CNRS Nantes University UFIP UFIP
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***  VIRAL PROTEIN 26-MAR-18 6G44  ***

elNémo ID: 210123201934113469

Job options:

ID        	=	 210123201934113469
JOBID     	=	 VIRAL PROTEIN 26-MAR-18 6G44
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    VIRAL PROTEIN                           26-MAR-18   6G44              
TITLE      TERMINAL DOMAIN                                                      
COMPND     TERMINAL DOMAIN                                                      
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0230                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) :   1.50                         
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) :  47.38                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) :  99.64                         
REMARK   3   NUMBER OF REFLECTIONS             :  354090                        
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) : 0.13585                         
REMARK   3   R VALUE            (WORKING SET) :  0.13459                        
REMARK   3   FREE R VALUE                     :  0.15977                        
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 18637                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           :      20                      
REMARK   3   BIN RESOLUTION RANGE HIGH           :    1.500                     
REMARK   3   BIN RESOLUTION RANGE LOW            :    1.539                     
REMARK   3   REFLECTION IN BIN     (WORKING SET) :    26077                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) :    99.77                     
REMARK   3   BIN R VALUE           (WORKING SET) :    0.191                     
REMARK   3   BIN FREE R VALUE SET COUNT          :     1373                     
REMARK   3   BIN FREE R VALUE                    :    0.227                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                :    14049                                
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) :  18.454                        
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) :    -0.11                                             
REMARK   3    B22 (A**2) :     0.36                                             
REMARK   3    B33 (A**2) :    -0.24                                             
REMARK   3    B12 (A**2) :     0.00                                             
REMARK   3    B13 (A**2) :     0.00                                             
REMARK   3    B23 (A**2) :    -0.00                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A):   0.051       
REMARK   3   ESU BASED ON FREE R VALUE                       (A):   0.049       
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A):   0.030       
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2):   1.792       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      :   0.974                       
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE :   0.967                       
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12735 ; 0.009 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A): 11599 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17414 ; 1.379 ; 1.669       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 27353 ; 0.968 ; 1.641       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1695 ; 6.541 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   602 ;35.708 ;24.053       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2186 ;10.805 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ; 8.755 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1761 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14312 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2228 ; 0.001 ; 0.020       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6326 ; 1.345 ; 1.619       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6325 ; 1.345 ; 1.619       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7949 ; 1.826 ; 2.439       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS (A**2)  :  7950 ; 1.825 ; 2.439       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6409 ; 1.887 ; 1.893       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS  (A**2)  :  6409 ; 1.886 ; 1.893       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS (A**2)  :  9390 ; 2.388 ; 2.733       
REMARK   3   LONG RANGE B REFINED ATOMS (A**2)    : 13818 ; 3.390 ;20.637       
REMARK   3   LONG RANGE B OTHER ATOMS (A**2)      : 13474 ; 3.030 ;19.926       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 24334 ; 2.028 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  1075 ;23.482 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 24573 ;10.728 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  :   3                               
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     2    516       B     2    516   16185  0.07  0.05     
REMARK   3    2     A     2    515       C     2    515   16105  0.07  0.05     
REMARK   3    3     B     2    515       C     2    515   16155  0.07  0.05     
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : NULL                                     
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED :  MASK                                                
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   :   1.10                                        
REMARK   3   ION PROBE RADIUS   :   0.70                                        
REMARK   3   SHRINKAGE RADIUS   :   0.70                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : REFINED INDIVIDUALLY                                
REMARK   3                                                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 372727                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.575                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.8900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.55                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6G43                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE, 1.2 - 1.7 M    
REMARK 280  AMMONIUM SULFATE, PH 3.5, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 31850 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 52220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -508.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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            
SEQRES   1 A  520  GLY ALA MET GLY MET ASN THR PRO PRO GLU LEU ASP THR          
SEQRES   2 A  520  VAL LEU GLN ALA PRO TYR ALA TYR ASN TRP PRO THR SER          
SEQRES   3 A  520  LYS ASN VAL LYS ILE ALA SER ARG ILE GLY ILE PRO TYR          
SEQRES   4 A  520  SER THR PHE GLN THR ILE GLN PRO VAL SER ASP ALA PRO          
SEQRES   5 A  520  ASN ASN GLY ILE GLY GLN ILE THR PHE ASN GLN PRO LEU          
SEQRES   6 A  520  GLY ASN LEU THR GLY GLY ALA PRO ARG LEU ARG VAL SER          
SEQRES   7 A  520  PHE THR ALA GLU ILE LYS ASN ILE LEU ALA ASP SER SER          
SEQRES   8 A  520  LEU LYS ASP GLN ILE GLY LEU LYS SER PHE PRO VAL ASN          
SEQRES   9 A  520  ARG SER ILE PRO VAL ALA VAL ILE ASN MET ASN GLY LYS          
SEQRES  10 A  520  THR PHE THR SER TYR PRO ALA GLN LEU ILE LYS LEU HIS          
SEQRES  11 A  520  GLN TYR ASN ALA ASP PRO LEU GLU LEU ALA LEU LEU SER          
SEQRES  12 A  520  PRO CYS SER ASP VAL ASP GLU TYR ASN LYS ILE LYS ALA          
SEQRES  13 A  520  VAL SER MET ASN ASN PRO TYR ARG GLN GLY THR GLU SER          
SEQRES  14 A  520  THR ASP SER ARG MET SER ARG GLY LEU GLY CYS ASN TYR          
SEQRES  15 A  520  ALA TYR TYR ILE HIS PRO ARG ALA ALA GLY SER THR SER          
SEQRES  16 A  520  VAL LYS ILE ASP PHE VAL VAL ASP GLU ALA LEU VAL ALA          
SEQRES  17 A  520  ASN PRO THR GLN TYR LYS ASN ILE LYS ASP PRO VAL PRO          
SEQRES  18 A  520  PHE ARG ASN LEU ASN THR PHE LYS VAL ILE LEU ASP GLY          
SEQRES  19 A  520  GLN PHE LYS PRO GLU ASN MET ILE GLY ILE ALA ASP ASP          
SEQRES  20 A  520  VAL LYS LEU VAL ALA GLY LYS ALA ASP PHE GLU VAL ASP          
SEQRES  21 A  520  ILE THR GLY PHE LYS ILE ASN MET LEU VAL GLN ASN TRP          
SEQRES  22 A  520  VAL ALA PRO LEU GLU ILE GLY ASP ILE PRO LYS THR ILE          
SEQRES  23 A  520  ILE TYR ASN THR PRO LEU ILE SER LEU GLU GLY ASN ILE          
SEQRES  24 A  520  SER SER MET CYS LEU ASN THR LYS ASP PRO TYR GLY ILE          
SEQRES  25 A  520  PRO GLY GLU ARG ASN LYS HIS ILE LEU THR THR HIS SER          
SEQRES  26 A  520  MET ALA MET ASN ASN VAL PRO SER MET PHE ALA VAL MET          
SEQRES  27 A  520  VAL SER GLN GLU THR PRO THR LYS LYS PHE ALA PRO ASP          
SEQRES  28 A  520  GLN LEU ALA GLY ILE ILE GLY LEU GLU ILE LYS VAL ASP          
SEQRES  29 A  520  SER ASP VAL GLY ILE PHE ARG GLU LEU GLU GLN GLN GLN          
SEQRES  30 A  520  LEU TYR GLU LEU SER SER SER ASN GLY TYR ASN LYS ARG          
SEQRES  31 A  520  PHE SER CYS PHE SER GLY ALA LEU ALA ASN GLY LEU THR          
SEQRES  32 A  520  VAL ALA ASP PRO ALA VAL ALA ALA GLY ASN LYS PHE LYS          
SEQRES  33 A  520  GLU ALA ILE PHE GLY ALA GLY SER VAL ILE PHE PHE ARG          
SEQRES  34 A  520  PRO SER ASP LEU GLY LEU LYS ASP TYR ASN VAL MET ALA          
SEQRES  35 A  520  ASN ALA ASN LYS SER ILE ASN MET GLN VAL GLN ALA THR          
SEQRES  36 A  520  PHE VAL THR PRO GLU ALA ALA GLY THR GLY ALA HIS TYR          
SEQRES  37 A  520  LYS LEU GLU VAL PHE SER ILE ARG ASP ASN LEU THR TYR          
SEQRES  38 A  520  SER PHE GLU ASP GLY THR PHE MET ASP ASP LEU THR LEU          
SEQRES  39 A  520  TYR THR PRO ASP GLN LEU LEU ARG SER PRO LEU LYS LEU          
SEQRES  40 A  520  THR ASP ASP ASN ASN LYS LEU MET ARG VAL MET GLY GLY          
SEQRES   1 B  520  GLY ALA MET GLY MET ASN THR PRO PRO GLU LEU ASP THR          
SEQRES   2 B  520  VAL LEU GLN ALA PRO TYR ALA TYR ASN TRP PRO THR SER          
SEQRES   3 B  520  LYS ASN VAL LYS ILE ALA SER ARG ILE GLY ILE PRO TYR          
SEQRES   4 B  520  SER THR PHE GLN THR ILE GLN PRO VAL SER ASP ALA PRO          
SEQRES   5 B  520  ASN ASN GLY ILE GLY GLN ILE THR PHE ASN GLN PRO LEU          
SEQRES   6 B  520  GLY ASN LEU THR GLY GLY ALA PRO ARG LEU ARG VAL SER          
SEQRES   7 B  520  PHE THR ALA GLU ILE LYS ASN ILE LEU ALA ASP SER SER          
SEQRES   8 B  520  LEU LYS ASP GLN ILE GLY LEU LYS SER PHE PRO VAL ASN          
SEQRES   9 B  520  ARG SER ILE PRO VAL ALA VAL ILE ASN MET ASN GLY LYS          
SEQRES  10 B  520  THR PHE THR SER TYR PRO ALA GLN LEU ILE LYS LEU HIS          
SEQRES  11 B  520  GLN TYR ASN ALA ASP PRO LEU GLU LEU ALA LEU LEU SER          
SEQRES  12 B  520  PRO CYS SER ASP VAL ASP GLU TYR ASN LYS ILE LYS ALA          
SEQRES  13 B  520  VAL SER MET ASN ASN PRO TYR ARG GLN GLY THR GLU SER          
SEQRES  14 B  520  THR ASP SER ARG MET SER ARG GLY LEU GLY CYS ASN TYR          
SEQRES  15 B  520  ALA TYR TYR ILE HIS PRO ARG ALA ALA GLY SER THR SER          
SEQRES  16 B  520  VAL LYS ILE ASP PHE VAL VAL ASP GLU ALA LEU VAL ALA          
SEQRES  17 B  520  ASN PRO THR GLN TYR LYS ASN ILE LYS ASP PRO VAL PRO          
SEQRES  18 B  520  PHE ARG ASN LEU ASN THR PHE LYS VAL ILE LEU ASP GLY          
SEQRES  19 B  520  GLN PHE LYS PRO GLU ASN MET ILE GLY ILE ALA ASP ASP          
SEQRES  20 B  520  VAL LYS LEU VAL ALA GLY LYS ALA ASP PHE GLU VAL ASP          
SEQRES  21 B  520  ILE THR GLY PHE LYS ILE ASN MET LEU VAL GLN ASN TRP          
SEQRES  22 B  520  VAL ALA PRO LEU GLU ILE GLY ASP ILE PRO LYS THR ILE          
SEQRES  23 B  520  ILE TYR ASN THR PRO LEU ILE SER LEU GLU GLY ASN ILE          
SEQRES  24 B  520  SER SER MET CYS LEU ASN THR LYS ASP PRO TYR GLY ILE          
SEQRES  25 B  520  PRO GLY GLU ARG ASN LYS HIS ILE LEU THR THR HIS SER          
SEQRES  26 B  520  MET ALA MET ASN ASN VAL PRO SER MET PHE ALA VAL MET          
SEQRES  27 B  520  VAL SER GLN GLU THR PRO THR LYS LYS PHE ALA PRO ASP          
SEQRES  28 B  520  GLN LEU ALA GLY ILE ILE GLY LEU GLU ILE LYS VAL ASP          
SEQRES  29 B  520  SER ASP VAL GLY ILE PHE ARG GLU LEU GLU GLN GLN GLN          
SEQRES  30 B  520  LEU TYR GLU LEU SER SER SER ASN GLY TYR ASN LYS ARG          
SEQRES  31 B  520  PHE SER CYS PHE SER GLY ALA LEU ALA ASN GLY LEU THR          
SEQRES  32 B  520  VAL ALA ASP PRO ALA VAL ALA ALA GLY ASN LYS PHE LYS          
SEQRES  33 B  520  GLU ALA ILE PHE GLY ALA GLY SER VAL ILE PHE PHE ARG          
SEQRES  34 B  520  PRO SER ASP LEU GLY LEU LYS ASP TYR ASN VAL MET ALA          
SEQRES  35 B  520  ASN ALA ASN LYS SER ILE ASN MET GLN VAL GLN ALA THR          
SEQRES  36 B  520  PHE VAL THR PRO GLU ALA ALA GLY THR GLY ALA HIS TYR          
SEQRES  37 B  520  LYS LEU GLU VAL PHE SER ILE ARG ASP ASN LEU THR TYR          
SEQRES  38 B  520  SER PHE GLU ASP GLY THR PHE MET ASP ASP LEU THR LEU          
SEQRES  39 B  520  TYR THR PRO ASP GLN LEU LEU ARG SER PRO LEU LYS LEU          
SEQRES  40 B  520  THR ASP ASP ASN ASN LYS LEU MET ARG VAL MET GLY GLY          
SEQRES   1 C  520  GLY ALA MET GLY MET ASN THR PRO PRO GLU LEU ASP THR          
SEQRES   2 C  520  VAL LEU GLN ALA PRO TYR ALA TYR ASN TRP PRO THR SER          
SEQRES   3 C  520  LYS ASN VAL LYS ILE ALA SER ARG ILE GLY ILE PRO TYR          
SEQRES   4 C  520  SER THR PHE GLN THR ILE GLN PRO VAL SER ASP ALA PRO          
SEQRES   5 C  520  ASN ASN GLY ILE GLY GLN ILE THR PHE ASN GLN PRO LEU          
SEQRES   6 C  520  GLY ASN LEU THR GLY GLY ALA PRO ARG LEU ARG VAL SER          
SEQRES   7 C  520  PHE THR ALA GLU ILE LYS ASN ILE LEU ALA ASP SER SER          
SEQRES   8 C  520  LEU LYS ASP GLN ILE GLY LEU LYS SER PHE PRO VAL ASN          
SEQRES   9 C  520  ARG SER ILE PRO VAL ALA VAL ILE ASN MET ASN GLY LYS          
SEQRES  10 C  520  THR PHE THR SER TYR PRO ALA GLN LEU ILE LYS LEU HIS          
SEQRES  11 C  520  GLN TYR ASN ALA ASP PRO LEU GLU LEU ALA LEU LEU SER          
SEQRES  12 C  520  PRO CYS SER ASP VAL ASP GLU TYR ASN LYS ILE LYS ALA          
SEQRES  13 C  520  VAL SER MET ASN ASN PRO TYR ARG GLN GLY THR GLU SER          
SEQRES  14 C  520  THR ASP SER ARG MET SER ARG GLY LEU GLY CYS ASN TYR          
SEQRES  15 C  520  ALA TYR TYR ILE HIS PRO ARG ALA ALA GLY SER THR SER          
SEQRES  16 C  520  VAL LYS ILE ASP PHE VAL VAL ASP GLU ALA LEU VAL ALA          
SEQRES  17 C  520  ASN PRO THR GLN TYR LYS ASN ILE LYS ASP PRO VAL PRO          
SEQRES  18 C  520  PHE ARG ASN LEU ASN THR PHE LYS VAL ILE LEU ASP GLY          
SEQRES  19 C  520  GLN PHE LYS PRO GLU ASN MET ILE GLY ILE ALA ASP ASP          
SEQRES  20 C  520  VAL LYS LEU VAL ALA GLY LYS ALA ASP PHE GLU VAL ASP          
SEQRES  21 C  520  ILE THR GLY PHE LYS ILE ASN MET LEU VAL GLN ASN TRP          
SEQRES  22 C  520  VAL ALA PRO LEU GLU ILE GLY ASP ILE PRO LYS THR ILE          
SEQRES  23 C  520  ILE TYR ASN THR PRO LEU ILE SER LEU GLU GLY ASN ILE          
SEQRES  24 C  520  SER SER MET CYS LEU ASN THR LYS ASP PRO TYR GLY ILE          
SEQRES  25 C  520  PRO GLY GLU ARG ASN LYS HIS ILE LEU THR THR HIS SER          
SEQRES  26 C  520  MET ALA MET ASN ASN VAL PRO SER MET PHE ALA VAL MET          
SEQRES  27 C  520  VAL SER GLN GLU THR PRO THR LYS LYS PHE ALA PRO ASP          
SEQRES  28 C  520  GLN LEU ALA GLY ILE ILE GLY LEU GLU ILE LYS VAL ASP          
SEQRES  29 C  520  SER ASP VAL GLY ILE PHE ARG GLU LEU GLU GLN GLN GLN          
SEQRES  30 C  520  LEU TYR GLU LEU SER SER SER ASN GLY TYR ASN LYS ARG          
