540 -12.398   3.832  1.00 15.22           C  
ATOM   1703  C   SER A 234      15.889 -12.297   5.297  1.00 21.40           C  
ATOM   1704  O   SER A 234      17.027 -12.502   5.674  1.00 23.65           O  
ATOM   1705  CB  SER A 234      15.814 -11.055   3.158  1.00 18.01           C  
ATOM   1706  OG  SER A 234      16.090 -11.274   1.791  1.00 29.80           O  
ATOM   1707  N   ILE A 235      14.914 -11.901   6.104  1.00 18.40           N  
ATOM   1708  CA  ILE A 235      15.119 -11.719   7.535  1.00 17.72           C  
ATOM   1709  C   ILE A 235      14.654 -12.935   8.355  1.00 22.84           C  
ATOM   1710  O   ILE A 235      15.379 -13.472   9.178  1.00 21.52           O  
ATOM   1711  CB  ILE A 235      14.415 -10.454   8.034  1.00 19.37           C  
ATOM   1712  CG1 ILE A 235      15.108  -9.197   7.477  1.00 19.60           C  
ATOM   1713  CG2 ILE A 235      14.416 -10.445   9.547  1.00 18.48           C  
ATOM   1714  CD1 ILE A 235      14.348  -7.903   7.752  1.00 23.98           C  
ATOM   1715  N   SER A 236      13.419 -13.353   8.134  1.00 20.36           N  
ATOM   1716  CA  SER A 236      12.856 -14.451   8.915  1.00 20.61           C  
ATOM   1717  C   SER A 236      13.471 -15.821   8.616  1.00 24.96           C  
ATOM   1718  O   SER A 236      13.353 -16.723   9.415  1.00 26.44           O  
ATOM   1719  CB  SER A 236      11.355 -14.518   8.691  1.00 20.34           C  
ATOM   1720  OG  SER A 236      11.143 -14.954   7.377  1.00 24.95           O  
ATOM   1721  N   ARG A 237      14.100 -15.986   7.463  1.00 19.84           N  
ATOM   1722  CA  ARG A 237      14.661 -17.288   7.088  1.00 18.94           C  
ATOM   1723  C   ARG A 237      16.125 -17.162   6.688  1.00 20.49           C  
ATOM   1724  O   ARG A 237      16.621 -17.849   5.789  1.00 19.13           O  
ATOM   1725  CB  ARG A 237      13.812 -17.885   5.972  1.00 18.46           C  
ATOM   1726  CG  ARG A 237      12.403 -18.214   6.522  1.00 24.76           C  
ATOM   1727  CD  ARG A 237      11.430 -18.555   5.458  1.00 19.25           C  
ATOM   1728  NE  ARG A 237      11.677 -19.914   4.987  1.00 22.40           N  
ATOM   1729  CZ  ARG A 237      10.973 -20.491   4.021  1.00 30.79           C  
ATOM   1730  NH1 ARG A 237       9.979 -19.836   3.449  1.00 17.19           N  
ATOM   1731  NH2 ARG A 237      11.247 -21.714   3.643  1.00 20.07           N  
ATOM   1732  N   TRP A 238      16.772 -16.217   7.358  1.00 17.41           N  
ATOM   1733  CA  TRP A 238      18.178 -15.892   7.196  1.00 18.19           C  
ATOM   1734  C   TRP A 238      19.107 -17.113   7.023  1.00 21.83           C  
ATOM   1735  O   TRP A 238      19.925 -17.148   6.095  1.00 20.65           O  
ATOM   1736  CB  TRP A 238      18.602 -15.082   8.418  1.00 17.19           C  
ATOM   1737  CG  TRP A 238      20.061 -14.770   8.479  1.00 18.78           C  
ATOM   1738  CD1 TRP A 238      20.973 -15.229   9.413  1.00 21.26           C  
ATOM   1739  CD2 TRP A 238      20.783 -13.862   7.627  1.00 18.98           C  
ATOM   1740  NE1 TRP A 238      22.203 -14.671   9.177  1.00 20.28           N  
ATOM   1741  CE2 TRP A 238      22.123 -13.829   8.095  1.00 21.98           C  
ATOM   1742  CE3 TRP A 238      20.427 -13.071   6.512  1.00 20.06           C  
ATOM   1743  CZ2 TRP A 238      23.105 -13.034   7.501  1.00 21.03           C  
ATOM   1744  CZ3 TRP A 238      21.420 -12.277   5.920  1.00 20.94           C  
ATOM   1745  CH2 TRP A 238      22.742 -12.269   6.427  1.00 21.07           C  
ATOM   1746  N   ALA A 239      19.010 -18.095   7.916  1.00 18.62           N  
ATOM   1747  CA  ALA A 239      19.903 -19.257   7.819  1.00 19.95           C  
ATOM   1748  C   ALA A 239      19.523 -20.183   6.691  1.00 24.60           C  
ATOM   1749  O   ALA A 239      20.366 -20.611   5.895  1.00 24.19           O  
ATOM   1750  CB  ALA A 239      19.970 -20.036   9.140  1.00 19.81           C  
ATOM   1751  N   GLU A 240      18.234 -20.478   6.613  1.00 20.12           N  
ATOM   1752  CA  GLU A 240      17.720 -21.406   5.601  1.00 17.97           C  
ATOM   1753  C   GLU A 240      17.940 -20.971   4.131  1.00 23.52           C  
ATOM   1754  O   GLU A 240      18.088 -21.811   3.230  1.00 23.91           O  
ATOM   1755  CB  GLU A 240      16.249 -21.708   5.908  1.00 18.32           C  
ATOM   1756  CG  GLU A 240      15.545 -22.557   4.855  1.00 23.57           C  
ATOM   1757  CD  GLU A 240      14.046 -22.714   5.120  1.00 34.16           C  
ATOM   1758  OE1 GLU A 240      13.504 -22.016   5.991  1.00 26.42           O  
ATOM   1759  OE2 GLU A 240      13.405 -23.564   4.485  1.00 30.51           O  
ATOM   1760  N   LEU A 241      17.945 -19.661   3.863  1.00 19.57           N  
ATOM   1761  CA  LEU A 241      18.131 -19.193   2.471  1.00 18.76           C  
ATOM   1762  C   LEU A 241      19.581 -19.328   1.962  1.00 23.21           C  
ATOM   1763  O   LEU A 241      19.843 -19.078   0.789  1.00 22.37           O  
ATOM   1764  CB  LEU A 241      17.646 -17.738   2.309  1.00 18.50           C  
ATOM   1765  CG  LEU A 241      18.356 -16.648   3.137  1.00 21.37           C  
ATOM   1766  CD1 LEU A 241      19.718 -16.255   2.559  1.00 19.55           C  
ATOM   1767  CD2 LEU A 241      17.442 -15.408   3.377  1.00 21.55           C  
ATOM   1768  N   PHE A 242      20.521 -19.637   2.854  1.00 21.61           N  
ATOM   1769  CA  PHE A 242      21.935 -19.820   2.487  1.00 21.77           C  
ATOM   1770  C   PHE A 242      22.427 -21.166   3.066  1.00 25.69           C  
ATOM   1771  O   PHE A 242      23.088 -21.199   4.108  1.00 24.27           O  
ATOM   1772  CB  PHE A 242      22.774 -18.690   3.069  1.00 23.32           C  
ATOM   1773  CG  PHE A 242      24.245 -18.777   2.739  1.00 24.54           C  
ATOM   1774  CD1 PHE A 242      24.677 -18.973   1.428  1.00 27.01           C  
ATOM   1775  CD2 PHE A 242      25.206 -18.603   3.743  1.00 25.65           C  
ATOM   1776  CE1 PHE A 242      26.028 -19.014   1.132  1.00 26.79           C  
ATOM   1777  CE2 PHE A 242      26.542 -18.654   3.457  1.00 27.10           C  
ATOM   1778  CZ  PHE A 242      26.963 -18.846   2.157  1.00 25.30           C  
ATOM   1779  N   PRO A 243      22.020 -22.268   2.442  1.00 20.98           N  
ATOM   1780  CA  PRO A 243      22.416 -23.608   2.935  1.00 21.67           C  
ATOM   1781  C   PRO A 243      23.867 -23.969   2.521  1.00 27.08           C  
ATOM   1782  O   PRO A 243      24.080 -24.935   1.785  1.00 25.07           O  
ATOM   1783  CB  PRO A 243      21.410 -24.553   2.246  1.00 22.08           C  
ATOM   1784  CG  PRO A 243      21.094 -23.856   0.953  1.00 25.34           C  
ATOM   1785  CD  PRO A 243      21.217 -22.342   1.209  1.00 20.54           C  
ATOM   1786  N   SER A 244      24.849 -23.171   2.962  1.00 24.60           N  
ATOM   1787  CA  SER A 244      26.246 -23.425   2.575  1.00 24.95           C  
ATOM   1788  C   SER A 244      26.738 -24.815   3.051  1.00 30.42           C  
ATOM   1789  O   SER A 244      27.452 -25.492   2.349  1.00 31.52           O  
ATOM   1790  CB  SER A 244      27.162 -22.289   3.051  1.00 27.03           C  
ATOM   1791  OG  SER A 244      27.142 -22.132   4.457  1.00 32.85           O  
ATOM   1792  N   ASP A 245      26.254 -25.264   4.200  1.00 26.56           N  
ATOM   1793  CA  ASP A 245      26.646 -26.549   4.776  1.00 27.79           C  
ATOM   1794  C   ASP A 245      26.157 -27.759   3.992  1.00 32.51           C  
ATOM   1795  O   ASP A 245      26.611 -28.870   4.228  1.00 33.51           O  
ATOM   1796  CB  ASP A 245      26.218 -26.668   6.262  1.00 30.44           C  
ATOM   1797  CG  ASP A 245      24.715 -26.522   6.461  1.00 55.18           C  
ATOM   1798  OD1 ASP A 245      24.042 -25.765   5.708  1.00 56.94           O  
ATOM   1799  OD2 ASP A 245      24.204 -27.138   7.419  1.00 71.89           O  
ATOM   1800  N   LYS A 246      25.231 -27.568   3.064  1.00 26.99           N  
ATOM   1801  CA  LYS A 246      24.719 -28.699   2.316  1.00 25.40           C  
ATOM   1802  C   LYS A 246      25.260 -28.677   0.896  1.00 29.13           C  
ATOM   1803  O   LYS A 246      24.946 -29.528   0.059  1.00 28.48           O  
ATOM   1804  CB  LYS A 246      23.197 -28.676   2.305  1.00 28.30           C  
ATOM   1805  CG  LYS A 246      22.581 -28.958   3.681  1.00 39.63           C  
ATOM   1806  CD  LYS A 246      21.190 -28.355   3.812  1.00 46.81           C  
ATOM   1807  N   LEU A 247      26.085 -27.683   0.611  1.00 25.46           N  
ATOM   1808  CA  LEU A 247      26.605 -27.557  -0.724  1.00 23.57           C  
ATOM   1809  C   LEU A 247      27.855 -28.404  -0.919  1.00 30.89           C  
ATOM   1810  O   LEU A 247      28.949 -27.878  -0.887  1.00 30.65           O  
ATOM   1811  CB  LEU A 247      26.842 -26.087  -1.086  1.00 22.02           C  
ATOM   1812  CG  LEU A 247      27.072 -25.883  -2.598  1.00 25.14           C  
ATOM   1813  CD1 LEU A 247      25.764 -25.894  -3.370  1.00 24.83           C  
ATOM   1814  CD2 LEU A 247      27.905 -24.636  -2.881  1.00 24.96           C  
ATOM   1815  N   ASN A 248      27.681 -29.704  -1.174  1.00 30.84           N  
ATOM   1816  CA  ASN A 248      28.819 -30.625  -1.364  1.00 32.25           C  
ATOM   1817  C   ASN A 248      29.328 -30.671  -2.818  1.00 38.02           C  
ATOM   1818  O   ASN A 248      30.322 -31.311  -3.109  1.00 39.41           O  
ATOM   1819  CB  ASN A 248      28.474 -32.043  -0.876  1.00 28.76           C  
ATOM   1820  CG  ASN A 248      27.225 -32.593  -1.544  1.00 55.59           C  
ATOM   1821  OD1 ASN A 248      26.256 -31.868  -1.770  1.00 43.44           O  
ATOM   1822  ND2 ASN A 248      27.258 -33.868  -1.907  1.00 58.68           N  
ATOM   1823  N   ARG A 249      28.619 -30.022  -3.729  1.00 32.14           N  
ATOM   1824  CA  ARG A 249      29.014 -29.951  -5.147  1.00 30.26           C  
ATOM   1825  C   ARG A 249      28.327 -28.705  -5.740  1.00 31.85           C  
ATOM   1826  O   ARG A 249      27.452 -28.117  -5.105  1.00 30.74           O  
ATOM   1827  CB  ARG A 249      28.552 -31.197  -5.908  1.00 26.13           C  
ATOM   1828  CG  ARG A 249      27.229 -31.683  -5.455  1.00 35.28           C  
ATOM   1829  CD  ARG A 249      26.646 -32.670  -6.411  1.00 40.98           C  
ATOM   1830  NE  ARG A 249      25.335 -33.145  -5.963  1.00 42.63           N  
ATOM   1831  CZ  ARG A 249      24.250 -33.091  -6.719  1.00 53.32           C  
ATOM   1832  NH1 ARG A 249      24.312 -32.578  -7.941  1.00 39.10           N  
ATOM   1833  NH2 ARG A 249      23.104 -33.525  -6.254  1.00 37.84           N  
ATOM   1834  N   PRO A 250      28.717 -28.307  -6.949  1.00 27.48           N  
ATOM   1835  CA  PRO A 250      28.147 -27.111  -7.575  1.00 26.77           C  
ATOM   1836  C   PRO A 250      26.639 -27.185  -7.827  1.00 31.28           C  
ATOM   1837  O   PRO A 250      26.117 -28.242  -8.207  1.00 31.06           O  
ATOM   1838  CB  PRO A 250      28.880 -27.039  -8.931  1.00 28.35           C  
ATOM   1839  CG  PRO A 250      30.101 -27.881  -8.773  1.00 32.43           C  
ATOM   1840  CD  PRO A 250      29.682 -28.983  -7.843  1.00 28.52           C  
ATOM   1841  N   ALA A 251      25.938 -26.071  -7.593  1.00 26.39           N  
ATOM   1842  CA  ALA A 251      24.498 -25.976  -7.853  1.00 25.87           C  
ATOM   1843  C   ALA A 251      24.308 -24.888  -8.899  1.00 31.40           C  
ATOM   1844  O   ALA A 251      25.155 -24.014  -9.057  1.00 30.65           O  
ATOM   1845  CB  ALA A 251      23.734 -25.620  -6.590  1.00 25.89           C  
ATOM   1846  N   GLN A 252      23.207 -24.935  -9.632  1.00 28.88           N  
ATOM   1847  CA  GLN A 252      22.958 -23.903 -10.633  1.00 28.22           C  
ATOM   1848  C   GLN A 252      21.489 -23.757 -11.014  1.00 30.35           C  
ATOM   1849  O   GLN A 252      20.696 -24.677 -10.835  1.00 29.28           O  
ATOM   1850  CB  GLN A 252      23.801 -24.146 -11.884  1.00 29.31           C  
ATOM   1851  CG  GLN A 252      23.383 -25.380 -12.687  1.00 40.29           C  
ATOM   1852  N   VAL A 253      21.146 -22.587 -11.550  1.00 27.04           N  
ATOM   1853  CA  VAL A 253      19.786 -22.301 -12.049  1.00 25.69           C  
ATOM   1854  C   VAL A 253      19.908 -21.476 -13.322  1.00 26.47           C  
ATOM   1855  O   VAL A 253      20.686 -20.521 -13.393  1.00 25.36           O  
ATOM   1856  CB  VAL A 253      18.897 -21.497 -11.062  1.00 29.67           C  
ATOM   1857  CG1 VAL A 253      17.452 -21.614 -11.476  1.00 29.24           C  
ATOM   1858  CG2 VAL A 253      19.054 -21.979  -9.672  1.00 30.47           C  
ATOM   1859  N   GLU A 254      19.142 -21.858 -14.325  1.00 20.36           N  
ATOM   1860  CA  GLU A 254      19.030 -21.101 -15.543  1.00 22.15           C  
ATOM   1861  C   GLU A 254      17.528 -20.764 -15.668  1.00 26.15           C  
ATOM   1862  O   GLU A 254      16.651 -21.610 -15.445  1.00 24.19           O  
ATOM   1863  CB  GLU A 254      19.462 -21.922 -16.747  1.00 24.45           C  
ATOM   1864  CG  GLU A 254      19.803 -21.064 -17.967  1.00 40.42           C  
ATOM   1865  N   ALA A 255      17.232 -19.519 -15.983  1.00 22.37           N  
ATOM   1866  CA  ALA A 255      15.844 -19.100 -16.075  1.00 22.48           C  
ATOM   1867  C   ALA A 255      15.765 -17.961 -17.089  1.00 28.55           C  
ATOM   1868  O   ALA A 255      16.749 -17.245 -17.306  1.00 29.72           O  
ATOM   1869  CB  ALA A 255      15.343 -18.626 -14.675  1.00 22.31           C  
ATOM   1870  N   GLY A 256      14.609 -17.782 -17.707  1.00 23.36           N  
ATOM   1871  CA  GLY A 256      14.456 -16.677 -18.616  1.00 22.43           C  
ATOM   1872  C   GLY A 256      12.992 -16.487 -18.967  1.00 25.67           C  
ATOM   1873  O   GLY A 256      12.195 -17.402 -18.829  1.00 26.21           O  
ATOM   1874  N   PHE A 257      12.660 -15.309 -19.479  1.00 19.10           N  
ATOM   1875  CA  PHE A 257      11.315 -15.021 -19.954  1.00 18.08           C  
ATOM   1876  C   PHE A 257      11.358 -14.162 -21.219  1.00 21.30           C  
ATOM   1877  O   PHE A 257      12.326 -13.464 -21.486  1.00 21.18           O  
ATOM   1878  CB  PHE A 257      10.427 -14.367 -18.849  1.00 18.85           C  
ATOM   1879  CG  PHE A 257      10.863 -12.966 -18.452  1.00 18.97           C  
ATOM   1880  CD1 PHE A 257      10.513 -11.860 -19.237  1.00 21.44           C  
ATOM   1881  CD2 PHE A 257      11.590 -12.752 -17.290  1.00 18.23           C  
ATOM   1882  CE1 PHE A 257      10.882 -10.553 -18.867  1.00 22.03           C  
ATOM   1883  CE2 PHE A 257      11.978 -11.454 -16.928  1.00 22.45           C  
ATOM   1884  CZ  PHE A 257      11.600 -10.350 -17.710  1.00 20.84           C  
ATOM   1885  N   ARG A 258      10.313 -14.258 -22.018  1.00 18.96           N  
ATOM   1886  CA  ARG A 258      10.167 -13.442 -23.226  1.00 19.15           C  
ATOM   1887  C   ARG A 258       8.805 -12.801 -23.050  1.00 23.73           C  
ATOM   1888  O   ARG A 258       7.856 -13.458 -22.608  1.00 23.03           O  
ATOM   1889  CB  ARG A 258      10.133 -14.309 -24.488  1.00 20.32           C  
ATOM   1890  CG  ARG A 258      11.408 -15.118 -24.744  1.00 31.50           C  
ATOM   1891  CD  ARG A 258      12.600 -14.188 -24.886  1.00 40.40           C  
ATOM   1892  NE  ARG A 258      13.857 -14.916 -25.048  1.00 48.51           N  
ATOM   1893  CZ  ARG A 258      14.712 -15.193 -24.063  1.00 56.82           C  
ATOM   1894  NH1 ARG A 258      14.462 -14.812 -22.820  1.00 33.12           N  
ATOM   1895  NH2 ARG A 258      15.827 -15.857 -24.323  1.00 48.15           N  
ATOM   1896  N   SER A 259       8.683 -11.514 -23.342  1.00 20.79           N  
ATOM   1897  CA  SER A 259       7.370 -10.928 -23.165  1.00 19.99           C  
ATOM   1898  C   SER A 259       7.161  -9.755 -24.093  1.00 24.34           C  
ATOM   1899  O   SER A 259       8.117  -9.082 -24.510  1.00 22.90           O  
ATOM   1900  CB  SER A 259       7.114 -10.522 -21.688  1.00 21.57           C  
ATOM   1901  OG  SER A 259       7.788  -9.304 -21.329  1.00 18.01           O  
ATOM   1902  N   ASP A 260       5.896  -9.561 -24.447  1.00 20.40           N  
ATOM   1903  CA  ASP A 260       5.471  -8.437 -25.264  1.00 19.67           C  
ATOM   1904  C   ASP A 260       3.985  -8.188 -25.006  1.00 23.32           C  
ATOM   1905  O   ASP A 260       3.408  -8.717 -24.062  1.00 22.28           O  
ATOM   1906  CB  ASP A 260       5.745  -8.652 -26.754  1.00 21.40           C  
ATOM   1907  CG  ASP A 260       5.101  -9.904 -27.312  1.00 26.62           C  
ATOM   1908  OD1 ASP A 260       4.080 -10.400 -26.798  1.00 29.12           O  
ATOM   1909  OD2 ASP A 260       5.567 -10.334 -28.358  1.00 39.01           O  
ATOM   1910  N   SER A 261       3.371  -7.389 -25.863  1.00 21.63           N  
ATOM   1911  CA  SER A 261       1.971  -7.011 -25.725  1.00 21.69           C  
ATOM   1912  C   SER A 261       1.002  -8.187 -25.829  1.00 26.62           C  
ATOM   1913  O   SER A 261      -0.146  -8.045 -25.466  1.00 26.64           O  
ATOM   1914  CB  SER A 261       1.622  -5.927 -26.751  1.00 23.77           C  
ATOM   1915  OG  SER A 261       1.423  -6.498 -28.040  1.00 37.90           O  
ATOM   1916  N   GLN A 262       1.468  -9.338 -26.313  1.00 23.64           N  
ATOM   1917  CA  GLN A 262       0.610 -10.509 -26.474  1.00 23.32           C  
ATOM   1918  C   GLN A 262       0.652 -11.500 -25.289  1.00 30.02           C  
ATOM   1919  O   GLN A 262      -0.299 -12.232 -25.062  1.00 31.61           O  
ATOM   1920  CB  GLN A 262       1.014 -11.271 -27.759  1.00 24.09           C  
ATOM   1921  CG  GLN A 262       0.881 -10.468 -29.053  1.00 46.71           C  
ATOM   1922  N   GLY A 263       1.778 -11.599 -24.587  1.00 25.85           N  
ATOM   1923  CA  GLY A 263       1.861 -12.595 -23.520  1.00 23.79           C  
ATOM   1924  C   GLY A 263       3.241 -12.719 -22.918  1.00 24.58           C  
ATOM   1925  O   GLY A 263       4.145 -11.915 -23.210  1.00 21.84           O  
ATOM   1926  N   ILE A 264       3.362 -13.690 -22.016  1.00 21.65           N  
ATOM   1927  CA  ILE A 264       4.590 -13.914 -21.270  1.00 21.62           C  
ATOM   1928  C   ILE A 264       4.899 -15.386 -21.380  1.00 25.23           C  
ATOM   1929  O   ILE A 264       4.009 -16.214 -21.267  1.00 25.21           O  
ATOM   1930  CB  ILE A 264       4.381 -13.546 -19.755  1.00 23.98           C  
ATOM   1931  CG1 ILE A 264       3.975 -12.092 -19.595  1.00 23.59           C  
ATOM   1932  CG2 ILE A 264       5.629 -13.873 -18.892  1.00 21.45           C  
ATOM   1933  CD1 ILE A 264       3.296 -11.807 -18.253  1.00 27.22           C  
ATOM   1934  N   GLU A 265       6.170 -15.708 -21.521  1.00 21.17           N  
ATOM   1935  CA  GLU A 265       6.591 -17.108 -21.576  1.00 20.46           C  
ATOM   1936  C   GLU A 265       7.812 -17.250 -20.690  1.00 22.85           C  
ATOM   1937  O   GLU A 265       8.717 -16.423 -20.732  1.00 22.54           O  
ATOM   1938  CB  GLU A 265       6.937 -17.467 -22.994  1.00 22.08           C  
ATOM   1939  CG  GLU A 265       6.851 -18.911 -23.283  1.00 44.44           C  
ATOM   1940  CD  GLU A 265       7.394 -19.195 -24.647  1.00 76.30           C  
ATOM   1941  OE1 GLU A 265       7.254 -18.290 -25.509  1.00 55.85           O  
ATOM   1942  OE2 GLU A 265       8.026 -20.264 -24.821  1.00 75.09           O  
ATOM   1943  N   VAL A 266       7.816 -18.255 -19.835  1.00 19.86           N  
ATOM   1944  CA  VAL A 266       8.901 -18.384 -18.888  1.00 19.87           C  
ATOM   1945  C   VAL A 266       9.410 -19.810 -18.805  1.00 24.21           C  
ATOM   1946  O   VAL A 266       8.651 -20.750 -18.996  1.00 24.13           O  
ATOM   1947  CB  VAL A 266       8.531 -17.705 -17.495  1.00 23.72           C  
ATOM   1948  CG1 VAL A 266       7.211 -18.106 -17.039  1.00 24.52           C  
ATOM   1949  CG2 VAL A 266       9.553 -17.995 -16.408  1.00 23.19           C  
ATOM   1950  N   LYS A 267      10.705 -19.961 -18.537  1.00 21.06           N  
ATOM   1951  CA  LYS A 267      11.292 -21.272 -18.337  1.00 21.18           C  
ATOM   1952  C   LYS A 267      12.329 -21.251 -17.225  1.00 24.25           C  
ATOM   1953  O   LYS A 267      13.091 -20.296 -17.096  1.00 24.98           O  
ATOM   1954  CB  LYS A 267      11.831 -21.870 -19.659  1.00 24.86           C  
ATOM   1955  CG  LYS A 267      13.165 -21.398 -20.112  1.00 44.32           C  
ATOM   1956  N   VAL A 268      12.323 -22.284 -16.385  1.00 19.43           N  
ATOM   1957  CA  VAL A 268      13.292 -22.376 -15.290  1.00 19.03           C  
ATOM   1958  C   VAL A 268      13.815 -23.818 -15.221  1.00 25.52           C  
ATOM   1959  O   VAL A 268      13.037 -24.778 -15.331  1.00 26.40           O  
ATOM   1960  CB  VAL A 268      12.633 -22.050 -13.941  1.00 21.34           C  
ATOM   1961  CG1 VAL A 268      13.563 -22.424 -12.802  1.00 19.40           C  
ATOM   1962  CG2 VAL A 268      12.206 -20.598 -13.880  1.00 22.17           C  
ATOM   1963  N   ASP A 269      15.091 -23.962 -14.898  1.00 21.47           N  
ATOM   1964  CA  ASP A 269      15.706 -25.276 -14.711  1.00 20.93           C  
ATOM   1965  C   ASP A 269      16.811 -25.099 -13.728  1.00 22.89           C  
ATOM   1966  O   ASP A 269      17.743 -24.308 -13.985  1.00 21.95           O  
ATOM   1967  CB  ASP A 269      16.349 -25.749 -16.004  1.00 24.15           C  
ATOM   1968  CG  ASP A 269      15.349 -26.270 -16.958  1.00 46.95           C  
ATOM   1969  OD1 ASP A 269      14.764 -27.319 -16.647  1.00 51.28           O  
ATOM   1970  OD2 ASP A 269      15.090 -25.604 -17.982  1.00 57.53           O  
ATOM   1971  N   GLY A 270      16.763 -25.845 -12.625  1.00 18.80           N  
ATOM   1972  CA  GLY A 270      17.853 -25.726 -11.662  1.00 19.47           C  
ATOM   1973  C   GLY A 270      18.008 -26.969 -10.826  1.00 26.69           C  
ATOM   1974  O   GLY A 270      17.131 -27.824 -10.836  1.00 26.35           O  
ATOM   1975  N   GLU A 271      19.090 -27.011 -10.040  1.00 24.41           N  
ATOM   1976  CA  GLU A 271      19.364 -28.082  -9.092  1.00 23.41           C  
ATOM   1977  C   GLU A 271      20.169 -27.453  -7.961  1.00 26.18           C  
ATOM   1978  O   GLU A 271      21.150 -26.768  -8.201  1.00 26.00           O  
ATOM   1979  CB  GLU A 271      20.203 -29.178  -9.740  1.00 24.51           C  
ATOM   1980  CG  GLU A 271      20.386 -30.353  -8.803  1.00 31.82           C  
ATOM   1981  CD  GLU A 271      21.320 -31.448  -9.344  1.00 42.31           C  
ATOM   1982  OE1 GLU A 271      21.888 -31.276 -10.432  1.00 50.15           O  
ATOM   1983  OE2 GLU A 271      21.487 -32.487  -8.666  1.00 39.64           O  
ATOM   1984  N   PHE A 272      19.735 -27.643  -6.722  1.00 22.70           N  
ATOM   1985  CA  PHE A 272      20.432 -27.019  -5.598  1.00 21.92           C  
ATOM   1986  C   PHE A 272      19.889 -27.676  -4.345  1.00 23.51           C  
ATOM   1987  O   PHE A 272      18.880 -28.352  -4.388  1.00 22.03           O  
ATOM   1988  CB  PHE A 272      20.167 -25.489  -5.566  1.00 22.94           C  
ATOM   1989  CG  PHE A 272      18.732 -25.128  -5.883  1.00 24.22           C  
ATOM   1990  CD1 PHE A 272      17.739 -25.259  -4.919  1.00 26.61           C  
ATOM   1991  CD2 PHE A 272      18.362 -24.824  -7.191  1.00 26.22           C  
ATOM   1992  CE1 PHE A 272      16.412 -25.031  -5.243  1.00 28.56           C  
ATOM   1993  CE2 PHE A 272      17.038 -24.600  -7.537  1.00 29.57           C  
ATOM   1994  CZ  PHE A 272      16.057 -24.700  -6.567  1.00 28.31           C  
ATOM   1995  N   PRO A 273      20.592 -27.506  -3.242  1.00 21.83           N  
ATOM   1996  CA  PRO A 273      20.149 -28.038  -1.969  1.00 22.59           C  
ATOM   1997  C   PRO A 273      19.098 -27.081  -1.321  1.00 29.72           C  
ATOM   1998  O   PRO A 273      18.945 -25.921  -1.760  1.00 28.19           O  
ATOM   1999  CB  PRO A 273      21.433 -28.009  -1.141  1.00 23.03           C  
ATOM   2000  CG  PRO A 273      22.187 -26.850  -1.673  1.00 25.83           C  
ATOM   2001  CD  PRO A 273      21.940 -26.911  -3.153  1.00 22.63           C  
ATOM   2002  N   GLY A 274      18.416 -27.561  -0.272  1.00 26.36           N  
ATOM   2003  CA  GLY A 274      17.440 -26.757   0.471  1.00 25.77           C  
ATOM   2004  C   GLY A 274      15.988 -26.922   0.041  1.00 28.44           C  
ATOM   2005  O   GLY A 274      15.115 -26.221   0.533  1.00 28.54           O  
ATOM   2006  N   VAL A 275      15.723 -27.827  -0.894  1.00 24.48           N  
ATOM   2007  CA  VAL A 275      14.363 -28.021  -1.387  1.00 24.33           C  
ATOM   2008  C   VAL A 275      13.468 -28.765  -0.381  1.00 27.91           C  
ATOM   2009  O   VAL A 275      12.253 -28.528  -0.325  1.00 25.77           O  
ATOM   2010  CB  VAL A 275      14.353 -28.688  -2.766  1.00 29.08           C  
ATOM   2011  CG1 VAL A 275      12.942 -28.765  -3.286  1.00 29.40           C  
ATOM   2012  CG2 VAL A 275      15.199 -27.906  -3.737  1.00 29.23           C  
ATOM   2013  N   SER A 276      14.065 -29.627   0.444  1.00 23.43           N  
ATOM   2014  CA  SER A 276      13.296 -30.356   1.446  1.00 22.34           C  
ATOM   2015  C   SER A 276      13.984 -30.126   2.784  1.00 28.37           C  
ATOM   2016  O   SER A 276      15.159 -29.776   2.820  1.00 27.38           O  
ATOM   2017  CB  SER A 276      13.223 -31.844   1.116  1.00 23.86           C  
ATOM   2018  OG  SER A 276      14.499 -32.443   1.175  1.00 29.94           O  
ATOM   2019  N   VAL A 277      13.228 -30.253   3.871  1.00 25.37           N  
ATOM   2020  CA  VAL A 277      13.754 -29.987   5.183  1.00 27.20           C  
ATOM   2021  C   VAL A 277      13.143 -30.946   6.171  1.00 32.67           C  
ATOM   2022  O   VAL A 277      12.097 -31.516   5.938  1.00 32.14           O  
ATOM   2023  CB  VAL A 277      13.516 -28.476   5.608  1.00 33.61           C  
ATOM   2024  CG1 VAL A 277      13.899 -27.550   4.455  1.00 34.80           C  
ATOM   2025  CG2 VAL A 277      12.068 -28.223   5.976  1.00 32.66           C  
ATOM   2026  N   ASP A 278      13.843 -31.141   7.272  1.00 32.52           N  
ATOM   2027  CA  ASP A 278      13.406 -32.020   8.343  1.00 33.58           C  
ATOM   2028  C   ASP A 278      12.164 -31.366   8.918  1.00 37.89           C  
ATOM   2029  O   ASP A 278      12.192 -30.186   9.215  1.00 39.62           O  
ATOM   2030  CB  ASP A 278      14.520 -32.031   9.404  1.00 35.67           C  
ATOM   2031  CG  ASP A 278      14.258 -33.002  10.551  1.00 47.95           C  
ATOM   2032  OD1 ASP A 278      13.184 -33.642  10.621  1.00 45.58           O  
ATOM   2033  OD2 ASP A 278      15.173 -33.148  11.385  1.00 62.70           O  
ATOM   2034  N   ALA A 279      11.077 -32.107   9.071  1.00 33.39           N  
ATOM   2035  CA  ALA A 279       9.862 -31.521   9.634  1.00 32.92           C  
ATOM   2036  C   ALA A 279       9.655 -32.075  11.012  1.00 40.55           C  
ATOM   2037  O   ALA A 279       8.625 -31.822  11.633  1.00 42.66           O  
ATOM   2038  CB  ALA A 279       8.620 -31.848   8.762  1.00 33.52           C  
ATOM   2039  N   GLY A 280      10.591 -32.907  11.457  1.00 36.88           N  
ATOM   2040  CA  GLY A 280      10.505 -33.536  12.765  1.00 37.39           C  
ATOM   2041  C   GLY A 280       9.626 -34.793  12.730  1.00 45.24           C  
ATOM   2042  O   GLY A 280       8.822 -34.981  11.810  1.00 45.40           O  
ATOM   2043  N   GLY A 281       9.809 -35.656  13.736  1.00 42.67           N  
ATOM   2044  CA  GLY A 281       9.016 -36.883  13.894  1.00 41.52           C  
ATOM   2045  C   GLY A 281       9.357 -37.942  12.861  1.00 43.75           C  
ATOM   2046  O   GLY A 281       8.596 -38.897  12.651  1.00 43.34           O  
ATOM   2047  N   GLY A 282      10.514 -37.773  12.223  1.00 39.27           N  
ATOM   2048  CA  GLY A 282      10.935 -38.658  11.133  1.00 38.17           C  
ATOM   2049  C   GLY A 282      10.379 -38.188   9.763  1.00 41.09           C  
ATOM   2050  O   GLY A 282      10.638 -38.822   8.737  1.00 41.45           O  
ATOM   2051  N   LEU A 283       9.627 -37.081   9.748  1.00 34.00           N  
ATOM   2052  CA  LEU A 283       9.043 -36.578   8.510  1.00 32.17           C  
ATOM   2053  C   LEU A 283       9.890 -35.510   7.832  1.00 33.22           C  
ATOM   2054  O   LEU A 283      10.631 -34.777   8.472  1.00 32.92           O  
ATOM   2055  CB  LEU A 283       7.635 -36.019   8.758  1.00 32.25           C  
ATOM   2056  CG  LEU A 283       6.519 -36.951   9.241  1.00 36.59           C  
ATOM   2057  CD1 LEU A 283       5.351 -36.111   9.767  1.00 36.39           C  
ATOM   2058  CD2 LEU A 283       6.063 -37.871   8.097  1.00 37.15           C  
ATOM   2059  N   ARG A 284       9.719 -35.368   6.527  1.00 27.79           N  
ATOM   2060  CA  ARG A 284      10.384 -34.291   5.810  1.00 26.64           C  
ATOM   2061  C   ARG A 284       9.287 -33.512   5.089  1.00 28.83           C  
ATOM   2062  O   ARG A 284       8.229 -34.075   4.803  1.00 28.83           O  
ATOM   2063  CB  ARG A 284      11.369 -34.883   4.798  1.00 25.40           C  
ATOM   2064  CG  ARG A 284      12.694 -35.357   5.405  1.00 27.70           C  
ATOM   2065  CD  ARG A 284      13.758 -35.615   4.322  1.00 33.07           C  
ATOM   2066  NE  ARG A 284      14.449 -34.399   3.861  1.00 32.21           N  
ATOM   2067  CZ  ARG A 284      15.385 -33.740   4.547  1.00 35.29           C  
ATOM   2068  NH1 ARG A 284      15.784 -34.166   5.727  1.00 26.03           N  
ATOM   2069  NH2 ARG A 284      15.946 -32.653   4.048  1.00 23.51           N  
ATOM   2070  N   ARG A 285       9.520 -32.233   4.789  1.00 23.20           N  
ATOM   2071  CA  ARG A 285       8.544 -31.466   3.999  1.00 22.52           C  
ATOM   2072  C   ARG A 285       9.258 -30.767   2.854  1.00 24.56           C  
ATOM   2073  O   ARG A 285      10.452 -30.529   2.939  1.00 22.96           O  
ATOM   2074  CB  ARG A 285       7.859 -30.399   4.847  1.00 19.84           C  
ATOM   2075  CG  ARG A 285       8.825 -29.326   5.397  1.00 24.19           C  
ATOM   2076  CD  ARG A 285       8.049 -28.055   5.831  1.00 35.24           C  
ATOM   2077  NE  ARG A 285       6.864 -28.398   6.637  1.00 31.69           N  
ATOM   2078  CZ  ARG A 285       6.906 -28.449   7.946  1.00 38.77           C  
ATOM   2079  NH1 ARG A 285       8.035 -28.150   8.563  1.00 46.63           N  
ATOM   2080  NH2 ARG A 285       5.853 -28.819   8.630  1.00 25.58           N  
ATOM   2081  N   ILE A 286       8.525 -30.390   1.808  1.00 20.90           N  
ATOM   2082  CA  ILE A 286       9.097 -29.493   0.794  1.00 20.38           C  
ATOM   2083  C   ILE A 286       9.182 -28.150   1.583  1.00 21.87           C  
ATOM   2084  O   ILE A 286       8.309 -27.857   2.403  1.00 19.48           O  
ATOM   2085  CB  ILE A 286       8.144 -29.331  -0.388  1.00 23.01           C  
ATOM   2086  CG1 ILE A 286       7.839 -30.692  -1.027  1.00 23.95           C  
ATOM   2087  CG2 ILE A 286       8.702 -28.323  -1.379  1.00 20.60           C  
ATOM   2088  CD1 ILE A 286       8.989 -31.256  -1.857  1.00 26.19           C  
ATOM   2089  N   LEU A 287      10.207 -27.337   1.378  1.00 19.28           N  
ATOM   2090  CA  LEU A 287      10.294 -26.109   2.196  1.00 18.89           C  
ATOM   2091  C   LEU A 287       9.060 -25.191   2.136  1.00 23.75           C  
ATOM   2092  O   LEU A 287       8.364 -25.148   1.127  1.00 22.86           O  
ATOM   2093  CB  LEU A 287      11.576 -25.324   1.901  1.00 17.96           C  
ATOM   2094  CG  LEU A 287      11.523 -24.385   0.689  1.00 20.70           C  
ATOM   2095  CD1 LEU A 287      12.753 -23.542   0.645  1.00 20.40           C  
ATOM   2096  CD2 LEU A 287      11.367 -25.168  -0.614  1.00 21.00           C  
ATOM   2097  N   ASN A 288       8.780 -24.478   3.225  1.00 19.27           N  
ATOM   2098  CA  ASN A 288       7.661 -23.532   3.232  1.00 19.93           C  
ATOM   2099  C   ASN A 288       7.854 -22.530   2.071  1.00 21.88           C  
ATOM   2100  O   ASN A 288       8.965 -22.054   1.843  1.00 18.28           O  
ATOM   2101  CB  ASN A 288       7.654 -22.758   4.556  1.00 15.65           C  
ATOM   2102  CG  ASN A 288       7.362 -23.662   5.758  1.00 26.46           C  
ATOM   2103  OD1 ASN A 288       6.579 -24.610   5.664  1.00 19.70           O  
ATOM   2104  ND2 ASN A 288       7.954 -23.345   6.897  1.00 12.29           N  
ATOM   2105  N   HIS A 289       6.777 -22.183   1.371  1.00 17.31           N  
ATOM   2106  CA  HIS A 289       6.888 -21.219   0.271  1.00 16.40           C  
ATOM   2107  C   HIS A 289       7.337 -19.837   0.790  1.00 19.44           C  
ATOM   2108  O   HIS A 289       6.757 -19.330   1.712  1.00 17.48           O  
ATOM   2109  CB  HIS A 289       5.561 -21.085  -0.495  1.00 15.92           C  
ATOM   2110  CG  HIS A 289       5.736 -20.581  -1.899  1.00 18.45           C  
ATOM   2111  ND1 HIS A 289       6.239 -19.329  -2.184  1.00 19.32           N  
ATOM   2112  CD2 HIS A 289       5.577 -21.199  -3.097  1.00 19.39           C  
ATOM   2113  CE1 HIS A 289       6.349 -19.185  -3.496  1.00 18.40           C  
ATOM   2114  NE2 HIS A 289       5.968 -20.310  -4.076  1.00 18.40           N  
ATOM   2115  N   PRO A 290       8.380 -19.237   0.223  1.00 17.73           N  
ATOM   2116  CA  PRO A 290       8.774 -17.897   0.675  1.00 16.78           C  
ATOM   2117  C   PRO A 290       7.592 -16.942   0.371  1.00 19.26           C  
ATOM   2118  O   PRO A 290       6.861 -17.147  -0.590  1.00 17.25           O  
ATOM   2119  CB  PRO A 290      10.030 -17.581  -0.192  1.00 18.11           C  
ATOM   2120  CG  PRO A 290       9.905 -18.458  -1.401  1.00 21.71           C  
ATOM   2121  CD  PRO A 290       9.259 -19.743  -0.857  1.00 18.13           C  
ATOM   2122  N   LEU A 291       7.348 -15.969   1.241  1.00 16.46           N  
ATOM   2123  CA  LEU A 291       6.192 -15.052   1.086  1.00 15.31           C  
ATOM   2124  C   LEU A 291       6.415 -13.862   0.134  1.00 20.39           C  
ATOM   2125  O   LEU A 291       5.523 -13.533  -0.657  1.00 21.45           O  
ATOM   2126  CB  LEU A 291       5.708 -14.550   2.462  1.00 15.08           C  
ATOM   2127  CG  LEU A 291       5.277 -15.681   3.430  1.00 19.13           C  
ATOM   2128  CD1 LEU A 291       4.911 -15.187   4.805  1.00 16.89           C  
ATOM   2129  CD2 LEU A 291       4.156 -16.585   2.857  1.00 19.60           C  
ATOM   2130  N   ILE A 292       7.586 -13.226   0.188  1.00 16.27           N  
ATOM   2131  CA  ILE A 292       7.900 -12.094  -0.699  1.00 14.75           C  
ATOM   2132  C   ILE A 292       7.532 -12.262  -2.179  1.00 18.57           C  
ATOM   2133  O   ILE A 292       6.846 -11.427  -2.758  1.00 18.82           O  
ATOM   2134  CB  ILE A 292       9.352 -11.559  -0.490  1.00 16.61           C  
ATOM   2135  CG1 ILE A 292       9.511 -10.971   0.919  1.00 16.93           C  
ATOM   2136  CG2 ILE A 292       9.720 -10.512  -1.551  1.00 13.38           C  
ATOM   2137  CD1 ILE A 292       8.646  -9.762   1.147  1.00 18.85           C  
ATOM   2138  N   PRO A 293       7.998 -13.332  -2.813  1.00 17.88           N  
ATOM   2139  CA  PRO A 293       7.697 -13.536  -4.243  1.00 16.37           C  
ATOM   2140  C   PRO A 293       6.197 -13.577  -4.507  1.00 18.46           C  
ATOM   2141  O   PRO A 293       5.740 -13.089  -5.530  1.00 18.19           O  
ATOM   2142  CB  PRO A 293       8.325 -14.916  -4.546  1.00 18.07           C  
ATOM   2143  CG  PRO A 293       9.258 -15.199  -3.439  1.00 22.16           C  
ATOM   2144  CD  PRO A 293       8.788 -14.448  -2.240  1.00 18.76           C  
ATOM   2145  N   LEU A 294       5.421 -14.190  -3.603  1.00 15.37           N  
ATOM   2146  CA  LEU A 294       3.973 -14.252  -3.820  1.00 15.28           C  
ATOM   2147  C   LEU A 294       3.296 -12.871  -3.665  1.00 18.47           C  
ATOM   2148  O   LEU A 294       2.378 -12.525  -4.404  1.00 18.50           O  
ATOM   2149  CB  LEU A 294       3.310 -15.273  -2.897  1.00 14.90           C  
ATOM   2150  CG  LEU A 294       3.800 -16.714  -3.055  1.00 18.72           C  
ATOM   2151  CD1 LEU A 294       3.076 -17.610  -1.995  1.00 17.35           C  
ATOM   2152  CD2 LEU A 294       3.621 -17.222  -4.503  1.00 16.24           C  
ATOM   2153  N   VAL A 295       3.728 -12.118  -2.666  1.00 15.55           N  
ATOM   2154  CA  VAL A 295       3.177 -10.804  -2.377  1.00 16.22           C  
ATOM   2155  C   VAL A 295       3.579  -9.808  -3.481  1.00 19.36           C  
ATOM   2156  O   VAL A 295       2.757  -9.019  -3.944  1.00 19.00           O  
ATOM   2157  CB  VAL A 295       3.654 -10.330  -0.967  1.00 21.15           C  
ATOM   2158  CG1 VAL A 295       3.190  -8.892  -0.720  1.00 21.02           C  
ATOM   2159  CG2 VAL A 295       3.085 -11.257   0.115  1.00 20.68           C  
ATOM   2160  N   HIS A 296       4.844  -9.843  -3.902  1.00 13.99           N  
ATOM   2161  CA  HIS A 296       5.284  -8.948  -4.954  1.00 13.81           C  
ATOM   2162  C   HIS A 296       4.639  -9.296  -6.304  1.00 18.59           C  
ATOM   2163  O   HIS A 296       4.142  -8.426  -7.031  1.00 18.78           O  
ATOM   2164  CB  HIS A 296       6.805  -8.902  -5.055  1.00 13.36           C  
ATOM   2165  CG  HIS A 296       7.454  -8.153  -3.936  1.00 15.69           C  
ATOM   2166  ND1 HIS A 296       8.812  -7.903  -3.903  1.00 16.11           N  
ATOM   2167  CD2 HIS A 296       6.940  -7.647  -2.786  1.00 16.04           C  
ATOM   2168  CE1 HIS A 296       9.104  -7.255  -2.786  1.00 15.52           C  
ATOM   2169  NE2 HIS A 296       7.990  -7.097  -2.085  1.00 15.93           N  
ATOM   2170  N   HIS A 297       4.650 -10.565  -6.659  1.00 16.04           N  
ATOM   2171  CA  HIS A 297       3.990 -10.930  -7.926  1.00 15.80           C  
ATOM   2172  C   HIS A 297       2.491 -10.630  -7.834  1.00 18.27           C  
ATOM   2173  O   HIS A 297       1.847 -10.368  -8.843  1.00 16.83           O  
ATOM   2174  CB  HIS A 297       4.222 -12.393  -8.298  1.00 14.62           C  
ATOM   2175  CG  HIS A 297       3.614 -12.777  -9.617  1.00 16.74           C  
ATOM   2176  ND1 HIS A 297       2.319 -13.226  -9.739  1.00 16.88           N  
ATOM   2177  CD2 HIS A 297       4.142 -12.815 -10.864  1.00 17.97           C  
ATOM   2178  CE1 HIS A 297       2.064 -13.502 -11.003  1.00 16.66           C  
ATOM   2179  NE2 HIS A 297       3.158 -13.270 -11.708  1.00 17.32           N  
ATOM   2180  N   GLY A 298       1.950 -10.635  -6.611  1.00 14.94           N  
ATOM   2181  CA  GLY A 298       0.521 -10.348  -6.395  1.00 14.39           C  
ATOM   2182  C   GLY A 298       0.159  -8.941  -6.884  1.00 17.49           C  
ATOM   2183  O   GLY A 298      -0.994  -8.673  -7.248  1.00 16.30           O  
ATOM   2184  N   MET A 299       1.144  -8.042  -6.888  1.00 13.62           N  
ATOM   2185  CA  MET A 299       0.979  -6.671  -7.404  1.00 12.53           C  
ATOM   2186  C   MET A 299       0.764  -6.612  -8.919  1.00 19.18           C  
ATOM   2187  O   MET A 299       0.251  -5.621  -9.409  1.00 19.61           O  
ATOM   2188  CB  MET A 299       2.159  -5.795  -7.013  1.00 14.11           C  
ATOM   2189  CG  MET A 299       2.346  -5.749  -5.508  1.00 18.46           C  
ATOM   2190  SD  MET A 299       3.768  -4.835  -4.936  1.00 23.39           S  
ATOM   2191  CE  MET A 299       3.212  -3.212  -5.269  1.00 19.83           C  
ATOM   2192  N   VAL A 300       1.134  -7.671  -9.659  1.00 15.68           N  
ATOM   2193  CA  VAL A 300       0.888  -7.721 -11.107  1.00 14.54           C  
ATOM   2194  C   VAL A 300      -0.057  -8.865 -11.549  1.00 18.78           C  
ATOM   2195  O   VAL A 300      -0.432  -8.948 -12.732  1.00 17.73           O  
ATOM   2196  CB  VAL A 300       2.209  -7.779 -11.912  1.00 17.75           C  
ATOM   2197  CG1 VAL A 300       3.080  -6.575 -11.614  1.00 16.74           C  
ATOM   2198  CG2 VAL A 300       2.988  -9.106 -11.620  1.00 17.25           C  
ATOM   2199  N   GLY A 301      -0.471  -9.729 -10.619  1.00 15.27           N  
ATOM   2200  CA  GLY A 301      -1.274 -10.900 -11.008  1.00 13.88           C  
ATOM   2201  C   GLY A 301      -2.784 -10.724 -11.129  1.00 18.51           C  
ATOM   2202  O   GLY A 301      -3.500 -11.665 -11.465  1.00 16.21           O  
ATOM   2203  N   LYS A 302      -3.272  -9.515 -10.915  1.00 16.31           N  
ATOM   2204  CA  LYS A 302      -4.706  -9.283 -10.871  1.00 16.82           C  
ATOM   2205  C   LYS A 302      -5.295  -8.446 -12.014  1.00 20.12           C  
ATOM   2206  O   LYS A 302      -6.414  -7.965 -11.894  1.00 19.75           O  
ATOM   2207  CB  LYS A 302      -5.075  -8.572  -9.524  1.00 18.77           C  
ATOM   2208  CG  LYS A 302      -4.753  -9.323  -8.227  1.00 21.59           C  
ATOM   2209  CD  LYS A 302      -5.267  -8.521  -7.008  1.00 21.88           C  
ATOM   2210  CE  LYS A 302      -4.735  -9.058  -5.665  1.00 17.68           C  
ATOM   2211  NZ  LYS A 302      -3.268  -8.885  -5.590  1.00 15.50           N  
ATOM   2212  N   PHE A 303      -4.539  -8.200 -13.073  1.00 15.98           N  
ATOM   2213  CA  PHE A 303      -5.013  -7.302 -14.160  1.00 14.54           C  
ATOM   2214  C   PHE A 303      -5.813  -7.981 -15.294  1.00 20.71           C  
ATOM   2215  O   PHE A 303      -6.488  -7.317 -16.069  1.00 20.33           O  
ATOM   2216  CB  PHE A 303      -3.861  -6.445 -14.741  1.00 14.79           C  
ATOM   2217  CG  PHE A 303      -3.036  -5.687 -13.692  1.00 14.44           C  
ATOM   2218  CD1 PHE A 303      -3.649  -4.902 -12.732  1.00 16.50           C  
ATOM   2219  CD2 PHE A 303      -1.650  -5.676 -13.759  1.00 15.22           C  
ATOM   2220  CE1 PHE A 303      -2.920  -4.189 -11.777  1.00 16.74           C  
ATOM   2221  CE2 PHE A 303      -0.885  -4.941 -12.849  1.00 17.50           C  
ATOM   2222  CZ  PHE A 303      -1.529  -4.214 -11.825  1.00 15.97           C  
ATOM   2223  N   ASN A 304      -5.739  -9.302 -15.399  1.00 20.01           N  
ATOM   2224  CA  ASN A 304      -6.511 -10.012 -16.440  1.00 20.24           C  
ATOM   2225  C   ASN A 304      -7.097 -11.282 -15.874  1.00 24.69           C  
ATOM   2226  O   ASN A 304      -6.431 -12.003 -15.165  1.00 25.24           O  
ATOM   2227  CB  ASN A 304      -5.652 -10.365 -17.666  1.00 13.78           C  
ATOM   2228  CG  ASN A 304      -5.399  -9.174 -18.575  1.00 25.85           C  
ATOM   2229  OD1 ASN A 304      -6.251  -8.781 -19.386  1.00 22.07           O  
ATOM   2230  ND2 ASN A 304      -4.201  -8.640 -18.500  1.00 15.74           N  
ATOM   2231  N   ASN A 305      -8.357 -11.541 -16.187  1.00 21.93           N  
ATOM   2232  CA  ASN A 305      -9.007 -12.770 -15.760  1.00 22.32           C  
ATOM   2233  C   ASN A 305      -8.395 -13.927 -16.518  1.00 23.15           C  
ATOM   2234  O   ASN A 305      -8.166 -13.828 -17.707  1.00 23.70           O  
ATOM   2235  CB  ASN A 305     -10.488 -12.707 -16.106  1.00 30.37           C  
ATOM   2236  CG  ASN A 305     -11.344 -12.471 -14.905  1.00 65.65           C  
ATOM   2237  OD1 ASN A 305     -11.338 -13.260 -13.960  1.00 65.67           O  
ATOM   2238  ND2 ASN A 305     -12.087 -11.371 -14.921  1.00 64.41           N  
ATOM   2239  N   PHE A 306      -8.122 -15.035 -15.842  1.00 18.15           N  
ATOM   2240  CA  PHE A 306      -7.572 -16.192 -16.532  1.00 16.66           C  
ATOM   2241  C   PHE A 306      -8.120 -17.533 -16.065  1.00 21.63           C  
ATOM   2242  O   PHE A 306      -8.537 -17.689 -14.916  1.00 18.11           O  
ATOM   2243  CB  PHE A 306      -6.047 -16.215 -16.401  1.00 16.51           C  
ATOM   2244  CG  PHE A 306      -5.562 -16.295 -14.975  1.00 18.05           C  
ATOM   2245  CD1 PHE A 306      -5.293 -17.527 -14.386  1.00 19.12           C  
ATOM   2246  CD2 PHE A 306      -5.371 -15.123 -14.201  1.00 19.75           C  
ATOM   2247  CE1 PHE A 306      -4.803 -17.590 -13.080  1.00 19.49           C  
ATOM   2248  CE2 PHE A 306      -4.903 -15.204 -12.881  1.00 20.32           C  
ATOM   2249  CZ  PHE A 306      -4.640 -16.422 -12.332  1.00 17.73           C  
ATOM   2250  N   ASN A 307      -7.992 -18.523 -16.946  1.00 21.34           N  
ATOM   2251  CA  ASN A 307      -8.263 -19.906 -16.609  1.00 22.56           C  
ATOM   2252  C   ASN A 307      -6.902 -20.559 -16.375  1.00 26.21           C  
ATOM   2253  O   ASN A 307      -5.904 -20.194 -17.000  1.00 25.51           O  
ATOM   2254  CB  ASN A 307      -8.964 -20.626 -17.766  1.00 27.97           C  
ATOM   2255  CG  ASN A 307     -10.416 -20.302 -17.825  1.00 54.50           C  
ATOM   2256  OD1 ASN A 307     -11.054 -20.144 -16.792  1.00 55.03           O  
ATOM   2257  ND2 ASN A 307     -10.912 -20.041 -19.016  1.00 44.69           N  
ATOM   2258  N   VAL A 308      -6.888 -21.549 -15.494  1.00 23.94           N  
ATOM   2259  CA  VAL A 308      -5.677 -22.263 -15.128  1.00 24.59           C  
ATOM   2260  C   VAL A 308      -5.618 -23.639 -15.768  1.00 24.73           C  
ATOM   2261  O   VAL A 308      -6.518 -24.438 -15.581  1.00 24.19           O  
ATOM   2262  CB  VAL A 308      -5.628 -22.440 -13.588  1.00 29.07           C  
ATOM   2263  CG1 VAL A 308      -4.443 -23.336 -13.177  1.00 28.79           C  
ATOM   2264  CG2 VAL A 308      -5.564 -21.103 -12.913  1.00 28.87           C  
ATOM   2265  N   ASP A 309      -4.513 -23.945 -16.436  1.00 19.40           N  
ATOM   2266  CA  ASP A 309      -4.281 -25.284 -16.969  1.00 18.42           C  
ATOM   2267  C   ASP A 309      -2.888 -25.651 -16.407  1.00 21.58           C  
ATOM   2268  O   ASP A 309      -1.867 -25.352 -17.012  1.00 21.80           O  
ATOM   2269  CB  ASP A 309      -4.278 -25.229 -18.489  1.00 21.29           C  
ATOM   2270  CG  ASP A 309      -3.622 -26.447 -19.119  1.00 32.59           C  
ATOM   2271  OD1 ASP A 309      -3.847 -27.563 -18.613  1.00 32.80           O  
ATOM   2272  OD2 ASP A 309      -2.871 -26.275 -20.100  1.00 41.89           O  
ATOM   2273  N   ALA A 310      -2.861 -26.179 -15.186  1.00 17.37           N  
ATOM   2274  CA  ALA A 310      -1.610 -26.408 -14.459  1.00 17.73           C  
ATOM   2275  C   ALA A 310      -1.398 -27.835 -13.950  1.00 24.32           C  
ATOM   2276  O   ALA A 310      -2.328 -28.501 -13.542  1.00 24.79           O  
ATOM   2277  CB  ALA A 310      -1.542 -25.450 -13.279  1.00 17.47           C  
ATOM   2278  N   GLN A 311      -0.146 -28.263 -13.904  1.00 22.49           N  
ATOM   2279  CA  GLN A 311       0.176 -29.577 -13.368  1.00 21.79           C  
ATOM   2280  C   GLN A 311       1.455 -29.568 -12.579  1.00 23.11           C  
ATOM   2281  O   GLN A 311       2.426 -28.969 -13.001  1.00 22.61           O  
ATOM   2282  CB  GLN A 311       0.325 -30.610 -14.477  1.00 23.67           C  
ATOM   2283  CG  GLN A 311       0.425 -32.014 -13.871  1.00 52.66           C  
ATOM   2284  CD  GLN A 311       0.549 -33.111 -14.909  1.00 74.95           C  
ATOM   2285  OE1 GLN A 311      -0.211 -34.086 -14.889  1.00 76.42           O  
ATOM   2286  NE2 GLN A 311       1.521 -32.972 -15.811  1.00 60.51           N  
ATOM   2287  N   LEU A 312       1.474 -30.309 -11.479  1.00 19.26           N  
ATOM   2288  CA  LEU A 312       2.673 -30.446 -10.673  1.00 19.44           C  
ATOM   2289  C   LEU A 312       3.023 -31.923 -10.537  1.00 24.79           C  
ATOM   2290  O   LEU A 312       2.152 -32.779 -10.293  1.00 24.13           O  
ATOM   2291  CB  LEU A 312       2.489 -29.829  -9.278  1.00 18.61           C  
ATOM   2292  CG  LEU A 312       3.512 -30.245  -8.211  1.00 21.99           C  
ATOM   2293  CD1 LEU A 312       4.875 -29.598  -8.441  1.00 21.13           C  
ATOM   2294  CD2 LEU A 312       2.941 -29.885  -6.840  1.00 22.09           C  
ATOM   2295  N   LYS A 313       4.309 -32.205 -10.676  1.00 22.98           N  
ATOM   2296  CA  LYS A 313       4.830 -33.560 -10.567  1.00 23.10           C  
ATOM   2297  C   LYS A 313       5.932 -33.551  -9.521  1.00 26.54           C  
ATOM   2298  O   LYS A 313       6.901 -32.798  -9.626  1.00 25.12           O  
ATOM   2299  CB  LYS A 313       5.412 -34.040 -11.913  1.00 25.50           C  
ATOM   2300  CG  LYS A 313       6.066 -35.417 -11.848  1.00 44.02           C  
ATOM   2301  CD  LYS A 313       6.319 -35.986 -13.244  1.00 60.69           C  
ATOM   2302  N   VAL A 314       5.779 -34.411  -8.519  1.00 23.30           N  
ATOM   2303  CA  VAL A 314       6.787 -34.566  -7.473  1.00 22.01           C  
ATOM   2304  C   VAL A 314       7.318 -35.992  -7.497  1.00 26.72           C  
ATOM   2305  O   VAL A 314       6.544 -36.953  -7.476  1.00 27.73           O  
ATOM   2306  CB  VAL A 314       6.214 -34.195  -6.107  1.00 25.61           C  
ATOM   2307  CG1 VAL A 314       7.185 -34.580  -4.973  1.00 25.07           C  
ATOM   2308  CG2 VAL A 314       5.880 -32.699  -6.076  1.00 24.91           C  
ATOM   2309  N   VAL A 315       8.623 -36.138  -7.665  1.00 23.22           N  
ATOM   2310  CA  VAL A 315       9.224 -37.474  -7.664  1.00 23.24           C  
ATOM   2311  C   VAL A 315      10.046 -37.633  -6.383  1.00 25.86           C  
ATOM   2312  O   VAL A 315      11.006 -36.931  -6.183  1.00 23.29           O  
ATOM   2313  CB  VAL A 315      10.088 -37.754  -8.905  1.00 26.41           C  
ATOM   2314  CG1 VAL A 315      10.592 -39.191  -8.855  1.00 25.49           C  
ATOM   2315  CG2 VAL A 315       9.300 -37.485 -10.187  1.00 25.95           C  
ATOM   2316  N   LEU A 316       9.617 -38.524  -5.498  1.00 27.15           N  
ATOM   2317  CA  LEU A 316      10.342 -38.822  -4.251  1.00 27.88           C  
ATOM   2318  C   LEU A 316      11.466 -39.839  -4.493  1.00 30.18           C  
ATOM   2319  O   LEU A 316      11.428 -40.578  -5.466  1.00 28.14           O  
ATOM   2320  CB  LEU A 316       9.372 -39.413  -3.224  1.00 28.57           C  
ATOM   2321  CG  LEU A 316       8.141 -38.585  -2.823  1.00 33.18           C  
ATOM   2322  CD1 LEU A 316       7.389 -39.281  -1.702  1.00 32.18           C  
ATOM   2323  CD2 LEU A 316       8.590 -37.210  -2.381  1.00 36.06           C  
ATOM   2324  N   PRO A 317      12.457 -39.888  -3.603  1.00 30.16           N  
ATOM   2325  CA  PRO A 317      13.528 -40.906  -3.710  1.00 30.50           C  
ATOM   2326  C   PRO A 317      12.906 -42.303  -3.478  1.00 37.87           C  
ATOM   2327  O   PRO A 317      11.864 -42.419  -2.822  1.00 36.54           O  
ATOM   2328  CB  PRO A 317      14.476 -40.555  -2.558  1.00 31.12           C  
ATOM   2329  CG  PRO A 317      14.048 -39.236  -2.044  1.00 35.36           C  
ATOM   2330  CD  PRO A 317      12.599 -39.085  -2.372  1.00 31.53           C  
ATOM   2331  N   LYS A 318      13.525 -43.347  -4.039  1.00 38.44           N  
ATOM   2332  CA  LYS A 318      12.998 -44.716  -3.940  1.00 38.90           C  
ATOM   2333  C   LYS A 318      12.693 -45.137  -2.500  1.00 42.72           C  
ATOM   2334  O   LYS A 318      13.471 -44.880  -1.595  1.00 42.24           O  
ATOM   2335  CB  LYS A 318      13.934 -45.712  -4.632  1.00 43.36           C  
ATOM   2336  CG  LYS A 318      13.555 -47.182  -4.414  1.00 60.75           C  
ATOM   2337  N   GLY A 319      11.516 -45.705  -2.275  1.00 39.88           N  
ATOM   2338  CA  GLY A 319      11.160 -46.133  -0.925  1.00 40.68           C  
ATOM   2339  C   GLY A 319      10.506 -45.070  -0.020  1.00 46.16           C  
ATOM   2340  O   GLY A 319      10.158 -45.354   1.137  1.00 46.48           O  
ATOM   2341  N   TYR A 320      10.333 -43.854  -0.528  1.00 40.42           N  
ATOM   2342  CA  TYR A 320       9.703 -42.807   0.291  1.00 37.99           C  
ATOM   2343  C   TYR A 320       8.275 -42.655  -0.146  1.00 35.38           C  
ATOM   2344  O   TYR A 320       7.957 -42.848  -1.315  1.00 33.74           O  
ATOM   2345  CB  TYR A 320      10.412 -41.470   0.100  1.00 39.39           C  
ATOM   2346  CG  TYR A 320      11.693 -41.340   0.868  1.00 42.20           C  
ATOM   2347  CD1 TYR A 320      11.731 -40.640   2.061  1.00 44.82           C  
ATOM   2348  CD2 TYR A 320      12.859 -41.938   0.419  1.00 43.42           C  
ATOM   2349  CE1 TYR A 320      12.900 -40.492   2.761  1.00 46.27           C  
ATOM   2350  CE2 TYR A 320      14.033 -41.818   1.130  1.00 44.56           C  
ATOM   2351  CZ  TYR A 320      14.047 -41.083   2.294  1.00 55.68           C  
ATOM   2352  OH  TYR A 320      15.206 -40.944   3.017  1.00 63.96           O  
ATOM   2353  N   LYS A 321       7.414 -42.289   0.784  1.00 30.67           N  
ATOM   2354  CA  LYS A 321       6.034 -42.033   0.430  1.00 29.87           C  
ATOM   2355  C   LYS A 321       5.451 -40.780   1.078  1.00 31.46           C  
ATOM   2356  O   LYS A 321       5.926 -40.301   2.119  1.00 30.48           O  
ATOM   2357  CB  LYS A 321       5.127 -43.267   0.573  1.00 32.90           C  
ATOM   2358  CG  LYS A 321       5.170 -43.958   1.900  1.00 55.76           C  
ATOM   2359  CD  LYS A 321       5.682 -45.389   1.715  1.00 69.82           C  
ATOM   2360  N   ILE A 322       4.425 -40.246   0.436  1.00 25.73           N  
ATOM   2361  CA  ILE A 322       3.752 -39.069   0.938  1.00 25.08           C  
ATOM   2362  C   ILE A 322       2.806 -39.490   2.053  1.00 29.65           C  
ATOM   2363  O   ILE A 322       1.958 -40.374   1.865  1.00 28.05           O  
ATOM   2364  CB  ILE A 322       3.052 -38.272  -0.218  1.00 27.48           C  
ATOM   2365  CG1 ILE A 322       4.124 -37.572  -1.085  1.00 27.63           C  
ATOM   2366  CG2 ILE A 322       2.040 -37.277   0.345  1.00 26.48           C  
ATOM   2367  CD1 ILE A 322       3.600 -36.482  -1.966  1.00 32.15           C  
ATOM   2368  N   ARG A 323       2.988 -38.867   3.221  1.00 27.05           N  
ATOM   2369  CA  ARG A 323       2.174 -39.135   4.390  1.00 27.55           C  
ATOM   2370  C   ARG A 323       1.048 -38.135   4.493  1.00 31.24           C  
ATOM   2371  O   ARG A 323       0.021 -38.412   5.100  1.00 30.71           O  
ATOM   2372  CB  ARG A 323       3.016 -39.021   5.659  1.00 32.45           C  
ATOM   2373  CG  ARG A 323       4.178 -40.014   5.728  1.00 51.68           C  
ATOM   2374  CD  ARG A 323       3.685 -41.451   5.929  1.00 64.03           C  
ATOM   2375  N   TYR A 324       1.258 -36.938   3.954  1.00 27.39           N  
ATOM   2376  CA  TYR A 324       0.207 -35.920   4.019  1.00 25.99           C  
ATOM   2377  C   TYR A 324       0.412 -34.887   2.942  1.00 27.12           C  
ATOM   2378  O   TYR A 324       1.532 -34.411   2.746  1.00 26.46           O  
ATOM   2379  CB  TYR A 324       0.242 -35.238   5.382  1.00 26.77           C  
ATOM   2380  CG  TYR A 324      -0.693 -34.064   5.522  1.00 28.55           C  
ATOM   2381  CD1 TYR A 324      -2.014 -34.255   5.889  1.00 30.31           C  
ATOM   2382  CD2 TYR A 324      -0.232 -32.740   5.363  1.00 29.37           C  
ATOM   2383  CE1 TYR A 324      -2.875 -33.185   6.073  1.00 31.80           C  
ATOM   2384  CE2 TYR A 324      -1.097 -31.645   5.558  1.00 29.77           C  
ATOM   2385  CZ  TYR A 324      -2.409 -31.880   5.921  1.00 38.90           C  
ATOM   2386  OH  TYR A 324      -3.284 -30.824   6.083  1.00 38.57           O  
ATOM   2387  N   ALA A 325      -0.663 -34.550   2.240  1.00 22.17           N  
ATOM   2388  CA  ALA A 325      -0.605 -33.498   1.230  1.00 21.84           C  
ATOM   2389  C   ALA A 325      -1.951 -32.787   1.233  1.00 25.35           C  
ATOM   2390  O   ALA A 325      -2.986 -33.425   1.214  1.00 26.10           O  
ATOM   2391  CB  ALA A 325      -0.292 -34.074  -0.181  1.00 22.26           C  
ATOM   2392  N   ALA A 326      -1.927 -31.466   1.292  1.00 21.71           N  
ATOM   2393  CA  ALA A 326      -3.155 -30.663   1.211  1.00 22.20           C  
ATOM   2394  C   ALA A 326      -2.795 -29.325   0.561  1.00 24.80           C  
ATOM   2395  O   ALA A 326      -2.021 -28.557   1.140  1.00 23.77           O  
ATOM   2396  CB  ALA A 326      -3.769 -30.434   2.639  1.00 22.71           C  
ATOM   2397  N   PRO A 327      -3.304 -29.077  -0.649  1.00 21.81           N  
ATOM   2398  CA  PRO A 327      -4.258 -29.988  -1.323  1.00 22.68           C  
ATOM   2399  C   PRO A 327      -3.712 -31.382  -1.666  1.00 29.16           C  
ATOM   2400  O   PRO A 327      -2.500 -31.573  -1.854  1.00 28.55           O  
ATOM   2401  CB  PRO A 327      -4.653 -29.249  -2.614  1.00 23.41           C  
ATOM   2402  CG  PRO A 327      -3.904 -27.953  -2.614  1.00 27.90           C  
ATOM   2403  CD  PRO A 327      -3.095 -27.808  -1.366  1.00 23.46           C  
ATOM   2404  N   GLN A 328      -4.646 -32.307  -1.851  1.00 25.51           N  
ATOM   2405  CA  GLN A 328      -4.366 -33.708  -2.152  1.00 25.57           C  
ATOM   2406  C   GLN A 328      -3.908 -33.944  -3.585  1.00 25.22           C  
ATOM   2407  O   GLN A 328      -4.363 -33.254  -4.489  1.00 24.52           O  
ATOM   2408  CB  GLN A 328      -5.628 -34.536  -1.851  1.00 27.02           C  
ATOM   2409  CG  GLN A 328      -5.459 -36.043  -1.960  1.00 57.41           C  
ATOM   2410  CD  GLN A 328      -4.334 -36.594  -1.101  1.00 80.79           C  
ATOM   2411  OE1 GLN A 328      -3.333 -35.925  -0.858  1.00 76.05           O  
ATOM   2412  NE2 GLN A 328      -4.474 -37.847  -0.682  1.00 76.94           N  
ATOM   2413  N   TYR A 329      -3.009 -34.917  -3.790  1.00 20.75           N  
ATOM   2414  CA  TYR A 329      -2.544 -35.248  -5.142  1.00 20.89           C  
ATOM   2415  C   TYR A 329      -3.621 -36.044  -5.847  1.00 25.17           C  
ATOM   2416  O   TYR A 329      -4.486 -36.608  -5.214  1.00 23.99           O  
ATOM   2417  CB  TYR A 329      -1.226 -36.013  -5.114  1.00 22.70           C  
ATOM   2418  CG  TYR A 329      -1.257 -37.238  -4.231  1.00 25.82           C  
ATOM   2419  CD1 TYR A 329      -1.745 -38.454  -4.706  1.00 27.61           C  
ATOM   2420  CD2 TYR A 329      -0.731 -37.202  -2.948  1.00 27.01           C  
ATOM   2421  CE1 TYR A 329      -1.784 -39.569  -3.900  1.00 26.57           C  
ATOM   2422  CE2 TYR A 329      -0.781 -38.323  -2.132  1.00 27.47           C  
ATOM   2423  CZ  TYR A 329      -1.282 -39.492  -2.621  1.00 32.06           C  
ATOM   2424  OH  TYR A 329      -1.323 -40.575  -1.801  1.00 36.54           O  
ATOM   2425  N   ARG A 330      -3.589 -36.043  -7.169  1.00 24.42           N  
ATOM   2426  CA  ARG A 330      -4.597 -36.733  -7.963  1.00 25.41           C  
ATOM   2427  C   ARG A 330      -4.219 -38.191  -8.253  1.00 32.04           C  
ATOM   2428  O   ARG A 330      -5.085 -39.048  -8.399  1.00 33.95           O  
ATOM   2429  CB  ARG A 330      -4.742 -36.007  -9.300  1.00 23.44           C  
ATOM   2430  CG  ARG A 330      -5.690 -36.644 -10.267  1.00 23.94           C  
ATOM   2431  CD  ARG A 330      -5.721 -35.811 -11.566  1.00 39.47           C  
ATOM   2432  NE  ARG A 330      -7.088 -35.565 -12.032  1.00 59.64           N  
ATOM   2433  CZ  ARG A 330      -8.000 -34.868 -11.362  1.00 81.32           C  
ATOM   2434  NH1 ARG A 330      -7.713 -34.327 -10.189  1.00 76.83           N  
ATOM   2435  NH2 ARG A 330      -9.210 -34.714 -11.865  1.00 72.07           N  
ATOM   2436  N   SER A 331      -2.940 -38.451  -8.452  1.00 26.17           N  
ATOM   2437  CA  SER A 331      -2.526 -39.782  -8.829  1.00 25.14           C  
ATOM   2438  C   SER A 331      -1.122 -40.045  -8.347  1.00 30.37           C  
ATOM   2439  O   SER A 331      -0.405 -39.131  -7.914  1.00 29.26           O  
ATOM   2440  CB  SER A 331      -2.582 -39.941 -10.326  1.00 26.49           C  
ATOM   2441  OG  SER A 331      -1.532 -39.213 -10.913  1.00 33.00           O  
ATOM   2442  N   GLN A 332      -0.775 -41.328  -8.318  1.00 26.97           N  
ATOM   2443  CA  GLN A 332       0.538 -41.763  -7.901  1.00 26.75           C  
ATOM   2444  C   GLN A 332       0.987 -43.000  -8.666  1.00 31.11           C  
ATOM   2445  O   GLN A 332       0.210 -43.904  -8.873  1.00 32.85           O  
ATOM   2446  CB  GLN A 332       0.551 -42.065  -6.430  1.00 27.87           C  
ATOM   2447  CG  GLN A 332       1.840 -42.779  -6.027  1.00 39.74           C  
ATOM   2448  CD  GLN A 332       1.650 -43.721  -4.858  1.00 53.93           C  
ATOM   2449  OE1 GLN A 332       0.608 -43.727  -4.204  1.00 52.29           O  
ATOM   2450  NE2 GLN A 332       2.679 -44.473  -4.548  1.00 43.54           N  
ATOM   2451  N   ASN A 333       2.229 -43.015  -9.125  1.00 27.19           N  
ATOM   2452  CA  ASN A 333       2.737 -44.143  -9.885  1.00 26.99           C  
ATOM   2453  C   ASN A 333       4.087 -44.387  -9.247  1.00 31.62           C  
ATOM   2454  O   ASN A 333       5.043 -43.643  -9.446  1.00 30.02           O  
ATOM   2455  CB  ASN A 333       2.860 -43.775 -11.366  1.00 27.32           C  
ATOM   2456  CG  ASN A 333       3.367 -44.916 -12.199  1.00 56.14           C  
ATOM   2457  OD1 ASN A 333       3.077 -46.056 -11.897  1.00 50.37           O  
ATOM   2458  ND2 ASN A 333       4.212 -44.624 -13.191  1.00 58.91           N  
ATOM   2459  N   LEU A 334       4.141 -45.366  -8.366  1.00 30.55           N  
ATOM   2460  CA  LEU A 334       5.385 -45.613  -7.647  1.00 32.23           C  
ATOM   2461  C   LEU A 334       5.807 -44.353  -6.871  1.00 35.33           C  
ATOM   2462  O   LEU A 334       5.077 -43.903  -5.986  1.00 35.18           O  
ATOM   2463  CB  LEU A 334       6.494 -46.098  -8.587  1.00 32.90           C  
ATOM   2464  CG  LEU A 334       6.370 -47.556  -9.075  1.00 38.32           C  
ATOM   2465  CD1 LEU A 334       7.573 -47.932  -9.954  1.00 38.24           C  
ATOM   2466  CD2 LEU A 334       6.225 -48.533  -7.883  1.00 36.10           C  
ATOM   2467  N   GLU A 335       6.970 -43.780  -7.184  1.00 29.90           N  
ATOM   2468  CA  GLU A 335       7.442 -42.606  -6.435  1.00 29.41           C  
ATOM   2469  C   GLU A 335       7.016 -41.256  -6.997  1.00 32.70           C  
ATOM   2470  O   GLU A 335       7.304 -40.194  -6.403  1.00 33.11           O  
ATOM   2471  CB  GLU A 335       8.964 -42.622  -6.267  1.00 30.90           C  
ATOM   2472  CG  GLU A 335       9.414 -43.518  -5.141  1.00 43.34           C  
ATOM   2473  CD  GLU A 335       9.563 -44.935  -5.623  1.00 68.27           C  
ATOM   2474  OE1 GLU A 335       9.816 -45.101  -6.846  1.00 45.66           O  
ATOM   2475  OE2 GLU A 335       9.364 -45.862  -4.802  1.00 65.79           O  
ATOM   2476  N   GLU A 336       6.372 -41.307  -8.153  1.00 27.28           N  
ATOM   2477  CA  GLU A 336       5.928 -40.117  -8.829  1.00 27.53           C  
ATOM   2478  C   GLU A 336       4.483 -39.745  -8.416  1.00 30.35           C  
ATOM   2479  O   GLU A 336       3.569 -40.578  -8.464  1.00 26.98           O  
ATOM   2480  CB  GLU A 336       6.051 -40.329 -10.336  1.00 28.62           C  