SEQRES  31 C  520  PHE SER CYS PHE SER GLY ALA LEU ALA ASN GLY LEU THR          
SEQRES  32 C  520  VAL ALA ASP PRO ALA VAL ALA ALA GLY ASN LYS PHE LYS          
SEQRES  33 C  520  GLU ALA ILE PHE GLY ALA GLY SER VAL ILE PHE PHE ARG          
SEQRES  34 C  520  PRO SER ASP LEU GLY LEU LYS ASP TYR ASN VAL MET ALA          
SEQRES  35 C  520  ASN ALA ASN LYS SER ILE ASN MET GLN VAL GLN ALA THR          
SEQRES  36 C  520  PHE VAL THR PRO GLU ALA ALA GLY THR GLY ALA HIS TYR          
SEQRES  37 C  520  LYS LEU GLU VAL PHE SER ILE ARG ASP ASN LEU THR TYR          
SEQRES  38 C  520  SER PHE GLU ASP GLY THR PHE MET ASP ASP LEU THR LEU          
SEQRES  39 C  520  TYR THR PRO ASP GLN LEU LEU ARG SER PRO LEU LYS LEU          
SEQRES  40 C  520  THR ASP ASP ASN ASN LYS LEU MET ARG VAL MET GLY GLY          
LINKR            THR A 504                     LYS A 509                gap     
LINKR            THR B 504                     LYS B 509                gap     
LINKR            THR C 504                     LEU C 510                gap     
CISPEP   1 ASN A  205    PRO A  206                    0.00                     
CISPEP   2 ASN B  205    PRO B  206                    0.00                     
CISPEP   3 ASN C  205    PRO C  206                    0.00                     
CRYST1  131.190  132.580  135.220  90.00  90.00  90.00 P 21 21 21               
SCALE1      0.007623  0.000000  0.000000        0.00000                         
SCALE2     -0.000000  0.007543  0.000000        0.00000                         
SCALE3      0.000000 -0.000000  0.007395        0.00000                         
ATOM      1  N   ASN A   2      -6.812 -56.537  20.271  1.00 30.44           N  
ANISOU    1  N   ASN A   2     4309   2417   4838     -4   -927   -623       N  
ATOM      2  CA  ASN A   2      -7.365 -55.151  20.175  1.00 26.72           C  
ANISOU    2  CA  ASN A   2     3825   2325   4001   -167   -974   -168       C  
ATOM      3  CB  ASN A   2      -6.271 -54.084  20.228  1.00 23.94           C  
ANISOU    3  CB  ASN A   2     3951   1895   3248   -113   -954    361       C  
ATOM      4  CG  ASN A   2      -5.440 -54.145  21.501  1.00 23.82           C  
ANISOU    4  CG  ASN A   2     3893   1978   3176   -118   -900    365       C  
ATOM      5  OD1 ASN A   2      -5.927 -53.811  22.586  1.00 25.21           O  
ANISOU    5  OD1 ASN A   2     3853   2366   3356     11   -519    478       O  
ATOM      6  ND2 ASN A   2      -4.180 -54.551  21.388  1.00 23.52           N  
ANISOU    6  ND2 ASN A   2     3689   2140   3107   -675   -180    173       N  
ATOM      7  C   ASN A   2      -8.163 -54.999  18.879  1.00 25.65           C  
ANISOU    7  C   ASN A   2     3808   1933   4002    -40   -955   -100       C  
ATOM      8  O   ASN A   2      -7.717 -55.414  17.804  1.00 27.64           O  
ANISOU    8  O   ASN A   2     3633   2443   4425    134  -1035   -584       O  
ATOM      9  N   THR A   3      -9.341 -54.389  18.990  1.00 24.82           N  
ANISOU    9  N   THR A   3     3768   1721   3941   -197   -696    132       N  
ATOM     10  CA ATHR A   3     -10.177 -54.102  17.836  0.50 25.70           C  
ANISOU   10  CA ATHR A   3     3806   1823   4132    110   -754    163       C  
ATOM     11  CA BTHR A   3     -10.175 -54.100  17.838  0.50 26.24           C  
ANISOU   11  CA BTHR A   3     3914   1907   4149    109   -959      5       C  
ATOM     12  CB ATHR A   3     -11.235 -55.197  17.582  0.50 25.95           C  
ANISOU   12  CB ATHR A   3     3770   1570   4518    191   -639    348       C  
ATOM     13  CB BTHR A   3     -11.192 -55.236  17.623  0.50 28.22           C  
ANISOU   13  CB BTHR A   3     3897   2457   4367   -111  -1438    138       C  
ATOM     14  OG1ATHR A   3     -12.428 -54.919  18.318  0.50 28.18           O  
ANISOU   14  OG1ATHR A   3     4187   1749   4771    378    -93    838       O  
ATOM     15  OG1BTHR A   3     -12.124 -54.866  16.602  0.50 31.65           O  
ANISOU   15  OG1BTHR A   3     5134   2622   4267    198  -2026    -62       O  
ATOM     16  CG2ATHR A   3     -10.775 -56.600  17.894  0.50 25.32           C  
ANISOU   16  CG2ATHR A   3     3738   1444   4438     95   -828    241       C  
ATOM     17  CG2BTHR A   3     -11.912 -55.615  18.900  0.50 29.34           C  
ANISOU   17  CG2BTHR A   3     4076   2484   4587   -351  -1371    150       C  
ATOM     18  C   THR A   3     -10.787 -52.713  18.025  1.00 24.95           C  
ANISOU   18  C   THR A   3     3843   1845   3791    115   -704    166       C  
ATOM     19  O   THR A   3     -11.162 -52.332  19.138  1.00 24.76           O  
ANISOU   19  O   THR A   3     3242   2088   4077     56   -738    -13       O  
ATOM     20  N   PRO A   4     -10.888 -51.884  16.966  1.00 22.97           N  
ANISOU   20  N   PRO A   4     3004   2021   3701    171   -711    117       N  
ATOM     21  CA  PRO A   4     -11.486 -50.564  17.136  1.00 22.31           C  
ANISOU   21  CA  PRO A   4     3083   1893   3499     96   -500    301       C  
ATOM     22  CB  PRO A   4     -11.430 -49.952  15.732  1.00 24.64           C  
ANISOU   22  CB  PRO A   4     3644   2104   3611     20   -356    369       C  
ATOM     23  CG  PRO A   4     -10.278 -50.691  15.079  1.00 27.11           C  
ANISOU   23  CG  PRO A   4     3904   2733   3662    150   -286    142       C  
ATOM     24  CD  PRO A   4     -10.391 -52.105  15.604  1.00 25.53           C  
ANISOU   24  CD  PRO A   4     3235   2606   3858    271   -487     84       C  
ATOM     25  C   PRO A   4     -12.912 -50.687  17.657  1.00 21.29           C  
ANISOU   25  C   PRO A   4     3120   1821   3148     -9   -796    349       C  
ATOM     26  O   PRO A   4     -13.667 -51.559  17.235  1.00 22.17           O  
ANISOU   26  O   PRO A   4     2972   2063   3386   -115   -699    134       O  
ATOM     27  N   PRO A   5     -13.314 -49.814  18.600  1.00 20.64           N  
ANISOU   27  N   PRO A   5     2829   1771   3239    -55   -460    320       N  
ATOM     28  CA  PRO A   5     -14.663 -49.850  19.150  1.00 21.27           C  
ANISOU   28  CA  PRO A   5     2902   1888   3289   -204   -365    411       C  
ATOM     29  CB  PRO A   5     -14.601 -48.861  20.309  1.00 21.94           C  
ANISOU   29  CB  PRO A   5     3056   1727   3551   -216   -458    394       C  
ATOM     30  CG  PRO A   5     -13.538 -47.884  19.873  1.00 22.76           C  
ANISOU   30  CG  PRO A   5     3096   1910   3640   -293   -388    243       C  
ATOM     31  CD  PRO A   5     -12.495 -48.746  19.196  1.00 22.15           C  
ANISOU   31  CD  PRO A   5     3170   1883   3363   -324   -410    422       C  
ATOM     32  C   PRO A   5     -15.712 -49.397  18.132  1.00 20.79           C  
ANISOU   32  C   PRO A   5     2978   1639   3281   -122   -259    555       C  
ATOM     33  O   PRO A   5     -15.416 -48.572  17.263  1.00 22.45           O  
ANISOU   33  O   PRO A   5     3346   2115   3066   -156    -54    613       O  
ATOM     34  N   GLU A   6     -16.925 -49.940  18.265  1.00 22.44           N  
ANISOU   34  N   GLU A   6     3226   1907   3391   -438   -377    402       N  
ATOM     35  CA  GLU A   6     -18.077 -49.459  17.541  1.00 21.30           C  
ANISOU   35  CA  GLU A   6     3318   1709   3062   -416   -476    612       C  
ATOM     36  CB  GLU A   6     -19.317 -50.309  17.846  1.00 24.03           C  
ANISOU   36  CB  GLU A   6     3398   2042   3691   -371   -380    998       C  
ATOM     37  CG  GLU A   6     -20.591 -49.838  17.134  1.00 29.14           C  
ANISOU   37  CG  GLU A   6     3884   2871   4317   -224   -848    954       C  
ATOM     38  CD  GLU A   6     -21.381 -48.690  17.770  1.00 32.07           C  
ANISOU   38  CD  GLU A   6     4252   3267   4664    -12   -806   1130       C  
ATOM     39  OE1 GLU A   6     -21.187 -48.392  18.979  1.00 35.62           O  
ANISOU   39  OE1 GLU A   6     4494   4372   4666    -55  -1040   1204       O  
ATOM     40  OE2 GLU A   6     -22.203 -48.087  17.052  1.00 34.25           O  
ANISOU   40  OE2 GLU A   6     4279   4026   4709   -193  -1119   1343       O  
ATOM     41  C   GLU A   6     -18.343 -47.992  17.889  1.00 20.33           C  
ANISOU   41  C   GLU A   6     3122   1891   2710   -183     84    819       C  
ATOM     42  O   GLU A   6     -18.303 -47.610  19.060  1.00 22.72           O  
ANISOU   42  O   GLU A   6     3248   2429   2954   -207   -205    672       O  
ATOM     43  N   LEU A   7     -18.598 -47.187  16.848  1.00 17.43           N  
ANISOU   43  N   LEU A   7     2238   2123   2261     84   -130    521       N  
ATOM     44  CA  LEU A   7     -18.994 -45.798  16.977  1.00 17.47           C  
ANISOU   44  CA  LEU A   7     2302   2018   2316    -72     51    469       C  
ATOM     45  CB  LEU A   7     -17.927 -44.901  16.349  1.00 16.90           C  
ANISOU   45  CB  LEU A   7     2388   1856   2176    -76   -131    581       C  
ATOM     46  CG  LEU A   7     -16.533 -45.018  16.951  1.00 16.21           C  
ANISOU   46  CG  LEU A   7     2330   1489   2339    -38   -217    387       C  
ATOM     47  CD1 LEU A   7     -15.540 -44.191  16.146  1.00 17.85           C  
ANISOU   47  CD1 LEU A   7     2449   1822   2509   -189   -283    539       C  
ATOM     48  CD2 LEU A   7     -16.556 -44.610  18.425  1.00 18.94           C  
ANISOU   48  CD2 LEU A   7     2599   2087   2510   -109   -531    401       C  
ATOM     49  C   LEU A   7     -20.339 -45.581  16.272  1.00 17.96           C  
ANISOU   49  C   LEU A   7     2468   2124   2229   -181   -125    521       C  
ATOM     50  O   LEU A   7     -20.557 -46.045  15.149  1.00 20.20           O  
ANISOU   50  O   LEU A   7     2796   2428   2450   -180   -185    431       O  
ATOM     51  N   ASP A   8     -21.227 -44.839  16.939  1.00 19.39           N  
ANISOU   51  N   ASP A   8     2789   2156   2420   -182     64    538       N  
ATOM     52  CA  ASP A   8     -22.515 -44.484  16.390  1.00 19.20           C  
ANISOU   52  CA  ASP A   8     2689   2120   2484   -206     75    403       C  
ATOM     53  CB  ASP A   8     -23.458 -43.960  17.460  1.00 22.11           C  
ANISOU   53  CB  ASP A   8     2744   2861   2793    -45    365    660       C  
ATOM     54  CG  ASP A   8     -23.906 -45.000  18.468  1.00 25.90           C  
ANISOU   54  CG  ASP A   8     3510   3028   3301   -129    706    908       C  
ATOM     55  OD1 ASP A   8     -23.728 -46.209  18.227  1.00 29.26           O  
ANISOU   55  OD1 ASP A   8     3817   3084   4214   -228    841   1299       O  
ATOM     56  OD2 ASP A   8     -24.461 -44.592  19.474  1.00 33.58           O  
ANISOU   56  OD2 ASP A   8     5192   4776   2791   -207    811    976       O  
ATOM     57  C   ASP A   8     -22.340 -43.427  15.303  1.00 18.11           C  
ANISOU   57  C   ASP A   8     2511   2084   2284   -122    148    239       C  
ATOM     58  O   ASP A   8     -21.382 -42.661  15.325  1.00 18.83           O  
ANISOU   58  O   ASP A   8     2877   1968   2310   -329   -198    520       O  
ATOM     59  N   THR A   9     -23.337 -43.347  14.410  1.00 17.89           N  
ANISOU   59  N   THR A   9     2355   2060   2381   -252     89    373       N  
ATOM     60  CA  THR A   9     -23.296 -42.438  13.266  1.00 17.30           C  
ANISOU   60  CA  THR A   9     2426   1800   2347    -89    110    278       C  
ATOM     61  CB  THR A   9     -23.311 -43.208  11.945  1.00 17.94           C  
ANISOU   61  CB  THR A   9     2345   2034   2437      7     49    120       C  
ATOM     62  OG1 THR A   9     -24.408 -44.128  11.933  1.00 18.75           O  
ANISOU   62  OG1 THR A   9     2465   1903   2753    -57   -118     56       O  
ATOM     63  CG2 THR A   9     -22.004 -43.938  11.731  1.00 17.75           C  
ANISOU   63  CG2 THR A   9     2231   2306   2207    -67    352   -134       C  
ATOM     64  C   THR A   9     -24.421 -41.411  13.313  1.00 16.86           C  
ANISOU   64  C   THR A   9     2376   1792   2238    -59    234    200       C  
ATOM     65  O   THR A   9     -25.510 -41.680  13.849  1.00 18.99           O  
ANISOU   65  O   THR A   9     2354   2086   2773     68    175    388       O  
ATOM     66  N   VAL A  10     -24.125 -40.238  12.734  1.00 15.47           N  
ANISOU   66  N   VAL A  10     2065   1827   1983     83     83    219       N  
ATOM     67  CA  VAL A  10     -25.097 -39.157  12.526  1.00 15.83           C  
ANISOU   67  CA  VAL A  10     2247   1719   2049     60   -115    169       C  
ATOM     68  CB  VAL A  10     -24.887 -37.996  13.520  1.00 16.34           C  
ANISOU   68  CB  VAL A  10     2254   1671   2280    132    121     88       C  
ATOM     69  CG1 VAL A  10     -24.990 -38.477  14.957  1.00 17.51           C  
ANISOU   69  CG1 VAL A  10     2384   2041   2228     67    216   -101       C  
ATOM     70  CG2 VAL A  10     -23.563 -37.289  13.280  1.00 16.66           C  
ANISOU   70  CG2 VAL A  10     2248   1704   2376    152    -46      3       C  
ATOM     71  C   VAL A  10     -24.957 -38.667  11.079  1.00 16.74           C  
ANISOU   71  C   VAL A  10     2539   1782   2038    178    -12    172       C  
ATOM     72  O   VAL A  10     -23.959 -38.943  10.424  1.00 17.21           O  
ANISOU   72  O   VAL A  10     2373   2243   1923    410   -410    220       O  
ATOM     73  N   LEU A  11     -25.953 -37.909  10.610  1.00 17.79           N  
ANISOU   73  N   LEU A  11     2353   2210   2194    366     66    -21       N  
ATOM     74  CA  LEU A  11     -25.852 -37.241   9.300  1.00 20.14           C  
ANISOU   74  CA  LEU A  11     2976   2496   2180    668    -94     89       C  
ATOM     75  CB  LEU A  11     -27.089 -37.513   8.449  1.00 23.05           C  
ANISOU   75  CB  LEU A  11     2666   3032   3057    319     80    -48       C  
ATOM     76  CG  LEU A  11     -27.371 -38.945   8.069  1.00 23.58           C  
ANISOU   76  CG  LEU A  11     2844   2924   3190     19   -143    164       C  
ATOM     77  CD1 LEU A  11     -28.495 -38.947   7.029  1.00 23.85           C  
ANISOU   77  CD1 LEU A  11     3399   3207   2455     97   -150   -337       C  
ATOM     78  CD2 LEU A  11     -26.113 -39.604   7.526  1.00 23.70           C  
ANISOU   78  CD2 LEU A  11     2916   2617   3472   -276    109    295       C  
ATOM     79  C   LEU A  11     -25.733 -35.738   9.498  1.00 19.62           C  
ANISOU   79  C   LEU A  11     3074   2456   1923    860   -191    216       C  
ATOM     80  O   LEU A  11     -26.703 -35.103   9.875  1.00 21.78           O  
ANISOU   80  O   LEU A  11     3189   2864   2222   1128   -146     88       O  
ATOM     81  N   GLN A  12     -24.543 -35.195   9.263  1.00 17.79           N  
ANISOU   81  N   GLN A  12     2939   1962   1858    990   -365     50       N  
ATOM     82  CA  GLN A  12     -24.353 -33.752   9.299  1.00 18.16           C  
ANISOU   82  CA  GLN A  12     3301   1861   1737   1048   -334    193       C  
ATOM     83  CB  GLN A  12     -22.869 -33.418   9.150  1.00 20.95           C  
ANISOU   83  CB  GLN A  12     3346   2097   2514    776   -660     15       C  
ATOM     84  CG  GLN A  12     -22.553 -31.925   9.195  1.00 24.96           C  
ANISOU   84  CG  GLN A  12     4083   2083   3315   1065   -679    -28       C  
ATOM     85  CD  GLN A  12     -22.783 -31.357  10.571  1.00 28.26           C  
ANISOU   85  CD  GLN A  12     4458   2686   3593    631   -565   -476       C  
ATOM     86  OE1 GLN A  12     -22.287 -31.882  11.555  1.00 33.27           O  
ANISOU   86  OE1 GLN A  12     4075   4451   4114   -128  -1448   -170       O  
ATOM     87  NE2 GLN A  12     -23.554 -30.276  10.644  1.00 34.41           N  
ANISOU   87  NE2 GLN A  12     5249   2805   5020    867     19   -857       N  
ATOM     88  C   GLN A  12     -25.171 -33.140   8.159  1.00 18.35           C  
ANISOU   88  C   GLN A  12     3212   2159   1600   1028   -239    178       C  
ATOM     89  O   GLN A  12     -25.109 -33.604   7.035  1.00 19.45           O  
ANISOU   89  O   GLN A  12     3421   2337   1630   1056   -205     -3       O  
ATOM     90  N   ALA A  13     -25.972 -32.126   8.491  1.00 17.84           N  
ANISOU   90  N   ALA A  13     3099   1861   1816    889    -22    453       N  
ATOM     91  CA  ALA A  13     -26.870 -31.488   7.555  1.00 17.74           C  
ANISOU   91  CA  ALA A  13     2674   2107   1959    564     50    663       C  
ATOM     92  CB  ALA A  13     -28.270 -32.020   7.742  1.00 21.18           C  
ANISOU   92  CB  ALA A  13     2985   2328   2733    230    247    690       C  
ATOM     93  C   ALA A  13     -26.820 -29.986   7.785  1.00 17.13           C  
ANISOU   93  C   ALA A  13     2366   2130   2013    500    100    515       C  
ATOM     94  O   ALA A  13     -26.586 -29.529   8.890  1.00 18.59           O  
ANISOU   94  O   ALA A  13     2947   1926   2189    363   -216    341       O  
ATOM     95  N   PRO A  14     -27.045 -29.175   6.740  1.00 16.50           N  
ANISOU   95  N   PRO A  14     2554   1736   1978    490    -92    359       N  
ATOM     96  CA  PRO A  14     -26.991 -27.724   6.907  1.00 17.13           C  
ANISOU   96  CA  PRO A  14     2616   1732   2159    182   -130    437       C  
ATOM     97  CB  PRO A  14     -27.174 -27.169   5.493  1.00 20.68           C  
ANISOU   97  CB  PRO A  14     3355   2184   2318    169   -174    645       C  
ATOM     98  CG  PRO A  14     -27.730 -28.295   4.676  1.00 21.20           C  
ANISOU   98  CG  PRO A  14     3297   2313   2442   -133   -486    784       C  
ATOM     99  CD  PRO A  14     -27.394 -29.594   5.372  1.00 18.05           C  
ANISOU   99  CD  PRO A  14     2738   2071   2047    266   -139    323       C  
ATOM    100  C   PRO A  14     -28.122 -27.239   7.820  1.00 16.68           C  
ANISOU  100  C   PRO A  14     2712   1516   2109    296   -305    215       C  
ATOM    101  O   PRO A  14     -29.208 -27.814   7.835  1.00 15.78           O  
ANISOU  101  O   PRO A  14     2349   1689   1955    409    -63    -63       O  
ATOM    102  N   TYR A  15     -27.838 -26.176   8.568  1.00 15.75           N  
ANISOU  102  N   TYR A  15     2381   1761   1841    245   -293    108       N  
ATOM    103  CA  TYR A  15     -28.810 -25.591   9.487  1.00 17.31           C  
ANISOU  103  CA  TYR A  15     2335   1968   2274    308   -247   -120       C  
ATOM    104  CB  TYR A  15     -28.129 -24.500  10.308  1.00 17.44           C  
ANISOU  104  CB  TYR A  15     1851   2396   2380    102   -371    -70       C  
ATOM    105  CG  TYR A  15     -28.898 -23.984  11.491  1.00 18.19           C  
ANISOU  105  CG  TYR A  15     2052   2499   2359    324   -422   -192       C  
ATOM    106  CD1 TYR A  15     -29.079 -24.764  12.624  1.00 19.65           C  
ANISOU  106  CD1 TYR A  15     2289   2953   2223    408   -229    -89       C  
ATOM    107  CE1 TYR A  15     -29.752 -24.280  13.739  1.00 21.35           C  
ANISOU  107  CE1 TYR A  15     2498   3173   2441    442   -188   -310       C  
ATOM    108  CZ  TYR A  15     -30.239 -22.990  13.738  1.00 22.25           C  
ANISOU  108  CZ  TYR A  15     2658   3368   2425    676   -116   -539       C  
ATOM    109  OH  TYR A  15     -30.906 -22.491  14.828  1.00 25.35           O  
ANISOU  109  OH  TYR A  15     2855   3898   2876   1151   -176  -1129       O  
ATOM    110  CE2 TYR A  15     -30.062 -22.199  12.616  1.00 20.82           C  
ANISOU  110  CE2 TYR A  15     2690   2627   2594    675   -488   -407       C  
ATOM    111  CD2 TYR A  15     -29.386 -22.691  11.514  1.00 20.33           C  
ANISOU  111  CD2 TYR A  15     2596   2599   2529    492   -443   -157       C  
ATOM    112  C   TYR A  15     -30.022 -25.058   8.718  1.00 16.89           C  
ANISOU  112  C   TYR A  15     2145   1748   2522    144   -358   -300       C  
ATOM    113  O   TYR A  15     -31.096 -24.908   9.299  1.00 19.09           O  
ANISOU  113  O   TYR A  15     2048   2306   2900    267   -508   -503       O  
ATOM    114  N   ALA A  16     -29.860 -24.803   7.411  1.00 17.04           N  
ANISOU  114  N   ALA A  16     2385   1480   2608    286   -561    -76       N  
ATOM    115  CA  ALA A  16     -30.981 -24.441   6.525  1.00 19.79           C  
ANISOU  115  CA  ALA A  16     2771   1724   3025    315   -758   -108       C  
ATOM    116  CB  ALA A  16     -30.472 -24.311   5.109  1.00 22.21           C  
ANISOU  116  CB  ALA A  16     3405   1834   3200    169   -789    607       C  
ATOM    117  C   ALA A  16     -32.119 -25.468   6.616  1.00 20.01           C  
ANISOU  117  C   ALA A  16     2563   1922   3117    401   -823    -56       C  
ATOM    118  O   ALA A  16     -33.257 -25.112   6.408  1.00 22.38           O  
ANISOU  118  O   ALA A  16     2438   2033   4029    225   -889   -364       O  
ATOM    119  N   TYR A  17     -31.791 -26.740   6.891  1.00 16.21           N  
ANISOU  119  N   TYR A  17     2256   1660   2241    107   -656    -90       N  
ATOM    120  CA  TYR A  17     -32.795 -27.781   6.973  1.00 16.47           C  
ANISOU  120  CA  TYR A  17     2270   1777   2211      3   -487   -320       C  
ATOM    121  CB  TYR A  17     -32.233 -29.145   6.562  1.00 16.59           C  
ANISOU  121  CB  TYR A  17     2746   1460   2095    -39   -463     56       C  
ATOM    122  CG  TYR A  17     -31.968 -29.341   5.086  1.00 16.64           C  
ANISOU  122  CG  TYR A  17     2599   1783   1939    -24   -587    245       C  
ATOM    123  CD1 TYR A  17     -32.712 -28.718   4.100  1.00 16.68           C  
ANISOU  123  CD1 TYR A  17     2439   1807   2091     83   -579    279       C  
ATOM    124  CE1 TYR A  17     -32.498 -28.971   2.751  1.00 17.22           C  
ANISOU  124  CE1 TYR A  17     2642   1760   2139    127   -519    256       C  
ATOM    125  CZ  TYR A  17     -31.482 -29.815   2.356  1.00 16.42           C  
ANISOU  125  CZ  TYR A  17     2711   1863   1664    132   -423    217       C  
ATOM    126  OH  TYR A  17     -31.221 -30.085   1.033  1.00 19.14           O  
ANISOU  126  OH  TYR A  17     3441   2119   1710    -14   -592    135       O  
ATOM    127  CE2 TYR A  17     -30.734 -30.450   3.326  1.00 17.52           C  
ANISOU  127  CE2 TYR A  17     2745   2107   1802    412   -471    181       C  
ATOM    128  CD2 TYR A  17     -30.983 -30.199   4.668  1.00 17.65           C  
ANISOU  128  CD2 TYR A  17     2842   2157   1706    394   -760    285       C  
ATOM    129  C   TYR A  17     -33.414 -27.867   8.370  1.00 18.11           C  
ANISOU  129  C   TYR A  17     2474   2114   2290    -28   -459   -158       C  
ATOM    130  O   TYR A  17     -34.350 -28.668   8.569  1.00 19.67           O  
ANISOU  130  O   TYR A  17     2504   2323   2646   -101    -41   -271       O  
ATOM    131  N   ASN A  18     -32.935 -27.052   9.320  1.00 17.33           N  
ANISOU  131  N   ASN A  18     2033   2293   2255    214   -326   -381       N  
ATOM    132  CA  ASN A  18     -33.676 -26.804  10.568  1.00 17.80           C  
ANISOU  132  CA  ASN A  18     2265   2180   2316    121   -146   -159       C  
ATOM    133  CB  ASN A  18     -32.764 -26.346  11.714  1.00 17.79           C  
ANISOU  133  CB  ASN A  18     2511   1949   2298    277   -316    -42       C  
ATOM    134  CG  ASN A  18     -33.517 -26.029  12.983  1.00 18.39           C  
ANISOU  134  CG  ASN A  18     2873   1870   2242    257   -311   -128       C  
ATOM    135  OD1 ASN A  18     -34.497 -26.702  13.322  1.00 21.41           O  
ANISOU  135  OD1 ASN A  18     3204   2711   2218     50    -74    -81       O  
ATOM    136  ND2 ASN A  18     -33.090 -24.979  13.677  1.00 18.53           N  
ANISOU  136  ND2 ASN A  18     2964   1881   2195    345    -49   -369       N  
ATOM    137  C   ASN A  18     -34.762 -25.774  10.256  1.00 17.50           C  
ANISOU  137  C   ASN A  18     2385   2077   2187     83   -151    -89       C  
ATOM    138  O   ASN A  18     -34.646 -24.609  10.596  1.00 17.86           O  
ANISOU  138  O   ASN A  18     2291   2079   2415      4   -208   -179       O  
ATOM    139  N   TRP A  19     -35.791 -26.214   9.537  1.00 16.49           N  
ANISOU  139  N   TRP A  19     2298   1949   2018    -17     55   -191       N  
ATOM    140  CA  TRP A  19     -36.765 -25.308   8.971  1.00 15.39           C  
ANISOU  140  CA  TRP A  19     2114   1790   1942   -152     69   -143       C  
ATOM    141  CB  TRP A  19     -37.921 -26.060   8.312  1.00 15.75           C  
ANISOU  141  CB  TRP A  19     2148   1911   1926   -236    115    -52       C  
ATOM    142  CG  TRP A  19     -37.505 -27.019   7.256  1.00 15.58           C  
ANISOU  142  CG  TRP A  19     2365   1595   1958   -264     66    -44       C  
ATOM    143  CD1 TRP A  19     -37.376 -28.369   7.385  1.00 15.76           C  
ANISOU  143  CD1 TRP A  19     2482   1554   1952   -181    -10   -121       C  
ATOM    144  NE1 TRP A  19     -37.023 -28.912   6.188  1.00 16.09           N  
ANISOU  144  NE1 TRP A  19     2635   1474   2003    -73    -34   -143       N  
ATOM    145  CE2 TRP A  19     -36.902 -27.923   5.252  1.00 15.34           C  
ANISOU  145  CE2 TRP A  19     2178   1795   1852   -135   -191    -86       C  
ATOM    146  CD2 TRP A  19     -37.195 -26.701   5.888  1.00 15.40           C  
ANISOU  146  CD2 TRP A  19     2201   1711   1939   -193     58    -67       C  
ATOM    147  CE3 TRP A  19     -37.165 -25.521   5.144  1.00 14.76           C  
ANISOU  147  CE3 TRP A  19     1998   1705   1906   -200    -94   -185       C  
ATOM    148  CZ3 TRP A  19     -36.829 -25.586   3.815  1.00 15.50           C  
ANISOU  148  CZ3 TRP A  19     2005   1853   2031   -278    103    -91       C  
ATOM    149  CH2 TRP A  19     -36.499 -26.801   3.216  1.00 15.68           C  
ANISOU  149  CH2 TRP A  19     2125   1812   2021   -212     31   -145       C  
ATOM    150  CZ2 TRP A  19     -36.531 -27.989   3.915  1.00 15.60           C  
ANISOU  150  CZ2 TRP A  19     2052   1846   2029   -327     59   -193       C  
ATOM    151  C   TRP A  19     -37.341 -24.437  10.068  1.00 15.24           C  
ANISOU  151  C   TRP A  19     2168   1889   1732   -241     58   -116       C  
ATOM    152  O   TRP A  19     -37.785 -24.965  11.092  1.00 15.38           O  
ANISOU  152  O   TRP A  19     2187   1803   1853   -198     48    114       O  
ATOM    153  N   PRO A  20     -37.407 -23.103   9.894  1.00 13.55           N  
ANISOU  153  N   PRO A  20     1956   1761   1430   -226     50    227       N  
ATOM    154  CA  PRO A  20     -38.077 -22.275  10.890  1.00 13.78           C  
ANISOU  154  CA  PRO A  20     2060   1752   1423   -199     -1    139       C  
ATOM    155  CB  PRO A  20     -37.662 -20.836  10.539  1.00 14.14           C  
ANISOU  155  CB  PRO A  20     2058   1803   1511   -328    -52     39       C  
ATOM    156  CG  PRO A  20     -36.486 -20.998   9.637  1.00 15.49           C  
ANISOU  156  CG  PRO A  20     2226   2000   1658   -167     59     73       C  
ATOM    157  CD  PRO A  20     -36.774 -22.275   8.861  1.00 13.98           C  
ANISOU  157  CD  PRO A  20     1770   2132   1407   -409     89     76       C  
ATOM    158  C   PRO A  20     -39.592 -22.472  10.806  1.00 13.94           C  
ANISOU  158  C   PRO A  20     2067   1631   1595    -72    -30     17       C  
ATOM    159  O   PRO A  20     -40.158 -22.319   9.725  1.00 14.52           O  
ANISOU  159  O   PRO A  20     1862   1861   1793   -252   -177    122       O  
ATOM    160  N   THR A  21     -40.197 -22.825  11.940  1.00 14.90           N  
ANISOU  160  N   THR A  21     2118   1851   1691   -207     79    -21       N  
ATOM    161  CA  THR A  21     -41.625 -23.069  12.058  1.00 16.58           C  
ANISOU  161  CA  THR A  21     2249   2001   2047   -373    233     40       C  
ATOM    162  CB  THR A  21     -41.955 -24.566  12.046  1.00 18.64           C  
ANISOU  162  CB  THR A  21     2635   2055   2392   -517     95    -68       C  
ATOM    163  OG1 THR A  21     -41.570 -25.160  13.300  1.00 20.93           O  
ANISOU  163  OG1 THR A  21     2935   2489   2526   -447    125    275       O  
ATOM    164  CG2 THR A  21     -41.300 -25.295  10.897  1.00 20.33           C  
ANISOU  164  CG2 THR A  21     3153   2145   2425   -592     58   -118       C  
ATOM    165  C   THR A  21     -42.136 -22.513  13.388  1.00 15.49           C  
ANISOU  165  C   THR A  21     2115   1790   1979   -177    215    211       C  
ATOM    166  O   THR A  21     -41.364 -22.051  14.221  1.00 16.68           O  
ANISOU  166  O   THR A  21     2220   2064   2051   -437    300     71       O  
ATOM    167  N   SER A  22     -43.441 -22.624  13.606  1.00 17.02           N  
ANISOU  167  N   SER A  22     2227   2136   2103   -445    461    139       N  
ATOM    168  CA  SER A  22     -44.006 -22.164  14.853  1.00 19.05           C  
ANISOU  168  CA  SER A  22     2162   2773   2302   -185    532     -2       C  
ATOM    169  CB  SER A  22     -45.511 -22.158  14.808  1.00 21.74           C  
ANISOU  169  CB  SER A  22     2189   3360   2711   -374    550     29       C  
ATOM    170  OG  SER A  22     -45.999 -23.474  14.679  1.00 26.19           O  
ANISOU  170  OG  SER A  22     2884   3443   3624   -620    708   -302       O  
ATOM    171  C   SER A  22     -43.502 -22.992  16.043  1.00 20.11           C  
ANISOU  171  C   SER A  22     2507   2942   2190    -97    738     81       C  
ATOM    172  O   SER A  22     -43.703 -22.579  17.172  1.00 24.47           O  
ANISOU  172  O   SER A  22     3545   3510   2241     15    526   -157       O  
ATOM    173  N   LYS A  23     -42.899 -24.167  15.785  1.00 19.78           N  
ANISOU  173  N   LYS A  23     2795   2686   2031   -180    396    229       N  
ATOM    174  CA  LYS A  23     -42.425 -25.036  16.847  1.00 21.61           C  
ANISOU  174  CA  LYS A  23     3027   3299   1882   -133    212    193       C  
ATOM    175  CB  LYS A  23     -42.391 -26.491  16.388  1.00 24.42           C  
ANISOU  175  CB  LYS A  23     3662   3314   2301   -302   -233    106       C  
ATOM    176  CG  LYS A  23     -43.765 -27.102  16.165  1.00 30.91           C  
ANISOU  176  CG  LYS A  23     4033   4031   3679   -611   -264     76       C  
ATOM    177  CD  LYS A  23     -43.695 -28.562  15.796  1.00 38.33           C  
ANISOU  177  CD  LYS A  23     5391   4059   5113   -702   -383     11       C  
ATOM    178  CE  LYS A  23     -45.060 -29.175  15.601  1.00 45.35           C  
ANISOU  178  CE  LYS A  23     5855   5058   6318  -1145   -819   -384       C  
ATOM    179  NZ  LYS A  23     -44.981 -30.654  15.575  1.00 52.45           N  
ANISOU  179  NZ  LYS A  23     6942   5303   7681   -765   -959   -587       N  
ATOM    180  C   LYS A  23     -41.045 -24.607  17.355  1.00 20.18           C  
ANISOU  180  C   LYS A  23     2946   3120   1600   -407    341    222       C  
ATOM    181  O   LYS A  23     -40.671 -24.979  18.470  1.00 25.19           O  