ATOM   2481  CG  GLU A 336       5.090 -39.503 -11.149  1.00 42.79           C  
ATOM   2482  CD  GLU A 336       5.456 -39.478 -12.610  1.00 69.86           C  
ATOM   2483  OE1 GLU A 336       6.640 -39.735 -12.925  1.00 63.57           O  
ATOM   2484  OE2 GLU A 336       4.555 -39.224 -13.439  1.00 65.77           O  
ATOM   2485  N   TYR A 337       4.302 -38.507  -7.942  1.00 26.03           N  
ATOM   2486  CA  TYR A 337       2.963 -38.015  -7.607  1.00 24.42           C  
ATOM   2487  C   TYR A 337       2.617 -36.808  -8.485  1.00 27.58           C  
ATOM   2488  O   TYR A 337       3.482 -35.943  -8.739  1.00 26.28           O  
ATOM   2489  CB  TYR A 337       2.860 -37.614  -6.137  1.00 24.69           C  
ATOM   2490  CG  TYR A 337       3.111 -38.721  -5.157  1.00 25.75           C  
ATOM   2491  CD1 TYR A 337       2.073 -39.237  -4.399  1.00 27.56           C  
ATOM   2492  CD2 TYR A 337       4.388 -39.201  -4.940  1.00 27.45           C  
ATOM   2493  CE1 TYR A 337       2.281 -40.226  -3.480  1.00 28.14           C  
ATOM   2494  CE2 TYR A 337       4.632 -40.196  -4.002  1.00 28.39           C  
ATOM   2495  CZ  TYR A 337       3.567 -40.719  -3.287  1.00 37.51           C  
ATOM   2496  OH  TYR A 337       3.788 -41.681  -2.330  1.00 37.81           O  
ATOM   2497  N   ARG A 338       1.356 -36.745  -8.919  1.00 24.73           N  
ATOM   2498  CA  ARG A 338       0.885 -35.649  -9.757  1.00 25.71           C  
ATOM   2499  C   ARG A 338      -0.322 -34.918  -9.172  1.00 27.91           C  
ATOM   2500  O   ARG A 338      -1.246 -35.548  -8.632  1.00 24.95           O  
ATOM   2501  CB  ARG A 338       0.517 -36.141 -11.159  1.00 24.51           C  
ATOM   2502  CG  ARG A 338       1.678 -36.603 -11.996  1.00 33.74           C  
ATOM   2503  CD  ARG A 338       1.176 -37.129 -13.340  1.00 41.38           C  
ATOM   2504  NE  ARG A 338       2.241 -37.776 -14.107  1.00 69.74           N  
ATOM   2505  CZ  ARG A 338       2.521 -37.540 -15.390  1.00 93.96           C  
ATOM   2506  NH1 ARG A 338       1.819 -36.658 -16.093  1.00 87.14           N  
ATOM   2507  NH2 ARG A 338       3.515 -38.199 -15.974  1.00 82.66           N  
ATOM   2508  N   TRP A 339      -0.324 -33.593  -9.349  1.00 23.49           N  
ATOM   2509  CA  TRP A 339      -1.472 -32.743  -8.961  1.00 22.43           C  
ATOM   2510  C   TRP A 339      -2.012 -32.067 -10.218  1.00 26.88           C  
ATOM   2511  O   TRP A 339      -1.240 -31.605 -11.051  1.00 25.88           O  
ATOM   2512  CB  TRP A 339      -1.037 -31.626  -8.000  1.00 19.75           C  
ATOM   2513  CG  TRP A 339      -0.833 -32.042  -6.581  1.00 19.89           C  
ATOM   2514  CD1 TRP A 339      -1.643 -31.763  -5.502  1.00 22.38           C  
ATOM   2515  CD2 TRP A 339       0.324 -32.720  -6.056  1.00 20.32           C  
ATOM   2516  NE1 TRP A 339      -1.057 -32.249  -4.336  1.00 22.48           N  
ATOM   2517  CE2 TRP A 339       0.146 -32.836  -4.651  1.00 24.30           C  
ATOM   2518  CE3 TRP A 339       1.459 -33.298  -6.648  1.00 21.36           C  
ATOM   2519  CZ2 TRP A 339       1.061 -33.499  -3.838  1.00 24.08           C  
ATOM   2520  CZ3 TRP A 339       2.350 -33.964  -5.844  1.00 23.03           C  
ATOM   2521  CH2 TRP A 339       2.159 -34.046  -4.445  1.00 23.89           C  
ATOM   2522  N   SER A 340      -3.331 -31.954 -10.328  1.00 25.47           N  
ATOM   2523  CA  SER A 340      -3.913 -31.176 -11.421  1.00 26.10           C  
ATOM   2524  C   SER A 340      -5.395 -31.015 -11.200  1.00 28.97           C  
ATOM   2525  O   SER A 340      -6.006 -31.871 -10.605  1.00 29.14           O  
ATOM   2526  CB  SER A 340      -3.626 -31.763 -12.788  1.00 30.11           C  
ATOM   2527  OG  SER A 340      -4.356 -32.948 -12.947  1.00 44.41           O  
ATOM   2528  N   GLY A 341      -5.951 -29.889 -11.643  1.00 25.51           N  
ATOM   2529  CA  GLY A 341      -7.367 -29.601 -11.498  1.00 23.95           C  
ATOM   2530  C   GLY A 341      -7.806 -29.486 -10.059  1.00 29.66           C  
ATOM   2531  O   GLY A 341      -6.995 -29.499  -9.129  1.00 31.39           O  
ATOM   2532  N   GLY A 342      -9.114 -29.319  -9.886  1.00 27.19           N  
ATOM   2533  CA  GLY A 342      -9.737 -29.277  -8.565  1.00 25.76           C  
ATOM   2534  C   GLY A 342      -9.104 -28.280  -7.638  1.00 28.05           C  
ATOM   2535  O   GLY A 342      -8.850 -27.154  -8.025  1.00 28.90           O  
ATOM   2536  N   ALA A 343      -8.908 -28.690  -6.394  1.00 23.35           N  
ATOM   2537  CA  ALA A 343      -8.340 -27.833  -5.372  1.00 22.72           C  
ATOM   2538  C   ALA A 343      -6.923 -27.322  -5.719  1.00 27.04           C  
ATOM   2539  O   ALA A 343      -6.539 -26.233  -5.298  1.00 27.86           O  
ATOM   2540  CB  ALA A 343      -8.357 -28.548  -3.967  1.00 22.96           C  
ATOM   2541  N   TYR A 344      -6.151 -28.098  -6.481  1.00 23.20           N  
ATOM   2542  CA  TYR A 344      -4.800 -27.661  -6.844  1.00 21.15           C  
ATOM   2543  C   TYR A 344      -4.909 -26.450  -7.795  1.00 24.94           C  
ATOM   2544  O   TYR A 344      -4.163 -25.484  -7.671  1.00 25.57           O  
ATOM   2545  CB  TYR A 344      -3.974 -28.782  -7.503  1.00 19.73           C  
ATOM   2546  CG  TYR A 344      -2.598 -28.285  -7.916  1.00 18.58           C  
ATOM   2547  CD1 TYR A 344      -1.662 -27.881  -6.944  1.00 19.43           C  
ATOM   2548  CD2 TYR A 344      -2.251 -28.154  -9.250  1.00 17.92           C  
ATOM   2549  CE1 TYR A 344      -0.430 -27.349  -7.304  1.00 17.23           C  
ATOM   2550  CE2 TYR A 344      -0.967 -27.666  -9.617  1.00 18.53           C  
ATOM   2551  CZ  TYR A 344      -0.095 -27.239  -8.634  1.00 23.23           C  
ATOM   2552  OH  TYR A 344       1.136 -26.721  -8.983  1.00 21.84           O  
ATOM   2553  N   ALA A 345      -5.829 -26.533  -8.751  1.00 19.80           N  
ATOM   2554  CA  ALA A 345      -6.063 -25.466  -9.720  1.00 18.98           C  
ATOM   2555  C   ALA A 345      -6.481 -24.171  -9.013  1.00 23.71           C  
ATOM   2556  O   ALA A 345      -6.026 -23.093  -9.390  1.00 25.06           O  
ATOM   2557  CB  ALA A 345      -7.153 -25.893 -10.733  1.00 19.23           C  
ATOM   2558  N   ARG A 346      -7.349 -24.266  -8.006  1.00 19.22           N  
ATOM   2559  CA  ARG A 346      -7.762 -23.088  -7.248  1.00 19.29           C  
ATOM   2560  C   ARG A 346      -6.601 -22.522  -6.451  1.00 22.34           C  
ATOM   2561  O   ARG A 346      -6.455 -21.309  -6.339  1.00 21.56           O  
ATOM   2562  CB  ARG A 346      -8.946 -23.394  -6.321  1.00 19.19           C  
ATOM   2563  CG  ARG A 346     -10.258 -23.494  -7.057  1.00 31.07           C  
ATOM   2564  CD  ARG A 346     -11.433 -23.510  -6.103  1.00 36.05           C  
ATOM   2565  NE  ARG A 346     -11.440 -24.757  -5.363  1.00 44.71           N  
ATOM   2566  CZ  ARG A 346     -11.985 -25.872  -5.818  1.00 62.72           C  
ATOM   2567  NH1 ARG A 346     -12.623 -25.857  -6.976  1.00 57.08           N  
ATOM   2568  NH2 ARG A 346     -11.914 -26.985  -5.109  1.00 52.55           N  
ATOM   2569  N   TRP A 347      -5.726 -23.400  -5.961  1.00 18.53           N  
ATOM   2570  CA  TRP A 347      -4.556 -22.940  -5.213  1.00 17.95           C  
ATOM   2571  C   TRP A 347      -3.588 -22.189  -6.127  1.00 22.57           C  
ATOM   2572  O   TRP A 347      -3.006 -21.183  -5.727  1.00 23.78           O  
ATOM   2573  CB  TRP A 347      -3.848 -24.108  -4.492  1.00 16.45           C  
ATOM   2574  CG  TRP A 347      -2.635 -23.656  -3.726  1.00 15.71           C  
ATOM   2575  CD1 TRP A 347      -2.620 -23.051  -2.511  1.00 17.99           C  
ATOM   2576  CD2 TRP A 347      -1.269 -23.701  -4.174  1.00 15.67           C  
ATOM   2577  NE1 TRP A 347      -1.332 -22.744  -2.147  1.00 16.53           N  
ATOM   2578  CE2 TRP A 347      -0.483 -23.096  -3.164  1.00 17.57           C  
ATOM   2579  CE3 TRP A 347      -0.630 -24.220  -5.323  1.00 16.28           C  
ATOM   2580  CZ2 TRP A 347       0.886 -22.974  -3.264  1.00 17.22           C  
ATOM   2581  CZ3 TRP A 347       0.735 -24.058  -5.443  1.00 16.92           C  
ATOM   2582  CH2 TRP A 347       1.483 -23.457  -4.411  1.00 17.86           C  
ATOM   2583  N   VAL A 348      -3.446 -22.641  -7.377  1.00 17.47           N  
ATOM   2584  CA  VAL A 348      -2.551 -21.964  -8.329  1.00 15.62           C  
ATOM   2585  C   VAL A 348      -3.079 -20.554  -8.672  1.00 20.19           C  
ATOM   2586  O   VAL A 348      -2.316 -19.562  -8.731  1.00 19.85           O  
ATOM   2587  CB  VAL A 348      -2.370 -22.807  -9.620  1.00 18.16           C  
ATOM   2588  CG1 VAL A 348      -1.664 -21.969 -10.760  1.00 15.21           C  
ATOM   2589  CG2 VAL A 348      -1.601 -24.102  -9.299  1.00 17.79           C  
ATOM   2590  N   GLU A 349      -4.369 -20.476  -8.962  1.00 16.79           N  
ATOM   2591  CA  GLU A 349      -5.004 -19.195  -9.231  1.00 17.01           C  
ATOM   2592  C   GLU A 349      -4.718 -18.286  -8.035  1.00 18.38           C  
ATOM   2593  O   GLU A 349      -4.216 -17.207  -8.178  1.00 18.02           O  
ATOM   2594  CB  GLU A 349      -6.520 -19.347  -9.385  1.00 17.66           C  
ATOM   2595  CG  GLU A 349      -7.198 -18.023  -9.627  1.00 20.23           C  
ATOM   2596  CD  GLU A 349      -8.704 -18.113  -9.650  1.00 28.36           C  
ATOM   2597  OE1 GLU A 349      -9.271 -19.175  -9.290  1.00 24.78           O  
ATOM   2598  OE2 GLU A 349      -9.323 -17.076  -9.932  1.00 20.98           O  
ATOM   2599  N   HIS A 350      -4.992 -18.791  -6.844  1.00 16.25           N  
ATOM   2600  CA  HIS A 350      -4.789 -18.066  -5.597  1.00 15.20           C  
ATOM   2601  C   HIS A 350      -3.352 -17.464  -5.472  1.00 18.62           C  
ATOM   2602  O   HIS A 350      -3.202 -16.277  -5.236  1.00 17.75           O  
ATOM   2603  CB  HIS A 350      -5.163 -19.038  -4.433  1.00 14.37           C  
ATOM   2604  CG  HIS A 350      -4.833 -18.545  -3.055  1.00 15.79           C  
ATOM   2605  ND1 HIS A 350      -5.748 -17.871  -2.275  1.00 16.34           N  
ATOM   2606  CD2 HIS A 350      -3.779 -18.817  -2.245  1.00 17.23           C  
ATOM   2607  CE1 HIS A 350      -5.208 -17.623  -1.090  1.00 16.17           C  
ATOM   2608  NE2 HIS A 350      -4.031 -18.227  -1.029  1.00 16.58           N  
ATOM   2609  N   VAL A 351      -2.311 -18.293  -5.580  1.00 15.64           N  
ATOM   2610  CA  VAL A 351      -0.926 -17.818  -5.413  1.00 14.52           C  
ATOM   2611  C   VAL A 351      -0.463 -16.904  -6.540  1.00 19.83           C  
ATOM   2612  O   VAL A 351       0.317 -15.997  -6.314  1.00 17.54           O  
ATOM   2613  CB  VAL A 351       0.106 -18.942  -5.077  1.00 17.38           C  
ATOM   2614  CG1 VAL A 351      -0.270 -19.697  -3.777  1.00 16.78           C  
ATOM   2615  CG2 VAL A 351       0.296 -19.883  -6.240  1.00 16.66           C  
ATOM   2616  N   CYS A 352      -0.961 -17.131  -7.752  1.00 17.50           N  
ATOM   2617  CA  CYS A 352      -0.609 -16.279  -8.873  1.00 16.86           C  
ATOM   2618  C   CYS A 352      -1.170 -14.867  -8.718  1.00 19.88           C  
ATOM   2619  O   CYS A 352      -0.654 -13.929  -9.343  1.00 16.44           O  
ATOM   2620  CB  CYS A 352      -1.144 -16.858 -10.184  1.00 17.82           C  
ATOM   2621  SG  CYS A 352      -0.221 -18.261 -10.778  1.00 21.01           S  
ATOM   2622  N   LYS A 353      -2.212 -14.725  -7.885  1.00 16.55           N  
ATOM   2623  CA  LYS A 353      -2.857 -13.437  -7.645  1.00 15.42           C  
ATOM   2624  C   LYS A 353      -2.379 -12.781  -6.383  1.00 16.95           C  
ATOM   2625  O   LYS A 353      -2.730 -11.647  -6.111  1.00 14.66           O  
ATOM   2626  CB  LYS A 353      -4.377 -13.567  -7.627  1.00 16.16           C  
ATOM   2627  CG  LYS A 353      -4.988 -13.844  -8.999  1.00 14.34           C  
ATOM   2628  CD  LYS A 353      -6.498 -13.882  -8.874  1.00 18.87           C  
ATOM   2629  CE  LYS A 353      -7.146 -14.214 -10.189  1.00 27.42           C  
ATOM   2630  NZ  LYS A 353      -8.585 -14.466 -10.032  1.00 34.49           N  
ATOM   2631  N   GLY A 354      -1.578 -13.492  -5.603  1.00 15.18           N  
ATOM   2632  CA  GLY A 354      -0.980 -12.879  -4.408  1.00 15.11           C  
ATOM   2633  C   GLY A 354      -1.264 -13.572  -3.087  1.00 19.97           C  
ATOM   2634  O   GLY A 354      -0.795 -13.117  -2.047  1.00 19.66           O  
ATOM   2635  N   GLY A 355      -2.075 -14.621  -3.110  1.00 16.37           N  
ATOM   2636  CA  GLY A 355      -2.414 -15.333  -1.872  1.00 16.59           C  
ATOM   2637  C   GLY A 355      -1.222 -16.170  -1.367  1.00 21.47           C  
ATOM   2638  O   GLY A 355      -0.374 -16.595  -2.142  1.00 20.89           O  
ATOM   2639  N   VAL A 356      -1.173 -16.409  -0.058  1.00 18.02           N  
ATOM   2640  CA  VAL A 356      -0.102 -17.197   0.537  1.00 15.42           C  
ATOM   2641  C   VAL A 356      -0.679 -18.427   1.242  1.00 17.40           C  
ATOM   2642  O   VAL A 356      -0.047 -18.976   2.144  1.00 17.13           O  
ATOM   2643  CB  VAL A 356       0.774 -16.324   1.493  1.00 19.08           C  
ATOM   2644  CG1 VAL A 356       1.476 -15.207   0.711  1.00 18.32           C  
ATOM   2645  CG2 VAL A 356      -0.068 -15.724   2.657  1.00 18.65           C  
ATOM   2646  N   GLY A 357      -1.889 -18.848   0.871  1.00 13.79           N  
ATOM   2647  CA  GLY A 357      -2.502 -20.027   1.525  1.00 13.87           C  
ATOM   2648  C   GLY A 357      -1.544 -21.219   1.505  1.00 19.68           C  
ATOM   2649  O   GLY A 357      -0.966 -21.547   0.454  1.00 18.25           O  
ATOM   2650  N   GLN A 358      -1.373 -21.866   2.660  1.00 16.36           N  
ATOM   2651  CA  GLN A 358      -0.448 -22.997   2.764  1.00 16.47           C  
ATOM   2652  C   GLN A 358      -0.727 -24.238   1.893  1.00 20.11           C  
ATOM   2653  O   GLN A 358      -1.824 -24.778   1.902  1.00 18.31           O  
ATOM   2654  CB  GLN A 358      -0.263 -23.415   4.228  1.00 17.38           C  
ATOM   2655  CG  GLN A 358       0.877 -24.444   4.411  1.00 18.53           C  
ATOM   2656  CD  GLN A 358       0.991 -25.001   5.806  1.00 23.69           C  
ATOM   2657  OE1 GLN A 358       0.023 -25.072   6.553  1.00 20.35           O  
ATOM   2658  NE2 GLN A 358       2.211 -25.314   6.202  1.00 16.97           N  
ATOM   2659  N   PHE A 359       0.287 -24.711   1.178  1.00 17.96           N  
ATOM   2660  CA  PHE A 359       0.187 -25.977   0.404  1.00 18.40           C  
ATOM   2661  C   PHE A 359       1.246 -26.880   1.053  1.00 23.41           C  
ATOM   2662  O   PHE A 359       2.420 -26.628   0.932  1.00 23.04           O  
ATOM   2663  CB  PHE A 359       0.491 -25.758  -1.079  1.00 20.13           C  
ATOM   2664  CG  PHE A 359       0.571 -27.037  -1.897  1.00 22.34           C  
ATOM   2665  CD1 PHE A 359       0.102 -28.249  -1.400  1.00 25.07           C  
ATOM   2666  CD2 PHE A 359       1.086 -27.013  -3.187  1.00 24.29           C  
ATOM   2667  CE1 PHE A 359       0.186 -29.432  -2.165  1.00 25.35           C  
ATOM   2668  CE2 PHE A 359       1.145 -28.188  -3.961  1.00 27.18           C  
ATOM   2669  CZ  PHE A 359       0.688 -29.399  -3.440  1.00 24.28           C  
ATOM   2670  N   GLU A 360       0.834 -27.791   1.914  1.00 22.81           N  
ATOM   2671  CA  GLU A 360       1.803 -28.602   2.650  1.00 22.80           C  
ATOM   2672  C   GLU A 360       1.944 -30.039   2.129  1.00 26.24           C  
ATOM   2673  O   GLU A 360       0.941 -30.696   1.784  1.00 26.27           O  
ATOM   2674  CB  GLU A 360       1.431 -28.640   4.138  1.00 24.19           C  
ATOM   2675  CG  GLU A 360       2.529 -29.201   5.067  1.00 30.54           C  
ATOM   2676  CD  GLU A 360       2.235 -28.929   6.538  1.00 38.28           C  
ATOM   2677  OE1 GLU A 360       1.056 -28.786   6.912  1.00 39.55           O  
ATOM   2678  OE2 GLU A 360       3.184 -28.798   7.328  1.00 38.06           O  
ATOM   2679  N   ILE A 361       3.199 -30.498   2.077  1.00 21.18           N  
ATOM   2680  CA  ILE A 361       3.566 -31.841   1.655  1.00 20.52           C  
ATOM   2681  C   ILE A 361       4.569 -32.405   2.655  1.00 27.16           C  
ATOM   2682  O   ILE A 361       5.709 -31.903   2.789  1.00 26.15           O  
ATOM   2683  CB  ILE A 361       4.184 -31.874   0.237  1.00 23.80           C  
ATOM   2684  CG1 ILE A 361       3.195 -31.399  -0.831  1.00 22.88           C  
ATOM   2685  CG2 ILE A 361       4.703 -33.305  -0.085  1.00 24.13           C  
ATOM   2686  CD1 ILE A 361       3.837 -31.298  -2.187  1.00 19.91           C  
ATOM   2687  N   LEU A 362       4.156 -33.473   3.342  1.00 23.81           N  
ATOM   2688  CA  LEU A 362       5.034 -34.184   4.268  1.00 22.11           C  
ATOM   2689  C   LEU A 362       5.250 -35.587   3.710  1.00 27.43           C  
ATOM   2690  O   LEU A 362       4.308 -36.236   3.281  1.00 26.68           O  
ATOM   2691  CB  LEU A 362       4.347 -34.300   5.621  1.00 21.38           C  
ATOM   2692  CG  LEU A 362       4.121 -32.955   6.285  1.00 25.59           C  
ATOM   2693  CD1 LEU A 362       3.151 -33.115   7.448  1.00 27.23           C  
ATOM   2694  CD2 LEU A 362       5.420 -32.443   6.805  1.00 26.32           C  
ATOM   2695  N   TYR A 363       6.493 -36.047   3.700  1.00 24.84           N  
ATOM   2696  CA  TYR A 363       6.806 -37.394   3.236  1.00 24.77           C  
ATOM   2697  C   TYR A 363       7.800 -38.075   4.185  1.00 31.86           C  
ATOM   2698  O   TYR A 363       8.437 -37.424   4.998  1.00 30.11           O  
ATOM   2699  CB  TYR A 363       7.319 -37.408   1.798  1.00 24.23           C  
ATOM   2700  CG  TYR A 363       8.667 -36.748   1.612  1.00 25.66           C  
ATOM   2701  CD1 TYR A 363       9.836 -37.516   1.539  1.00 27.04           C  
ATOM   2702  CD2 TYR A 363       8.777 -35.352   1.464  1.00 26.26           C  
ATOM   2703  CE1 TYR A 363      11.070 -36.918   1.349  1.00 28.58           C  
ATOM   2704  CE2 TYR A 363      10.028 -34.735   1.268  1.00 27.07           C  
ATOM   2705  CZ  TYR A 363      11.164 -35.519   1.218  1.00 36.27           C  
ATOM   2706  OH  TYR A 363      12.403 -34.923   1.067  1.00 36.58           O  
ATOM   2707  N   ALA A 364       7.921 -39.394   4.075  1.00 32.67           N  
ATOM   2708  CA  ALA A 364       8.806 -40.160   4.955  1.00 33.69           C  
ATOM   2709  C   ALA A 364       9.023 -41.565   4.414  1.00 41.60           C  
ATOM   2710  O   ALA A 364       8.266 -42.038   3.561  1.00 41.35           O  
ATOM   2711  CB  ALA A 364       8.204 -40.245   6.366  1.00 33.77           C  
ATOM   2712  N   GLN A 365      10.055 -42.229   4.931  1.00 41.23           N  
ATOM   2713  CA  GLN A 365      10.366 -43.625   4.577  1.00 46.01           C  
ATOM   2714  C   GLN A 365       9.437 -44.542   5.367  1.00 53.39           C  
ATOM   2715  O   GLN A 365       8.870 -45.474   4.759  1.00 63.91           O  
ATOM   2716  CB  GLN A 365      11.822 -43.969   4.902  1.00 47.05           C  
ATOM   2717  CG  GLN A 365      12.534 -44.740   3.804  1.00 65.93           C  
ATOM   2718  CD  GLN A 365      13.997 -45.005   4.122  1.00 80.58           C  
ATOM   2719  OXT GLN A 365       9.223 -44.270   6.566  1.00 57.73           O  
TER    2720      GLN A 365                                                      
ATOM   2721  N   VAL C   8      50.514 -65.461  28.086  1.00 54.85           N  
ATOM   2722  CA  VAL C   8      50.461 -64.000  27.943  1.00 53.96           C  
ATOM   2723  C   VAL C   8      49.016 -63.543  28.112  1.00 53.68           C  
ATOM   2724  O   VAL C   8      48.082 -64.302  27.806  1.00 56.79           O  
ATOM   2725  CB  VAL C   8      51.020 -63.533  26.570  1.00 57.95           C  
ATOM   2726  N   THR C   9      48.817 -62.326  28.608  1.00 41.67           N  
ATOM   2727  CA  THR C   9      47.461 -61.824  28.747  1.00 38.74           C  
ATOM   2728  C   THR C   9      47.137 -61.106  27.444  1.00 34.74           C  
ATOM   2729  O   THR C   9      47.821 -60.161  27.043  1.00 31.02           O  
ATOM   2730  CB  THR C   9      47.252 -60.931  29.998  1.00 46.75           C  
ATOM   2731  OG1 THR C   9      47.461 -61.705  31.184  1.00 54.66           O  
ATOM   2732  CG2 THR C   9      45.847 -60.403  30.031  1.00 39.76           C  
ATOM   2733  N   THR C  10      46.092 -61.579  26.780  1.00 29.53           N  
ATOM   2734  CA  THR C  10      45.689 -61.010  25.516  1.00 29.03           C  
ATOM   2735  C   THR C  10      44.238 -60.618  25.512  1.00 30.95           C  
ATOM   2736  O   THR C  10      43.403 -61.374  25.954  1.00 34.05           O  
ATOM   2737  CB  THR C  10      45.995 -61.955  24.344  1.00 38.52           C  
ATOM   2738  OG1 THR C  10      47.412 -62.124  24.245  1.00 39.43           O  
ATOM   2739  CG2 THR C  10      45.495 -61.360  23.031  1.00 36.05           C  
ATOM   2740  N   ALA C  11      43.942 -59.429  25.001  1.00 24.16           N  
ATOM   2741  CA  ALA C  11      42.577 -58.980  24.840  1.00 22.46           C  
ATOM   2742  C   ALA C  11      42.243 -59.122  23.341  1.00 27.48           C  
ATOM   2743  O   ALA C  11      42.976 -58.601  22.503  1.00 26.52           O  
ATOM   2744  CB  ALA C  11      42.470 -57.518  25.253  1.00 22.35           C  
ATOM   2745  N   HIS C  12      41.176 -59.858  23.004  1.00 24.22           N  
ATOM   2746  CA  HIS C  12      40.728 -60.031  21.603  1.00 23.39           C  
ATOM   2747  C   HIS C  12      39.392 -59.339  21.506  1.00 24.15           C  
ATOM   2748  O   HIS C  12      38.493 -59.662  22.264  1.00 22.29           O  
ATOM   2749  CB  HIS C  12      40.474 -61.499  21.269  1.00 24.73           C  
ATOM   2750  CG  HIS C  12      41.671 -62.372  21.456  1.00 30.10           C  
ATOM   2751  ND1 HIS C  12      42.685 -62.461  20.520  1.00 32.63           N  
ATOM   2752  CD2 HIS C  12      42.044 -63.160  22.496  1.00 32.73           C  
ATOM   2753  CE1 HIS C  12      43.624 -63.274  20.974  1.00 33.03           C  
ATOM   2754  NE2 HIS C  12      43.258 -63.714  22.168  1.00 33.22           N  
ATOM   2755  N   SER C  13      39.257 -58.364  20.619  1.00 19.08           N  
ATOM   2756  CA  SER C  13      37.977 -57.673  20.507  1.00 18.74           C  
ATOM   2757  C   SER C  13      37.689 -57.363  19.045  1.00 23.34           C  
ATOM   2758  O   SER C  13      38.587 -57.217  18.233  1.00 23.06           O  
ATOM   2759  CB  SER C  13      37.963 -56.376  21.323  1.00 20.53           C  
ATOM   2760  OG  SER C  13      39.076 -55.562  21.009  1.00 24.33           O  
ATOM   2761  N   ASP C  14      36.425 -57.192  18.747  1.00 21.90           N  
ATOM   2762  CA  ASP C  14      35.996 -56.910  17.399  1.00 23.58           C  
ATOM   2763  C   ASP C  14      34.818 -55.971  17.528  1.00 24.10           C  
ATOM   2764  O   ASP C  14      33.873 -56.280  18.255  1.00 23.63           O  
ATOM   2765  CB  ASP C  14      35.506 -58.204  16.769  1.00 27.60           C  
ATOM   2766  CG  ASP C  14      36.009 -58.378  15.391  1.00 54.12           C  
ATOM   2767  OD1 ASP C  14      35.377 -57.812  14.471  1.00 59.03           O  
ATOM   2768  OD2 ASP C  14      37.090 -58.991  15.240  1.00 66.61           O  
ATOM   2769  N   TYR C  15      34.875 -54.820  16.863  1.00 18.43           N  
ATOM   2770  CA  TYR C  15      33.775 -53.850  16.929  1.00 18.11           C  
ATOM   2771  C   TYR C  15      33.284 -53.551  15.513  1.00 23.54           C  
ATOM   2772  O   TYR C  15      34.062 -53.468  14.567  1.00 22.76           O  
ATOM   2773  CB  TYR C  15      34.241 -52.529  17.586  1.00 19.63           C  
ATOM   2774  CG  TYR C  15      35.108 -52.718  18.812  1.00 22.66           C  
ATOM   2775  CD1 TYR C  15      34.574 -53.228  20.007  1.00 24.76           C  
ATOM   2776  CD2 TYR C  15      36.468 -52.486  18.750  1.00 23.27           C  
ATOM   2777  CE1 TYR C  15      35.386 -53.418  21.145  1.00 23.98           C  
ATOM   2778  CE2 TYR C  15      37.291 -52.680  19.866  1.00 24.41           C  
ATOM   2779  CZ  TYR C  15      36.741 -53.112  21.067  1.00 28.50           C  
ATOM   2780  OH  TYR C  15      37.577 -53.353  22.144  1.00 21.99           O  
ATOM   2781  N   GLU C  16      31.996 -53.317  15.367  1.00 23.14           N  
ATOM   2782  CA  GLU C  16      31.494 -53.011  14.046  1.00 24.42           C  
ATOM   2783  C   GLU C  16      30.374 -52.021  14.110  1.00 27.56           C  
ATOM   2784  O   GLU C  16      29.459 -52.197  14.884  1.00 27.01           O  
ATOM   2785  CB  GLU C  16      31.010 -54.284  13.355  1.00 26.24           C  
ATOM   2786  CG  GLU C  16      30.161 -53.999  12.122  1.00 43.73           C  
ATOM   2787  CD  GLU C  16      29.826 -55.260  11.337  1.00 67.38           C  
ATOM   2788  OE1 GLU C  16      30.121 -56.369  11.829  1.00 70.89           O  
ATOM   2789  OE2 GLU C  16      29.297 -55.143  10.215  1.00 67.78           O  
ATOM   2790  N   ILE C  17      30.460 -50.969  13.304  1.00 23.91           N  
ATOM   2791  CA  ILE C  17      29.409 -49.953  13.223  1.00 24.24           C  
ATOM   2792  C   ILE C  17      28.907 -49.891  11.771  1.00 27.26           C  
ATOM   2793  O   ILE C  17      29.701 -49.748  10.840  1.00 26.42           O  
ATOM   2794  CB  ILE C  17      29.920 -48.570  13.638  1.00 27.58           C  
ATOM   2795  CG1 ILE C  17      30.696 -48.646  14.949  1.00 28.61           C  
ATOM   2796  CG2 ILE C  17      28.779 -47.551  13.682  1.00 27.97           C  
ATOM   2797  CD1 ILE C  17      31.396 -47.375  15.305  1.00 35.79           C  
ATOM   2798  N   VAL C  18      27.595 -49.997  11.582  1.00 23.17           N  
ATOM   2799  CA  VAL C  18      26.997 -49.885  10.239  1.00 21.96           C  
ATOM   2800  C   VAL C  18      26.108 -48.665  10.294  1.00 27.19           C  
ATOM   2801  O   VAL C  18      25.142 -48.659  11.020  1.00 26.72           O  
ATOM   2802  CB  VAL C  18      26.143 -51.153   9.861  1.00 23.37           C  
ATOM   2803  CG1 VAL C  18      25.475 -50.948   8.483  1.00 21.42           C  
ATOM   2804  CG2 VAL C  18      27.009 -52.413   9.871  1.00 22.61           C  
ATOM   2805  N   LEU C  19      26.432 -47.620   9.558  1.00 27.28           N  
ATOM   2806  CA  LEU C  19      25.612 -46.393   9.596  1.00 29.30           C  
ATOM   2807  C   LEU C  19      24.477 -46.330   8.560  1.00 39.24           C  
ATOM   2808  O   LEU C  19      24.638 -46.816   7.437  1.00 38.45           O  
ATOM   2809  CB  LEU C  19      26.499 -45.150   9.429  1.00 28.43           C  
ATOM   2810  CG  LEU C  19      27.570 -45.004  10.506  1.00 33.44           C  
ATOM   2811  CD1 LEU C  19      28.547 -43.922  10.132  1.00 33.25           C  
ATOM   2812  CD2 LEU C  19      26.899 -44.684  11.844  1.00 35.70           C  
ATOM   2813  N   GLU C  20      23.367 -45.679   8.930  1.00 41.37           N  
ATOM   2814  CA  GLU C  20      22.231 -45.425   8.017  1.00 44.60           C  
ATOM   2815  C   GLU C  20      22.444 -44.071   7.333  1.00 56.29           C  
ATOM   2816  O   GLU C  20      23.035 -43.164   7.919  1.00 55.96           O  
ATOM   2817  CB  GLU C  20      20.925 -45.337   8.776  1.00 45.74           C  
ATOM   2818  CG  GLU C  20      20.224 -46.635   8.961  1.00 56.24           C  
ATOM   2819  CD  GLU C  20      18.839 -46.440   9.553  1.00 84.76           C  
ATOM   2820  OE1 GLU C  20      18.224 -45.351   9.341  1.00 48.43           O  
ATOM   2821  OE2 GLU C  20      18.395 -47.370  10.262  1.00 87.36           O  
ATOM   2822  N   GLY C  21      21.933 -43.921   6.115  1.00 57.38           N  
ATOM   2823  CA  GLY C  21      22.130 -42.683   5.347  1.00 58.69           C  
ATOM   2824  C   GLY C  21      21.301 -41.462   5.759  1.00 66.23           C  
ATOM   2825  O   GLY C  21      20.248 -41.596   6.389  1.00 67.05           O  
ATOM   2826  N   GLY C  22      21.725 -40.283   5.302  1.00 63.52           N  
ATOM   2827  N   SER C  23      20.791 -37.662   7.551  1.00 65.00           N  
ATOM   2828  CA  SER C  23      20.105 -36.982   8.649  1.00 63.30           C  
ATOM   2829  C   SER C  23      19.759 -38.043   9.673  1.00 61.63           C  
ATOM   2830  O   SER C  23      19.786 -37.799  10.885  1.00 62.63           O  
ATOM   2831  CB  SER C  23      18.835 -36.264   8.162  1.00 67.91           C  
ATOM   2832  N   SER C  24      19.450 -39.237   9.177  1.00 51.57           N  
ATOM   2833  CA  SER C  24      19.253 -40.368  10.067  1.00 48.44           C  
ATOM   2834  C   SER C  24      20.611 -40.562  10.761  1.00 47.62           C  
ATOM   2835  O   SER C  24      21.687 -40.666  10.113  1.00 49.17           O  
ATOM   2836  CB  SER C  24      18.899 -41.636   9.289  1.00 49.32           C  
ATOM   2837  OG  SER C  24      18.932 -42.768  10.128  1.00 51.44           O  
ATOM   2838  N   SER C  25      20.553 -40.558  12.084  1.00 35.08           N  
ATOM   2839  CA  SER C  25      21.720 -40.735  12.902  1.00 31.15           C  
ATOM   2840  C   SER C  25      21.756 -42.188  13.364  1.00 30.75           C  
ATOM   2841  O   SER C  25      22.525 -42.540  14.257  1.00 30.01           O  
ATOM   2842  CB  SER C  25      21.563 -39.817  14.110  1.00 30.79           C  
ATOM   2843  OG  SER C  25      20.325 -40.057  14.755  1.00 29.29           O  
ATOM   2844  N   TRP C  26      20.870 -43.016  12.827  1.00 26.21           N  
ATOM   2845  CA  TRP C  26      20.794 -44.424  13.257  1.00 25.75           C  
ATOM   2846  C   TRP C  26      22.044 -45.230  12.906  1.00 29.89           C  
ATOM   2847  O   TRP C  26      22.708 -44.969  11.885  1.00 28.32           O  
ATOM   2848  CB  TRP C  26      19.581 -45.145  12.658  1.00 22.74           C  
ATOM   2849  CG  TRP C  26      18.275 -44.821  13.341  1.00 23.35           C  
ATOM   2850  CD1 TRP C  26      17.552 -43.645  13.235  1.00 25.68           C  
ATOM   2851  CD2 TRP C  26      17.472 -45.712  14.161  1.00 22.45           C  
ATOM   2852  NE1 TRP C  26      16.383 -43.746  13.967  1.00 24.59           N  
ATOM   2853  CE2 TRP C  26      16.295 -45.001  14.519  1.00 25.68           C  
ATOM   2854  CE3 TRP C  26      17.661 -47.011  14.656  1.00 23.54           C  
ATOM   2855  CZ2 TRP C  26      15.310 -45.549  15.349  1.00 24.82           C  
ATOM   2856  CZ3 TRP C  26      16.691 -47.565  15.462  1.00 25.13           C  
ATOM   2857  CH2 TRP C  26      15.513 -46.829  15.801  1.00 25.93           C  
ATOM   2858  N   GLY C  27      22.336 -46.221  13.749  1.00 25.52           N  
ATOM   2859  CA  GLY C  27      23.440 -47.130  13.461  1.00 25.04           C  
ATOM   2860  C   GLY C  27      23.206 -48.455  14.133  1.00 27.31           C  
ATOM   2861  O   GLY C  27      22.431 -48.540  15.087  1.00 27.44           O  
ATOM   2862  N   LYS C  28      23.855 -49.489  13.599  1.00 23.72           N  
ATOM   2863  CA  LYS C  28      23.860 -50.806  14.214  1.00 24.30           C  
ATOM   2864  C   LYS C  28      25.251 -50.952  14.835  1.00 28.56           C  
ATOM   2865  O   LYS C  28      26.265 -50.665  14.176  1.00 27.06           O  
ATOM   2866  CB  LYS C  28      23.692 -51.897  13.161  1.00 27.36           C  
ATOM   2867  CG  LYS C  28      22.309 -52.014  12.594  1.00 36.90           C  
ATOM   2868  CD  LYS C  28      22.225 -53.294  11.762  1.00 48.38           C  
ATOM   2869  CE  LYS C  28      21.558 -53.021  10.422  1.00 67.23           C  
ATOM   2870  NZ  LYS C  28      20.118 -52.670  10.600  1.00 87.18           N  
ATOM   2871  N   VAL C  29      25.314 -51.418  16.075  1.00 25.25           N  
ATOM   2872  CA  VAL C  29      26.610 -51.600  16.741  1.00 23.61           C  
ATOM   2873  C   VAL C  29      26.708 -53.016  17.214  1.00 26.08           C  
ATOM   2874  O   VAL C  29      25.787 -53.522  17.872  1.00 25.99           O  
ATOM   2875  CB  VAL C  29      26.777 -50.604  17.935  1.00 26.36           C  
ATOM   2876  CG1 VAL C  29      28.077 -50.869  18.703  1.00 26.94           C  
ATOM   2877  CG2 VAL C  29      26.723 -49.181  17.452  1.00 24.33           C  
ATOM   2878  N   LYS C  30      27.805 -53.666  16.855  1.00 22.81           N  
ATOM   2879  CA  LYS C  30      28.118 -55.018  17.320  1.00 23.44           C  
ATOM   2880  C   LYS C  30      29.507 -54.999  17.963  1.00 26.62           C  
ATOM   2881  O   LYS C  30      30.427 -54.392  17.410  1.00 25.86           O  
ATOM   2882  CB  LYS C  30      28.162 -55.998  16.160  1.00 26.57           C  
ATOM   2883  CG  LYS C  30      26.828 -56.463  15.659  1.00 51.79           C  
ATOM   2884  CD  LYS C  30      27.036 -57.575  14.643  1.00 65.51           C  
ATOM   2885  N   ALA C  31      29.672 -55.706  19.079  1.00 22.32           N  
ATOM   2886  CA  ALA C  31      30.987 -55.828  19.750  1.00 21.44           C  
ATOM   2887  C   ALA C  31      31.125 -57.202  20.406  1.00 24.58           C  
ATOM   2888  O   ALA C  31      30.169 -57.712  20.995  1.00 23.63           O  
ATOM   2889  CB  ALA C  31      31.144 -54.756  20.823  1.00 21.95           C  
ATOM   2890  N   ARG C  32      32.310 -57.788  20.292  1.00 20.44           N  
ATOM   2891  CA  ARG C  32      32.669 -59.034  20.977  1.00 21.46           C  
ATOM   2892  C   ARG C  32      34.028 -58.774  21.621  1.00 25.09           C  
ATOM   2893  O   ARG C  32      34.890 -58.136  21.016  1.00 24.00           O  
ATOM   2894  CB  ARG C  32      32.838 -60.221  20.017  1.00 22.96           C  
ATOM   2895  CG  ARG C  32      31.802 -60.313  18.899  1.00 42.23           C  
ATOM   2896  CD  ARG C  32      30.602 -61.169  19.260  1.00 48.14           C  
ATOM   2897  NE  ARG C  32      29.546 -60.293  19.726  1.00 63.63           N  
ATOM   2898  CZ  ARG C  32      28.397 -60.061  19.110  1.00 64.84           C  
ATOM   2899  NH1 ARG C  32      28.063 -60.693  17.994  1.00 57.42           N  
ATOM   2900  NH2 ARG C  32      27.571 -59.190  19.650  1.00 42.13           N  
ATOM   2901  N   ALA C  33      34.226 -59.267  22.838  1.00 20.89           N  
ATOM   2902  CA  ALA C  33      35.526 -59.116  23.478  1.00 19.96           C  
ATOM   2903  C   ALA C  33      35.772 -60.271  24.391  1.00 25.03           C  
ATOM   2904  O   ALA C  33      34.841 -60.809  24.997  1.00 23.65           O  
ATOM   2905  CB  ALA C  33      35.621 -57.806  24.255  1.00 20.36           C  
ATOM   2906  N   LYS C  34      37.039 -60.627  24.528  1.00 23.96           N  
ATOM   2907  CA  LYS C  34      37.411 -61.664  25.464  1.00 24.75           C  
ATOM   2908  C   LYS C  34      38.817 -61.421  25.975  1.00 27.43           C  
ATOM   2909  O   LYS C  34      39.690 -61.024  25.207  1.00 28.24           O  
ATOM   2910  CB  LYS C  34      37.178 -63.059  24.881  1.00 27.52           C  
ATOM   2911  CG  LYS C  34      38.385 -63.792  24.446  1.00 47.22           C  
ATOM   2912  CD  LYS C  34      38.280 -65.247  24.891  1.00 63.31           C  
ATOM   2913  N   VAL C  35      38.972 -61.455  27.300  1.00 22.40           N  
ATOM   2914  CA  VAL C  35      40.284 -61.245  27.926  1.00 21.73           C  
ATOM   2915  C   VAL C  35      40.497 -62.272  29.017  1.00 23.57           C  
ATOM   2916  O   VAL C  35      39.585 -62.541  29.804  1.00 22.93           O  
ATOM   2917  CB  VAL C  35      40.546 -59.794  28.418  1.00 24.37           C  
ATOM   2918  CG1 VAL C  35      39.642 -59.417  29.541  1.00 24.11           C  
ATOM   2919  CG2 VAL C  35      42.038 -59.633  28.887  1.00 23.80           C  
ATOM   2920  N   ASN C  36      41.677 -62.881  29.022  1.00 19.39           N  
ATOM   2921  CA  ASN C  36      41.988 -63.883  30.036  1.00 20.84           C  
ATOM   2922  C   ASN C  36      42.685 -63.231  31.231  1.00 25.49           C  
ATOM   2923  O   ASN C  36      43.848 -63.475  31.490  1.00 25.87           O  
ATOM   2924  CB  ASN C  36      42.816 -65.041  29.430  1.00 22.99           C  
ATOM   2925  CG  ASN C  36      44.126 -64.573  28.849  1.00 43.65           C  
ATOM   2926  OD1 ASN C  36      44.244 -63.430  28.388  1.00 39.73           O  
ATOM   2927  ND2 ASN C  36      45.134 -65.426  28.916  1.00 34.86           N  
ATOM   2928  N   ALA C  37      41.972 -62.349  31.919  1.00 21.56           N  
ATOM   2929  CA  ALA C  37      42.499 -61.704  33.121  1.00 21.12           C  
ATOM   2930  C   ALA C  37      41.300 -61.710  34.070  1.00 23.44           C  
ATOM   2931  O   ALA C  37      40.156 -61.661  33.608  1.00 21.39           O  
ATOM   2932  CB  ALA C  37      42.958 -60.283  32.831  1.00 21.67           C  
ATOM   2933  N   PRO C  38      41.551 -61.873  35.368  1.00 19.18           N  
ATOM   2934  CA  PRO C  38      40.439 -61.916  36.336  1.00 19.56           C  
ATOM   2935  C   PRO C  38      39.750 -60.567  36.522  1.00 22.88           C  
ATOM   2936  O   PRO C  38      40.368 -59.519  36.503  1.00 20.08           O  
ATOM   2937  CB  PRO C  38      41.111 -62.354  37.648  1.00 20.26           C  
ATOM   2938  CG  PRO C  38      42.577 -61.993  37.489  1.00 23.36           C  
ATOM   2939  CD  PRO C  38      42.872 -62.077  35.996  1.00 18.66           C  
ATOM   2940  N   PRO C  39      38.443 -60.607  36.713  1.00 21.20           N  
ATOM   2941  CA  PRO C  39      37.688 -59.389  36.966  1.00 19.25           C  
ATOM   2942  C   PRO C  39      37.981 -58.926  38.405  1.00 22.17           C  
ATOM   2943  O   PRO C  39      38.399 -59.720  39.271  1.00 21.07           O  
ATOM   2944  CB  PRO C  39      36.231 -59.850  36.841  1.00 20.84           C  
ATOM   2945  CG  PRO C  39      36.259 -61.299  37.085  1.00 25.54           C  
ATOM   2946  CD  PRO C  39      37.578 -61.799  36.597  1.00 22.07           C  
ATOM   2947  N   ALA C  40      37.780 -57.646  38.670  1.00 17.30           N  
ATOM   2948  CA  ALA C  40      38.000 -57.168  40.024  1.00 17.77           C  
ATOM   2949  C   ALA C  40      36.748 -57.298  40.895  1.00 22.10           C  
ATOM   2950  O   ALA C  40      36.392 -56.368  41.580  1.00 22.97           O  
ATOM   2951  CB  ALA C  40      38.503 -55.699  40.018  1.00 18.05           C  
ATOM   2952  N   SER C  41      36.062 -58.428  40.845  1.00 18.53           N  
ATOM   2953  CA  SER C  41      34.888 -58.626  41.722  1.00 17.34           C  
ATOM   2954  C   SER C  41      35.273 -59.541  42.886  1.00 19.44           C  
ATOM   2955  O   SER C  41      35.860 -60.584  42.664  1.00 19.09           O  
ATOM   2956  CB  SER C  41      33.733 -59.265  40.939  1.00 19.25           C  
ATOM   2957  OG  SER C  41      32.666 -59.568  41.820  1.00 24.30           O  
ATOM   2958  N   PRO C  42      34.980 -59.129  44.121  1.00 16.03           N  
ATOM   2959  CA  PRO C  42      35.337 -59.933  45.276  1.00 15.34           C  
ATOM   2960  C   PRO C  42      34.447 -61.182  45.422  1.00 19.80           C  
ATOM   2961  O   PRO C  42      34.699 -62.016  46.301  1.00 17.14           O  
ATOM   2962  CB  PRO C  42      35.180 -58.963  46.474  1.00 15.92           C  
ATOM   2963  CG  PRO C  42      34.253 -57.889  45.979  1.00 20.33           C  
ATOM   2964  CD  PRO C  42      34.528 -57.768  44.506  1.00 16.43           C  
ATOM   2965  N   LEU C  43      33.450 -61.316  44.533  1.00 16.89           N  
ATOM   2966  CA  LEU C  43      32.585 -62.527  44.441  1.00 16.28           C  
ATOM   2967  C   LEU C  43      32.578 -63.017  42.981  1.00 21.96           C  
ATOM   2968  O   LEU C  43      32.241 -62.278  42.051  1.00 22.82           O  
ATOM   2969  CB  LEU C  43      31.133 -62.239  44.912  1.00 15.64           C  
ATOM   2970  CG  LEU C  43      30.974 -62.093  46.418  1.00 18.51           C  
ATOM   2971  CD1 LEU C  43      29.563 -61.692  46.705  1.00 19.13           C  
ATOM   2972  CD2 LEU C  43      31.346 -63.398  47.125  1.00 17.93           C  
ATOM   2973  N   LEU C  44      32.989 -64.255  42.784  1.00 20.36           N  
ATOM   2974  CA  LEU C  44      33.035 -64.883  41.452  1.00 20.74           C  
ATOM   2975  C   LEU C  44      32.395 -66.255  41.627  1.00 25.46           C  
ATOM   2976  O   LEU C  44      32.394 -66.791  42.736  1.00 26.52           O  
ATOM   2977  CB  LEU C  44      34.502 -65.018  40.962  1.00 20.50           C  
ATOM   2978  CG  LEU C  44      35.206 -63.699  40.536  1.00 23.50           C  
ATOM   2979  CD1 LEU C  44      36.708 -63.809  40.182  1.00 21.46           C  
ATOM   2980  CD2 LEU C  44      34.440 -62.956  39.412  1.00 21.27           C  
ATOM   2981  N   PRO C  45      31.757 -66.783  40.582  1.00 21.34           N  
ATOM   2982  CA  PRO C  45      31.710 -66.128  39.273  1.00 20.15           C  
ATOM   2983  C   PRO C  45      30.600 -65.092  39.220  1.00 23.29           C  
ATOM   2984  O   PRO C  45      29.760 -65.006  40.123  1.00 21.02           O  
ATOM   2985  CB  PRO C  45      31.410 -67.276  38.298  1.00 21.96           C  
ATOM   2986  CG  PRO C  45      31.052 -68.457  39.125  1.00 24.68           C  
ATOM   2987  CD  PRO C  45      31.591 -68.243  40.497  1.00 19.98           C  
ATOM   2988  N   ALA C  46      30.596 -64.321  38.133  1.00 19.75           N  
ATOM   2989  CA  ALA C  46      29.581 -63.305  37.913  1.00 19.22           C  
ATOM   2990  C   ALA C  46      29.230 -63.231  36.404  1.00 25.34           C  
ATOM   2991  O   ALA C  46      30.072 -62.925  35.565  1.00 25.45           O  
ATOM   2992  CB  ALA C  46      30.108 -61.928  38.423  1.00 19.44           C  
ATOM   2993  N   ASP C  47      27.982 -63.544  36.083  1.00 22.12           N  
ATOM   2994  CA  ASP C  47      27.461 -63.491  34.717  1.00 20.21           C  
ATOM   2995  C   ASP C  47      26.295 -62.506  34.720  1.00 23.83           C  
ATOM   2996  O   ASP C  47      25.537 -62.416  35.697  1.00 23.36           O  
ATOM   2997  CB  ASP C  47      26.902 -64.860  34.289  1.00 21.52           C  
ATOM   2998  CG  ASP C  47      27.940 -65.985  34.346  1.00 29.85           C  
ATOM   2999  OD1 ASP C  47      29.144 -65.734  34.209  1.00 29.59           O  
ATOM   3000  OD2 ASP C  47      27.538 -67.159  34.498  1.00 45.31           O  
ATOM   3001  N   CYS C  48      26.098 -61.821  33.597  1.00 21.79           N  
ATOM   3002  CA  CYS C  48      25.004 -60.867  33.481  1.00 22.02           C  
ATOM   3003  C   CYS C  48      24.527 -60.717  32.053  1.00 26.86           C  
ATOM   3004  O   CYS C  48      25.341 -60.681  31.120  1.00 26.39           O  
ATOM   3005  CB  CYS C  48      25.454 -59.493  33.995  1.00 22.56           C  
ATOM   3006  SG  CYS C  48      24.162 -58.228  34.126  1.00 26.37           S  
ATOM   3007  N   ASP C  49      23.203 -60.623  31.897  1.00 23.50           N  
ATOM   3008  CA  ASP C  49      22.546 -60.381  30.602  1.00 23.23           C  
ATOM   3009  C   ASP C  49      21.671 -59.142  30.759  1.00 25.23           C  
ATOM   3010  O   ASP C  49      21.045 -58.944  31.810  1.00 24.87           O  
ATOM   3011  CB  ASP C  49      21.648 -61.544  30.188  1.00 26.16           C  
ATOM   3012  CG  ASP C  49      22.438 -62.772  29.819  1.00 42.01           C  
ATOM   3013  OD1 ASP C  49      22.064 -63.866  30.277  1.00 46.21           O  
ATOM   3014  OD2 ASP C  49      23.463 -62.633  29.128  1.00 45.76           O  
ATOM   3015  N   VAL C  50      21.692 -58.291  29.737  1.00 20.28           N  
ATOM   3016  CA  VAL C  50      20.934 -57.048  29.727  1.00 19.92           C  
ATOM   3017  C   VAL C  50      20.197 -56.933  28.413  1.00 25.67           C  
ATOM   3018  O   VAL C  50      20.743 -57.206  27.327  1.00 24.81           O  
ATOM   3019  CB  VAL C  50      21.854 -55.853  29.884  1.00 24.12           C  
ATOM   3020  CG1 VAL C  50      21.080 -54.590  30.226  1.00 22.75           C  
ATOM   3021  CG2 VAL C  50      22.854 -56.162  30.920  1.00 25.23           C  
ATOM   3022  N   LYS C  51      18.946 -56.514  28.525  1.00 23.17           N  
ATOM   3023  CA  LYS C  51      18.114 -56.312  27.362  1.00 23.43           C  
ATOM   3024  C   LYS C  51      17.387 -54.973  27.539  1.00 27.20           C  
ATOM   3025  O   LYS C  51      16.815 -54.705  28.589  1.00 26.71           O  
ATOM   3026  CB  LYS C  51      17.145 -57.489  27.220  1.00 26.48           C  
ATOM   3027  CG  LYS C  51      16.619 -57.704  25.805  1.00 49.14           C  
ATOM   3028  N   LEU C  52      17.532 -54.089  26.556  1.00 24.74           N  
ATOM   3029  CA  LEU C  52      16.901 -52.750  26.583  1.00 25.10           C  
ATOM   3030  C   LEU C  52      16.118 -52.575  25.284  1.00 28.12           C  
ATOM   3031  O   LEU C  52      16.572 -52.990  24.206  1.00 26.21           O  
ATOM   3032  CB  LEU C  52      17.958 -51.625  26.689  1.00 25.50           C  
ATOM   3033  CG  LEU C  52      18.903 -51.656  27.901  1.00 31.57           C  
ATOM   3034  CD1 LEU C  52      19.902 -50.545  27.754  1.00 33.65           C  
ATOM   3035  CD2 LEU C  52      18.123 -51.432  29.164  1.00 34.56           C  
ATOM   3036  N   ASN C  53      14.946 -51.951  25.399  1.00 24.31           N  
ATOM   3037  CA  ASN C  53      14.070 -51.742  24.250  1.00 24.21           C  
ATOM   3038  C   ASN C  53      13.402 -50.423  24.471  1.00 26.53           C  
ATOM   3039  O   ASN C  53      13.001 -50.122  25.581  1.00 26.58           O  
ATOM   3040  CB  ASN C  53      12.930 -52.805  24.215  1.00 26.13           C  
ATOM   3041  CG  ASN C  53      13.439 -54.202  23.949  1.00 62.56           C  
ATOM   3042  OD1 ASN C  53      13.704 -54.971  24.880  1.00 64.83           O  
ATOM   3043  ND2 ASN C  53      13.541 -54.559  22.675  1.00 54.58           N  
ATOM   3044  N   VAL C  54      13.205 -49.678  23.399  1.00 21.99           N  
ATOM   3045  CA  VAL C  54      12.476 -48.431  23.483  1.00 21.26           C  
ATOM   3046  C   VAL C  54      11.632 -48.265  22.227  1.00 28.00           C  
ATOM   3047  O   VAL C  54      12.056 -48.634  21.136  1.00 28.38           O  
ATOM   3048  CB  VAL C  54      13.375 -47.211  23.757  1.00 23.37           C  
ATOM   3049  CG1 VAL C  54      14.307 -46.908  22.540  1.00 21.56           C  
ATOM   3050  CG2 VAL C  54      12.474 -45.981  24.075  1.00 23.25           C  
ATOM   3051  N   LYS C  55      10.419 -47.756  22.398  1.00 26.96           N  
ATOM   3052  CA  LYS C  55       9.510 -47.532  21.278  1.00 27.46           C  
ATOM   3053  C   LYS C  55       8.769 -46.202  21.409  1.00 31.57           C  
ATOM   3054  O   LYS C  55       8.485 -45.739  22.522  1.00 29.46           O  
ATOM   3055  CB  LYS C  55       8.515 -48.699  21.140  1.00 29.75           C  
ATOM   3056  CG  LYS C  55       7.478 -48.772  22.214  1.00 37.45           C  
ATOM   3057  CD  LYS C  55       6.953 -50.189  22.354  1.00 45.27           C  
ATOM   3058  CE  LYS C  55       5.728 -50.241  23.263  1.00 61.86           C  
ATOM   3059  NZ  LYS C  55       4.679 -51.188  22.768  1.00 74.86           N  
ATOM   3060  N   PRO C  56       8.497 -45.583  20.261  1.00 29.83           N  
ATOM   3061  CA  PRO C  56       7.728 -44.337  20.205  1.00 30.31           C  
ATOM   3062  C   PRO C  56       6.335 -44.627  20.765  1.00 38.02           C  
ATOM   3063  O   PRO C  56       5.712 -45.639  20.447  1.00 37.28           O  
ATOM   3064  CB  PRO C  56       7.635 -44.047  18.707  1.00 31.34           C  
ATOM   3065  CG  PRO C  56       8.609 -44.956  18.053  1.00 34.72           C  
ATOM   3066  CD  PRO C  56       8.753 -46.138  18.920  1.00 30.36           C  
ATOM   3067  N   LEU C  57       5.897 -43.788  21.681  1.00 39.77           N  
ATOM   3068  CA  LEU C  57       4.610 -43.977  22.335  1.00 42.18           C  
ATOM   3069  C   LEU C  57       3.653 -42.953  21.723  1.00 52.41           C  
ATOM   3070  O   LEU C  57       2.728 -43.295  20.998  1.00 52.47           O  
ATOM   3071  CB  LEU C  57       4.769 -43.715  23.833  1.00 42.22           C  
ATOM   3072  CG  LEU C  57       3.819 -44.429  24.773  1.00 46.61           C  
ATOM   3073  CD1 LEU C  57       3.899 -45.886  24.463  1.00 47.69           C  
ATOM   3074  CD2 LEU C  57       4.164 -44.144  26.233  1.00 47.47           C  
ATOM   3075  N   ASP C  58       3.927 -41.682  21.980  1.00 54.18           N  
ATOM   3076  CA  ASP C  58       3.114 -40.597  21.432  1.00 56.10           C  
ATOM   3077  C   ASP C  58       4.019 -39.448  20.991  1.00 61.22           C  
ATOM   3078  O   ASP C  58       4.330 -38.551  21.774  1.00 60.94           O  
ATOM   3079  CB  ASP C  58       2.082 -40.125  22.475  1.00 58.66           C  
ATOM   3080  CG  ASP C  58       1.465 -38.778  22.130  1.00 73.33           C  
ATOM   3081  OD1 ASP C  58       1.483 -38.374  20.937  1.00 73.55           O  
ATOM   3082  OD2 ASP C  58       0.950 -38.133  23.068  1.00 81.39           O  
ATOM   3083  N   PRO C  59       4.433 -39.485  19.731  1.00 59.57           N  
ATOM   3084  CA  PRO C  59       5.329 -38.462  19.176  1.00 60.19           C  
ATOM   3085  C   PRO C  59       4.830 -37.003  19.298  1.00 65.77           C  
ATOM   3086  O   PRO C  59       5.629 -36.049  19.223  1.00 65.49           O  
ATOM   3087  CB  PRO C  59       5.460 -38.874  17.706  1.00 61.66           C  
ATOM   3088  CG  PRO C  59       5.295 -40.380  17.727  1.00 65.61           C  
ATOM   3089  CD  PRO C  59       4.429 -40.725  18.933  1.00 61.10           C  
ATOM   3090  N   ALA C  60       3.518 -36.825  19.479  1.00 62.57           N  
ATOM   3091  CA  ALA C  60       2.953 -35.474  19.613  1.00 62.25           C  
ATOM   3092  C   ALA C  60       3.404 -34.819  20.925  1.00 64.64           C  
ATOM   3093  O   ALA C  60       3.722 -33.621  20.970  1.00 64.35           O  
ATOM   3094  CB  ALA C  60       1.426 -35.507  19.531  1.00 62.91           C  
ATOM   3095  N   LYS C  61       3.433 -35.609  21.993  1.00 58.67           N  
ATOM   3096  CA  LYS C  61       3.862 -35.092  23.278  1.00 57.16           C  
ATOM   3097  C   LYS C  61       5.308 -35.495  23.613  1.00 56.01           C  
ATOM   3098  O   LYS C  61       5.814 -35.170  24.696  1.00 56.07           O  
ATOM   3099  CB  LYS C  61       2.865 -35.469  24.388  1.00 60.31           C  
ATOM   3100  CG  LYS C  61       2.835 -36.949  24.746  1.00 81.04           C  
ATOM   3101  N   GLY C  62       5.981 -36.149  22.657  1.00 47.28           N  
ATOM   3102  CA  GLY C  62       7.374 -36.584  22.834  1.00 44.62           C  
ATOM   3103  C   GLY C  62       7.624 -37.819  23.753  1.00 44.26           C  
ATOM   3104  O   GLY C  62       8.770 -38.078  24.158  1.00 42.32           O  
ATOM   3105  N   PHE C  63       6.570 -38.584  24.054  1.00 37.22           N  
ATOM   3106  CA  PHE C  63       6.697 -39.757  24.922  1.00 35.18           C  
ATOM   3107  C   PHE C  63       7.261 -41.004  24.241  1.00 35.39           C  
ATOM   3108  O   PHE C  63       6.842 -41.369  23.154  1.00 34.85           O  
ATOM   3109  CB  PHE C  63       5.340 -40.111  25.559  1.00 36.49           C  
ATOM   3110  CG  PHE C  63       5.119 -39.487  26.912  1.00 37.77           C  
ATOM   3111  CD1 PHE C  63       5.594 -40.103  28.066  1.00 40.42           C  
ATOM   3112  CD2 PHE C  63       4.432 -38.285  27.029  1.00 39.29           C  
ATOM   3113  CE1 PHE C  63       5.410 -39.513  29.320  1.00 41.24           C  
ATOM   3114  CE2 PHE C  63       4.247 -37.690  28.268  1.00 41.72           C  
ATOM   3115  CZ  PHE C  63       4.739 -38.308  29.421  1.00 39.82           C  
ATOM   3116  N   VAL C  64       8.123 -41.717  24.957  1.00 28.48           N  
ATOM   3117  CA  VAL C  64       8.663 -43.002  24.496  1.00 25.57           C  
ATOM   3118  C   VAL C  64       8.491 -43.960  25.678  1.00 28.49           C  
ATOM   3119  O   VAL C  64       8.411 -43.549  26.840  1.00 26.22           O  
ATOM   3120  CB  VAL C  64      10.155 -42.918  24.022  1.00 27.15           C  
ATOM   3121  CG1 VAL C  64      10.340 -41.807  23.002  1.00 25.93           C  
ATOM   3122  CG2 VAL C  64      11.109 -42.752  25.209  1.00 26.69           C  
ATOM   3123  N   ARG C  65       8.384 -45.238  25.376  1.00 26.24           N  
ATOM   3124  CA  ARG C  65       8.252 -46.219  26.422  1.00 27.57           C  
ATOM   3125  C   ARG C  65       9.528 -47.048  26.408  1.00 31.31           C  
ATOM   3126  O   ARG C  65       9.870 -47.663  25.401  1.00 29.04           O  
ATOM   3127  CB  ARG C  65       7.045 -47.135  26.178  1.00 30.56           C  
ATOM   3128  CG  ARG C  65       7.066 -48.337  27.128  1.00 38.71           C  
ATOM   3129  CD  ARG C  65       5.677 -48.879  27.396  1.00 46.04           C  
ATOM   3130  NE  ARG C  65       4.779 -47.852  27.894  1.00 52.79           N  
ATOM   3131  CZ  ARG C  65       3.462 -47.871  27.708  1.00 68.66           C  
ATOM   3132  NH1 ARG C  65       2.912 -48.860  27.007  1.00 61.09           N  
ATOM   3133  NH2 ARG C  65       2.694 -46.906  28.213  1.00 48.46           N  
ATOM   3134  N   ILE C  66      10.247 -47.040  27.524  1.00 29.03           N  
ATOM   3135  CA  ILE C  66      11.497 -47.785  27.593  1.00 29.17           C  
ATOM   3136  C   ILE C  66      11.347 -48.963  28.526  1.00 31.31           C  
ATOM   3137  O   ILE C  66      10.657 -48.872  29.537  1.00 31.82           O  
ATOM   3138  CB  ILE C  66      12.689 -46.858  27.968  1.00 32.87           C  
ATOM   3139  CG1 ILE C  66      14.018 -47.594  27.934  1.00 33.81           C  
ATOM   3140  CG2 ILE C  66      12.514 -46.288  29.323  1.00 35.57           C  
ATOM   3141  CD1 ILE C  66      15.190 -46.622  27.750  1.00 39.09           C  
ATOM   3142  N   SER C  67      11.955 -50.085  28.170  1.00 26.94           N  
ATOM   3143  CA  SER C  67      11.896 -51.227  29.062  1.00 27.63           C  
ATOM   3144  C   SER C  67      13.262 -51.867  29.178  1.00 33.38           C  
ATOM   3145  O   SER C  67      14.002 -51.952  28.188  1.00 34.15           O  
ATOM   3146  CB  SER C  67      10.829 -52.222  28.639  1.00 31.33           C  
ATOM   3147  OG  SER C  67      11.287 -52.982  27.556  1.00 44.40           O  
ATOM   3148  N   ALA C  68      13.638 -52.200  30.411  1.00 28.14           N  
ATOM   3149  CA  ALA C  68      14.934 -52.800  30.678  1.00 27.33           C  
ATOM   3150  C   ALA C  68      14.810 -54.059  31.523  1.00 30.18           C  
ATOM   3151  O   ALA C  68      14.013 -54.115  32.480  1.00 30.24           O  
ATOM   3152  CB  ALA C  68      15.842 -51.773  31.394  1.00 28.08           C  
ATOM   3153  N   VAL C  69      15.651 -55.044  31.219  1.00 25.12           N  
ATOM   3154  CA  VAL C  69      15.726 -56.264  32.014  1.00 24.70           C  
ATOM   3155  C   VAL C  69      17.190 -56.545  32.296  1.00 28.54           C  
ATOM   3156  O   VAL C  69      17.995 -56.645  31.355  1.00 27.31           O  
ATOM   3157  CB  VAL C  69      15.116 -57.482  31.284  1.00 29.29           C  
ATOM   3158  CG1 VAL C  69      15.144 -58.706  32.217  1.00 28.66           C  
ATOM   3159  CG2 VAL C  69      13.685 -57.180  30.840  1.00 29.38           C  
ATOM   3160  N   PHE C  70      17.526 -56.722  33.577  1.00 25.72           N  
ATOM   3161  CA  PHE C  70      18.883 -57.096  33.988  1.00 24.50           C  
ATOM   3162  C   PHE C  70      18.789 -58.437  34.662  1.00 30.18           C  
ATOM   3163  O   PHE C  70      17.990 -58.593  35.584  1.00 31.55           O  
ATOM   3164  CB  PHE C  70      19.451 -56.105  34.988  1.00 24.88           C  
ATOM   3165  CG  PHE C  70      19.635 -54.736  34.423  1.00 26.42           C  
ATOM   3166  CD1 PHE C  70      20.885 -54.313  33.976  1.00 30.91           C  
ATOM   3167  CD2 PHE C  70      18.571 -53.855  34.343  1.00 27.75           C  
ATOM   3168  CE1 PHE C  70      21.056 -53.029  33.443  1.00 31.06           C  
ATOM   3169  CE2 PHE C  70      18.746 -52.571  33.811  1.00 30.15           C  
ATOM   3170  CZ  PHE C  70      19.975 -52.166  33.364  1.00 27.97           C  
ATOM   3171  N   GLU C  71      19.612 -59.398  34.250  1.00 24.55           N  
ATOM   3172  CA  GLU C  71      19.578 -60.674  34.927  1.00 24.63           C  
ATOM   3173  C   GLU C  71      20.998 -61.126  35.194  1.00 25.68           C  
ATOM   3174  O   GLU C  71      21.828 -61.119  34.288  1.00 24.48           O  
ATOM   3175  CB  GLU C  71      18.901 -61.694  34.028  1.00 26.73           C  
ATOM   3176  CG  GLU C  71      17.472 -61.943  34.324  1.00 45.92           C  
ATOM   3177  CD  GLU C  71      16.931 -63.044  33.440  1.00 73.64           C  
ATOM   3178  OE1 GLU C  71      16.655 -62.757  32.253  1.00 58.27           O  
ATOM   3179  OE2 GLU C  71      16.910 -64.213  33.895  1.00 73.97           O  
ATOM   3180  N   SER C  72      21.289 -61.570  36.412  1.00 22.03           N  
ATOM   3181  CA  SER C  72      22.667 -62.012  36.675  1.00 22.33           C  
ATOM   3182  C   SER C  72      22.725 -63.170  37.638  1.00 25.57           C  
ATOM   3183  O   SER C  72      21.725 -63.476  38.280  1.00 25.05           O  
ATOM   3184  CB  SER C  72      23.530 -60.840  37.194  1.00 23.79           C  
ATOM   3185  OG  SER C  72      23.040 -60.354  38.440  1.00 27.56           O  
ATOM   3186  N   ILE C  73      23.893 -63.811  37.720  1.00 22.17           N  
ATOM   3187  CA  ILE C  73      24.152 -64.860  38.705  1.00 22.21           C  
ATOM   3188  C   ILE C  73      25.475 -64.483  39.311  1.00 25.57           C  
ATOM   3189  O   ILE C  73      26.455 -64.324  38.588  1.00 26.44           O  
ATOM   3190  CB  ILE C  73      24.243 -66.254  38.087  1.00 26.40           C  
ATOM   3191  CG1 ILE C  73      22.969 -66.564  37.337  1.00 28.74           C  
ATOM   3192  CG2 ILE C  73      24.424 -67.302  39.195  1.00 26.71           C  
ATOM   3193  CD1 ILE C  73      22.784 -68.044  37.072  1.00 46.79           C  
ATOM   3194  N   VAL C  74      25.485 -64.254  40.617  1.00 20.44           N  
ATOM   3195  CA  VAL C  74      26.698 -63.852  41.330  1.00 20.32           C  
ATOM   3196  C   VAL C  74      26.952 -64.833  42.456  1.00 22.99           C  
ATOM   3197  O   VAL C  74      26.164 -64.908  43.416  1.00 21.13           O  
ATOM   3198  CB  VAL C  74      26.578 -62.382  41.911  1.00 23.63           C  
ATOM   3199  CG1 VAL C  74      27.856 -62.013  42.687  1.00 21.84           C  
ATOM   3200  CG2 VAL C  74      26.293 -61.384  40.767  1.00 23.32           C  
ATOM   3201  N   ASP C  75      28.047 -65.574  42.340  1.00 20.75           N  
ATOM   3202  CA  ASP C  75      28.395 -66.594  43.340  1.00 20.96           C  
ATOM   3203  C   ASP C  75      27.194 -67.496  43.605  1.00 25.04           C  
ATOM   3204  O   ASP C  75      26.829 -67.741  44.742  1.00 24.93           O  
ATOM   3205  CB  ASP C  75      28.882 -65.936  44.653  1.00 22.08           C  
ATOM   3206  CG  ASP C  75      29.559 -66.930  45.584  1.00 30.53           C  
ATOM   3207  OD1 ASP C  75      29.960 -68.000  45.063  1.00 33.21           O  
ATOM   3208  OD2 ASP C  75      29.662 -66.677  46.818  1.00 29.08           O  
ATOM   3209  N   SER C  76      26.525 -67.928  42.548  1.00 25.52           N  
ATOM   3210  CA  SER C  76      25.323 -68.783  42.682  1.00 27.20           C  
ATOM   3211  C   SER C  76      23.994 -68.130  43.062  1.00 33.33           C  
ATOM   3212  O   SER C  76      22.974 -68.806  43.053  1.00 35.93           O  
ATOM   3213  CB  SER C  76      25.579 -69.972  43.601  1.00 31.75           C  
ATOM   3214  OG  SER C  76      25.204 -69.643  44.932  1.00 43.36           O  
ATOM   3215  N   THR C  77      23.976 -66.835  43.365  1.00 27.47           N  
ATOM   3216  CA  THR C  77      22.720 -66.148  43.691  1.00 26.65           C  
ATOM   3217  C   THR C  77      22.145 -65.558  42.410  1.00 31.63           C  
ATOM   3218  O   THR C  77      22.837 -64.848  41.695  1.00 32.35           O  
ATOM   3219  CB  THR C  77      22.956 -64.978  44.713  1.00 32.09           C  
ATOM   3220  OG1 THR C  77      23.531 -65.477  45.917  1.00 30.77           O  
ATOM   3221  CG2 THR C  77      21.673 -64.237  45.015  1.00 26.60           C  
ATOM   3222  N   LYS C  78      20.887 -65.848  42.113  1.00 28.44           N  
ATOM   3223  CA  LYS C  78      20.232 -65.301  40.921  1.00 28.27           C  
ATOM   3224  C   LYS C  78      19.545 -63.976  41.254  1.00 28.64           C  
ATOM   3225  O   LYS C  78      18.751 -63.890  42.181  1.00 26.20           O  
ATOM   3226  CB  LYS C  78      19.169 -66.269  40.387  1.00 31.87           C  
ATOM   3227  CG  LYS C  78      19.701 -67.615  39.927  1.00 51.57           C  
ATOM   3228  CD  LYS C  78      18.717 -68.290  38.974  1.00 70.97           C  
ATOM   3229  CE  LYS C  78      19.053 -69.766  38.755  1.00 92.80           C  
ATOM   3230  NZ  LYS C  78      19.669 -70.405  39.957  1.00103.06           N  
ATOM   3231  N   ASN C  79      19.851 -62.946  40.484  1.00 24.87           N  
ATOM   3232  CA  ASN C  79      19.243 -61.637  40.690  1.00 23.99           C  
ATOM   3233  C   ASN C  79      18.535 -61.200  39.409  1.00 26.66           C  
ATOM   3234  O   ASN C  79      18.884 -61.601  38.319  1.00 25.68           O  
ATOM   3235  CB  ASN C  79      20.315 -60.611  41.028  1.00 21.58           C  
ATOM   3236  CG  ASN C  79      21.394 -61.173  41.906  1.00 33.18           C  
ATOM   3237  OD1 ASN C  79      21.277 -61.176  43.127  1.00 32.57           O  
ATOM   3238  ND2 ASN C  79      22.488 -61.589  41.293  1.00 23.36           N  
ATOM   3239  N   LYS C  80      17.559 -60.333  39.554  1.00 23.92           N  
ATOM   3240  CA  LYS C  80      16.843 -59.831  38.401  1.00 23.58           C  
ATOM   3241  C   LYS C  80      16.243 -58.459  38.715  1.00 29.56           C  
ATOM   3242  O   LYS C  80      15.725 -58.230  39.816  1.00 30.15           O  
ATOM   3243  CB  LYS C  80      15.714 -60.810  38.017  1.00 24.37           C  
ATOM   3244  CG  LYS C  80      14.875 -60.338  36.852  1.00 36.53           C  
ATOM   3245  CD  LYS C  80      14.283 -61.509  36.111  1.00 46.80           C  
ATOM   3246  CE  LYS C  80      13.053 -61.093  35.311  1.00 53.59           C  
ATOM   3247  NZ  LYS C  80      12.565 -62.193  34.429  1.00 54.87           N  
ATOM   3248  N   LEU C  81      16.281 -57.569  37.729  1.00 25.02           N  
ATOM   3249  CA  LEU C  81      15.623 -56.288  37.841  1.00 25.75           C  
ATOM   3250  C   LEU C  81      14.957 -55.951  36.508  1.00 27.66           C  
ATOM   3251  O   LEU C  81      15.579 -56.071  35.442  1.00 27.27           O  
ATOM   3252  CB  LEU C  81      16.606 -55.176  38.203  1.00 27.55           C  
ATOM   3253  CG  LEU C  81      15.919 -53.792  38.333  1.00 33.70           C  
ATOM   3254  CD1 LEU C  81      15.762 -53.424  39.778  1.00 34.56           C  
ATOM   3255  CD2 LEU C  81      16.738 -52.729  37.648  1.00 37.62           C  
ATOM   3256  N   THR C  82      13.686 -55.569  36.559  1.00 22.22           N  
ATOM   3257  CA  THR C  82      12.994 -55.142  35.358  1.00 23.01           C  
ATOM   3258  C   THR C  82      12.428 -53.781  35.651  1.00 28.48           C  
ATOM   3259  O   THR C  82      12.031 -53.480  36.781  1.00 27.49           O  
ATOM   3260  CB  THR C  82      11.833 -56.071  34.931  1.00 29.08           C  
ATOM   3261  OG1 THR C  82      10.798 -55.957  35.897  1.00 37.75           O  
ATOM   3262  CG2 THR C  82      12.269 -57.508  34.834  1.00 21.98           C  
ATOM   3263  N   ILE C  83      12.375 -52.960  34.619  1.00 26.96           N  
ATOM   3264  CA  ILE C  83      11.801 -51.643  34.747  1.00 28.24           C  
ATOM   3265  C   ILE C  83      11.145 -51.228  33.434  1.00 32.56           C  
ATOM   3266  O   ILE C  83      11.594 -51.609  32.352  1.00 31.06           O  
ATOM   3267  CB  ILE C  83      12.801 -50.612  35.325  1.00 32.63           C  
ATOM   3268  CG1 ILE C  83      12.332 -49.187  35.078  1.00 33.31           C  
ATOM   3269  CG2 ILE C  83      14.208 -50.827  34.813  1.00 34.69           C  
ATOM   3270  CD1 ILE C  83      12.575 -48.289  36.273  1.00 47.46           C  
ATOM   3271  N   GLU C  84      10.007 -50.547  33.533  1.00 29.66           N  
ATOM   3272  CA  GLU C  84       9.295 -50.067  32.340  1.00 29.33           C  
ATOM   3273  C   GLU C  84       8.902 -48.638  32.650  1.00 30.19           C  
ATOM   3274  O   GLU C  84       8.390 -48.350  33.728  1.00 28.54           O  
ATOM   3275  CB  GLU C  84       8.039 -50.896  32.081  1.00 31.15           C  
ATOM   3276  CG  GLU C  84       8.298 -52.199  31.355  1.00 48.94           C  
ATOM   3277  CD  GLU C  84       7.232 -52.510  30.330  1.00 84.16           C  
ATOM   3278  OE1 GLU C  84       6.419 -51.606  30.026  1.00 72.87           O  
ATOM   3279  OE2 GLU C  84       7.217 -53.658  29.829  1.00 87.60           O  
ATOM   3280  N   ALA C  85       9.199 -47.722  31.743  1.00 25.83           N  
ATOM   3281  CA  ALA C  85       8.900 -46.316  32.037  1.00 25.37           C  
ATOM   3282  C   ALA C  85       8.504 -45.548  30.799  1.00 27.44           C  
ATOM   3283  O   ALA C  85       8.939 -45.863  29.697  1.00 28.63           O  
ATOM   3284  CB  ALA C  85      10.110 -45.626  32.708  1.00 26.05           C  
ATOM   3285  N   ASP C  86       7.707 -44.516  31.001  1.00 22.04           N  
ATOM   3286  CA  ASP C  86       7.308 -43.626  29.920  1.00 23.34           C  
ATOM   3287  C   ASP C  86       8.057 -42.320  30.219  1.00 26.58           C  
ATOM   3288  O   ASP C  86       7.989 -41.782  31.330  1.00 25.59           O  
ATOM   3289  CB  ASP C  86       5.793 -43.366  29.959  1.00 26.39           C  
ATOM   3290  CG  ASP C  86       4.974 -44.580  29.525  1.00 36.26           C  
ATOM   3291  OD1 ASP C  86       5.543 -45.521  28.938  1.00 35.75           O  
ATOM   3292  OD2 ASP C  86       3.765 -44.597  29.810  1.00 42.81           O  
ATOM   3293  N   ILE C  87       8.772 -41.808  29.230  1.00 22.60           N  
ATOM   3294  CA  ILE C  87       9.581 -40.625  29.455  1.00 22.92           C  
ATOM   3295  C   ILE C  87       9.349 -39.586  28.384  1.00 27.14           C  
ATOM   3296  O   ILE C  87       9.220 -39.928  27.210  1.00 25.89           O  
ATOM   3297  CB  ILE C  87      11.104 -41.023  29.487  1.00 25.48           C  
ATOM   3298  CG1 ILE C  87      11.358 -42.036  30.598  1.00 25.29           C  
ATOM   3299  CG2 ILE C  87      12.003 -39.754  29.594  1.00 23.34           C  
ATOM   3300  CD1 ILE C  87      12.694 -42.681  30.524  1.00 37.42           C  
ATOM   3301  N   ALA C  88       9.391 -38.314  28.780  1.00 23.12           N  
ATOM   3302  CA  ALA C  88       9.225 -37.231  27.808  1.00 23.26           C  
ATOM   3303  C   ALA C  88       9.913 -35.974  28.261  1.00 25.79           C  
ATOM   3304  O   ALA C  88       9.985 -35.687  29.465  1.00 24.44           O  
ATOM   3305  CB  ALA C  88       7.726 -36.913  27.579  1.00 23.44           C  
ATOM   3306  N   ASN C  89      10.352 -35.186  27.284  1.00 21.66           N  
ATOM   3307  CA  ASN C  89      10.873 -33.876  27.598  1.00 22.89           C  
ATOM   3308  C   ASN C  89       9.641 -32.981  27.804  1.00 28.15           C  
ATOM   3309  O   ASN C  89       8.716 -33.059  27.023  1.00 27.27           O  
ATOM   3310  CB  ASN C  89      11.677 -33.319  26.408  1.00 20.25           C  
ATOM   3311  CG  ASN C  89      13.093 -33.862  26.346  1.00 34.18           C  
ATOM   3312  OD1 ASN C  89      13.766 -34.053  27.363  1.00 30.83           O  
ATOM   3313  ND2 ASN C  89      13.546 -34.126  25.140  1.00 22.28           N  
ATOM   3314  N   GLU C  90       9.636 -32.130  28.829  1.00 26.90           N  
ATOM   3315  CA  GLU C  90       8.585 -31.135  28.997  1.00 28.04           C  
ATOM   3316  C   GLU C  90       9.130 -29.855  28.396  1.00 33.02           C  
ATOM   3317  O   GLU C  90       8.444 -29.172  27.651  1.00 36.01           O  
ATOM   3318  CB  GLU C  90       8.261 -30.883  30.461  1.00 29.72           C  
ATOM   3319  CG  GLU C  90       7.191 -31.763  30.983  1.00 44.21           C  
ATOM   3320  CD  GLU C  90       6.620 -31.200  32.234  1.00 66.61           C  
ATOM   3321  OE1 GLU C  90       7.097 -30.131  32.647  1.00 61.89           O  
ATOM   3322  OE2 GLU C  90       5.701 -31.815  32.795  1.00 66.32           O  
ATOM   3323  N   THR C  91      10.358 -29.512  28.768  1.00 27.31           N  
ATOM   3324  CA  THR C  91      11.087 -28.371  28.195  1.00 26.22           C  
ATOM   3325  C   THR C  91      12.480 -28.902  27.846  1.00 29.57           C  
ATOM   3326  O   THR C  91      12.725 -30.101  27.911  1.00 28.08           O  
ATOM   3327  CB  THR C  91      11.205 -27.182  29.165  1.00 32.72           C  
ATOM   3328  OG1 THR C  91      12.096 -27.517  30.237  1.00 32.48           O  
ATOM   3329  CG2 THR C  91       9.824 -26.759  29.718  1.00 28.16           C  
ATOM   3330  N   LYS C  92      13.396 -28.003  27.518  1.00 28.13           N  
ATOM   3331  CA  LYS C  92      14.766 -28.380  27.181  1.00 28.66           C  
ATOM   3332  C   LYS C  92      15.566 -28.712  28.463  1.00 32.02           C  
ATOM   3333  O   LYS C  92      16.487 -29.498  28.424  1.00 31.93           O  
ATOM   3334  CB  LYS C  92      15.443 -27.270  26.378  1.00 31.00           C  
ATOM   3335  CG  LYS C  92      15.580 -25.974  27.154  1.00 51.00           C  
ATOM   3336  CD  LYS C  92      15.875 -24.803  26.240  1.00 66.92           C  
ATOM   3337  CE  LYS C  92      15.460 -23.485  26.888  1.00 81.19           C  
ATOM   3338  NZ  LYS C  92      16.579 -22.831  27.632  1.00 90.84           N  
ATOM   3339  N   GLU C  93      15.132 -28.193  29.609  1.00 28.69           N  
ATOM   3340  CA  GLU C  93      15.784 -28.502  30.883  1.00 28.80           C  
ATOM   3341  C   GLU C  93      15.054 -29.512  31.766  1.00 31.74           C  
ATOM   3342  O   GLU C  93      15.658 -30.088  32.662  1.00 32.85           O  
ATOM   3343  CB  GLU C  93      15.986 -27.242  31.718  1.00 30.36           C  
ATOM   3344  CG  GLU C  93      16.905 -26.246  31.080  1.00 48.91           C  
ATOM   3345  CD  GLU C  93      16.225 -24.935  30.860  1.00 85.79           C  
ATOM   3346  OE1 GLU C  93      15.001 -24.944  30.578  1.00 81.04           O  
ATOM   3347  OE2 GLU C  93      16.908 -23.899  31.013  1.00 92.71           O  
ATOM   3348  N   ARG C  94      13.761 -29.702  31.524  1.00 25.91           N  
ATOM   3349  CA  ARG C  94      12.913 -30.543  32.356  1.00 24.08           C  
ATOM   3350  C   ARG C  94      12.352 -31.768  31.646  1.00 28.51           C  
ATOM   3351  O   ARG C  94      11.740 -31.655  30.585  1.00 27.72           O  
ATOM   3352  CB  ARG C  94      11.764 -29.705  32.933  1.00 23.40           C  
ATOM   3353  CG  ARG C  94      10.994 -30.429  34.004  1.00 34.30           C  
ATOM   3354  CD  ARG C  94      10.165 -29.507  34.870  1.00 47.52           C  
ATOM   3355  NE  ARG C  94       8.917 -30.169  35.232  1.00 67.30           N  
ATOM   3356  CZ  ARG C  94       8.734 -30.859  36.355  1.00 80.43           C  
ATOM   3357  NH1 ARG C  94       7.566 -31.461  36.594  1.00 51.14           N  
ATOM   3358  NH2 ARG C  94       9.714 -30.931  37.250  1.00 74.70           N  
ATOM   3359  N   ARG C  95      12.602 -32.943  32.233  1.00 23.79           N  
ATOM   3360  CA  ARG C  95      12.149 -34.214  31.694  1.00 22.32           C  
ATOM   3361  C   ARG C  95      11.306 -34.903  32.790  1.00 26.17           C  
ATOM   3362  O   ARG C  95      11.563 -34.730  33.984  1.00 23.57           O  
ATOM   3363  CB  ARG C  95      13.380 -35.075  31.328  1.00 19.53           C  
ATOM   3364  CG  ARG C  95      13.139 -36.261  30.397  1.00 17.40           C  
ATOM   3365  CD  ARG C  95      14.479 -36.873  29.931  1.00 19.04           C  
ATOM   3366  NE  ARG C  95      15.190 -36.006  28.996  1.00 19.96           N  
ATOM   3367  CZ  ARG C  95      16.507 -35.973  28.823  1.00 34.27           C  
ATOM   3368  NH1 ARG C  95      17.318 -36.774  29.518  1.00 18.94           N  
ATOM   3369  NH2 ARG C  95      17.014 -35.128  27.936  1.00 19.05           N  
ATOM   3370  N   ILE C  96      10.279 -35.648  32.388  1.00 23.11           N  
ATOM   3371  CA  ILE C  96       9.432 -36.323  33.359  1.00 24.23           C  
ATOM   3372  C   ILE C  96       9.346 -37.796  33.019  1.00 24.86           C  
ATOM   3373  O   ILE C  96       9.568 -38.199  31.886  1.00 22.93           O  
ATOM   3374  CB  ILE C  96       8.005 -35.687  33.461  1.00 29.04           C  
ATOM   3375  CG1 ILE C  96       7.206 -35.967  32.181  1.00 30.30           C  
ATOM   3376  CG2 ILE C  96       8.108 -34.179  33.746  1.00 30.00           C  
ATOM   3377  CD1 ILE C  96       6.119 -34.981  31.937  1.00 45.06           C  
ATOM   3378  N   SER C  97       9.036 -38.598  34.025  1.00 22.49           N  
ATOM   3379  CA  SER C  97       8.923 -40.033  33.826  1.00 22.92           C  
ATOM   3380  C   SER C  97       7.902 -40.636  34.776  1.00 26.44           C  
ATOM   3381  O   SER C  97       7.658 -40.122  35.880  1.00 25.15           O  
ATOM   3382  CB  SER C  97      10.263 -40.702  34.072  1.00 23.91           C  
ATOM   3383  OG  SER C  97      10.622 -40.498  35.425  1.00 32.77           O  
ATOM   3384  N   VAL C  98       7.372 -41.775  34.373  1.00 23.44           N  
ATOM   3385  CA  VAL C  98       6.424 -42.502  35.194  1.00 23.68           C  
ATOM   3386  C   VAL C  98       6.653 -43.966  34.885  1.00 25.21           C  
ATOM   3387  O   VAL C  98       6.742 -44.351  33.709  1.00 24.36           O  
ATOM   3388  CB  VAL C  98       4.965 -42.042  34.864  1.00 29.81           C  
ATOM   3389  CG1 VAL C  98       4.501 -42.610  33.535  1.00 29.94           C  
ATOM   3390  CG2 VAL C  98       3.999 -42.437  35.952  1.00 30.32           C  
ATOM   3391  N   GLY C  99       6.800 -44.806  35.902  1.00 21.78           N  
ATOM   3392  CA  GLY C  99       6.992 -46.214  35.564  1.00 21.19           C  
ATOM   3393  C   GLY C  99       6.803 -47.184  36.711  1.00 26.59           C  
ATOM   3394  O   GLY C  99       6.307 -46.819  37.798  1.00 26.86           O  
ATOM   3395  N   GLU C 100       7.257 -48.411  36.480  1.00 23.45           N  
ATOM   3396  CA  GLU C 100       7.141 -49.479  37.474  1.00 24.41           C  
ATOM   3397  C   GLU C 100       8.151 -50.554  37.157  1.00 27.23           C  
ATOM   3398  O   GLU C 100       8.689 -50.609  36.039  1.00 25.47           O  
ATOM   3399  CB  GLU C 100       5.751 -50.117  37.414  1.00 25.34           C  
ATOM   3400  CG  GLU C 100       5.596 -50.929  36.139  1.00 40.63           C  
ATOM   3401  CD  GLU C 100       4.160 -51.140  35.741  1.00 75.08           C  
ATOM   3402  OE1 GLU C 100       3.257 -50.867  36.564  1.00 69.35           O  
ATOM   3403  OE2 GLU C 100       3.943 -51.589  34.600  1.00 77.18           O  
ATOM   3404  N   GLY C 101       8.384 -51.432  38.130  1.00 22.77           N  
ATOM   3405  CA  GLY C 101       9.323 -52.519  37.913  1.00 22.02           C  
ATOM   3406  C   GLY C 101       9.354 -53.450  39.098  1.00 28.85           C  
ATOM   3407  O   GLY C 101       8.490 -53.395  39.979  1.00 28.87           O  
ATOM   3408  N   MET C 102      10.405 -54.251  39.151  1.00 26.96           N  
ATOM   3409  CA  MET C 102      10.516 -55.272  40.152  1.00 28.62           C  
ATOM   3410  C   MET C 102      11.987 -55.635  40.383  1.00 28.20           C  
ATOM   3411  O   MET C 102      12.794 -55.608  39.461  1.00 27.64           O  
ATOM   3412  CB  MET C 102       9.798 -56.499  39.587  1.00 33.52           C  
ATOM   3413  CG  MET C 102       9.486 -57.559  40.599  1.00 42.27           C  
ATOM   3414  SD  MET C 102       9.614 -59.225  39.844  1.00 51.05           S  
ATOM   3415  CE  MET C 102      11.380 -59.094  39.225  1.00 46.82           C  
ATOM   3416  N   VAL C 103      12.314 -56.023  41.606  1.00 22.86           N  
ATOM   3417  CA  VAL C 103      13.650 -56.504  41.942  1.00 23.28           C  
ATOM   3418  C   VAL C 103      13.444 -57.885  42.580  1.00 27.18           C  
ATOM   3419  O   VAL C 103      12.552 -58.088  43.439  1.00 27.55           O  
ATOM   3420  CB  VAL C 103      14.402 -55.631  43.001  1.00 28.37           C  
ATOM   3421  CG1 VAL C 103      15.887 -55.996  42.982  1.00 27.69           C  
ATOM   3422  CG2 VAL C 103      14.230 -54.173  42.747  1.00 29.90           C  
ATOM   3423  N   SER C 104      14.327 -58.801  42.248  1.00 22.22           N  
ATOM   3424  CA  SER C 104      14.250 -60.115  42.850  1.00 23.50           C  
ATOM   3425  C   SER C 104      15.660 -60.704  43.055  1.00 26.37           C  
ATOM   3426  O   SER C 104      16.525 -60.595  42.181  1.00 25.86           O  
ATOM   3427  CB  SER C 104      13.350 -61.036  42.006  1.00 27.85           C  
ATOM   3428  OG  SER C 104      14.086 -62.118  41.510  1.00 37.48           O  
ATOM   3429  N   VAL C 105      15.896 -61.238  44.253  1.00 21.37           N  
ATOM   3430  CA  VAL C 105      17.176 -61.832  44.625  1.00 20.95           C  
ATOM   3431  C   VAL C 105      16.820 -63.150  45.334  1.00 24.64           C  
ATOM   3432  O   VAL C 105      16.159 -63.118  46.368  1.00 22.57           O  
ATOM   3433  CB  VAL C 105      17.978 -60.886  45.579  1.00 23.90           C  
ATOM   3434  CG1 VAL C 105      19.262 -61.590  46.111  1.00 23.74           C  
ATOM   3435  CG2 VAL C 105      18.329 -59.566  44.875  1.00 23.04           C  
ATOM   3436  N   GLY C 106      17.216 -64.290  44.762  1.00 22.25           N  
ATOM   3437  CA  GLY C 106      16.937 -65.591  45.385  1.00 22.51           C  
ATOM   3438  C   GLY C 106      15.443 -65.738  45.692  1.00 27.25           C  
ATOM   3439  O   GLY C 106      14.611 -65.472  44.840  1.00 27.41           O  
ATOM   3440  N   ASP C 107      15.094 -66.113  46.916  1.00 22.23           N  
ATOM   3441  CA  ASP C 107      13.658 -66.299  47.244  1.00 21.31           C  
ATOM   3442  C   ASP C 107      12.922 -65.001  47.513  1.00 26.26           C  
ATOM   3443  O   ASP C 107      11.772 -65.021  47.941  1.00 25.48           O  
ATOM   3444  CB  ASP C 107      13.471 -67.242  48.458  1.00 21.13           C  
ATOM   3445  CG  ASP C 107      14.014 -66.647  49.778  1.00 32.78           C  
ATOM   3446  OD1 ASP C 107      14.122 -65.409  49.922  1.00 34.59           O  
ATOM   3447  OD2 ASP C 107      14.328 -67.433  50.701  1.00 42.12           O  
ATOM   3448  N   PHE C 108      13.617 -63.873  47.372  1.00 23.48           N  
ATOM   3449  CA  PHE C 108      13.003 -62.596  47.690  1.00 22.45           C  
ATOM   3450  C   PHE C 108      12.668 -61.722  46.480  1.00 26.73           C  
ATOM   3451  O   PHE C 108      13.399 -61.702  45.498  1.00 25.74           O  
ATOM   3452  CB  PHE C 108      13.882 -61.819  48.665  1.00 23.79           C  
ATOM   3453  CG  PHE C 108      13.339 -60.460  49.003  1.00 25.52           C  
ATOM   3454  CD1 PHE C 108      12.399 -60.304  50.011  1.00 27.97           C  
ATOM   3455  CD2 PHE C 108      13.694 -59.344  48.237  1.00 28.83           C  
ATOM   3456  CE1 PHE C 108      11.880 -59.056  50.326  1.00 28.59           C  
ATOM   3457  CE2 PHE C 108      13.167 -58.074  48.528  1.00 31.80           C  
ATOM   3458  CZ  PHE C 108      12.265 -57.933  49.589  1.00 29.77           C  
ATOM   3459  N   SER C 109      11.567 -60.976  46.576  1.00 23.52           N  
ATOM   3460  CA  SER C 109      11.216 -60.041  45.534  1.00 23.16           C  
ATOM   3461  C   SER C 109      10.313 -58.949  46.027  1.00 25.83           C  
ATOM   3462  O   SER C 109       9.710 -59.084  47.077  1.00 24.59           O  
ATOM   3463  CB  SER C 109      10.632 -60.745  44.323  1.00 26.80           C  
ATOM   3464  OG  SER C 109       9.289 -61.019  44.568  1.00 36.86           O  
ATOM   3465  N   HIS C 110      10.280 -57.841  45.295  1.00 22.02           N  
ATOM   3466  CA  HIS C 110       9.390 -56.724  45.609  1.00 21.76           C  
ATOM   3467  C   HIS C 110       9.136 -55.885  44.364  1.00 24.88           C  
ATOM   3468  O   HIS C 110       9.935 -55.908  43.419  1.00 24.14           O  
ATOM   3469  CB  HIS C 110       9.836 -55.906  46.867  1.00 23.22           C  
ATOM   3470  CG  HIS C 110      10.847 -54.810  46.627  1.00 25.91           C  
ATOM   3471  ND1 HIS C 110      10.519 -53.603  46.038  1.00 27.31           N  
ATOM   3472  CD2 HIS C 110      12.121 -54.663  47.089  1.00 26.58           C  
ATOM   3473  CE1 HIS C 110      11.565 -52.790  46.094  1.00 26.13           C  
ATOM   3474  NE2 HIS C 110      12.556 -53.411  46.721  1.00 25.52           N  
ATOM   3475  N   THR C 111       8.001 -55.197  44.313  1.00 21.20           N  
ATOM   3476  CA  THR C 111       7.699 -54.371  43.142  1.00 20.35           C  
ATOM   3477  C   THR C 111       7.777 -52.920  43.547  1.00 25.34           C  
ATOM   3478  O   THR C 111       7.937 -52.609  44.712  1.00 25.81           O  
ATOM   3479  CB  THR C 111       6.309 -54.692  42.598  1.00 22.26           C  
ATOM   3480  OG1 THR C 111       5.354 -54.394  43.619  1.00 27.85           O  
ATOM   3481  CG2 THR C 111       6.199 -56.159  42.228  1.00 14.85           C  
ATOM   3482  N   PHE C 112       7.610 -52.027  42.582  1.00 22.54           N  
ATOM   3483  CA  PHE C 112       7.636 -50.606  42.873  1.00 22.67           C  
ATOM   3484  C   PHE C 112       6.993 -49.826  41.735  1.00 25.73           C  
ATOM   3485  O   PHE C 112       6.945 -50.284  40.603  1.00 25.07           O  
ATOM   3486  CB  PHE C 112       9.092 -50.111  43.093  1.00 24.62           C  
ATOM   3487  CG  PHE C 112      10.022 -50.349  41.906  1.00 25.61           C  
ATOM   3488  CD1 PHE C 112      10.137 -49.410  40.888  1.00 28.99           C  
ATOM   3489  CD2 PHE C 112      10.836 -51.496  41.849  1.00 26.95           C  
ATOM   3490  CE1 PHE C 112      11.025 -49.620  39.811  1.00 30.43           C  
ATOM   3491  CE2 PHE C 112      11.715 -51.717  40.792  1.00 29.53           C  
ATOM   3492  CZ  PHE C 112      11.800 -50.790  39.753  1.00 28.19           C  
ATOM   3493  N   SER C 113       6.501 -48.632  42.038  1.00 22.39           N  
ATOM   3494  CA  SER C 113       6.014 -47.765  40.971  1.00 22.72           C  
ATOM   3495  C   SER C 113       6.537 -46.385  41.314  1.00 26.25           C  
ATOM   3496  O   SER C 113       6.919 -46.141  42.444  1.00 25.61           O  
ATOM   3497  CB  SER C 113       4.508 -47.813  40.787  1.00 25.21           C  
ATOM   3498  OG  SER C 113       3.868 -47.123  41.825  1.00 38.66           O  
ATOM   3499  N   PHE C 114       6.692 -45.522  40.320  1.00 23.20           N  
ATOM   3500  CA  PHE C 114       7.238 -44.206  40.618  1.00 22.18           C  
ATOM   3501  C   PHE C 114       6.873 -43.172  39.568  1.00 25.39           C  
ATOM   3502  O   PHE C 114       6.491 -43.492  38.435  1.00 24.31           O  
ATOM   3503  CB  PHE C 114       8.772 -44.297  40.644  1.00 23.00           C  
ATOM   3504  CG  PHE C 114       9.390 -44.473  39.275  1.00 22.79           C  
ATOM   3505  CD1 PHE C 114       9.748 -43.362  38.504  1.00 23.07           C  
ATOM   3506  CD2 PHE C 114       9.540 -45.748  38.718  1.00 23.86           C  
ATOM   3507  CE1 PHE C 114      10.299 -43.521  37.244  1.00 23.37           C  
ATOM   3508  CE2 PHE C 114      10.092 -45.913  37.418  1.00 24.81           C  
ATOM   3509  CZ  PHE C 114      10.481 -44.793  36.703  1.00 21.99           C  
ATOM   3510  N   GLU C 115       7.064 -41.925  39.952  1.00 23.62           N  
ATOM   3511  CA  GLU C 115       6.979 -40.826  39.013  1.00 26.24           C  
ATOM   3512  C   GLU C 115       8.025 -39.809  39.463  1.00 29.14           C  
ATOM   3513  O   GLU C 115       8.245 -39.636  40.658  1.00 28.59           O  
ATOM   3514  CB  GLU C 115       5.564 -40.239  38.911  1.00 28.16           C  
ATOM   3515  CG  GLU C 115       5.153 -39.377  40.044  1.00 44.47           C  
ATOM   3516  CD  GLU C 115       3.656 -39.046  39.983  1.00 79.18           C  
ATOM   3517  OE1 GLU C 115       2.830 -39.980  39.822  1.00 63.02           O  
ATOM   3518  OE2 GLU C 115       3.310 -37.846  40.056  1.00 84.44           O  
ATOM   3519  N   GLY C 116       8.759 -39.239  38.514  1.00 24.17           N  
ATOM   3520  CA  GLY C 116       9.783 -38.280  38.900  1.00 23.62           C  
ATOM   3521  C   GLY C 116      10.113 -37.294  37.793  1.00 25.85           C  
ATOM   3522  O   GLY C 116       9.855 -37.536  36.619  1.00 23.40           O  
ATOM   3523  N   SER C 117      10.713 -36.179  38.173  1.00 23.13           N  
ATOM   3524  CA  SER C 117      11.141 -35.233  37.170  1.00 22.70           C  
ATOM   3525  C   SER C 117      12.613 -34.918  37.433  1.00 25.87           C  
ATOM   3526  O   SER C 117      13.088 -35.019  38.574  1.00 24.38           O  
ATOM   3527  CB  SER C 117      10.304 -33.977  37.241  1.00 24.13           C  
ATOM   3528  OG  SER C 117      10.511 -33.344  38.478  1.00 37.01           O  
ATOM   3529  N   VAL C 118      13.337 -34.596  36.367  1.00 21.55           N  
ATOM   3530  CA  VAL C 118      14.725 -34.239  36.490  1.00 20.33           C  
ATOM   3531  C   VAL C 118      14.880 -32.930  35.746  1.00 24.50           C  
ATOM   3532  O   VAL C 118      14.395 -32.802  34.636  1.00 26.39           O  
ATOM   3533  CB  VAL C 118      15.647 -35.355  35.929  1.00 22.78           C  
ATOM   3534  CG1 VAL C 118      17.099 -34.906  35.913  1.00 21.10           C  
ATOM   3535  CG2 VAL C 118      15.502 -36.666  36.774  1.00 22.44           C  
ATOM   3536  N   VAL C 119      15.528 -31.955  36.376  1.00 19.77           N  
ATOM   3537  CA  VAL C 119      15.825 -30.661  35.762  1.00 19.81           C  
ATOM   3538  C   VAL C 119      17.344 -30.530  35.660  1.00 24.76           C  
ATOM   3539  O   VAL C 119      18.043 -30.642  36.649  1.00 25.05           O  
ATOM   3540  CB  VAL C 119      15.263 -29.504  36.614  1.00 24.28           C  
ATOM   3541  CG1 VAL C 119      15.697 -28.159  36.045  1.00 23.83           C  
ATOM   3542  CG2 VAL C 119      13.735 -29.596  36.715  1.00 23.80           C  
ATOM   3543  N   ASN C 120      17.842 -30.339  34.445  1.00 22.22           N  
ATOM   3544  CA  ASN C 120      19.264 -30.228  34.169  1.00 21.87           C  
ATOM   3545  C   ASN C 120      19.602 -28.776  33.922  1.00 27.70           C  
ATOM   3546  O   ASN C 120      19.033 -28.162  33.012  1.00 27.85           O  
ATOM   3547  CB  ASN C 120      19.629 -31.014  32.896  1.00 17.86           C  
ATOM   3548  CG  ASN C 120      21.119 -31.289  32.806  1.00 33.19           C  
ATOM   3549  OD1 ASN C 120      21.661 -32.088  33.578  1.00 25.25           O  
ATOM   3550  ND2 ASN C 120      21.806 -30.542  31.961  1.00 18.95           N  
ATOM   3551  N   LEU C 121      20.545 -28.242  34.692  1.00 24.38           N  
ATOM   3552  CA  LEU C 121      20.983 -26.851  34.541  1.00 24.21           C  
ATOM   3553  C   LEU C 121      22.502 -26.721  34.344  1.00 28.02           C  
ATOM   3554  O   LEU C 121      23.287 -27.281  35.119  1.00 27.53           O  
ATOM   3555  CB  LEU C 121      20.583 -26.037  35.778  1.00 24.71           C  
ATOM   3556  CG  LEU C 121      19.066 -25.889  36.044  1.00 32.44           C  
ATOM   3557  CD1 LEU C 121      18.784 -25.238  37.395  1.00 33.25           C  
ATOM   3558  CD2 LEU C 121      18.308 -25.153  34.906  1.00 34.80           C  
ATOM   3559  N   PHE C 122      22.908 -25.931  33.349  1.00 24.49           N  
ATOM   3560  CA  PHE C 122      24.326 -25.615  33.124  1.00 25.02           C  
ATOM   3561  C   PHE C 122      24.664 -24.383  33.981  1.00 29.11           C  
ATOM   3562  O   PHE C 122      23.813 -23.527  34.208  1.00 27.61           O  
ATOM   3563  CB  PHE C 122      24.604 -25.334  31.646  1.00 26.76           C  
ATOM   3564  CG  PHE C 122      24.446 -26.550  30.769  1.00 28.42           C  
ATOM   3565  CD1 PHE C 122      25.090 -27.731  31.084  1.00 30.43           C  
ATOM   3566  CD2 PHE C 122      23.607 -26.530  29.673  1.00 31.60           C  
ATOM   3567  CE1 PHE C 122      24.904 -28.867  30.332  1.00 31.29           C  
ATOM   3568  CE2 PHE C 122      23.432 -27.671  28.904  1.00 34.67           C  
ATOM   3569  CZ  PHE C 122      24.089 -28.843  29.245  1.00 31.64           C  
ATOM   3570  N   TYR C 123      25.873 -24.319  34.518  1.00 25.36           N  
ATOM   3571  CA  TYR C 123      26.216 -23.201  35.381  1.00 23.63           C  
ATOM   3572  C   TYR C 123      26.326 -21.882  34.620  1.00 29.66           C  
ATOM   3573  O   TYR C 123      26.162 -20.845  35.206  1.00 29.61           O  
ATOM   3574  CB  TYR C 123      27.499 -23.499  36.153  1.00 22.95           C  
ATOM   3575  CG  TYR C 123      27.328 -24.486  37.276  1.00 24.08           C  
ATOM   3576  CD1 TYR C 123      26.410 -24.245  38.323  1.00 26.66           C  
ATOM   3577  CD2 TYR C 123      28.107 -25.641  37.352  1.00 23.04           C  
ATOM   3578  CE1 TYR C 123      26.260 -25.144  39.383  1.00 25.88           C  
ATOM   3579  CE2 TYR C 123      27.980 -26.533  38.443  1.00 22.27           C  
ATOM   3580  CZ  TYR C 123      27.063 -26.278  39.449  1.00 27.64           C  
ATOM   3581  OH  TYR C 123      26.932 -27.159  40.513  1.00 24.14           O  
ATOM   3582  N   TYR C 124      26.617 -21.917  33.322  1.00 26.84           N  
ATOM   3583  CA  TYR C 124      26.801 -20.693  32.531  1.00 27.27           C  
ATOM   3584  C   TYR C 124      26.407 -20.966  31.085  1.00 32.55           C  
ATOM   3585  O   TYR C 124      26.420 -22.099  30.648  1.00 32.46           O  
ATOM   3586  CB  TYR C 124      28.289 -20.248  32.537  1.00 28.95           C  
ATOM   3587  CG  TYR C 124      29.152 -20.994  31.503  1.00 31.99           C  
ATOM   3588  CD1 TYR C 124      29.682 -22.250  31.787  1.00 34.14           C  
ATOM   3589  CD2 TYR C 124      29.444 -20.439  30.258  1.00 33.14           C  
ATOM   3590  CE1 TYR C 124      30.443 -22.946  30.874  1.00 34.45           C  
ATOM   3591  CE2 TYR C 124      30.220 -21.149  29.315  1.00 33.95           C  
ATOM   3592  CZ  TYR C 124      30.708 -22.407  29.642  1.00 40.44           C  
ATOM   3593  OH  TYR C 124      31.487 -23.134  28.765  1.00 39.30           O  
ATOM   3594  N   ARG C 125      26.075 -19.921  30.340  1.00 30.67           N  
ATOM   3595  CA  ARG C 125      25.807 -20.078  28.900  1.00 32.37           C  
ATOM   3596  C   ARG C 125      26.517 -18.891  28.302  1.00 33.52           C  
ATOM   3597  O   ARG C 125      26.326 -17.789  28.769  1.00 33.58           O  
ATOM   3598  CB  ARG C 125      24.307 -19.996  28.567  1.00 36.18           C  
ATOM   3599  N   SER C 126      27.413 -19.113  27.355  1.00 27.73           N  
ATOM   3600  CA  SER C 126      28.129 -17.990  26.786  1.00 26.25           C  
ATOM   3601  C   SER C 126      28.266 -18.113  25.286  1.00 28.99           C  
ATOM   3602  O   SER C 126      28.707 -19.141  24.773  1.00 28.99           O  
ATOM   3603  CB  SER C 126      29.493 -17.847  27.423  1.00 28.22           C  
ATOM   3604  OG  SER C 126      30.202 -16.807  26.801  1.00 34.10           O  
ATOM   3605  N   ASP C 127      27.916 -17.042  24.579  1.00 25.51           N  
ATOM   3606  CA  ASP C 127      28.061 -17.037  23.131  1.00 25.64           C  
ATOM   3607  C   ASP C 127      29.531 -16.969  22.739  1.00 26.09           C  
ATOM   3608  O   ASP C 127      29.910 -17.423  21.671  1.00 25.44           O  
ATOM   3609  CB  ASP C 127      27.292 -15.868  22.501  1.00 28.89           C  
ATOM   3610  CG  ASP C 127      27.206 -15.996  20.981  1.00 47.27           C  
ATOM   3611  OD1 ASP C 127      26.729 -17.053  20.506  1.00 49.82           O  
ATOM   3612  OD2 ASP C 127      27.693 -15.093  20.267  1.00 53.05           O  
ATOM   3613  N   ALA C 128      30.353 -16.404  23.620  1.00 23.53           N  
ATOM   3614  CA  ALA C 128      31.782 -16.278  23.339  1.00 23.90           C  
ATOM   3615  C   ALA C 128      32.430 -17.665  23.211  1.00 28.17           C  
ATOM   3616  O   ALA C 128      33.340 -17.864  22.396  1.00 25.88           O  
ATOM   3617  CB  ALA C 128      32.462 -15.457  24.425  1.00 23.48           C  
ATOM   3618  N   VAL C 129      31.937 -18.619  24.012  1.00 23.93           N  
ATOM   3619  CA  VAL C 129      32.453 -19.990  23.975  1.00 22.49           C  
ATOM   3620  C   VAL C 129      31.845 -20.697  22.756  1.00 26.30           C  
ATOM   3621  O   VAL C 129      32.549 -21.283  21.927  1.00 25.33           O  
ATOM   3622  CB  VAL C 129      32.140 -20.738  25.310  1.00 25.56           C  
ATOM   3623  CG1 VAL C 129      32.380 -22.226  25.156  1.00 25.39           C  
ATOM   3624  CG2 VAL C 129      32.971 -20.185  26.439  1.00 25.30           C  
ATOM   3625  N   ARG C 130      30.528 -20.591  22.646  1.00 26.24           N  
ATOM   3626  CA  ARG C 130      29.754 -21.187  21.549  1.00 27.74           C  
ATOM   3627  C   ARG C 130      30.238 -20.918  20.117  1.00 32.01           C  
ATOM   3628  O   ARG C 130      30.315 -21.832  19.308  1.00 32.31           O  
ATOM   3629  CB  ARG C 130      28.278 -20.816  21.681  1.00 31.28           C  
ATOM   3630  CG  ARG C 130      27.362 -21.650  20.788  1.00 48.03           C  
ATOM   3631  N   ARG C 131      30.570 -19.678  19.786  1.00 28.28           N  
ATOM   3632  CA  ARG C 131      31.047 -19.425  18.421  1.00 28.14           C  
ATOM   3633  C   ARG C 131      32.527 -19.665  18.230  1.00 31.31           C  
ATOM   3634  O   ARG C 131      33.015 -19.639  17.112  1.00 32.21           O  
ATOM   3635  CB  ARG C 131      30.718 -17.991  17.957  1.00 27.93           C  
ATOM   3636  CG  ARG C 131      31.019 -16.918  18.940  1.00 29.61           C  
ATOM   3637  CD  ARG C 131      30.821 -15.525  18.342  1.00 33.80           C  
ATOM   3638  NE  ARG C 131      31.725 -14.606  19.004  1.00 28.36           N  
ATOM   3639  CZ  ARG C 131      31.433 -13.999  20.142  1.00 32.42           C  
ATOM   3640  NH1 ARG C 131      30.239 -14.156  20.700  1.00 21.96           N  
ATOM   3641  NH2 ARG C 131      32.330 -13.240  20.721  1.00 27.55           N  
ATOM   3642  N   ASN C 132      33.270 -19.844  19.310  1.00 25.36           N  
ATOM   3643  CA  ASN C 132      34.705 -20.031  19.165  1.00 23.76           C  
ATOM   3644  C   ASN C 132      35.195 -21.473  19.316  1.00 26.74           C  
ATOM   3645  O   ASN C 132      36.297 -21.804  18.921  1.00 25.24           O  
ATOM   3646  CB  ASN C 132      35.435 -19.077  20.115  1.00 22.68           C  
ATOM   3647  CG  ASN C 132      35.400 -17.643  19.619  1.00 28.39           C  
ATOM   3648  OD1 ASN C 132      35.937 -17.326  18.557  1.00 25.31           O  
ATOM   3649  ND2 ASN C 132      34.713 -16.775  20.360  1.00 17.51           N  
ATOM   3650  N   VAL C 133      34.361 -22.339  19.886  1.00 23.79           N  
ATOM   3651  CA  VAL C 133      34.745 -23.726  20.089  1.00 20.77           C  
ATOM   3652  C   VAL C 133      33.824 -24.611  19.257  1.00 26.36           C  
ATOM   3653  O   VAL C 133      32.644 -24.720  19.546  1.00 28.65           O  
ATOM   3654  CB  VAL C 133      34.690 -24.061  21.608  1.00 22.76           C  
ATOM   3655  CG1 VAL C 133      35.044 -25.517  21.854  1.00 21.41           C  
ATOM   3656  CG2 VAL C 133      35.604 -23.100  22.413  1.00 21.01           C  
ATOM   3657  N   PRO C 134      34.347 -25.211  18.199  1.00 22.64           N  
ATOM   3658  CA  PRO C 134      33.503 -26.003  17.338  1.00 22.13           C  
ATOM   3659  C   PRO C 134      32.980 -27.303  17.898  1.00 27.64           C  
ATOM   3660  O   PRO C 134      31.872 -27.725  17.550  1.00 27.72           O  
ATOM   3661  CB  PRO C 134      34.332 -26.201  16.066  1.00 22.86           C  
ATOM   3662  CG  PRO C 134      35.735 -25.862  16.420  1.00 27.90           C  
ATOM   3663  CD  PRO C 134      35.765 -25.259  17.794  1.00 24.50           C  
ATOM   3664  N   ASN C 135      33.743 -27.936  18.779  1.00 23.70           N  
ATOM   3665  CA  ASN C 135      33.311 -29.221  19.345  1.00 22.88           C  
ATOM   3666  C   ASN C 135      33.576 -29.218  20.845  1.00 25.39           C  
ATOM   3667  O   ASN C 135      34.545 -29.814  21.319  1.00 23.31           O  
ATOM   3668  CB  ASN C 135      34.053 -30.401  18.649  1.00 20.15           C  
ATOM   3669  CG  ASN C 135      33.499 -31.753  19.033  1.00 28.74           C  
ATOM   3670  OD1 ASN C 135      32.389 -31.849  19.532  1.00 22.42           O  
ATOM   3671  ND2 ASN C 135      34.243 -32.816  18.729  1.00 23.46           N  
ATOM   3672  N   PRO C 136      32.711 -28.526  21.577  1.00 23.66           N  
ATOM   3673  CA  PRO C 136      32.853 -28.379  23.046  1.00 23.80           C  
ATOM   3674  C   PRO C 136      32.625 -29.704  23.781  1.00 25.64           C  
ATOM   3675  O   PRO C 136      31.738 -30.483  23.434  1.00 24.63           O  
ATOM   3676  CB  PRO C 136      31.745 -27.367  23.417  1.00 25.00           C  
ATOM   3677  CG  PRO C 136      30.723 -27.519  22.290  1.00 28.48           C  
ATOM   3678  CD  PRO C 136      31.506 -27.855  21.050  1.00 24.33           C  
ATOM   3679  N   ILE C 137      33.476 -29.978  24.755  1.00 21.75           N  
ATOM   3680  CA  ILE C 137      33.400 -31.228  25.519  1.00 20.62           C  
ATOM   3681  C   ILE C 137      32.915 -31.001  26.945  1.00 23.93           C  
ATOM   3682  O   ILE C 137      31.866 -31.471  27.310  1.00 23.95           O  
ATOM   3683  CB  ILE C 137      34.752 -32.003  25.529  1.00 22.39           C  
ATOM   3684  CG1 ILE C 137      35.259 -32.235  24.092  1.00 21.80           C  
ATOM   3685  CG2 ILE C 137      34.599 -33.304  26.312  1.00 20.44           C  
ATOM   3686  CD1 ILE C 137      34.430 -33.224  23.258  1.00 18.00           C  
ATOM   3687  N   TYR C 138      33.711 -30.341  27.776  1.00 21.91           N  
ATOM   3688  CA  TYR C 138      33.326 -30.162  29.199  1.00 21.32           C  
ATOM   3689  C   TYR C 138      32.242 -29.112  29.363  1.00 26.27           C  
ATOM   3690  O   TYR C 138      32.381 -27.995  28.858  1.00 27.65           O  
ATOM   3691  CB  TYR C 138      34.531 -29.724  30.029  1.00 20.00           C  
ATOM   3692  CG  TYR C 138      35.732 -30.634  29.907  1.00 18.85           C  
ATOM   3693  CD1 TYR C 138      35.616 -32.013  30.109  1.00 19.16           C  
ATOM   3694  CD2 TYR C 138      36.997 -30.097  29.811  1.00 18.87           C  
ATOM   3695  CE1 TYR C 138      36.736 -32.819  30.083  1.00 21.00           C  
ATOM   3696  CE2 TYR C 138      38.121 -30.883  29.802  1.00 18.44           C  
ATOM   3697  CZ  TYR C 138      37.995 -32.232  29.912  1.00 24.55           C  
ATOM   3698  OH  TYR C 138      39.149 -32.971  29.887  1.00 19.50           O  
ATOM   3699  N   MET C 139      31.175 -29.465  30.070  1.00 22.88           N  
ATOM   3700  CA  MET C 139      30.092 -28.522  30.371  1.00 25.21           C  
ATOM   3701  C   MET C 139      29.696 -28.784  31.801  1.00 23.91           C  
ATOM   3702  O   MET C 139      29.141 -29.822  32.105  1.00 23.10           O  
ATOM   3703  CB  MET C 139      28.867 -28.718  29.459  1.00 30.23           C  
ATOM   3704  CG  MET C 139      28.895 -27.872  28.197  1.00 39.46           C  
ATOM   3705  SD  MET C 139      28.878 -26.090  28.594  1.00 49.09           S  
ATOM   3706  CE  MET C 139      28.014 -26.053  30.108  1.00 45.78           C  
ATOM   3707  N   GLN C 140      30.039 -27.858  32.680  1.00 18.14           N  
ATOM   3708  CA  GLN C 140      29.795 -27.989  34.099  1.00 17.48           C  
ATOM   3709  C   GLN C 140      28.342 -27.687  34.361  1.00 22.71           C  
ATOM   3710  O   GLN C 140      27.790 -26.765  33.785  1.00 22.57           O  
ATOM   3711  CB  GLN C 140      30.661 -26.995  34.894  1.00 17.93           C  
ATOM   3712  CG  GLN C 140      32.146 -26.952  34.528  1.00 11.16           C  
ATOM   3713  CD  GLN C 140      32.460 -25.837  33.530  1.00 21.44           C  
ATOM   3714  OE1 GLN C 140      31.906 -25.786  32.435  1.00 18.64           O  
ATOM   3715  NE2 GLN C 140      33.420 -25.008  33.867  1.00 14.21           N  
ATOM   3716  N   GLY C 141      27.726 -28.432  35.271  1.00 18.53           N  
ATOM   3717  CA  GLY C 141      26.331 -28.181  35.583  1.00 17.97           C  
ATOM   3718  C   GLY C 141      25.838 -28.971  36.784  1.00 20.77           C  
ATOM   3719  O   GLY C 141      26.589 -29.678  37.423  1.00 20.48           O  
ATOM   3720  N   ARG C 142      24.542 -28.863  37.056  1.00 18.08           N  
ATOM   3721  CA  ARG C 142      23.927 -29.559  38.176  1.00 18.16           C  
ATOM   3722  C   ARG C 142      22.547 -30.050  37.743  1.00 22.28           C  
ATOM   3723  O   ARG C 142      21.822 -29.365  36.991  1.00 22.57           O  
ATOM   3724  CB  ARG C 142      23.832 -28.620  39.407  1.00 18.46           C  
ATOM   3725  CG  ARG C 142      23.495 -29.369  40.707  1.00 16.41           C  
ATOM   3726  CD  ARG C 142      23.912 -28.582  41.951  1.00 23.69           C  
ATOM   3727  NE  ARG C 142      25.309 -28.825  42.297  1.00 19.88           N  
ATOM   3728  CZ  ARG C 142      25.732 -29.681  43.218  1.00 26.06           C  
ATOM   3729  NH1 ARG C 142      24.854 -30.366  43.930  1.00 17.77           N  
ATOM   3730  NH2 ARG C 142      27.045 -29.864  43.421  1.00 17.11           N  
ATOM   3731  N   GLN C 143      22.173 -31.211  38.259  1.00 18.69           N  
ATOM   3732  CA  GLN C 143      20.928 -31.880  37.900  1.00 20.27           C  
ATOM   3733  C   GLN C 143      20.046 -32.168  39.115  1.00 24.75           C  
ATOM   3734  O   GLN C 143      20.511 -32.729  40.097  1.00 26.56           O  
ATOM   3735  CB  GLN C 143      21.310 -33.216  37.251  1.00 21.85           C  
ATOM   3736  CG  GLN C 143      20.440 -33.652  36.134  1.00 31.08           C  
ATOM   3737  CD  GLN C 143      20.960 -34.923  35.501  1.00 34.82           C  
ATOM   3738  OE1 GLN C 143      21.051 -35.952  36.148  1.00 25.87           O  
ATOM   3739  NE2 GLN C 143      21.378 -34.828  34.252  1.00 24.18           N  
ATOM   3740  N   PHE C 144      18.755 -31.852  39.035  1.00 20.62           N  
ATOM   3741  CA  PHE C 144      17.853 -32.004  40.177  1.00 18.86           C  
ATOM   3742  C   PHE C 144      16.803 -33.081  39.997  1.00 23.86           C  
ATOM   3743  O   PHE C 144      16.083 -33.077  39.009  1.00 24.48           O  
ATOM   3744  CB  PHE C 144      17.194 -30.644  40.518  1.00 19.56           C  
ATOM   3745  CG  PHE C 144      18.193 -29.545  40.823  1.00 18.97           C  
ATOM   3746  CD1 PHE C 144      18.543 -29.237  42.148  1.00 20.39           C  
ATOM   3747  CD2 PHE C 144      18.785 -28.843  39.789  1.00 19.06           C  
ATOM   3748  CE1 PHE C 144      19.507 -28.256  42.433  1.00 21.00           C  
ATOM   3749  CE2 PHE C 144      19.752 -27.874  40.041  1.00 22.68           C  
ATOM   3750  CZ  PHE C 144      20.122 -27.575  41.375  1.00 20.76           C  
ATOM   3751  N   HIS C 145      16.723 -34.000  40.964  1.00 19.32           N  
ATOM   3752  CA  HIS C 145      15.798 -35.133  40.896  1.00 18.64           C  
ATOM   3753  C   HIS C 145      14.701 -34.902  41.948  1.00 24.12           C  
ATOM   3754  O   HIS C 145      14.987 -34.523  43.098  1.00 21.88           O  
ATOM   3755  CB  HIS C 145      16.533 -36.451  41.242  1.00 18.24           C  
ATOM   3756  CG  HIS C 145      17.249 -37.110  40.086  1.00 20.72           C  
ATOM   3757  ND1 HIS C 145      18.336 -36.541  39.444  1.00 21.02           N  
ATOM   3758  CD2 HIS C 145      17.090 -38.342  39.527  1.00 21.70           C  
ATOM   3759  CE1 HIS C 145      18.767 -37.364  38.495  1.00 20.27           C  
ATOM   3760  NE2 HIS C 145      18.047 -38.478  38.545  1.00 20.94           N  
ATOM   3761  N   ASP C 146      13.450 -35.170  41.563  1.00 21.39           N  
ATOM   3762  CA  ASP C 146      12.299 -35.047  42.470  1.00 20.64           C  
ATOM   3763  C   ASP C 146      11.552 -36.341  42.241  1.00 25.34           C  
ATOM   3764  O   ASP C 146      11.118 -36.620  41.118  1.00 23.66           O  
ATOM   3765  CB  ASP C 146      11.448 -33.852  42.063  1.00 23.55           C  
ATOM   3766  CG  ASP C 146      10.278 -33.627  42.995  1.00 34.18           C  
ATOM   3767  OD1 ASP C 146      10.128 -34.392  43.958  1.00 32.02           O  
ATOM   3768  OD2 ASP C 146       9.475 -32.706  42.729  1.00 47.92           O  
ATOM   3769  N   ILE C 147      11.534 -37.206  43.253  1.00 22.97           N  
ATOM   3770  CA  ILE C 147      11.010 -38.557  43.059  1.00 23.42           C  
ATOM   3771  C   ILE C 147       9.882 -38.930  44.018  1.00 27.50           C  
ATOM   3772  O   ILE C 147       9.952 -38.698  45.236  1.00 26.79           O  
ATOM   3773  CB  ILE C 147      12.157 -39.602  43.207  1.00 26.86           C  
ATOM   3774  CG1 ILE C 147      13.218 -39.434  42.112  1.00 27.46           C  
ATOM   3775  CG2 ILE C 147      11.610 -41.010  43.276  1.00 25.69           C  
ATOM   3776  CD1 ILE C 147      14.643 -39.594  42.631  1.00 25.85           C  
ATOM   3777  N   LEU C 148       8.863 -39.559  43.475  1.00 24.43           N  
ATOM   3778  CA  LEU C 148       7.801 -40.084  44.313  1.00 25.01           C  
ATOM   3779  C   LEU C 148       7.757 -41.581  43.997  1.00 28.83           C  
ATOM   3780  O   LEU C 148       7.570 -41.967  42.837  1.00 29.68           O  
ATOM   3781  CB  LEU C 148       6.446 -39.429  43.994  1.00 25.87           C  
ATOM   3782  CG  LEU C 148       5.225 -40.141  44.628  1.00 31.55           C  
ATOM   3783  CD1 LEU C 148       5.141 -39.798  46.071  1.00 30.41           C  
ATOM   3784  CD2 LEU C 148       3.901 -39.731  43.937  1.00 37.19           C  
ATOM   3785  N   MET C 149       8.001 -42.420  45.002  1.00 23.80           N  
ATOM   3786  CA  MET C 149       7.975 -43.863  44.775  1.00 22.78           C  
ATOM   3787  C   MET C 149       7.096 -44.632  45.750  1.00 26.85           C  
ATOM   3788  O   MET C 149       6.922 -44.236  46.908  1.00 26.04           O  
ATOM   3789  CB  MET C 149       9.370 -44.467  44.735  1.00 24.26           C  
ATOM   3790  CG  MET C 149      10.218 -44.196  45.971  1.00 25.99           C  
ATOM   3791  SD  MET C 149      11.957 -44.725  45.763  1.00 28.28           S  
ATOM   3792  CE  MET C 149      12.384 -45.052  47.512  1.00 24.68           C  
ATOM   3793  N   LYS C 150       6.519 -45.723  45.256  1.00 24.08           N  
ATOM   3794  CA  LYS C 150       5.596 -46.548  46.065  1.00 23.04           C  
ATOM   3795  C   LYS C 150       5.961 -48.014  45.971  1.00 27.29           C  
ATOM   3796  O   LYS C 150       6.190 -48.541  44.895  1.00 26.70           O  
ATOM   3797  CB  LYS C 150       4.150 -46.363  45.573  1.00 23.74           C  
ATOM   3798  CG  LYS C 150       3.730 -44.902  45.460  1.00 35.38           C  
ATOM   3799  CD  LYS C 150       2.357 -44.733  44.827  1.00 43.69           C  
ATOM   3800  CE  LYS C 150       1.639 -43.531  45.434  1.00 57.78           C  
ATOM   3801  NZ  LYS C 150       0.176 -43.520  45.146  1.00 66.39           N  
ATOM   3802  N   VAL C 151       5.976 -48.672  47.122  1.00 25.75           N  
ATOM   3803  CA  VAL C 151       6.322 -50.082  47.200  1.00 24.78           C  
ATOM   3804  C   VAL C 151       5.313 -50.761  48.093  1.00 28.75           C  
ATOM   3805  O   VAL C 151       5.197 -50.418  49.257  1.00 28.12           O  
ATOM   3806  CB  VAL C 151       7.778 -50.273  47.771  1.00 27.33           C  
ATOM   3807  CG1 VAL C 151       8.096 -51.785  48.055  1.00 25.76           C  
ATOM   3808  CG2 VAL C 151       8.801 -49.657  46.824  1.00 26.95           C  
ATOM   3809  N   PRO C 152       4.610 -51.752  47.563  1.00 26.27           N  
ATOM   3810  CA  PRO C 152       3.650 -52.499  48.395  1.00 26.40           C  
ATOM   3811  C   PRO C 152       4.454 -53.280  49.444  1.00 30.34           C  
ATOM   3812  O   PRO C 152       5.387 -54.010  49.102  1.00 29.96           O  
ATOM   3813  CB  PRO C 152       2.977 -53.468  47.413  1.00 27.66           C  
ATOM   3814  CG  PRO C 152       3.320 -52.927  46.022  1.00 32.04           C  
ATOM   3815  CD  PRO C 152       4.641 -52.225  46.168  1.00 27.52           C  
ATOM   3816  N   LEU C 153       4.099 -53.095  50.712  1.00 26.76           N  
ATOM   3817  CA  LEU C 153       4.744 -53.771  51.839  1.00 26.84           C  
ATOM   3818  C   LEU C 153       4.073 -55.127  52.016  1.00 33.41           C  
ATOM   3819  O   LEU C 153       3.327 -55.341  52.972  1.00 35.37           O  
ATOM   3820  CB  LEU C 153       4.554 -52.925  53.112  1.00 26.18           C  
ATOM   3821  CG  LEU C 153       5.045 -51.481  52.921  1.00 29.86           C  
ATOM   3822  CD1 LEU C 153       4.747 -50.593  54.123  1.00 27.79           C  
ATOM   3823  CD2 LEU C 153       6.561 -51.480  52.582  1.00 29.23           C  
ATOM   3824  N   ASP C 154       4.300 -56.033  51.076  1.00 30.39           N  
ATOM   3825  CA  ASP C 154       3.614 -57.309  51.088  1.00 30.29           C  
ATOM   3826  C   ASP C 154       4.389 -58.508  51.600  1.00 33.87           C  
ATOM   3827  O   ASP C 154       4.050 -59.645  51.290  1.00 33.39           O  
ATOM   3828  CB  ASP C 154       2.950 -57.614  49.751  1.00 31.91           C  
ATOM   3829  CG  ASP C 154       3.898 -57.482  48.591  1.00 46.30           C  
ATOM   3830  OD1 ASP C 154       5.113 -57.407  48.834  1.00 46.55           O  
ATOM   3831  OD2 ASP C 154       3.430 -57.466  47.434  1.00 56.28           O  
ATOM   3832  N   ASN C 155       5.401 -58.255  52.412  1.00 28.79           N  
ATOM   3833  CA  ASN C 155       6.128 -59.332  53.044  1.00 27.54           C  
ATOM   3834  C   ASN C 155       6.847 -58.791  54.263  1.00 30.05           C  
ATOM   3835  O   ASN C 155       6.958 -57.561  54.446  1.00 30.30           O  
ATOM   3836  CB  ASN C 155       6.977 -60.161  52.061  1.00 30.47           C  
ATOM   3837  CG  ASN C 155       8.255 -59.433  51.587  1.00 39.10           C  
ATOM   3838  OD1 ASN C 155       9.047 -58.964  52.384  1.00 31.64           O  
ATOM   3839  ND2 ASN C 155       8.502 -59.466  50.296  1.00 27.77           N  
ATOM   3840  N   ASN C 156       7.241 -59.677  55.163  1.00 24.77           N  
ATOM   3841  CA  ASN C 156       7.830 -59.217  56.417  1.00 25.36           C  
ATOM   3842  C   ASN C 156       9.152 -58.485  56.267  1.00 30.44           C  
ATOM   3843  O   ASN C 156       9.502 -57.619  57.095  1.00 30.00           O  
ATOM   3844  CB  ASN C 156       7.966 -60.373  57.419  1.00 32.02           C  
ATOM   3845  CG  ASN C 156       6.622 -60.887  57.889  1.00 73.35           C  
ATOM   3846  OD1 ASN C 156       5.831 -60.138  58.473  1.00 66.70           O  
ATOM   3847  ND2 ASN C 156       6.316 -62.144  57.558  1.00 68.79           N  
ATOM   3848  N   ASP C 157       9.918 -58.866  55.246  1.00 27.48           N  
ATOM   3849  CA  ASP C 157      11.204 -58.215  55.004  1.00 27.32           C  
ATOM   3850  C   ASP C 157      10.990 -56.749  54.639  1.00 27.34           C  
ATOM   3851  O   ASP C 157      11.636 -55.861  55.202  1.00 25.87           O  
ATOM   3852  CB  ASP C 157      11.986 -58.974  53.928  1.00 30.06           C  
ATOM   3853  CG  ASP C 157      12.363 -60.365  54.381  1.00 34.27           C  
ATOM   3854  OD1 ASP C 157      12.894 -60.472  55.493  1.00 37.00           O  
ATOM   3855  OD2 ASP C 157      12.108 -61.331  53.647  1.00 38.36           O  
ATOM   3856  N   LEU C 158      10.011 -56.487  53.786  1.00 22.75           N  
ATOM   3857  CA  LEU C 158       9.677 -55.108  53.410  1.00 22.79           C  
ATOM   3858  C   LEU C 158       9.222 -54.293  54.641  1.00 29.35           C  
ATOM   3859  O   LEU C 158       9.651 -53.161  54.840  1.00 28.74           O  
ATOM   3860  CB  LEU C 158       8.559 -55.123  52.360  1.00 22.47           C  
ATOM   3861  CG  LEU C 158       9.025 -55.643  51.000  1.00 25.46           C  
ATOM   3862  CD1 LEU C 158       7.823 -55.977  50.116  1.00 24.90           C  
ATOM   3863  CD2 LEU C 158       9.894 -54.591  50.355  1.00 23.01           C  
ATOM   3864  N   ILE C 159       8.365 -54.889  55.470  1.00 28.90           N  
ATOM   3865  CA  ILE C 159       7.850 -54.223  56.664  1.00 28.44           C  
ATOM   3866  C   ILE C 159       8.996 -53.895  57.599  1.00 32.08           C  
ATOM   3867  O   ILE C 159       9.103 -52.753  58.087  1.00 31.06           O  
ATOM   3868  CB  ILE C 159       6.711 -55.039  57.355  1.00 31.63           C  
ATOM   3869  CG1 ILE C 159       5.440 -54.977  56.503  1.00 32.60           C  
ATOM   3870  CG2 ILE C 159       6.385 -54.475  58.767  1.00 29.39           C  
ATOM   3871  CD1 ILE C 159       4.552 -56.177  56.675  1.00 42.12           C  
ATOM   3872  N   ASP C 160       9.881 -54.870  57.825  1.00 29.09           N  
ATOM   3873  CA  ASP C 160      11.049 -54.621  58.680  1.00 29.40           C  
ATOM   3874  C   ASP C 160      11.882 -53.463  58.196  1.00 31.44           C  
ATOM   3875  O   ASP C 160      12.261 -52.602  58.981  1.00 32.18           O  
ATOM   3876  CB  ASP C 160      11.949 -55.845  58.769  1.00 33.01           C  
ATOM   3877  CG  ASP C 160      11.348 -56.941  59.611  1.00 54.91           C  
ATOM   3878  OD1 ASP C 160      10.439 -56.632  60.419  1.00 56.81           O  
ATOM   3879  OD2 ASP C 160      11.752 -58.110  59.419  1.00 64.26           O  
ATOM   3880  N   THR C 161      12.204 -53.461  56.909  1.00 26.38           N  
ATOM   3881  CA  THR C 161      13.014 -52.402  56.338  1.00 25.76           C  
ATOM   3882  C   THR C 161      12.326 -51.053  56.415  1.00 29.01           C  
ATOM   3883  O   THR C 161      12.952 -50.053  56.729  1.00 27.47           O  
ATOM   3884  CB  THR C 161      13.446 -52.731  54.892  1.00 33.11           C  
ATOM   3885  OG1 THR C 161      14.213 -53.941  54.898  1.00 32.09           O  
ATOM   3886  CG2 THR C 161      14.285 -51.569  54.319  1.00 29.03           C  
ATOM   3887  N   TRP C 162      11.036 -51.023  56.104  1.00 27.69           N  
ATOM   3888  CA  TRP C 162      10.270 -49.789  56.192  1.00 28.39           C  
ATOM   3889  C   TRP C 162      10.286 -49.237  57.611  1.00 33.50           C  
ATOM   3890  O   TRP C 162      10.556 -48.071  57.834  1.00 32.35           O  
ATOM   3891  CB  TRP C 162       8.827 -50.071  55.804  1.00 28.06           C  
ATOM   3892  CG  TRP C 162       7.920 -48.862  55.890  1.00 29.66           C  
ATOM   3893  CD1 TRP C 162       6.842 -48.698  56.732  1.00 32.18           C  
ATOM   3894  CD2 TRP C 162       7.917 -47.720  55.010  1.00 29.27           C  
ATOM   3895  NE1 TRP C 162       6.194 -47.519  56.450  1.00 31.58           N  
ATOM   3896  CE2 TRP C 162       6.815 -46.903  55.392  1.00 33.75           C  
ATOM   3897  CE3 TRP C 162       8.740 -47.299  53.959  1.00 29.37           C  
ATOM   3898  CZ2 TRP C 162       6.531 -45.675  54.757  1.00 32.83           C  
ATOM   3899  CZ3 TRP C 162       8.455 -46.086  53.329  1.00 30.33           C  
ATOM   3900  CH2 TRP C 162       7.355 -45.300  53.716  1.00 31.25           C  
ATOM   3901  N   GLU C 163       9.984 -50.081  58.587  1.00 32.09           N  
ATOM   3902  CA  GLU C 163       9.947 -49.604  59.968  1.00 32.32           C  
ATOM   3903  C   GLU C 163      11.307 -49.168  60.476  1.00 34.68           C  
ATOM   3904  O   GLU C 163      11.427 -48.171  61.183  1.00 33.79           O  
ATOM   3905  CB  GLU C 163       9.321 -50.641  60.884  1.00 33.92           C  
ATOM   3906  CG  GLU C 163       7.805 -50.663  60.770  1.00 46.47           C  
ATOM   3907  CD  GLU C 163       7.205 -51.898  61.405  1.00 75.67           C  
ATOM   3908  OE1 GLU C 163       7.979 -52.732  61.952  1.00 60.05           O  
ATOM   3909  OE2 GLU C 163       5.960 -52.035  61.344  1.00 76.32           O  
ATOM   3910  N   GLY C 164      12.344 -49.893  60.077  1.00 30.93           N  
ATOM   3911  CA  GLY C 164      13.691 -49.526  60.484  1.00 30.70           C  
ATOM   3912  C   GLY C 164      14.072 -48.169  59.897  1.00 35.22           C  
ATOM   3913  O   GLY C 164      14.760 -47.392  60.547  1.00 35.03           O  
ATOM   3914  N   THR C 165      13.635 -47.900  58.663  1.00 30.62           N  
ATOM   3915  CA  THR C 165      13.967 -46.644  57.992  1.00 29.68           C  
ATOM   3916  C   THR C 165      13.247 -45.464  58.624  1.00 32.52           C  
ATOM   3917  O   THR C 165      13.850 -44.410  58.856  1.00 30.04           O  
ATOM   3918  CB  THR C 165      13.713 -46.741  56.474  1.00 28.06           C  
ATOM   3919  OG1 THR C 165      14.585 -47.742  55.930  1.00 27.04           O  
ATOM   3920  CG2 THR C 165      13.965 -45.421  55.791  1.00 24.14           C  
ATOM   3921  N   VAL C 166      11.950 -45.641  58.889  1.00 30.59           N  
ATOM   3922  CA  VAL C 166      11.137 -44.595  59.516  1.00 30.48           C  
ATOM   3923  C   VAL C 166      11.716 -44.284  60.904  1.00 35.21           C  
ATOM   3924  O   VAL C 166      11.782 -43.127  61.312  1.00 34.09           O  
ATOM   3925  CB  VAL C 166       9.647 -44.989  59.557  1.00 35.24           C  
ATOM   3926  CG1 VAL C 166       8.847 -43.988  60.384  1.00 35.00           C  
ATOM   3927  CG2 VAL C 166       9.065 -45.056  58.131  1.00 34.69           C  
ATOM   3928  N   LYS C 167      12.217 -45.314  61.590  1.00 32.85           N  
ATOM   3929  CA  LYS C 167      12.858 -45.110  62.884  1.00 32.93           C  
ATOM   3930  C   LYS C 167      14.141 -44.283  62.723  1.00 35.84           C  
ATOM   3931  O   LYS C 167      14.361 -43.321  63.444  1.00 35.36           O  
ATOM   3932  CB  LYS C 167      13.149 -46.454  63.565  1.00 35.53           C  
ATOM   3933  N   ALA C 168      14.977 -44.644  61.751  1.00 32.16           N  
ATOM   3934  CA  ALA C 168      16.252 -43.948  61.536  1.00 31.32           C  
ATOM   3935  C   ALA C 168      16.056 -42.486  61.187  1.00 35.33           C  
ATOM   3936  O   ALA C 168      16.740 -41.612  61.712  1.00 33.50           O  
ATOM   3937  CB  ALA C 168      17.079 -44.648  60.460  1.00 31.40           C  
ATOM   3938  N   ILE C 169      15.146 -42.226  60.256  1.00 33.83           N  
ATOM   3939  CA  ILE C 169      14.890 -40.862  59.815  1.00 35.39           C  
ATOM   3940  C   ILE C 169      14.488 -39.961  60.980  1.00 44.17           C  
ATOM   3941  O   ILE C 169      14.932 -38.823  61.074  1.00 43.67           O  
ATOM   3942  CB  ILE C 169      13.817 -40.824  58.677  1.00 38.59           C  
ATOM   3943  CG1 ILE C 169      14.410 -41.333  57.377  1.00 38.88           C  
ATOM   3944  CG2 ILE C 169      13.354 -39.422  58.433  1.00 39.93           C  
ATOM   3945  CD1 ILE C 169      13.372 -41.810  56.403  1.00 52.03           C  
ATOM   3946  N   GLY C 170      13.631 -40.477  61.860  1.00 43.85           N  
ATOM   3947  CA  GLY C 170      13.129 -39.697  62.982  1.00 44.29           C  
ATOM   3948  C   GLY C 170      14.073 -39.594  64.168  1.00 49.85           C  
ATOM   3949  O   GLY C 170      13.859 -38.793  65.072  1.00 51.35           O  
ATOM   3950  N   SER C 171      15.101 -40.422  64.194  1.00 46.18           N  
ATOM   3951  CA  SER C 171      16.026 -40.422  65.320  1.00 46.06           C  
ATOM   3952  C   SER C 171      17.420 -39.842  65.011  1.00 50.56           C  
ATOM   3953  O   SER C 171      18.102 -39.343  65.906  1.00 49.35           O  
ATOM   3954  CB  SER C 171      16.177 -41.852  65.833  1.00 49.45           C  
ATOM   3955  OG  SER C 171      17.292 -42.487  65.225  1.00 60.40           O  
ATOM   3956  N   THR C 172      17.854 -39.972  63.754  1.00 47.81           N  
ATOM   3957  CA  THR C 172      19.188 -39.547  63.318  1.00 46.50           C  
ATOM   3958  C   THR C 172      19.133 -38.277  62.482  1.00 47.08           C  
ATOM   3959  O   THR C 172      18.590 -38.278  61.384  1.00 45.37           O  
ATOM   3960  CB  THR C 172      19.900 -40.678  62.514  1.00 54.02           C  
ATOM   3961  OG1 THR C 172      19.538 -41.960  63.047  1.00 55.36           O  
ATOM   3962  CG2 THR C 172      21.415 -40.508  62.578  1.00 49.92           C  
ATOM   3963  N   GLY C 173      19.731 -37.204  62.978  1.00 41.99           N  
ATOM   3964  CA  GLY C 173      19.753 -35.966  62.209  1.00 41.05           C  
ATOM   3965  C   GLY C 173      20.664 -36.072  60.976  1.00 43.58           C  
ATOM   3966  O   GLY C 173      20.440 -35.396  59.968  1.00 44.49           O  
ATOM   3967  N   ALA C 174      21.655 -36.963  61.040  1.00 35.43           N  
ATOM   3968  CA  ALA C 174      22.620 -37.109  59.974  1.00 31.88           C  
ATOM   3969  C   ALA C 174      22.176 -38.074  58.880  1.00 31.45           C  
ATOM   3970  O   ALA C 174      22.908 -38.322  57.926  1.00 29.71           O  
ATOM   3971  CB  ALA C 174      23.967 -37.510  60.539  1.00 32.28           C  
ATOM   3972  N   PHE C 175      20.959 -38.582  59.003  1.00 25.24           N  
ATOM   3973  CA  PHE C 175      20.428 -39.516  58.026  1.00 24.38           C  
ATOM   3974  C   PHE C 175      20.590 -39.090  56.552  1.00 27.87           C  
ATOM   3975  O   PHE C 175      20.949 -39.897  55.705  1.00 29.32           O  
ATOM   3976  CB  PHE C 175      18.975 -39.863  58.351  1.00 25.53           C  
ATOM   3977  CG  PHE C 175      18.340 -40.814  57.373  1.00 26.42           C  
ATOM   3978  CD1 PHE C 175      17.753 -40.339  56.210  1.00 28.16           C  
ATOM   3979  CD2 PHE C 175      18.313 -42.179  57.627  1.00 27.64           C  
ATOM   3980  CE1 PHE C 175      17.213 -41.209  55.284  1.00 28.98           C  
ATOM   3981  CE2 PHE C 175      17.762 -43.074  56.703  1.00 30.03           C  
ATOM   3982  CZ  PHE C 175      17.208 -42.588  55.528  1.00 28.11           C  
ATOM   3983  N   ASN C 176      20.282 -37.836  56.260  1.00 23.85           N  
ATOM   3984  CA  ASN C 176      20.314 -37.263  54.909  1.00 24.66           C  
ATOM   3985  C   ASN C 176      21.740 -37.186  54.361  1.00 27.26           C  
ATOM   3986  O   ASN C 176      21.960 -37.029  53.155  1.00 25.15           O  
ATOM   3987  CB  ASN C 176      19.716 -35.839  54.926  1.00 26.43           C  
ATOM   3988  CG  ASN C 176      18.226 -35.850  55.188  1.00 62.65           C  
ATOM   3989  OD1 ASN C 176      17.584 -36.889  55.073  1.00 63.26           O  
ATOM   3990  ND2 ASN C 176      17.672 -34.702  55.562  1.00 59.23           N  
ATOM   3991  N   ASP C 177      22.694 -37.234  55.283  1.00 23.17           N  
ATOM   3992  CA  ASP C 177      24.099 -37.243  54.948  1.00 21.84           C  
ATOM   3993  C   ASP C 177      24.606 -38.716  54.854  1.00 23.34           C  
ATOM   3994  O   ASP C 177      24.981 -39.181  53.804  1.00 22.18           O  
ATOM   3995  CB  ASP C 177      24.840 -36.451  56.009  1.00 23.57           C  
ATOM   3996  CG  ASP C 177      26.346 -36.494  55.850  1.00 27.45           C  
ATOM   3997  OD1 ASP C 177      26.896 -37.123  54.904  1.00 25.15           O  
ATOM   3998  OD2 ASP C 177      26.986 -35.924  56.744  1.00 33.76           O  
ATOM   3999  N   TRP C 178      24.564 -39.447  55.955  1.00 19.55           N  
ATOM   4000  CA  TRP C 178      25.007 -40.834  55.991  1.00 18.72           C  
ATOM   4001  C   TRP C 178      24.369 -41.813  55.003  1.00 23.54           C  
ATOM   4002  O   TRP C 178      24.966 -42.842  54.651  1.00 24.01           O  
ATOM   4003  CB  TRP C 178      24.881 -41.366  57.399  1.00 16.75           C  
ATOM   4004  CG  TRP C 178      25.717 -40.586  58.392  1.00 17.71           C  
ATOM   4005  CD1 TRP C 178      26.696 -39.656  58.118  1.00 19.99           C  
ATOM   4006  CD2 TRP C 178      25.632 -40.677  59.836  1.00 18.18           C  
ATOM   4007  NE1 TRP C 178      27.184 -39.127  59.306  1.00 20.03           N  
ATOM   4008  CE2 TRP C 178      26.557 -39.738  60.370  1.00 21.93           C  
ATOM   4009  CE3 TRP C 178      24.823 -41.418  60.721  1.00 19.44           C  
ATOM   4010  CZ2 TRP C 178      26.719 -39.551  61.740  1.00 21.16           C  
ATOM   4011  CZ3 TRP C 178      24.969 -41.201  62.110  1.00 20.65           C  
ATOM   4012  CH2 TRP C 178      25.949 -40.327  62.593  1.00 21.06           C  
ATOM   4013  N   ILE C 179      23.177 -41.494  54.524  1.00 19.04           N  
ATOM   4014  CA  ILE C 179      22.506 -42.382  53.608  1.00 18.87           C  
ATOM   4015  C   ILE C 179      23.393 -42.601  52.366  1.00 22.17           C  
ATOM   4016  O   ILE C 179      23.271 -43.615  51.693  1.00 19.49           O  
ATOM   4017  CB  ILE C 179      21.081 -41.848  53.250  1.00 21.91           C  
ATOM   4018  CG1 ILE C 179      20.254 -42.919  52.498  1.00 22.47           C  
ATOM   4019  CG2 ILE C 179      21.172 -40.569  52.395  1.00 19.99           C  
ATOM   4020  CD1 ILE C 179      19.880 -44.158  53.311  1.00 29.96           C  
ATOM   4021  N   ARG C 180      24.254 -41.627  52.053  1.00 19.38           N  
ATOM   4022  CA  ARG C 180      25.132 -41.729  50.893  1.00 19.43           C  
ATOM   4023  C   ARG C 180      26.151 -42.856  51.033  1.00 24.09           C  
ATOM   4024  O   ARG C 180      26.504 -43.478  50.035  1.00 24.65           O  
ATOM   4025  CB  ARG C 180      25.785 -40.382  50.542  1.00 18.84           C  
ATOM   4026  CG  ARG C 180      24.768 -39.351  49.925  1.00 20.52           C  
ATOM   4027  CD  ARG C 180      25.356 -37.951  49.863  1.00 21.69           C  
ATOM   4028  NE  ARG C 180      25.826 -37.465  51.176  1.00 21.03           N  
ATOM   4029  CZ  ARG C 180      26.430 -36.290  51.360  1.00 27.50           C  
ATOM   4030  NH1 ARG C 180      26.626 -35.454  50.339  1.00 20.41           N  
ATOM   4031  NH2 ARG C 180      26.820 -35.934  52.570  1.00 18.47           N  
ATOM   4032  N   ASP C 181      26.591 -43.148  52.266  1.00 18.50           N  
ATOM   4033  CA  ASP C 181      27.530 -44.261  52.489  1.00 17.44           C  
ATOM   4034  C   ASP C 181      26.818 -45.581  52.146  1.00 21.85           C  
ATOM   4035  O   ASP C 181      27.435 -46.525  51.684  1.00 22.38           O  
ATOM   4036  CB  ASP C 181      27.953 -44.359  53.978  1.00 18.83           C  
ATOM   4037  CG  ASP C 181      28.511 -43.058  54.546  1.00 24.72           C  
ATOM   4038  OD1 ASP C 181      28.844 -42.123  53.779  1.00 27.35           O  