ANISOU  181  O   LYS A  23     3558   3902   2110   -527    -64    572       O  
ATOM    182  N   ASN A  24     -40.265 -23.903  16.522  1.00 17.32           N  
ANISOU  182  N   ASN A  24     2564   2227   1789   -121    202     58       N  
ATOM    183  CA  ASN A  24     -38.879 -23.588  16.886  1.00 16.13           C  
ANISOU  183  CA  ASN A  24     2587   2157   1385    -69     90    268       C  
ATOM    184  CB  ASN A  24     -37.896 -24.494  16.149  1.00 16.83           C  
ANISOU  184  CB  ASN A  24     2854   1987   1553   -101    248    233       C  
ATOM    185  CG  ASN A  24     -37.844 -24.232  14.659  1.00 16.90           C  
ANISOU  185  CG  ASN A  24     2845   2137   1439    192    327    -37       C  
ATOM    186  OD1 ASN A  24     -38.553 -23.384  14.159  1.00 19.55           O  
ANISOU  186  OD1 ASN A  24     3052   2511   1864    278     75    211       O  
ATOM    187  ND2 ASN A  24     -37.004 -24.945  13.939  1.00 19.79           N  
ANISOU  187  ND2 ASN A  24     3123   2692   1703    630    458      4       N  
ATOM    188  C   ASN A  24     -38.518 -22.113  16.683  1.00 17.84           C  
ANISOU  188  C   ASN A  24     2509   2138   2130   -117     78    -47       C  
ATOM    189  O   ASN A  24     -37.349 -21.797  16.758  1.00 23.20           O  
ANISOU  189  O   ASN A  24     2584   2239   3989    -95   -176    341       O  
ATOM    190  N   VAL A  25     -39.496 -21.235  16.440  1.00 16.47           N  
ANISOU  190  N   VAL A  25     2440   1914   1904   -144    117   -228       N  
ATOM    191  CA  VAL A  25     -39.251 -19.809  16.304  1.00 16.63           C  
ANISOU  191  CA  VAL A  25     2471   1960   1886   -171     12   -355       C  
ATOM    192  CB  VAL A  25     -39.759 -19.280  14.953  1.00 15.47           C  
ANISOU  192  CB  VAL A  25     2112   1873   1893    -85    197   -287       C  
ATOM    193  CG1 VAL A  25     -39.765 -17.758  14.924  1.00 16.57           C  
ANISOU  193  CG1 VAL A  25     2288   1962   2044    -44     49     -1       C  
ATOM    194  CG2 VAL A  25     -38.931 -19.866  13.820  1.00 15.81           C  
ANISOU  194  CG2 VAL A  25     2317   1869   1819    -43    140   -390       C  
ATOM    195  C   VAL A  25     -39.957 -19.080  17.442  1.00 17.84           C  
ANISOU  195  C   VAL A  25     2688   1806   2282     18     93   -420       C  
ATOM    196  O   VAL A  25     -41.151 -19.308  17.695  1.00 20.68           O  
ANISOU  196  O   VAL A  25     2983   2341   2533   -370    362   -435       O  
ATOM    197  N   LYS A  26     -39.215 -18.165  18.066  1.00 18.42           N  
ANISOU  197  N   LYS A  26     2690   2202   2104    124   -232   -522       N  
ATOM    198  CA  LYS A  26     -39.800 -17.131  18.921  1.00 18.19           C  
ANISOU  198  CA  LYS A  26     2950   1910   2051    -59    184   -259       C  
ATOM    199  CB  LYS A  26     -39.368 -17.306  20.375  1.00 21.14           C  
ANISOU  199  CB  LYS A  26     3550   2367   2112     72    -36   -336       C  
ATOM    200  CG  LYS A  26     -39.859 -18.599  21.028  1.00 23.55           C  
ANISOU  200  CG  LYS A  26     3945   2538   2465     93    -68     79       C  
ATOM    201  CD  LYS A  26     -39.278 -18.817  22.399  1.00 26.52           C  
ANISOU  201  CD  LYS A  26     4443   3136   2497   -200    -73    332       C  
ATOM    202  CE  LYS A  26     -39.331 -20.267  22.809  1.00 31.07           C  
ANISOU  202  CE  LYS A  26     5205   3161   3439     -6   -147    563       C  
ATOM    203  NZ  LYS A  26     -40.567 -20.523  23.571  1.00 39.43           N  
ANISOU  203  NZ  LYS A  26     5507   4601   4870    311    439    391       N  
ATOM    204  C   LYS A  26     -39.401 -15.761  18.371  1.00 16.66           C  
ANISOU  204  C   LYS A  26     2563   1987   1778      8   -135   -202       C  
ATOM    205  O   LYS A  26     -38.369 -15.618  17.696  1.00 18.30           O  
ANISOU  205  O   LYS A  26     2787   2257   1907    -88    140   -455       O  
ATOM    206  N   ILE A  27     -40.234 -14.764  18.658  1.00 15.71           N  
ANISOU  206  N   ILE A  27     2232   2030   1705    -78     50   -264       N  
ATOM    207  CA  ILE A  27     -39.994 -13.411  18.191  1.00 15.50           C  
ANISOU  207  CA  ILE A  27     2170   1958   1759    -99    -81   -246       C  
ATOM    208  CB  ILE A  27     -41.234 -12.832  17.503  1.00 15.95           C  
ANISOU  208  CB  ILE A  27     2127   1823   2110   -145    -60   -144       C  
ATOM    209  CG1 ILE A  27     -41.659 -13.710  16.326  1.00 16.83           C  
ANISOU  209  CG1 ILE A  27     2163   2199   2032    -26   -177   -223       C  
ATOM    210  CG2 ILE A  27     -40.976 -11.387  17.083  1.00 17.52           C  
ANISOU  210  CG2 ILE A  27     2502   1876   2279   -157     23    -25       C  
ATOM    211  CD1 ILE A  27     -40.573 -13.987  15.327  1.00 17.92           C  
ANISOU  211  CD1 ILE A  27     2345   2223   2238   -169    -89   -207       C  
ATOM    212  C   ILE A  27     -39.560 -12.552  19.373  1.00 14.96           C  
ANISOU  212  C   ILE A  27     2219   1535   1930   -107    -35   -261       C  
ATOM    213  O   ILE A  27     -40.214 -12.545  20.439  1.00 17.35           O  
ANISOU  213  O   ILE A  27     2512   2241   1838   -247     63   -667       O  
ATOM    214  N   ALA A  28     -38.460 -11.823  19.176  1.00 15.58           N  
ANISOU  214  N   ALA A  28     2347   1776   1793   -241    -31   -273       N  
ATOM    215  CA  ALA A  28     -37.929 -10.983  20.219  1.00 15.59           C  
ANISOU  215  CA  ALA A  28     2504   1536   1882   -154   -293   -178       C  
ATOM    216  CB  ALA A  28     -36.411 -11.031  20.190  1.00 16.78           C  
ANISOU  216  CB  ALA A  28     2458   1751   2165   -208   -430   -203       C  
ATOM    217  C   ALA A  28     -38.419  -9.543  20.065  1.00 17.16           C  
ANISOU  217  C   ALA A  28     2738   1751   2030    135   -173   -129       C  
ATOM    218  O   ALA A  28     -38.428  -8.973  18.964  1.00 17.94           O  
ANISOU  218  O   ALA A  28     2799   1861   2153   -338   -489     53       O  
ATOM    219  N   SER A  29     -38.762  -8.948  21.210  1.00 17.45           N  
ANISOU  219  N   SER A  29     2831   1691   2106    -61    -20   -168       N  
ATOM    220  CA  SER A  29     -38.649  -7.507  21.376  1.00 16.27           C  
ANISOU  220  CA  SER A  29     2295   1629   2256   -141   -224   -208       C  
ATOM    221  CB  SER A  29     -39.843  -6.915  22.128  1.00 17.28           C  
ANISOU  221  CB  SER A  29     2284   1783   2496   -374    -27   -185       C  
ATOM    222  OG  SER A  29     -39.745  -5.504  22.247  1.00 16.04           O  
ANISOU  222  OG  SER A  29     2205   1739   2150   -243    212   -265       O  
ATOM    223  C   SER A  29     -37.299  -7.284  22.062  1.00 18.46           C  
ANISOU  223  C   SER A  29     2359   2006   2647   -270   -190      2       C  
ATOM    224  O   SER A  29     -36.433  -8.137  21.989  1.00 20.49           O  
ANISOU  224  O   SER A  29     2487   1972   3325   -211   -344    -49       O  
ATOM    225  N   ARG A  30     -37.100  -6.159  22.723  1.00 17.74           N  
ANISOU  225  N   ARG A  30     2325   1893   2520   -132   -189    -84       N  
ATOM    226  CA  ARG A  30     -35.744  -5.841  23.176  1.00 17.21           C  
ANISOU  226  CA  ARG A  30     2355   1820   2363   -204    -65   -220       C  
ATOM    227  CB  ARG A  30     -34.913  -5.262  22.024  1.00 19.47           C  
ANISOU  227  CB  ARG A  30     2688   2381   2328    -26    232   -167       C  
ATOM    228  CG  ARG A  30     -33.431  -5.169  22.332  1.00 20.17           C  
ANISOU  228  CG  ARG A  30     2818   2134   2710     91    -46    190       C  
ATOM    229  CD  ARG A  30     -32.618  -4.653  21.159  1.00 23.39           C  
ANISOU  229  CD  ARG A  30     3472   2359   3056   -245     25    593       C  
ATOM    230  NE  ARG A  30     -32.537  -5.698  20.164  1.00 30.70           N  
ANISOU  230  NE  ARG A  30     3958   4072   3631    262   -235   -163       N  
ATOM    231  CZ  ARG A  30     -31.516  -6.542  20.002  1.00 26.07           C  
ANISOU  231  CZ  ARG A  30     3665   3412   2827     83    221    670       C  
ATOM    232  NH1 ARG A  30     -30.394  -6.417  20.695  1.00 30.98           N  
ANISOU  232  NH1 ARG A  30     4631   3412   3727   -325   -986    184       N  
ATOM    233  NH2 ARG A  30     -31.624  -7.491  19.104  1.00 34.37           N  
ANISOU  233  NH2 ARG A  30     4702   4383   3973   -570   -308   -272       N  
ATOM    234  C   ARG A  30     -35.792  -4.805  24.289  1.00 17.49           C  
ANISOU  234  C   ARG A  30     2501   1921   2224   -142   -205   -229       C  
ATOM    235  O   ARG A  30     -36.604  -3.897  24.287  1.00 19.22           O  
ANISOU  235  O   ARG A  30     2997   1879   2424     58   -272   -115       O  
ATOM    236  N   ILE A  31     -34.907  -5.015  25.257  1.00 16.06           N  
ANISOU  236  N   ILE A  31     2353   1560   2187   -476   -203   -146       N  
ATOM    237  CA  ILE A  31     -34.492  -3.970  26.180  1.00 16.44           C  
ANISOU  237  CA  ILE A  31     2384   1760   2101   -398    -23   -368       C  
ATOM    238  CB  ILE A  31     -34.896  -4.301  27.635  1.00 19.32           C  
ANISOU  238  CB  ILE A  31     2424   2585   2332    -91    114     30       C  
ATOM    239  CG1 ILE A  31     -34.274  -5.619  28.105  1.00 18.98           C  
ANISOU  239  CG1 ILE A  31     2700   2245   2267   -269    107   -230       C  
ATOM    240  CG2 ILE A  31     -36.415  -4.297  27.777  1.00 20.85           C  
ANISOU  240  CG2 ILE A  31     2461   2903   2556     16     25    158       C  
ATOM    241  CD1 ILE A  31     -34.514  -5.934  29.569  1.00 22.15           C  
ANISOU  241  CD1 ILE A  31     3419   2696   2299   -170    149   -211       C  
ATOM    242  C   ILE A  31     -32.980  -3.827  26.016  1.00 17.34           C  
ANISOU  242  C   ILE A  31     2400   1853   2333   -327     17   -282       C  
ATOM    243  O   ILE A  31     -32.304  -4.726  25.536  1.00 18.96           O  
ANISOU  243  O   ILE A  31     2458   1907   2839   -203   -273   -307       O  
ATOM    244  N   GLY A  32     -32.441  -2.692  26.424  1.00 18.52           N  
ANISOU  244  N   GLY A  32     2508   1763   2763   -146    107   -433       N  
ATOM    245  CA  GLY A  32     -31.045  -2.432  26.240  1.00 18.85           C  
ANISOU  245  CA  GLY A  32     2594   2119   2449   -233    269   -230       C  
ATOM    246  C   GLY A  32     -30.588  -1.300  27.116  1.00 19.36           C  
ANISOU  246  C   GLY A  32     2712   2108   2537   -242    390   -432       C  
ATOM    247  O   GLY A  32     -31.380  -0.735  27.871  1.00 28.03           O  
ANISOU  247  O   GLY A  32     3018   3351   4280   -796   1121  -1535       O  
ATOM    248  N   ILE A  33     -29.294  -1.019  27.057  1.00 17.77           N  
ANISOU  248  N   ILE A  33     2788   1814   2146   -261     97   -329       N  
ATOM    249  CA  ILE A  33     -28.708   0.044  27.831  1.00 16.05           C  
ANISOU  249  CA  ILE A  33     2638   1891   1568   -222     64   -223       C  
ATOM    250  CB  ILE A  33     -27.254  -0.280  28.203  1.00 16.84           C  
ANISOU  250  CB  ILE A  33     2784   1853   1759   -290   -221   -353       C  
ATOM    251  CG1 ILE A  33     -27.200  -1.547  29.076  1.00 18.78           C  
ANISOU  251  CG1 ILE A  33     3031   1968   2134      7   -306   -167       C  
ATOM    252  CG2 ILE A  33     -26.649   0.925  28.904  1.00 15.40           C  
ANISOU  252  CG2 ILE A  33     2449   1729   1671   -364    -87   -204       C  
ATOM    253  CD1 ILE A  33     -25.822  -1.917  29.613  1.00 21.48           C  
ANISOU  253  CD1 ILE A  33     3185   2524   2453    399     23   -169       C  
ATOM    254  C   ILE A  33     -28.842   1.336  27.032  1.00 15.00           C  
ANISOU  254  C   ILE A  33     2458   1830   1410   -435    -94   -324       C  
ATOM    255  O   ILE A  33     -28.366   1.454  25.905  1.00 17.47           O  
ANISOU  255  O   ILE A  33     3288   1775   1571   -357    281   -228       O  
ATOM    256  N   PRO A  34     -29.552   2.354  27.542  1.00 14.15           N  
ANISOU  256  N   PRO A  34     2277   1881   1216   -299    141     25       N  
ATOM    257  CA  PRO A  34     -29.830   3.533  26.729  1.00 13.97           C  
ANISOU  257  CA  PRO A  34     2254   1665   1389   -272    -77    -99       C  
ATOM    258  CB  PRO A  34     -30.992   4.247  27.412  1.00 17.06           C  
ANISOU  258  CB  PRO A  34     2280   2206   1994   -171    153     67       C  
ATOM    259  CG  PRO A  34     -31.036   3.695  28.759  1.00 20.11           C  
ANISOU  259  CG  PRO A  34     2955   2912   1774    385    257   -165       C  
ATOM    260  CD  PRO A  34     -30.265   2.397  28.808  1.00 16.64           C  
ANISOU  260  CD  PRO A  34     2645   2290   1387   -121    341   -153       C  
ATOM    261  C   PRO A  34     -28.648   4.504  26.600  1.00 12.91           C  
ANISOU  261  C   PRO A  34     1995   1581   1326   -111      9   -216       C  
ATOM    262  O   PRO A  34     -27.665   4.447  27.372  1.00 14.15           O  
ANISOU  262  O   PRO A  34     2118   1807   1450   -145   -162   -102       O  
ATOM    263  N   TYR A  35     -28.806   5.400  25.627  1.00 12.87           N  
ANISOU  263  N   TYR A  35     1939   1687   1262    -86    -62   -150       N  
ATOM    264  CA  TYR A  35     -27.871   6.493  25.364  1.00 13.45           C  
ANISOU  264  CA  TYR A  35     1880   1768   1460   -168    114   -199       C  
ATOM    265  CB  TYR A  35     -27.473   6.468  23.887  1.00 14.52           C  
ANISOU  265  CB  TYR A  35     1985   1959   1572   -266    363    -99       C  
ATOM    266  CG  TYR A  35     -26.341   5.523  23.607  1.00 15.35           C  
ANISOU  266  CG  TYR A  35     2123   2249   1460    -37    329   -297       C  
ATOM    267  CD1 TYR A  35     -26.564   4.156  23.570  1.00 16.47           C  
ANISOU  267  CD1 TYR A  35     2474   2333   1448    270    414   -326       C  
ATOM    268  CE1 TYR A  35     -25.527   3.266  23.374  1.00 19.53           C  
ANISOU  268  CE1 TYR A  35     3083   2678   1657    734    376   -358       C  
ATOM    269  CZ  TYR A  35     -24.248   3.739  23.188  1.00 20.11           C  
ANISOU  269  CZ  TYR A  35     2785   3241   1614   1043    143   -482       C  
ATOM    270  OH  TYR A  35     -23.237   2.850  22.965  1.00 29.15           O  
ANISOU  270  OH  TYR A  35     3816   5068   2191   2328    -44   -911       O  
ATOM    271  CE2 TYR A  35     -24.003   5.093  23.202  1.00 19.48           C  
ANISOU  271  CE2 TYR A  35     2193   3451   1758    416    220  -1008       C  
ATOM    272  CD2 TYR A  35     -25.042   5.977  23.426  1.00 16.77           C  
ANISOU  272  CD2 TYR A  35     2116   2422   1831     83    341   -696       C  
ATOM    273  C   TYR A  35     -28.449   7.843  25.782  1.00 14.48           C  
ANISOU  273  C   TYR A  35     1991   1753   1756   -153    163   -108       C  
ATOM    274  O   TYR A  35     -27.810   8.859  25.568  1.00 14.65           O  
ANISOU  274  O   TYR A  35     2157   1645   1763   -113    221     43       O  
ATOM    275  N   SER A  36     -29.647   7.823  26.368  1.00 13.77           N  
ANISOU  275  N   SER A  36     1841   1389   2001   -101    107   -299       N  
ATOM    276  CA  SER A  36     -30.250   8.980  27.022  1.00 17.20           C  
ANISOU  276  CA  SER A  36     2100   2012   2422    119    299   -597       C  