ATOM   4039  OD2 ASP C 181      28.623 -42.971  55.795  1.00 25.53           O  
ATOM   4040  N   PHE C 182      25.512 -45.645  52.382  1.00 17.69           N  
ATOM   4041  CA  PHE C 182      24.745 -46.861  52.120  1.00 18.34           C  
ATOM   4042  C   PHE C 182      24.442 -47.037  50.639  1.00 21.85           C  
ATOM   4043  O   PHE C 182      24.534 -48.131  50.075  1.00 22.38           O  
ATOM   4044  CB  PHE C 182      23.423 -46.814  52.905  1.00 20.51           C  
ATOM   4045  CG  PHE C 182      22.419 -47.844  52.460  1.00 22.50           C  
ATOM   4046  CD1 PHE C 182      22.501 -49.145  52.914  1.00 24.12           C  
ATOM   4047  CD2 PHE C 182      21.370 -47.487  51.616  1.00 24.67           C  
ATOM   4048  CE1 PHE C 182      21.578 -50.085  52.511  1.00 25.81           C  
ATOM   4049  CE2 PHE C 182      20.459 -48.421  51.208  1.00 27.20           C  
ATOM   4050  CZ  PHE C 182      20.571 -49.732  51.642  1.00 24.58           C  
ATOM   4051  N   TRP C 183      24.048 -45.934  50.034  1.00 17.68           N  
ATOM   4052  CA  TRP C 183      23.662 -45.834  48.629  1.00 17.76           C  
ATOM   4053  C   TRP C 183      24.770 -46.226  47.624  1.00 21.28           C  
ATOM   4054  O   TRP C 183      24.563 -47.023  46.705  1.00 21.57           O  
ATOM   4055  CB  TRP C 183      23.257 -44.372  48.447  1.00 17.08           C  
ATOM   4056  CG  TRP C 183      22.716 -43.926  47.138  1.00 18.20           C  
ATOM   4057  CD1 TRP C 183      22.597 -44.648  45.971  1.00 20.58           C  
ATOM   4058  CD2 TRP C 183      22.216 -42.599  46.854  1.00 18.26           C  
ATOM   4059  NE1 TRP C 183      22.074 -43.844  44.983  1.00 19.85           N  
ATOM   4060  CE2 TRP C 183      21.820 -42.588  45.492  1.00 21.85           C  
ATOM   4061  CE3 TRP C 183      22.009 -41.446  47.639  1.00 19.00           C  
ATOM   4062  CZ2 TRP C 183      21.268 -41.443  44.876  1.00 21.11           C  
ATOM   4063  CZ3 TRP C 183      21.448 -40.306  47.031  1.00 20.73           C  
ATOM   4064  CH2 TRP C 183      21.116 -40.308  45.648  1.00 21.52           C  
ATOM   4065  N   PHE C 184      25.957 -45.673  47.811  1.00 17.60           N  
ATOM   4066  CA  PHE C 184      27.051 -45.932  46.891  1.00 17.26           C  
ATOM   4067  C   PHE C 184      27.937 -47.048  47.373  1.00 20.19           C  
ATOM   4068  O   PHE C 184      29.068 -46.844  47.747  1.00 20.04           O  
ATOM   4069  CB  PHE C 184      27.785 -44.622  46.592  1.00 18.82           C  
ATOM   4070  CG  PHE C 184      26.888 -43.585  45.976  1.00 19.48           C  
ATOM   4071  CD1 PHE C 184      26.430 -43.740  44.673  1.00 20.55           C  
ATOM   4072  CD2 PHE C 184      26.340 -42.572  46.754  1.00 21.76           C  
ATOM   4073  CE1 PHE C 184      25.552 -42.825  44.110  1.00 21.39           C  
ATOM   4074  CE2 PHE C 184      25.433 -41.654  46.200  1.00 23.10           C  
ATOM   4075  CZ  PHE C 184      25.036 -41.791  44.880  1.00 20.37           C  
ATOM   4076  N   ILE C 185      27.348 -48.227  47.418  1.00 17.34           N  
ATOM   4077  CA  ILE C 185      27.975 -49.446  47.917  1.00 18.01           C  
ATOM   4078  C   ILE C 185      29.355 -49.746  47.356  1.00 21.02           C  
ATOM   4079  O   ILE C 185      29.626 -49.550  46.157  1.00 19.61           O  
ATOM   4080  CB  ILE C 185      26.995 -50.662  47.726  1.00 20.91           C  
ATOM   4081  CG1 ILE C 185      27.491 -51.897  48.480  1.00 22.15           C  
ATOM   4082  CG2 ILE C 185      26.764 -50.929  46.248  1.00 18.86           C  
ATOM   4083  CD1 ILE C 185      26.426 -52.940  48.704  1.00 25.86           C  
ATOM   4084  N   GLY C 186      30.238 -50.214  48.229  1.00 17.10           N  
ATOM   4085  CA  GLY C 186      31.585 -50.581  47.818  1.00 16.84           C  
ATOM   4086  C   GLY C 186      32.331 -49.465  47.070  1.00 21.65           C  
ATOM   4087  O   GLY C 186      32.345 -48.313  47.489  1.00 19.33           O  
ATOM   4088  N   PRO C 187      32.921 -49.821  45.934  1.00 19.81           N  
ATOM   4089  CA  PRO C 187      33.694 -48.868  45.144  1.00 18.76           C  
ATOM   4090  C   PRO C 187      32.879 -47.866  44.313  1.00 20.31           C  
ATOM   4091  O   PRO C 187      33.455 -47.030  43.612  1.00 19.55           O  
ATOM   4092  CB  PRO C 187      34.573 -49.776  44.261  1.00 19.40           C  
ATOM   4093  CG  PRO C 187      33.790 -51.038  44.136  1.00 23.22           C  
ATOM   4094  CD  PRO C 187      32.953 -51.184  45.364  1.00 19.84           C  
ATOM   4095  N   ALA C 188      31.554 -47.958  44.377  1.00 17.22           N  
ATOM   4096  CA  ALA C 188      30.674 -46.979  43.706  1.00 17.34           C  
ATOM   4097  C   ALA C 188      30.928 -45.621  44.381  1.00 20.73           C  
ATOM   4098  O   ALA C 188      30.980 -44.582  43.741  1.00 20.30           O  
ATOM   4099  CB  ALA C 188      29.159 -47.387  43.855  1.00 17.93           C  
ATOM   4100  N   PHE C 189      31.174 -45.652  45.677  1.00 17.29           N  
ATOM   4101  CA  PHE C 189      31.520 -44.445  46.376  1.00 18.80           C  
ATOM   4102  C   PHE C 189      32.719 -43.728  45.743  1.00 20.05           C  
ATOM   4103  O   PHE C 189      32.688 -42.513  45.484  1.00 18.94           O  
ATOM   4104  CB  PHE C 189      31.861 -44.794  47.825  1.00 22.30           C  
ATOM   4105  CG  PHE C 189      32.048 -43.590  48.701  1.00 25.38           C  
ATOM   4106  CD1 PHE C 189      30.985 -43.084  49.428  1.00 30.48           C  
ATOM   4107  CD2 PHE C 189      33.272 -42.924  48.726  1.00 29.59           C  
ATOM   4108  CE1 PHE C 189      31.152 -41.959  50.221  1.00 33.80           C  
ATOM   4109  CE2 PHE C 189      33.465 -41.802  49.522  1.00 33.69           C  
ATOM   4110  CZ  PHE C 189      32.408 -41.313  50.276  1.00 32.59           C  
ATOM   4111  N   THR C 190      33.800 -44.479  45.590  1.00 16.63           N  
ATOM   4112  CA  THR C 190      35.073 -43.981  45.048  1.00 16.10           C  
ATOM   4113  C   THR C 190      34.917 -43.417  43.636  1.00 19.17           C  
ATOM   4114  O   THR C 190      35.565 -42.441  43.268  1.00 19.17           O  
ATOM   4115  CB  THR C 190      36.083 -45.159  44.977  1.00 19.51           C  
ATOM   4116  OG1 THR C 190      36.141 -45.812  46.232  1.00 16.36           O  
ATOM   4117  CG2 THR C 190      37.478 -44.667  44.598  1.00 15.63           C  
ATOM   4118  N   ALA C 191      34.101 -44.078  42.826  1.00 16.63           N  
ATOM   4119  CA  ALA C 191      33.890 -43.663  41.428  1.00 16.71           C  
ATOM   4120  C   ALA C 191      33.331 -42.230  41.290  1.00 20.51           C  
ATOM   4121  O   ALA C 191      33.600 -41.556  40.308  1.00 20.82           O  
ATOM   4122  CB  ALA C 191      32.991 -44.688  40.675  1.00 16.64           C  
ATOM   4123  N   LEU C 192      32.586 -41.764  42.292  1.00 15.45           N  
ATOM   4124  CA  LEU C 192      32.022 -40.412  42.271  1.00 14.53           C  
ATOM   4125  C   LEU C 192      33.109 -39.380  42.001  1.00 20.41           C  
ATOM   4126  O   LEU C 192      33.036 -38.628  41.010  1.00 21.14           O  
ATOM   4127  CB  LEU C 192      31.262 -40.084  43.592  1.00 12.71           C  
ATOM   4128  CG  LEU C 192      29.944 -40.865  43.781  1.00 16.12           C  
ATOM   4129  CD1 LEU C 192      29.323 -40.605  45.192  1.00 15.46           C  
ATOM   4130  CD2 LEU C 192      28.919 -40.478  42.695  1.00 15.82           C  
ATOM   4131  N   ASN C 193      34.107 -39.334  42.887  1.00 16.41           N  
ATOM   4132  CA  ASN C 193      35.195 -38.377  42.746  1.00 16.26           C  
ATOM   4133  C   ASN C 193      35.979 -38.498  41.443  1.00 19.21           C  
ATOM   4134  O   ASN C 193      36.436 -37.494  40.863  1.00 19.27           O  
ATOM   4135  CB  ASN C 193      36.179 -38.498  43.915  1.00 18.19           C  
ATOM   4136  CG  ASN C 193      37.272 -37.456  43.839  1.00 33.18           C  
ATOM   4137  OD1 ASN C 193      37.014 -36.303  44.114  1.00 32.05           O  
ATOM   4138  ND2 ASN C 193      38.485 -37.853  43.420  1.00 27.55           N  
ATOM   4139  N   GLU C 194      36.234 -39.739  41.054  1.00 15.00           N  
ATOM   4140  CA  GLU C 194      36.984 -40.070  39.842  1.00 14.66           C  
ATOM   4141  C   GLU C 194      36.374 -39.425  38.602  1.00 19.99           C  
ATOM   4142  O   GLU C 194      37.096 -39.061  37.661  1.00 18.53           O  
ATOM   4143  CB  GLU C 194      37.015 -41.588  39.666  1.00 15.63           C  
ATOM   4144  CG  GLU C 194      38.118 -42.071  38.799  1.00 26.41           C  
ATOM   4145  CD  GLU C 194      39.476 -41.983  39.488  1.00 48.03           C  
ATOM   4146  OE1 GLU C 194      39.539 -41.930  40.744  1.00 40.37           O  
ATOM   4147  OE2 GLU C 194      40.488 -41.973  38.762  1.00 48.66           O  
ATOM   4148  N   GLY C 195      35.045 -39.315  38.568  1.00 15.20           N  
ATOM   4149  CA  GLY C 195      34.390 -38.694  37.420  1.00 14.62           C  
ATOM   4150  C   GLY C 195      34.059 -37.210  37.643  1.00 19.72           C  
ATOM   4151  O   GLY C 195      33.360 -36.606  36.811  1.00 20.62           O  
ATOM   4152  N   GLY C 196      34.511 -36.620  38.758  1.00 14.85           N  
ATOM   4153  CA  GLY C 196      34.238 -35.177  39.033  1.00 13.97           C  
ATOM   4154  C   GLY C 196      32.764 -34.982  39.319  1.00 20.19           C  
ATOM   4155  O   GLY C 196      32.134 -34.022  38.887  1.00 19.64           O  
ATOM   4156  N   GLN C 197      32.199 -35.950  40.022  1.00 18.26           N  
ATOM   4157  CA  GLN C 197      30.784 -35.972  40.294  1.00 18.62           C  
ATOM   4158  C   GLN C 197      30.476 -35.884  41.791  1.00 20.98           C  
ATOM   4159  O   GLN C 197      31.179 -36.470  42.609  1.00 20.34           O  
ATOM   4160  CB  GLN C 197      30.228 -37.260  39.686  1.00 20.35           C  
ATOM   4161  CG  GLN C 197      28.759 -37.399  39.804  1.00 25.66           C  
ATOM   4162  CD  GLN C 197      28.237 -38.558  38.970  1.00 32.68           C  
ATOM   4163  OE1 GLN C 197      28.997 -39.440  38.588  1.00 25.26           O  
ATOM   4164  NE2 GLN C 197      26.932 -38.571  38.720  1.00 25.21           N  
ATOM   4165  N   ARG C 198      29.492 -35.071  42.140  1.00 17.10           N  
ATOM   4166  CA  ARG C 198      29.107 -34.860  43.540  1.00 18.13           C  
ATOM   4167  C   ARG C 198      27.605 -35.131  43.742  1.00 21.59           C  
ATOM   4168  O   ARG C 198      26.779 -34.664  42.959  1.00 21.93           O  
ATOM   4169  CB  ARG C 198      29.341 -33.386  43.973  1.00 19.72           C  
ATOM   4170  CG  ARG C 198      30.756 -32.879  43.932  1.00 29.89           C  
ATOM   4171  CD  ARG C 198      30.802 -31.354  44.075  1.00 36.58           C  
ATOM   4172  NE  ARG C 198      30.504 -30.975  45.444  1.00 30.33           N  
ATOM   4173  CZ  ARG C 198      30.214 -29.752  45.859  1.00 30.19           C  
ATOM   4174  NH1 ARG C 198      30.191 -28.723  45.020  1.00 19.00           N  
ATOM   4175  NH2 ARG C 198      29.964 -29.574  47.137  1.00 21.79           N  
ATOM   4176  N   ILE C 199      27.258 -35.758  44.859  1.00 18.70           N  
ATOM   4177  CA  ILE C 199      25.864 -36.024  45.226  1.00 18.58           C  
ATOM   4178  C   ILE C 199      25.554 -35.227  46.496  1.00 22.91           C  
ATOM   4179  O   ILE C 199      26.265 -35.381  47.489  1.00 21.79           O  
ATOM   4180  CB  ILE C 199      25.632 -37.532  45.529  1.00 21.30           C  
ATOM   4181  CG1 ILE C 199      26.101 -38.406  44.362  1.00 21.01           C  
ATOM   4182  CG2 ILE C 199      24.125 -37.784  45.771  1.00 21.15           C  
ATOM   4183  CD1 ILE C 199      25.235 -38.241  43.110  1.00 25.21           C  
ATOM   4184  N   SER C 200      24.512 -34.381  46.467  1.00 19.27           N  
ATOM   4185  CA  SER C 200      24.139 -33.579  47.645  1.00 18.17           C  
ATOM   4186  C   SER C 200      23.507 -34.475  48.711  1.00 22.38           C  
ATOM   4187  O   SER C 200      23.169 -35.612  48.440  1.00 20.53           O  
ATOM   4188  CB  SER C 200      23.074 -32.557  47.241  1.00 20.95           C  
ATOM   4189  OG  SER C 200      21.817 -33.207  47.006  1.00 21.19           O  
ATOM   4190  N   ARG C 201      23.255 -33.919  49.888  1.00 21.77           N  
ATOM   4191  CA  ARG C 201      22.503 -34.629  50.914  1.00 21.87           C  
ATOM   4192  C   ARG C 201      21.088 -34.760  50.346  1.00 24.95           C  
ATOM   4193  O   ARG C 201      20.678 -33.976  49.501  1.00 22.85           O  
ATOM   4194  CB  ARG C 201      22.414 -33.764  52.167  1.00 21.94           C  
ATOM   4195  CG  ARG C 201      23.712 -33.630  52.896  1.00 28.51           C  
ATOM   4196  CD  ARG C 201      23.600 -32.599  53.977  1.00 35.14           C  
ATOM   4197  NE  ARG C 201      24.902 -32.401  54.601  1.00 53.22           N  
ATOM   4198  CZ  ARG C 201      25.129 -32.492  55.906  1.00 70.55           C  
ATOM   4199  NH1 ARG C 201      24.137 -32.782  56.754  1.00 51.70           N  
ATOM   4200  NH2 ARG C 201      26.360 -32.294  56.367  1.00 58.08           N  
ATOM   4201  N   ILE C 202      20.336 -35.760  50.761  1.00 23.57           N  
ATOM   4202  CA  ILE C 202      18.988 -35.862  50.205  1.00 23.95           C  
ATOM   4203  C   ILE C 202      18.012 -35.009  51.027  1.00 28.85           C  
ATOM   4204  O   ILE C 202      18.288 -34.641  52.173  1.00 27.68           O  
ATOM   4205  CB  ILE C 202      18.496 -37.341  50.114  1.00 26.84           C  
ATOM   4206  CG1 ILE C 202      18.242 -37.901  51.529  1.00 27.63           C  
ATOM   4207  CG2 ILE C 202      19.471 -38.189  49.319  1.00 25.71           C  
ATOM   4208  CD1 ILE C 202      17.364 -39.143  51.536  1.00 32.34           C  
ATOM   4209  N   GLU C 203      16.869 -34.704  50.425  1.00 25.70           N  
ATOM   4210  CA  GLU C 203      15.801 -34.034  51.136  1.00 25.74           C  
ATOM   4211  C   GLU C 203      14.598 -34.965  51.144  1.00 28.81           C  
ATOM   4212  O   GLU C 203      14.206 -35.514  50.122  1.00 27.01           O  
ATOM   4213  CB  GLU C 203      15.495 -32.666  50.555  1.00 27.35           C  
ATOM   4214  CG  GLU C 203      14.032 -32.207  50.674  1.00 47.04           C  
ATOM   4215  CD  GLU C 203      13.816 -30.737  50.238  1.00 78.20           C  
ATOM   4216  OE1 GLU C 203      13.441 -29.914  51.098  1.00 89.66           O  
ATOM   4217  OE2 GLU C 203      13.987 -30.406  49.041  1.00 64.46           O  
ATOM   4218  N   VAL C 204      14.101 -35.261  52.334  1.00 27.84           N  
ATOM   4219  CA  VAL C 204      12.951 -36.169  52.458  1.00 27.65           C  
ATOM   4220  C   VAL C 204      11.698 -35.320  52.639  1.00 31.76           C  
ATOM   4221  O   VAL C 204      11.490 -34.755  53.699  1.00 32.96           O  
ATOM   4222  CB  VAL C 204      13.126 -37.169  53.637  1.00 29.61           C  
ATOM   4223  CG1 VAL C 204      11.884 -38.048  53.779  1.00 28.54           C  
ATOM   4224  CG2 VAL C 204      14.381 -37.991  53.469  1.00 28.79           C  
ATOM   4225  N   ASN C 205      10.872 -35.232  51.607  1.00 28.90           N  
ATOM   4226  CA  ASN C 205       9.684 -34.372  51.654  1.00 29.89           C  
ATOM   4227  C   ASN C 205       8.443 -35.035  52.227  1.00 36.53           C  
ATOM   4228  O   ASN C 205       7.512 -34.352  52.648  1.00 36.33           O  
ATOM   4229  CB  ASN C 205       9.375 -33.737  50.281  1.00 31.33           C  
ATOM   4230  CG  ASN C 205      10.581 -33.031  49.677  1.00 60.26           C  
ATOM   4231  OD1 ASN C 205      10.950 -33.301  48.533  1.00 65.85           O  
ATOM   4232  ND2 ASN C 205      11.226 -32.158  50.454  1.00 45.72           N  
ATOM   4233  N   GLY C 206       8.437 -36.364  52.244  1.00 34.27           N  
ATOM   4234  CA  GLY C 206       7.307 -37.106  52.768  1.00 33.68           C  
ATOM   4235  C   GLY C 206       7.578 -38.600  52.787  1.00 35.99           C  
ATOM   4236  O   GLY C 206       8.193 -39.143  51.862  1.00 35.59           O  
ATOM   4237  N   LEU C 207       7.108 -39.245  53.854  1.00 32.31           N  
ATOM   4238  CA  LEU C 207       7.194 -40.689  54.044  1.00 32.58           C  
ATOM   4239  C   LEU C 207       5.809 -41.082  54.618  1.00 36.50           C  
ATOM   4240  O   LEU C 207       5.444 -40.637  55.697  1.00 36.86           O  
ATOM   4241  CB  LEU C 207       8.259 -40.982  55.107  1.00 33.12           C  
ATOM   4242  CG  LEU C 207       9.612 -41.594  54.786  1.00 39.48           C  
ATOM   4243  CD1 LEU C 207       9.762 -42.865  55.567  1.00 41.36           C  
ATOM   4244  CD2 LEU C 207       9.756 -41.877  53.343  1.00 43.12           C  
ATOM   4245  N   ASN C 208       5.062 -41.945  53.945  1.00 33.71           N  
ATOM   4246  CA  ASN C 208       3.755 -42.316  54.451  1.00 33.81           C  
ATOM   4247  C   ASN C 208       3.332 -43.717  54.028  1.00 36.52           C  
ATOM   4248  O   ASN C 208       3.698 -44.207  52.959  1.00 34.51           O  
ATOM   4249  CB  ASN C 208       2.697 -41.294  53.982  1.00 36.04           C  
ATOM   4250  CG  ASN C 208       1.375 -41.412  54.760  1.00 69.66           C  
ATOM   4251  OD1 ASN C 208       1.361 -41.793  55.943  1.00 71.16           O  
ATOM   4252  ND2 ASN C 208       0.261 -41.063  54.102  1.00 50.58           N  
ATOM   4253  N   THR C 209       2.525 -44.342  54.874  1.00 32.97           N  
ATOM   4254  CA  THR C 209       1.975 -45.663  54.581  1.00 33.64           C  
ATOM   4255  C   THR C 209       0.565 -45.394  54.110  1.00 41.91           C  
ATOM   4256  O   THR C 209      -0.217 -44.761  54.820  1.00 43.26           O  
ATOM   4257  CB  THR C 209       1.962 -46.534  55.846  1.00 39.22           C  
ATOM   4258  OG1 THR C 209       3.249 -46.493  56.484  1.00 38.31           O  
ATOM   4259  CG2 THR C 209       1.638 -47.961  55.494  1.00 39.83           C  
ATOM   4260  N   GLU C 210       0.273 -45.773  52.880  1.00 40.38           N  
ATOM   4261  CA  GLU C 210      -1.066 -45.587  52.309  1.00 41.30           C  
ATOM   4262  C   GLU C 210      -1.813 -46.919  52.392  1.00 50.81           C  
ATOM   4263  O   GLU C 210      -1.208 -47.983  52.551  1.00 48.80           O  
ATOM   4264  CB  GLU C 210      -0.961 -45.225  50.826  1.00 41.82           C  
ATOM   4265  CG  GLU C 210      -0.774 -43.777  50.515  1.00 48.83           C  
ATOM   4266  CD  GLU C 210      -0.866 -43.505  49.020  1.00 68.90           C  
ATOM   4267  OE1 GLU C 210      -0.665 -42.342  48.631  1.00 58.91           O  
ATOM   4268  OE2 GLU C 210      -1.123 -44.453  48.236  1.00 62.64           O  
ATOM   4269  N   SER C 211      -3.128 -46.879  52.236  1.00 54.74           N  
ATOM   4270  CA  SER C 211      -3.881 -48.122  52.203  1.00 57.25           C  
ATOM   4271  C   SER C 211      -4.240 -48.428  50.755  1.00 66.55           C  
ATOM   4272  O   SER C 211      -5.072 -47.742  50.159  1.00 67.94           O  
ATOM   4273  CB  SER C 211      -5.108 -48.049  53.080  1.00 61.87           C  
ATOM   4274  OG  SER C 211      -4.779 -48.550  54.361  1.00 74.82           O  
ATOM   4275  N   GLY C 212      -3.523 -49.391  50.170  1.00 64.15           N  
ATOM   4276  CA  GLY C 212      -3.713 -49.784  48.775  1.00 63.84           C  
ATOM   4277  CA  LYS C 214      -4.407 -54.731  48.108  1.00 59.15           C  
ATOM   4278  C   LYS C 214      -3.559 -54.830  49.383  1.00 60.18           C  
ATOM   4279  O   LYS C 214      -3.071 -55.917  49.742  1.00 61.00           O  
ATOM   4280  N   GLY C 215      -3.395 -53.708  50.083  1.00 50.98           N  
ATOM   4281  CA  GLY C 215      -2.612 -53.713  51.326  1.00 47.45           C  
ATOM   4282  C   GLY C 215      -1.829 -52.424  51.536  1.00 43.09           C  
ATOM   4283  O   GLY C 215      -1.891 -51.507  50.723  1.00 42.15           O  
ATOM   4284  N   PRO C 216      -1.140 -52.333  52.665  1.00 35.48           N  
ATOM   4285  CA  PRO C 216      -0.340 -51.141  52.975  1.00 35.09           C  
ATOM   4286  C   PRO C 216       0.764 -50.895  51.914  1.00 37.60           C  
ATOM   4287  O   PRO C 216       1.330 -51.840  51.357  1.00 36.93           O  
ATOM   4288  CB  PRO C 216       0.279 -51.473  54.336  1.00 36.62           C  
ATOM   4289  CG  PRO C 216       0.312 -52.963  54.397  1.00 40.86           C  
ATOM   4290  CD  PRO C 216      -0.871 -53.451  53.585  1.00 36.24           C  
ATOM   4291  N   VAL C 217       1.013 -49.625  51.611  1.00 31.98           N  
ATOM   4292  CA  VAL C 217       2.010 -49.234  50.621  1.00 30.36           C  
ATOM   4293  C   VAL C 217       2.895 -48.180  51.261  1.00 32.97           C  
ATOM   4294  O   VAL C 217       2.389 -47.233  51.885  1.00 31.03           O  
ATOM   4295  CB  VAL C 217       1.344 -48.644  49.357  1.00 33.79           C  
ATOM   4296  CG1 VAL C 217       2.402 -48.299  48.317  1.00 33.07           C  
ATOM   4297  CG2 VAL C 217       0.305 -49.609  48.789  1.00 33.28           C  
ATOM   4298  N   GLY C 218       4.214 -48.354  51.130  1.00 28.81           N  
ATOM   4299  CA  GLY C 218       5.181 -47.387  51.665  1.00 27.96           C  
ATOM   4300  C   GLY C 218       5.422 -46.364  50.566  1.00 29.73           C  
ATOM   4301  O   GLY C 218       5.853 -46.720  49.484  1.00 30.14           O  
ATOM   4302  N   VAL C 219       5.062 -45.112  50.823  1.00 25.20           N  
ATOM   4303  CA  VAL C 219       5.184 -44.030  49.826  1.00 24.55           C  
ATOM   4304  C   VAL C 219       6.213 -43.037  50.291  1.00 27.40           C  
ATOM   4305  O   VAL C 219       6.182 -42.604  51.438  1.00 26.49           O  
ATOM   4306  CB  VAL C 219       3.814 -43.299  49.630  1.00 27.79           C  
ATOM   4307  CG1 VAL C 219       3.897 -42.282  48.494  1.00 26.91           C  
ATOM   4308  CG2 VAL C 219       2.716 -44.319  49.342  1.00 27.72           C  
ATOM   4309  N   SER C 220       7.133 -42.666  49.414  1.00 25.30           N  
ATOM   4310  CA  SER C 220       8.142 -41.664  49.795  1.00 25.71           C  
ATOM   4311  C   SER C 220       8.345 -40.646  48.686  1.00 28.52           C  
ATOM   4312  O   SER C 220       8.228 -40.961  47.505  1.00 26.41           O  
ATOM   4313  CB  SER C 220       9.484 -42.313  50.198  1.00 29.92           C  
ATOM   4314  OG  SER C 220      10.016 -43.098  49.143  1.00 35.41           O  
ATOM   4315  N   ARG C 221       8.604 -39.414  49.102  1.00 25.97           N  
ATOM   4316  CA  ARG C 221       8.840 -38.310  48.189  1.00 26.00           C  
ATOM   4317  C   ARG C 221      10.143 -37.668  48.622  1.00 27.86           C  
ATOM   4318  O   ARG C 221      10.240 -37.165  49.725  1.00 25.40           O  
ATOM   4319  CB  ARG C 221       7.710 -37.298  48.293  1.00 25.72           C  
ATOM   4320  CG  ARG C 221       7.887 -36.064  47.458  1.00 29.04           C  
ATOM   4321  CD  ARG C 221       7.713 -36.361  46.005  1.00 41.54           C  
ATOM   4322  NE  ARG C 221       7.781 -35.138  45.212  1.00 59.55           N  
ATOM   4323  CZ  ARG C 221       6.743 -34.340  44.967  1.00 76.93           C  
ATOM   4324  NH1 ARG C 221       5.543 -34.651  45.452  1.00 67.10           N  
ATOM   4325  NH2 ARG C 221       6.906 -33.229  44.239  1.00 56.19           N  
ATOM   4326  N   TRP C 222      11.161 -37.729  47.768  1.00 24.21           N  
ATOM   4327  CA  TRP C 222      12.458 -37.177  48.140  1.00 22.87           C  
ATOM   4328  C   TRP C 222      13.149 -36.572  46.949  1.00 24.19           C  
ATOM   4329  O   TRP C 222      12.811 -36.871  45.806  1.00 21.84           O  
ATOM   4330  CB  TRP C 222      13.343 -38.289  48.735  1.00 21.15           C  
ATOM   4331  CG  TRP C 222      13.520 -39.510  47.843  1.00 21.87           C  
ATOM   4332  CD1 TRP C 222      12.562 -40.452  47.510  1.00 24.61           C  
ATOM   4333  CD2 TRP C 222      14.736 -39.951  47.212  1.00 21.46           C  
ATOM   4334  NE1 TRP C 222      13.116 -41.431  46.717  1.00 22.93           N  
ATOM   4335  CE2 TRP C 222      14.444 -41.155  46.528  1.00 24.42           C  
ATOM   4336  CE3 TRP C 222      16.047 -39.444  47.162  1.00 22.25           C  
ATOM   4337  CZ2 TRP C 222      15.409 -41.848  45.790  1.00 23.77           C  
ATOM   4338  CZ3 TRP C 222      17.001 -40.154  46.461  1.00 23.36           C  
ATOM   4339  CH2 TRP C 222      16.672 -41.341  45.778  1.00 23.93           C  
ATOM   4340  N   ARG C 223      14.163 -35.768  47.228  1.00 21.64           N  
ATOM   4341  CA  ARG C 223      14.938 -35.140  46.174  1.00 22.75           C  
ATOM   4342  C   ARG C 223      16.421 -35.179  46.485  1.00 24.16           C  
ATOM   4343  O   ARG C 223      16.822 -35.286  47.657  1.00 22.67           O  
ATOM   4344  CB  ARG C 223      14.547 -33.662  46.059  1.00 24.16           C  
ATOM   4345  CG  ARG C 223      13.076 -33.353  46.286  1.00 37.95           C  
ATOM   4346  CD  ARG C 223      12.891 -31.856  46.388  1.00 53.33           C  
ATOM   4347  NE  ARG C 223      11.682 -31.407  45.723  1.00 79.44           N  
ATOM   4348  CZ  ARG C 223      11.228 -30.161  45.791  1.00103.53           C  
ATOM   4349  NH1 ARG C 223      11.903 -29.249  46.487  1.00 90.14           N  
ATOM   4350  NH2 ARG C 223      10.103 -29.825  45.166  1.00 94.72           N  
ATOM   4351  N   PHE C 224      17.222 -34.981  45.440  1.00 19.12           N  
ATOM   4352  CA  PHE C 224      18.681 -34.817  45.578  1.00 18.26           C  
ATOM   4353  C   PHE C 224      19.176 -34.084  44.310  1.00 22.81           C  
ATOM   4354  O   PHE C 224      18.458 -34.032  43.318  1.00 22.07           O  
ATOM   4355  CB  PHE C 224      19.379 -36.176  45.766  1.00 18.06           C  
ATOM   4356  CG  PHE C 224      19.488 -36.993  44.498  1.00 19.74           C  
ATOM   4357  CD1 PHE C 224      20.619 -36.899  43.677  1.00 21.54           C  
ATOM   4358  CD2 PHE C 224      18.507 -37.934  44.169  1.00 20.58           C  
ATOM   4359  CE1 PHE C 224      20.740 -37.697  42.546  1.00 21.86           C  
ATOM   4360  CE2 PHE C 224      18.635 -38.731  43.067  1.00 23.09           C  
ATOM   4361  CZ  PHE C 224      19.751 -38.622  42.253  1.00 21.84           C  
ATOM   4362  N   SER C 225      20.354 -33.478  44.374  1.00 18.52           N  
ATOM   4363  CA  SER C 225      20.981 -32.868  43.200  1.00 18.56           C  
ATOM   4364  C   SER C 225      22.358 -33.534  42.986  1.00 24.34           C  
ATOM   4365  O   SER C 225      22.925 -34.160  43.893  1.00 22.87           O  
ATOM   4366  CB  SER C 225      21.121 -31.329  43.318  1.00 20.58           C  
ATOM   4367  OG  SER C 225      22.043 -30.944  44.327  1.00 24.57           O  
ATOM   4368  N   HIS C 226      22.837 -33.494  41.754  1.00 23.09           N  
ATOM   4369  CA  HIS C 226      24.141 -34.038  41.457  1.00 22.87           C  
ATOM   4370  C   HIS C 226      24.891 -33.095  40.551  1.00 25.27           C  
ATOM   4371  O   HIS C 226      24.316 -32.597  39.578  1.00 25.73           O  
ATOM   4372  CB  HIS C 226      24.115 -35.539  41.093  1.00 23.97           C  
ATOM   4373  CG  HIS C 226      24.051 -35.854  39.631  1.00 27.32           C  
ATOM   4374  ND1 HIS C 226      25.140 -36.357  38.936  1.00 28.10           N  
ATOM   4375  CD2 HIS C 226      22.989 -35.950  38.787  1.00 28.94           C  
ATOM   4376  CE1 HIS C 226      24.779 -36.624  37.695  1.00 27.13           C  
ATOM   4377  NE2 HIS C 226      23.478 -36.398  37.578  1.00 28.08           N  
ATOM   4378  N   GLY C 227      26.078 -32.677  40.998  1.00 18.37           N  
ATOM   4379  CA  GLY C 227      26.895 -31.713  40.268  1.00 17.73           C  
ATOM   4380  C   GLY C 227      27.980 -32.466  39.465  1.00 21.68           C  
ATOM   4381  O   GLY C 227      28.375 -33.576  39.813  1.00 21.00           O  
ATOM   4382  N   GLY C 228      28.463 -31.842  38.407  1.00 16.64           N  
ATOM   4383  CA  GLY C 228      29.448 -32.462  37.548  1.00 17.08           C  
ATOM   4384  C   GLY C 228      30.358 -31.342  37.072  1.00 21.05           C  
ATOM   4385  O   GLY C 228      29.885 -30.262  36.749  1.00 20.13           O  
ATOM   4386  N   SER C 229      31.661 -31.584  37.129  1.00 16.43           N  
ATOM   4387  CA  SER C 229      32.647 -30.598  36.699  1.00 14.94           C  
ATOM   4388  C   SER C 229      32.860 -30.608  35.177  1.00 18.41           C  
ATOM   4389  O   SER C 229      33.642 -29.808  34.676  1.00 19.98           O  
ATOM   4390  CB  SER C 229      33.975 -30.828  37.449  1.00 16.84           C  
ATOM   4391  OG  SER C 229      34.641 -32.005  36.988  1.00 18.12           O  
ATOM   4392  N   GLY C 230      32.137 -31.453  34.425  1.00 15.38           N  
ATOM   4393  CA  GLY C 230      32.256 -31.404  32.962  1.00 14.01           C  
ATOM   4394  C   GLY C 230      32.445 -32.723  32.227  1.00 21.58           C  
ATOM   4395  O   GLY C 230      32.225 -32.790  31.010  1.00 22.31           O  
ATOM   4396  N   MET C 231      32.853 -33.767  32.951  1.00 18.01           N  
ATOM   4397  CA  MET C 231      33.004 -35.092  32.360  1.00 17.27           C  
ATOM   4398  C   MET C 231      31.736 -35.925  32.529  1.00 20.76           C  
ATOM   4399  O   MET C 231      31.609 -36.990  31.929  1.00 21.31           O  
ATOM   4400  CB  MET C 231      34.163 -35.838  33.030  1.00 19.34           C  
ATOM   4401  CG  MET C 231      35.505 -35.097  32.976  1.00 22.84           C  
ATOM   4402  SD  MET C 231      36.847 -36.212  33.482  1.00 26.03           S  
ATOM   4403  CE  MET C 231      36.533 -36.321  35.260  1.00 20.47           C  
ATOM   4404  N   VAL C 232      30.827 -35.495  33.399  1.00 17.38           N  
ATOM   4405  CA  VAL C 232      29.593 -36.265  33.653  1.00 16.91           C  
ATOM   4406  C   VAL C 232      28.647 -36.137  32.464  1.00 21.44           C  
ATOM   4407  O   VAL C 232      27.954 -35.132  32.322  1.00 22.15           O  
ATOM   4408  CB  VAL C 232      28.921 -35.839  34.998  1.00 19.50           C  
ATOM   4409  CG1 VAL C 232      27.767 -36.741  35.345  1.00 17.91           C  
ATOM   4410  CG2 VAL C 232      29.950 -35.843  36.127  1.00 19.86           C  
ATOM   4411  N   ASP C 233      28.658 -37.125  31.568  1.00 16.29           N  
ATOM   4412  CA  ASP C 233      27.815 -37.025  30.348  1.00 14.80           C  
ATOM   4413  C   ASP C 233      26.326 -36.815  30.607  1.00 19.60           C  
ATOM   4414  O   ASP C 233      25.638 -36.179  29.801  1.00 18.57           O  
ATOM   4415  CB  ASP C 233      28.057 -38.176  29.387  1.00 14.69           C  
ATOM   4416  CG  ASP C 233      29.504 -38.636  29.393  1.00 16.53           C  
ATOM   4417  OD1 ASP C 233      30.328 -38.075  28.634  1.00 20.27           O  
ATOM   4418  OD2 ASP C 233      29.815 -39.539  30.190  1.00 18.23           O  
ATOM   4419  N   SER C 234      25.832 -37.353  31.723  1.00 15.33           N  
ATOM   4420  CA  SER C 234      24.426 -37.208  32.087  1.00 14.66           C  
ATOM   4421  C   SER C 234      24.081 -35.730  32.177  1.00 21.91           C  
ATOM   4422  O   SER C 234      22.947 -35.336  32.001  1.00 23.66           O  
ATOM   4423  CB  SER C 234      24.197 -37.807  33.466  1.00 17.90           C  
ATOM   4424  OG  SER C 234      24.006 -39.190  33.358  1.00 30.48           O  
ATOM   4425  N   ILE C 235      25.063 -34.907  32.526  1.00 19.01           N  
ATOM   4426  CA  ILE C 235      24.834 -33.484  32.671  1.00 17.71           C  
ATOM   4427  C   ILE C 235      25.256 -32.740  31.400  1.00 22.98           C  
ATOM   4428  O   ILE C 235      24.498 -31.946  30.853  1.00 22.77           O  
ATOM   4429  CB  ILE C 235      25.572 -32.916  33.902  1.00 19.42           C  
ATOM   4430  CG1 ILE C 235      24.976 -33.499  35.194  1.00 20.31           C  
ATOM   4431  CG2 ILE C 235      25.508 -31.398  33.889  1.00 17.68           C  
ATOM   4432  CD1 ILE C 235      25.762 -33.173  36.432  1.00 23.63           C  
ATOM   4433  N   SER C 236      26.490 -32.933  30.977  1.00 19.71           N  
ATOM   4434  CA  SER C 236      27.000 -32.189  29.828  1.00 20.60           C  
ATOM   4435  C   SER C 236      26.370 -32.514  28.489  1.00 25.12           C  
ATOM   4436  O   SER C 236      26.500 -31.730  27.571  1.00 26.84           O  
ATOM   4437  CB  SER C 236      28.495 -32.353  29.707  1.00 20.48           C  
ATOM   4438  OG  SER C 236      28.705 -33.680  29.338  1.00 25.09           O  
ATOM   4439  N   ARG C 237      25.730 -33.672  28.363  1.00 19.84           N  
ATOM   4440  CA  ARG C 237      25.142 -34.079  27.084  1.00 19.17           C  
ATOM   4441  C   ARG C 237      23.701 -34.533  27.264  1.00 20.79           C  
ATOM   4442  O   ARG C 237      23.194 -35.399  26.552  1.00 19.13           O  
ATOM   4443  CB  ARG C 237      25.997 -35.163  26.428  1.00 18.21           C  
ATOM   4444  CG  ARG C 237      27.419 -34.642  26.200  1.00 24.56           C  
ATOM   4445  CD  ARG C 237      28.366 -35.741  25.805  1.00 19.82           C  
ATOM   4446  NE  ARG C 237      28.125 -36.197  24.436  1.00 22.16           N  
ATOM   4447  CZ  ARG C 237      28.862 -37.131  23.845  1.00 31.29           C  
ATOM   4448  NH1 ARG C 237      29.906 -37.637  24.492  1.00 18.16           N  
ATOM   4449  NH2 ARG C 237      28.591 -37.545  22.608  1.00 20.15           N  
ATOM   4450  N   TRP C 238      23.057 -33.854  28.189  1.00 17.20           N  
ATOM   4451  CA  TRP C 238      21.678 -34.038  28.556  1.00 18.63           C  
ATOM   4452  C   TRP C 238      20.726 -34.213  27.356  1.00 22.15           C  
ATOM   4453  O   TRP C 238      19.901 -35.104  27.351  1.00 21.43           O  
ATOM   4454  CB  TRP C 238      21.247 -32.804  29.398  1.00 17.72           C  
ATOM   4455  CG  TRP C 238      19.802 -32.750  29.734  1.00 18.88           C  
ATOM   4456  CD1 TRP C 238      18.874 -31.839  29.274  1.00 21.71           C  
ATOM   4457  CD2 TRP C 238      19.105 -33.590  30.677  1.00 18.94           C  
ATOM   4458  NE1 TRP C 238      17.640 -32.098  29.827  1.00 20.76           N  
ATOM   4459  CE2 TRP C 238      17.754 -33.139  30.717  1.00 22.15           C  
ATOM   4460  CE3 TRP C 238      19.503 -34.643  31.534  1.00 19.45           C  
ATOM   4461  CZ2 TRP C 238      16.790 -33.724  31.560  1.00 21.34           C  
ATOM   4462  CZ3 TRP C 238      18.558 -35.224  32.357  1.00 20.51           C  
ATOM   4463  CH2 TRP C 238      17.207 -34.763  32.374  1.00 21.23           C  
ATOM   4464  N   ALA C 239      20.783 -33.333  26.374  1.00 18.95           N  
ATOM   4465  CA  ALA C 239      19.859 -33.471  25.235  1.00 19.78           C  
ATOM   4466  C   ALA C 239      20.240 -34.636  24.324  1.00 24.93           C  
ATOM   4467  O   ALA C 239      19.399 -35.449  23.937  1.00 25.11           O  
ATOM   4468  CB  ALA C 239      19.787 -32.159  24.421  1.00 19.42           C  
ATOM   4469  N   GLU C 240      21.522 -34.691  23.970  1.00 20.92           N  
ATOM   4470  CA  GLU C 240      22.034 -35.709  23.081  1.00 18.22           C  
ATOM   4471  C   GLU C 240      21.813 -37.153  23.563  1.00 23.63           C  
ATOM   4472  O   GLU C 240      21.649 -38.054  22.739  1.00 24.32           O  
ATOM   4473  CB  GLU C 240      23.516 -35.419  22.802  1.00 18.30           C  
ATOM   4474  CG  GLU C 240      24.175 -36.407  21.833  1.00 23.31           C  
ATOM   4475  CD  GLU C 240      25.677 -36.174  21.684  1.00 34.27           C  
ATOM   4476  OE1 GLU C 240      26.224 -35.293  22.379  1.00 26.56           O  
ATOM   4477  OE2 GLU C 240      26.309 -36.850  20.849  1.00 29.75           O  
ATOM   4478  N   LEU C 241      21.853 -37.391  24.879  1.00 18.98           N  
ATOM   4479  CA  LEU C 241      21.713 -38.761  25.402  1.00 19.07           C  
ATOM   4480  C   LEU C 241      20.275 -39.342  25.328  1.00 24.00           C  
ATOM   4481  O   LEU C 241      20.053 -40.521  25.590  1.00 22.16           O  
ATOM   4482  CB  LEU C 241      22.275 -38.868  26.840  1.00 18.29           C  
ATOM   4483  CG  LEU C 241      21.577 -38.020  27.926  1.00 21.19           C  
ATOM   4484  CD1 LEU C 241      20.253 -38.658  28.385  1.00 20.47           C  
ATOM   4485  CD2 LEU C 241      22.492 -37.775  29.153  1.00 21.57           C  
ATOM   4486  N   PHE C 242      19.304 -38.493  24.989  1.00 22.39           N  
ATOM   4487  CA  PHE C 242      17.899 -38.905  24.852  1.00 21.82           C  
ATOM   4488  C   PHE C 242      17.373 -38.346  23.521  1.00 25.73           C  
ATOM   4489  O   PHE C 242      16.666 -37.328  23.474  1.00 24.58           O  
ATOM   4490  CB  PHE C 242      17.100 -38.306  26.010  1.00 23.55           C  
ATOM   4491  CG  PHE C 242      15.634 -38.640  25.983  1.00 24.75           C  
ATOM   4492  CD1 PHE C 242      15.208 -39.959  25.846  1.00 27.03           C  
ATOM   4493  CD2 PHE C 242      14.680 -37.639  26.103  1.00 25.81           C  
ATOM   4494  CE1 PHE C 242      13.871 -40.275  25.797  1.00 26.84           C  
ATOM   4495  CE2 PHE C 242      13.320 -37.961  26.104  1.00 27.86           C  
ATOM   4496  CZ  PHE C 242      12.923 -39.288  25.955  1.00 25.60           C  
ATOM   4497  N   PRO C 243      17.777 -38.960  22.423  1.00 21.36           N  
ATOM   4498  CA  PRO C 243      17.357 -38.479  21.086  1.00 21.14           C  
ATOM   4499  C   PRO C 243      15.901 -38.943  20.726  1.00 26.62           C  
ATOM   4500  O   PRO C 243      15.693 -39.638  19.721  1.00 24.88           O  
ATOM   4501  CB  PRO C 243      18.382 -39.155  20.159  1.00 22.14           C  
ATOM   4502  CG  PRO C 243      18.673 -40.479  20.857  1.00 25.79           C  
ATOM   4503  CD  PRO C 243      18.589 -40.185  22.358  1.00 20.85           C  
ATOM   4504  N   SER C 244      14.919 -38.561  21.548  1.00 23.57           N  
ATOM   4505  CA  SER C 244      13.528 -38.955  21.346  1.00 24.62           C  
ATOM   4506  C   SER C 244      12.981 -38.506  19.991  1.00 30.65           C  
ATOM   4507  O   SER C 244      12.252 -39.240  19.345  1.00 32.51           O  
ATOM   4508  CB  SER C 244      12.630 -38.465  22.502  1.00 27.51           C  
ATOM   4509  OG  SER C 244      12.631 -37.044  22.610  1.00 33.41           O  
ATOM   4510  N   ASP C 245      13.422 -37.350  19.519  1.00 26.78           N  
ATOM   4511  CA  ASP C 245      13.023 -36.821  18.227  1.00 27.71           C  
ATOM   4512  C   ASP C 245      13.475 -37.613  17.026  1.00 32.35           C  
ATOM   4513  O   ASP C 245      13.001 -37.375  15.945  1.00 33.65           O  
ATOM   4514  CB  ASP C 245      13.518 -35.382  18.078  1.00 30.72           C  
ATOM   4515  N   LYS C 246      14.433 -38.515  17.183  1.00 27.65           N  
ATOM   4516  CA  LYS C 246      14.900 -39.293  16.041  1.00 25.76           C  
ATOM   4517  C   LYS C 246      14.367 -40.710  16.108  1.00 28.95           C  
ATOM   4518  O   LYS C 246      14.676 -41.544  15.269  1.00 29.00           O  
ATOM   4519  CB  LYS C 246      16.430 -39.293  16.023  1.00 28.64           C  
ATOM   4520  CG  LYS C 246      17.033 -37.928  15.683  1.00 39.87           C  
ATOM   4521  CD  LYS C 246      18.420 -37.769  16.284  1.00 47.01           C  
ATOM   4522  N   LEU C 247      13.611 -41.013  17.155  1.00 25.51           N  
ATOM   4523  CA  LEU C 247      13.123 -42.363  17.316  1.00 23.28           C  
ATOM   4524  C   LEU C 247      11.841 -42.570  16.513  1.00 31.11           C  
ATOM   4525  O   LEU C 247      10.759 -42.474  17.042  1.00 30.04           O  
ATOM   4526  CB  LEU C 247      12.966 -42.717  18.783  1.00 21.52           C  
ATOM   4527  CG  LEU C 247      12.731 -44.199  19.060  1.00 24.74           C  
ATOM   4528  CD1 LEU C 247      14.016 -45.020  19.028  1.00 24.98           C  
ATOM   4529  CD2 LEU C 247      11.941 -44.401  20.335  1.00 25.27           C  
ATOM   4530  N   ASN C 248      11.986 -42.850  15.220  1.00 31.01           N  
ATOM   4531  CA  ASN C 248      10.831 -43.088  14.340  1.00 32.57           C  
ATOM   4532  C   ASN C 248      10.356 -44.558  14.340  1.00 37.98           C  
ATOM   4533  O   ASN C 248       9.330 -44.864  13.732  1.00 39.29           O  
ATOM   4534  CB  ASN C 248      11.140 -42.631  12.892  1.00 29.20           C  
ATOM   4535  CG  ASN C 248      12.388 -43.292  12.328  1.00 55.41           C  
ATOM   4536  OD1 ASN C 248      13.376 -43.463  13.025  1.00 43.37           O  
ATOM   4537  ND2 ASN C 248      12.329 -43.694  11.070  1.00 58.74           N  
ATOM   4538  N   ARG C 249      11.112 -45.447  14.992  1.00 31.94           N  
ATOM   4539  CA  ARG C 249      10.761 -46.872  15.123  1.00 30.52           C  
ATOM   4540  C   ARG C 249      11.468 -47.411  16.376  1.00 31.85           C  
ATOM   4541  O   ARG C 249      12.277 -46.714  16.953  1.00 31.01           O  
ATOM   4542  CB  ARG C 249      11.207 -47.675  13.888  1.00 26.62           C  
ATOM   4543  CG  ARG C 249      12.513 -47.171  13.329  1.00 35.21           C  
ATOM   4544  CD  ARG C 249      13.078 -48.147  12.352  1.00 41.27           C  
ATOM   4545  NE  ARG C 249      14.366 -47.705  11.835  1.00 42.78           N  
ATOM   4546  CZ  ARG C 249      15.475 -48.433  11.893  1.00 53.68           C  
ATOM   4547  NH1 ARG C 249      15.468 -49.639  12.467  1.00 39.57           N  
ATOM   4548  NH2 ARG C 249      16.597 -47.945  11.390  1.00 38.14           N  
ATOM   4549  N   PRO C 250      11.145 -48.628  16.797  1.00 27.29           N  
ATOM   4550  CA  PRO C 250      11.747 -49.188  18.003  1.00 26.66           C  
ATOM   4551  C   PRO C 250      13.262 -49.375  17.878  1.00 30.81           C  
ATOM   4552  O   PRO C 250      13.763 -49.672  16.808  1.00 30.74           O  
ATOM   4553  CB  PRO C 250      11.055 -50.559  18.145  1.00 28.29           C  
ATOM   4554  CG  PRO C 250       9.800 -50.470  17.304  1.00 32.74           C  
ATOM   4555  CD  PRO C 250      10.189 -49.571  16.160  1.00 28.84           C  
ATOM   4556  N   ALA C 251      13.983 -49.154  18.973  1.00 25.92           N  
ATOM   4557  CA  ALA C 251      15.428 -49.392  19.021  1.00 25.72           C  
ATOM   4558  C   ALA C 251      15.658 -50.426  20.121  1.00 31.44           C  
ATOM   4559  O   ALA C 251      14.792 -50.613  20.984  1.00 30.72           O  
ATOM   4560  CB  ALA C 251      16.219 -48.084  19.325  1.00 25.59           C  
ATOM   4561  N   GLN C 252      16.797 -51.119  20.091  1.00 29.16           N  
ATOM   4562  CA  GLN C 252      17.066 -52.112  21.150  1.00 28.49           C  
ATOM   4563  C   GLN C 252      18.536 -52.455  21.267  1.00 30.70           C  
ATOM   4564  O   GLN C 252      19.290 -52.250  20.320  1.00 30.23           O  
ATOM   4565  CB  GLN C 252      16.248 -53.394  20.937  1.00 29.25           C  
ATOM   4566  CG  GLN C 252      16.638 -54.195  19.715  1.00 40.36           C  
ATOM   4567  N   VAL C 253      18.933 -52.960  22.434  1.00 26.67           N  
ATOM   4568  CA  VAL C 253      20.296 -53.430  22.676  1.00 25.82           C  
ATOM   4569  C   VAL C 253      20.197 -54.684  23.528  1.00 26.71           C  
ATOM   4570  O   VAL C 253      19.416 -54.737  24.491  1.00 25.31           O  
ATOM   4571  CB  VAL C 253      21.207 -52.381  23.447  1.00 29.90           C  
ATOM   4572  CG1 VAL C 253      22.663 -52.754  23.291  1.00 29.22           C  
ATOM   4573  CG2 VAL C 253      21.023 -51.014  22.908  1.00 30.56           C  
ATOM   4574  N   GLU C 254      21.005 -55.678  23.181  1.00 22.81           N  
ATOM   4575  CA  GLU C 254      21.122 -56.892  23.986  1.00 23.50           C  
ATOM   4576  C   GLU C 254      22.602 -56.949  24.273  1.00 27.09           C  
ATOM   4577  O   GLU C 254      23.391 -56.767  23.366  1.00 27.52           O  
ATOM   4578  CB  GLU C 254      20.750 -58.145  23.200  1.00 25.32           C  
ATOM   4579  CG  GLU C 254      19.283 -58.216  22.845  1.00 45.51           C  
ATOM   4580  CD  GLU C 254      18.916 -59.516  22.152  1.00 84.80           C  
ATOM   4581  OE1 GLU C 254      17.957 -60.175  22.611  1.00 97.99           O  
ATOM   4582  OE2 GLU C 254      19.590 -59.881  21.159  1.00 81.42           O  
ATOM   4583  N   ALA C 255      22.978 -57.173  25.524  1.00 23.02           N  
ATOM   4584  CA  ALA C 255      24.401 -57.245  25.900  1.00 22.57           C  
ATOM   4585  C   ALA C 255      24.537 -58.236  27.072  1.00 28.43           C  
ATOM   4586  O   ALA C 255      23.581 -58.496  27.784  1.00 29.77           O  
ATOM   4587  CB  ALA C 255      24.903 -55.858  26.295  1.00 22.36           C  
ATOM   4588  N   GLY C 256      25.707 -58.829  27.247  1.00 24.09           N  
ATOM   4589  CA  GLY C 256      25.891 -59.760  28.350  1.00 23.19           C  
ATOM   4590  C   GLY C 256      27.372 -60.073  28.508  1.00 26.29           C  
ATOM   4591  O   GLY C 256      28.138 -59.899  27.559  1.00 26.08           O  
ATOM   4592  N   PHE C 257      27.762 -60.526  29.708  1.00 19.62           N  
ATOM   4593  CA  PHE C 257      29.134 -60.954  29.950  1.00 17.82           C  
ATOM   4594  C   PHE C 257      29.117 -62.198  30.842  1.00 22.02           C  
ATOM   4595  O   PHE C 257      28.163 -62.427  31.626  1.00 21.21           O  
ATOM   4596  CB  PHE C 257      30.017 -59.825  30.560  1.00 18.90           C  
ATOM   4597  CG  PHE C 257      29.615 -59.403  31.974  1.00 18.81           C  
ATOM   4598  CD1 PHE C 257      30.004 -60.155  33.085  1.00 21.32           C  
ATOM   4599  CD2 PHE C 257      28.866 -58.249  32.181  1.00 18.89           C  
ATOM   4600  CE1 PHE C 257      29.634 -59.770  34.394  1.00 22.49           C  
ATOM   4601  CE2 PHE C 257      28.471 -57.857  33.476  1.00 22.60           C  
ATOM   4602  CZ  PHE C 257      28.859 -58.613  34.584  1.00 21.57           C  
ATOM   4603  N   ARG C 258      30.176 -62.989  30.722  1.00 18.97           N  
ATOM   4604  CA  ARG C 258      30.366 -64.176  31.551  1.00 19.67           C  
ATOM   4605  C   ARG C 258      31.756 -63.968  32.129  1.00 23.50           C  
ATOM   4606  O   ARG C 258      32.652 -63.538  31.418  1.00 22.89           O  
ATOM   4607  CB  ARG C 258      30.400 -65.432  30.675  1.00 20.71           C  
ATOM   4608  CG  ARG C 258      29.105 -65.747  29.979  1.00 31.40           C  
ATOM   4609  CD  ARG C 258      27.955 -65.895  30.965  1.00 40.46           C  
ATOM   4610  NE  ARG C 258      26.678 -66.106  30.275  1.00 48.79           N  
ATOM   4611  CZ  ARG C 258      25.808 -65.144  29.970  1.00 57.02           C  
ATOM   4612  NH1 ARG C 258      26.048 -63.881  30.292  1.00 32.61           N  
ATOM   4613  NH2 ARG C 258      24.683 -65.451  29.341  1.00 48.47           N  
ATOM   4614  N   SER C 259      31.930 -64.192  33.419  1.00 20.72           N  
ATOM   4615  CA  SER C 259      33.246 -63.996  33.999  1.00 19.95           C  
ATOM   4616  C   SER C 259      33.508 -64.875  35.204  1.00 24.23           C  
ATOM   4617  O   SER C 259      32.608 -65.218  35.963  1.00 23.86           O  
ATOM   4618  CB  SER C 259      33.484 -62.524  34.324  1.00 21.23           C  
ATOM   4619  OG  SER C 259      32.853 -62.143  35.526  1.00 18.90           O  
ATOM   4620  N   ASP C 260      34.768 -65.238  35.357  1.00 20.84           N  
ATOM   4621  CA  ASP C 260      35.217 -66.002  36.498  1.00 19.76           C  
ATOM   4622  C   ASP C 260      36.701 -65.717  36.689  1.00 23.30           C  
ATOM   4623  O   ASP C 260      37.224 -64.764  36.093  1.00 22.79           O  
ATOM   4624  CB  ASP C 260      34.929 -67.506  36.313  1.00 21.79           C  
ATOM   4625  CG  ASP C 260      35.601 -68.104  35.100  1.00 26.83           C  
ATOM   4626  OD1 ASP C 260      36.561 -67.543  34.525  1.00 29.15           O  
ATOM   4627  OD2 ASP C 260      35.173 -69.200  34.730  1.00 39.68           O  
ATOM   4628  N   SER C 261      37.358 -66.517  37.523  1.00 20.91           N  
ATOM   4629  CA  SER C 261      38.771 -66.352  37.844  1.00 21.77           C  
ATOM   4630  C   SER C 261      39.681 -66.479  36.624  1.00 26.45           C  
ATOM   4631  O   SER C 261      40.835 -66.106  36.658  1.00 26.87           O  
ATOM   4632  CB  SER C 261      39.217 -67.333  38.952  1.00 23.46           C  
ATOM   4633  OG  SER C 261      39.406 -68.648  38.444  1.00 37.77           O  
ATOM   4634  N   GLN C 262      39.168 -67.001  35.536  1.00 23.40           N  
ATOM   4635  CA  GLN C 262      40.015 -67.158  34.348  1.00 23.70           C  
ATOM   4636  C   GLN C 262      39.909 -66.001  33.329  1.00 30.46           C  
ATOM   4637  O   GLN C 262      40.818 -65.778  32.517  1.00 32.13           O  
ATOM   4638  CB  GLN C 262      39.663 -68.474  33.627  1.00 24.43           C  
ATOM   4639  CG  GLN C 262      39.791 -69.728  34.477  1.00 46.81           C  
ATOM   4640  CD  GLN C 262      41.234 -70.144  34.673  1.00 74.99           C  
ATOM   4641  OE1 GLN C 262      41.874 -69.756  35.656  1.00 80.18           O  
ATOM   4642  NE2 GLN C 262      41.765 -70.908  33.724  1.00 53.39           N  
ATOM   4643  N   GLY C 263      38.772 -65.315  33.279  1.00 25.52           N  
ATOM   4644  CA  GLY C 263      38.648 -64.291  32.260  1.00 23.74           C  
ATOM   4645  C   GLY C 263      37.268 -63.692  32.140  1.00 24.65           C  
ATOM   4646  O   GLY C 263      36.363 -63.981  32.936  1.00 22.03           O  
ATOM   4647  N   ILE C 264      37.122 -62.848  31.125  1.00 21.67           N  
ATOM   4648  CA  ILE C 264      35.883 -62.119  30.900  1.00 21.73           C  
ATOM   4649  C   ILE C 264      35.515 -62.266  29.457  1.00 25.80           C  
ATOM   4650  O   ILE C 264      36.377 -62.150  28.589  1.00 25.71           O  
ATOM   4651  CB  ILE C 264      36.054 -60.594  31.215  1.00 24.11           C  
ATOM   4652  CG1 ILE C 264      36.467 -60.375  32.680  1.00 24.21           C  
ATOM   4653  CG2 ILE C 264      34.787 -59.840  30.885  1.00 21.11           C  
ATOM   4654  CD1 ILE C 264      37.201 -59.062  32.918  1.00 27.49           C  
ATOM   4655  N   GLU C 265      34.232 -62.461  29.183  1.00 21.19           N  
ATOM   4656  CA  GLU C 265      33.791 -62.551  27.795  1.00 20.91           C  
ATOM   4657  C   GLU C 265      32.553 -61.687  27.653  1.00 23.39           C  
ATOM   4658  O   GLU C 265      31.652 -61.734  28.490  1.00 22.49           O  
ATOM   4659  CB  GLU C 265      33.433 -63.973  27.469  1.00 22.51           C  
ATOM   4660  CG  GLU C 265      33.539 -64.309  26.030  1.00 44.75           C  
ATOM   4661  CD  GLU C 265      33.043 -65.706  25.788  1.00 76.53           C  
ATOM   4662  OE1 GLU C 265      33.211 -66.549  26.711  1.00 56.14           O  
ATOM   4663  OE2 GLU C 265      32.397 -65.918  24.737  1.00 75.28           O  
ATOM   4664  N   VAL C 266      32.510 -60.870  26.617  1.00 19.54           N  
ATOM   4665  CA  VAL C 266      31.404 -59.957  26.498  1.00 19.73           C  
ATOM   4666  C   VAL C 266      30.860 -59.887  25.092  1.00 24.15           C  
ATOM   4667  O   VAL C 266      31.582 -60.119  24.126  1.00 23.79           O  
ATOM   4668  CB  VAL C 266      31.753 -58.548  27.139  1.00 24.26           C  
ATOM   4669  CG1 VAL C 266      33.136 -58.090  26.745  1.00 24.94           C  
ATOM   4670  CG2 VAL C 266      30.712 -57.464  26.793  1.00 23.04           C  
ATOM   4671  N   LYS C 267      29.558 -59.640  24.987  1.00 21.39           N  
ATOM   4672  CA  LYS C 267      28.905 -59.499  23.674  1.00 21.56           C  
ATOM   4673  C   LYS C 267      27.833 -58.412  23.679  1.00 24.35           C  
ATOM   4674  O   LYS C 267      27.101 -58.240  24.658  1.00 24.96           O  
ATOM   4675  CB  LYS C 267      28.430 -60.847  23.092  1.00 24.67           C  
ATOM   4676  CG  LYS C 267      27.103 -61.339  23.597  1.00 44.90           C  
ATOM   4677  CD  LYS C 267      26.706 -62.657  22.925  1.00 48.96           C  
ATOM   4678  N   VAL C 268      27.809 -57.610  22.624  1.00 19.05           N  
ATOM   4679  CA  VAL C 268      26.841 -56.530  22.529  1.00 18.48           C  
ATOM   4680  C   VAL C 268      26.261 -56.537  21.124  1.00 25.45           C  
ATOM   4681  O   VAL C 268      26.983 -56.730  20.147  1.00 26.22           O  
ATOM   4682  CB  VAL C 268      27.510 -55.129  22.797  1.00 21.71           C  
ATOM   4683  CG1 VAL C 268      26.574 -53.993  22.399  1.00 20.28           C  
ATOM   4684  CG2 VAL C 268      27.960 -54.975  24.256  1.00 22.00           C  
ATOM   4685  N   ASP C 269      24.979 -56.213  21.009  1.00 21.18           N  
ATOM   4686  CA  ASP C 269      24.328 -56.098  19.707  1.00 20.96           C  
ATOM   4687  C   ASP C 269      23.188 -55.148  19.881  1.00 22.94           C  
ATOM   4688  O   ASP C 269      22.310 -55.384  20.723  1.00 22.60           O  
ATOM   4689  CB  ASP C 269      23.713 -57.429  19.276  1.00 24.22           C  
ATOM   4690  CG  ASP C 269      24.723 -58.363  18.737  1.00 47.14           C  
ATOM   4691  OD1 ASP C 269      25.299 -58.036  17.679  1.00 51.55           O  
ATOM   4692  OD2 ASP C 269      25.009 -59.378  19.410  1.00 57.44           O  
ATOM   4693  N   GLY C 270      23.150 -54.097  19.074  1.00 19.33           N  
ATOM   4694  CA  GLY C 270      22.052 -53.145  19.195  1.00 19.89           C  
ATOM   4695  C   GLY C 270      21.914 -52.276  17.973  1.00 26.37           C  
ATOM   4696  O   GLY C 270      22.764 -52.276  17.087  1.00 25.43           O  
ATOM   4697  N   GLU C 271      20.809 -51.551  17.941  1.00 23.80           N  
ATOM   4698  CA  GLU C 271      20.485 -50.636  16.858  1.00 23.60           C  
ATOM   4699  C   GLU C 271      19.662 -49.501  17.471  1.00 25.94           C  
ATOM   4700  O   GLU C 271      18.626 -49.732  18.080  1.00 25.04           O  
ATOM   4701  CB  GLU C 271      19.640 -51.329  15.786  1.00 24.33           C  
ATOM   4702  CG  GLU C 271      19.418 -50.407  14.611  1.00 32.03           C  
ATOM   4703  CD  GLU C 271      18.535 -50.995  13.528  1.00 42.19           C  
ATOM   4704  OE1 GLU C 271      17.943 -52.066  13.734  1.00 50.42           O  
ATOM   4705  OE2 GLU C 271      18.378 -50.335  12.492  1.00 39.83           O  
ATOM   4706  N   PHE C 272      20.114 -48.272  17.296  1.00 22.75           N  
ATOM   4707  CA  PHE C 272      19.401 -47.122  17.866  1.00 21.86           C  
ATOM   4708  C   PHE C 272      19.892 -45.884  17.147  1.00 23.51           C  
ATOM   4709  O   PHE C 272      20.874 -45.932  16.432  1.00 22.43           O  
ATOM   4710  CB  PHE C 272      19.722 -47.002  19.382  1.00 23.31           C  
ATOM   4711  CG  PHE C 272      21.162 -47.310  19.711  1.00 24.23           C  
ATOM   4712  CD1 PHE C 272      22.134 -46.343  19.562  1.00 27.05           C  
ATOM   4713  CD2 PHE C 272      21.555 -48.594  20.033  1.00 26.15           C  
ATOM   4714  CE1 PHE C 272      23.496 -46.641  19.767  1.00 28.32           C  
ATOM   4715  CE2 PHE C 272      22.900 -48.897  20.256  1.00 29.62           C  
ATOM   4716  CZ  PHE C 272      23.870 -47.920  20.093  1.00 27.92           C  
ATOM   4717  N   PRO C 273      19.192 -44.777  17.330  1.00 22.31           N  
ATOM   4718  CA  PRO C 273      19.607 -43.496  16.743  1.00 22.77           C  
ATOM   4719  C   PRO C 273      20.649 -42.811  17.648  1.00 29.36           C  
ATOM   4720  O   PRO C 273      20.847 -43.200  18.800  1.00 27.87           O  
ATOM   4721  CB  PRO C 273      18.315 -42.682  16.783  1.00 23.25           C  
ATOM   4722  CG  PRO C 273      17.602 -43.203  17.962  1.00 26.18           C  
ATOM   4723  CD  PRO C 273      17.860 -44.688  17.951  1.00 22.54           C  
ATOM   4724  N   GLY C 274      21.313 -41.790  17.114  1.00 27.12           N  
ATOM   4725  CA  GLY C 274      22.294 -41.010  17.885  1.00 26.20           C  
ATOM   4726  C   GLY C 274      23.755 -41.417  17.690  1.00 28.50           C  
ATOM   4727  O   GLY C 274      24.644 -40.897  18.365  1.00 28.27           O  
ATOM   4728  N   VAL C 275      24.002 -42.362  16.795  1.00 24.27           N  
ATOM   4729  CA  VAL C 275      25.360 -42.825  16.559  1.00 24.18           C  
ATOM   4730  C   VAL C 275      26.229 -41.808  15.796  1.00 27.67           C  
ATOM   4731  O   VAL C 275      27.441 -41.688  16.039  1.00 25.39           O  
ATOM   4732  CB  VAL C 275      25.372 -44.221  15.928  1.00 29.04           C  
ATOM   4733  CG1 VAL C 275      26.780 -44.714  15.761  1.00 29.49           C  
ATOM   4734  CG2 VAL C 275      24.553 -45.212  16.795  1.00 29.27           C  
ATOM   4735  N   SER C 276      25.600 -41.047  14.904  1.00 23.40           N  
ATOM   4736  CA  SER C 276      26.315 -40.035  14.129  1.00 22.71           C  
ATOM   4737  C   SER C 276      25.621 -38.702  14.342  1.00 28.62           C  
ATOM   4738  O   SER C 276      24.454 -38.676  14.679  1.00 28.22           O  
ATOM   4739  CB  SER C 276      26.366 -40.380  12.643  1.00 23.24           C  
ATOM   4740  OG  SER C 276      25.075 -40.296  12.079  1.00 30.03           O  
ATOM   4741  N   VAL C 277      26.352 -37.603  14.175  1.00 25.74           N  
ATOM   4742  CA  VAL C 277      25.804 -36.306  14.417  1.00 27.33           C  
ATOM   4743  C   VAL C 277      26.387 -35.322  13.422  1.00 33.07           C  
ATOM   4744  O   VAL C 277      27.448 -35.552  12.855  1.00 32.31           O  
ATOM   4745  CB  VAL C 277      26.078 -35.852  15.902  1.00 33.66           C  
ATOM   4746  CG1 VAL C 277      25.738 -36.976  16.888  1.00 34.37           C  
ATOM   4747  CG2 VAL C 277      27.524 -35.454  16.079  1.00 33.12           C  
ATOM   4748  N   ASP C 278      25.640 -34.253  13.177  1.00 32.41           N  
ATOM   4749  CA  ASP C 278      26.049 -33.191  12.283  1.00 33.70           C  
ATOM   4750  C   ASP C 278      27.324 -32.586  12.912  1.00 38.25           C  
ATOM   4751  O   ASP C 278      27.341 -32.259  14.095  1.00 39.58           O  
ATOM   4752  CB  ASP C 278      24.938 -32.138  12.299  1.00 36.18           C  
ATOM   4753  CG  ASP C 278      25.155 -31.011  11.297  1.00 47.93           C  
ATOM   4754  OD1 ASP C 278      26.219 -30.932  10.665  1.00 45.20           O  
ATOM   4755  OD2 ASP C 278      24.209 -30.207  11.132  1.00 62.82           O  
ATOM   4756  N   ALA C 279      28.394 -32.458  12.139  1.00 33.45           N  
ATOM   4757  CA  ALA C 279      29.615 -31.867  12.673  1.00 32.96           C  
ATOM   4758  C   ALA C 279      29.787 -30.447  12.131  1.00 40.73           C  
ATOM   4759  O   ALA C 279      30.759 -29.778  12.462  1.00 41.55           O  
ATOM   4760  CB  ALA C 279      30.818 -32.710  12.317  1.00 32.76           C  
ATOM   4761  N   GLY C 280      28.872 -30.024  11.256  1.00 36.82           N  
ATOM   4762  CA  GLY C 280      28.942 -28.704  10.655  1.00 37.65           C  
ATOM   4763  C   GLY C 280      29.762 -28.768   9.384  1.00 45.01           C  
ATOM   4764  O   GLY C 280      30.544 -29.696   9.198  1.00 45.34           O  
ATOM   4765  N   GLY C 281      29.565 -27.793   8.502  1.00 42.16           N  
ATOM   4766  CA  GLY C 281      30.304 -27.722   7.244  1.00 41.26           C  
ATOM   4767  C   GLY C 281      29.953 -28.802   6.235  1.00 43.37           C  
ATOM   4768  O   GLY C 281      30.707 -29.036   5.304  1.00 43.32           O  
ATOM   4769  N   GLY C 282      28.815 -29.457   6.424  1.00 39.02           N  
ATOM   4770  CA  GLY C 282      28.389 -30.532   5.540  1.00 37.94           C  
ATOM   4771  C   GLY C 282      29.001 -31.859   5.998  1.00 41.24           C  
ATOM   4772  O   GLY C 282      28.775 -32.911   5.373  1.00 41.76           O  
ATOM   4773  N   LEU C 283      29.747 -31.826   7.105  1.00 34.02           N  
ATOM   4774  CA  LEU C 283      30.347 -33.054   7.629  1.00 32.50           C  
ATOM   4775  C   LEU C 283      29.555 -33.710   8.750  1.00 33.00           C  
ATOM   4776  O   LEU C 283      28.862 -33.040   9.520  1.00 32.96           O  
ATOM   4777  CB  LEU C 283      31.755 -32.781   8.150  1.00 32.51           C  
ATOM   4778  CG  LEU C 283      32.841 -32.333   7.166  1.00 36.71           C  
ATOM   4779  CD1 LEU C 283      34.045 -31.855   7.961  1.00 36.55           C  
ATOM   4780  CD2 LEU C 283      33.256 -33.459   6.244  1.00 37.14           C  
ATOM   4781  N   ARG C 284      29.714 -35.016   8.885  1.00 27.06           N  
ATOM   4782  CA  ARG C 284      29.090 -35.742  10.003  1.00 26.62           C  
ATOM   4783  C   ARG C 284      30.229 -36.437  10.790  1.00 29.17           C  
ATOM   4784  O   ARG C 284      31.295 -36.712  10.238  1.00 28.35           O  
ATOM   4785  CB  ARG C 284      28.092 -36.789   9.503  1.00 25.51           C  
ATOM   4786  CG  ARG C 284      26.731 -36.214   9.053  1.00 28.54           C  
ATOM   4787  CD  ARG C 284      25.701 -37.306   8.843  1.00 33.45           C  
ATOM   4788  NE  ARG C 284      25.060 -37.747  10.090  1.00 32.32           N  
ATOM   4789  CZ  ARG C 284      24.135 -37.065  10.752  1.00 35.25           C  
ATOM   4790  NH1 ARG C 284      23.731 -35.890  10.304  1.00 25.06           N  
ATOM   4791  NH2 ARG C 284      23.620 -37.563  11.871  1.00 23.52           N  
ATOM   4792  N   ARG C 285      30.027 -36.692  12.080  1.00 23.55           N  
ATOM   4793  CA  ARG C 285      31.027 -37.433  12.844  1.00 22.19           C  
ATOM   4794  C   ARG C 285      30.309 -38.540  13.602  1.00 24.59           C  
ATOM   4795  O   ARG C 285      29.114 -38.431  13.854  1.00 23.01           O  
ATOM   4796  CB  ARG C 285      31.717 -36.515  13.873  1.00 20.21           C  
ATOM   4797  CG  ARG C 285      30.772 -36.010  14.994  1.00 24.65           C  
ATOM   4798  CD  ARG C 285      31.574 -35.514  16.224  1.00 35.21           C  
ATOM   4799  NE  ARG C 285      32.697 -34.675  15.820  1.00 31.49           N  
ATOM   4800  CZ  ARG C 285      32.608 -33.363  15.706  1.00 38.85           C  
ATOM   4801  NH1 ARG C 285      31.474 -32.763  16.034  1.00 46.32           N  
ATOM   4802  NH2 ARG C 285      33.626 -32.659  15.245  1.00 24.50           N  
ATOM   4803  N   ILE C 286      31.049 -39.571  14.010  1.00 21.55           N  
ATOM   4804  CA  ILE C 286      30.541 -40.591  14.937  1.00 20.36           C  
ATOM   4805  C   ILE C 286      30.510 -39.771  16.231  1.00 21.88           C  
ATOM   4806  O   ILE C 286      31.352 -38.909  16.428  1.00 20.44           O  
ATOM   4807  CB  ILE C 286      31.532 -41.761  15.094  1.00 22.97           C  
ATOM   4808  CG1 ILE C 286      31.821 -42.414  13.746  1.00 23.66           C  
ATOM   4809  CG2 ILE C 286      31.055 -42.751  16.149  1.00 20.14           C  
ATOM   4810  CD1 ILE C 286      30.718 -43.274  13.227  1.00 26.60           C  
ATOM   4811  N   LEU C 287      29.514 -39.946  17.079  1.00 19.58           N  
ATOM   4812  CA  LEU C 287      29.421 -39.075  18.276  1.00 19.00           C  
ATOM   4813  C   LEU C 287      30.672 -39.119  19.178  1.00 23.99           C  
ATOM   4814  O   LEU C 287      31.380 -40.118  19.235  1.00 23.16           O  
ATOM   4815  CB  LEU C 287      28.156 -39.405  19.104  1.00 18.01           C  
ATOM   4816  CG  LEU C 287      28.291 -40.595  20.046  1.00 20.73           C  
ATOM   4817  CD1 LEU C 287      27.093 -40.601  21.000  1.00 21.53           C  