ATOM    277  CB  SER A  36     -31.740   8.788  27.079  1.00 18.78           C  
ANISOU  277  CB  SER A  36     2198   2268   2668    -20    290   -885       C  
ATOM    278  OG  SER A  36     -32.039   7.563  27.724  1.00 19.25           O  
ANISOU  278  OG  SER A  36     2038   2829   2447   -284    266   -663       O  
ATOM    279  C   SER A  36     -29.617   9.116  28.418  1.00 16.97           C  
ANISOU  279  C   SER A  36     2265   1859   2321    -13    285   -693       C  
ATOM    280  O   SER A  36     -29.127   8.160  28.989  1.00 18.40           O  
ANISOU  280  O   SER A  36     2318   2164   2506    -44     75   -505       O  
ATOM    281  N   THR A  37     -29.695  10.310  28.996  1.00 16.67           N  
ANISOU  281  N   THR A  37     2090   1746   2498   -359    270   -582       N  
ATOM    282  CA  THR A  37     -29.037  10.668  30.270  1.00 16.70           C  
ANISOU  282  CA  THR A  37     2146   2112   2086    -93    230   -230       C  
ATOM    283  CB  THR A  37     -29.906  10.312  31.485  1.00 17.18           C  
ANISOU  283  CB  THR A  37     2273   2120   2134   -219    325   -220       C  
ATOM    284  OG1 THR A  37     -30.081   8.905  31.691  1.00 18.06           O  
ANISOU  284  OG1 THR A  37     2150   2135   2576   -197    142   -359       O  
ATOM    285  CG2 THR A  37     -31.276  10.943  31.417  1.00 18.67           C  
ANISOU  285  CG2 THR A  37     2586   2220   2286    -19    427   -167       C  
ATOM    286  C   THR A  37     -27.612  10.088  30.352  1.00 15.27           C  
ANISOU  286  C   THR A  37     2213   1962   1628    -58     17   -115       C  
ATOM    287  O   THR A  37     -27.144   9.663  31.429  1.00 17.17           O  
ANISOU  287  O   THR A  37     2507   2180   1837   -436   -166    266       O  
ATOM    288  N   PHE A  38     -26.870  10.178  29.241  1.00 14.18           N  
ANISOU  288  N   PHE A  38     2131   1773   1482   -177   -118   -188       N  
ATOM    289  CA  PHE A  38     -25.460   9.854  29.198  1.00 13.67           C  
ANISOU  289  CA  PHE A  38     2040   1508   1645   -289    -13    -30       C  
ATOM    290  CB  PHE A  38     -25.031   9.687  27.737  1.00 15.64           C  
ANISOU  290  CB  PHE A  38     2230   1950   1759   -175    -68   -293       C  
ATOM    291  CG  PHE A  38     -23.811   8.847  27.418  1.00 14.25           C  
ANISOU  291  CG  PHE A  38     1970   1745   1698   -338    -62   -144       C  
ATOM    292  CD1 PHE A  38     -22.637   8.901  28.153  1.00 15.82           C  
ANISOU  292  CD1 PHE A  38     1921   2135   1952   -252    -13   -138       C  
ATOM    293  CE1 PHE A  38     -21.542   8.125  27.800  1.00 14.08           C  
ANISOU  293  CE1 PHE A  38     2014   1723   1612   -319   -184   -235       C  
ATOM    294  CZ  PHE A  38     -21.581   7.317  26.701  1.00 15.19           C  
ANISOU  294  CZ  PHE A  38     2147   1828   1797   -264   -110   -305       C  
ATOM    295  CD2 PHE A  38     -23.833   8.015  26.323  1.00 15.55           C  
ANISOU  295  CD2 PHE A  38     2300   1675   1932   -202     -3   -256       C  
ATOM    296  CE2 PHE A  38     -22.719   7.271  25.950  1.00 15.55           C  
ANISOU  296  CE2 PHE A  38     2233   1994   1678    -73   -198   -361       C  
ATOM    297  C   PHE A  38     -24.705  10.997  29.890  1.00 13.68           C  
ANISOU  297  C   PHE A  38     2167   1304   1727   -245     24      4       C  
ATOM    298  O   PHE A  38     -24.865  12.140  29.506  1.00 16.89           O  
ANISOU  298  O   PHE A  38     2731   1286   2400   -196   -399    204       O  
ATOM    299  N   GLN A  39     -23.947  10.694  30.940  1.00 12.94           N  
ANISOU  299  N   GLN A  39     2002   1235   1678   -195      3   -203       N  
ATOM    300  CA  GLN A  39     -23.313  11.738  31.756  1.00 12.93           C  
ANISOU  300  CA  GLN A  39     2074   1025   1811   -183     61   -202       C  
ATOM    301  CB  GLN A  39     -23.086  11.234  33.177  1.00 14.43           C  
ANISOU  301  CB  GLN A  39     2402   1241   1840   -240     75   -141       C  
ATOM    302  CG  GLN A  39     -24.356  10.778  33.873  1.00 15.84           C  
ANISOU  302  CG  GLN A  39     2644   1449   1923   -434    241   -144       C  
ATOM    303  CD  GLN A  39     -25.400  11.854  33.978  1.00 21.74           C  
ANISOU  303  CD  GLN A  39     3314   1902   3044   -297    335   -302       C  
ATOM    304  OE1 GLN A  39     -25.142  12.865  34.607  1.00 28.25           O  
ANISOU  304  OE1 GLN A  39     4390   2769   3572     -9    676  -1487       O  
ATOM    305  NE2 GLN A  39     -26.557  11.652  33.333  1.00 27.03           N  
ANISOU  305  NE2 GLN A  39     3313   3070   3887   -547    433    -92       N  
ATOM    306  C   GLN A  39     -21.974  12.171  31.154  1.00 12.81           C  
ANISOU  306  C   GLN A  39     1990   1173   1703   -131    -52   -200       C  
ATOM    307  O   GLN A  39     -21.139  11.330  30.799  1.00 13.49           O  
ANISOU  307  O   GLN A  39     1628   1462   2035   -208      5   -315       O  
ATOM    308  N   THR A  40     -21.801  13.488  31.053  1.00 13.68           N  
ANISOU  308  N   THR A  40     1963   1146   2088    -54     37   -147       N  
ATOM    309  CA  THR A  40     -20.512  14.142  30.813  1.00 12.96           C  
ANISOU  309  CA  THR A  40     2167    945   1812   -109     15   -232       C  
ATOM    310  CB  THR A  40     -20.546  15.044  29.582  1.00 13.83           C  
ANISOU  310  CB  THR A  40     2423   1213   1616   -250     21   -218       C  
ATOM    311  OG1 THR A  40     -20.724  14.251  28.396  1.00 16.73           O  
ANISOU  311  OG1 THR A  40     3007   1631   1718   -272   -278   -293       O  
ATOM    312  CG2 THR A  40     -19.257  15.820  29.422  1.00 15.65           C  
ANISOU  312  CG2 THR A  40     2540   1383   2023   -278     95    -49       C  
ATOM    313  C   THR A  40     -20.169  14.881  32.105  1.00 12.99           C  
ANISOU  313  C   THR A  40     2087   1170   1677    -75    201   -254       C  
ATOM    314  O   THR A  40     -20.823  15.859  32.458  1.00 15.31           O  
ANISOU  314  O   THR A  40     2419   1348   2047    232     51   -355       O  
ATOM    315  N   ILE A  41     -19.189  14.339  32.843  1.00 12.54           N  
ANISOU  315  N   ILE A  41     1980   1173   1608   -115    215   -443       N  
ATOM    316  CA  ILE A  41     -18.873  14.796  34.185  1.00 12.66           C  
ANISOU  316  CA  ILE A  41     2089   1205   1516   -151    401   -435       C  
ATOM    317  CB  ILE A  41     -18.737  13.606  35.134  1.00 13.20           C  
ANISOU  317  CB  ILE A  41     2133   1286   1596   -293    328   -364       C  
ATOM    318  CG1 ILE A  41     -20.002  12.739  35.070  1.00 14.00           C  
ANISOU  318  CG1 ILE A  41     2033   1450   1833   -341    579   -301       C  
ATOM    319  CG2 ILE A  41     -18.394  14.060  36.550  1.00 13.66           C  
ANISOU  319  CG2 ILE A  41     2281   1261   1646   -356    392   -437       C  
ATOM    320  CD1 ILE A  41     -19.881  11.441  35.794  1.00 15.18           C  
ANISOU  320  CD1 ILE A  41     2197   1444   2127   -408    633   -238       C  
ATOM    321  C   ILE A  41     -17.600  15.642  34.146  1.00 13.67           C  
ANISOU  321  C   ILE A  41     2035   1424   1734   -166    404   -460       C  
ATOM    322  O   ILE A  41     -16.561  15.190  33.655  1.00 13.52           O  
ANISOU  322  O   ILE A  41     1675   1592   1868   -274    303   -634       O  
ATOM    323  N   GLN A  42     -17.724  16.875  34.639  1.00 13.15           N  
ANISOU  323  N   GLN A  42     1997   1239   1758   -133     83   -320       N  
ATOM    324  CA  GLN A  42     -16.591  17.819  34.709  1.00 13.69           C  
ANISOU  324  CA  GLN A  42     1805   1607   1789   -152      3   -329       C  
ATOM    325  CB  GLN A  42     -17.078  19.270  34.724  1.00 17.63           C  
ANISOU  325  CB  GLN A  42     2529   1557   2610   -201   -351   -208       C  
ATOM    326  CG  GLN A  42     -17.795  19.651  33.434  1.00 23.48           C  
ANISOU  326  CG  GLN A  42     3135   2478   3307    152   -868   -274       C  
ATOM    327  CD  GLN A  42     -18.204  21.103  33.423  1.00 31.12           C  
ANISOU  327  CD  GLN A  42     5048   2709   4066    441   -729   -132       C  
ATOM    328  OE1 GLN A  42     -18.412  21.724  34.466  1.00 40.14           O  
ANISOU  328  OE1 GLN A  42     6881   3395   4973    523   -578   -987       O  
ATOM    329  NE2 GLN A  42     -18.334  21.650  32.225  1.00 40.72           N  
ANISOU  329  NE2 GLN A  42     6556   4695   4218    699      4    579       N  
ATOM    330  C   GLN A  42     -15.778  17.533  35.960  1.00 12.01           C  
ANISOU  330  C   GLN A  42     1829   1317   1418   -182    169   -381       C  
ATOM    331  O   GLN A  42     -16.329  17.090  36.968  1.00 12.78           O  
ANISOU  331  O   GLN A  42     1885   1590   1378   -212    251   -423       O  
ATOM    332  N   PRO A  43     -14.464  17.806  35.945  1.00 11.81           N  
ANISOU  332  N   PRO A  43     1941   1271   1272   -311    140   -316       N  
ATOM    333  CA  PRO A  43     -13.653  17.660  37.150  1.00 12.09           C  
ANISOU  333  CA  PRO A  43     1763   1406   1423   -421     38   -358       C  
ATOM    334  CB  PRO A  43     -12.202  17.838  36.673  1.00 13.82           C  
ANISOU  334  CB  PRO A  43     1967   1637   1646   -417    175   -493       C  
ATOM    335  CG  PRO A  43     -12.332  18.605  35.378  1.00 17.41           C  
ANISOU  335  CG  PRO A  43     2245   2465   1905   -661    143   -213       C  
ATOM    336  CD  PRO A  43     -13.696  18.310  34.807  1.00 14.19           C  
ANISOU  336  CD  PRO A  43     2150   1706   1536   -644    155   -143       C  
ATOM    337  C   PRO A  43     -14.050  18.713  38.195  1.00 12.98           C  
ANISOU  337  C   PRO A  43     2002   1358   1572   -178    135   -323       C  
ATOM    338  O   PRO A  43     -14.672  19.731  37.871  1.00 13.18           O  
ANISOU  338  O   PRO A  43     1985   1300   1723    -88     20   -427       O  
ATOM    339  N   VAL A  44     -13.688  18.455  39.462  1.00 12.09           N  
ANISOU  339  N   VAL A  44     1851   1292   1449   -234    298   -443       N  
ATOM    340  CA  VAL A  44     -14.074  19.335  40.551  1.00 12.78           C  
ANISOU  340  CA  VAL A  44     1951   1390   1513   -243    426   -498       C  
ATOM    341  CB  VAL A  44     -13.885  18.669  41.922  1.00 14.18           C  
ANISOU  341  CB  VAL A  44     2155   1679   1552   -303    331   -331       C  
ATOM    342  CG1 VAL A  44     -14.727  17.392  42.040  1.00 14.36           C  
ANISOU  342  CG1 VAL A  44     2194   1711   1548   -375    369   -222       C  
ATOM    343  CG2 VAL A  44     -12.425  18.414  42.243  1.00 15.37           C  
ANISOU  343  CG2 VAL A  44     2276   1951   1609   -262    254   -385       C  
ATOM    344  C   VAL A  44     -13.328  20.674  40.504  1.00 12.86           C  
ANISOU  344  C   VAL A  44     1903   1520   1461   -350    290   -603       C  
ATOM    345  O   VAL A  44     -13.792  21.663  41.084  1.00 13.41           O  
ANISOU  345  O   VAL A  44     1898   1345   1849   -367    410   -608       O  
ATOM    346  N   SER A  45     -12.176  20.699  39.845  1.00 14.23           N  
ANISOU  346  N   SER A  45     2168   1594   1645   -576    566   -747       N  
ATOM    347  CA  SER A  45     -11.397  21.923  39.645  1.00 15.71           C  
ANISOU  347  CA  SER A  45     2240   1867   1859   -869    513   -720       C  
ATOM    348  CB  SER A  45     -10.206  22.007  40.565  1.00 16.30           C  
ANISOU  348  CB  SER A  45     2588   1901   1701  -1174    451   -697       C  
ATOM    349  OG  SER A  45      -9.270  20.957  40.326  1.00 18.57           O  
ANISOU  349  OG  SER A  45     2588   2327   2141  -1059    -56   -545       O  
ATOM    350  C   SER A  45     -10.983  21.983  38.182  1.00 14.93           C  
ANISOU  350  C   SER A  45     2121   1817   1732   -779    261   -667       C  
ATOM    351  O   SER A  45     -10.955  20.949  37.518  1.00 14.74           O  
ANISOU  351  O   SER A  45     2085   1810   1704   -650    137   -693       O  
ATOM    352  N   ASP A  46     -10.702  23.184  37.677  1.00 14.82           N  
ANISOU  352  N   ASP A  46     2251   1633   1745   -517    382   -637       N  
ATOM    353  CA AASP A  46     -10.323  23.323  36.287  0.70 15.93           C  
ANISOU  353  CA AASP A  46     2283   1893   1877   -371    322   -505       C  
ATOM    354  CA BASP A  46     -10.283  23.368  36.285  0.30 15.25           C  
ANISOU  354  CA BASP A  46     2132   1940   1721   -426    314   -618       C  
ATOM    355  CB AASP A  46      -9.999  24.776  35.951  0.70 17.73           C  
ANISOU  355  CB AASP A  46     2640   1828   2267   -446    350   -559       C  
ATOM    356  CB BASP A  46      -9.856  24.816  35.991  0.30 14.86           C  
ANISOU  356  CB BASP A  46     2131   1944   1571   -439    340   -694       C  
ATOM    357  CG AASP A  46     -11.198  25.712  35.915  0.70 21.67           C  
ANISOU  357  CG AASP A  46     2907   2203   3122   -210    211   -369       C  
ATOM    358  CG BASP A  46      -9.585  25.147  34.519  0.30 15.72           C  
ANISOU  358  CG BASP A  46     2062   2275   1637   -359    397   -579       C  
ATOM    359  OD1AASP A  46     -12.353  25.233  35.941  0.70 25.77           O  
ANISOU  359  OD1AASP A  46     3032   2962   3797   -175    160   -144       O  
ATOM    360  OD1BASP A  46     -10.228  24.544  33.672  0.30 16.96           O  
ANISOU  360  OD1BASP A  46     2072   2586   1784   -538    321   -452       O  
ATOM    361  OD2AASP A  46     -10.956  26.940  35.856  0.70 28.34           O  
ANISOU  361  OD2AASP A  46     3795   2166   4806     97     38   -268       O  
ATOM    362  OD2BASP A  46      -8.756  26.053  34.228  0.30 15.42           O  
ANISOU  362  OD2BASP A  46     1951   2412   1494   -678   -217  -1132       O  
ATOM    363  C   ASP A  46      -9.122  22.410  36.023  1.00 14.28           C  
ANISOU  363  C   ASP A  46     2189   1593   1644   -507    339   -570       C  
ATOM    364  O   ASP A  46      -8.185  22.323  36.837  1.00 15.53           O  
ANISOU  364  O   ASP A  46     2239   2047   1613   -480    238   -614       O  
ATOM    365  N   ALA A  47      -9.169  21.709  34.894  1.00 13.62           N  
ANISOU  365  N   ALA A  47     1863   1753   1558   -481    292   -543       N  
ATOM    366  CA  ALA A  47      -8.108  20.798  34.516  1.00 13.91           C  
ANISOU  366  CA  ALA A  47     1914   1624   1747   -472    220   -641       C  
ATOM    367  CB  ALA A  47      -8.440  20.157  33.192  1.00 14.51           C  
ANISOU  367  CB  ALA A  47     1948   1792   1771   -713     97   -591       C  
ATOM    368  C   ALA A  47      -6.788  21.551  34.396  1.00 13.10           C  
ANISOU  368  C   ALA A  47     1978   1472   1525   -534    208   -539       C  
ATOM    369  O   ALA A  47      -6.758  22.717  33.981  1.00 13.60           O  
ANISOU  369  O   ALA A  47     2019   1493   1652   -344    182   -420       O  
ATOM    370  N   PRO A  48      -5.649  20.910  34.720  1.00 13.28           N  
ANISOU  370  N   PRO A  48     2077   1477   1488   -553    362   -287       N  
ATOM    371  CA  PRO A  48      -4.357  21.578  34.599  1.00 13.21           C  
ANISOU  371  CA  PRO A  48     1959   1481   1576   -569      0   -522       C  
ATOM    372  CB  PRO A  48      -3.362  20.562  35.147  1.00 15.10           C  
ANISOU  372  CB  PRO A  48     2084   1905   1745   -458     65   -302       C  
ATOM    373  CG  PRO A  48      -4.087  19.213  34.980  1.00 15.47           C  
ANISOU  373  CG  PRO A  48     2143   1746   1986   -315   -106   -111       C  
ATOM    374  CD  PRO A  48      -5.547  19.535  35.215  1.00 15.21           C  
ANISOU  374  CD  PRO A  48     2269   1571   1939   -430    157   -218       C  
ATOM    375  C   PRO A  48      -4.089  21.882  33.122  1.00 12.91           C  
ANISOU  375  C   PRO A  48     1837   1412   1656   -692    119   -390       C  
ATOM    376  O   PRO A  48      -4.225  20.999  32.270  1.00 13.60           O  
ANISOU  376  O   PRO A  48     1877   1447   1842   -466    107   -516       O  
ATOM    377  N   ASN A  49      -3.710  23.122  32.817  1.00 13.13           N  
ANISOU  377  N   ASN A  49     2175   1289   1525   -563    182   -444       N  
ATOM    378  CA  ASN A  49      -3.676  23.587  31.416  1.00 13.55           C  
ANISOU  378  CA  ASN A  49     2124   1403   1619   -455    188   -402       C  
ATOM    379  CB  ASN A  49      -3.311  25.063  31.362  1.00 15.08           C  
ANISOU  379  CB  ASN A  49     2623   1365   1741   -532    141   -646       C  
ATOM    380  CG  ASN A  49      -3.450  25.642  29.973  1.00 16.07           C  
ANISOU  380  CG  ASN A  49     2651   1623   1829   -212    230   -559       C  
ATOM    381  OD1 ASN A  49      -4.494  25.515  29.346  1.00 18.08           O  
ANISOU  381  OD1 ASN A  49     3174   1776   1919   -290    -96   -310       O  
ATOM    382  ND2 ASN A  49      -2.405  26.283  29.499  1.00 19.04           N  
ANISOU  382  ND2 ASN A  49     3158   1719   2357   -268    894   -676       N  
ATOM    383  C   ASN A  49      -2.682  22.782  30.564  1.00 13.11           C  
ANISOU  383  C   ASN A  49     2175   1267   1538   -557    265   -370       C  
ATOM    384  O   ASN A  49      -2.892  22.626  29.368  1.00 13.67           O  
ANISOU  384  O   ASN A  49     2151   1552   1488   -449    236   -373       O  
ATOM    385  N   ASN A  50      -1.625  22.262  31.191  1.00 13.53           N  
ANISOU  385  N   ASN A  50     1857   1456   1827   -409    396   -327       N  
ATOM    386  CA  ASN A  50      -0.593  21.483  30.500  1.00 14.74           C  
ANISOU  386  CA  ASN A  50     2019   1637   1941   -237    381   -418       C  
ATOM    387  CB  ASN A  50       0.805  21.958  30.891  1.00 16.10           C  
ANISOU  387  CB  ASN A  50     1916   1764   2434   -266    389   -403       C  
ATOM    388  CG  ASN A  50       1.172  21.554  32.299  1.00 19.99           C  
ANISOU  388  CG  ASN A  50     2451   2338   2805   -374   -162   -528       C  
ATOM    389  OD1 ASN A  50       0.285  21.131  33.054  1.00 22.96           O  
ANISOU  389  OD1 ASN A  50     2854   2371   3498   -701   -174   -800       O  
ATOM    390  ND2 ASN A  50       2.436  21.669  32.665  1.00 28.09           N  
ANISOU  390  ND2 ASN A  50     2600   3427   4643   -558   -535   -475       N  
ATOM    391  C   ASN A  50      -0.720  19.971  30.767  1.00 13.82           C  
ANISOU  391  C   ASN A  50     1867   1596   1789   -184    289   -342       C  
ATOM    392  O   ASN A  50       0.208  19.209  30.454  1.00 15.32           O  
ANISOU  392  O   ASN A  50     2112   1742   1968    -72    507   -328       O  
ATOM    393  N   GLY A  51      -1.845  19.526  31.333  1.00 13.41           N  
ANISOU  393  N   GLY A  51     1985   1472   1636   -283    261   -332       N  
ATOM    394  CA  GLY A  51      -2.103  18.107  31.525  1.00 13.76           C  
ANISOU  394  CA  GLY A  51     2194   1471   1560   -331    284   -395       C  
ATOM    395  C   GLY A  51      -1.455  17.460  32.748  1.00 13.23           C  
ANISOU  395  C   GLY A  51     1958   1586   1483   -457    171   -464       C  
ATOM    396  O   GLY A  51      -1.685  16.277  32.982  1.00 13.60           O  
ANISOU  396  O   GLY A  51     2072   1449   1644   -352   -104   -532       O  
ATOM    397  N  AILE A  52      -0.736  18.218  33.577  0.50 12.91           N  
ANISOU  397  N  AILE A  52     1972   1454   1480   -361    182   -497       N  
ATOM    398  N  BILE A  52      -0.722  18.217  33.568  0.50 13.31           N  
ANISOU  398  N  BILE A  52     2015   1458   1584   -357     98   -494       N  
ATOM    399  CA AILE A  52       0.006  17.649  34.703  0.50 13.94           C  
ANISOU  399  CA AILE A  52     2063   1738   1494   -455    101   -538       C  
ATOM    400  CA BILE A  52      -0.009  17.667  34.720  0.50 14.71           C  
ANISOU  400  CA BILE A  52     2179   1776   1634   -438    -16   -530       C  
ATOM    401  CB AILE A  52       1.486  18.043  34.626  0.50 14.47           C  
ANISOU  401  CB AILE A  52     2028   2044   1424   -368    181   -583       C  
ATOM    402  CB BILE A  52       1.461  18.091  34.742  0.50 16.32           C  
ANISOU  402  CB BILE A  52     2157   2213   1830   -362   -152   -518       C  
ATOM    403  CG1AILE A  52       2.189  17.297  33.491  0.50 13.88           C  
ANISOU  403  CG1AILE A  52     1868   2000   1405   -455    276   -515       C  
ATOM    404  CG1BILE A  52       2.114  17.919  33.382  0.50 17.55           C  
ANISOU  404  CG1BILE A  52     2268   2522   1876   -354   -121   -566       C  
ATOM    405  CG2AILE A  52       2.155  17.816  35.972  0.50 16.16           C  
ANISOU  405  CG2AILE A  52     2142   2417   1582   -343     27   -520       C  
ATOM    406  CG2BILE A  52       2.197  17.297  35.813  0.50 16.69           C  
ANISOU  406  CG2BILE A  52     2049   2449   1841   -312   -272   -566       C  
ATOM    407  CD1AILE A  52       3.559  17.837  33.151  0.50 13.78           C  
ANISOU  407  CD1AILE A  52     1818   2164   1253   -378    391   -615       C  
ATOM    408  CD1BILE A  52       2.113  16.505  32.958  0.50 18.98           C  
ANISOU  408  CD1BILE A  52     2555   2604   2051   -394    -39   -713       C  
ATOM    409  C  AILE A  52      -0.607  18.113  36.025  0.50 14.14           C  
ANISOU  409  C  AILE A  52     2161   1732   1478   -489     86   -595       C  
ATOM    410  C  BILE A  52      -0.673  18.135  36.011  0.50 14.52           C  
ANISOU  410  C  BILE A  52     2229   1673   1614   -526     21   -556       C  
ATOM    411  O  AILE A  52      -0.497  19.294  36.371  0.50 15.49           O  
ANISOU  411  O  AILE A  52     2464   1792   1628   -536    141   -687       O  
ATOM    412  O  BILE A  52      -0.686  19.348  36.309  0.50 15.51           O  
ANISOU  412  O  BILE A  52     2569   1670   1652   -549    271   -536       O  
ATOM    413  N   GLY A  53      -1.177  17.181  36.792  1.00 14.83           N  
ANISOU  413  N   GLY A  53     2358   1702   1574   -491    123   -612       N  
ATOM    414  CA  GLY A  53      -1.767  17.510  38.077  1.00 16.23           C  
ANISOU  414  CA  GLY A  53     2568   1970   1629   -660    247   -713       C  
ATOM    415  C   GLY A  53      -2.905  16.588  38.430  1.00 15.21           C  
ANISOU  415  C   GLY A  53     2660   1642   1474   -619    350   -929       C  
ATOM    416  O   GLY A  53      -3.399  15.817  37.619  1.00 14.59           O  
ANISOU  416  O   GLY A  53     2246   1689   1606   -570    356  -1007       O  
ATOM    417  N   GLN A  54      -3.328  16.671  39.688  1.00 17.50           N  
ANISOU  417  N   GLN A  54     3266   1791   1589   -647    608   -752       N  
ATOM    418  CA AGLN A  54      -4.404  15.820  40.160  0.70 17.66           C  
ANISOU  418  CA AGLN A  54     3172   1742   1796   -493    644   -740       C  
ATOM    419  CA BGLN A  54      -4.415  15.830  40.168  0.30 16.85           C  
ANISOU  419  CA BGLN A  54     3076   1430   1894   -396    669   -737       C  
ATOM    420  CB AGLN A  54      -4.424  15.849  41.685  0.70 19.53           C  
ANISOU  420  CB AGLN A  54     3446   2162   1810   -339    809   -655       C  
ATOM    421  CB BGLN A  54      -4.622  15.943  41.671  0.30 16.27           C  
ANISOU  421  CB BGLN A  54     2965   1288   1927   -380    769   -693       C  
ATOM    422  CG AGLN A  54      -5.279  14.773  42.313  0.70 19.65           C  
ANISOU  422  CG AGLN A  54     3369   2199   1899    -21    824   -395       C  
ATOM    423  CG BGLN A  54      -3.594  15.201  42.459  0.30 14.92           C  
ANISOU  423  CG BGLN A  54     2831    854   1981   -256    790   -761       C  
ATOM    424  CD AGLN A  54      -5.224  14.871  43.822  0.70 21.39           C  
ANISOU  424  CD AGLN A  54     3685   2522   1920    348    242   -168       C  
ATOM    425  CD BGLN A  54      -4.036  15.170  43.894  0.30 13.88           C  
ANISOU  425  CD BGLN A  54     2619    654   2000   -171    829   -813       C  
ATOM    426  OE1AGLN A  54      -5.847  15.742  44.416  0.70 21.33           O  
ANISOU  426  OE1AGLN A  54     3167   2651   2285    623    175    129       O  
ATOM    427  OE1BGLN A  54      -5.111  15.661  44.238  0.30 14.32           O  
ANISOU  427  OE1BGLN A  54     2515    822   2102     17    576   -650       O  
ATOM    428  NE2AGLN A  54      -4.462  14.000  44.473  0.70 22.43           N  
ANISOU  428  NE2AGLN A  54     3821   2552   2149    486    144   -226       N  
ATOM    429  NE2BGLN A  54      -3.182  14.635  44.742  0.30 15.25           N  
ANISOU  429  NE2BGLN A  54     2668    789   2335     31    677   -823       N  
ATOM    430  C   GLN A  54      -5.708  16.268  39.500  1.00 17.33           C  
ANISOU  430  C   GLN A  54     3158   1310   2115   -202    820   -518       C  
ATOM    431  O   GLN A  54      -5.980  17.488  39.368  1.00 20.55           O  
ANISOU  431  O   GLN A  54     3800   1297   2709    -37    833   -560       O  
ATOM    432  N   ILE A  55      -6.531  15.282  39.138  1.00 14.84           N  
ANISOU  432  N   ILE A  55     2524   1282   1830    -18    529   -220       N  
ATOM    433  CA  ILE A  55      -7.824  15.494  38.518  1.00 16.06           C  
ANISOU  433  CA  ILE A  55     2472   1623   2006    178    664     21       C  
ATOM    434  CB  ILE A  55      -7.773  15.133  37.021  1.00 16.12           C  
ANISOU  434  CB  ILE A  55     2251   1932   1939    257    764     15       C  
ATOM    435  CG1 ILE A  55      -6.762  15.983  36.239  1.00 16.52           C  
ANISOU  435  CG1 ILE A  55     2123   2018   2135    270    768    -26       C  
ATOM    436  CG2 ILE A  55      -9.152  15.196  36.414  1.00 17.71           C  
ANISOU  436  CG2 ILE A  55     2267   2436   2023     83    801    148       C  
ATOM    437  CD1 ILE A  55      -6.256  15.307  34.989  1.00 16.21           C  
ANISOU  437  CD1 ILE A  55     2068   2155   1934    330    610     43       C  
ATOM    438  C   ILE A  55      -8.829  14.615  39.251  1.00 14.38           C  
ANISOU  438  C   ILE A  55     2090   1472   1901    427    560    139       C  
ATOM    439  O   ILE A  55      -8.607  13.428  39.357  1.00 14.67           O  
ANISOU  439  O   ILE A  55     2227   1328   2017    214    582     22       O  
ATOM    440  N   THR A  56      -9.915  15.202  39.753  1.00 14.25           N  
ANISOU  440  N   THR A  56     2294   1574   1543    393    650    -39       N  
ATOM    441  CA  THR A  56     -10.920  14.445  40.485  1.00 15.39           C  
ANISOU  441  CA  THR A  56     2324   1885   1636    475    658    195       C  
ATOM    442  CB  THR A  56     -10.956  14.797  41.975  1.00 16.61           C  
ANISOU  442  CB  THR A  56     2486   2253   1572    475    567    219       C  
ATOM    443  OG1 THR A  56      -9.710  14.407  42.532  1.00 20.33           O  
ANISOU  443  OG1 THR A  56     2576   3347   1802    763    592    581       O  
ATOM    444  CG2 THR A  56     -12.075  14.107  42.722  1.00 19.05           C  
ANISOU  444  CG2 THR A  56     2604   2913   1718    577    953    171       C  
ATOM    445  C   THR A  56     -12.303  14.667  39.876  1.00 14.02           C  
ANISOU  445  C   THR A  56     2181   1527   1618    538    664     19       C  
ATOM    446  O   THR A  56     -12.700  15.811  39.629  1.00 15.42           O  
ANISOU  446  O   THR A  56     2434   1583   1839    711    257     36       O  
ATOM    447  N   PHE A  57     -13.023  13.560  39.694  1.00 14.41           N  
ANISOU  447  N   PHE A  57     2245   1649   1578    534    727      1       N  
ATOM    448  CA  PHE A  57     -14.437  13.569  39.371  1.00 13.74           C  
ANISOU  448  CA  PHE A  57     2194   1382   1642    352    667    101       C  
ATOM    449  CB  PHE A  57     -14.748  12.661  38.179  1.00 14.48           C  
ANISOU  449  CB  PHE A  57     2172   1434   1893    368    634    -78       C  
ATOM    450  CG  PHE A  57     -13.963  13.016  36.947  1.00 14.09           C  
ANISOU  450  CG  PHE A  57     2229   1474   1647    141    517   -263       C  
ATOM    451  CD1 PHE A  57     -14.348  14.072  36.134  1.00 13.17           C  
ANISOU  451  CD1 PHE A  57     2025   1586   1393    147    347   -458       C  
ATOM    452  CE1 PHE A  57     -13.586  14.430  35.041  1.00 13.66           C  
ANISOU  452  CE1 PHE A  57     2300   1398   1490   -198    285   -444       C  
ATOM    453  CZ  PHE A  57     -12.415  13.787  34.780  1.00 14.63           C  
ANISOU  453  CZ  PHE A  57     2538   1502   1517      0    223   -417       C  
ATOM    454  CD2 PHE A  57     -12.765  12.374  36.667  1.00 15.62           C  
ANISOU  454  CD2 PHE A  57     2494   1595   1846    329    561     67       C  
ATOM    455  CE2 PHE A  57     -12.011  12.743  35.572  1.00 15.58           C  
ANISOU  455  CE2 PHE A  57     2544   1679   1695    216    527   -248       C  
ATOM    456  C   PHE A  57     -15.203  13.119  40.621  1.00 14.15           C  
ANISOU  456  C   PHE A  57     2150   1593   1630    427    716    101       C  
ATOM    457  O   PHE A  57     -14.823  12.120  41.243  1.00 16.09           O  
ANISOU  457  O   PHE A  57     2495   1732   1884    525    799    403       O  
ATOM    458  N   ASN A  58     -16.252  13.850  40.982  1.00 12.14           N  
ANISOU  458  N   ASN A  58     1777   1373   1461     87    530   -127       N  
ATOM    459  CA  ASN A  58     -17.020  13.572  42.186  1.00 12.17           C  
ANISOU  459  CA  ASN A  58     1913   1305   1403    -81    537   -273       C  
ATOM    460  CB  ASN A  58     -16.576  14.480  43.332  1.00 13.10           C  
ANISOU  460  CB  ASN A  58     2007   1604   1365   -100    486   -374       C  
ATOM    461  CG  ASN A  58     -17.327  14.237  44.625  1.00 16.42           C  
ANISOU  461  CG  ASN A  58     2653   2061   1522   -425    735   -408       C  
ATOM    462  OD1 ASN A  58     -18.418  13.675  44.628  1.00 21.38           O  
ANISOU  462  OD1 ASN A  58     3421   2897   1804  -1146    800   -583       O  
ATOM    463  ND2 ASN A  58     -16.829  14.802  45.711  1.00 22.00           N  
ANISOU  463  ND2 ASN A  58     3600   3057   1699   -547    442   -573       N  
ATOM    464  C   ASN A  58     -18.493  13.752  41.829  1.00 11.96           C  
ANISOU  464  C   ASN A  58     1806   1316   1420   -176    631   -293       C  
ATOM    465  O   ASN A  58     -18.971  14.889  41.695  1.00 15.23           O  
ANISOU  465  O   ASN A  58     2344   1414   2029   -155    354   -160       O  
ATOM    466  N   GLN A  59     -19.208  12.633  41.639  1.00 12.20           N  
ANISOU  466  N   GLN A  59     1923   1258   1454   -128    448   -138       N  
ATOM    467  CA  GLN A  59     -20.547  12.710  41.108  1.00 12.51           C  
ANISOU  467  CA  GLN A  59     1848   1335   1569   -196    385   -319       C  