ATOM   4818  CD2 LEU C 287      28.420 -41.891  19.302  1.00 20.51           C  
ATOM   4819  N   ASN C 288      30.948 -38.018  19.865  1.00 20.05           N  
ATOM   4820  CA  ASN C 288      32.083 -37.966  20.774  1.00 20.30           C  
ATOM   4821  C   ASN C 288      31.932 -39.102  21.812  1.00 21.94           C  
ATOM   4822  O   ASN C 288      30.820 -39.372  22.296  1.00 17.90           O  
ATOM   4823  CB  ASN C 288      32.094 -36.607  21.515  1.00 16.32           C  
ATOM   4824  CG  ASN C 288      32.292 -35.431  20.584  1.00 26.35           C  
ATOM   4825  OD1 ASN C 288      33.034 -35.506  19.614  1.00 20.22           O  
ATOM   4826  ND2 ASN C 288      31.687 -34.309  20.926  1.00 13.01           N  
ATOM   4827  N   HIS C 289      33.041 -39.769  22.141  1.00 17.44           N  
ATOM   4828  CA  HIS C 289      32.986 -40.841  23.147  1.00 16.25           C  
ATOM   4829  C   HIS C 289      32.558 -40.285  24.512  1.00 18.95           C  
ATOM   4830  O   HIS C 289      33.104 -39.293  24.932  1.00 16.52           O  
ATOM   4831  CB  HIS C 289      34.335 -41.566  23.269  1.00 16.18           C  
ATOM   4832  CG  HIS C 289      34.201 -42.964  23.802  1.00 18.92           C  
ATOM   4833  ND1 HIS C 289      33.727 -43.228  25.069  1.00 20.12           N  
ATOM   4834  CD2 HIS C 289      34.385 -44.169  23.209  1.00 19.15           C  
ATOM   4835  CE1 HIS C 289      33.659 -44.538  25.243  1.00 18.87           C  
ATOM   4836  NE2 HIS C 289      34.033 -45.130  24.123  1.00 18.86           N  
ATOM   4837  N   PRO C 290      31.561 -40.889  25.180  1.00 17.78           N  
ATOM   4838  CA  PRO C 290      31.168 -40.396  26.527  1.00 16.84           C  
ATOM   4839  C   PRO C 290      32.361 -40.662  27.468  1.00 19.51           C  
ATOM   4840  O   PRO C 290      33.130 -41.628  27.269  1.00 17.65           O  
ATOM   4841  CB  PRO C 290      29.955 -41.283  26.909  1.00 17.53           C  
ATOM   4842  CG  PRO C 290      30.101 -42.506  26.050  1.00 21.66           C  
ATOM   4843  CD  PRO C 290      30.698 -42.010  24.745  1.00 17.47           C  
ATOM   4844  N   LEU C 291      32.571 -39.768  28.426  1.00 16.42           N  
ATOM   4845  CA  LEU C 291      33.737 -39.844  29.312  1.00 15.73           C  
ATOM   4846  C   LEU C 291      33.607 -40.759  30.517  1.00 20.43           C  
ATOM   4847  O   LEU C 291      34.532 -41.477  30.842  1.00 21.07           O  
ATOM   4848  CB  LEU C 291      34.228 -38.443  29.700  1.00 15.34           C  
ATOM   4849  CG  LEU C 291      34.640 -37.521  28.517  1.00 19.24           C  
ATOM   4850  CD1 LEU C 291      35.025 -36.122  28.968  1.00 17.39           C  
ATOM   4851  CD2 LEU C 291      35.711 -38.115  27.641  1.00 19.50           C  
ATOM   4852  N   ILE C 292      32.445 -40.742  31.172  1.00 17.01           N  
ATOM   4853  CA  ILE C 292      32.184 -41.586  32.353  1.00 14.96           C  
ATOM   4854  C   ILE C 292      32.573 -43.059  32.208  1.00 18.57           C  
ATOM   4855  O   ILE C 292      33.332 -43.568  33.020  1.00 18.81           O  
ATOM   4856  CB  ILE C 292      30.718 -41.409  32.875  1.00 17.09           C  
ATOM   4857  CG1 ILE C 292      30.545 -39.989  33.421  1.00 17.32           C  
ATOM   4858  CG2 ILE C 292      30.389 -42.427  33.977  1.00 12.83           C  
ATOM   4859  CD1 ILE C 292      31.472 -39.658  34.573  1.00 19.39           C  
ATOM   4860  N   PRO C 293      32.111 -43.731  31.149  1.00 17.60           N  
ATOM   4861  CA  PRO C 293      32.457 -45.135  30.939  1.00 16.26           C  
ATOM   4862  C   PRO C 293      33.965 -45.354  30.902  1.00 18.77           C  
ATOM   4863  O   PRO C 293      34.470 -46.346  31.424  1.00 18.93           O  
ATOM   4864  CB  PRO C 293      31.849 -45.449  29.553  1.00 17.67           C  
ATOM   4865  CG  PRO C 293      30.839 -44.448  29.317  1.00 22.13           C  
ATOM   4866  CD  PRO C 293      31.275 -43.216  30.040  1.00 19.00           C  
ATOM   4867  N   LEU C 294      34.698 -44.446  30.264  1.00 15.36           N  
ATOM   4868  CA  LEU C 294      36.138 -44.645  30.141  1.00 15.83           C  
ATOM   4869  C   LEU C 294      36.850 -44.430  31.484  1.00 18.71           C  
ATOM   4870  O   LEU C 294      37.765 -45.172  31.865  1.00 18.59           O  
ATOM   4871  CB  LEU C 294      36.727 -43.747  29.044  1.00 15.38           C  
ATOM   4872  CG  LEU C 294      36.230 -43.998  27.625  1.00 18.94           C  
ATOM   4873  CD1 LEU C 294      36.935 -43.015  26.637  1.00 17.77           C  
ATOM   4874  CD2 LEU C 294      36.428 -45.456  27.222  1.00 16.68           C  
ATOM   4875  N   VAL C 295      36.407 -43.409  32.193  1.00 15.30           N  
ATOM   4876  CA  VAL C 295      36.972 -43.096  33.496  1.00 16.43           C  
ATOM   4877  C   VAL C 295      36.635 -44.211  34.530  1.00 19.51           C  
ATOM   4878  O   VAL C 295      37.498 -44.631  35.309  1.00 18.98           O  
ATOM   4879  CB  VAL C 295      36.478 -41.696  33.965  1.00 21.42           C  
ATOM   4880  CG1 VAL C 295      36.912 -41.429  35.415  1.00 21.11           C  
ATOM   4881  CG2 VAL C 295      36.993 -40.602  33.009  1.00 20.88           C  
ATOM   4882  N   HIS C 296      35.378 -44.657  34.552  1.00 14.41           N  
ATOM   4883  CA  HIS C 296      34.972 -45.697  35.491  1.00 14.09           C  
ATOM   4884  C   HIS C 296      35.627 -47.055  35.163  1.00 18.81           C  
ATOM   4885  O   HIS C 296      36.134 -47.745  36.063  1.00 19.04           O  
ATOM   4886  CB  HIS C 296      33.452 -45.818  35.541  1.00 13.81           C  
ATOM   4887  CG  HIS C 296      32.791 -44.686  36.268  1.00 16.44           C  
ATOM   4888  ND1 HIS C 296      31.448 -44.698  36.602  1.00 17.00           N  
ATOM   4889  CD2 HIS C 296      33.272 -43.484  36.670  1.00 16.63           C  
ATOM   4890  CE1 HIS C 296      31.151 -43.580  37.246  1.00 16.01           C  
ATOM   4891  NE2 HIS C 296      32.236 -42.822  37.291  1.00 16.74           N  
ATOM   4892  N   HIS C 297      35.606 -47.458  33.898  1.00 15.56           N  
ATOM   4893  CA  HIS C 297      36.278 -48.707  33.554  1.00 15.51           C  
ATOM   4894  C   HIS C 297      37.792 -48.567  33.817  1.00 18.39           C  
ATOM   4895  O   HIS C 297      38.471 -49.540  34.101  1.00 17.10           O  
ATOM   4896  CB  HIS C 297      36.031 -49.114  32.100  1.00 14.95           C  
ATOM   4897  CG  HIS C 297      36.672 -50.424  31.725  1.00 16.94           C  
ATOM   4898  ND1 HIS C 297      37.965 -50.520  31.246  1.00 17.04           N  
ATOM   4899  CD2 HIS C 297      36.191 -51.689  31.769  1.00 18.51           C  
ATOM   4900  CE1 HIS C 297      38.243 -51.786  30.987  1.00 17.00           C  
ATOM   4901  NE2 HIS C 297      37.181 -52.518  31.297  1.00 18.05           N  
ATOM   4902  N   GLY C 298      38.307 -47.348  33.708  1.00 15.28           N  
ATOM   4903  CA  GLY C 298      39.722 -47.078  33.997  1.00 14.88           C  
ATOM   4904  C   GLY C 298      40.120 -47.491  35.401  1.00 17.10           C  
ATOM   4905  O   GLY C 298      41.270 -47.801  35.652  1.00 16.11           O  
ATOM   4906  N   MET C 299      39.154 -47.541  36.308  1.00 13.99           N  
ATOM   4907  CA  MET C 299      39.404 -47.994  37.691  1.00 12.86           C  
ATOM   4908  C   MET C 299      39.722 -49.485  37.793  1.00 19.37           C  
ATOM   4909  O   MET C 299      40.298 -49.908  38.783  1.00 19.70           O  
ATOM   4910  CB  MET C 299      38.213 -47.648  38.580  1.00 14.67           C  
ATOM   4911  CG  MET C 299      37.995 -46.112  38.630  1.00 18.66           C  
ATOM   4912  SD  MET C 299      36.599 -45.583  39.627  1.00 23.82           S  
ATOM   4913  CE  MET C 299      37.250 -45.802  41.222  1.00 20.20           C  
ATOM   4914  N   VAL C 300      39.331 -50.278  36.783  1.00 15.95           N  
ATOM   4915  CA  VAL C 300      39.571 -51.720  36.782  1.00 14.38           C  
ATOM   4916  C   VAL C 300      40.476 -52.156  35.639  1.00 18.30           C  
ATOM   4917  O   VAL C 300      40.858 -53.330  35.548  1.00 18.02           O  
ATOM   4918  CB  VAL C 300      38.227 -52.549  36.760  1.00 18.10           C  
ATOM   4919  CG1 VAL C 300      37.369 -52.254  37.971  1.00 16.51           C  
ATOM   4920  CG2 VAL C 300      37.421 -52.329  35.418  1.00 16.89           C  
ATOM   4921  N   GLY C 301      40.817 -51.249  34.736  1.00 14.96           N  
ATOM   4922  CA  GLY C 301      41.579 -51.660  33.536  1.00 13.85           C  
ATOM   4923  C   GLY C 301      43.112 -51.736  33.663  1.00 18.61           C  
ATOM   4924  O   GLY C 301      43.776 -52.031  32.694  1.00 15.75           O  
ATOM   4925  N   LYS C 302      43.669 -51.447  34.850  1.00 16.83           N  
ATOM   4926  CA  LYS C 302      45.113 -51.394  35.025  1.00 16.55           C  
ATOM   4927  C   LYS C 302      45.747 -52.521  35.879  1.00 20.33           C  
ATOM   4928  O   LYS C 302      46.874 -52.349  36.338  1.00 19.11           O  
ATOM   4929  CB  LYS C 302      45.456 -50.043  35.690  1.00 18.84           C  
ATOM   4930  CG  LYS C 302      45.064 -48.771  34.899  1.00 22.11           C  
ATOM   4931  CD  LYS C 302      45.594 -47.532  35.605  1.00 22.30           C  
ATOM   4932  CE  LYS C 302      44.979 -46.255  35.088  1.00 18.27           C  
ATOM   4933  NZ  LYS C 302      43.537 -46.125  35.461  1.00 16.05           N  
ATOM   4934  N   PHE C 303      45.004 -53.590  36.206  1.00 15.93           N  
ATOM   4935  CA  PHE C 303      45.520 -54.630  37.110  1.00 14.13           C  
ATOM   4936  C   PHE C 303      46.331 -55.759  36.430  1.00 20.65           C  
ATOM   4937  O   PHE C 303      47.061 -56.482  37.094  1.00 20.76           O  
ATOM   4938  CB  PHE C 303      44.405 -55.214  38.002  1.00 14.87           C  
ATOM   4939  CG  PHE C 303      43.580 -54.175  38.744  1.00 14.80           C  
ATOM   4940  CD1 PHE C 303      44.201 -53.166  39.474  1.00 16.46           C  
ATOM   4941  CD2 PHE C 303      42.188 -54.278  38.800  1.00 14.55           C  
ATOM   4942  CE1 PHE C 303      43.461 -52.196  40.188  1.00 16.98           C  
ATOM   4943  CE2 PHE C 303      41.445 -53.374  39.543  1.00 17.48           C  
ATOM   4944  CZ  PHE C 303      42.076 -52.316  40.250  1.00 15.91           C  
ATOM   4945  N   ASN C 304      46.209 -55.919  35.116  1.00 19.90           N  
ATOM   4946  CA  ASN C 304      46.987 -56.955  34.415  1.00 20.41           C  
ATOM   4947  C   ASN C 304      47.512 -56.400  33.093  1.00 25.02           C  
ATOM   4948  O   ASN C 304      46.779 -55.763  32.352  1.00 25.04           O  
ATOM   4949  CB  ASN C 304      46.180 -58.236  34.121  1.00 14.39           C  
ATOM   4950  CG  ASN C 304      45.970 -59.108  35.360  1.00 25.83           C  
ATOM   4951  OD1 ASN C 304      46.851 -59.844  35.768  1.00 21.56           O  
ATOM   4952  ND2 ASN C 304      44.787 -59.056  35.917  1.00 14.55           N  
ATOM   4953  N   ASN C 305      48.784 -56.650  32.824  1.00 21.57           N  
ATOM   4954  CA  ASN C 305      49.397 -56.276  31.567  1.00 22.43           C  
ATOM   4955  C   ASN C 305      48.791 -57.090  30.457  1.00 23.62           C  
ATOM   4956  O   ASN C 305      48.569 -58.280  30.611  1.00 23.96           O  
ATOM   4957  CB  ASN C 305      50.881 -56.604  31.594  1.00 30.79           C  
ATOM   4958  CG  ASN C 305      51.715 -55.404  31.806  1.00 65.57           C  
ATOM   4959  OD1 ASN C 305      51.654 -54.464  31.027  1.00 65.70           O  
ATOM   4960  ND2 ASN C 305      52.475 -55.395  32.889  1.00 64.52           N  
ATOM   4961  N   PHE C 306      48.526 -56.459  29.322  1.00 18.34           N  
ATOM   4962  CA  PHE C 306      47.921 -57.210  28.220  1.00 16.77           C  
ATOM   4963  C   PHE C 306      48.404 -56.749  26.846  1.00 21.81           C  
ATOM   4964  O   PHE C 306      48.802 -55.604  26.643  1.00 17.95           O  
ATOM   4965  CB  PHE C 306      46.394 -57.103  28.258  1.00 16.69           C  
ATOM   4966  CG  PHE C 306      45.861 -55.677  28.128  1.00 17.78           C  
ATOM   4967  CD1 PHE C 306      45.496 -55.157  26.888  1.00 19.12           C  
ATOM   4968  CD2 PHE C 306      45.723 -54.854  29.260  1.00 20.03           C  
ATOM   4969  CE1 PHE C 306      44.982 -53.856  26.776  1.00 19.42           C  
ATOM   4970  CE2 PHE C 306      45.197 -53.541  29.183  1.00 20.87           C  
ATOM   4971  CZ  PHE C 306      44.806 -53.046  27.936  1.00 18.04           C  
ATOM   4972  N   ASN C 307      48.269 -57.651  25.895  1.00 22.30           N  
ATOM   4973  CA  ASN C 307      48.490 -57.352  24.496  1.00 23.15           C  
ATOM   4974  C   ASN C 307      47.082 -57.168  23.909  1.00 26.70           C  
ATOM   4975  O   ASN C 307      46.104 -57.814  24.355  1.00 25.72           O  
ATOM   4976  CB  ASN C 307      49.176 -58.536  23.790  1.00 27.50           C  
ATOM   4977  CG  ASN C 307      50.639 -58.579  24.065  1.00 54.57           C  
ATOM   4978  OD1 ASN C 307      51.282 -57.535  24.221  1.00 55.16           O  
ATOM   4979  ND2 ASN C 307      51.149 -59.772  24.293  1.00 44.90           N  
ATOM   4980  N   VAL C 308      47.015 -56.327  22.889  1.00 23.56           N  
ATOM   4981  CA  VAL C 308      45.805 -56.003  22.173  1.00 24.52           C  
ATOM   4982  C   VAL C 308      45.731 -56.684  20.802  1.00 24.88           C  
ATOM   4983  O   VAL C 308      46.609 -56.546  19.989  1.00 24.08           O  
ATOM   4984  CB  VAL C 308      45.739 -54.473  21.948  1.00 29.08           C  
ATOM   4985  CG1 VAL C 308      44.512 -54.116  21.089  1.00 28.70           C  
ATOM   4986  CG2 VAL C 308      45.723 -53.748  23.269  1.00 28.92           C  
ATOM   4987  N   ASP C 309      44.615 -57.327  20.518  1.00 19.98           N  
ATOM   4988  CA  ASP C 309      44.368 -57.938  19.217  1.00 18.77           C  
ATOM   4989  C   ASP C 309      42.960 -57.427  18.906  1.00 21.57           C  
ATOM   4990  O   ASP C 309      41.969 -58.039  19.265  1.00 22.34           O  
ATOM   4991  CB  ASP C 309      44.390 -59.468  19.345  1.00 20.98           C  
ATOM   4992  CG  ASP C 309      43.736 -60.144  18.182  1.00 32.82           C  
ATOM   4993  OD1 ASP C 309      43.900 -59.633  17.064  1.00 34.04           O  
ATOM   4994  OD2 ASP C 309      43.022 -61.146  18.377  1.00 42.67           O  
ATOM   4995  N   ALA C 310      42.882 -56.231  18.350  1.00 17.81           N  
ATOM   4996  CA  ALA C 310      41.611 -55.539  18.159  1.00 17.89           C  
ATOM   4997  C   ALA C 310      41.348 -55.086  16.721  1.00 24.36           C  
ATOM   4998  O   ALA C 310      42.263 -54.655  16.041  1.00 25.17           O  
ATOM   4999  CB  ALA C 310      41.542 -54.317  19.093  1.00 17.13           C  
ATOM   5000  N   GLN C 311      40.079 -55.055  16.331  1.00 21.29           N  
ATOM   5001  CA  GLN C 311      39.711 -54.583  15.011  1.00 21.41           C  
ATOM   5002  C   GLN C 311      38.425 -53.804  15.027  1.00 22.92           C  
ATOM   5003  O   GLN C 311      37.461 -54.206  15.683  1.00 21.50           O  
ATOM   5004  CB  GLN C 311      39.541 -55.724  14.013  1.00 23.09           C  
ATOM   5005  CG  GLN C 311      39.431 -55.148  12.570  1.00 52.80           C  
ATOM   5006  CD  GLN C 311      39.315 -56.201  11.503  1.00 74.83           C  
ATOM   5007  OE1 GLN C 311      40.042 -56.174  10.505  1.00 76.41           O  
ATOM   5008  NE2 GLN C 311      38.400 -57.136  11.697  1.00 60.26           N  
ATOM   5009  N   LEU C 312      38.400 -52.710  14.265  1.00 19.15           N  
ATOM   5010  CA  LEU C 312      37.177 -51.931  14.110  1.00 19.47           C  
ATOM   5011  C   LEU C 312      36.777 -51.851  12.636  1.00 24.59           C  
ATOM   5012  O   LEU C 312      37.615 -51.586  11.758  1.00 23.42           O  
ATOM   5013  CB  LEU C 312      37.340 -50.525  14.683  1.00 18.91           C  
ATOM   5014  CG  LEU C 312      36.283 -49.501  14.297  1.00 22.22           C  
ATOM   5015  CD1 LEU C 312      34.987 -49.734  15.062  1.00 21.31           C  
ATOM   5016  CD2 LEU C 312      36.819 -48.118  14.543  1.00 22.76           C  
ATOM   5017  N   LYS C 313      35.492 -52.081  12.384  1.00 22.40           N  
ATOM   5018  CA  LYS C 313      34.931 -52.003  11.053  1.00 22.59           C  
ATOM   5019  C   LYS C 313      33.817 -50.971  11.035  1.00 26.67           C  
ATOM   5020  O   LYS C 313      32.894 -51.024  11.858  1.00 25.52           O  
ATOM   5021  CB  LYS C 313      34.376 -53.359  10.615  1.00 25.35           C  
ATOM   5022  CG  LYS C 313      33.639 -53.333   9.278  1.00 44.04           C  
ATOM   5023  CD  LYS C 313      33.498 -54.724   8.684  1.00 60.64           C  
ATOM   5024  CE  LYS C 313      32.140 -55.326   8.953  1.00 78.92           C  
ATOM   5025  NZ  LYS C 313      32.135 -56.782   8.631  1.00 93.06           N  
ATOM   5026  N   VAL C 314      33.919 -50.016  10.115  1.00 22.79           N  
ATOM   5027  CA  VAL C 314      32.897 -48.958   9.979  1.00 22.36           C  
ATOM   5028  C   VAL C 314      32.334 -49.024   8.553  1.00 27.02           C  
ATOM   5029  O   VAL C 314      33.090 -48.988   7.569  1.00 27.09           O  
ATOM   5030  CB  VAL C 314      33.474 -47.552  10.292  1.00 25.28           C  
ATOM   5031  CG1 VAL C 314      32.461 -46.493   9.959  1.00 25.29           C  
ATOM   5032  CG2 VAL C 314      33.873 -47.451  11.753  1.00 24.99           C  
ATOM   5033  N   VAL C 315      31.029 -49.235   8.443  1.00 23.24           N  
ATOM   5034  CA  VAL C 315      30.384 -49.272   7.129  1.00 23.02           C  
ATOM   5035  C   VAL C 315      29.538 -48.033   6.936  1.00 25.68           C  
ATOM   5036  O   VAL C 315      28.559 -47.843   7.638  1.00 23.40           O  
ATOM   5037  CB  VAL C 315      29.522 -50.550   6.906  1.00 26.56           C  
ATOM   5038  CG1 VAL C 315      28.988 -50.566   5.441  1.00 25.13           C  
ATOM   5039  CG2 VAL C 315      30.324 -51.835   7.204  1.00 25.68           C  
ATOM   5040  N   LEU C 316      29.939 -47.175   6.008  1.00 26.97           N  
ATOM   5041  CA  LEU C 316      29.195 -45.941   5.708  1.00 28.24           C  
ATOM   5042  C   LEU C 316      28.036 -46.209   4.719  1.00 30.64           C  
ATOM   5043  O   LEU C 316      28.052 -47.210   3.991  1.00 28.72           O  
ATOM   5044  CB  LEU C 316      30.147 -44.914   5.088  1.00 28.94           C  
ATOM   5045  CG  LEU C 316      31.368 -44.464   5.905  1.00 33.43           C  
ATOM   5046  CD1 LEU C 316      32.084 -43.325   5.170  1.00 32.30           C  
ATOM   5047  CD2 LEU C 316      30.900 -43.986   7.252  1.00 36.40           C  
ATOM   5048  N   PRO C 317      27.038 -45.326   4.682  1.00 30.02           N  
ATOM   5049  CA  PRO C 317      25.943 -45.491   3.709  1.00 30.58           C  
ATOM   5050  C   PRO C 317      26.546 -45.299   2.293  1.00 38.10           C  
ATOM   5051  O   PRO C 317      27.603 -44.662   2.127  1.00 36.49           O  
ATOM   5052  CB  PRO C 317      24.990 -44.325   4.041  1.00 31.41           C  
ATOM   5053  CG  PRO C 317      25.455 -43.766   5.341  1.00 35.83           C  
ATOM   5054  CD  PRO C 317      26.912 -44.064   5.438  1.00 31.60           C  
ATOM   5055  N   LYS C 318      25.907 -45.880   1.280  1.00 38.24           N  
ATOM   5056  CA  LYS C 318      26.411 -45.806  -0.103  1.00 39.06           C  
ATOM   5057  C   LYS C 318      26.665 -44.366  -0.590  1.00 42.94           C  
ATOM   5058  O   LYS C 318      25.866 -43.471  -0.354  1.00 42.83           O  
ATOM   5059  CB  LYS C 318      25.451 -46.523  -1.048  1.00 43.92           C  
ATOM   5060  CG  LYS C 318      25.782 -46.344  -2.518  1.00 60.81           C  
ATOM   5061  N   GLY C 319      27.821 -44.122  -1.189  1.00 39.61           N  
ATOM   5062  CA  GLY C 319      28.134 -42.781  -1.638  1.00 40.23           C  
ATOM   5063  C   GLY C 319      28.837 -41.860  -0.620  1.00 46.34           C  
ATOM   5064  O   GLY C 319      29.212 -40.730  -0.960  1.00 47.01           O  
ATOM   5065  N   TYR C 320      28.996 -42.309   0.626  1.00 40.50           N  
ATOM   5066  CA  TYR C 320      29.648 -41.476   1.628  1.00 37.86           C  
ATOM   5067  C   TYR C 320      31.091 -41.865   1.740  1.00 35.45           C  
ATOM   5068  O   TYR C 320      31.441 -43.003   1.512  1.00 33.43           O  
ATOM   5069  CB  TYR C 320      28.981 -41.631   2.985  1.00 39.50           C  
ATOM   5070  CG  TYR C 320      27.679 -40.868   3.125  1.00 42.59           C  
ATOM   5071  CD1 TYR C 320      27.625 -39.671   3.838  1.00 44.81           C  
ATOM   5072  CD2 TYR C 320      26.505 -41.340   2.535  1.00 43.77           C  
ATOM   5073  CE1 TYR C 320      26.438 -38.993   4.001  1.00 46.48           C  
ATOM   5074  CE2 TYR C 320      25.316 -40.644   2.668  1.00 44.99           C  
ATOM   5075  CZ  TYR C 320      25.294 -39.476   3.403  1.00 55.84           C  
ATOM   5076  OH  TYR C 320      24.122 -38.788   3.548  1.00 64.07           O  
ATOM   5077  N   LYS C 321      31.940 -40.912   2.087  1.00 30.71           N  
ATOM   5078  CA  LYS C 321      33.340 -41.230   2.298  1.00 30.23           C  
ATOM   5079  C   LYS C 321      33.976 -40.550   3.521  1.00 32.19           C  
ATOM   5080  O   LYS C 321      33.539 -39.468   3.976  1.00 31.57           O  
ATOM   5081  CB  LYS C 321      34.199 -41.087   1.029  1.00 33.39           C  
ATOM   5082  CG  LYS C 321      34.119 -39.752   0.336  1.00 55.85           C  
ATOM   5083  N   ILE C 322      34.993 -41.205   4.066  1.00 25.59           N  
ATOM   5084  CA  ILE C 322      35.696 -40.642   5.209  1.00 24.99           C  
ATOM   5085  C   ILE C 322      36.601 -39.494   4.743  1.00 29.56           C  
ATOM   5086  O   ILE C 322      37.418 -39.658   3.837  1.00 28.45           O  
ATOM   5087  CB  ILE C 322      36.429 -41.746   6.010  1.00 27.18           C  
ATOM   5088  CG1 ILE C 322      35.394 -42.629   6.720  1.00 27.91           C  
ATOM   5089  CG2 ILE C 322      37.444 -41.169   6.973  1.00 26.17           C  
ATOM   5090  CD1 ILE C 322      35.931 -43.451   7.857  1.00 32.80           C  
ATOM   5091  N   ARG C 323      36.435 -38.333   5.353  1.00 27.29           N  
ATOM   5092  CA  ARG C 323      37.204 -37.160   4.989  1.00 27.74           C  
ATOM   5093  C   ARG C 323      38.356 -37.020   5.951  1.00 31.30           C  
ATOM   5094  O   ARG C 323      39.395 -36.435   5.634  1.00 30.82           O  
ATOM   5095  CB  ARG C 323      36.328 -35.900   5.065  1.00 32.54           C  
ATOM   5096  CG  ARG C 323      35.121 -35.903   4.123  1.00 51.37           C  
ATOM   5097  CD  ARG C 323      35.554 -35.655   2.693  1.00 64.13           C  
ATOM   5098  NE  ARG C 323      34.822 -36.493   1.753  1.00 81.67           N  
ATOM   5099  CZ  ARG C 323      33.912 -36.033   0.901  1.00103.79           C  
ATOM   5100  NH1 ARG C 323      33.621 -34.737   0.872  1.00 97.42           N  
ATOM   5101  NH2 ARG C 323      33.290 -36.871   0.082  1.00 89.70           N  
ATOM   5102  N   TYR C 324      38.160 -37.515   7.161  1.00 27.33           N  
ATOM   5103  CA  TYR C 324      39.215 -37.407   8.162  1.00 26.06           C  
ATOM   5104  C   TYR C 324      39.055 -38.457   9.235  1.00 26.97           C  
ATOM   5105  O   TYR C 324      37.972 -38.628   9.794  1.00 25.87           O  
ATOM   5106  CB  TYR C 324      39.184 -36.011   8.808  1.00 26.71           C  
ATOM   5107  CG  TYR C 324      40.161 -35.842   9.946  1.00 28.50           C  
ATOM   5108  CD1 TYR C 324      41.465 -35.442   9.700  1.00 30.71           C  
ATOM   5109  CD2 TYR C 324      39.758 -35.997  11.281  1.00 29.51           C  
ATOM   5110  CE1 TYR C 324      42.368 -35.203  10.758  1.00 32.49           C  
ATOM   5111  CE2 TYR C 324      40.643 -35.770  12.345  1.00 30.03           C  
ATOM   5112  CZ  TYR C 324      41.951 -35.383  12.067  1.00 39.05           C  
ATOM   5113  OH  TYR C 324      42.856 -35.171  13.071  1.00 38.61           O  
ATOM   5114  N   ALA C 325      40.144 -39.141   9.544  1.00 22.47           N  
ATOM   5115  CA  ALA C 325      40.158 -40.106  10.654  1.00 21.72           C  
ATOM   5116  C   ALA C 325      41.531 -40.068  11.309  1.00 25.83           C  
ATOM   5117  O   ALA C 325      42.544 -40.136  10.619  1.00 26.89           O  
ATOM   5118  CB  ALA C 325      39.862 -41.505  10.160  1.00 22.27           C  
ATOM   5119  N   ALA C 326      41.571 -39.976  12.633  1.00 22.23           N  
ATOM   5120  CA  ALA C 326      42.826 -40.012  13.403  1.00 21.65           C  
ATOM   5121  C   ALA C 326      42.492 -40.611  14.773  1.00 24.75           C  
ATOM   5122  O   ALA C 326      41.753 -40.028  15.566  1.00 24.54           O  
ATOM   5123  CB  ALA C 326      43.395 -38.607  13.585  1.00 22.20           C  
ATOM   5124  N   PRO C 327      43.032 -41.778  15.052  1.00 22.36           N  
ATOM   5125  CA  PRO C 327      43.962 -42.479  14.143  1.00 22.56           C  
ATOM   5126  C   PRO C 327      43.380 -42.902  12.779  1.00 29.21           C  
ATOM   5127  O   PRO C 327      42.168 -43.148  12.618  1.00 28.58           O  
ATOM   5128  CB  PRO C 327      44.384 -43.725  14.926  1.00 23.72           C  
ATOM   5129  CG  PRO C 327      43.691 -43.679  16.239  1.00 28.09           C  
ATOM   5130  CD  PRO C 327      42.804 -42.476  16.328  1.00 23.93           C  
ATOM   5131  N   GLN C 328      44.293 -43.058  11.830  1.00 25.50           N  
ATOM   5132  CA  GLN C 328      43.992 -43.421  10.449  1.00 25.49           C  
ATOM   5133  C   GLN C 328      43.542 -44.879  10.231  1.00 25.40           C  
ATOM   5134  O   GLN C 328      44.059 -45.790  10.861  1.00 23.76           O  
ATOM   5135  CB  GLN C 328      45.219 -43.106   9.568  1.00 26.71           C  
ATOM   5136  CG  GLN C 328      44.987 -43.243   8.064  1.00 57.49           C  
ATOM   5137  CD  GLN C 328      43.837 -42.399   7.523  1.00 80.93           C  
ATOM   5138  OE1 GLN C 328      42.859 -42.120   8.220  1.00 76.18           O  
ATOM   5139  NE2 GLN C 328      43.924 -42.048   6.244  1.00 77.05           N  
ATOM   5140  N   TYR C 329      42.590 -45.099   9.326  1.00 20.44           N  
ATOM   5141  CA  TYR C 329      42.160 -46.464   9.030  1.00 21.11           C  
ATOM   5142  C   TYR C 329      43.245 -47.171   8.236  1.00 25.51           C  
ATOM   5143  O   TYR C 329      44.065 -46.523   7.618  1.00 25.41           O  
ATOM   5144  CB  TYR C 329      40.823 -46.505   8.262  1.00 23.03           C  
ATOM   5145  CG  TYR C 329      40.813 -45.652   7.025  1.00 25.86           C  
ATOM   5146  CD1 TYR C 329      41.321 -46.137   5.817  1.00 28.09           C  
ATOM   5147  CD2 TYR C 329      40.244 -44.391   7.038  1.00 27.18           C  
ATOM   5148  CE1 TYR C 329      41.319 -45.347   4.664  1.00 26.90           C  
ATOM   5149  CE2 TYR C 329      40.237 -43.604   5.897  1.00 27.86           C  
ATOM   5150  CZ  TYR C 329      40.745 -44.103   4.720  1.00 32.45           C  
ATOM   5151  OH  TYR C 329      40.740 -43.321   3.617  1.00 36.81           O  
ATOM   5152  N   ARG C 330      43.268 -48.493   8.292  1.00 23.60           N  
ATOM   5153  CA  ARG C 330      44.261 -49.291   7.591  1.00 25.05           C  
ATOM   5154  C   ARG C 330      43.845 -49.672   6.143  1.00 32.16           C  
ATOM   5155  O   ARG C 330      44.686 -49.840   5.264  1.00 33.14           O  
ATOM   5156  CB  ARG C 330      44.436 -50.592   8.359  1.00 23.07           C  
ATOM   5157  CG  ARG C 330      45.382 -51.576   7.753  1.00 24.39           C  
ATOM   5158  CD  ARG C 330      45.439 -52.842   8.599  1.00 39.57           C  
ATOM   5159  NE  ARG C 330      46.812 -53.286   8.827  1.00 59.76           N  
ATOM   5160  CZ  ARG C 330      47.739 -52.563   9.455  1.00 81.57           C  
ATOM   5161  NH1 ARG C 330      47.451 -51.354   9.932  1.00 77.00           N  
ATOM   5162  NH2 ARG C 330      48.959 -53.048   9.610  1.00 71.95           N  
ATOM   5163  N   SER C 331      42.560 -49.949   5.946  1.00 26.77           N  
ATOM   5164  CA  SER C 331      42.087 -50.349   4.637  1.00 25.92           C  
ATOM   5165  C   SER C 331      40.656 -49.913   4.406  1.00 30.56           C  
ATOM   5166  O   SER C 331      39.948 -49.547   5.336  1.00 29.35           O  
ATOM   5167  CB  SER C 331      42.189 -51.856   4.497  1.00 26.66           C  
ATOM   5168  OG  SER C 331      41.232 -52.459   5.340  1.00 33.41           O  
ATOM   5169  N   GLN C 332      40.236 -49.982   3.149  1.00 27.61           N  
ATOM   5170  CA  GLN C 332      38.897 -49.550   2.736  1.00 26.85           C  
ATOM   5171  C   GLN C 332      38.504 -50.374   1.525  1.00 31.16           C  
ATOM   5172  O   GLN C 332      39.308 -50.667   0.673  1.00 33.44           O  
ATOM   5173  CB  GLN C 332      38.879 -48.065   2.357  1.00 27.92           C  
ATOM   5174  CG  GLN C 332      37.614 -47.698   1.600  1.00 39.82           C  
ATOM   5175  CD  GLN C 332      37.785 -46.529   0.653  1.00 54.07           C  
ATOM   5176  OE1 GLN C 332      38.822 -45.851   0.630  1.00 52.06           O  
ATOM   5177  NE2 GLN C 332      36.730 -46.238  -0.081  1.00 44.23           N  
ATOM   5178  N   ASN C 333      37.275 -50.828   1.504  1.00 26.92           N  
ATOM   5179  CA  ASN C 333      36.776 -51.610   0.405  1.00 26.99           C  
ATOM   5180  C   ASN C 333      35.387 -51.036   0.156  1.00 31.69           C  
ATOM   5181  O   ASN C 333      34.458 -51.280   0.930  1.00 29.66           O  
ATOM   5182  CB  ASN C 333      36.682 -53.067   0.809  1.00 26.59           C  
ATOM   5183  CG  ASN C 333      36.158 -53.931  -0.304  1.00 56.24           C  
ATOM   5184  OD1 ASN C 333      36.415 -53.676  -1.471  1.00 50.37           O  
ATOM   5185  ND2 ASN C 333      35.333 -54.898   0.043  1.00 59.14           N  
ATOM   5186  N   LEU C 334      35.284 -50.169  -0.837  1.00 30.61           N  
ATOM   5187  CA  LEU C 334      34.031 -49.454  -1.046  1.00 32.43           C  
ATOM   5188  C   LEU C 334      33.633 -48.637   0.193  1.00 35.39           C  
ATOM   5189  O   LEU C 334      34.326 -47.691   0.553  1.00 36.07           O  
ATOM   5190  CB  LEU C 334      32.917 -50.396  -1.485  1.00 33.09           C  
ATOM   5191  CG  LEU C 334      33.041 -50.912  -2.930  1.00 38.43           C  
ATOM   5192  CD1 LEU C 334      31.844 -51.799  -3.234  1.00 38.34           C  
ATOM   5193  CD2 LEU C 334      33.163 -49.748  -3.929  1.00 36.41           C  
ATOM   5194  N   GLU C 335      32.508 -48.957   0.823  1.00 30.03           N  
ATOM   5195  CA  GLU C 335      32.058 -48.141   1.962  1.00 29.52           C  
ATOM   5196  C   GLU C 335      32.516 -48.686   3.313  1.00 32.62           C  
ATOM   5197  O   GLU C 335      32.273 -48.107   4.361  1.00 33.26           O  
ATOM   5198  CB  GLU C 335      30.544 -47.970   1.959  1.00 30.79           C  
ATOM   5199  CG  GLU C 335      30.052 -46.888   1.034  1.00 43.61           C  
ATOM   5200  CD  GLU C 335      29.868 -47.417  -0.374  1.00 68.47           C  
ATOM   5201  OE1 GLU C 335      29.598 -48.641  -0.511  1.00 46.07           O  
ATOM   5202  OE2 GLU C 335      30.072 -46.635  -1.333  1.00 66.05           O  
ATOM   5203  N   GLU C 336      33.170 -49.825   3.267  1.00 27.77           N  
ATOM   5204  CA  GLU C 336      33.673 -50.467   4.453  1.00 27.57           C  
ATOM   5205  C   GLU C 336      35.116 -50.043   4.798  1.00 30.22           C  
ATOM   5206  O   GLU C 336      36.033 -50.193   3.979  1.00 26.68           O  
ATOM   5207  CB  GLU C 336      33.594 -51.963   4.261  1.00 28.54           C  
ATOM   5208  CG  GLU C 336      34.549 -52.723   5.135  1.00 42.96           C  
ATOM   5209  CD  GLU C 336      34.197 -54.199   5.230  1.00 70.12           C  
ATOM   5210  OE1 GLU C 336      33.007 -54.558   5.045  1.00 63.56           O  
ATOM   5211  OE2 GLU C 336      35.121 -55.000   5.483  1.00 65.75           O  
ATOM   5212  N   TYR C 337      35.304 -49.496   6.004  1.00 25.83           N  
ATOM   5213  CA  TYR C 337      36.640 -49.124   6.469  1.00 24.41           C  
ATOM   5214  C   TYR C 337      37.033 -49.960   7.691  1.00 27.40           C  
ATOM   5215  O   TYR C 337      36.207 -50.280   8.551  1.00 26.06           O  
ATOM   5216  CB  TYR C 337      36.717 -47.643   6.805  1.00 24.50           C  
ATOM   5217  CG  TYR C 337      36.431 -46.732   5.664  1.00 25.88           C  
ATOM   5218  CD1 TYR C 337      37.438 -45.983   5.088  1.00 27.70           C  
ATOM   5219  CD2 TYR C 337      35.131 -46.556   5.196  1.00 27.71           C  
ATOM   5220  CE1 TYR C 337      37.174 -45.088   4.061  1.00 28.10           C  
ATOM   5221  CE2 TYR C 337      34.855 -45.649   4.163  1.00 28.81           C  
ATOM   5222  CZ  TYR C 337      35.898 -44.932   3.591  1.00 37.38           C  
ATOM   5223  OH  TYR C 337      35.663 -44.020   2.571  1.00 38.42           O  
ATOM   5224  N   ARG C 338      38.296 -50.330   7.747  1.00 24.57           N  
ATOM   5225  CA  ARG C 338      38.811 -51.132   8.855  1.00 25.50           C  
ATOM   5226  C   ARG C 338      40.044 -50.503   9.531  1.00 27.62           C  
ATOM   5227  O   ARG C 338      40.944 -49.958   8.860  1.00 23.95           O  
ATOM   5228  CB  ARG C 338      39.204 -52.537   8.390  1.00 24.79           C  
ATOM   5229  CG  ARG C 338      38.040 -53.446   8.045  1.00 34.22           C  
ATOM   5230  CD  ARG C 338      38.562 -54.806   7.544  1.00 41.35           C  
ATOM   5231  NE  ARG C 338      37.506 -55.567   6.886  1.00 69.90           N  
ATOM   5232  CZ  ARG C 338      37.233 -56.843   7.144  1.00 94.14           C  
ATOM   5233  NH1 ARG C 338      37.959 -57.509   8.030  1.00 87.35           N  
ATOM   5234  NH2 ARG C 338      36.237 -57.456   6.517  1.00 82.80           N  
ATOM   5235  N   TRP C 339      40.089 -50.660  10.856  1.00 22.65           N  
ATOM   5236  CA  TRP C 339      41.226 -50.244  11.673  1.00 21.98           C  
ATOM   5237  C   TRP C 339      41.793 -51.465  12.397  1.00 26.82           C  
ATOM   5238  O   TRP C 339      41.059 -52.274  12.962  1.00 26.05           O  
ATOM   5239  CB  TRP C 339      40.806 -49.225  12.763  1.00 19.57           C  
ATOM   5240  CG  TRP C 339      40.553 -47.845  12.300  1.00 20.13           C  
ATOM   5241  CD1 TRP C 339      41.351 -46.754  12.508  1.00 22.84           C  
ATOM   5242  CD2 TRP C 339      39.376 -47.366  11.632  1.00 20.17           C  
ATOM   5243  NE1 TRP C 339      40.741 -45.625  12.005  1.00 23.29           N  
ATOM   5244  CE2 TRP C 339      39.532 -45.972  11.457  1.00 24.83           C  
ATOM   5245  CE3 TRP C 339      38.229 -47.987  11.113  1.00 21.32           C  
ATOM   5246  CZ2 TRP C 339      38.564 -45.179  10.806  1.00 24.40           C  
ATOM   5247  CZ3 TRP C 339      37.273 -47.201  10.453  1.00 22.82           C  
ATOM   5248  CH2 TRP C 339      37.448 -45.820  10.300  1.00 23.51           C  
ATOM   5249  N   SER C 340      43.108 -51.547  12.475  1.00 25.87           N  
ATOM   5250  CA  SER C 340      43.740 -52.610  13.251  1.00 26.41           C  
ATOM   5251  C   SER C 340      45.233 -52.348  13.348  1.00 29.19           C  
ATOM   5252  O   SER C 340      45.816 -51.744  12.457  1.00 29.10           O  
ATOM   5253  CB  SER C 340      43.457 -53.996  12.668  1.00 30.89           C  
ATOM   5254  OG  SER C 340      44.156 -54.163  11.451  1.00 45.04           O  
ATOM   5255  N   GLY C 341      45.823 -52.741  14.473  1.00 25.74           N  
ATOM   5256  CA  GLY C 341      47.255 -52.559  14.709  1.00 24.25           C  
ATOM   5257  C   GLY C 341      47.665 -51.119  14.805  1.00 30.08           C  
ATOM   5258  O   GLY C 341      46.822 -50.207  14.860  1.00 31.51           O  
ATOM   5259  N   GLY C 342      48.976 -50.907  14.849  1.00 27.28           N  
ATOM   5260  CA  GLY C 342      49.554 -49.559  14.861  1.00 25.66           C  
ATOM   5261  C   GLY C 342      48.925 -48.621  15.874  1.00 28.47           C  
ATOM   5262  O   GLY C 342      48.683 -48.981  17.013  1.00 29.03           O  
ATOM   5263  N   ALA C 343      48.716 -47.385  15.454  1.00 23.82           N  
ATOM   5264  CA  ALA C 343      48.156 -46.371  16.303  1.00 22.72           C  
ATOM   5265  C   ALA C 343      46.766 -46.746  16.840  1.00 26.73           C  
ATOM   5266  O   ALA C 343      46.383 -46.279  17.891  1.00 27.71           O  
ATOM   5267  CB  ALA C 343      48.118 -45.037  15.554  1.00 22.90           C  
ATOM   5268  N   TYR C 344      46.004 -47.568  16.125  1.00 22.18           N  
ATOM   5269  CA  TYR C 344      44.657 -47.927  16.597  1.00 20.47           C  
ATOM   5270  C   TYR C 344      44.759 -48.820  17.819  1.00 24.63           C  
ATOM   5271  O   TYR C 344      44.004 -48.670  18.767  1.00 25.26           O  
ATOM   5272  CB  TYR C 344      43.814 -48.622  15.523  1.00 19.68           C  
ATOM   5273  CG  TYR C 344      42.447 -49.024  16.047  1.00 18.45           C  
ATOM   5274  CD1 TYR C 344      41.524 -48.048  16.471  1.00 19.24           C  
ATOM   5275  CD2 TYR C 344      42.122 -50.351  16.227  1.00 17.70           C  
ATOM   5276  CE1 TYR C 344      40.291 -48.410  17.020  1.00 17.69           C  
ATOM   5277  CE2 TYR C 344      40.859 -50.736  16.728  1.00 18.28           C  
ATOM   5278  CZ  TYR C 344      39.965 -49.757  17.162  1.00 24.04           C  
ATOM   5279  OH  TYR C 344      38.746 -50.107  17.740  1.00 21.89           O  
ATOM   5280  N   ALA C 345      45.714 -49.740  17.777  1.00 19.86           N  
ATOM   5281  CA  ALA C 345      45.992 -50.688  18.837  1.00 19.17           C  
ATOM   5282  C   ALA C 345      46.450 -49.934  20.103  1.00 23.64           C  
ATOM   5283  O   ALA C 345      46.051 -50.283  21.204  1.00 24.77           O  
ATOM   5284  CB  ALA C 345      47.081 -51.705  18.362  1.00 19.11           C  
ATOM   5285  N   ARG C 346      47.265 -48.894  19.943  1.00 19.64           N  
ATOM   5286  CA  ARG C 346      47.725 -48.088  21.095  1.00 19.42           C  
ATOM   5287  C   ARG C 346      46.580 -47.280  21.675  1.00 22.39           C  
ATOM   5288  O   ARG C 346      46.487 -47.105  22.907  1.00 21.34           O  
ATOM   5289  CB  ARG C 346      48.872 -47.147  20.717  1.00 19.37           C  
ATOM   5290  CG  ARG C 346      50.196 -47.871  20.617  1.00 31.54           C  
ATOM   5291  CD  ARG C 346      51.368 -46.909  20.553  1.00 36.43           C  
ATOM   5292  NE  ARG C 346      51.330 -46.207  19.289  1.00 44.63           N  
ATOM   5293  CZ  ARG C 346      51.858 -46.681  18.175  1.00 62.81           C  
ATOM   5294  NH1 ARG C 346      52.520 -47.824  18.207  1.00 57.19           N  
ATOM   5295  NH2 ARG C 346      51.732 -46.007  17.040  1.00 52.80           N  
ATOM   5296  N   TRP C 347      45.663 -46.857  20.803  1.00 18.01           N  
ATOM   5297  CA  TRP C 347      44.499 -46.111  21.270  1.00 18.07           C  
ATOM   5298  C   TRP C 347      43.577 -47.052  22.079  1.00 22.59           C  
ATOM   5299  O   TRP C 347      43.025 -46.660  23.101  1.00 23.60           O  
ATOM   5300  CB  TRP C 347      43.732 -45.478  20.091  1.00 16.23           C  
ATOM   5301  CG  TRP C 347      42.509 -44.721  20.548  1.00 15.87           C  
ATOM   5302  CD1 TRP C 347      42.482 -43.469  21.120  1.00 17.90           C  
ATOM   5303  CD2 TRP C 347      41.161 -45.205  20.580  1.00 15.69           C  
ATOM   5304  NE1 TRP C 347      41.192 -43.133  21.447  1.00 17.11           N  
ATOM   5305  CE2 TRP C 347      40.363 -44.181  21.144  1.00 18.25           C  
ATOM   5306  CE3 TRP C 347      40.534 -46.387  20.132  1.00 16.59           C  
ATOM   5307  CZ2 TRP C 347      38.975 -44.319  21.324  1.00 18.27           C  
ATOM   5308  CZ3 TRP C 347      39.142 -46.499  20.270  1.00 17.11           C  
ATOM   5309  CH2 TRP C 347      38.386 -45.485  20.887  1.00 17.68           C  
ATOM   5310  N   VAL C 348      43.446 -48.304  21.646  1.00 17.21           N  
ATOM   5311  CA  VAL C 348      42.601 -49.268  22.364  1.00 16.18           C  
ATOM   5312  C   VAL C 348      43.163 -49.556  23.749  1.00 20.58           C  
ATOM   5313  O   VAL C 348      42.424 -49.610  24.741  1.00 20.40           O  
ATOM   5314  CB  VAL C 348      42.373 -50.587  21.548  1.00 17.91           C  
ATOM   5315  CG1 VAL C 348      41.684 -51.641  22.399  1.00 15.54           C  
ATOM   5316  CG2 VAL C 348      41.544 -50.277  20.299  1.00 17.61           C  
ATOM   5317  N   GLU C 349      44.473 -49.772  23.812  1.00 17.45           N  
ATOM   5318  CA  GLU C 349      45.128 -50.021  25.102  1.00 17.06           C  
ATOM   5319  C   GLU C 349      44.850 -48.830  26.002  1.00 18.46           C  
ATOM   5320  O   GLU C 349      44.411 -48.973  27.110  1.00 18.36           O  
ATOM   5321  CB  GLU C 349      46.645 -50.118  24.919  1.00 18.05           C  
ATOM   5322  CG  GLU C 349      47.369 -50.402  26.240  1.00 20.64           C  
ATOM   5323  CD  GLU C 349      48.885 -50.286  26.138  1.00 28.47           C  
ATOM   5324  OE1 GLU C 349      49.402 -49.990  25.043  1.00 24.97           O  
ATOM   5325  OE2 GLU C 349      49.561 -50.471  27.167  1.00 21.05           O  
ATOM   5326  N   HIS C 350      45.072 -47.645  25.458  1.00 16.12           N  
ATOM   5327  CA  HIS C 350      44.852 -46.367  26.135  1.00 14.99           C  
ATOM   5328  C   HIS C 350      43.444 -46.244  26.749  1.00 18.80           C  
ATOM   5329  O   HIS C 350      43.322 -46.030  27.951  1.00 18.69           O  
ATOM   5330  CB  HIS C 350      45.179 -45.227  25.118  1.00 14.74           C  
ATOM   5331  CG  HIS C 350      44.839 -43.831  25.575  1.00 16.46           C  
ATOM   5332  ND1 HIS C 350      45.749 -43.011  26.219  1.00 16.80           N  
ATOM   5333  CD2 HIS C 350      43.756 -43.057  25.324  1.00 17.66           C  
ATOM   5334  CE1 HIS C 350      45.211 -41.821  26.411  1.00 16.17           C  
ATOM   5335  NE2 HIS C 350      43.994 -41.824  25.895  1.00 16.87           N  
ATOM   5336  N   VAL C 351      42.386 -46.422  25.955  1.00 15.47           N  
ATOM   5337  CA  VAL C 351      41.011 -46.255  26.465  1.00 14.68           C  
ATOM   5338  C   VAL C 351      40.576 -47.345  27.425  1.00 20.49           C  
ATOM   5339  O   VAL C 351      39.802 -47.066  28.352  1.00 18.15           O  
ATOM   5340  CB  VAL C 351      39.939 -45.977  25.354  1.00 17.56           C  
ATOM   5341  CG1 VAL C 351      40.302 -44.724  24.566  1.00 16.95           C  
ATOM   5342  CG2 VAL C 351      39.751 -47.179  24.456  1.00 16.49           C  
ATOM   5343  N   CYS C 352      41.088 -48.570  27.220  1.00 18.25           N  
ATOM   5344  CA  CYS C 352      40.780 -49.705  28.128  1.00 17.27           C  
ATOM   5345  C   CYS C 352      41.355 -49.454  29.527  1.00 19.87           C  
ATOM   5346  O   CYS C 352      40.869 -50.012  30.498  1.00 16.71           O  
ATOM   5347  CB  CYS C 352      41.349 -51.032  27.591  1.00 17.60           C  
ATOM   5348  SG  CYS C 352      40.377 -51.622  26.208  1.00 21.77           S  
ATOM   5349  N   LYS C 353      42.418 -48.648  29.602  1.00 16.94           N  
ATOM   5350  CA  LYS C 353      43.075 -48.336  30.893  1.00 15.88           C  
ATOM   5351  C   LYS C 353      42.592 -47.054  31.522  1.00 17.20           C  
ATOM   5352  O   LYS C 353      42.990 -46.731  32.623  1.00 15.32           O  
ATOM   5353  CB  LYS C 353      44.586 -48.313  30.796  1.00 16.09           C  
ATOM   5354  CG  LYS C 353      45.182 -49.650  30.393  1.00 14.34           C  
ATOM   5355  CD  LYS C 353      46.694 -49.489  30.366  1.00 18.93           C  
ATOM   5356  CE  LYS C 353      47.376 -50.788  30.104  1.00 27.54           C  
ATOM   5357  NZ  LYS C 353      48.792 -50.541  29.727  1.00 34.94           N  
ATOM   5358  N   GLY C 354      41.712 -46.332  30.833  1.00 15.80           N  
ATOM   5359  CA  GLY C 354      41.116 -45.124  31.412  1.00 15.52           C  
ATOM   5360  C   GLY C 354      41.405 -43.820  30.669  1.00 20.49           C  
ATOM   5361  O   GLY C 354      40.920 -42.768  31.089  1.00 19.66           O  
ATOM   5362  N   GLY C 355      42.176 -43.884  29.573  1.00 16.73           N  
ATOM   5363  CA  GLY C 355      42.497 -42.671  28.815  1.00 16.43           C  
ATOM   5364  C   GLY C 355      41.289 -42.186  28.016  1.00 21.63           C  
ATOM   5365  O   GLY C 355      40.430 -42.990  27.636  1.00 21.23           O  
ATOM   5366  N   VAL C 356      41.215 -40.875  27.774  1.00 17.65           N  
ATOM   5367  CA  VAL C 356      40.103 -40.305  26.989  1.00 15.96           C  
ATOM   5368  C   VAL C 356      40.603 -39.608  25.719  1.00 17.66           C  
ATOM   5369  O   VAL C 356      39.896 -38.801  25.160  1.00 17.24           O  
ATOM   5370  CB  VAL C 356      39.205 -39.347  27.846  1.00 19.27           C  
ATOM   5371  CG1 VAL C 356      38.531 -40.099  29.017  1.00 17.95           C  
ATOM   5372  CG2 VAL C 356      40.055 -38.200  28.391  1.00 19.05           C  
ATOM   5373  N   GLY C 357      41.820 -39.920  25.270  1.00 13.90           N  
ATOM   5374  CA  GLY C 357      42.351 -39.335  24.039  1.00 13.65           C  
ATOM   5375  C   GLY C 357      41.345 -39.457  22.903  1.00 19.92           C  
ATOM   5376  O   GLY C 357      40.779 -40.543  22.665  1.00 18.65           O  
ATOM   5377  N   GLN C 358      41.145 -38.347  22.188  1.00 16.80           N  
ATOM   5378  CA  GLN C 358      40.187 -38.280  21.092  1.00 16.58           C  
ATOM   5379  C   GLN C 358      40.480 -39.142  19.862  1.00 20.69           C  
ATOM   5380  O   GLN C 358      41.563 -39.077  19.301  1.00 18.95           O  
ATOM   5381  CB  GLN C 358      39.979 -36.830  20.644  1.00 17.70           C  
ATOM   5382  CG  GLN C 358      38.826 -36.702  19.635  1.00 19.24           C  
ATOM   5383  CD  GLN C 358      38.659 -35.299  19.060  1.00 24.58           C  
ATOM   5384  OE1 GLN C 358      39.628 -34.557  18.943  1.00 21.28           O  
ATOM   5385  NE2 GLN C 358      37.421 -34.933  18.693  1.00 16.03           N  
ATOM   5386  N   PHE C 359      39.487 -39.918  19.428  1.00 18.12           N  
ATOM   5387  CA  PHE C 359      39.580 -40.714  18.192  1.00 18.69           C  
ATOM   5388  C   PHE C 359      38.483 -40.124  17.314  1.00 23.76           C  
ATOM   5389  O   PHE C 359      37.313 -40.353  17.558  1.00 22.84           O  
ATOM   5390  CB  PHE C 359      39.275 -42.187  18.454  1.00 20.78           C  
ATOM   5391  CG  PHE C 359      39.183 -43.048  17.203  1.00 22.34           C  
ATOM   5392  CD1 PHE C 359      39.681 -42.605  15.979  1.00 25.23           C  
ATOM   5393  CD2 PHE C 359      38.626 -44.325  17.266  1.00 23.79           C  
ATOM   5394  CE1 PHE C 359      39.604 -43.411  14.837  1.00 24.73           C  
ATOM   5395  CE2 PHE C 359      38.581 -45.141  16.141  1.00 26.68           C  
ATOM   5396  CZ  PHE C 359      39.093 -44.679  14.922  1.00 23.98           C  
ATOM   5397  N   GLU C 360      38.861 -39.282  16.360  1.00 23.29           N  
ATOM   5398  CA  GLU C 360      37.860 -38.579  15.547  1.00 22.97           C  
ATOM   5399  C   GLU C 360      37.686 -39.144  14.130  1.00 26.21           C  
ATOM   5400  O   GLU C 360      38.671 -39.494  13.453  1.00 25.85           O  
ATOM   5401  CB  GLU C 360      38.166 -37.076  15.515  1.00 24.08           C  
ATOM   5402  CG  GLU C 360      37.038 -36.192  14.921  1.00 31.13           C  
ATOM   5403  CD  GLU C 360      37.308 -34.716  15.132  1.00 38.61           C  
ATOM   5404  OE1 GLU C 360      38.500 -34.321  15.230  1.00 40.18           O  
ATOM   5405  OE2 GLU C 360      36.333 -33.977  15.341  1.00 37.76           O  
ATOM   5406  N   ILE C 361      36.419 -39.250  13.723  1.00 21.22           N  
ATOM   5407  CA  ILE C 361      36.016 -39.704  12.391  1.00 21.08           C  
ATOM   5408  C   ILE C 361      34.969 -38.752  11.824  1.00 27.20           C  
ATOM   5409  O   ILE C 361      33.872 -38.578  12.404  1.00 26.87           O  
ATOM   5410  CB  ILE C 361      35.424 -41.151  12.389  1.00 24.09           C  
ATOM   5411  CG1 ILE C 361      36.470 -42.186  12.852  1.00 23.35           C  
ATOM   5412  CG2 ILE C 361      34.936 -41.510  10.979  1.00 23.99           C  
ATOM   5413  CD1 ILE C 361      35.852 -43.593  13.045  1.00 20.59           C  
ATOM   5414  N   LEU C 362      35.318 -38.129  10.700  1.00 23.77           N  
ATOM   5415  CA  LEU C 362      34.444 -37.174  10.013  1.00 22.14           C  
ATOM   5416  C   LEU C 362      34.193 -37.755   8.632  1.00 27.40           C  
ATOM   5417  O   LEU C 362      35.127 -38.223   7.980  1.00 26.20           O  
ATOM   5418  CB  LEU C 362      35.150 -35.830   9.866  1.00 21.11           C  
ATOM   5419  CG  LEU C 362      35.399 -35.117  11.189  1.00 25.77           C  
ATOM   5420  CD1 LEU C 362      36.328 -33.928  10.937  1.00 27.16           C  
ATOM   5421  CD2 LEU C 362      34.085 -34.615  11.756  1.00 26.86           C  
ATOM   5422  N   TYR C 363      32.930 -37.805   8.221  1.00 24.15           N  
ATOM   5423  CA  TYR C 363      32.611 -38.327   6.898  1.00 24.99           C  
ATOM   5424  C   TYR C 363      31.573 -37.424   6.215  1.00 32.16           C  
ATOM   5425  O   TYR C 363      30.898 -36.624   6.876  1.00 30.17           O  
ATOM   5426  CB  TYR C 363      32.145 -39.796   6.954  1.00 24.56           C  
ATOM   5427  CG  TYR C 363      30.813 -40.006   7.651  1.00 25.91           C  
ATOM   5428  CD1 TYR C 363      29.620 -40.092   6.920  1.00 27.37           C  
ATOM   5429  CD2 TYR C 363      30.737 -40.086   9.044  1.00 26.25           C  
ATOM   5430  CE1 TYR C 363      28.413 -40.271   7.552  1.00 28.33           C  
ATOM   5431  CE2 TYR C 363      29.523 -40.285   9.686  1.00 26.97           C  
ATOM   5432  CZ  TYR C 363      28.365 -40.376   8.941  1.00 36.39           C  
ATOM   5433  OH  TYR C 363      27.159 -40.541   9.589  1.00 36.77           O  
ATOM   5434  N   ALA C 364      31.443 -37.569   4.901  1.00 32.44           N  
ATOM   5435  CA  ALA C 364      30.518 -36.737   4.133  1.00 33.69           C  
ATOM   5436  C   ALA C 364      30.257 -37.308   2.743  1.00 41.64           C  
ATOM   5437  O   ALA C 364      30.978 -38.193   2.285  1.00 41.23           O  
ATOM   5438  CB  ALA C 364      31.052 -35.305   4.021  1.00 33.68           C  
ATOM   5439  N   GLN C 365      29.224 -36.779   2.081  1.00 41.22           N  
ATOM   5440  CA  GLN C 365      28.860 -37.190   0.720  1.00 46.34           C  
ATOM   5441  C   GLN C 365      29.736 -36.422  -0.255  1.00 53.52           C  
ATOM   5442  O   GLN C 365      30.255 -37.073  -1.180  1.00 63.87           O  
ATOM   5443  CB  GLN C 365      27.374 -36.912   0.429  1.00 47.54           C  
ATOM   5444  CG  GLN C 365      26.679 -38.028  -0.336  1.00 66.14           C  
ATOM   5445  CD  GLN C 365      25.202 -37.757  -0.555  1.00 80.64           C  
ATOM   5446  OXT GLN C 365      29.970 -35.219   0.005  1.00 57.96           O  
TER    5447      GLN C 365                                                      
HETATM 5448 MG   BCL A 371      26.510   2.597 -11.349  1.00 23.03          MG  
HETATM 5449  CHA BCL A 371      24.143   3.065 -13.857  1.00 23.26           C  
HETATM 5450  CHB BCL A 371      27.755   5.705 -12.049  1.00 21.60           C  
HETATM 5451  CHC BCL A 371      28.234   2.555  -8.409  1.00 23.15           C  
HETATM 5452  CHD BCL A 371      24.585  -0.115 -10.175  1.00 22.78           C  
HETATM 5453  NA  BCL A 371      25.974   4.167 -12.757  1.00 22.82           N  
HETATM 5454  C1A BCL A 371      25.008   4.141 -13.762  1.00 23.21           C  
HETATM 5455  C2A BCL A 371      25.166   5.330 -14.702  1.00 23.18           C  
HETATM 5456  C3A BCL A 371      26.099   6.269 -13.915  1.00 23.07           C  
HETATM 5457  C4A BCL A 371      26.671   5.379 -12.843  1.00 22.80           C  
HETATM 5458  CMA BCL A 371      27.232   6.845 -14.798  1.00 23.03           C  
HETATM 5459  CAA BCL A 371      23.830   6.040 -15.162  1.00 23.84           C  
HETATM 5460  CBA BCL A 371      23.117   6.870 -14.063  1.00 25.48           C  
HETATM 5461  CGA BCL A 371      22.600   6.021 -12.929  1.00 27.39           C  
HETATM 5462  O1A BCL A 371      21.631   5.247 -13.042  1.00 29.19           O  
HETATM 5463  O2A BCL A 371      23.243   6.085 -11.762  1.00 26.20           O  
HETATM 5464  NB  BCL A 371      27.763   3.925 -10.354  1.00 22.75           N  
HETATM 5465  C1B BCL A 371      28.204   5.158 -10.831  1.00 22.07           C  
HETATM 5466  C2B BCL A 371      29.247   5.658 -10.011  1.00 22.43           C  
HETATM 5467  C3B BCL A 371      29.435   4.733  -8.970  1.00 22.53           C  
HETATM 5468  C4B BCL A 371      28.478   3.675  -9.212  1.00 22.74           C  
HETATM 5469  CMB BCL A 371      30.021   6.966 -10.268  1.00 21.45           C  
HETATM 5470  CAB BCL A 371      30.376   4.793  -7.844  1.00 23.61           C  
HETATM 5471  OBB BCL A 371      30.210   4.185  -6.763  1.00 23.91           O  
HETATM 5472  CBB BCL A 371      31.647   5.605  -7.922  1.00 23.13           C  
HETATM 5473  NC  BCL A 371      26.413   1.411  -9.570  1.00 23.14           N  
HETATM 5474  C1C BCL A 371      27.357   1.466  -8.571  1.00 23.90           C  
HETATM 5475  C2C BCL A 371      27.288   0.308  -7.621  1.00 23.98           C  
HETATM 5476  C3C BCL A 371      25.896  -0.306  -7.974  1.00 24.32           C  
HETATM 5477  C4C BCL A 371      25.664   0.262  -9.369  1.00 23.56           C  
HETATM 5478  CMC BCL A 371      28.483  -0.636  -7.736  1.00 23.18           C  
HETATM 5479  CAC BCL A 371      24.763   0.069  -6.947  1.00 24.30           C  
HETATM 5480  CBC BCL A 371      24.909  -0.622  -5.579  1.00 24.19           C  
HETATM 5481  ND  BCL A 371      24.744   1.641 -11.860  1.00 22.28           N  
HETATM 5482  C1D BCL A 371      24.111   0.501 -11.374  1.00 21.61           C  
HETATM 5483  C2D BCL A 371      23.136   0.043 -12.265  1.00 22.14           C  
HETATM 5484  C3D BCL A 371      23.118   0.980 -13.294  1.00 23.07           C  
HETATM 5485  C4D BCL A 371      24.022   1.971 -12.959  1.00 22.52           C  
HETATM 5486  CMD BCL A 371      22.289  -1.212 -12.099  1.00 20.99           C  
HETATM 5487  CAD BCL A 371      22.407   1.447 -14.433  1.00 23.53           C  
HETATM 5488  OBD BCL A 371      21.527   0.881 -15.107  1.00 24.48           O  
HETATM 5489  CBD BCL A 371      22.979   2.856 -14.839  1.00 23.05           C  
HETATM 5490  CGD BCL A 371      23.385   2.811 -16.253  1.00 24.48           C  
HETATM 5491  O1D BCL A 371      24.287   2.146 -16.711  1.00 24.70           O  
HETATM 5492  O2D BCL A 371      22.656   3.562 -17.067  1.00 26.56           O  
HETATM 5493  CED BCL A 371      23.124   3.789 -18.436  1.00 25.79           C  
HETATM 5494  C1  BCL A 371      23.127   4.909 -10.875  1.00 25.54           C  
HETATM 5495  C2  BCL A 371      24.146   5.146  -9.745  1.00 24.97           C  
HETATM 5496  C3  BCL A 371      24.112   4.311  -8.740  1.00 24.71           C  
HETATM 5497  C4  BCL A 371      23.127   3.156  -8.673  1.00 23.80           C  
HETATM 5498  C5  BCL A 371      25.074   4.429  -7.522  1.00 23.38           C  
HETATM 5499  C6  BCL A 371      25.936   5.704  -7.445  1.00 22.57           C  
HETATM 5500  C7  BCL A 371      26.837   5.688  -6.213  1.00 22.22           C  
HETATM 5501  C8  BCL A 371      27.384   7.061  -5.804  1.00 24.03           C  
HETATM 5502  C9  BCL A 371      28.101   7.816  -7.012  1.00 23.85           C  
HETATM 5503  C10 BCL A 371      28.338   6.896  -4.599  1.00 24.27           C  
HETATM 5504  C11 BCL A 371      27.655   6.385  -3.328  1.00 25.46           C  
HETATM 5505  C12 BCL A 371      26.347   7.177  -2.997  1.00 26.97           C  
HETATM 5506  C13 BCL A 371      25.693   6.659  -1.702  1.00 27.72           C  
HETATM 5507  C14 BCL A 371      26.703   6.646  -0.562  1.00 27.37           C  
HETATM 5508  C15 BCL A 371      25.214   5.195  -1.967  1.00 28.46           C  
HETATM 5509  C16ABCL A 371      23.903   5.059  -2.733  0.48 29.33           C  
HETATM 5510  C16BBCL A 371      23.926   5.117  -2.765  0.52 28.92           C  
HETATM 5511  C17ABCL A 371      23.561   3.693  -3.335  0.48 29.91           C  
HETATM 5512  C17BBCL A 371      23.213   3.773  -2.876  0.52 29.05           C  
HETATM 5513  C18ABCL A 371      22.074   3.566  -3.594  0.48 30.34           C  
HETATM 5514  C18BBCL A 371      22.229   3.793  -4.023  0.52 29.13           C  
HETATM 5515  C19ABCL A 371      21.879   2.061  -3.852  0.48 30.14           C  
HETATM 5516  C19BBCL A 371      20.927   4.288  -3.349  0.52 28.87           C  
HETATM 5517  C20ABCL A 371      21.566   4.418  -4.771  0.48 30.14           C  
HETATM 5518  C20BBCL A 371      22.052   2.406  -4.665  0.52 28.76           C  
HETATM 5519 MG   BCL A 372      15.607  -1.517 -17.246  1.00 20.14          MG  
HETATM 5520  CHA BCL A 372      14.705   1.765 -16.734  1.00 19.77           C  
HETATM 5521  CHB BCL A 372      18.798  -0.691 -16.399  1.00 19.41           C  
HETATM 5522  CHC BCL A 372      16.308  -4.840 -16.699  1.00 18.86           C  
HETATM 5523  CHD BCL A 372      12.227  -2.377 -17.485  1.00 19.23           C  
HETATM 5524  NA  BCL A 372      16.584   0.315 -16.627  1.00 19.93           N  
HETATM 5525  C1A BCL A 372      16.043   1.586 -16.557  1.00 20.13           C  
HETATM 5526  C2A BCL A 372      17.099   2.624 -16.259  1.00 20.08           C  
HETATM 5527  C3A BCL A 372      18.406   1.841 -16.442  1.00 18.83           C  
HETATM 5528  C4A BCL A 372      17.948   0.409 -16.450  1.00 19.23           C  
HETATM 5529  CMA BCL A 372      19.192   2.270 -17.706  1.00 16.72           C  
HETATM 5530  CAA BCL A 372      16.952   3.166 -14.826  1.00 21.57           C  
HETATM 5531  CBA BCL A 372      17.902   4.297 -14.554  1.00 23.01           C  
HETATM 5532  CGA BCL A 372      18.155   4.460 -13.124  1.00 26.06           C  
HETATM 5533  O1A BCL A 372      17.788   5.307 -12.457  1.00 26.41           O  
HETATM 5534  O2A BCL A 372      18.894   3.572 -12.653  1.00 30.14           O  
HETATM 5535  NB  BCL A 372      17.270  -2.597 -16.664  1.00 19.43           N  
HETATM 5536  C1B BCL A 372      18.542  -2.070 -16.455  1.00 19.67           C  
HETATM 5537  C2B BCL A 372      19.497  -3.102 -16.277  1.00 19.94           C  
HETATM 5538  C3B BCL A 372      18.818  -4.314 -16.390  1.00 20.44           C  
HETATM 5539  C4B BCL A 372      17.403  -3.959 -16.603  1.00 19.43           C  
HETATM 5540  CMB BCL A 372      21.000  -2.858 -16.000  1.00 18.91           C  
HETATM 5541  CAB BCL A 372      19.373  -5.676 -16.351  1.00 22.44           C  
HETATM 5542  OBB BCL A 372      18.735  -6.676 -16.812  1.00 23.63           O  
HETATM 5543  CBB BCL A 372      20.770  -5.921 -15.801  1.00 21.36           C  
HETATM 5544  NC  BCL A 372      14.439  -3.336 -17.156  1.00 18.74           N  
HETATM 5545  C1C BCL A 372      14.927  -4.575 -16.772  1.00 19.08           C  
HETATM 5546  C2C BCL A 372      13.892  -5.662 -16.796  1.00 18.32           C  
HETATM 5547  C3C BCL A 372      12.640  -4.942 -17.316  1.00 18.61           C  
HETATM 5548  C4C BCL A 372      13.072  -3.456 -17.230  1.00 19.20           C  
HETATM 5549  CMC BCL A 372      14.260  -6.909 -17.673  1.00 17.91           C  
HETATM 5550  CAC BCL A 372      11.375  -5.269 -16.424  1.00 19.89           C  
HETATM 5551  CBC BCL A 372      10.869  -6.715 -16.504  1.00 19.86           C  
HETATM 5552  ND  BCL A 372      13.828  -0.574 -17.095  1.00 19.92           N  
HETATM 5553  C1D BCL A 372      12.528  -0.975 -17.410  1.00 19.38           C  
HETATM 5554  C2D BCL A 372      11.633   0.121 -17.412  1.00 19.49           C  
HETATM 5555  C3D BCL A 372      12.423   1.235 -17.188  1.00 20.31           C  
HETATM 5556  C4D BCL A 372      13.730   0.779 -16.977  1.00 20.81           C  
HETATM 5557  CMD BCL A 372      10.132   0.032 -17.576  1.00 18.81           C  
HETATM 5558  CAD BCL A 372      12.478   2.657 -17.116  1.00 19.66           C  
HETATM 5559  OBD BCL A 372      11.614   3.500 -17.350  1.00 19.89           O  
HETATM 5560  CBD BCL A 372      13.892   3.073 -16.649  1.00 19.98           C  
HETATM 5561  CGD BCL A 372      14.401   4.165 -17.495  1.00 20.86           C  
HETATM 5562  O1D BCL A 372      14.456   4.087 -18.713  1.00 22.46           O  
HETATM 5563  O2D BCL A 372      14.834   5.258 -16.869  1.00 20.55           O  
HETATM 5564  CED BCL A 372      15.482   6.263 -17.691  1.00 20.01           C  
HETATM 5565  C1  BCL A 372      19.233   3.761 -11.229  1.00 33.51           C  
HETATM 5566  C2  BCL A 372      19.479   2.378 -10.739  1.00 36.60           C  
HETATM 5567  C3  BCL A 372      18.845   2.021  -9.686  1.00 40.39           C  
HETATM 5568  C4  BCL A 372      17.935   2.948  -8.925  1.00 40.93           C  
HETATM 5569  C5  BCL A 372      18.961   0.616  -9.071  1.00 43.43           C  
HETATM 5570  C6  BCL A 372      19.849   0.543  -7.860  1.00 45.45           C  
HETATM 5571  C7  BCL A 372      20.773  -0.642  -7.990  1.00 46.89           C  
HETATM 5572  C8  BCL A 372      20.044  -1.952  -7.847  1.00 46.80           C  
HETATM 5573  C9  BCL A 372      18.734  -1.651  -7.154  1.00 47.28           C  
HETATM 5574  C10 BCL A 372      20.941  -2.788  -6.963  1.00 46.47           C  
HETATM 5575  C11 BCL A 372      22.054  -3.418  -7.783  1.00 46.81           C  
HETATM 5576  C12 BCL A 372      22.270  -4.859  -7.350  1.00 47.18           C  
HETATM 5577  C13 BCL A 372      23.625  -5.457  -7.755  1.00 47.72           C  
HETATM 5578  C14 BCL A 372      23.441  -6.913  -8.227  1.00 47.65           C  
HETATM 5579  C15 BCL A 372      24.324  -5.536  -6.382  1.00 47.49           C  
HETATM 5580  C16 BCL A 372      25.810  -5.689  -6.371  1.00 47.39           C  
HETATM 5581  C17 BCL A 372      26.479  -4.345  -6.103  1.00 46.58           C  
HETATM 5582  C18 BCL A 372      26.906  -4.299  -4.681  1.00 44.96           C  
HETATM 5583  C19 BCL A 372      28.239  -3.567  -4.778  1.00 44.23           C  
HETATM 5584  C20 BCL A 372      27.072  -5.734  -4.196  1.00 44.62           C  
HETATM 5585 MG   BCL A 373       3.389 -13.614 -13.851  1.00 16.81          MG  
HETATM 5586  CHA BCL A 373       5.355 -10.840 -14.478  1.00 15.94           C  
HETATM 5587  CHB BCL A 373       6.252 -15.547 -13.960  1.00 16.89           C  
HETATM 5588  CHC BCL A 373       1.507 -16.411 -13.793  1.00 16.77           C  
HETATM 5589  CHD BCL A 373       0.598 -11.830 -15.062  1.00 13.80           C  
HETATM 5590  NA  BCL A 373       5.498 -13.201 -14.171  1.00 16.91           N  
HETATM 5591  C1A BCL A 373       6.117 -11.976 -14.354  1.00 16.58           C  
HETATM 5592  C2A BCL A 373       7.613 -12.091 -14.205  1.00 15.55           C  
HETATM 5593  C3A BCL A 373       7.864 -13.612 -14.276  1.00 16.89           C  
HETATM 5594  C4A BCL A 373       6.497 -14.196 -14.111  1.00 17.18           C  
HETATM 5595  CMA BCL A 373       8.514 -14.069 -15.621  1.00 17.12           C  
HETATM 5596  CAA BCL A 373       8.139 -11.480 -12.884  1.00 16.32           C  
HETATM 5597  CBA BCL A 373       9.698 -11.280 -13.014  1.00 18.26           C  
HETATM 5598  CGA BCL A 373      10.402 -11.130 -11.724  1.00 19.79           C  
HETATM 5599  O1A BCL A 373      10.524 -11.925 -10.913  1.00 20.20           O  
HETATM 5600  O2A BCL A 373      10.983  -9.963 -11.519  1.00 21.23           O  
HETATM 5601  NB  BCL A 373       3.802 -15.642 -13.828  1.00 18.14           N  
HETATM 5602  C1B BCL A 373       5.050 -16.266 -13.884  1.00 17.33           C  
HETATM 5603  C2B BCL A 373       4.914 -17.660 -13.683  1.00 17.19           C  
HETATM 5604  C3B BCL A 373       3.568 -17.946 -13.682  1.00 18.43           C  
HETATM 5605  C4B BCL A 373       2.886 -16.654 -13.778  1.00 19.12           C  
HETATM 5606  CMB BCL A 373       6.061 -18.622 -13.507  1.00 16.19           C  
HETATM 5607  CAB BCL A 373       2.950 -19.241 -13.564  1.00 18.14           C  
HETATM 5608  OBB BCL A 373       3.561 -20.167 -13.068  1.00 19.41           O  
HETATM 5609  CBB BCL A 373       1.515 -19.500 -13.988  1.00 15.92           C  
HETATM 5610  NC  BCL A 373       1.380 -14.065 -14.376  1.00 15.86           N  
HETATM 5611  C1C BCL A 373       0.791 -15.293 -14.197  1.00 15.48           C  
HETATM 5612  C2C BCL A 373      -0.705 -15.187 -14.081  1.00 14.67           C  
HETATM 5613  C3C BCL A 373      -0.943 -13.899 -14.934  1.00 14.68           C  
HETATM 5614  C4C BCL A 373       0.374 -13.169 -14.755  1.00 14.42           C  
HETATM 5615  CMC BCL A 373      -1.432 -16.403 -14.631  1.00 12.69           C  
HETATM 5616  CAC BCL A 373      -2.239 -13.168 -14.626  1.00 15.02           C  
HETATM 5617  CBC BCL A 373      -2.892 -12.618 -15.896  1.00 15.55           C  
HETATM 5618  ND  BCL A 373       3.005 -11.771 -14.681  1.00 15.16           N  
HETATM 5619  C1D BCL A 373       1.828 -11.092 -14.981  1.00 13.23           C  
HETATM 5620  C2D BCL A 373       2.078  -9.705 -15.240  1.00 13.20           C  
HETATM 5621  C3D BCL A 373       3.433  -9.532 -15.027  1.00 14.72           C  
HETATM 5622  C4D BCL A 373       3.959 -10.780 -14.700  1.00 15.25           C  
HETATM 5623  CMD BCL A 373       1.028  -8.653 -15.656  1.00 12.29           C  
HETATM 5624  CAD BCL A 373       4.547  -8.607 -15.030  1.00 16.72           C  
HETATM 5625  OBD BCL A 373       4.608  -7.388 -15.361  1.00 16.43           O  
HETATM 5626  CBD BCL A 373       5.840  -9.388 -14.651  1.00 16.58           C  
HETATM 5627  CGD BCL A 373       6.899  -9.143 -15.662  1.00 20.38           C  
HETATM 5628  O1D BCL A 373       7.961  -8.531 -15.496  1.00 21.87           O  
HETATM 5629  O2D BCL A 373       6.657  -9.657 -16.862  1.00 20.29           O  
HETATM 5630  CED BCL A 373       7.693  -9.471 -17.853  1.00 19.94           C  
HETATM 5631  C1  BCL A 373      11.308  -9.592 -10.152  1.00 21.23           C  
HETATM 5632  C2  BCL A 373      12.001  -8.284 -10.335  1.00 21.19           C  
HETATM 5633  C3  BCL A 373      12.757  -7.726  -9.434  1.00 21.63           C  
HETATM 5634  C4  BCL A 373      13.050  -8.338  -8.063  1.00 19.85           C  
HETATM 5635  C5  BCL A 373      13.467  -6.365  -9.768  1.00 22.62           C  
HETATM 5636  C6  BCL A 373      13.578  -5.374  -8.634  1.00 23.33           C  
HETATM 5637  C7  BCL A 373      14.288  -4.092  -9.083  1.00 22.93           C  
HETATM 5638  C8 ABCL A 373      14.558  -3.275  -7.814  0.47 20.52           C  
HETATM 5639  C8 BBCL A 373      14.089  -3.060  -7.966  0.53 24.02           C  
HETATM 5640  C9 ABCL A 373      14.677  -1.747  -8.101  0.47 20.20           C  
HETATM 5641  C9 BBCL A 373      14.732  -1.679  -8.273  0.53 23.63           C  
HETATM 5642  C10ABCL A 373      15.821  -3.795  -7.127  0.47 18.81           C  
HETATM 5643  C10BBCL A 373      14.637  -3.637  -6.659  0.53 25.78           C  
HETATM 5644  C11ABCL A 373      15.698  -3.417  -5.630  0.47 17.80           C  
HETATM 5645  C11BBCL A 373      16.082  -3.908  -6.251  0.53 27.40           C  
HETATM 5646  C12ABCL A 373      16.855  -3.907  -4.781  0.47 17.04           C  
HETATM 5647  C12BBCL A 373      16.196  -5.199  -5.404  0.53 28.40           C  
HETATM 5648  C13ABCL A 373      17.225  -5.409  -4.891  0.47 16.97           C  
HETATM 5649  C13BBCL A 373      17.458  -5.258  -4.542  0.53 29.29           C  
HETATM 5650  C14ABCL A 373      16.088  -6.394  -4.553  0.47 15.39           C  
HETATM 5651  C14BBCL A 373      18.084  -3.898  -4.280  0.53 29.84           C  
HETATM 5652  C15ABCL A 373      18.411  -5.590  -3.870  0.47 18.01           C  
HETATM 5653  C15BBCL A 373      18.527  -6.161  -5.179  0.53 29.03           C  
HETATM 5654  C16ABCL A 373      19.812  -6.108  -4.292  0.47 19.06           C  
HETATM 5655  C16BBCL A 373      18.932  -7.175  -4.071  0.53 28.81           C  
HETATM 5656  C17ABCL A 373      20.059  -7.595  -3.926  0.47 19.58           C  
HETATM 5657  C17BBCL A 373      20.333  -6.997  -3.435  0.53 28.27           C  
HETATM 5658  C18ABCL A 373      21.240  -8.423  -4.433  0.47 19.08           C  
HETATM 5659  C18BBCL A 373      20.912  -8.298  -2.849  0.53 27.53           C  
HETATM 5660  C19ABCL A 373      21.589  -9.299  -3.232  0.47 18.11           C  
HETATM 5661  C19BBCL A 373      22.357  -8.349  -3.357  0.53 27.28           C  
HETATM 5662  C20ABCL A 373      22.505  -7.665  -4.876  0.47 19.87           C  
HETATM 5663  C20BBCL A 373      20.134  -9.560  -3.245  0.53 26.59           C  
HETATM 5664 MG   BCL A 374       6.678 -20.848  -6.036  1.00 18.53          MG  
HETATM 5665  CHA BCL A 374       6.005 -24.249  -6.052  1.00 18.36           C  
HETATM 5666  CHB BCL A 374       9.582 -21.524  -4.367  1.00 16.59           C  
HETATM 5667  CHC BCL A 374       7.891 -17.841  -7.051  1.00 16.00           C  
HETATM 5668  CHD BCL A 374       3.838 -20.301  -8.028  1.00 18.20           C  
HETATM 5669  NA  BCL A 374       7.653 -22.679  -5.348  1.00 17.41           N  
HETATM 5670  C1A BCL A 374       7.126 -23.961  -5.328  1.00 17.93           C  
HETATM 5671  C2A BCL A 374       7.955 -24.899  -4.420  1.00 19.29           C  
HETATM 5672  C3A BCL A 374       8.914 -23.905  -3.695  1.00 17.52           C  
HETATM 5673  C4A BCL A 374       8.801 -22.652  -4.533  1.00 17.17           C  
HETATM 5674  CMA BCL A 374       8.494 -23.696  -2.239  1.00 15.75           C  
HETATM 5675  CAA BCL A 374       8.713 -25.968  -5.276  1.00 20.85           C  
HETATM 5676  CBA BCL A 374       9.541 -25.392  -6.471  1.00 21.71           C  
HETATM 5677  CGA BCL A 374       8.753 -25.183  -7.725  1.00 23.94           C  
HETATM 5678  O1A BCL A 374       7.965 -25.923  -8.230  1.00 25.20           O  
HETATM 5679  O2A BCL A 374       8.977 -24.063  -8.326  1.00 24.54           O  
HETATM 5680  NB  BCL A 374       8.483 -19.846  -5.821  1.00 17.74           N  
HETATM 5681  C1B BCL A 374       9.582 -20.298  -5.105  1.00 17.27           C  
HETATM 5682  C2B BCL A 374      10.613 -19.329  -5.133  1.00 18.28           C  
HETATM 5683  C3B BCL A 374      10.172 -18.283  -5.967  1.00 19.15           C  
HETATM 5684  C4B BCL A 374       8.815 -18.637  -6.351  1.00 17.87           C  
HETATM 5685  CMB BCL A 374      11.944 -19.431  -4.306  1.00 16.40           C  
HETATM 5686  CAB BCL A 374      10.851 -17.041  -6.353  1.00 20.81           C  
HETATM 5687  OBB BCL A 374      10.273 -16.123  -6.965  1.00 21.91           O  
HETATM 5688  CBB BCL A 374      12.311 -16.818  -6.049  1.00 21.28           C  
HETATM 5689  NC  BCL A 374       5.953 -19.294  -7.306  1.00 18.39           N  
HETATM 5690  C1C BCL A 374       6.600 -18.099  -7.525  1.00 17.40           C  
HETATM 5691  C2C BCL A 374       5.816 -17.144  -8.371  1.00 17.64           C  
HETATM 5692  C3C BCL A 374       4.429 -17.814  -8.440  1.00 18.57           C  
HETATM 5693  C4C BCL A 374       4.715 -19.222  -7.929  1.00 18.84           C  
HETATM 5694  CMC BCL A 374       5.840 -15.719  -7.829  1.00 16.78           C  
HETATM 5695  CAC BCL A 374       3.743 -17.811  -9.831  1.00 18.56           C  
HETATM 5696  CBC BCL A 374       3.521 -16.406 -10.426  1.00 18.01           C  
HETATM 5697  ND  BCL A 374       5.270 -21.991  -6.933  1.00 18.13           N  
HETATM 5698  C1D BCL A 374       4.106 -21.672  -7.679  1.00 18.32           C  
HETATM 5699  C2D BCL A 374       3.330 -22.839  -7.942  1.00 17.16           C  
HETATM 5700  C3D BCL A 374       4.030 -23.885  -7.348  1.00 17.93           C  
HETATM 5701  C4D BCL A 374       5.167 -23.344  -6.732  1.00 18.23           C  
HETATM 5702  CMD BCL A 374       2.006 -22.878  -8.646  1.00 16.19           C  
HETATM 5703  CAD BCL A 374       4.000 -25.263  -7.004  1.00 19.55           C  
HETATM 5704  OBD BCL A 374       3.199 -26.153  -7.341  1.00 20.48           O  
HETATM 5705  CBD BCL A 374       5.262 -25.596  -6.152  1.00 19.93           C  
HETATM 5706  CGD BCL A 374       4.853 -26.166  -4.855  1.00 21.88           C  
HETATM 5707  O1D BCL A 374       4.291 -25.561  -3.974  1.00 21.95           O  
HETATM 5708  O2D BCL A 374       5.151 -27.448  -4.663  1.00 23.96           O  
HETATM 5709  CED BCL A 374       4.943 -27.926  -3.295  1.00 23.60           C  
HETATM 5710  C1  BCL A 374       8.072 -23.737  -9.424  1.00 24.29           C  
HETATM 5711  C2  BCL A 374       8.775 -22.579 -10.134  1.00 25.74           C  
HETATM 5712  C3  BCL A 374       8.146 -21.447 -10.509  1.00 25.35           C  
HETATM 5713  C4  BCL A 374       6.683 -21.209 -10.313  1.00 24.70           C  
HETATM 5714  C5  BCL A 374       8.883 -20.301 -11.259  1.00 24.18           C  
HETATM 5715  C6  BCL A 374       9.026 -18.990 -10.531  1.00 22.60           C  
HETATM 5716  C7  BCL A 374       9.962 -17.968 -11.176  1.00 21.43           C  
HETATM 5717  C8  BCL A 374       9.794 -16.598 -10.503  1.00 20.94           C  
HETATM 5718  C9  BCL A 374       8.470 -15.918 -10.916  1.00 18.83           C  
HETATM 5719  C10 BCL A 374      10.997 -15.732 -10.919  1.00 22.14           C  
HETATM 5720  C11 BCL A 374      11.431 -15.618 -12.370  1.00 21.95           C  
HETATM 5721  C12 BCL A 374      12.545 -14.578 -12.482  1.00 23.17           C  
HETATM 5722  C13 BCL A 374      12.829 -14.120 -13.930  1.00 23.79           C  
HETATM 5723  C14 BCL A 374      13.173 -15.305 -14.840  1.00 22.69           C  
HETATM 5724  C15 BCL A 374      13.974 -13.102 -13.885  1.00 24.52           C  
HETATM 5725  C16 BCL A 374      13.605 -11.701 -13.378  1.00 25.30           C  
HETATM 5726  C17 BCL A 374      14.863 -10.809 -13.407  1.00 27.26           C  
HETATM 5727  C18 BCL A 374      14.701  -9.332 -13.029  1.00 28.33           C  
HETATM 5728  C19 BCL A 374      13.740  -8.605 -13.982  1.00 27.16           C  
HETATM 5729  C20 BCL A 374      15.976  -8.543 -12.762  1.00 28.41           C  
HETATM 5730 MG   BCL A 375      19.378 -18.571  -1.076  1.00 20.60          MG  
HETATM 5731  CHA BCL A 375      15.906 -18.758  -1.354  1.00 21.14           C  
HETATM 5732  CHB BCL A 375      19.499 -21.861  -2.074  1.00 22.39           C  
HETATM 5733  CHC BCL A 375      22.720 -18.228  -1.688  1.00 22.45           C  
HETATM 5734  CHD BCL A 375      19.138 -15.041  -0.891  1.00 20.39           C  
HETATM 5735  NA  BCL A 375      17.889 -20.085  -1.604  1.00 21.18           N  
HETATM 5736  C1A BCL A 375      16.498 -19.995  -1.496  1.00 20.84           C  
HETATM 5737  C2A BCL A 375      15.850 -21.333  -1.631  1.00 20.47           C  
HETATM 5738  C3A BCL A 375      17.036 -22.313  -1.556  1.00 20.91           C  
HETATM 5739  C4A BCL A 375      18.220 -21.424  -1.774  1.00 21.73           C  
HETATM 5740  CMA BCL A 375      17.161 -22.943  -0.155  1.00 20.91           C  
HETATM 5741  CAA BCL A 375      15.077 -21.428  -2.961  1.00 21.04           C  
HETATM 5742  CBA BCL A 375      14.231 -22.700  -2.943  1.00 21.33           C  
HETATM 5743  CGA BCL A 375      13.432 -22.968  -4.148  1.00 22.71           C  
HETATM 5744  O1A BCL A 375      12.745 -23.855  -4.270  1.00 23.80           O  
HETATM 5745  O2A BCL A 375      13.567 -22.120  -5.131  1.00 23.42           O  
HETATM 5746  NB  BCL A 375      20.862 -19.812  -1.822  1.00 22.85           N  
HETATM 5747  C1B BCL A 375      20.732 -21.176  -2.109  1.00 23.32           C  
HETATM 5748  C2B BCL A 375      22.020 -21.781  -2.247  1.00 23.22           C  
HETATM 5749  C3B BCL A 375      22.965 -20.772  -2.079  1.00 23.81           C  
HETATM 5750  C4B BCL A 375      22.203 -19.526  -1.907  1.00 22.80           C  
HETATM 5751  CMB BCL A 375      22.239 -23.249  -2.577  1.00 22.41           C  
HETATM 5752  CAB BCL A 375      24.404 -20.840  -1.971  1.00 23.46           C  
HETATM 5753  OBB BCL A 375      25.109 -19.863  -2.316  1.00 23.16           O  
HETATM 5754  CBB BCL A 375      25.078 -21.998  -1.284  1.00 22.25           C  
HETATM 5755  NC  BCL A 375      20.709 -16.878  -1.282  1.00 21.26           N  
HETATM 5756  C1C BCL A 375      22.082 -16.985  -1.411  1.00 22.36           C  
HETATM 5757  C2C BCL A 375      22.815 -15.698  -1.152  1.00 22.77           C  
HETATM 5758  C3C BCL A 375      21.666 -14.674  -0.960  1.00 22.62           C  
HETATM 5759  C4C BCL A 375      20.419 -15.538  -1.026  1.00 21.55           C  
HETATM 5760  CMC BCL A 375      23.752 -15.748   0.053  1.00 22.65           C  
HETATM 5761  CAC BCL A 375      21.642 -13.580  -2.082  1.00 23.68           C  
HETATM 5762  CBC BCL A 375      22.786 -12.587  -1.985  1.00 24.11           C  
HETATM 5763  ND  BCL A 375      17.893 -17.170  -1.161  1.00 20.49           N  
HETATM 5764  C1D BCL A 375      17.896 -15.762  -0.966  1.00 21.30           C  
HETATM 5765  C2D BCL A 375      16.580 -15.263  -0.787  1.00 21.08           C  
HETATM 5766  C3D BCL A 375      15.740 -16.396  -0.945  1.00 21.83           C  
HETATM 5767  C4D BCL A 375      16.563 -17.498  -1.186  1.00 20.52           C  
HETATM 5768  CMD BCL A 375      16.216 -13.826  -0.521  1.00 18.95           C  
HETATM 5769  CAD BCL A 375      14.386 -16.887  -0.932  1.00 23.03           C  
HETATM 5770  OBD BCL A 375      13.331 -16.303  -0.638  1.00 23.26           O  
HETATM 5771  CBD BCL A 375      14.403 -18.426  -1.223  1.00 22.16           C  
HETATM 5772  CGD BCL A 375      13.744 -19.116  -0.119  1.00 23.07           C  
HETATM 5773  O1D BCL A 375      12.788 -19.829  -0.179  1.00 23.19           O  
HETATM 5774  O2D BCL A 375      14.301 -18.902   1.055  1.00 24.73           O  
HETATM 5775  CED BCL A 375      13.942 -19.832   2.095  1.00 24.63           C  
HETATM 5776  C1  BCL A 375      12.848 -22.438  -6.364  1.00 23.88           C  
HETATM 5777  C2  BCL A 375      13.569 -21.708  -7.480  1.00 25.50           C  
HETATM 5778  C3  BCL A 375      12.905 -20.974  -8.336  1.00 27.66           C  
HETATM 5779  C4  BCL A 375      11.381 -20.817  -8.301  1.00 28.28           C  
HETATM 5780  C5  BCL A 375      13.590 -20.254  -9.516  1.00 28.08           C  
HETATM 5781  C6  BCL A 375      14.325 -19.002  -9.226  1.00 28.87           C  
HETATM 5782  C7  BCL A 375      15.142 -18.585 -10.397  1.00 29.23           C  
HETATM 5783  C8  BCL A 375      15.474 -17.140 -10.556  1.00 31.81           C  
HETATM 5784  C9  BCL A 375      16.583 -17.072 -11.624  1.00 32.84           C  
HETATM 5785  C10 BCL A 375      16.118 -16.569  -9.297  1.00 34.76           C  
HETATM 5786  C11 BCL A 375      15.340 -15.455  -8.593  1.00 36.40           C  
HETATM 5787  C12 BCL A 375      15.634 -14.096  -9.183  1.00 37.02           C  
HETATM 5788  C13 BCL A 375      14.996 -12.963  -8.360  1.00 37.18           C  
HETATM 5789  C14 BCL A 375      13.457 -12.964  -8.406  1.00 36.22           C  
HETATM 5790  C15 BCL A 375      15.495 -11.735  -9.143  1.00 38.52           C  
HETATM 5791  C16 BCL A 375      16.801 -11.299  -8.516  1.00 39.77           C  
HETATM 5792  C17 BCL A 375      16.777  -9.777  -8.572  1.00 41.25           C  
HETATM 5793  C18 BCL A 375      17.958  -9.149  -7.895  1.00 42.61           C  
HETATM 5794  C19 BCL A 375      17.842  -7.666  -8.280  1.00 43.18           C  
HETATM 5795  C20 BCL A 375      19.263  -9.679  -8.490  1.00 43.13           C  
HETATM 5796 MG   BCL A 376      21.834  -7.175   0.634  1.00 20.66          MG  
HETATM 5797  CHACBCL A 376      23.832  -9.993   1.024  0.37 20.38           C  
HETATM 5798  CHADBCL A 376      23.848  -9.973   1.081  0.63 22.83           C  
HETATM 5799  CHB BCL A 376      24.481  -5.605  -0.869  1.00 19.57           C  
HETATM 5800  CHC BCL A 376      19.666  -4.855  -0.644  1.00 18.99           C  
HETATM 5801  CHD BCL A 376      19.051  -9.104   1.574  1.00 19.60           C  
HETATM 5802  NA  BCL A 376      23.877  -7.765   0.135  1.00 22.32           N  
HETATM 5803  C1A BCL A 376      24.523  -8.971   0.424  1.00 22.36           C  
HETATM 5804  C2A BCL A 376      26.005  -8.917   0.034  1.00 23.87           C  
HETATM 5805  C3A BCL A 376      26.232  -7.427  -0.312  1.00 21.84           C  
HETATM 5806  C4A BCL A 376      24.801  -6.892  -0.467  1.00 21.68           C  
HETATM 5807  CMA BCL A 376      27.055  -6.702   0.761  1.00 18.68           C  
HETATM 5808  CAA BCL A 376      26.299  -9.852  -1.155  1.00 24.83           C  
HETATM 5809  CBA BCL A 376      25.360  -9.716  -2.318  1.00 26.68           C  
HETATM 5810  CGA BCL A 376      25.806 -10.608  -3.445  1.00 30.46           C  
HETATM 5811  O1A BCL A 376      26.777 -11.246  -3.476  1.00 32.41           O  
HETATM 5812  O2A BCL A 376      25.067 -10.686  -4.512  1.00 31.42           O  
HETATM 5813  NB  BCL A 376      22.019  -5.543  -0.614  1.00 20.47           N  
HETATM 5814  C1B BCL A 376      23.223  -4.997  -1.058  1.00 21.01           C  
HETATM 5815  C2B BCL A 376      22.956  -3.802  -1.769  1.00 21.28           C  
HETATM 5816  C3B BCL A 376      21.592  -3.580  -1.724  1.00 20.29           C  
HETATM 5817  C4B BCL A 376      21.039  -4.633  -0.932  1.00 19.92           C  
HETATM 5818  CMB BCL A 376      24.030  -2.968  -2.486  1.00 20.24           C  
HETATM 5819  CAB BCL A 376      20.866  -2.487  -2.309  1.00 22.26           C  
HETATM 5820  OBB BCL A 376      19.618  -2.501  -2.409  1.00 24.14           O  
HETATM 5821  CBB BCL A 376      21.613  -1.247  -2.776  1.00 21.35           C  
HETATM 5822  NC ABCL A 376      19.694  -7.013   0.495  0.47 19.55           N  
HETATM 5823  NC BBCL A 376      19.691  -7.016   0.489  0.53 19.89           N  
HETATM 5824  C1CABCL A 376      19.018  -5.914   0.007  0.47 18.97           C  
HETATM 5825  C1CBBCL A 376      19.012  -5.947  -0.051  0.53 19.35           C  
HETATM 5826  C2CABCL A 376      17.573  -5.878   0.399  0.47 18.47           C  
HETATM 5827  C2CBBCL A 376      17.560  -5.963   0.312  0.53 19.33           C  
HETATM 5828  C3CABCL A 376      17.411  -7.165   1.234  0.47 18.21           C  
HETATM 5829  C3CBBCL A 376      17.325  -7.471   0.523  0.53 19.80           C  
HETATM 5830  C4CABCL A 376      18.760  -7.849   1.068  0.47 19.30           C  
HETATM 5831  C4CBBCL A 376      18.741  -7.936   0.894  0.53 19.97           C  
HETATM 5832  CMCABCL A 376      17.162  -4.606   1.158  0.47 18.02           C  
HETATM 5833  CMCBBCL A 376      17.203  -5.115   1.543  0.53 18.67           C  
HETATM 5834  CACABCL A 376      16.248  -8.051   0.771  0.47 16.65           C  
HETATM 5835  CACBBCL A 376      16.821  -8.045  -0.821  0.53 20.14           C  
HETATM 5836  CBCABCL A 376      16.439  -8.565  -0.640  0.47 16.55           C  
HETATM 5837  CBCBBCL A 376      16.787  -9.547  -0.893  0.53 20.63           C  
HETATM 5838  ND  BCL A 376      21.472  -9.105   1.237  1.00 20.69           N  
HETATM 5839  C1D BCL A 376      20.303  -9.784   1.609  1.00 19.87           C  
HETATM 5840  C2D BCL A 376      20.572 -11.136   1.934  1.00 20.23           C  
HETATM 5841  C3DCBCL A 376      21.970 -11.275   1.789  0.37 19.88           C  
HETATM 5842  C3DDBCL A 376      21.975 -11.262   1.821  0.63 21.65           C  
HETATM 5843  C4DCBCL A 376      22.450 -10.060   1.309  0.37 20.15           C  
HETATM 5844  C4DDBCL A 376      22.457 -10.049   1.345  0.63 21.49           C  
HETATM 5845  CMD BCL A 376      19.524 -12.189   2.300  1.00 17.64           C  
HETATM 5846  CADCBCL A 376      23.074 -12.173   1.781  0.37 19.19           C  
HETATM 5847  CADDBCL A 376      23.115 -12.079   2.062  0.63 23.00           C  
HETATM 5848  OBDCBCL A 376      23.109 -13.418   1.905  0.37 19.25           O  
HETATM 5849  OBDDBCL A 376      23.204 -13.208   2.588  0.63 23.04           O  
HETATM 5850  CBDCBCL A 376      24.365 -11.349   1.488  0.37 18.27           C  
HETATM 5851  CBDDBCL A 376      24.344 -11.384   1.409  0.63 24.04           C  
HETATM 5852  CGDCBCL A 376      25.244 -11.235   2.650  0.37 15.69           C  
HETATM 5853  CGDDBCL A 376      25.615 -11.519   2.128  0.63 26.80           C  
HETATM 5854  O1DCBCL A 376      24.889 -11.435   3.807  0.37 14.80           O  
HETATM 5855  O1DDBCL A 376      26.565 -12.176   1.766  0.63 28.34           O  
HETATM 5856  O2DCBCL A 376      26.479 -10.855   2.297  0.37 14.18           O  
HETATM 5857  O2DDBCL A 376      25.741 -10.840   3.247  0.63 28.23           O  
HETATM 5858  CEDCBCL A 376      27.535 -10.724   3.297  0.37 12.91           C  
HETATM 5859  CEDDBCL A 376      27.142 -10.590   3.625  0.63 27.50           C  
HETATM 5860  C1  BCL A 376      25.090 -11.893  -5.360  1.00 31.74           C  
HETATM 5861  C2  BCL A 376      23.884 -11.710  -6.309  1.00 32.28           C  
HETATM 5862  C3  BCL A 376      23.114 -12.700  -6.692  1.00 33.85           C  
HETATM 5863  C4  BCL A 376      23.280 -14.206  -6.302  1.00 33.03           C  
HETATM 5864  C5  BCL A 376      21.918 -12.416  -7.614  1.00 35.87           C  
HETATM 5865  C6  BCL A 376      20.569 -13.141  -7.283  1.00 36.16           C  
HETATM 5866  C7  BCL A 376      20.284 -13.290  -5.811  1.00 35.73           C  
HETATM 5867  C8  BCL A 376      18.859 -13.817  -5.573  1.00 35.10           C  
HETATM 5868  C9  BCL A 376      18.111 -12.996  -4.488  1.00 34.10           C  
HETATM 5869  C10 BCL A 376      18.997 -15.272  -5.132  1.00 34.68           C  
HETATM 5870  C11 BCL A 376      17.772 -16.067  -5.303  1.00 34.70           C  
HETATM 5871  C12 BCL A 376      18.074 -17.533  -5.023  1.00 34.81           C  
HETATM 5872  C13 BCL A 376      17.216 -18.465  -5.884  1.00 34.57           C  
HETATM 5873  C14 BCL A 376      15.773 -18.439  -5.399  1.00 34.04           C  
HETATM 5874  C15 BCL A 376      17.829 -19.864  -5.656  1.00 34.89           C  
HETATM 5875  C16 BCL A 376      19.340 -19.857  -5.906  1.00 35.08           C  
HETATM 5876  C17 BCL A 376      20.085 -21.178  -6.260  1.00 35.16           C  
HETATM 5877  C18 BCL A 376      21.469 -20.885  -6.879  1.00 34.90           C  
HETATM 5878  C19 BCL A 376      22.075 -22.207  -7.379  1.00 34.49           C  
HETATM 5879  C20 BCL A 376      22.457 -20.075  -6.025  1.00 33.97           C  
HETATM 5880 MG   BCL A 377      10.274  -8.207  -5.544  1.00 15.66          MG  
HETATM 5881  CHA BCL A 377       8.073  -8.170  -8.218  1.00 16.42           C  
HETATM 5882  CHB BCL A 377      10.474  -4.794  -5.765  1.00 15.10           C  
HETATM 5883  CHC BCL A 377      12.922  -8.300  -3.435  1.00 15.62           C  
HETATM 5884  CHD BCL A 377      10.684 -11.659  -6.051  1.00 15.23           C  
HETATM 5885  NA  BCL A 377       9.393  -6.707  -6.848  1.00 16.27           N  
HETATM 5886  C1A BCL A 377       8.478  -6.899  -7.888  1.00 17.42           C  
HETATM 5887  C2A BCL A 377       7.921  -5.570  -8.381  1.00 17.52           C  
HETATM 5888  C3A BCL A 377       8.896  -4.540  -7.765  1.00 16.49           C  
HETATM 5889  C4A BCL A 377       9.611  -5.333  -6.698  1.00 16.33           C  
HETATM 5890  CMA BCL A 377       9.914  -4.060  -8.797  1.00 15.31           C  
HETATM 5891  CAA BCL A 377       6.497  -5.483  -7.845  1.00 18.85           C  
HETATM 5892  CBA BCL A 377       5.682  -4.264  -8.210  1.00 21.38           C  
HETATM 5893  CGA BCL A 377       5.357  -4.059  -9.637  1.00 25.02           C  
HETATM 5894  O1A BCL A 377       4.447  -3.572 -10.025  1.00 28.04           O  
HETATM 5895  O2A BCL A 377       6.213  -4.352 -10.552  1.00 25.62           O  
HETATM 5896  NB  BCL A 377      11.572  -6.787  -4.819  1.00 14.84           N  
HETATM 5897  C1B BCL A 377      11.341  -5.415  -4.840  1.00 14.88           C  
HETATM 5898  C2B BCL A 377      12.018  -4.774  -3.774  1.00 16.00           C  
HETATM 5899  C3BABCL A 377      12.730  -5.749  -3.081  0.47 16.10           C  
HETATM 5900  C3BBBCL A 377      12.762  -5.753  -3.114  0.53 15.84           C  
HETATM 5901  C4B BCL A 377      12.475  -6.998  -3.797  1.00 16.33           C  
HETATM 5902  CMB BCL A 377      11.915  -3.266  -3.468  1.00 15.80           C  
HETATM 5903  CABABCL A 377      13.524  -5.569  -1.860  0.47 16.33           C  
HETATM 5904  CABBBCL A 377      13.651  -5.681  -1.977  0.53 15.56           C  
HETATM 5905  OBBABCL A 377      13.618  -6.436  -0.945  0.47 16.73           O  
HETATM 5906  OBBBBCL A 377      13.970  -6.721  -1.345  0.53 15.63           O  
HETATM 5907  CBBABCL A 377      14.221  -4.250  -1.600  0.47 15.25           C  
HETATM 5908  CBBBBCL A 377      14.207  -4.352  -1.492  0.53 14.38           C  
HETATM 5909  NC  BCL A 377      11.658  -9.737  -4.912  1.00 16.23           N  
HETATM 5910  C1CCBCL A 377      12.551  -9.568  -3.890  0.45 15.53           C  
HETATM 5911  C1CDBCL A 377      12.706  -9.531  -4.053  0.55 15.54           C  
HETATM 5912  C2CCBCL A 377      13.071 -10.861  -3.345  0.45 15.25           C  
HETATM 5913  C2CDBCL A 377      13.602 -10.722  -3.899  0.55 15.31           C  
HETATM 5914  C3CCBCL A 377      12.676 -11.844  -4.464  0.45 15.46           C  
HETATM 5915  C3CDBCL A 377      12.932 -11.780  -4.823  0.55 15.57           C  
HETATM 5916  C4CCBCL A 377      11.555 -11.094  -5.142  0.45 15.90           C  
HETATM 5917  C4CDBCL A 377      11.679 -11.065  -5.296  0.55 15.98           C  
HETATM 5918  CMCCBCL A 377      14.571 -10.835  -3.096  0.45 15.11           C  
HETATM 5919  CMCDBCL A 377      15.076 -10.436  -4.250  0.55 14.17           C  
HETATM 5920  CACCBCL A 377      12.329 -13.275  -3.997  0.45 14.85           C  
HETATM 5921  CACDBCL A 377      12.607 -13.129  -4.115  0.55 15.13           C  
HETATM 5922  CBCCBCL A 377      13.549 -14.167  -3.912  0.45 14.72           C  
HETATM 5923  CBCDBCL A 377      13.843 -13.894  -3.685  0.55 14.96           C  
HETATM 5924  ND  BCL A 377       9.589  -9.624  -6.834  1.00 15.39           N  
HETATM 5925  C1D BCL A 377       9.792 -11.023  -6.931  1.00 15.23           C  
HETATM 5926  C2D BCL A 377       8.918 -11.624  -7.902  1.00 14.80           C  
HETATM 5927  C3D BCL A 377       8.207 -10.546  -8.447  1.00 16.41           C  
HETATM 5928  C4D BCL A 377       8.675  -9.363  -7.820  1.00 15.99           C  
HETATM 5929  CMD BCL A 377       8.784 -13.098  -8.205  1.00 12.43           C  
HETATM 5930  CAD BCL A 377       7.192 -10.148  -9.361  1.00 17.37           C  
HETATM 5931  OBD BCL A 377       6.506 -10.821 -10.149  1.00 18.38           O  
HETATM 5932  CBD BCL A 377       7.084  -8.598  -9.324  1.00 17.21           C  
HETATM 5933  CGD BCL A 377       7.342  -8.075 -10.681  1.00 19.08           C  
HETATM 5934  O1D BCL A 377       6.475  -7.865 -11.480  1.00 19.55           O  
HETATM 5935  O2D BCL A 377       8.611  -7.813 -11.002  1.00 19.75           O  
HETATM 5936  CED BCL A 377       8.833  -7.257 -12.333  1.00 19.75           C  
HETATM 5937  C1  BCL A 377       5.820  -4.393 -11.957  1.00 23.19           C  
HETATM 5938  C2  BCL A 377       7.051  -3.818 -12.697  1.00 20.83           C  
HETATM 5939  C3  BCL A 377       7.412  -4.197 -13.898  1.00 20.11           C  
HETATM 5940  C4  BCL A 377       6.716  -5.248 -14.741  1.00 19.92           C  
HETATM 5941  C5  BCL A 377       8.621  -3.594 -14.609  1.00 21.54           C  
HETATM 5942  C6  BCL A 377       9.404  -2.508 -13.842  1.00 22.75           C  
HETATM 5943  C7  BCL A 377      10.612  -3.123 -13.228  1.00 23.84           C  
HETATM 5944  C8  BCL A 377      11.630  -2.323 -12.408  1.00 24.93           C  
HETATM 5945  C9  BCL A 377      10.974  -1.474 -11.338  1.00 23.66           C  
HETATM 5946  C10 BCL A 377      12.610  -1.567 -13.326  1.00 27.87           C  
HETATM 5947  C11 BCL A 377      13.980  -2.234 -13.133  1.00 29.46           C  
HETATM 5948  C12 BCL A 377      15.042  -1.218 -13.380  1.00 31.07           C  
HETATM 5949  C13 BCL A 377      16.291  -1.437 -12.516  1.00 31.76           C  
HETATM 5950  C14 BCL A 377      17.447  -0.530 -12.913  1.00 30.94           C  
HETATM 5951  C15EBCL A 377      16.791  -2.900 -12.500  0.33 32.18           C  
HETATM 5952  C15FBCL A 377      16.606  -2.937 -12.753  0.67 32.67           C  
HETATM 5953  C16EBCL A 377      18.112  -3.147 -11.741  0.33 32.06           C  
HETATM 5954  C16FBCL A 377      17.946  -3.641 -12.433  0.67 32.54           C  
HETATM 5955  C17EBCL A 377      18.146  -4.432 -10.905  0.33 32.44           C  
HETATM 5956  C17FBCL A 377      17.801  -5.139 -12.718  0.67 33.24           C  
HETATM 5957  C18EBCL A 377      19.530  -5.075 -10.868  0.33 33.07           C  
HETATM 5958  C18FBCL A 377      18.621  -5.856 -11.702  0.67 34.61           C  
HETATM 5959  C19EBCL A 377      20.031  -5.014 -12.318  0.33 32.94           C  
HETATM 5960  C19FBCL A 377      19.469  -4.651 -11.268  0.67 35.47           C  
HETATM 5961  C20EBCL A 377      19.580  -6.530 -10.381  0.33 33.16           C  
HETATM 5962  C20FBCL A 377      19.545  -6.972 -12.207  0.67 34.47           C  
HETATM 5963 MG  BBCL A 378      13.748  -7.718  21.766  1.00 82.38          MG  
HETATM 5964  CHABBCL A 378      15.903  -5.434  20.291  1.00 81.91           C  
HETATM 5965  CHBBBCL A 378      16.444  -9.596  22.625  1.00 83.83           C  
HETATM 5966  CHCBBCL A 378      11.771  -9.409  23.952  1.00 81.01           C  
HETATM 5967  CHDBBCL A 378      11.067  -5.606  21.041  1.00 80.78           C  
HETATM 5968  NA BBCL A 378      15.903  -7.480  21.525  1.00 83.64           N  
HETATM 5969  C1ABBCL A 378      16.573  -6.542  20.740  1.00 83.62           C  
HETATM 5970  C2ABBCL A 378      18.028  -6.894  20.567  1.00 85.17           C  
HETATM 5971  C3ABBCL A 378      18.211  -8.102  21.500  1.00 85.21           C  
HETATM 5972  C4ABBCL A 378      16.800  -8.489  21.860  1.00 84.39           C  
HETATM 5973  CMABBCL A 378      18.981  -9.232  20.803  1.00 85.49           C  
HETATM 5974  CAABBCL A 378      18.974  -5.728  20.900  1.00 86.76           C  
HETATM 5975  CBABBCL A 378      19.085  -5.443  22.406  1.00 88.68           C  
HETATM 5976  CGABBCL A 378      20.488  -5.239  22.877  1.00 90.55           C  
HETATM 5977  O1ABBCL A 378      20.830  -4.489  23.771  1.00 91.00           O  
HETATM 5978  O2ABBCL A 378      21.365  -5.983  22.197  1.00 91.25           O  
HETATM 5979  NB BBCL A 378      14.060  -9.194  23.183  1.00 82.09           N  
HETATM 5980  C1BBBCL A 378      15.185 -10.016  23.161  1.00 82.87           C  
HETATM 5981  C2BBBCL A 378      14.886 -11.283  23.707  1.00 82.46           C  
HETATM 5982  C3BBBCL A 378      13.528 -11.292  24.046  1.00 81.22           C  
HETATM 5983  C4BBBCL A 378      13.065  -9.930  23.775  1.00 81.30           C  
HETATM 5984  CMBBBCL A 378      15.932 -12.376  23.902  1.00 83.05           C  
HETATM 5985  CABBBCL A 378      12.749 -12.427  24.567  1.00 80.43           C  
HETATM 5986  OBBBBCL A 378      11.541 -12.661  24.297  1.00 79.48           O  
HETATM 5987  CBBBBCL A 378      13.420 -13.431  25.476  1.00 80.58           C  
HETATM 5988  NC BBCL A 378      11.731  -7.471  22.472  1.00 81.28           N  
HETATM 5989  C1CBBCL A 378      11.091  -8.374  23.276  1.00 80.74           C  
HETATM 5990  C2CBBCL A 378       9.613  -8.267  23.216  1.00 80.04           C  
HETATM 5991  C3CBBCL A 378       9.389  -7.178  22.162  1.00 79.95           C  
HETATM 5992  C4CBBCL A 378      10.775  -6.644  21.925  1.00 80.60           C  
HETATM 5993  CMCBBCL A 378       8.917  -9.598  22.927  1.00 79.64           C  
HETATM 5994  CACBBCL A 378       8.474  -6.109  22.760  1.00 79.62           C  
HETATM 5995  CBCBBCL A 378       8.487  -6.163  24.274  1.00 79.50           C  
HETATM 5996  ND BBCL A 378      13.500  -5.870  20.944  1.00 81.34           N  
HETATM 5997  C1DBBCL A 378      12.351  -5.155  20.578  1.00 80.67           C  
HETATM 5998  C2DBBCL A 378      12.671  -4.061  19.737  1.00 79.75           C  
HETATM 5999  C3DBBCL A 378      14.057  -4.072  19.640  1.00 80.12           C  
HETATM 6000  C4DBBCL A 378      14.511  -5.200  20.314  1.00 81.12           C  
HETATM 6001  CMDBBCL A 378      11.691  -3.131  19.100  1.00 79.40           C  
HETATM 6002  CADBBCL A 378      15.210  -3.313  19.333  1.00 80.29           C  
HETATM 6003  OBDBBCL A 378      15.310  -2.131  18.967  1.00 80.47           O  
HETATM 6004  CBDBBCL A 378      16.471  -4.201  19.595  1.00 80.83           C  
HETATM 6005  CGDBBCL A 378      17.292  -4.474  18.391  1.00 80.39           C  
HETATM 6006  O1DBBCL A 378      18.351  -3.922  18.136  1.00 80.28           O  
HETATM 6007  O2DBBCL A 378      16.792  -5.408  17.582  1.00 79.70           O  
HETATM 6008  CEDBBCL A 378      17.600  -5.914  16.479  1.00 79.23           C  
HETATM 6009 MG   BCL C 371      14.202 -52.217  47.723  1.00 23.85          MG  
HETATM 6010  CHA BCL C 371      16.640 -54.664  48.198  1.00 24.98           C  
HETATM 6011  CHB BCL C 371      13.034 -52.903  50.866  1.00 22.98           C  
HETATM 6012  CHC BCL C 371      12.384 -49.345  47.649  1.00 24.37           C  
HETATM 6013  CHD BCL C 371      15.990 -51.096  44.909  1.00 23.87           C  
HETATM 6014  NA  BCL C 371      14.791 -53.613  49.314  1.00 23.62           N  
HETATM 6015  C1A BCL C 371      15.816 -54.546  49.316  1.00 24.82           C  
HETATM 6016  C2A BCL C 371      15.704 -55.481  50.511  1.00 24.55           C  
HETATM 6017  C3A BCL C 371      14.782 -54.693  51.453  1.00 24.50           C  
HETATM 6018  C4A BCL C 371      14.154 -53.664  50.545  1.00 24.12           C  
HETATM 6019  CMA BCL C 371      13.726 -55.606  52.132  1.00 23.77           C  
HETATM 6020  CAA BCL C 371      17.046 -55.880  51.182  1.00 25.22           C  
HETATM 6021  CBA BCL C 371      17.774 -54.729  51.982  1.00 26.45           C  
HETATM 6022  CGA BCL C 371      18.250 -53.623  51.105  1.00 28.47           C  
HETATM 6023  O1A BCL C 371      19.112 -53.712  50.336  1.00 30.57           O  
HETATM 6024  O2A BCL C 371      17.592 -52.474  51.129  1.00 28.04           O  
HETATM 6025  NB  BCL C 371      12.956 -51.218  49.069  1.00 24.40           N  
HETATM 6026  C1B BCL C 371      12.561 -51.684  50.326  1.00 23.60           C  
HETATM 6027  C2B BCL C 371      11.518 -50.871  50.854  1.00 23.90           C  
HETATM 6028  C3B BCL C 371      11.283 -49.854  49.928  1.00 23.96           C  
HETATM 6029  C4B BCL C 371      12.212 -50.105  48.818  1.00 24.06           C  
HETATM 6030  CMB BCL C 371      10.781 -51.141  52.207  1.00 22.42           C  
HETATM 6031  CAB BCL C 371      10.329 -48.741  50.021  1.00 24.42           C  
HETATM 6032  OBB BCL C 371      10.479 -47.704  49.340  1.00 25.01           O  
HETATM 6033  CBB BCL C 371       9.068 -48.832  50.873  1.00 23.10           C  
HETATM 6034  NC  BCL C 371      14.239 -50.465  46.498  1.00 24.49           N  
HETATM 6035  C1C BCL C 371      13.285 -49.471  46.564  1.00 25.04           C  
HETATM 6036  C2C BCL C 371      13.296 -48.564  45.390  1.00 25.07           C  
HETATM 6037  C3C BCL C 371      14.649 -48.916  44.722  1.00 25.68           C  
HETATM 6038  C4C BCL C 371      14.966 -50.262  45.340  1.00 24.77           C  
HETATM 6039  CMC BCL C 371      12.064 -48.750  44.480  1.00 24.45           C  
HETATM 6040  CAC BCL C 371      15.785 -47.834  44.992  1.00 25.80           C  
HETATM 6041  CBC BCL C 371      15.583 -46.517  44.231  1.00 25.69           C  
HETATM 6042  ND  BCL C 371      15.942 -52.703  46.743  1.00 23.44           N  
HETATM 6043  C1D BCL C 371      16.461 -52.303  45.510  1.00 23.24           C  
HETATM 6044  C2D BCL C 371      17.495 -53.170  45.072  1.00 23.49           C  
HETATM 6045  C3D BCL C 371      17.569 -54.166  46.054  1.00 24.45           C  
HETATM 6046  C4D BCL C 371      16.694 -53.800  47.070  1.00 24.09           C  
HETATM 6047  CMD BCL C 371      18.323 -52.999  43.816  1.00 21.91           C  
HETATM 6048  CAD BCL C 371      18.345 -55.243  46.567  1.00 25.27           C  
HETATM 6049  OBD BCL C 371      19.324 -55.841  46.058  1.00 26.91           O  
HETATM 6050  CBD BCL C 371      17.805 -55.634  47.970  1.00 24.47           C  
HETATM 6051  CGD BCL C 371      17.441 -57.056  47.996  1.00 25.85           C  
HETATM 6052  O1D BCL C 371      16.500 -57.526  47.366  1.00 25.69           O  
HETATM 6053  O2D BCL C 371      18.220 -57.827  48.775  1.00 27.14           O  
HETATM 6054  CED BCL C 371      17.801 -59.212  48.956  1.00 26.39           C  
HETATM 6055  C1  BCL C 371      17.623 -51.621  49.934  1.00 27.05           C  
HETATM 6056  C2  BCL C 371      16.579 -50.527  50.168  1.00 26.50           C  
HETATM 6057  C3  BCL C 371      16.546 -49.508  49.307  1.00 26.35           C  
HETATM 6058  C4  BCL C 371      17.505 -49.390  48.103  1.00 25.43           C  
HETATM 6059  C5  BCL C 371      15.563 -48.328  49.409  1.00 24.60           C  
HETATM 6060  C6  BCL C 371      14.807 -48.185  50.727  1.00 23.98           C  
HETATM 6061  C7  BCL C 371      13.807 -47.034  50.700  1.00 23.16           C  
HETATM 6062  C8  BCL C 371      13.319 -46.601  52.069  1.00 24.88           C  
HETATM 6063  C9  BCL C 371      12.641 -47.786  52.875  1.00 25.49           C  
HETATM 6064  C10 BCL C 371      12.325 -45.430  51.928  1.00 25.52           C  
HETATM 6065  C11 BCL C 371      12.997 -44.154  51.369  1.00 27.19           C  
HETATM 6066  C12 BCL C 371      14.309 -43.766  52.113  1.00 28.16           C  
HETATM 6067  C13 BCL C 371      14.926 -42.477  51.543  1.00 29.21           C  
HETATM 6068  C14 BCL C 371      13.853 -41.378  51.496  1.00 29.00           C  
HETATM 6069  C15 BCL C 371      15.360 -42.758  50.067  1.00 30.01           C  
HETATM 6070  C16ABCL C 371      16.681 -43.499  49.916  0.48 30.70           C  
HETATM 6071  C16BBCL C 371      16.668 -43.522  49.967  0.52 30.27           C  
HETATM 6072  C17ABCL C 371      17.012 -44.111  48.542  0.48 31.14           C  
HETATM 6073  C17BBCL C 371      17.342 -43.666  48.586  0.52 30.25           C  
HETATM 6074  C18ABCL C 371      18.492 -44.350  48.387  0.48 31.45           C  
HETATM 6075  C18BBCL C 371      18.344 -44.790  48.620  0.52 30.21           C  
HETATM 6076  C19ABCL C 371      18.658 -44.652  46.886  0.48 31.63           C  
HETATM 6077  C19BBCL C 371      19.634 -44.085  49.077  0.52 30.14           C  
HETATM 6078  C20ABCL C 371      19.052 -45.499  49.240  0.48 31.35           C  
HETATM 6079  C20BBCL C 371      18.505 -45.501  47.266  0.52 30.10           C  
HETATM 6080 MG   BCL C 372      25.139 -58.006  43.456  1.00 21.09          MG  
HETATM 6081  CHA BCL C 372      26.114 -57.334  46.717  1.00 20.89           C  
HETATM 6082  CHB BCL C 372      21.957 -57.216  44.362  1.00 20.39           C  
HETATM 6083  CHC BCL C 372      24.307 -57.589  40.177  1.00 20.27           C  
HETATM 6084  CHD BCL C 372      28.501 -58.193  42.523  1.00 19.63           C  
HETATM 6085  NA  BCL C 372      24.188 -57.321  45.305  1.00 21.28           N  
HETATM 6086  C1A BCL C 372      24.752 -57.269  46.579  1.00 21.29           C  
HETATM 6087  C2A BCL C 372      23.718 -56.927  47.628  1.00 21.52           C  
HETATM 6088  C3A BCL C 372      22.389 -57.128  46.884  1.00 20.45           C  
HETATM 6089  C4A BCL C 372      22.814 -57.202  45.433  1.00 20.48           C  
HETATM 6090  CMA BCL C 372      21.678 -58.399  47.385  1.00 18.89           C  
HETATM 6091  CAA BCL C 372      23.879 -55.508  48.164  1.00 22.88           C  
HETATM 6092  CBA BCL C 372      22.935 -55.229  49.324  1.00 24.77           C  
HETATM 6093  CGA BCL C 372      22.583 -53.797  49.468  1.00 27.46           C  
HETATM 6094  O1A BCL C 372      22.948 -53.039  50.308  1.00 27.66           O  
HETATM 6095  O2A BCL C 372      21.827 -53.398  48.576  1.00 31.59           O  
HETATM 6096  NB  BCL C 372      23.420 -57.499  42.410  1.00 20.39           N  
HETATM 6097  C1B BCL C 372      22.177 -57.265  42.973  1.00 20.56           C  
HETATM 6098  C2B BCL C 372      21.186 -57.122  41.955  1.00 21.34           C  
HETATM 6099  C3B BCL C 372      21.833 -57.262  40.731  1.00 21.81           C  
HETATM 6100  C4B BCL C 372      23.257 -57.396  41.060  1.00 20.72           C  
HETATM 6101  CMB BCL C 372      19.687 -56.894  42.232  1.00 19.82           C  
HETATM 6102  CAB BCL C 372      21.225 -57.306  39.393  1.00 23.64           C  
HETATM 6103  OBB BCL C 372      21.816 -57.783  38.385  1.00 24.30           O  
HETATM 6104  CBB BCL C 372      19.817 -56.776  39.169  1.00 22.68           C  
HETATM 6105  NC  BCL C 372      26.240 -57.979  41.634  1.00 20.09           N  
HETATM 6106  C1C BCL C 372      25.709 -57.647  40.406  1.00 20.64           C  
HETATM 6107  C2C BCL C 372      26.717 -57.624  39.297  1.00 18.98           C  
HETATM 6108  C3C BCL C 372      28.010 -58.063  40.003  1.00 19.78           C  
HETATM 6109  C4C BCL C 372      27.620 -57.989  41.478  1.00 20.10           C  
HETATM 6110  CMC BCL C 372      26.315 -58.556  38.150  1.00 18.79           C  
HETATM 6111  CAC BCL C 372      29.302 -57.209  39.626  1.00 20.97           C  
HETATM 6112  CBC BCL C 372      29.746 -57.246  38.165  1.00 21.13           C  
HETATM 6113  ND  BCL C 372      26.949 -57.735  44.355  1.00 21.07           N  
HETATM 6114  C1D BCL C 372      28.257 -57.999  43.914  1.00 20.38           C  
HETATM 6115  C2D BCL C 372      29.184 -57.945  44.976  1.00 20.89           C  
HETATM 6116  C3D BCL C 372      28.390 -57.726  46.136  1.00 21.82           C  
HETATM 6117  C4D BCL C 372      27.074 -57.568  45.710  1.00 21.47           C  
HETATM 6118  CMD BCL C 372      30.683 -58.117  44.856  1.00 19.39           C  
HETATM 6119  CAD BCL C 372      28.365 -57.663  47.563  1.00 21.06           C  
HETATM 6120  OBD BCL C 372      29.263 -57.909  48.402  1.00 21.16           O  
HETATM 6121  CBD BCL C 372      26.942 -57.219  48.005  1.00 21.13           C  
HETATM 6122  CGD BCL C 372      26.488 -58.073  49.111  1.00 21.68           C  
HETATM 6123  O1D BCL C 372      26.474 -59.265  49.092  1.00 23.05           O  
HETATM 6124  O2D BCL C 372      26.072 -57.450  50.196  1.00 22.39           O  
HETATM 6125  CED BCL C 372      25.463 -58.279  51.241  1.00 21.48           C  
HETATM 6126  C1  BCL C 372      21.525 -51.944  48.706  1.00 35.15           C  
HETATM 6127  C2  BCL C 372      21.259 -51.481  47.290  1.00 37.89           C  
HETATM 6128  C3  BCL C 372      21.848 -50.414  46.910  1.00 41.44           C  
HETATM 6129  C4  BCL C 372      22.754 -49.604  47.781  1.00 42.05           C  
HETATM 6130  C5  BCL C 372      21.666 -49.832  45.499  1.00 44.75           C  
HETATM 6131  C6  BCL C 372      20.724 -48.638  45.422  1.00 46.73           C  
HETATM 6132  C7  BCL C 372      19.767 -48.843  44.280  1.00 48.19           C  
HETATM 6133  C8  BCL C 372      20.452 -48.695  42.951  1.00 48.43           C  
HETATM 6134  C9  BCL C 372      21.776 -47.949  43.207  1.00 48.94           C  
HETATM 6135  C10 BCL C 372      19.505 -47.865  42.097  1.00 47.86           C  
HETATM 6136  C11 BCL C 372      18.447 -48.769  41.500  1.00 47.99           C  
HETATM 6137  C12 BCL C 372      18.175 -48.379  40.059  1.00 48.35           C  
HETATM 6138  C13 BCL C 372      16.802 -48.803  39.531  1.00 48.76           C  
HETATM 6139  C14 BCL C 372      16.944 -49.318  38.103  1.00 48.81           C  
HETATM 6140  C15 BCL C 372      16.056 -47.467  39.440  1.00 48.78           C  
HETATM 6141  C16 BCL C 372      14.567 -47.450  39.316  1.00 48.74           C  
HETATM 6142  C17 BCL C 372      13.923 -47.179  40.676  1.00 47.90           C  
HETATM 6143  C18 BCL C 372      13.451 -45.758  40.683  1.00 46.28           C  
HETATM 6144  C19 BCL C 372      12.123 -45.846  41.425  1.00 45.42           C  
HETATM 6145  C20 BCL C 372      13.239 -45.348  39.227  1.00 45.88           C  
HETATM 6146 MG   BCL C 373      36.962 -54.656  30.982  1.00 18.22          MG  
HETATM 6147  CHA BCL C 373      35.068 -55.259  33.819  1.00 17.57           C  
HETATM 6148  CHB BCL C 373      34.070 -54.848  29.133  1.00 18.65           C  
HETATM 6149  CHC BCL C 373      38.778 -54.613  28.105  1.00 17.98           C  
HETATM 6150  CHD BCL C 373      39.805 -55.702  32.720  1.00 15.06           C  
HETATM 6151  NA  BCL C 373      34.848 -54.966  31.462  1.00 18.36           N  
HETATM 6152  C1A BCL C 373      34.260 -55.184  32.710  1.00 18.16           C  
HETATM 6153  C2A BCL C 373      32.749 -55.068  32.632  1.00 16.80           C  
HETATM 6154  C3A BCL C 373      32.481 -55.171  31.125  1.00 17.99           C  
HETATM 6155  C4A BCL C 373      33.850 -55.025  30.499  1.00 18.68           C  
HETATM 6156  CMA BCL C 373      31.862 -56.514  30.706  1.00 18.95           C  
HETATM 6157  CAA BCL C 373      32.212 -53.767  33.215  1.00 17.21           C  
HETATM 6158  CBA BCL C 373      30.675 -53.909  33.469  1.00 19.52           C  
HETATM 6159  CGA BCL C 373      29.971 -52.594  33.593  1.00 21.15           C  
HETATM 6160  O1A BCL C 373      29.836 -51.768  32.733  1.00 21.05           O  
HETATM 6161  O2A BCL C 373      29.435 -52.382  34.760  1.00 22.44           O  
HETATM 6162  NB  BCL C 373      36.492 -54.784  28.961  1.00 19.49           N  
HETATM 6163  C1B BCL C 373      35.226 -54.775  28.389  1.00 18.52           C  
HETATM 6164  C2B BCL C 373      35.319 -54.641  26.978  1.00 18.77           C  
HETATM 6165  C3B BCL C 373      36.663 -54.633  26.646  1.00 19.58           C  
HETATM 6166  C4B BCL C 373      37.383 -54.688  27.908  1.00 20.11           C  
HETATM 6167  CMB BCL C 373      34.129 -54.518  26.037  1.00 17.53           C  
HETATM 6168  CAB BCL C 373      37.242 -54.528  25.300  1.00 19.33           C  
HETATM 6169  OBB BCL C 373      36.588 -54.075  24.355  1.00 20.37           O  
HETATM 6170  CBB BCL C 373      38.679 -54.887  25.016  1.00 15.99           C  
HETATM 6171  NC  BCL C 373      38.980 -55.095  30.497  1.00 17.46           N  
HETATM 6172  C1C BCL C 373      39.544 -54.924  29.241  1.00 17.07           C  
HETATM 6173  C2C BCL C 373      41.036 -54.822  29.309  1.00 15.76           C  
HETATM 6174  C3C BCL C 373      41.298 -55.658  30.573  1.00 15.63           C  
HETATM 6175  C4C BCL C 373      39.999 -55.438  31.362  1.00 15.89           C  
HETATM 6176  CMC BCL C 373      41.766 -55.348  28.073  1.00 14.13           C  
HETATM 6177  CAC BCL C 373      42.611 -55.261  31.299  1.00 15.96           C  
HETATM 6178  CBC BCL C 373      43.282 -56.529  31.817  1.00 16.47           C  
HETATM 6179  ND  BCL C 373      37.392 -55.418  32.826  1.00 16.32           N  
HETATM 6180  C1D BCL C 373      38.598 -55.689  33.478  1.00 14.65           C  
HETATM 6181  C2D BCL C 373      38.395 -55.898  34.890  1.00 14.28           C  
HETATM 6182  C3D BCL C 373      37.025 -55.762  35.067  1.00 16.02           C  
HETATM 6183  C4D BCL C 373      36.464 -55.473  33.831  1.00 16.36           C  
HETATM 6184  CMD BCL C 373      39.476 -56.226  35.943  1.00 12.51           C  
HETATM 6185  CAD BCL C 373      35.954 -55.749  36.017  1.00 17.69           C  
HETATM 6186  OBD BCL C 373      35.952 -56.042  37.218  1.00 17.93           O  
HETATM 6187  CBD BCL C 373      34.654 -55.391  35.292  1.00 18.25           C  
HETATM 6188  CGD BCL C 373      33.632 -56.411  35.603  1.00 21.65           C  
HETATM 6189  O1D BCL C 373      32.626 -56.207  36.252  1.00 23.27           O  
HETATM 6190  O2D BCL C 373      33.872 -57.620  35.125  1.00 22.34           O  
HETATM 6191  CED BCL C 373      32.855 -58.664  35.376  1.00 21.36           C  
HETATM 6192  C1  BCL C 373      29.093 -50.995  35.103  1.00 22.75           C  
HETATM 6193  C2  BCL C 373      28.408 -51.161  36.456  1.00 22.41           C  
HETATM 6194  C3  BCL C 373      27.657 -50.257  37.021  1.00 22.90           C  
HETATM 6195  C4  BCL C 373      27.321 -48.920  36.391  1.00 21.60           C  
HETATM 6196  C5  BCL C 373      26.966 -50.552  38.406  1.00 23.97           C  
HETATM 6197  C6  BCL C 373      26.941 -49.441  39.416  1.00 24.74           C  
HETATM 6198  C7  BCL C 373      26.189 -49.862  40.690  1.00 24.01           C  
HETATM 6199  C8 ABCL C 373      25.930 -48.584  41.460  0.47 21.74           C  
HETATM 6200  C8 BBCL C 373      26.415 -48.724  41.666  0.53 25.13           C  
HETATM 6201  C9 ABCL C 373      25.849 -48.833  42.978  0.47 21.48           C  
HETATM 6202  C9 BBCL C 373      25.793 -49.003  43.045  0.53 24.94           C  
HETATM 6203  C10ABCL C 373      24.638 -47.927  40.947  0.47 20.19           C  
HETATM 6204  C10BBCL C 373      25.808 -47.467  41.043  0.53 27.21           C  
HETATM 6205  C11ABCL C 373      24.734 -46.422  41.288  0.47 19.17           C  
HETATM 6206  C11BBCL C 373      24.348 -47.097  40.807  0.53 28.73           C  
HETATM 6207  C12ABCL C 373      23.534 -45.615  40.798  0.47 18.77           C  
HETATM 6208  C12BBCL C 373      24.189 -46.241  39.529  0.53 29.73           C  
HETATM 6209  C13ABCL C 373      23.132 -45.748  39.309  0.47 18.39           C  
HETATM 6210  C13BBCL C 373      22.892 -45.407  39.465  0.53 30.52           C  
HETATM 6211  C14ABCL C 373      24.248 -45.339  38.324  0.47 16.67           C  
HETATM 6212  C14BBCL C 373      22.281 -45.142  40.838  0.53 31.16           C  
HETATM 6213  C15ABCL C 373      21.935 -44.785  39.122  0.47 19.10           C  
HETATM 6214  C15BBCL C 373      21.827 -46.084  38.598  0.53 30.04           C  
HETATM 6215  C16ABCL C 373      20.541 -45.253  38.653  0.47 20.32           C  
HETATM 6216  C16BBCL C 373      21.357 -45.077  37.564  0.53 29.94           C  
HETATM 6217  C17ABCL C 373      20.245 -44.924  37.170  0.47 20.84           C  
HETATM 6218  C17BBCL C 373      19.965 -44.431  37.777  0.53 29.56           C  
HETATM 6219  C18ABCL C 373      19.035 -45.484  36.415  0.47 20.33           C  
HETATM 6220  C18BBCL C 373      19.332 -43.865  36.504  0.53 28.85           C  
HETATM 6221  C19ABCL C 373      18.628 -44.305  35.517  0.47 19.41           C  
HETATM 6222  C19BBCL C 373      17.900 -44.421  36.490  0.53 28.75           C  
HETATM 6223  C20ABCL C 373      17.830 -45.925  37.267  0.47 20.96           C  
HETATM 6224  C20BBCL C 373      20.069 -44.259  35.224  0.53 28.28           C  
HETATM 6225 MG   BCL C 374      33.257 -47.112  23.629  1.00 19.44          MG  
HETATM 6226  CHA BCL C 374      33.896 -47.167  20.236  1.00 19.33           C  
HETATM 6227  CHB BCL C 374      30.324 -45.592  22.999  1.00 17.69           C  
HETATM 6228  CHC BCL C 374      32.148 -48.136  26.698  1.00 17.32           C  
HETATM 6229  CHD BCL C 374      36.176 -48.971  24.196  1.00 19.17           C  
HETATM 6230  NA  BCL C 374      32.254 -46.501  21.823  1.00 18.34           N  
HETATM 6231  C1A BCL C 374      32.765 -46.457  20.542  1.00 18.70           C  
HETATM 6232  C2A BCL C 374      31.878 -45.643  19.617  1.00 20.18           C  
HETATM 6233  C3A BCL C 374      30.940 -44.938  20.580  1.00 18.76           C  
HETATM 6234  C4A BCL C 374      31.080 -45.763  21.849  1.00 18.60           C  
HETATM 6235  CMA BCL C 374      31.354 -43.472  20.727  1.00 17.27           C  
HETATM 6236  CAA BCL C 374      31.121 -46.524  18.577  1.00 21.89           C  
HETATM 6237  CBA BCL C 374      30.328 -47.727  19.160  1.00 22.78           C  
HETATM 6238  CGA BCL C 374      31.153 -48.933  19.427  1.00 25.16           C  
HETATM 6239  O1A BCL C 374      31.971 -49.398  18.669  1.00 27.16           O  
HETATM 6240  O2A BCL C 374      30.947 -49.520  20.564  1.00 25.06           O  
HETATM 6241  NB  BCL C 374      31.476 -46.971  24.663  1.00 19.33           N  
HETATM 6242  C1B BCL C 374      30.382 -46.216  24.255  1.00 18.53           C  
HETATM 6243  C2B BCL C 374      29.384 -46.234  25.263  1.00 19.63           C  
HETATM 6244  C3B BCL C 374      29.884 -46.994  26.322  1.00 20.17           C  
HETATM 6245  C4B BCL C 374      31.208 -47.426  25.917  1.00 19.02           C  
HETATM 6246  CMB BCL C 374      28.023 -45.503  25.203  1.00 18.25           C  
HETATM 6247  CAB BCL C 374      29.256 -47.358  27.574  1.00 22.39           C  
HETATM 6248  OBB BCL C 374      29.864 -48.020  28.437  1.00 24.09           O  
HETATM 6249  CBB BCL C 374      27.779 -47.094  27.849  1.00 23.34           C  
HETATM 6250  NC  BCL C 374      34.078 -48.324  25.233  1.00 20.04           N  
HETATM 6251  C1C BCL C 374      33.455 -48.550  26.439  1.00 19.07           C  
HETATM 6252  C2C BCL C 374      34.289 -49.348  27.387  1.00 19.06           C  
HETATM 6253  C3C BCL C 374      35.680 -49.335  26.684  1.00 20.08           C  
HETATM 6254  C4C BCL C 374      35.347 -48.871  25.296  1.00 19.65           C  
HETATM 6255  CMC BCL C 374      34.310 -48.758  28.822  1.00 18.37           C  
HETATM 6256  CAC BCL C 374      36.403 -50.713  26.729  1.00 20.66           C  
HETATM 6257  CBC BCL C 374      36.627 -51.288  28.114  1.00 19.92           C  
HETATM 6258  ND  BCL C 374      34.671 -48.001  22.490  1.00 19.27           N  
HETATM 6259  C1D BCL C 374      35.859 -48.680  22.816  1.00 19.57           C  
HETATM 6260  C2D BCL C 374      36.642 -48.944  21.641  1.00 18.67           C  
HETATM 6261  C3D BCL C 374      35.879 -48.442  20.590  1.00 19.37           C  
HETATM 6262  C4D BCL C 374      34.749 -47.835  21.130  1.00 19.46           C  
HETATM 6263  CMD BCL C 374      38.024 -49.596  21.617  1.00 16.62           C  
HETATM 6264  CAD BCL C 374      35.881 -48.140  19.207  1.00 21.35           C  
HETATM 6265  OBD BCL C 374      36.734 -48.460  18.327  1.00 22.27           O  
HETATM 6266  CBD BCL C 374      34.592 -47.306  18.872  1.00 21.19           C  
HETATM 6267  CGD BCL C 374      34.951 -46.014  18.262  1.00 23.08           C  
HETATM 6268  O1D BCL C 374      35.483 -45.080  18.822  1.00 23.44           O  
HETATM 6269  O2D BCL C 374      34.668 -45.874  16.983  1.00 24.59           O  
HETATM 6270  CED BCL C 374      34.904 -44.527  16.469  1.00 24.49           C  
HETATM 6271  C1  BCL C 374      31.882 -50.579  20.880  1.00 25.52           C  
HETATM 6272  C2  BCL C 374      31.201 -51.315  22.072  1.00 27.09           C  
HETATM 6273  C3  BCL C 374      31.885 -51.676  23.197  1.00 26.79           C  
HETATM 6274  C4  BCL C 374      33.395 -51.407  23.408  1.00 25.82           C  
HETATM 6275  C5  BCL C 374      31.190 -52.430  24.353  1.00 24.94           C  
HETATM 6276  C6  BCL C 374      31.089 -51.668  25.671  1.00 23.89           C  
HETATM 6277  C7  BCL C 374      30.189 -52.267  26.726  1.00 22.94           C  
HETATM 6278  C8  BCL C 374      30.364 -51.570  28.091  1.00 22.83           C  
HETATM 6279  C9  BCL C 374      31.757 -51.905  28.795  1.00 20.91           C  
HETATM 6280  C10 BCL C 374      29.182 -51.930  28.988  1.00 23.31           C  
HETATM 6281  C11 BCL C 374      28.749 -53.371  29.122  1.00 23.45           C  
HETATM 6282  C12 BCL C 374      27.709 -53.463  30.234  1.00 24.41           C  
HETATM 6283  C13 BCL C 374      27.461 -54.917  30.717  1.00 25.27           C  
HETATM 6284  C14 BCL C 374      27.155 -55.907  29.591  1.00 24.19           C  
HETATM 6285  C15 BCL C 374      26.350 -54.879  31.759  1.00 25.79           C  
HETATM 6286  C16 BCL C 374      26.757 -54.360  33.167  1.00 26.86           C  
HETATM 6287  C17 BCL C 374      25.541 -54.431  34.119  1.00 28.44           C  
HETATM 6288  C18 BCL C 374      25.746 -53.923  35.528  1.00 29.94           C  
HETATM 6289  C19 BCL C 374      26.722 -54.855  36.289  1.00 29.06           C  
HETATM 6290  C20 BCL C 374      24.510 -53.648  36.402  1.00 30.20           C  
HETATM 6291 MG   BCL C 375      20.539 -42.393  26.143  1.00 22.35          MG  
HETATM 6292  CHA BCL C 375      24.005 -42.519  25.863  1.00 22.19           C  
HETATM 6293  CHB BCL C 375      20.355 -43.399  22.876  1.00 23.73           C  
HETATM 6294  CHC BCL C 375      17.242 -43.032  26.581  1.00 23.79           C  
HETATM 6295  CHD BCL C 375      20.869 -41.985  29.614  1.00 22.17           C  
HETATM 6296  NA  BCL C 375      21.995 -42.911  24.620  1.00 22.69           N  
HETATM 6297  C1A BCL C 375      23.386 -42.737  24.667  1.00 22.39           C  
HETATM 6298  C2A BCL C 375      24.007 -42.904  23.302  1.00 22.22           C  
HETATM 6299  C3A BCL C 375      22.797 -42.869  22.370  1.00 22.00           C  
HETATM 6300  C4A BCL C 375      21.642 -43.109  23.289  1.00 22.92           C  
HETATM 6301  CMA BCL C 375      22.640 -41.495  21.733  1.00 22.01           C  
HETATM 6302  CAA BCL C 375      24.784 -44.218  23.181  1.00 22.50           C  
HETATM 6303  CBA BCL C 375      25.674 -44.176  21.944  1.00 22.89           C  
HETATM 6304  CGA BCL C 375      26.452 -45.412  21.671  1.00 24.42           C  
HETATM 6305  O1A BCL C 375      27.144 -45.582  20.748  1.00 25.64           O  
HETATM 6306  O2A BCL C 375      26.274 -46.416  22.503  1.00 25.01           O  
HETATM 6307  NB  BCL C 375      19.031 -43.135  24.948  1.00 24.33           N  
HETATM 6308  C1B BCL C 375      19.135 -43.426  23.585  1.00 24.82           C  
HETATM 6309  C2B BCL C 375      17.854 -43.651  23.033  1.00 24.61           C  
HETATM 6310  C3B BCL C 375      16.935 -43.481  24.066  1.00 25.48           C  
HETATM 6311  C4B BCL C 375      17.720 -43.234  25.271  1.00 24.12           C  
HETATM 6312  CMB BCL C 375      17.604 -44.028  21.595  1.00 23.78           C  
HETATM 6313  CAB BCL C 375      15.489 -43.396  24.038  1.00 24.83           C  
HETATM 6314  OBB BCL C 375      14.813 -43.787  24.992  1.00 24.17           O  
HETATM 6315  CBB BCL C 375      14.808 -42.662  22.911  1.00 24.00           C  
HETATM 6316  NC  BCL C 375      19.258 -42.480  27.844  1.00 22.18           N  
HETATM 6317  C1C BCL C 375      17.898 -42.697  27.785  1.00 23.26           C  
HETATM 6318  C2C BCL C 375      17.183 -42.416  29.077  1.00 24.12           C  
HETATM 6319  C3C BCL C 375      18.363 -42.181  30.088  1.00 24.21           C  
HETATM 6320  C4C BCL C 375      19.581 -42.168  29.158  1.00 23.00           C  
HETATM 6321  CMC BCL C 375      16.205 -41.242  29.015  1.00 24.07           C  
HETATM 6322  CAC BCL C 375      18.445 -43.307  31.181  1.00 24.82           C  
HETATM 6323  CBC BCL C 375      17.323 -43.223  32.205  1.00 25.35           C  
HETATM 6324  ND  BCL C 375      22.062 -42.356  27.502  1.00 21.82           N  
HETATM 6325  C1D BCL C 375      22.091 -42.101  28.877  1.00 22.71           C  
HETATM 6326  C2D BCL C 375      23.427 -41.905  29.350  1.00 22.55           C  
HETATM 6327  C3D BCL C 375      24.249 -42.078  28.196  1.00 23.20           C  
HETATM 6328  C4D BCL C 375      23.389 -42.305  27.119  1.00 21.90           C  
HETATM 6329  CMD BCL C 375      23.808 -41.590  30.784  1.00 20.24           C  
HETATM 6330  CAD BCL C 375      25.579 -42.034  27.655  1.00 24.05           C  
HETATM 6331  OBD BCL C 375      26.669 -41.746  28.196  1.00 24.34           O  
HETATM 6332  CBD BCL C 375      25.508 -42.357  26.133  1.00 23.41           C  
HETATM 6333  CGD BCL C 375      26.155 -41.274  25.394  1.00 24.32           C  
HETATM 6334  O1D BCL C 375      27.092 -41.341  24.655  1.00 24.47           O  
HETATM 6335  O2D BCL C 375      25.598 -40.108  25.599  1.00 25.75           O  
HETATM 6336  CED BCL C 375      25.787 -39.079  24.604  1.00 25.78           C  
HETATM 6337  C1  BCL C 375      27.124 -47.602  22.289  1.00 25.35           C  
HETATM 6338  C2  BCL C 375      26.417 -48.716  23.050  1.00 27.17           C  
HETATM 6339  C3  BCL C 375      27.141 -49.542  23.744  1.00 29.25           C  
HETATM 6340  C4  BCL C 375      28.664 -49.470  23.804  1.00 29.39           C  
HETATM 6341  C5  BCL C 375      26.523 -50.725  24.536  1.00 29.77           C  
HETATM 6342  C6  BCL C 375      25.764 -50.421  25.809  1.00 30.61           C  
HETATM 6343  C7  BCL C 375      24.953 -51.593  26.251  1.00 30.51           C  
HETATM 6344  C8  BCL C 375      24.723 -51.710  27.730  1.00 33.07           C  
HETATM 6345  C9  BCL C 375      23.666 -52.784  27.866  1.00 34.33           C  
HETATM 6346  C10 BCL C 375      24.044 -50.460  28.276  1.00 36.14           C  
HETATM 6347  C11 BCL C 375      24.850 -49.718  29.342  1.00 37.77           C  
HETATM 6348  C12 BCL C 375      24.597 -50.270  30.724  1.00 38.24           C  
HETATM 6349  C13 BCL C 375      25.262 -49.435  31.820  1.00 38.41           C  
HETATM 6350  C14 BCL C 375      26.785 -49.466  31.775  1.00 37.58           C  
HETATM 6351  C15 BCL C 375      24.821 -50.178  33.064  1.00 39.71           C  
HETATM 6352  C16 BCL C 375      23.515 -49.559  33.529  1.00 41.05           C  
HETATM 6353  C17 BCL C 375      23.571 -49.551  35.041  1.00 42.63           C  
HETATM 6354  C18 BCL C 375      22.371 -48.894  35.681  1.00 44.09           C  
HETATM 6355  C19 BCL C 375      22.530 -49.194  37.176  1.00 44.79           C  
HETATM 6356  C20 BCL C 375      21.115 -49.620  35.213  1.00 44.43           C  
HETATM 6357 MG   BCL C 376      18.372 -40.390  37.539  1.00 21.62          MG  
HETATM 6358  CHACBCL C 376      16.266 -40.134  34.759  0.37 21.73           C  
HETATM 6359  CHADBCL C 376      16.253 -40.078  34.774  0.63 24.20           C  
HETATM 6360  CHB BCL C 376      15.765 -41.902  39.205  1.00 21.41           C  
HETATM 6361  CHC BCL C 376      20.597 -41.573  39.824  1.00 20.34           C  
HETATM 6362  CHD BCL C 376      21.066 -39.475  35.499  1.00 21.44           C  
HETATM 6363  NA  BCL C 376      16.291 -40.933  37.022  1.00 23.51           N  
HETATM 6364  C1A BCL C 376      15.603 -40.684  35.832  1.00 23.66           C  
HETATM 6365  C2A BCL C 376      14.154 -41.159  35.924  1.00 24.88           C  
HETATM 6366  C3A BCL C 376      13.969 -41.443  37.432  1.00 23.37           C  
HETATM 6367  C4A BCL C 376      15.399 -41.516  37.936  1.00 22.78           C  
HETATM 6368  CMA BCL C 376      13.093 -40.358  38.156  1.00 20.33           C  
HETATM 6369  CAA BCL C 376      13.837 -42.369  35.042  1.00 25.94           C  
HETATM 6370  CBA BCL C 376      14.851 -43.490  35.125  1.00 28.19           C  
HETATM 6371  CGA BCL C 376      14.391 -44.664  34.320  1.00 31.75           C  
HETATM 6372  O1A BCL C 376      13.375 -44.750  33.793  1.00 33.92           O  
HETATM 6373  O2A BCL C 376      15.176 -45.690  34.217  1.00 32.81           O  
HETATM 6374  NB  BCL C 376      18.252 -41.615  39.203  1.00 21.05           N  
HETATM 6375  C1B BCL C 376      17.072 -42.030  39.811  1.00 22.28           C  