ATOM    468  CB  GLN A  59     -20.524  12.845  39.591  1.00 13.81           C  
ANISOU  468  CB  GLN A  59     2112   1465   1670   -118    317    -78       C  
ATOM    469  CG  GLN A  59     -21.907  12.995  39.008  1.00 15.03           C  
ANISOU  469  CG  GLN A  59     2058   1913   1737   -309    315     22       C  
ATOM    470  CD  GLN A  59     -22.608  14.211  39.565  1.00 15.73           C  
ANISOU  470  CD  GLN A  59     2128   1682   2165   -335    231     81       C  
ATOM    471  OE1 GLN A  59     -22.211  15.356  39.271  1.00 18.83           O  
ANISOU  471  OE1 GLN A  59     2412   1825   2917   -331    333    342       O  
ATOM    472  NE2 GLN A  59     -23.654  14.004  40.363  1.00 15.56           N  
ANISOU  472  NE2 GLN A  59     1966   1990   1955   -315      3    265       N  
ATOM    473  C   GLN A  59     -21.369  11.508  41.561  1.00 12.59           C  
ANISOU  473  C   GLN A  59     1859   1553   1371   -212    277   -175       C  
ATOM    474  O   GLN A  59     -21.362  10.451  40.930  1.00 12.79           O  
ANISOU  474  O   GLN A  59     1852   1500   1505     12    274   -251       O  
ATOM    475  N   PRO A  60     -22.152  11.654  42.640  1.00 11.62           N  
ANISOU  475  N   PRO A  60     1773   1308   1333   -158    274   -279       N  
ATOM    476  CA  PRO A  60     -23.142  10.626  42.964  1.00 11.77           C  
ANISOU  476  CA  PRO A  60     1728   1397   1347    -96    321   -227       C  
ATOM    477  CB  PRO A  60     -23.904  11.228  44.147  1.00 12.39           C  
ANISOU  477  CB  PRO A  60     1575   1792   1340   -125    333   -313       C  
ATOM    478  CG  PRO A  60     -22.903  12.207  44.766  1.00 12.44           C  
ANISOU  478  CG  PRO A  60     1656   1595   1475   -108    445   -416       C  
ATOM    479  CD  PRO A  60     -22.145  12.780  43.591  1.00 12.72           C  
ANISOU  479  CD  PRO A  60     1842   1516   1475   -182    354   -375       C  
ATOM    480  C   PRO A  60     -24.076  10.373  41.785  1.00 12.26           C  
ANISOU  480  C   PRO A  60     1797   1400   1458    -19    226   -304       C  
ATOM    481  O   PRO A  60     -24.489  11.334  41.129  1.00 13.05           O  
ANISOU  481  O   PRO A  60     2025   1404   1529    -23    129   -276       O  
ATOM    482  N   LEU A  61     -24.399   9.101  41.538  1.00 13.27           N  
ANISOU  482  N   LEU A  61     1963   1507   1571   -113    264   -346       N  
ATOM    483  CA  LEU A  61     -25.266   8.721  40.433  1.00 13.76           C  
ANISOU  483  CA  LEU A  61     2036   1676   1515     -4    253   -451       C  
ATOM    484  CB  LEU A  61     -24.460   8.118  39.285  1.00 12.66           C  
ANISOU  484  CB  LEU A  61     1939   1273   1595    -57    294   -363       C  
ATOM    485  CG  LEU A  61     -23.531   9.083  38.541  1.00 13.76           C  
ANISOU  485  CG  LEU A  61     2309   1313   1604   -278    170   -249       C  
ATOM    486  CD1 LEU A  61     -22.680   8.309  37.541  1.00 15.58           C  
ANISOU  486  CD1 LEU A  61     2830   1316   1773   -216    277   -351       C  
ATOM    487  CD2 LEU A  61     -24.335  10.161  37.831  1.00 16.24           C  
ANISOU  487  CD2 LEU A  61     2800   1578   1792      0     62   -274       C  
ATOM    488  C   LEU A  61     -26.305   7.725  40.929  1.00 13.90           C  
ANISOU  488  C   LEU A  61     1934   1729   1617    -18    365   -657       C  
ATOM    489  O   LEU A  61     -25.956   6.692  41.511  1.00 13.95           O  
ANISOU  489  O   LEU A  61     2039   1957   1301   -358    227   -283       O  
ATOM    490  N   GLY A  62     -27.585   8.064  40.703  1.00 14.59           N  
ANISOU  490  N   GLY A  62     1989   1449   2103   -106    338   -705       N  
ATOM    491  CA  GLY A  62     -28.651   7.140  41.023  1.00 14.99           C  
ANISOU  491  CA  GLY A  62     1702   1741   2250    -42    589   -840       C  
ATOM    492  C   GLY A  62     -28.690   5.967  40.051  1.00 14.44           C  
ANISOU  492  C   GLY A  62     1767   1573   2144   -175    442   -708       C  
ATOM    493  O   GLY A  62     -28.082   5.988  38.983  1.00 14.72           O  
ANISOU  493  O   GLY A  62     1831   1859   1900     52    246   -700       O  
ATOM    494  N   ASN A  63     -29.407   4.917  40.452  1.00 13.50           N  
ANISOU  494  N   ASN A  63     1999   1573   1557    -99    537   -526       N  
ATOM    495  CA  ASN A  63     -29.758   3.858  39.513  1.00 12.14           C  
ANISOU  495  CA  ASN A  63     1905   1414   1292     10    422   -352       C  
ATOM    496  CB  ASN A  63     -30.767   4.395  38.497  1.00 13.82           C  
ANISOU  496  CB  ASN A  63     1880   1805   1565     42    324   -430       C  
ATOM    497  CG  ASN A  63     -32.033   4.849  39.174  1.00 15.66           C  
ANISOU  497  CG  ASN A  63     1946   2237   1766    175    317   -660       C  
ATOM    498  OD1 ASN A  63     -32.311   6.054  39.251  1.00 23.04           O  
ANISOU  498  OD1 ASN A  63     2947   2682   3122    715   -362   -936       O  
ATOM    499  ND2 ASN A  63     -32.724   3.889  39.741  1.00 16.23           N  
ANISOU  499  ND2 ASN A  63     1476   3030   1658    -93    413   -414       N  
ATOM    500  C   ASN A  63     -28.488   3.203  38.957  1.00 12.20           C  
ANISOU  500  C   ASN A  63     1840   1530   1265     15    318   -261       C  
ATOM    501  O   ASN A  63     -27.561   2.906  39.702  1.00 12.73           O  
ANISOU  501  O   ASN A  63     1980   1592   1263    146    280   -203       O  
ATOM    502  N   LEU A  64     -28.490   2.873  37.654  1.00 11.75           N  
ANISOU  502  N   LEU A  64     1834   1378   1251    129    268   -239       N  
ATOM    503  CA  LEU A  64     -27.397   2.112  37.067  1.00 11.43           C  
ANISOU  503  CA  LEU A  64     1773   1261   1308    109    274    -78       C  
ATOM    504  CB  LEU A  64     -27.956   1.083  36.099  1.00 12.32           C  
ANISOU  504  CB  LEU A  64     2046   1110   1524     67    296   -119       C  
ATOM    505  CG  LEU A  64     -28.934   0.067  36.693  1.00 13.13           C  
ANISOU  505  CG  LEU A  64     1971   1414   1601   -150    420   -336       C  
ATOM    506  CD1 LEU A  64     -29.340  -0.967  35.653  1.00 14.44           C  
ANISOU  506  CD1 LEU A  64     2301   1328   1857   -163    296   -408       C  
ATOM    507  CD2 LEU A  64     -28.387  -0.606  37.940  1.00 14.11           C  
ANISOU  507  CD2 LEU A  64     2314   1363   1681   -220    309   -328       C  
ATOM    508  C   LEU A  64     -26.405   3.029  36.350  1.00 11.74           C  
ANISOU  508  C   LEU A  64     1914   1206   1340     90    419   -163       C  
ATOM    509  O   LEU A  64     -26.787   3.954  35.640  1.00 12.11           O  
ANISOU  509  O   LEU A  64     1890   1380   1331    -12    358    -75       O  
ATOM    510  N   THR A  65     -25.126   2.714  36.535  1.00 11.97           N  
ANISOU  510  N   THR A  65     1920   1222   1406    -28    466     19       N  
ATOM    511  CA  THR A  65     -24.004   3.435  35.936  1.00 10.68           C  
ANISOU  511  CA  THR A  65     1605    989   1463    106    438    -90       C  
ATOM    512  CB  THR A  65     -23.147   4.115  37.013  1.00 12.01           C  
ANISOU  512  CB  THR A  65     1842   1106   1612    115    439   -165       C  
ATOM    513  OG1 THR A  65     -23.935   5.115  37.662  1.00 13.74           O  
ANISOU  513  OG1 THR A  65     2077   1417   1727    251    489   -359       O  
ATOM    514  CG2 THR A  65     -21.863   4.705  36.451  1.00 13.32           C  
ANISOU  514  CG2 THR A  65     1964   1466   1631   -114    350   -150       C  
ATOM    515  C   THR A  65     -23.189   2.447  35.089  1.00 11.66           C  
ANISOU  515  C   THR A  65     1930   1078   1422    111    479   -175       C  
ATOM    516  O   THR A  65     -22.875   1.338  35.511  1.00 12.91           O  
ANISOU  516  O   THR A  65     2326   1114   1461    110    526    -64       O  
ATOM    517  N   GLY A  66     -22.803   2.881  33.893  1.00 10.47           N  
ANISOU  517  N   GLY A  66     1633    917   1426     61    332    -66       N  
ATOM    518  CA  GLY A  66     -22.034   2.049  32.998  1.00 10.75           C  
ANISOU  518  CA  GLY A  66     1728   1073   1283    165    243   -145       C  
ATOM    519  C   GLY A  66     -20.771   1.500  33.643  1.00 10.50           C  
ANISOU  519  C   GLY A  66     1720   1048   1219    141    266   -154       C  
ATOM    520  O   GLY A  66     -20.045   2.190  34.359  1.00 11.24           O  
ANISOU  520  O   GLY A  66     1571   1288   1409     40    205   -291       O  
ATOM    521  N   GLY A  67     -20.469   0.235  33.331  1.00 10.61           N  
ANISOU  521  N   GLY A  67     1689   1140   1202    173    197   -373       N  
ATOM    522  CA  GLY A  67     -19.359  -0.446  33.961  1.00 10.56           C  
ANISOU  522  CA  GLY A  67     1675   1044   1291    136    131   -227       C  
ATOM    523  C   GLY A  67     -17.999  -0.096  33.383  1.00 10.53           C  
ANISOU  523  C   GLY A  67     1637   1094   1267     88     25    -94       C  
ATOM    524  O   GLY A  67     -16.982  -0.410  34.013  1.00 11.44           O  
ANISOU  524  O   GLY A  67     1638   1387   1320     21    -25      4       O  
ATOM    525  N   ALA A  68     -17.946   0.556  32.219  1.00 10.67           N  
ANISOU  525  N   ALA A  68     1498   1215   1338     18      4      1       N  
ATOM    526  CA  ALA A  68     -16.689   0.925  31.555  1.00 10.74           C  
ANISOU  526  CA  ALA A  68     1612   1242   1226    -26     91   -147       C  
ATOM    527  CB  ALA A  68     -16.426   0.073  30.335  1.00 11.11           C  
ANISOU  527  CB  ALA A  68     1526   1234   1459    -77    150   -306       C  
ATOM    528  C   ALA A  68     -16.681   2.416  31.259  1.00 11.12           C  
ANISOU  528  C   ALA A  68     1815   1242   1165   -174    178    -95       C  
ATOM    529  O   ALA A  68     -16.737   2.842  30.103  1.00 11.08           O  
ANISOU  529  O   ALA A  68     1739   1389   1081   -129    202   -135       O  
ATOM    530  N   PRO A  69     -16.574   3.271  32.299  1.00 10.85           N  
ANISOU  530  N   PRO A  69     1772   1104   1246   -109    202   -112       N  
ATOM    531  CA  PRO A  69     -16.513   4.716  32.073  1.00 11.05           C  
ANISOU  531  CA  PRO A  69     1797   1071   1328   -110    201   -242       C  
ATOM    532  CB  PRO A  69     -16.448   5.300  33.480  1.00 11.65           C  
ANISOU  532  CB  PRO A  69     1966   1060   1398   -136    147   -322       C  
ATOM    533  CG  PRO A  69     -15.891   4.191  34.325  1.00 12.45           C  
ANISOU  533  CG  PRO A  69     2062   1229   1440   -239     89   -129       C  
ATOM    534  CD  PRO A  69     -16.447   2.916  33.718  1.00 11.65           C  
ANISOU  534  CD  PRO A  69     2047   1013   1365   -102    214    -76       C  
ATOM    535  C   PRO A  69     -15.274   5.109  31.261  1.00 11.08           C  
ANISOU  535  C   PRO A  69     1663   1161   1383    -34    110   -130       C  
ATOM    536  O   PRO A  69     -14.238   4.441  31.296  1.00 11.52           O  
ANISOU  536  O   PRO A  69     1626   1309   1440      7    313   -123       O  
ATOM    537  N   ARG A  70     -15.412   6.182  30.498  1.00 10.18           N  
ANISOU  537  N   ARG A  70     1459    937   1470    163    179   -178       N  
ATOM    538  CA  ARG A  70     -14.369   6.665  29.629  1.00 10.62           C  
ANISOU  538  CA  ARG A  70     1508   1143   1383     16    181   -205       C  
ATOM    539  CB  ARG A  70     -14.832   6.663  28.176  1.00 11.34           C  
ANISOU  539  CB  ARG A  70     1581   1315   1410     56    182   -208       C  
ATOM    540  CG  ARG A  70     -15.424   5.338  27.708  1.00 11.56           C  
ANISOU  540  CG  ARG A  70     1545   1356   1489     -4    107   -199       C  
ATOM    541  CD  ARG A  70     -15.852   5.348  26.246  1.00 12.19           C  
ANISOU  541  CD  ARG A  70     1762   1349   1519    -76     57   -227       C  
ATOM    542  NE  ARG A  70     -14.728   5.314  25.330  1.00 12.32           N  
ANISOU  542  NE  ARG A  70     1887   1193   1601    -89    126   -105       N  
ATOM    543  CZ  ARG A  70     -14.136   4.208  24.874  1.00 11.72           C  
ANISOU  543  CZ  ARG A  70     1678   1296   1479     31    103    -97       C  
ATOM    544  NH1 ARG A  70     -14.517   3.011  25.320  1.00 11.76           N  
ANISOU  544  NH1 ARG A  70     1782   1340   1343   -145    -57   -180       N  
ATOM    545  NH2 ARG A  70     -13.175   4.326  23.974  1.00 12.65           N  
ANISOU  545  NH2 ARG A  70     1680   1605   1520    -93     67   -238       N  
ATOM    546  C   ARG A  70     -13.937   8.085  30.026  1.00 10.91           C  
ANISOU  546  C   ARG A  70     1693   1174   1278     -3    252   -214       C  
ATOM    547  O   ARG A  70     -14.658   8.807  30.694  1.00 11.63           O  
ANISOU  547  O   ARG A  70     1595   1238   1584   -190    413   -315       O  
ATOM    548  N   LEU A  71     -12.732   8.456  29.583  1.00 11.04           N  
ANISOU  548  N   LEU A  71     1672   1035   1489     34    359   -214       N  
ATOM    549  CA  LEU A  71     -12.216   9.786  29.723  1.00 10.94           C  
ANISOU  549  CA  LEU A  71     1751   1079   1327     -5    392   -252       C  
ATOM    550  CB  LEU A  71     -10.877   9.784  30.474  1.00 11.18           C  
ANISOU  550  CB  LEU A  71     1717   1071   1457    -50    445   -184       C  
ATOM    551  CG  LEU A  71     -10.912   9.193  31.877  1.00 12.69           C  
ANISOU  551  CG  LEU A  71     1975   1359   1486    -25    302   -132       C  
ATOM    552  CD1 LEU A  71      -9.497   8.945  32.391  1.00 12.87           C  
ANISOU  552  CD1 LEU A  71     2017   1402   1468    -75     91   -134       C  
ATOM    553  CD2 LEU A  71     -11.666  10.087  32.819  1.00 12.85           C  
ANISOU  553  CD2 LEU A  71     1866   1570   1447    -67    252   -207       C  
ATOM    554  C   LEU A  71     -12.075  10.381  28.330  1.00 10.94           C  
ANISOU  554  C   LEU A  71     1712   1045   1396    -50    273   -177       C  
ATOM    555  O   LEU A  71     -11.431   9.789  27.463  1.00 12.17           O  
ANISOU  555  O   LEU A  71     2090   1112   1420   -110    385   -296       O  
ATOM    556  N   ARG A  72     -12.638  11.584  28.171  1.00 10.70           N  
ANISOU  556  N   ARG A  72     1766    994   1304    -22    269   -264       N  
ATOM    557  CA AARG A  72     -12.477  12.368  26.955  0.50 11.51           C  
ANISOU  557  CA AARG A  72     1870   1187   1315   -128    311   -196       C  
ATOM    558  CA BARG A  72     -12.474  12.366  26.958  0.50 11.40           C  
ANISOU  558  CA BARG A  72     1866   1143   1323    -82    304   -207       C  
ATOM    559  CB AARG A  72     -13.816  12.930  26.465  0.50 12.77           C  
ANISOU  559  CB AARG A  72     1829   1529   1493   -163    272   -105       C  
ATOM    560  CB BARG A  72     -13.823  12.908  26.482  0.50 12.82           C  
ANISOU  560  CB BARG A  72     1869   1459   1543    -29    268   -155       C  
ATOM    561  CG AARG A  72     -13.710  13.784  25.202  0.50 14.52           C  
ANISOU  561  CG AARG A  72     1969   2003   1545   -230    295     71       C  
ATOM    562  CG BARG A  72     -13.766  13.765  25.224  0.50 14.48           C  
ANISOU  562  CG BARG A  72     2036   1856   1607     32    289     -2       C  