HETATM 6376  C2B BCL C 376      17.371 -42.738  40.997  1.00 22.75           C  
HETATM 6377  C3B BCL C 376      18.742 -42.665  41.191  1.00 22.13           C  
HETATM 6378  C4B BCL C 376      19.254 -41.895  40.082  1.00 21.11           C  
HETATM 6379  CMB BCL C 376      16.324 -43.494  41.825  1.00 21.76           C  
HETATM 6380  CAB BCL C 376      19.513 -43.242  42.293  1.00 23.76           C  
HETATM 6381  OBB BCL C 376      20.772 -43.314  42.297  1.00 24.62           O  
HETATM 6382  CBB BCL C 376      18.783 -43.685  43.543  1.00 22.61           C  
HETATM 6383  NC ABCL C 376      20.505 -40.508  37.638  0.47 20.76           N  
HETATM 6384  NC BBCL C 376      20.505 -40.516  37.637  0.53 21.10           N  
HETATM 6385  C1CABCL C 376      21.210 -40.922  38.737  0.47 20.18           C  
HETATM 6386  C1CBBCL C 376      21.215 -40.981  38.707  0.53 20.56           C  
HETATM 6387  C2CABCL C 376      22.647 -40.497  38.728  0.47 19.67           C  
HETATM 6388  C2CBBCL C 376      22.660 -40.596  38.646  0.53 20.53           C  
HETATM 6389  C3CABCL C 376      22.754 -39.690  37.422  0.47 19.66           C  
HETATM 6390  C3CBBCL C 376      22.854 -40.429  37.134  0.53 21.38           C  
HETATM 6391  C4CABCL C 376      21.397 -39.912  36.777  0.47 20.78           C  
HETATM 6392  C4CBBCL C 376      21.421 -40.099  36.693  0.53 21.48           C  
HETATM 6393  CMCABCL C 376      23.070 -39.691  39.969  0.47 19.40           C  
HETATM 6394  CMCBBCL C 376      23.016 -39.339  39.450  0.53 20.03           C  
HETATM 6395  CACABCL C 376      23.915 -40.173  36.502  0.47 18.25           C  
HETATM 6396  CACBBCL C 376      23.405 -41.769  36.566  0.53 21.39           C  
HETATM 6397  CBCABCL C 376      23.735 -41.604  36.027  0.47 17.82           C  
HETATM 6398  CBCBBCL C 376      23.366 -41.879  35.067  0.53 21.80           C  
HETATM 6399  ND  BCL C 376      18.652 -39.866  35.576  1.00 21.41           N  
HETATM 6400  C1D BCL C 376      19.781 -39.454  34.858  1.00 21.15           C  
HETATM 6401  C2D BCL C 376      19.460 -39.160  33.506  1.00 21.02           C  
HETATM 6402  C3DCBCL C 376      18.082 -39.361  33.409  0.37 21.16           C  
HETATM 6403  C3DDBCL C 376      18.085 -39.326  33.422  0.63 22.95           C  
HETATM 6404  C4DCBCL C 376      17.643 -39.823  34.652  0.37 21.35           C  
HETATM 6405  C4DDBCL C 376      17.640 -39.790  34.663  0.63 22.68           C  
HETATM 6406  CMD BCL C 376      20.439 -38.773  32.432  1.00 19.33           C  
HETATM 6407  CADCBCL C 376      16.957 -39.430  32.531  0.37 20.59           C  
HETATM 6408  CADDBCL C 376      16.923 -39.146  32.615  0.63 24.45           C  
HETATM 6409  OBDCBCL C 376      16.896 -39.336  31.269  0.37 20.32           O  
HETATM 6410  OBDDBCL C 376      16.810 -38.648  31.463  0.63 24.13           O  
HETATM 6411  CBDCBCL C 376      15.693 -39.735  33.395  0.37 19.53           C  
HETATM 6412  CBDDBCL C 376      15.726 -39.827  33.352  0.63 25.21           C  
HETATM 6413  CGDCBCL C 376      14.781 -38.581  33.501  0.37 17.07           C  
HETATM 6414  CGDDBCL C 376      14.437 -39.111  33.239  0.63 28.15           C  
HETATM 6415  O1DCBCL C 376      15.097 -37.424  33.275  0.37 15.69           O  
HETATM 6416  O1DDBCL C 376      13.473 -39.537  32.651  0.63 29.43           O  
HETATM 6417  O2DCBCL C 376      13.556 -38.944  33.921  0.37 15.49           O  
HETATM 6418  O2DDBCL C 376      14.312 -37.950  33.866  0.63 29.29           O  
HETATM 6419  CEDCBCL C 376      12.524 -37.944  34.094  0.37 14.23           C  
HETATM 6420  CEDDBCL C 376      12.922 -37.626  34.207  0.63 28.69           C  
HETATM 6421  C1  BCL C 376      15.103 -46.588  33.036  1.00 33.12           C  
HETATM 6422  C2  BCL C 376      16.343 -47.491  33.198  1.00 33.67           C  
HETATM 6423  C3  BCL C 376      17.086 -47.897  32.220  1.00 34.85           C  
HETATM 6424  C4  BCL C 376      16.863 -47.574  30.765  1.00 34.40           C  
HETATM 6425  C5  BCL C 376      18.316 -48.787  32.488  1.00 37.14           C  
HETATM 6426  C6  BCL C 376      19.660 -48.469  31.728  1.00 37.39           C  
HETATM 6427  C7  BCL C 376      19.923 -46.981  31.581  1.00 37.20           C  
HETATM 6428  C8  BCL C 376      21.301 -46.742  30.986  1.00 36.18           C  
HETATM 6429  C9  BCL C 376      22.021 -45.649  31.795  1.00 35.48           C  
HETATM 6430  C10 BCL C 376      21.104 -46.351  29.530  1.00 35.80           C  
HETATM 6431  C11 BCL C 376      22.343 -46.488  28.700  1.00 36.01           C  
HETATM 6432  C12 BCL C 376      21.978 -46.242  27.238  1.00 36.06           C  
HETATM 6433  C13 BCL C 376      22.822 -47.096  26.310  1.00 35.51           C  
HETATM 6434  C14 BCL C 376      24.234 -46.523  26.274  1.00 35.17           C  
HETATM 6435  C15 BCL C 376      22.170 -46.929  24.935  1.00 36.15           C  
HETATM 6436  C16 BCL C 376      20.674 -47.211  24.957  1.00 36.99           C  
HETATM 6437  C17 BCL C 376      19.858 -47.600  23.684  1.00 36.57           C  
HETATM 6438  C18 BCL C 376      18.551 -48.283  24.034  1.00 35.81           C  
HETATM 6439  C19 BCL C 376      17.980 -48.812  22.702  1.00 35.79           C  
HETATM 6440  C20 BCL C 376      17.542 -47.451  24.813  1.00 35.08           C  
HETATM 6441 MG   BCL C 377      30.002 -46.362  36.342  1.00 17.03          MG  
HETATM 6442  CHA BCL C 377      32.277 -49.011  36.413  1.00 18.11           C  
HETATM 6443  CHB BCL C 377      29.937 -46.459  39.764  1.00 15.96           C  
HETATM 6444  CHC BCL C 377      27.324 -44.286  36.287  1.00 16.74           C  
HETATM 6445  CHD BCL C 377      29.505 -46.994  32.925  1.00 16.79           C  
HETATM 6446  NA  BCL C 377      30.935 -47.640  37.855  1.00 17.67           N  
HETATM 6447  C1A BCL C 377      31.867 -48.680  37.673  1.00 18.18           C  
HETATM 6448  C2A BCL C 377      32.495 -49.086  38.981  1.00 19.00           C  
HETATM 6449  C3A BCL C 377      31.538 -48.459  40.027  1.00 18.25           C  
HETATM 6450  C4A BCL C 377      30.777 -47.425  39.225  1.00 17.47           C  
HETATM 6451  CMA BCL C 377      30.596 -49.505  40.655  1.00 16.83           C  
HETATM 6452  CAA BCL C 377      33.898 -48.504  39.062  1.00 20.45           C  
HETATM 6453  CBA BCL C 377      34.681 -48.824  40.313  1.00 22.92           C  
HETATM 6454  CGA BCL C 377      35.066 -50.247  40.530  1.00 26.26           C  
HETATM 6455  O1A BCL C 377      36.067 -50.604  40.963  1.00 29.16           O  
HETATM 6456  O2A BCL C 377      34.233 -51.159  40.275  1.00 26.48           O  
HETATM 6457  NB  BCL C 377      28.742 -45.591  37.795  1.00 16.15           N  
HETATM 6458  C1B BCL C 377      29.007 -45.593  39.161  1.00 16.01           C  
HETATM 6459  C2B BCL C 377      28.313 -44.545  39.797  1.00 17.25           C  
HETATM 6460  C3BABCL C 377      27.570 -43.877  38.819  0.47 17.40           C  
HETATM 6461  C3BBBCL C 377      27.539 -43.911  38.816  0.53 17.15           C  
HETATM 6462  C4B BCL C 377      27.815 -44.601  37.584  1.00 17.17           C  
HETATM 6463  CMB BCL C 377      28.447 -44.205  41.297  1.00 16.86           C  
HETATM 6464  CABABCL C 377      26.762 -42.664  38.993  0.47 17.72           C  
HETATM 6465  CABBBCL C 377      26.622 -42.789  38.895  0.53 17.00           C  
HETATM 6466  OBBABCL C 377      26.650 -41.773  38.112  0.47 18.05           O  
HETATM 6467  OBBBBCL C 377      26.263 -42.186  37.862  0.53 17.15           O  
HETATM 6468  CBBABCL C 377      26.077 -42.388  40.322  0.47 16.45           C  
HETATM 6469  CBBBBCL C 377      26.090 -42.290  40.234  0.53 15.60           C  
HETATM 6470  NC  BCL C 377      28.601 -45.790  34.849  1.00 17.50           N  
HETATM 6471  C1CCBCL C 377      27.674 -44.786  35.017  0.45 16.97           C  
HETATM 6472  C1CDBCL C 377      27.527 -44.947  35.062  0.55 17.00           C  
HETATM 6473  C2CCBCL C 377      27.117 -44.291  33.724  0.45 16.51           C  
HETATM 6474  C2CDBCL C 377      26.597 -44.855  33.895  0.55 16.51           C  
HETATM 6475  C3CCBCL C 377      27.507 -45.426  32.769  0.45 16.72           C  
HETATM 6476  C3CDBCL C 377      27.257 -45.787  32.852  0.55 16.80           C  
HETATM 6477  C4CCBCL C 377      28.664 -46.057  33.495  0.45 17.23           C  
HETATM 6478  C4CDBCL C 377      28.541 -46.213  33.531  0.55 17.29           C  
HETATM 6479  CMCCBCL C 377      25.613 -44.077  33.785  0.45 16.59           C  
HETATM 6480  CMCDBCL C 377      25.156 -45.249  34.252  0.55 15.44           C  
HETATM 6481  CACCBCL C 377      27.795 -44.974  31.316  0.45 16.54           C  
HETATM 6482  CACDBCL C 377      27.505 -45.081  31.492  0.55 16.86           C  
HETATM 6483  CBCCBCL C 377      26.526 -44.922  30.469  0.45 16.02           C  
HETATM 6484  CBCDBCL C 377      26.213 -44.711  30.766  0.55 16.11           C  
HETATM 6485  ND  BCL C 377      30.693 -47.687  34.930  1.00 17.75           N  
HETATM 6486  C1D BCL C 377      30.480 -47.810  33.543  1.00 16.48           C  
HETATM 6487  C2D BCL C 377      31.401 -48.732  32.951  1.00 15.94           C  
HETATM 6488  C3D BCL C 377      32.130 -49.255  34.024  1.00 17.57           C  
HETATM 6489  C4D BCL C 377      31.664 -48.630  35.195  1.00 17.88           C  
HETATM 6490  CMD BCL C 377      31.513 -49.062  31.496  1.00 14.13           C  
HETATM 6491  CAD BCL C 377      33.137 -50.185  34.429  1.00 18.41           C  
HETATM 6492  OBD BCL C 377      33.806 -51.008  33.743  1.00 18.53           O  
HETATM 6493  CBD BCL C 377      33.300 -50.089  35.988  1.00 18.71           C  
HETATM 6494  CGD BCL C 377      33.083 -51.427  36.576  1.00 20.14           C  
HETATM 6495  O1D BCL C 377      33.958 -52.213  36.808  1.00 20.44           O  
HETATM 6496  O2D BCL C 377      31.821 -51.760  36.830  1.00 21.03           O  
HETATM 6497  CED BCL C 377      31.565 -53.100  37.393  1.00 21.27           C  
HETATM 6498  C1  BCL C 377      34.673 -52.579  40.218  1.00 24.68           C  
HETATM 6499  C2  BCL C 377      33.538 -53.356  40.881  1.00 22.11           C  
HETATM 6500  C3  BCL C 377      33.188 -54.551  40.559  1.00 21.00           C  
HETATM 6501  C4  BCL C 377      33.849 -55.381  39.505  1.00 21.64           C  
HETATM 6502  C5  BCL C 377      32.049 -55.274  41.212  1.00 22.42           C  
HETATM 6503  C6  BCL C 377      31.239 -54.509  42.263  1.00 24.08           C  
HETATM 6504  C7  BCL C 377      30.036 -53.877  41.650  1.00 24.89           C  
HETATM 6505  C8  BCL C 377      28.968 -53.079  42.416  1.00 26.47           C  
HETATM 6506  C9  BCL C 377      29.566 -51.924  43.272  1.00 25.56           C  
HETATM 6507  C10 BCL C 377      28.034 -54.009  43.210  1.00 28.96           C  
HETATM 6508  C11 BCL C 377      26.668 -53.850  42.625  1.00 30.85           C  
HETATM 6509  C12 BCL C 377      25.626 -54.042  43.715  1.00 32.53           C  
HETATM 6510  C13 BCL C 377      24.337 -53.247  43.465  1.00 33.00           C  
HETATM 6511  C14 BCL C 377      23.206 -53.668  44.388  1.00 32.25           C  
HETATM 6512  C15EBCL C 377      23.807 -53.301  42.019  0.33 33.43           C  
HETATM 6513  C15FBCL C 377      24.002 -53.553  41.988  0.67 33.88           C  
HETATM 6514  C16EBCL C 377      22.459 -52.572  41.802  0.33 33.39           C  
HETATM 6515  C16FBCL C 377      22.634 -53.319  41.314  0.67 34.02           C  
HETATM 6516  C17EBCL C 377      22.361 -51.762  40.489  0.33 33.83           C  
HETATM 6517  C17FBCL C 377      22.748 -53.630  39.793  0.67 34.41           C  
HETATM 6518  C18EBCL C 377      20.964 -51.795  39.877  0.33 34.34           C  
HETATM 6519  C18FBCL C 377      21.868 -52.654  39.098  0.67 35.88           C  
HETATM 6520  C19EBCL C 377      20.504 -53.258  39.987  0.33 34.13           C  
HETATM 6521  C19FBCL C 377      21.021 -52.176  40.287  0.67 36.75           C  
HETATM 6522  C20EBCL C 377      20.862 -51.331  38.418  0.33 34.56           C  
HETATM 6523  C20FBCL C 377      20.936 -53.233  38.022  0.67 36.06           C  
HETATM 6524 MG  BBCL C 378      25.939 -19.102  36.258  1.00 83.59          MG  
HETATM 6525  CHABBCL C 378      23.880 -20.566  38.628  1.00 83.26           C  
HETATM 6526  CHBBBCL C 378      23.169 -18.363  34.411  1.00 85.04           C  
HETATM 6527  CHCBBCL C 378      27.828 -16.953  34.434  1.00 82.30           C  
HETATM 6528  CHDBBCL C 378      28.687 -19.725  38.299  1.00 82.04           C  
HETATM 6529  NA BBCL C 378      23.798 -19.393  36.548  1.00 84.87           N  
HETATM 6530  C1ABBCL C 378      23.172 -20.165  37.525  1.00 84.97           C  
HETATM 6531  C2ABBCL C 378      21.716 -20.385  37.213  1.00 86.55           C  
HETATM 6532  C3ABBCL C 378      21.478 -19.485  35.987  1.00 86.54           C  
HETATM 6533  C4ABBCL C 378      22.867 -19.109  35.550  1.00 85.64           C  
HETATM 6534  CMABBCL C 378      20.693 -20.229  34.898  1.00 86.88           C  
HETATM 6535  CAABBCL C 378      20.788 -20.047  38.394  1.00 88.13           C  
HETATM 6536  CBABBCL C 378      20.650 -18.529  38.638  1.00 89.98           C  
HETATM 6537  CGABBCL C 378      19.238 -18.090  38.878  1.00 91.79           C  
HETATM 6538  O1ABBCL C 378      18.888 -17.179  39.607  1.00 92.13           O  
HETATM 6539  O2ABBCL C 378      18.353 -18.826  38.201  1.00 92.48           O  
HETATM 6540  NB BBCL C 378      25.560 -17.738  34.742  1.00 83.51           N  
HETATM 6541  C1BBBCL C 378      24.407 -17.800  33.952  1.00 84.25           C  
HETATM 6542  C2BBBCL C 378      24.663 -17.293  32.667  1.00 83.76           C  
HETATM 6543  C3BBBCL C 378      26.018 -16.937  32.607  1.00 82.56           C  
HETATM 6544  C4BBBCL C 378      26.525 -17.158  33.959  1.00 82.56           C  
HETATM 6545  CMBBBCL C 378      23.587 -17.150  31.610  1.00 84.37           C  
HETATM 6546  CABBBCL C 378      26.754 -16.440  31.436  1.00 81.79           C  
HETATM 6547  OBBBBCL C 378      27.951 -16.708  31.168  1.00 80.91           O  
HETATM 6548  CBBBBCL C 378      26.054 -15.544  30.440  1.00 81.96           C  
HETATM 6549  NC BBCL C 378      27.943 -18.356  36.427  1.00 82.52           N  
HETATM 6550  C1CBBCL C 378      28.546 -17.584  35.473  1.00 82.03           C  
HETATM 6551  C2CBBCL C 378      30.022 -17.603  35.549  1.00 81.28           C  
HETATM 6552  C3CBBCL C 378      30.298 -18.617  36.655  1.00 81.16           C  
HETATM 6553  C4CBBCL C 378      28.933 -18.864  37.234  1.00 81.80           C  
HETATM 6554  CMCBBCL C 378      30.688 -17.917  34.211  1.00 81.01           C  
HETATM 6555  CACBBCL C 378      31.252 -17.980  37.669  1.00 80.93           C  
HETATM 6556  CBCBBCL C 378      31.194 -16.469  37.589  1.00 80.91           C  
HETATM 6557  ND BBCL C 378      26.252 -19.860  38.118  1.00 82.62           N  
HETATM 6558  C1DBBCL C 378      27.425 -20.192  38.802  1.00 81.98           C  
HETATM 6559  C2DBBCL C 378      27.151 -21.019  39.927  1.00 81.14           C  
HETATM 6560  C3DBBCL C 378      25.771 -21.148  39.954  1.00 81.44           C  
HETATM 6561  C4DBBCL C 378      25.273 -20.499  38.829  1.00 82.41           C  
HETATM 6562  CMDBBCL C 378      28.169 -21.621  40.843  1.00 80.78           C  
HETATM 6563  CADBBCL C 378      24.650 -21.477  40.747  1.00 81.64           C  
HETATM 6564  OBDBBCL C 378      24.592 -21.817  41.948  1.00 81.70           O  
HETATM 6565  CBDBBCL C 378      23.360 -21.254  39.888  1.00 82.16           C  
HETATM 6566  CGDBBCL C 378      22.549 -22.468  39.652  1.00 81.67           C  
HETATM 6567  O1DBBCL C 378      21.500 -22.719  40.221  1.00 81.65           O  
HETATM 6568  O2DBBCL C 378      23.045 -23.291  38.728  1.00 81.17           O  
HETATM 6569  CEDBBCL C 378      22.248 -24.443  38.285  1.00 80.68           C  
HETATM 6570  O   HOH A1043      15.985  -1.198 -19.215  1.00 21.51           O  
HETATM 6571  O  AHOH A1044      17.975  -0.369 -20.159  0.75 35.88           O  
HETATM 6572  O   HOH A1045      14.807   0.852 -23.148  1.00 23.24           O  
HETATM 6573  O   HOH A1046      13.149   3.004 -24.347  1.00 25.60           O  
HETATM 6574  O   HOH A1047      14.951   0.922 -20.457  1.00 25.53           O  
HETATM 6575  O   HOH A1048      10.614 -10.533   8.299  1.00 17.98           O  
HETATM 6576  O   HOH A1049      -1.998  -8.688 -17.291  1.00 17.76           O  
HETATM 6577  O   HOH A1050      13.545   1.643   9.259  1.00 20.21           O  
HETATM 6578  O   HOH A1051       8.531  -5.753   0.425  1.00 19.06           O  
HETATM 6579  O   HOH A1052       2.731 -26.586   8.727  1.00 17.68           O  
HETATM 6580  O   HOH A1053      12.237 -13.577  -0.349  1.00 19.20           O  
HETATM 6581  O   HOH A1054      -5.851 -11.959 -12.688  1.00 21.00           O  
HETATM 6582  O   HOH A1055       4.433 -25.693   4.092  1.00 29.00           O  
HETATM 6583  O   HOH A1056      -2.460  -9.528 -14.521  1.00 23.79           O  
HETATM 6584  O   HOH A1057      12.432  -8.630   0.259  1.00 23.63           O  
HETATM 6585  O   HOH A1058      -2.360  -6.922  -9.819  1.00 20.89           O  
HETATM 6586  O   HOH A1059       4.373 -23.347   2.344  1.00 20.19           O  
HETATM 6587  O   HOH A1060       9.634 -23.072  10.153  1.00 34.77           O  
HETATM 6588  O   HOH A1061       1.780 -13.886  -6.771  1.00 19.50           O  
HETATM 6589  O   HOH A1062       6.875  -8.434   6.786  1.00 21.44           O  
HETATM 6590  O   HOH A1063       6.358   1.436   0.314  1.00 22.18           O  
HETATM 6591  O   HOH A1064      -2.357 -26.997   3.361  1.00 26.00           O  
HETATM 6592  O   HOH A1065       0.132  -8.251  -3.267  1.00 26.80           O  
HETATM 6593  O   HOH A1066      23.460 -20.203   6.691  1.00 31.10           O  
HETATM 6594  O   HOH A1067      29.120 -20.308   5.344  1.00 31.29           O  
HETATM 6595  O   HOH A1068       2.536 -23.205   0.292  1.00 22.39           O  
HETATM 6596  O   HOH A1069      26.894  11.875 -18.244  1.00 34.51           O  
HETATM 6597  O   HOH A1070      15.657   5.849   9.473  1.00 35.31           O  
HETATM 6598  O   HOH A1071      15.343 -25.037   2.777  1.00 32.95           O  
HETATM 6599  O   HOH A1072      34.317   1.398 -14.352  1.00 30.76           O  
HETATM 6600  O   HOH A1073      25.041 -15.608   9.362  1.00 28.15           O  
HETATM 6601  O   HOH A1074       0.736 -13.559   5.302  1.00 21.62           O  
HETATM 6602  O   HOH A1075      21.117 -31.944   1.423  1.00 37.13           O  
HETATM 6603  O   HOH A1076      15.620 -33.650  -0.986  1.00 35.82           O  
HETATM 6604  O   HOH A1077       4.082  -1.545 -13.320  1.00 24.39           O  
HETATM 6605  O   HOH A1078      13.188 -11.364   0.960  1.00 25.13           O  
HETATM 6606  O   HOH A1079      -0.682  -9.365   1.305  1.00 44.11           O  
HETATM 6607  O   HOH A1080      27.514 -22.115   8.292  1.00 51.90           O  
HETATM 6608  O   HOH A1081       4.222 -24.333  -1.403  1.00 28.20           O  
HETATM 6609  O   HOH A1082      -8.801 -11.818 -19.506  1.00 26.25           O  
HETATM 6610  O   HOH A1083      26.298  10.296 -16.100  1.00 36.08           O  
HETATM 6611  O   HOH A1084      16.247 -19.928   8.778  1.00 32.72           O  
HETATM 6612  O   HOH A1085      12.154   3.109   7.595  1.00 28.71           O  
HETATM 6613  O   HOH A1086      10.903 -24.772   5.281  1.00 24.46           O  
HETATM 6614  O   HOH A1087      19.577 -33.599  -7.173  1.00 37.47           O  
HETATM 6615  O   HOH A1088       8.419 -17.983   4.976  1.00 50.76           O  
HETATM 6616  O   HOH A1089      -2.293  -8.958  -3.054  1.00 38.03           O  
HETATM 6617  O   HOH A1090      24.740  -4.205 -22.613  1.00 32.52           O  
HETATM 6618  O   HOH A1091      -2.179 -28.190   5.780  1.00 27.35           O  
HETATM 6619  O   HOH A1092      21.470  -1.417 -26.714  1.00 32.92           O  
HETATM 6620  O   HOH A1093      31.921   4.083  -4.671  1.00 27.24           O  
HETATM 6621  O   HOH A1094       5.865 -25.845   0.189  1.00 31.97           O  
HETATM 6622  O   HOH A1095       2.578 -19.962   1.919  1.00 28.86           O  
HETATM 6623  O   HOH A1096      -7.395 -31.681  -1.667  1.00 39.81           O  
HETATM 6624  O   HOH A1097      30.677 -19.859  -9.037  1.00 43.15           O  
HETATM 6625  O   HOH A1098     -12.967  -8.675 -15.665  1.00 45.59           O  
HETATM 6626  O   HOH A1099      -0.874  -3.406  -7.928  1.00 36.27           O  
HETATM 6627  O   HOH A1100      13.928 -21.118   8.708  1.00 44.20           O  
HETATM 6628  O   HOH A1101       7.876   0.675   4.159  1.00 34.76           O  
HETATM 6629  O   HOH A1102      19.575   1.986  10.888  1.00 31.81           O  
HETATM 6630  O   HOH A1103       5.767 -19.626   4.096  1.00 32.96           O  
HETATM 6631  O   HOH A1104       1.523  -1.257  -0.351  1.00 45.71           O  
HETATM 6632  O   HOH A1105      10.937   2.214   4.034  1.00 35.12           O  
HETATM 6633  O   HOH A1106       4.230   3.592 -21.483  1.00 30.89           O  
HETATM 6634  O   HOH A1107      26.865  -5.102   9.184  1.00 34.87           O  
HETATM 6635  O   HOH A1108      18.325 -11.973 -23.810  1.00 46.98           O  
HETATM 6636  O   HOH A1109       6.997 -14.373  15.554  1.00 26.53           O  
HETATM 6637  O   HOH A1110      -0.578 -10.470  -1.456  1.00 33.47           O  
HETATM 6638  O   HOH A1111      -4.499 -32.728  -7.753  1.00 34.94           O  
HETATM 6639  O   HOH A1112      21.230 -23.339   6.378  1.00 46.33           O  
HETATM 6640  O   HOH A1113      23.361 -18.185   8.946  1.00 44.13           O  
HETATM 6641  O   HOH A1114       9.242 -20.486   7.624  1.00 48.88           O  
HETATM 6642  O   HOH A1115      17.949 -24.525   3.383  1.00 30.34           O  
HETATM 6643  O   HOH A1116      -8.576 -10.274 -12.492  1.00 50.31           O  
HETATM 6644  O   HOH A1117      25.680  10.242   6.727  1.00 42.98           O  
HETATM 6645  O   HOH A1118      28.794  -1.549 -23.397  1.00 44.61           O  
HETATM 6646  O   HOH A1119       5.520 -28.094   2.390  1.00 33.33           O  
HETATM 6647  O   HOH A1120       9.814 -10.602 -26.534  1.00 28.66           O  
HETATM 6648  O   HOH A1121       8.722 -15.490   6.700  1.00 35.51           O  
HETATM 6649  O   HOH A1122      36.576  -0.698 -15.431  1.00 38.58           O  
HETATM 6650  O   HOH A1123      24.260  15.366   3.265  1.00 41.26           O  
HETATM 6651  O   HOH A1124      -1.514 -13.138   0.872  1.00 40.17           O  
HETATM 6652  O   HOH A1125       7.841  -0.532 -27.353  1.00 30.44           O  
HETATM 6653  O   HOH A1126      12.874   6.638   7.959  1.00 49.65           O  
HETATM 6654  O   HOH A1127       9.395 -24.902  16.531  1.00 47.22           O  
HETATM 6655  O   HOH A1128      -6.298 -29.810   5.931  1.00 54.53           O  
HETATM 6656  O   HOH A1129      36.718  -5.240 -10.499  1.00 47.19           O  
HETATM 6657  O   HOH A1130       7.629   2.559   2.456  1.00 39.31           O  
HETATM 6658  O   HOH A1131      11.667   3.429 -29.026  1.00 41.35           O  
HETATM 6659  O   HOH A1132       4.753  -5.370 -27.598  1.00 33.08           O  
HETATM 6660  O   HOH A1133      35.049  -6.662 -12.254  1.00 42.44           O  
HETATM 6661  O   HOH A1134      17.267 -28.088   3.749  1.00 48.57           O  
HETATM 6662  O   HOH A1135      -5.984 -27.425 -14.114  1.00 42.30           O  
HETATM 6663  O   HOH A1136      14.969 -36.316   1.058  1.00 41.78           O  
HETATM 6664  O   HOH A1137      11.392  14.029   3.449  1.00 32.87           O  
HETATM 6665  O   HOH A1138      28.895 -24.236   6.026  1.00 55.49           O  
HETATM 6666  O   HOH A1139      20.437   4.979   9.595  1.00 40.82           O  
HETATM 6667  O   HOH A1140      13.206  -5.368 -27.282  1.00 43.16           O  
HETATM 6668  O   HOH A1141      11.421 -11.611  16.152  1.00 30.24           O  
HETATM 6669  O   HOH A1142     -10.490  -8.853  -8.530  1.00 47.49           O  
HETATM 6670  O   HOH A1143      12.098 -26.090 -18.728  1.00 46.14           O  
HETATM 6671  O   HOH A1144      -6.324 -31.063  -6.974  1.00 56.38           O  
HETATM 6672  O   HOH A1145       0.792 -30.328   9.786  1.00 52.29           O  
HETATM 6673  O   HOH A1146      24.169  -1.224   9.368  1.00 42.18           O  
HETATM 6674  O   HOH C1043      24.800 -59.954  43.878  1.00 22.87           O  
HETATM 6675  O  AHOH C1044      22.858 -60.905  44.756  0.75 37.32           O  
HETATM 6676  O   HOH C1045      26.179 -63.773  46.039  1.00 25.46           O  
HETATM 6677  O   HOH C1046      27.944 -64.899  48.043  1.00 26.92           O  
HETATM 6678  O   HOH C1047      25.870 -61.070  46.048  1.00 27.12           O  
HETATM 6679  O   HOH C1048      42.887 -55.007  34.913  1.00 21.96           O  
HETATM 6680  O   HOH C1049      42.586 -57.811  35.868  1.00 17.07           O  
HETATM 6681  O   HOH C1050      27.875 -41.350  30.975  1.00 18.19           O  
HETATM 6682  O   HOH C1051      38.405 -47.505  30.449  1.00 17.64           O  
HETATM 6683  O   HOH C1052      39.162 -35.394  30.544  1.00 20.59           O  
HETATM 6684  O   HOH C1053      31.656 -40.305  38.667  1.00 18.51           O  
HETATM 6685  O   HOH C1054      27.802 -40.615  35.854  1.00 23.00           O  
HETATM 6686  O   HOH C1055      33.135 -33.938  35.771  1.00 19.96           O  
HETATM 6687  O   HOH C1056      36.865 -32.400  17.400  1.00 17.59           O  
HETATM 6688  O   HOH C1057      29.405 -32.449  33.779  1.00 17.43           O  
HETATM 6689  O   HOH C1058      10.563 -36.103  24.473  1.00 30.58           O  
HETATM 6690  O   HOH C1059      34.103 -40.260  45.758  1.00 20.83           O  
HETATM 6691  O   HOH C1060       8.703 -45.540  49.184  1.00 25.67           O  
HETATM 6692  O   HOH C1061      46.203 -53.165  32.436  1.00 20.86           O  
HETATM 6693  O   HOH C1062      36.444 -53.899  42.984  1.00 23.43           O  
HETATM 6694  O   HOH C1063      35.638 -42.537  19.942  1.00 26.85           O  
HETATM 6695  O   HOH C1064      37.298 -38.986  24.224  1.00 27.13           O  
HETATM 6696  O   HOH C1065      26.775 -40.031  33.214  1.00 23.49           O  
HETATM 6697  O   HOH C1066      34.141 -38.848  16.135  1.00 31.86           O  
HETATM 6698  O   HOH C1067      21.779 -38.099  20.031  1.00 28.77           O  
HETATM 6699  O   HOH C1068      32.407 -36.364  44.988  1.00 33.21           O  
HETATM 6700  O   HOH C1069      42.835 -50.389  37.489  1.00 21.27           O  
HETATM 6701  O   HOH C1070      36.740 -61.833  48.413  1.00 30.33           O  
HETATM 6702  O   HOH C1071      41.858 -35.333  15.766  1.00 26.96           O  
HETATM 6703  O   HOH C1072      24.597 -31.094  50.185  1.00 33.84           O  
HETATM 6704  O   HOH C1073      31.038 -67.284  34.400  1.00 27.28           O  
HETATM 6705  O   HOH C1074      26.755 -31.350  45.838  1.00 21.01           O  
HETATM 6706  O   HOH C1075      40.782 -42.048  33.812  1.00 32.33           O  
HETATM 6707  O   HOH C1076      41.975 -37.924  17.057  1.00 25.11           O  
HETATM 6708  O   HOH C1077      16.413 -37.272  59.997  1.00 39.99           O  
HETATM 6709  O   HOH C1078       6.503 -55.384  46.755  1.00 29.82           O  
HETATM 6710  O   HOH C1079      16.024 -63.601  41.072  1.00 31.07           O  
HETATM 6711  O   HOH C1080      44.258 -48.855  11.578  1.00 33.09           O  
HETATM 6712  O   HOH C1081      49.296 -59.996  32.675  1.00 25.51           O  
HETATM 6713  O   HOH C1082      16.268 -34.719  24.403  1.00 30.51           O  
HETATM 6714  O   HOH C1083      37.330 -40.715  21.018  1.00 20.83           O  
HETATM 6715  O   HOH C1084      34.084 -36.876  24.564  1.00 32.05           O  
HETATM 6716  O   HOH C1085      23.412 -32.436  24.442  1.00 32.79           O  
HETATM 6717  O   HOH C1086      28.881 -35.943  19.516  1.00 23.35           O  
HETATM 6718  O   HOH C1087      33.925 -41.016  18.518  1.00 30.78           O  
HETATM 6719  O   HOH C1088      29.419 -36.610  46.516  1.00 34.25           O  
HETATM 6720  O   HOH C1089      40.761 -39.288  34.794  1.00 43.63           O  
HETATM 6721  O   HOH C1090      20.622 -29.851  46.371  1.00 30.38           O  
HETATM 6722  O   HOH C1091      18.486 -40.140  12.791  1.00 36.21           O  
HETATM 6723  O   HOH C1092      24.062 -42.526  10.956  1.00 35.06           O  
HETATM 6724  O   HOH C1093      31.163 -34.304  28.688  1.00 34.07           O  
HETATM 6725  O   HOH C1094      22.329 -64.938  33.219  1.00 46.02           O  
HETATM 6726  O   HOH C1095      42.563 -43.564  35.243  1.00 37.21           O  
HETATM 6727  O   HOH C1096      13.167 -31.947  39.477  1.00 33.61           O  
HETATM 6728  O   HOH C1097      29.973 -31.027  21.059  1.00 34.44           O  
HETATM 6729  O   HOH C1098      14.805 -31.953  28.996  1.00 27.59           O  
HETATM 6730  O   HOH C1099      24.370 -38.593  19.471  1.00 31.49           O  
HETATM 6731  O   HOH C1100      35.270 -37.091  18.587  1.00 28.70           O  
HETATM 6732  O   HOH C1101      28.045 -32.967  47.414  1.00 27.89           O  
HETATM 6733  O   HOH C1102      41.606 -39.761  30.995  1.00 39.65           O  
HETATM 6734  O   HOH C1103       4.161 -56.638  44.762  1.00 37.59           O  
HETATM 6735  O   HOH C1104      12.123 -64.397  43.920  1.00 43.45           O  
HETATM 6736  O   HOH C1105      16.393 -32.367  26.398  1.00 42.79           O  
HETATM 6737  O   HOH C1106      12.175 -33.129  22.490  1.00 51.18           O  
HETATM 6738  O   HOH C1107      20.170 -48.789  11.380  1.00 36.49           O  
HETATM 6739  O   HOH C1108      35.386 -38.612  20.868  1.00 19.74           O  
HETATM 6740  O   HOH C1109      14.765 -34.012  54.855  1.00 41.70           O  
HETATM 6741  O   HOH C1110      31.453 -35.995  26.320  1.00 49.81           O  
HETATM 6742  O   HOH C1111      38.883 -40.778  43.008  1.00 45.46           O  
HETATM 6743  O   HOH C1112      18.479 -35.001  21.228  1.00 45.50           O  
HETATM 6744  O   HOH C1113      19.544 -67.521  43.965  1.00 32.07           O  
HETATM 6745  O   HOH C1114      41.353 -48.408  40.982  1.00 36.00           O  
HETATM 6746  O   HOH C1115      47.093 -42.699  12.384  1.00 39.32           O  
HETATM 6747  O   HOH C1116      40.159 -43.869  35.962  1.00 25.58           O  
HETATM 6748  O   HOH C1117      14.208 -58.947  57.154  1.00 34.03           O  
HETATM 6749  O   HOH C1118      32.712 -25.292  29.589  1.00 25.97           O  
HETATM 6750  O   HOH C1119      14.663 -56.757  55.458  1.00 34.87           O  
HETATM 6751  O   HOH C1120      25.761 -32.489  23.273  1.00 42.84           O  
HETATM 6752  O   HOH C1121      53.503 -55.978  35.557  1.00 45.24           O  
HETATM 6753  O   HOH C1122      30.476 -33.456  23.728  1.00 48.21           O  
HETATM 6754  O   HOH C1123       9.486 -50.481  25.385  1.00 42.28           O  
HETATM 6755  O   HOH C1124      48.901 -52.900  34.037  1.00 49.20           O  
HETATM 6756  O   HOH C1125      13.696 -55.046  27.380  1.00 34.03           O  
HETATM 6757  O   HOH C1126      44.942 -54.562  16.682  1.00 42.46           O  
HETATM 6758  O   HOH C1127      29.727 -37.923  50.530  1.00 43.11           O  
HETATM 6759  O   HOH C1128      23.278 -47.063   2.022  1.00 55.30           O  
HETATM 6760  O   HOH C1129      32.277 -63.150  23.063  1.00 46.17           O  
HETATM 6761  O   HOH C1130      40.034 -59.266  16.887  1.00 45.27           O  
HETATM 6762  O   HOH C1131      36.444 -67.251  31.726  1.00 47.35           O  
HETATM 6763  O   HOH C1132      29.323 -39.294  48.565  1.00 40.84           O  
HETATM 6764  O   HOH C1133      38.160 -41.004  23.568  1.00 36.20           O  
HETATM 6765  O   HOH C1134      42.021 -55.127   9.398  1.00 46.75           O  
HETATM 6766  O   HOH C1135      12.290 -52.646  20.960  1.00 40.45           O  
HETATM 6767  O   HOH C1136      29.903 -24.448  20.103  1.00 45.71           O  
HETATM 6768  O   HOH C1137      18.802 -32.111  53.249  1.00 40.41           O  
HETATM 6769  O   HOH C1138       0.673 -54.453  50.460  1.00 48.14           O  
HETATM 6770  O   HOH C1139      15.189 -45.580  11.553  1.00 44.93           O  
HETATM 6771  O   HOH C1140      31.278 -69.975  35.435  1.00 48.17           O  
HETATM 6772  O   HOH C1141       6.544 -62.604  54.805  1.00 46.25           O  
HETATM 6773  O   HOH C1142      47.163 -43.726  18.939  1.00 40.43           O  
HETATM 6774  O   HOH C1143      27.243 -21.531  26.649  1.00 42.29           O  
HETATM 6775  O   HOH C1144      20.690 -24.542  31.798  1.00 55.61           O  
CONECT  743 5448                                                                
CONECT  842 5963                                                                
CONECT 1029 5796                                                                
CONECT 1763 5730                                                                
CONECT 2114 5664                                                                
CONECT 2166 5880                                                                
CONECT 2179 5585                                                                
CONECT 3474 6009                                                                
CONECT 3573 6524                                                                
CONECT 3760 6357                                                                
CONECT 4481 6291                                                                
CONECT 4836 6225                                                                
CONECT 4888 6441                                                                
CONECT 4901 6146                                                                
CONECT 5448  743 5453 5464 5473                                                 
CONECT 5448 5481                                                                
CONECT 5449 5454 5485 5489                                                      
CONECT 5450 5457 5465                                                           
CONECT 5451 5468 5474                                                           
CONECT 5452 5477 5482                                                           
CONECT 5453 5448 5454 5457                                                      
CONECT 5454 5449 5453 5455                                                      
CONECT 5455 5454 5456 5459                                                      
CONECT 5456 5455 5457 5458                                                      
CONECT 5457 5450 5453 5456                                                      
CONECT 5458 5456                                                                
CONECT 5459 5455 5460                                                           
CONECT 5460 5459 5461                                                           
CONECT 5461 5460 5462 5463                                                      
CONECT 5462 5461                                                                
CONECT 5463 5461 5494                                                           
CONECT 5464 5448 5465 5468                                                      
CONECT 5465 5450 5464 5466                                                      
CONECT 5466 5465 5467 5469                                                      
CONECT 5467 5466 5468 5470                                                      
CONECT 5468 5451 5464 5467                                                      
CONECT 5469 5466                                                                
CONECT 5470 5467 5471 5472                                                      
CONECT 5471 5470                                                                
CONECT 5472 5470                                                                
CONECT 5473 5448 5474 5477                                                      
CONECT 5474 5451 5473 5475                                                      
CONECT 5475 5474 5476 5478                                                      
CONECT 5476 5475 5477 5479                                                      
CONECT 5477 5452 5473 5476                                                      
CONECT 5478 5475                                                                
CONECT 5479 5476 5480                                                           
CONECT 5480 5479                                                                
CONECT 5481 5448 5482 5485                                                      
CONECT 5482 5452 5481 5483                                                      
CONECT 5483 5482 5484 5486                                                      
CONECT 5484 5483 5485 5487                                                      
CONECT 5485 5449 5481 5484                                                      
CONECT 5486 5483                                                                
CONECT 5487 5484 5488 5489                                                      
CONECT 5488 5487                                                                
CONECT 5489 5449 5487 5490                                                      
CONECT 5490 5489 5491 5492                                                      
CONECT 5491 5490                                                                
CONECT 5492 5490 5493                                                           
CONECT 5493 5492                                                                
CONECT 5494 5463 5495                                                           
CONECT 5495 5494 5496                                                           
CONECT 5496 5495 5497 5498                                                      
CONECT 5497 5496                                                                
CONECT 5498 5496 5499                                                           
CONECT 5499 5498 5500                                                           
CONECT 5500 5499 5501                                                           
CONECT 5501 5500 5502 5503                                                      
CONECT 5502 5501                                                                
CONECT 5503 5501 5504                                                           
CONECT 5504 5503 5505                                                           
CONECT 5505 5504 5506                                                           
CONECT 5506 5505 5507 5508                                                      
CONECT 5507 5506                                                                
CONECT 5508 5506 5509 5510                                                      
CONECT 5509 5508 5511                                                           
CONECT 5510 5508 5512                                                           
CONECT 5511 5509 5513                                                           
CONECT 5512 5510 5514                                                           
CONECT 5513 5511 5515 5517                                                      
CONECT 5514 5512 5516 5518                                                      
CONECT 5515 5513                                                                
CONECT 5516 5514                                                                
CONECT 5517 5513                                                                
CONECT 5518 5514                                                                
CONECT 5519 5524 5535 5544 5552                                                 
CONECT 5519 6570                                                                
CONECT 5520 5525 5556 5560                                                      
CONECT 5521 5528 5536                                                           
CONECT 5522 5539 5545                                                           
CONECT 5523 5548 5553                                                           
CONECT 5524 5519 5525 5528                                                      
CONECT 5525 5520 5524 5526                                                      
CONECT 5526 5525 5527 5530                                                      
CONECT 5527 5526 5528 5529                                                      
CONECT 5528 5521 5524 5527                                                      
CONECT 5529 5527                                                                
CONECT 5530 5526 5531                                                           
CONECT 5531 5530 5532                                                           
CONECT 5532 5531 5533 5534                                                      
CONECT 5533 5532                                                                
CONECT 5534 5532 5565                                                           
CONECT 5535 5519 5536 5539                                                      
CONECT 5536 5521 5535 5537                                                      
CONECT 5537 5536 5538 5540                                                      
CONECT 5538 5537 5539 5541                                                      
CONECT 5539 5522 5535 5538                                                      
CONECT 5540 5537                                                                
CONECT 5541 5538 5542 5543                                                      
CONECT 5542 5541                                                                
CONECT 5543 5541                                                                
CONECT 5544 5519 5545 5548                                                      
CONECT 5545 5522 5544 5546                                                      
CONECT 5546 5545 5547 5549                                                      
CONECT 5547 5546 5548 5550                                                      
CONECT 5548 5523 5544 5547                                                      
CONECT 5549 5546                                                                
CONECT 5550 5547 5551                                                           
CONECT 5551 5550                                                                
CONECT 5552 5519 5553 5556                                                      
CONECT 5553 5523 5552 5554                                                      
CONECT 5554 5553 5555 5557                                                      
CONECT 5555 5554 5556 5558                                                      
CONECT 5556 5520 5552 5555                                                      
CONECT 5557 5554                                                                
CONECT 5558 5555 5559 5560                                                      
CONECT 5559 5558                                                                
CONECT 5560 5520 5558 5561                                                      
CONECT 5561 5560 5562 5563                                                      
CONECT 5562 5561                                                                
CONECT 5563 5561 5564                                                           
CONECT 5564 5563                                                                
CONECT 5565 5534 5566                                                           
CONECT 5566 5565 5567                                                           
CONECT 5567 5566 5568 5569                                                      
CONECT 5568 5567                                                                
CONECT 5569 5567 5570                                                           
CONECT 5570 5569 5571                                                           
CONECT 5571 5570 5572                                                           
CONECT 5572 5571 5573 5574                                                      
CONECT 5573 5572                                                                
CONECT 5574 5572 5575                                                           
CONECT 5575 5574 5576                                                           
CONECT 5576 5575 5577                                                           
CONECT 5577 5576 5578 5579                                                      
CONECT 5578 5577                                                                
CONECT 5579 5577 5580                                                           
CONECT 5580 5579 5581                                                           
CONECT 5581 5580 5582                                                           
CONECT 5582 5581 5583 5584                                                      
CONECT 5583 5582                                                                
CONECT 5584 5582                                                                
CONECT 5585 2179 5590 5601 5610                                                 
CONECT 5585 5618                                                                
CONECT 5586 5591 5622 5626                                                      
CONECT 5587 5594 5602                                                           
CONECT 5588 5605 5611                                                           
CONECT 5589 5614 5619                                                           
CONECT 5590 5585 5591 5594                                                      
CONECT 5591 5586 5590 5592                                                      
CONECT 5592 5591 5593 5596                                                      
CONECT 5593 5592 5594 5595                                                      
CONECT 5594 5587 5590 5593                                                      
CONECT 5595 5593                                                                
CONECT 5596 5592 5597                                                           
CONECT 5597 5596 5598                                                           
CONECT 5598 5597 5599 5600                                                      
CONECT 5599 5598                                                                
CONECT 5600 5598 5631                                                           
CONECT 5601 5585 5602 5605                                                      
CONECT 5602 5587 5601 5603                                                      
CONECT 5603 5602 5604 5606                                                      
CONECT 5604 5603 5605 5607                                                      
CONECT 5605 5588 5601 5604                                                      
CONECT 5606 5603                                                                
CONECT 5607 5604 5608 5609                                                      
CONECT 5608 5607                                                                
CONECT 5609 5607                                                                
CONECT 5610 5585 5611 5614                                                      
CONECT 5611 5588 5610 5612                                                      
CONECT 5612 5611 5613 5615                                                      
CONECT 5613 5612 5614 5616                                                      
CONECT 5614 5589 5610 5613                                                      
CONECT 5615 5612                                                                
CONECT 5616 5613 5617                                                           
CONECT 5617 5616                                                                
CONECT 5618 5585 5619 5622                                                      
CONECT 5619 5589 5618 5620                                                      
CONECT 5620 5619 5621 5623                                                      
CONECT 5621 5620 5622 5624                                                      
CONECT 5622 5586 5618 5621                                                      
CONECT 5623 5620                                                                
CONECT 5624 5621 5625 5626                                                      
CONECT 5625 5624                                                                
CONECT 5626 5586 5624 5627                                                      
CONECT 5627 5626 5628 5629                                                      
CONECT 5628 5627                                                                
CONECT 5629 5627 5630                                                           
CONECT 5630 5629                                                                
CONECT 5631 5600 5632                                                           
CONECT 5632 5631 5633                                                           
CONECT 5633 5632 5634 5635                                                      
CONECT 5634 5633                                                                
CONECT 5635 5633 5636                                                           
CONECT 5636 5635 5637                                                           
CONECT 5637 5636 5638 5639                                                      
CONECT 5638 5637 5640 5642                                                      
CONECT 5639 5637 5641 5643                                                      
CONECT 5640 5638                                                                
CONECT 5641 5639                                                                
CONECT 5642 5638 5644                                                           
CONECT 5643 5639 5645                                                           
CONECT 5644 5642 5646                                                           
CONECT 5645 5643 5647                                                           
CONECT 5646 5644 5648                                                           
CONECT 5647 5645 5649                                                           
CONECT 5648 5646 5650 5652                                                      
CONECT 5649 5647 5651 5653                                                      
CONECT 5650 5648                                                                
CONECT 5651 5649                                                                
CONECT 5652 5648 5654                                                           
CONECT 5653 5649 5655                                                           
CONECT 5654 5652 5656                                                           
CONECT 5655 5653 5657                                                           
CONECT 5656 5654 5658                                                           
CONECT 5657 5655 5659                                                           
CONECT 5658 5656 5660 5662                                                      
CONECT 5659 5657 5661 5663                                                      
CONECT 5660 5658                                                                
CONECT 5661 5659                                                                
CONECT 5662 5658                                                                
CONECT 5663 5659                                                                
CONECT 5664 2114 5669 5680 5689                                                 
CONECT 5664 5697                                                                
CONECT 5665 5670 5701 5705                                                      
CONECT 5666 5673 5681                                                           
CONECT 5667 5684 5690                                                           
CONECT 5668 5693 5698                                                           
CONECT 5669 5664 5670 5673                                                      
CONECT 5670 5665 5669 5671                                                      
CONECT 5671 5670 5672 5675                                                      
CONECT 5672 5671 5673 5674                                                      
CONECT 5673 5666 5669 5672                                                      
CONECT 5674 5672                                                                
CONECT 5675 5671 5676                                                           
CONECT 5676 5675 5677                                                           
CONECT 5677 5676 5678 5679                                                      
CONECT 5678 5677                                                                
CONECT 5679 5677 5710                                                           
CONECT 5680 5664 5681 5684                                                      
CONECT 5681 5666 5680 5682                                                      
CONECT 5682 5681 5683 5685                                                      
CONECT 5683 5682 5684 5686                                                      
CONECT 5684 5667 5680 5683                                                      
CONECT 5685 5682                                                                
CONECT 5686 5683 5687 5688                                                      
CONECT 5687 5686                                                                
CONECT 5688 5686                                                                
CONECT 5689 5664 5690 5693                                                      
CONECT 5690 5667 5689 5691                                                      
CONECT 5691 5690 5692 5694                                                      
CONECT 5692 5691 5693 5695                                                      
CONECT 5693 5668 5689 5692                                                      
CONECT 5694 5691                                                                
CONECT 5695 5692 5696                                                           
CONECT 5696 5695                                                                
CONECT 5697 5664 5698 5701                                                      
CONECT 5698 5668 5697 5699                                                      
CONECT 5699 5698 5700 5702                                                      
CONECT 5700 5699 5701 5703                                                      
CONECT 5701 5665 5697 5700                                                      
CONECT 5702 5699                                                                
CONECT 5703 5700 5704 5705                                                      
CONECT 5704 5703                                                                
CONECT 5705 5665 5703 5706                                                      
CONECT 5706 5705 5707 5708                                                      
CONECT 5707 5706                                                                
CONECT 5708 5706 5709                                                           
CONECT 5709 5708                                                                
CONECT 5710 5679 5711                                                           
CONECT 5711 5710 5712                                                           
CONECT 5712 5711 5713 5714                                                      
CONECT 5713 5712                                                                
CONECT 5714 5712 5715                                                           
CONECT 5715 5714 5716                                                           
CONECT 5716 5715 5717                                                           
CONECT 5717 5716 5718 5719                                                      
CONECT 5718 5717                                                                
CONECT 5719 5717 5720                                                           
CONECT 5720 5719 5721                                                           
CONECT 5721 5720 5722                                                           
CONECT 5722 5721 5723 5724                                                      
CONECT 5723 5722                                                                
CONECT 5724 5722 5725                                                           
CONECT 5725 5724 5726                                                           
CONECT 5726 5725 5727                                                           
CONECT 5727 5726 5728 5729                                                      
CONECT 5728 5727                                                                
CONECT 5729 5727                                                                
CONECT 5730 1763 5735 5746 5755                                                 
CONECT 5730 5763                                                                
CONECT 5731 5736 5767 5771                                                      
CONECT 5732 5739 5747                                                           
CONECT 5733 5750 5756                                                           
CONECT 5734 5759 5764                                                           
CONECT 5735 5730 5736 5739                                                      
CONECT 5736 5731 5735 5737                                                      
CONECT 5737 5736 5738 5741                                                      
CONECT 5738 5737 5739 5740                                                      
CONECT 5739 5732 5735 5738                                                      
CONECT 5740 5738                                                                
CONECT 5741 5737 5742                                                           
CONECT 5742 5741 5743                                                           
CONECT 5743 5742 5744 5745                                                      
CONECT 5744 5743                                                                
CONECT 5745 5743 5776                                                           
CONECT 5746 5730 5747 5750                                                      
CONECT 5747 5732 5746 5748                                                      
CONECT 5748 5747 5749 5751                                                      
CONECT 5749 5748 5750 5752                                                      
CONECT 5750 5733 5746 5749                                                      
CONECT 5751 5748                                                                
CONECT 5752 5749 5753 5754                                                      
CONECT 5753 5752                                                                
CONECT 5754 5752                                                                
CONECT 5755 5730 5756 5759                                                      
CONECT 5756 5733 5755 5757                                                      
CONECT 5757 5756 5758 5760                                                      
CONECT 5758 5757 5759 5761                                                      
CONECT 5759 5734 5755 5758                                                      
CONECT 5760 5757                                                                
CONECT 5761 5758 5762                                                           
CONECT 5762 5761                                                                
CONECT 5763 5730 5764 5767                                                      
CONECT 5764 5734 5763 5765                                                      
CONECT 5765 5764 5766 5768                                                      
CONECT 5766 5765 5767 5769                                                      
CONECT 5767 5731 5763 5766                                                      
CONECT 5768 5765                                                                
CONECT 5769 5766 5770 5771                                                      
CONECT 5770 5769                                                                
CONECT 5771 5731 5769 5772                                                      
CONECT 5772 5771 5773 5774                                                      
CONECT 5773 5772                                                                
CONECT 5774 5772 5775                                                           
CONECT 5775 5774                                                                
CONECT 5776 5745 5777                                                           
CONECT 5777 5776 5778                                                           
CONECT 5778 5777 5779 5780                                                      
CONECT 5779 5778                                                                
CONECT 5780 5778 5781                                                           
CONECT 5781 5780 5782                                                           
CONECT 5782 5781 5783                                                           
CONECT 5783 5782 5784 5785                                                      
CONECT 5784 5783                                                                
CONECT 5785 5783 5786                                                           
CONECT 5786 5785 5787                                                           
CONECT 5787 5786 5788                                                           
CONECT 5788 5787 5789 5790                                                      
CONECT 5789 5788                                                                
CONECT 5790 5788 5791                                                           
CONECT 5791 5790 5792                                                           
CONECT 5792 5791 5793                                                           
CONECT 5793 5792 5794 5795                                                      
CONECT 5794 5793                                                                
CONECT 5795 5793                                                                
CONECT 5796 1029 5802 5813 5822                                                 
CONECT 5796 5823 5838                                                           
CONECT 5797 5803 5843 5850                                                      
CONECT 5798 5803 5844 5851                                                      
CONECT 5799 5806 5814                                                           
CONECT 5800 5817 5824 5825                                                      
CONECT 5801 5830 5831 5839                                                      
CONECT 5802 5796 5803 5806                                                      
CONECT 5803 5797 5798 5802 5804                                                 
CONECT 5804 5803 5805 5808                                                      
CONECT 5805 5804 5806 5807                                                      
CONECT 5806 5799 5802 5805                                                      
CONECT 5807 5805                                                                
CONECT 5808 5804 5809                                                           
CONECT 5809 5808 5810                                                           
CONECT 5810 5809 5811 5812                                                      
CONECT 5811 5810                                                                
CONECT 5812 5810 5860                                                           
CONECT 5813 5796 5814 5817                                                      
CONECT 5814 5799 5813 5815                                                      
CONECT 5815 5814 5816 5818                                                      
CONECT 5816 5815 5817 5819                                                      
CONECT 5817 5800 5813 5816                                                      
CONECT 5818 5815                                                                
CONECT 5819 5816 5820 5821                                                      
CONECT 5820 5819                                                                
CONECT 5821 5819                                                                
CONECT 5822 5796 5824 5830                                                      
CONECT 5823 5796 5825 5831                                                      
CONECT 5824 5800 5822 5826                                                      
CONECT 5825 5800 5823 5827                                                      
CONECT 5826 5824 5828 5832                                                      
CONECT 5827 5825 5829 5833                                                      
CONECT 5828 5826 5830 5834                                                      
CONECT 5829 5827 5831 5835                                                      
CONECT 5830 5801 5822 5828                                                      
CONECT 5831 5801 5823 5829                                                      
CONECT 5832 5826                                                                
CONECT 5833 5827                                                                
CONECT 5834 5828 5836                                                           
CONECT 5835 5829 5837                                                           
CONECT 5836 5834                                                                
CONECT 5837 5835                                                                
CONECT 5838 5796 5839 5843 5844                                                 
CONECT 5839 5801 5838 5840                                                      
CONECT 5840 5839 5841 5842 5845                                                 
CONECT 5841 5840 5843 5846                                                      
CONECT 5842 5840 5844 5847                                                      
CONECT 5843 5797 5838 5841                                                      
CONECT 5844 5798 5838 5842                                                      
CONECT 5845 5840                                                                
CONECT 5846 5841 5848 5850                                                      
CONECT 5847 5842 5849 5851                                                      
CONECT 5848 5846                                                                
CONECT 5849 5847                                                                
CONECT 5850 5797 5846 5852                                                      
CONECT 5851 5798 5847 5853                                                      
CONECT 5852 5850 5854 5856                                                      
CONECT 5853 5851 5855 5857                                                      
CONECT 5854 5852                                                                
CONECT 5855 5853                                                                
CONECT 5856 5852 5858                                                           
CONECT 5857 5853 5859                                                           
CONECT 5858 5856                                                                
CONECT 5859 5857                                                                
CONECT 5860 5812 5861                                                           
CONECT 5861 5860 5862                                                           
CONECT 5862 5861 5863 5864                                                      
CONECT 5863 5862                                                                
CONECT 5864 5862 5865                                                           
CONECT 5865 5864 5866                                                           
CONECT 5866 5865 5867                                                           
CONECT 5867 5866 5868 5869                                                      
CONECT 5868 5867                                                                
CONECT 5869 5867 5870                                                           
CONECT 5870 5869 5871                                                           
CONECT 5871 5870 5872                                                           
CONECT 5872 5871 5873 5874                                                      
CONECT 5873 5872                                                                
CONECT 5874 5872 5875                                                           
CONECT 5875 5874 5876                                                           
CONECT 5876 5875 5877                                                           
CONECT 5877 5876 5878 5879                                                      
CONECT 5878 5877                                                                
CONECT 5879 5877                                                                
CONECT 5880 2166 5885 5896 5909                                                 
CONECT 5880 5924                                                                
CONECT 5881 5886 5928 5932                                                      
CONECT 5882 5889 5897                                                           
CONECT 5883 5901 5910 5911                                                      
CONECT 5884 5916 5917 5925                                                      
CONECT 5885 5880 5886 5889                                                      
CONECT 5886 5881 5885 5887                                                      
CONECT 5887 5886 5888 5891                                                      
CONECT 5888 5887 5889 5890                                                      
CONECT 5889 5882 5885 5888                                                      
CONECT 5890 5888                                                                
CONECT 5891 5887 5892                                                           
CONECT 5892 5891 5893                                                           
CONECT 5893 5892 5894 5895                                                      
CONECT 5894 5893                                                                
CONECT 5895 5893 5937                                                           
CONECT 5896 5880 5897 5901                                                      
CONECT 5897 5882 5896 5898                                                      
CONECT 5898 5897 5899 5900 5902                                                 
CONECT 5899 5898 5901 5903                                                      
CONECT 5900 5898 5901 5904                                                      
CONECT 5901 5883 5896 5899 5900                                                 
CONECT 5902 5898                                                                
CONECT 5903 5899 5905 5907                                                      
CONECT 5904 5900 5906 5908                                                      
CONECT 5905 5903                                                                
CONECT 5906 5904                                                                
CONECT 5907 5903                                                                
CONECT 5908 5904                                                                
CONECT 5909 5880 5910 5911 5916                                                 
CONECT 5909 5917                                                                
CONECT 5910 5883 5909 5912                                                      
CONECT 5911 5883 5909 5913                                                      
CONECT 5912 5910 5914 5918                                                      
CONECT 5913 5911 5915 5919                                                      
CONECT 5914 5912 5916 5920                                                      
CONECT 5915 5913 5917 5921                                                      
CONECT 5916 5884 5909 5914                                                      
CONECT 5917 5884 5909 5915                                                      
CONECT 5918 5912                                                                
CONECT 5919 5913                                                                
CONECT 5920 5914 5922                                                           
CONECT 5921 5915 5923                                                           
CONECT 5922 5920                                                                
CONECT 5923 5921                                                                
CONECT 5924 5880 5925 5928                                                      
CONECT 5925 5884 5924 5926                                                      
CONECT 5926 5925 5927 5929                                                      
CONECT 5927 5926 5928 5930                                                      
CONECT 5928 5881 5924 5927                                                      
CONECT 5929 5926                                                                
CONECT 5930 5927 5931 5932                                                      
CONECT 5931 5930                                                                
CONECT 5932 5881 5930 5933                                                      
CONECT 5933 5932 5934 5935                                                      
CONECT 5934 5933                                                                
CONECT 5935 5933 5936                                                           
CONECT 5936 5935                                                                
CONECT 5937 5895 5938                                                           
CONECT 5938 5937 5939                                                           
CONECT 5939 5938 5940 5941                                                      
CONECT 5940 5939                                                                
CONECT 5941 5939 5942                                                           
CONECT 5942 5941 5943                                                           
CONECT 5943 5942 5944                                                           
CONECT 5944 5943 5945 5946                                                      
CONECT 5945 5944                                                                
CONECT 5946 5944 5947                                                           
CONECT 5947 5946 5948                                                           
CONECT 5948 5947 5949                                                           
CONECT 5949 5948 5950 5951 5952                                                 
CONECT 5950 5949                                                                
CONECT 5951 5949 5953                                                           
CONECT 5952 5949 5954                                                           
CONECT 5953 5951 5955                                                           
CONECT 5954 5952 5956                                                           
CONECT 5955 5953 5957                                                           
CONECT 5956 5954 5958                                                           
CONECT 5957 5955 5959 5961                                                      
CONECT 5958 5956 5960 5962                                                      
CONECT 5959 5957                                                                
CONECT 5960 5958                                                                
CONECT 5961 5957                                                                
CONECT 5962 5958                                                                
CONECT 5963  842 5968 5979 5988                                                 
CONECT 5963 5996                                                                
CONECT 5964 5969 6000 6004                                                      
CONECT 5965 5972 5980                                                           
CONECT 5966 5983 5989                                                           
CONECT 5967 5992 5997                                                           
CONECT 5968 5963 5969 5972                                                      
CONECT 5969 5964 5968 5970                                                      
CONECT 5970 5969 5971 5974                                                      
CONECT 5971 5970 5972 5973                                                      
CONECT 5972 5965 5968 5971                                                      
CONECT 5973 5971                                                                
CONECT 5974 5970 5975                                                           
CONECT 5975 5974 5976                                                           
CONECT 5976 5975 5977 5978                                                      
CONECT 5977 5976                                                                
CONECT 5978 5976                                                                
CONECT 5979 5963 5980 5983                                                      
CONECT 5980 5965 5979 5981                                                      
CONECT 5981 5980 5982 5984                                                      
CONECT 5982 5981 5983 5985                                                      
CONECT 5983 5966 5979 5982                                                      
CONECT 5984 5981                                                                
CONECT 5985 5982 5986 5987                                                      
CONECT 5986 5985                                                                
CONECT 5987 5985                                                                
CONECT 5988 5963 5989 5992                                                      
CONECT 5989 5966 5988 5990                                                      
CONECT 5990 5989 5991 5993                                                      
CONECT 5991 5990 5992 5994                                                      
CONECT 5992 5967 5988 5991                                                      
CONECT 5993 5990                                                                
CONECT 5994 5991 5995                                                           
CONECT 5995 5994                                                                
CONECT 5996 5963 5997 6000                                                      
CONECT 5997 5967 5996 5998                                                      
CONECT 5998 5997 5999 6001                                                      
CONECT 5999 5998 6000 6002                                                      
CONECT 6000 5964 5996 5999                                                      
CONECT 6001 5998                                                                
CONECT 6002 5999 6003 6004                                                      
CONECT 6003 6002                                                                
CONECT 6004 5964 6002 6005                                                      
CONECT 6005 6004 6006 6007                                                      
CONECT 6006 6005                                                                
CONECT 6007 6005 6008                                                           
CONECT 6008 6007                                                                
CONECT 6009 3474 6014 6025 6034                                                 
CONECT 6009 6042                                                                
CONECT 6010 6015 6046 6050                                                      
CONECT 6011 6018 6026                                                           
CONECT 6012 6029 6035                                                           
CONECT 6013 6038 6043                                                           
CONECT 6014 6009 6015 6018                                                      
CONECT 6015 6010 6014 6016                                                      
CONECT 6016 6015 6017 6020                                                      
CONECT 6017 6016 6018 6019                                                      
CONECT 6018 6011 6014 6017                                                      
CONECT 6019 6017                                                                
CONECT 6020 6016 6021                                                           
CONECT 6021 6020 6022                                                           
CONECT 6022 6021 6023 6024                                                      
CONECT 6023 6022                                                                
CONECT 6024 6022 6055                                                           
CONECT 6025 6009 6026 6029                                                      
CONECT 6026 6011 6025 6027                                                      
CONECT 6027 6026 6028 6030                                                      
CONECT 6028 6027 6029 6031                                                      
CONECT 6029 6012 6025 6028                                                      
CONECT 6030 6027                                                                
CONECT 6031 6028 6032 6033                                                      
CONECT 6032 6031                                                                
CONECT 6033 6031                                                                
CONECT 6034 6009 6035 6038                                                      
CONECT 6035 6012 6034 6036                                                      
CONECT 6036 6035 6037 6039                                                      
CONECT 6037 6036 6038 6040                                                      
CONECT 6038 6013 6034 6037                                                      
CONECT 6039 6036                                                                
CONECT 6040 6037 6041                                                           
CONECT 6041 6040                                                                
CONECT 6042 6009 6043 6046                                                      
CONECT 6043 6013 6042 6044                                                      
CONECT 6044 6043 6045 6047                                                      
CONECT 6045 6044 6046 6048                                                      
CONECT 6046 6010 6042 6045                                                      
CONECT 6047 6044                                                                
CONECT 6048 6045 6049 6050                                                      
CONECT 6049 6048                                                                
CONECT 6050 6010 6048 6051                                                      
CONECT 6051 6050 6052 6053                                                      
CONECT 6052 6051                                                                
CONECT 6053 6051 6054                                                           
CONECT 6054 6053                                                                
CONECT 6055 6024 6056                                                           
CONECT 6056 6055 6057                                                           
CONECT 6057 6056 6058 6059                                                      
CONECT 6058 6057                                                                
CONECT 6059 6057 6060                                                           
CONECT 6060 6059 6061                                                           
CONECT 6061 6060 6062                                                           
CONECT 6062 6061 6063 6064                                                      
CONECT 6063 6062                                                                
CONECT 6064 6062 6065                                                           
CONECT 6065 6064 6066                                                           
CONECT 6066 6065 6067                                                           
CONECT 6067 6066 6068 6069                                                      
CONECT 6068 6067                                                                
CONECT 6069 6067 6070 6071                                                      
CONECT 6070 6069 6072                                                           
CONECT 6071 6069 6073                                                           
CONECT 6072 6070 6074                                                           
CONECT 6073 6071 6075                                                           
CONECT 6074 6072 6076 6078                                                      
CONECT 6075 6073 6077 6079                                                      
CONECT 6076 6074                                                                
CONECT 6077 6075                                                                
CONECT 6078 6074                                                                
CONECT 6079 6075                                                                
CONECT 6080 6085 6096 6105 6113                                                 
CONECT 6080 6674                                                                
CONECT 6081 6086 6117 6121                                                      
CONECT 6082 6089 6097                                                           
CONECT 6083 6100 6106                                                           
CONECT 6084 6109 6114                                                           
CONECT 6085 6080 6086 6089                                                      
CONECT 6086 6081 6085 6087                                                      
CONECT 6087 6086 6088 6091                                                      
CONECT 6088 6087 6089 6090                                                      
CONECT 6089 6082 6085 6088                                                      
CONECT 6090 6088                                                                
CONECT 6091 6087 6092                                                           
CONECT 6092 6091 6093                                                           
CONECT 6093 6092 6094 6095                                                      
CONECT 6094 6093                                                                
CONECT 6095 6093 6126                                                           
CONECT 6096 6080 6097 6100                                                      
CONECT 6097 6082 6096 6098                                                      
CONECT 6098 6097 6099 6101                                                      
CONECT 6099 6098 6100 6102                                                      
CONECT 6100 6083 6096 6099                                                      
CONECT 6101 6098                                                                
CONECT 6102 6099 6103 6104                                                      
CONECT 6103 6102                                                                
CONECT 6104 6102                                                                
CONECT 6105 6080 6106 6109                                                      
CONECT 6106 6083 6105 6107                                                      
CONECT 6107 6106 6108 6110                                                      
CONECT 6108 6107 6109 6111                                                      
CONECT 6109 6084 6105 6108                                                      
CONECT 6110 6107                                                                
CONECT 6111 6108 6112                                                           
CONECT 6112 6111                                                                
CONECT 6113 6080 6114 6117                                                      
CONECT 6114 6084 6113 6115                                                      
CONECT 6115 6114 6116 6118                                                      
CONECT 6116 6115 6117 6119                                                      
CONECT 6117 6081 6113 6116                                                      
CONECT 6118 6115                                                                
CONECT 6119 6116 6120 6121                                                      
CONECT 6120 6119                                                                
CONECT 6121 6081 6119 6122                                                      
CONECT 6122 6121 6123 6124                                                      
CONECT 6123 6122                                                                
CONECT 6124 6122 6125                                                           
CONECT 6125 6124                                                                
CONECT 6126 6095 6127                                                           
CONECT 6127 6126 6128                                                           
CONECT 6128 6127 6129 6130                                                      
CONECT 6129 6128                                                                
CONECT 6130 6128 6131                                                           
CONECT 6131 6130 6132                                                           
CONECT 6132 6131 6133                                                           
CONECT 6133 6132 6134 6135                                                      
CONECT 6134 6133                                                                
CONECT 6135 6133 6136                                                           
CONECT 6136 6135 6137                                                           
CONECT 6137 6136 6138                                                           
CONECT 6138 6137 6139 6140                                                      
CONECT 6139 6138                                                                
CONECT 6140 6138 6141                                                           
CONECT 6141 6140 6142                                                           
CONECT 6142 6141 6143                                                           
CONECT 6143 6142 6144 6145                                                      
CONECT 6144 6143                                                                
CONECT 6145 6143                                                                
CONECT 6146 4901 6151 6162 6171                                                 
CONECT 6146 6179                                                                
CONECT 6147 6152 6183 6187                                                      
CONECT 6148 6155 6163                                                           
CONECT 6149 6166 6172                                                           
CONECT 6150 6175 6180                                                           
CONECT 6151 6146 6152 6155                                                      
CONECT 6152 6147 6151 6153                                                      
CONECT 6153 6152 6154 6157                                                      
CONECT 6154 6153 6155 6156                                                      
CONECT 6155 6148 6151 6154                                                      
CONECT 6156 6154                                                                
CONECT 6157 6153 6158                                                           
CONECT 6158 6157 6159                                                           
CONECT 6159 6158 6160 6161                                                      
CONECT 6160 6159                                                                
CONECT 6161 6159 6192                                                           
CONECT 6162 6146 6163 6166                                                      
CONECT 6163 6148 6162 6164                                                      
CONECT 6164 6163 6165 6167                                                      
CONECT 6165 6164 6166 6168                                                      
CONECT 6166 6149 6162 6165                                                      
CONECT 6167 6164                                                                
CONECT 6168 6165 6169 6170                                                      
CONECT 6169 6168                                                                
CONECT 6170 6168                                                                
CONECT 6171 6146 6172 6175                                                      
CONECT 6172 6149 6171 6173                                                      
CONECT 6173 6172 6174 6176                                                      
CONECT 6174 6173 6175 6177                                                      
CONECT 6175 6150 6171 6174                                                      
CONECT 6176 6173                                                                
CONECT 6177 6174 6178                                                           
CONECT 6178 6177                                                                
CONECT 6179 6146 6180 6183                                                      
CONECT 6180 6150 6179 6181                                                      
CONECT 6181 6180 6182 6184                                                      
CONECT 6182 6181 6183 6185                                                      
CONECT 6183 6147 6179 6182                                                      
CONECT 6184 6181                                                                
CONECT 6185 6182 6186 6187                                                      
CONECT 6186 6185                                                                
CONECT 6187 6147 6185 6188                                                      
CONECT 6188 6187 6189 6190                                                      
CONECT 6189 6188                                                                
CONECT 6190 6188 6191                                                           
CONECT 6191 6190                                                                
CONECT 6192 6161 6193                                                           
CONECT 6193 6192 6194                                                           
CONECT 6194 6193 6195 6196                                                      
CONECT 6195 6194                                                                
CONECT 6196 6194 6197                                                           
CONECT 6197 6196 6198                                                           
CONECT 6198 6197 6199 6200                                                      
CONECT 6199 6198 6201 6203                                                      
CONECT 6200 6198 6202 6204                                                      
CONECT 6201 6199                                                                
CONECT 6202 6200                                                                
CONECT 6203 6199 6205                                                           
CONECT 6204 6200 6206                                                           
CONECT 6205 6203 6207                                                           
CONECT 6206 6204 6208                                                           
CONECT 6207 6205 6209                                                           
CONECT 6208 6206 6210                                                           
CONECT 6209 6207 6211 6213                                                      
CONECT 6210 6208 6212 6214                                                      
CONECT 6211 6209                                                                
CONECT 6212 6210                                                                
CONECT 6213 6209 6215                                                           
CONECT 6214 6210 6216                                                           
CONECT 6215 6213 6217                                                           
CONECT 6216 6214 6218                                                           
CONECT 6217 6215 6219                                                           
CONECT 6218 6216 6220                                                           
CONECT 6219 6217 6221 6223                                                      
CONECT 6220 6218 6222 6224                                                      
CONECT 6221 6219                                                                
CONECT 6222 6220                                                                
CONECT 6223 6219                                                                
CONECT 6224 6220                                                                
CONECT 6225 4836 6230 6241 6250                                                 
CONECT 6225 6258                                                                
CONECT 6226 6231 6262 6266                                                      
CONECT 6227 6234 6242                                                           
CONECT 6228 6245 6251                                                           
CONECT 6229 6254 6259                                                           
CONECT 6230 6225 6231 6234                                                      
CONECT 6231 6226 6230 6232                                                      
CONECT 6232 6231 6233 6236                                                      
CONECT 6233 6232 6234 6235                                                      
CONECT 6234 6227 6230 6233                                                      
CONECT 6235 6233                                                                
CONECT 6236 6232 6237                                                           
CONECT 6237 6236 6238                                                           
CONECT 6238 6237 6239 6240                                                      
CONECT 6239 6238                                                                
CONECT 6240 6238 6271                                                           
CONECT 6241 6225 6242 6245                                                      
CONECT 6242 6227 6241 6243                                                      
CONECT 6243 6242 6244 6246                                                      
CONECT 6244 6243 6245 6247                                                      
CONECT 6245 6228 6241 6244                                                      
CONECT 6246 6243                                                                
CONECT 6247 6244 6248 6249                                                      
CONECT 6248 6247                                                                
CONECT 6249 6247                                                                
CONECT 6250 6225 6251 6254                                                      
CONECT 6251 6228 6250 6252                                                      
CONECT 6252 6251 6253 6255                                                      
CONECT 6253 6252 6254 6256                                                      
CONECT 6254 6229 6250 6253                                                      
CONECT 6255 6252                                                                
CONECT 6256 6253 6257                                                           
CONECT 6257 6256                                                                
CONECT 6258 6225 6259 6262                                                      
CONECT 6259 6229 6258 6260                                                      
CONECT 6260 6259 6261 6263                                                      
CONECT 6261 6260 6262 6264                                                      
CONECT 6262 6226 6258 6261                                                      
CONECT 6263 6260                                                                
CONECT 6264 6261 6265 6266                                                      
CONECT 6265 6264                                                                
CONECT 6266 6226 6264 6267                                                      
CONECT 6267 6266 6268 6269                                                      
CONECT 6268 6267                                                                
CONECT 6269 6267 6270                                                           
CONECT 6270 6269                                                                
CONECT 6271 6240 6272                                                           
CONECT 6272 6271 6273                                                           
CONECT 6273 6272 6274 6275                                                      
CONECT 6274 6273                                                                
CONECT 6275 6273 6276                                                           
CONECT 6276 6275 6277                                                           
CONECT 6277 6276 6278                                                           
CONECT 6278 6277 6279 6280                                                      
CONECT 6279 6278                                                                
CONECT 6280 6278 6281                                                           
CONECT 6281 6280 6282                                                           
CONECT 6282 6281 6283                                                           
CONECT 6283 6282 6284 6285                                                      
CONECT 6284 6283                                                                
CONECT 6285 6283 6286                                                           
CONECT 6286 6285 6287                                                           
CONECT 6287 6286 6288                                                           
CONECT 6288 6287 6289 6290                                                      
CONECT 6289 6288                                                                
CONECT 6290 6288                                                                
CONECT 6291 4481 6296 6307 6316                                                 
CONECT 6291 6324                                                                
CONECT 6292 6297 6328 6332                                                      
CONECT 6293 6300 6308                                                           
CONECT 6294 6311 6317                                                           
CONECT 6295 6320 6325                                                           
CONECT 6296 6291 6297 6300                                                      
CONECT 6297 6292 6296 6298                                                      
CONECT 6298 6297 6299 6302                                                      
CONECT 6299 6298 6300 6301                                                      
CONECT 6300 6293 6296 6299                                                      
CONECT 6301 6299                                                                
CONECT 6302 6298 6303                                                           
CONECT 6303 6302 6304                                                           
CONECT 6304 6303 6305 6306                                                      
CONECT 6305 6304                                                                
CONECT 6306 6304 6337                                                           
CONECT 6307 6291 6308 6311                                                      
CONECT 6308 6293 6307 6309                                                      
CONECT 6309 6308 6310 6312                                                      
CONECT 6310 6309 6311 6313                                                      
CONECT 6311 6294 6307 6310                                                      
CONECT 6312 6309                                                                
CONECT 6313 6310 6314 6315                                                      
CONECT 6314 6313                                                                
CONECT 6315 6313                                                                
CONECT 6316 6291 6317 6320                                                      
CONECT 6317 6294 6316 6318                                                      
CONECT 6318 6317 6319 6321                                                      
CONECT 6319 6318 6320 6322                                                      
CONECT 6320 6295 6316 6319                                                      
CONECT 6321 6318                                                                
CONECT 6322 6319 6323                                                           
CONECT 6323 6322                                                                
CONECT 6324 6291 6325 6328                                                      
CONECT 6325 6295 6324 6326                                                      
CONECT 6326 6325 6327 6329                                                      
CONECT 6327 6326 6328 6330                                                      
CONECT 6328 6292 6324 6327                                                      
CONECT 6329 6326                                                                
CONECT 6330 6327 6331 6332                                                      
CONECT 6331 6330                                                                
CONECT 6332 6292 6330 6333                                                      
CONECT 6333 6332 6334 6335                                                      
CONECT 6334 6333                                                                
CONECT 6335 6333 6336                                                           
CONECT 6336 6335                                                                
CONECT 6337 6306 6338                                                           
CONECT 6338 6337 6339                                                           
CONECT 6339 6338 6340 6341                                                      
CONECT 6340 6339                                                                
CONECT 6341 6339 6342                                                           
CONECT 6342 6341 6343                                                           
CONECT 6343 6342 6344                                                           
CONECT 6344 6343 6345 6346                                                      
CONECT 6345 6344                                                                
CONECT 6346 6344 6347                                                           
CONECT 6347 6346 6348                                                           
CONECT 6348 6347 6349                                                           
CONECT 6349 6348 6350 6351                                                      
CONECT 6350 6349                                                                
CONECT 6351 6349 6352                                                           
CONECT 6352 6351 6353                                                           
CONECT 6353 6352 6354                                                           
CONECT 6354 6353 6355 6356                                                      
CONECT 6355 6354                                                                
CONECT 6356 6354                                                                
CONECT 6357 3760 6363 6374 6383                                                 
CONECT 6357 6384 6399                                                           
CONECT 6358 6364 6404 6411                                                      
CONECT 6359 6364 6405 6412                                                      
CONECT 6360 6367 6375                                                           
CONECT 6361 6378 6385 6386                                                      
CONECT 6362 6391 6392 6400                                                      
CONECT 6363 6357 6364 6367                                                      
CONECT 6364 6358 6359 6363 6365                                                 
CONECT 6365 6364 6366 6369                                                      
CONECT 6366 6365 6367 6368                                                      
CONECT 6367 6360 6363 6366                                                      
CONECT 6368 6366                                                                
CONECT 6369 6365 6370                                                           
CONECT 6370 6369 6371                                                           
CONECT 6371 6370 6372 6373                                                      
CONECT 6372 6371                                                                
CONECT 6373 6371 6421                                                           
CONECT 6374 6357 6375 6378                                                      
CONECT 6375 6360 6374 6376                                                      
CONECT 6376 6375 6377 6379                                                      
CONECT 6377 6376 6378 6380                                                      
CONECT 6378 6361 6374 6377                                                      
CONECT 6379 6376                                                                
CONECT 6380 6377 6381 6382                                                      
CONECT 6381 6380                                                                
CONECT 6382 6380                                                                
CONECT 6383 6357 6385 6391                                                      
CONECT 6384 6357 6386 6392                                                      
CONECT 6385 6361 6383 6387                                                      
CONECT 6386 6361 6384 6388                                                      
CONECT 6387 6385 6389 6393                                                      
CONECT 6388 6386 6390 6394                                                      
CONECT 6389 6387 6391 6395                                                      
CONECT 6390 6388 6392 6396                                                      
CONECT 6391 6362 6383 6389                                                      
CONECT 6392 6362 6384 6390                                                      
CONECT 6393 6387                                                                
CONECT 6394 6388                                                                
CONECT 6395 6389 6397                                                           
CONECT 6396 6390 6398                                                           
CONECT 6397 6395                                                                
CONECT 6398 6396                                                                
CONECT 6399 6357 6400 6404 6405                                                 
CONECT 6400 6362 6399 6401                                                      
CONECT 6401 6400 6402 6403 6406                                                 
CONECT 6402 6401 6404 6407                                                      
CONECT 6403 6401 6405 6408                                                      
CONECT 6404 6358 6399 6402                                                      
CONECT 6405 6359 6399 6403                                                      
CONECT 6406 6401                                                                
CONECT 6407 6402 6409 6411                                                      
CONECT 6408 6403 6410 6412                                                      
CONECT 6409 6407                                                                
CONECT 6410 6408                                                                
CONECT 6411 6358 6407 6413                                                      
CONECT 6412 6359 6408 6414                                                      
CONECT 6413 6411 6415 6417                                                      
CONECT 6414 6412 6416 6418                                                      
CONECT 6415 6413                                                                
CONECT 6416 6414                                                                
CONECT 6417 6413 6419                                                           
CONECT 6418 6414 6420                                                           
CONECT 6419 6417                                                                
CONECT 6420 6418                                                                
CONECT 6421 6373 6422                                                           
CONECT 6422 6421 6423                                                           
CONECT 6423 6422 6424 6425                                                      
CONECT 6424 6423                                                                
CONECT 6425 6423 6426                                                           
CONECT 6426 6425 6427                                                           
CONECT 6427 6426 6428                                                           
CONECT 6428 6427 6429 6430                                                      
CONECT 6429 6428                                                                
CONECT 6430 6428 6431                                                           
CONECT 6431 6430 6432                                                           
CONECT 6432 6431 6433                                                           
CONECT 6433 6432 6434 6435                                                      
CONECT 6434 6433                                                                
CONECT 6435 6433 6436                                                           
CONECT 6436 6435 6437                                                           
CONECT 6437 6436 6438                                                           
CONECT 6438 6437 6439 6440                                                      
CONECT 6439 6438                                                                
CONECT 6440 6438                                                                
CONECT 6441 4888 6446 6457 6470                                                 
CONECT 6441 6485                                                                
CONECT 6442 6447 6489 6493                                                      
CONECT 6443 6450 6458                                                           
CONECT 6444 6462 6471 6472                                                      
CONECT 6445 6477 6478 6486                                                      
CONECT 6446 6441 6447 6450                                                      
CONECT 6447 6442 6446 6448                                                      
CONECT 6448 6447 6449 6452                                                      
CONECT 6449 6448 6450 6451                                                      
CONECT 6450 6443 6446 6449                                                      
CONECT 6451 6449                                                                
CONECT 6452 6448 6453                                                           
CONECT 6453 6452 6454                                                           
CONECT 6454 6453 6455 6456                                                      
CONECT 6455 6454                                                                
CONECT 6456 6454 6498                                                           
CONECT 6457 6441 6458 6462                                                      
CONECT 6458 6443 6457 6459                                                      
CONECT 6459 6458 6460 6461 6463                                                 
CONECT 6460 6459 6462 6464                                                      
CONECT 6461 6459 6462 6465                                                      
CONECT 6462 6444 6457 6460 6461                                                 
CONECT 6463 6459                                                                
CONECT 6464 6460 6466 6468                                                      
CONECT 6465 6461 6467 6469                                                      
CONECT 6466 6464                                                                
CONECT 6467 6465                                                                
CONECT 6468 6464                                                                
CONECT 6469 6465                                                                
CONECT 6470 6441 6471 6472 6477                                                 
CONECT 6470 6478                                                                
CONECT 6471 6444 6470 6473                                                      
CONECT 6472 6444 6470 6474                                                      
CONECT 6473 6471 6475 6479                                                      
CONECT 6474 6472 6476 6480                                                      
CONECT 6475 6473 6477 6481                                                      
CONECT 6476 6474 6478 6482                                                      
CONECT 6477 6445 6470 6475                                                      
CONECT 6478 6445 6470 6476                                                      
CONECT 6479 6473                                                                
CONECT 6480 6474                                                                
CONECT 6481 6475 6483                                                           
CONECT 6482 6476 6484                                                           
CONECT 6483 6481                                                                
CONECT 6484 6482                                                                
CONECT 6485 6441 6486 6489                                                      
CONECT 6486 6445 6485 6487                                                      
CONECT 6487 6486 6488 6490                                                      
CONECT 6488 6487 6489 6491                                                      
CONECT 6489 6442 6485 6488                                                      
CONECT 6490 6487                                                                
CONECT 6491 6488 6492 6493                                                      
CONECT 6492 6491                                                                
CONECT 6493 6442 6491 6494                                                      
CONECT 6494 6493 6495 6496                                                      
CONECT 6495 6494                                                                
CONECT 6496 6494 6497                                                           
CONECT 6497 6496                                                                
CONECT 6498 6456 6499                                                           
CONECT 6499 6498 6500                                                           
CONECT 6500 6499 6501 6502                                                      
CONECT 6501 6500                                                                
CONECT 6502 6500 6503                                                           
CONECT 6503 6502 6504                                                           
CONECT 6504 6503 6505                                                           
CONECT 6505 6504 6506 6507                                                      
CONECT 6506 6505                                                                
CONECT 6507 6505 6508                                                           
CONECT 6508 6507 6509                                                           
CONECT 6509 6508 6510                                                           
CONECT 6510 6509 6511 6512 6513                                                 
CONECT 6511 6510                                                                
CONECT 6512 6510 6514                                                           
CONECT 6513 6510 6515                                                           
CONECT 6514 6512 6516                                                           
CONECT 6515 6513 6517                                                           
CONECT 6516 6514 6518                                                           
CONECT 6517 6515 6519                                                           
CONECT 6518 6516 6520 6522                                                      
CONECT 6519 6517 6521 6523                                                      
CONECT 6520 6518                                                                
CONECT 6521 6519                                                                
CONECT 6522 6518                                                                
CONECT 6523 6519                                                                
CONECT 6524 3573 6529 6540 6549                                                 
CONECT 6524 6557                                                                
CONECT 6525 6530 6561 6565                                                      
CONECT 6526 6533 6541                                                           
CONECT 6527 6544 6550                                                           
CONECT 6528 6553 6558                                                           
CONECT 6529 6524 6530 6533                                                      
CONECT 6530 6525 6529 6531                                                      
CONECT 6531 6530 6532 6535                                                      
CONECT 6532 6531 6533 6534                                                      
CONECT 6533 6526 6529 6532                                                      
CONECT 6534 6532                                                                
CONECT 6535 6531 6536                                                           
CONECT 6536 6535 6537                                                           
CONECT 6537 6536 6538 6539                                                      
CONECT 6538 6537                                                                
CONECT 6539 6537                                                                
CONECT 6540 6524 6541 6544                                                      
CONECT 6541 6526 6540 6542                                                      
CONECT 6542 6541 6543 6545                                                      
CONECT 6543 6542 6544 6546                                                      
CONECT 6544 6527 6540 6543                                                      
CONECT 6545 6542                                                                
CONECT 6546 6543 6547 6548                                                      
CONECT 6547 6546                                                                
CONECT 6548 6546                                                                
CONECT 6549 6524 6550 6553                                                      
CONECT 6550 6527 6549 6551                                                      
CONECT 6551 6550 6552 6554                                                      
CONECT 6552 6551 6553 6555                                                      
CONECT 6553 6528 6549 6552                                                      
CONECT 6554 6551                                                                
CONECT 6555 6552 6556                                                           
CONECT 6556 6555                                                                
CONECT 6557 6524 6558 6561                                                      
CONECT 6558 6528 6557 6559                                                      
CONECT 6559 6558 6560 6562                                                      
CONECT 6560 6559 6561 6563                                                      
CONECT 6561 6525 6557 6560                                                      
CONECT 6562 6559                                                                
CONECT 6563 6560 6564 6565                                                      
CONECT 6564 6563                                                                
CONECT 6565 6525 6563 6566                                                      
CONECT 6566 6565 6567 6568                                                      
CONECT 6567 6566                                                                
CONECT 6568 6566 6569                                                           
CONECT 6569 6568                                                                
CONECT 6570 5519                                                                
CONECT 6674 6080                                                                
MASTER      700    0   16   16   44    0   68    6 6773    2 1156   58          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.