ATOM    563  CD AARG A  72     -14.789  14.853  25.104  0.50 17.05           C  
ANISOU  563  CD AARG A  72     2251   2250   1975   -110     41    165       C  
ATOM    564  CD BARG A  72     -15.180  14.258  24.918  0.50 17.31           C  
ANISOU  564  CD BARG A  72     2306   2223   2046    260     61     85       C  
ATOM    565  NE AARG A  72     -14.885  15.592  23.849  0.50 19.64           N  
ANISOU  565  NE AARG A  72     2700   2729   2031     32    139    360       N  
ATOM    566  NE BARG A  72     -15.532  15.379  25.811  0.50 19.19           N  
ANISOU  566  NE BARG A  72     2651   2399   2241    352    -54   -102       N  
ATOM    567  CZ AARG A  72     -14.369  16.796  23.643  0.50 19.32           C  
ANISOU  567  CZ AARG A  72     2566   2643   2129    255   -103    345       C  
ATOM    568  CZ BARG A  72     -16.765  15.824  26.118  0.50 21.23           C  
ANISOU  568  CZ BARG A  72     2859   2709   2499    602   -213   -319       C  
ATOM    569  NH1AARG A  72     -13.729  17.407  24.618  0.50 22.23           N  
ANISOU  569  NH1AARG A  72     2708   2884   2852    137    -75   -260       N  
ATOM    570  NH1BARG A  72     -17.885  15.255  25.663  0.50 21.71           N  
ANISOU  570  NH1BARG A  72     4076   2043   2129    607  -1256   -540       N  
ATOM    571  NH2AARG A  72     -14.485  17.395  22.472  0.50 22.76           N  
ANISOU  571  NH2AARG A  72     2961   3191   2494    705    552    885       N  
ATOM    572  NH2BARG A  72     -16.853  16.894  26.874  0.50 21.60           N  
ANISOU  572  NH2BARG A  72     3074   2882   2249    439   -144   -354       N  
ATOM    573  C   ARG A  72     -11.490  13.497  27.265  1.00 11.08           C  
ANISOU  573  C   ARG A  72     1875   1078   1254    -42    183   -238       C  
ATOM    574  O   ARG A  72     -11.787  14.362  28.098  1.00 12.17           O  
ANISOU  574  O   ARG A  72     2022   1051   1548     40    387   -289       O  
ATOM    575  N   VAL A  73     -10.342  13.478  26.596  1.00 11.51           N  
ANISOU  575  N   VAL A  73     2048   1043   1283   -112    234   -328       N  
ATOM    576  CA  VAL A  73      -9.329  14.526  26.742  1.00 12.46           C  
ANISOU  576  CA  VAL A  73     2081   1214   1437   -165    177   -293       C  
ATOM    577  CB  VAL A  73      -7.946  13.976  27.108  1.00 15.41           C  
ANISOU  577  CB  VAL A  73     2224   1884   1745    -71    140     27       C  
ATOM    578  CG1 VAL A  73      -7.983  13.283  28.461  1.00 15.89           C  
ANISOU  578  CG1 VAL A  73     2245   1910   1879    287    254    197       C  
ATOM    579  CG2 VAL A  73      -7.378  13.101  26.031  1.00 16.99           C  
ANISOU  579  CG2 VAL A  73     2507   1882   2064     50     83    -64       C  
ATOM    580  C   VAL A  73      -9.256  15.328  25.455  1.00 12.36           C  
ANISOU  580  C   VAL A  73     2108   1144   1444   -218    239   -306       C  
ATOM    581  O   VAL A  73      -9.434  14.784  24.358  1.00 13.84           O  
ANISOU  581  O   VAL A  73     2439   1313   1506   -494    116   -315       O  
ATOM    582  N   SER A  74      -9.025  16.628  25.619  1.00 12.04           N  
ANISOU  582  N   SER A  74     2103   1190   1279   -353    141   -325       N  
ATOM    583  CA  SER A  74      -8.752  17.483  24.483  1.00 12.41           C  
ANISOU  583  CA  SER A  74     2286   1092   1337   -360    295   -333       C  
ATOM    584  CB  SER A  74      -9.958  18.251  24.026  1.00 15.25           C  
ANISOU  584  CB  SER A  74     2258   1841   1693   -448     20   -222       C  
ATOM    585  OG  SER A  74     -10.374  19.163  25.017  1.00 18.30           O  
ANISOU  585  OG  SER A  74     2696   2428   1826    -13     91   -260       O  
ATOM    586  C   SER A  74      -7.601  18.409  24.849  1.00 12.64           C  
ANISOU  586  C   SER A  74     2369   1147   1286   -437    440   -330       C  
ATOM    587  O   SER A  74      -7.455  18.788  26.013  1.00 14.69           O  
ANISOU  587  O   SER A  74     2541   1634   1406   -597    388   -491       O  
ATOM    588  N   PHE A  75      -6.770  18.735  23.849  1.00 11.81           N  
ANISOU  588  N   PHE A  75     1979   1166   1341   -386    366   -258       N  
ATOM    589  CA  PHE A  75      -5.631  19.575  24.093  1.00 12.97           C  
ANISOU  589  CA  PHE A  75     2117   1303   1505   -452    254   -165       C  
ATOM    590  CB  PHE A  75      -4.575  18.870  24.944  1.00 13.09           C  
ANISOU  590  CB  PHE A  75     2200   1347   1423   -441    128   -165       C  
ATOM    591  CG  PHE A  75      -4.080  17.583  24.351  1.00 13.52           C  
ANISOU  591  CG  PHE A  75     2224   1586   1324   -252    111   -204       C  
ATOM    592  CD1 PHE A  75      -3.027  17.564  23.460  1.00 13.69           C  
ANISOU  592  CD1 PHE A  75     1967   1684   1549   -184     81   -268       C  
ATOM    593  CE1 PHE A  75      -2.610  16.371  22.897  1.00 13.62           C  
ANISOU  593  CE1 PHE A  75     2124   1735   1314   -116     68   -210       C  
ATOM    594  CZ  PHE A  75      -3.236  15.182  23.196  1.00 13.62           C  
ANISOU  594  CZ  PHE A  75     1923   1748   1503    -81     15   -186       C  
ATOM    595  CD2 PHE A  75      -4.712  16.387  24.646  1.00 13.62           C  
ANISOU  595  CD2 PHE A  75     2141   1587   1447   -225    232   -121       C  
ATOM    596  CE2 PHE A  75      -4.304  15.194  24.055  1.00 13.63           C  
ANISOU  596  CE2 PHE A  75     2253   1440   1483   -271    246    -98       C  
ATOM    597  C   PHE A  75      -5.039  19.982  22.751  1.00 12.59           C  
ANISOU  597  C   PHE A  75     2001   1342   1441   -397    217   -153       C  
ATOM    598  O   PHE A  75      -5.357  19.404  21.711  1.00 13.54           O  
ANISOU  598  O   PHE A  75     2000   1622   1522   -477    245   -325       O  
ATOM    599  N   THR A  76      -4.165  20.975  22.821  1.00 13.01           N  
ANISOU  599  N   THR A  76     2001   1344   1598   -439    164   -311       N  
ATOM    600  CA  THR A  76      -3.332  21.368  21.699  1.00 13.51           C  
ANISOU  600  CA  THR A  76     2032   1511   1589   -474    170   -171       C  
ATOM    601  CB  THR A  76      -3.501  22.863  21.400  1.00 15.14           C  
ANISOU  601  CB  THR A  76     2333   1498   1917   -314    230   -265       C  
ATOM    602  OG1 THR A  76      -4.868  23.125  21.073  1.00 16.12           O  
ANISOU  602  OG1 THR A  76     2473   1802   1849   -239    314   -113       O  
ATOM    603  CG2 THR A  76      -2.613  23.328  20.273  1.00 15.91           C  
ANISOU  603  CG2 THR A  76     2497   1435   2112   -319    165    102       C  
ATOM    604  C   THR A  76      -1.880  21.017  22.035  1.00 14.16           C  
ANISOU  604  C   THR A  76     2129   1638   1609   -419    261   -232       C  
ATOM    605  O   THR A  76      -1.403  21.334  23.138  1.00 14.45           O  
ANISOU  605  O   THR A  76     1839   1964   1684   -307    212   -380       O  
ATOM    606  N   ALA A  77      -1.198  20.355  21.085  1.00 12.76           N  
ANISOU  606  N   ALA A  77     1937   1346   1564   -599    229   -261       N  
ATOM    607  CA  ALA A  77       0.229  20.097  21.178  1.00 13.86           C  
ANISOU  607  CA  ALA A  77     2079   1531   1655   -536    415   -438       C  
ATOM    608  CB  ALA A  77       0.540  18.661  20.920  1.00 14.58           C  
ANISOU  608  CB  ALA A  77     2276   1458   1804   -461    598   -192       C  
ATOM    609  C   ALA A  77       0.950  20.982  20.173  1.00 13.76           C  
ANISOU  609  C   ALA A  77     1978   1708   1541   -494    306   -315       C  
ATOM    610  O   ALA A  77       0.581  21.019  19.009  1.00 14.80           O  
ANISOU  610  O   ALA A  77     2228   1755   1640   -523     72   -237       O  
ATOM    611  N   GLU A  78       1.985  21.677  20.649  1.00 13.88           N  
ANISOU  611  N   GLU A  78     2126   1675   1470   -674    379   -260       N  
ATOM    612  CA  GLU A  78       2.877  22.432  19.790  1.00 13.89           C  
ANISOU  612  CA  GLU A  78     2079   1615   1581   -620    360   -164       C  
ATOM    613  CB  GLU A  78       3.060  23.872  20.279  1.00 16.13           C  
ANISOU  613  CB  GLU A  78     2485   1597   2044   -551    568   -312       C  
ATOM    614  CG  GLU A  78       3.974  24.670  19.377  1.00 18.89           C  
ANISOU  614  CG  GLU A  78     2873   2075   2226   -705    657    -85       C  
ATOM    615  CD  GLU A  78       4.149  26.147  19.671  1.00 21.34           C  
ANISOU  615  CD  GLU A  78     3339   2129   2641   -907    713    -60       C  
ATOM    616  OE1 GLU A  78       3.730  26.610  20.739  1.00 23.40           O  
ANISOU  616  OE1 GLU A  78     3643   1948   3299   -608   1051   -470       O  
ATOM    617  OE2 GLU A  78       4.731  26.835  18.802  1.00 28.40           O  
ANISOU  617  OE2 GLU A  78     4594   2828   3366  -1508   1180    226       O  
ATOM    618  C   GLU A  78       4.208  21.703  19.749  1.00 14.59           C  
ANISOU  618  C   GLU A  78     2190   1824   1527   -552    246   -260       C  
ATOM    619  O   GLU A  78       4.829  21.502  20.811  1.00 15.60           O  
ANISOU  619  O   GLU A  78     2193   2164   1568   -370    176   -200       O  
ATOM    620  N   ILE A  79       4.603  21.287  18.545  1.00 14.50           N  
ANISOU  620  N   ILE A  79     2065   1925   1517   -520    285   -177       N  
ATOM    621  CA  ILE A  79       5.826  20.551  18.298  1.00 14.87           C  
ANISOU  621  CA  ILE A  79     1993   1820   1836   -532    261   -219       C  
ATOM    622  CB  ILE A  79       5.570  19.329  17.398  1.00 15.50           C  
ANISOU  622  CB  ILE A  79     2401   1857   1631   -584    155   -132       C  
ATOM    623  CG1 ILE A  79       4.483  18.415  17.990  1.00 15.76           C  
ANISOU  623  CG1 ILE A  79     2479   1663   1846   -627    149   -143       C  
ATOM    624  CG2 ILE A  79       6.879  18.589  17.161  1.00 15.44           C  
ANISOU  624  CG2 ILE A  79     2618   1652   1596   -415     21   -224       C  
ATOM    625  CD1 ILE A  79       4.066  17.297  17.071  1.00 17.92           C  
ANISOU  625  CD1 ILE A  79     3003   1653   2152   -596    -76   -171       C  
ATOM    626  C   ILE A  79       6.814  21.510  17.651  1.00 15.04           C  
ANISOU  626  C   ILE A  79     2140   1892   1683   -418    387    -87       C  
ATOM    627  O   ILE A  79       6.508  22.060  16.576  1.00 15.01           O  
ANISOU  627  O   ILE A  79     2144   1634   1924   -620    112     39       O  
ATOM    628  N   LYS A  80       7.964  21.700  18.306  1.00 16.54           N  
ANISOU  628  N   LYS A  80     1996   2164   2124   -584    494   -354       N  
ATOM    629  CA  LYS A  80       9.002  22.619  17.848  1.00 16.68           C  
ANISOU  629  CA  LYS A  80     2244   1904   2189   -623    541   -491       C  
ATOM    630  CB  LYS A  80       9.348  23.632  18.938  1.00 20.49           C  
ANISOU  630  CB  LYS A  80     2630   2537   2615   -715    412   -947       C  
ATOM    631  CG  LYS A  80       8.194  24.495  19.402  1.00 23.26           C  
ANISOU  631  CG  LYS A  80     2823   2795   3218   -477    327  -1064       C  
ATOM    632  CD  LYS A  80       8.560  25.327  20.604  1.00 30.68           C  
ANISOU  632  CD  LYS A  80     3866   3777   4011   -607     81  -1822       C  
ATOM    633  CE  LYS A  80       7.405  26.149  21.119  1.00 35.79           C  
ANISOU  633  CE  LYS A  80     4647   3983   4967   -387     42  -2337       C  
ATOM    634  NZ  LYS A  80       7.798  26.942  22.301  1.00 45.06           N  
ANISOU  634  NZ  LYS A  80     5748   6197   5172   -837   -917  -2599       N  
ATOM    635  C   LYS A  80      10.276  21.845  17.471  1.00 16.88           C  
ANISOU  635  C   LYS A  80     2006   2072   2335   -593    320   -558       C  
ATOM    636  O   LYS A  80      10.452  20.691  17.866  1.00 17.57           O  
ANISOU  636  O   LYS A  80     2108   2071   2494   -593    288   -393       O  
ATOM    637  N   ASN A  81      11.155  22.527  16.717  1.00 17.76           N  
ANISOU  637  N   ASN A  81     2246   1974   2527   -627    329   -417       N  
ATOM    638  CA  ASN A  81      12.482  22.057  16.282  1.00 20.18           C  
ANISOU  638  CA  ASN A  81     2430   2524   2709   -615    499   -524       C  
ATOM    639  CB  ASN A  81      13.262  21.318  17.374  1.00 19.65           C  
ANISOU  639  CB  ASN A  81     2077   2684   2702   -503    348   -660       C  
ATOM    640  CG  ASN A  81      13.483  22.140  18.626  1.00 21.75           C  
ANISOU  640  CG  ASN A  81     2689   2756   2816   -661    237   -729       C  
ATOM    641  OD1 ASN A  81      13.421  23.369  18.587  1.00 23.49           O  
ANISOU  641  OD1 ASN A  81     2591   2754   3578   -684    256  -1151       O  
ATOM    642  ND2 ASN A  81      13.747  21.462  19.735  1.00 23.42           N  
ANISOU  642  ND2 ASN A  81     2449   3641   2808   -484    163   -573       N  
ATOM    643  C   ASN A  81      12.389  21.168  15.035  1.00 18.67           C  
ANISOU  643  C   ASN A  81     2077   2428   2587   -711    527   -394       C  
ATOM    644  O   ASN A  81      13.324  20.402  14.766  1.00 20.30           O  
ANISOU  644  O   ASN A  81     2260   2469   2981   -477    514   -545       O  
ATOM    645  N   ILE A  82      11.320  21.327  14.248  1.00 18.06           N  
ANISOU  645  N   ILE A  82     2235   2314   2312   -608    501   -391       N  
ATOM    646  CA  ILE A  82      11.139  20.588  12.990  1.00 17.42           C  
ANISOU  646  CA  ILE A  82     2215   2008   2397   -682    498   -311       C  
ATOM    647  CB  ILE A  82       9.640  20.457  12.660  1.00 17.08           C  
ANISOU  647  CB  ILE A  82     2141   2084   2265   -676    440   -127       C  
ATOM    648  CG1 ILE A  82       8.855  19.809  13.801  1.00 18.51           C  
ANISOU  648  CG1 ILE A  82     2145   2484   2401   -678    517     42       C  
ATOM    649  CG2 ILE A  82       9.437  19.733  11.343  1.00 17.42           C  
ANISOU  649  CG2 ILE A  82     2472   1857   2289   -663    509   -139       C  
ATOM    650  CD1 ILE A  82       7.349  19.860  13.648  1.00 17.73           C  
ANISOU  650  CD1 ILE A  82     2100   2617   2020   -593    655    -57       C  
ATOM    651  C   ILE A  82      11.855  21.343  11.862  1.00 17.74           C  
ANISOU  651  C   ILE A  82     2138   2056   2545   -663    626   -282       C  
ATOM    652  O   ILE A  82      11.631  22.522  11.650  1.00 19.65           O  
ANISOU  652  O   ILE A  82     2517   1995   2953   -696    783   -321       O  
ATOM    653  N   LEU A  83      12.718  20.643  11.124  1.00 18.09           N  
ANISOU  653  N   LEU A  83     2214   1934   2723   -764    794   -309       N  
ATOM    654  CA  LEU A  83      13.422  21.258  10.008  1.00 19.73           C  
ANISOU  654  CA  LEU A  83     2686   2093   2717   -983    839   -238       C  
ATOM    655  CB  LEU A  83      14.192  20.196   9.212  1.00 21.86           C  
ANISOU  655  CB  LEU A  83     2825   2665   2814   -801    864   -366       C  
ATOM    656  CG  LEU A  83      15.078  20.728   8.084  1.00 23.32           C  
ANISOU  656  CG  LEU A  83     3064   2872   2922   -767    945   -187       C  
ATOM    657  CD1 LEU A  83      16.239  21.520   8.634  1.00 25.64           C  
ANISOU  657  CD1 LEU A  83     2946   3426   3370   -900    940    -75       C  
ATOM    658  CD2 LEU A  83      15.602  19.566   7.262  1.00 23.45           C  
ANISOU  658  CD2 LEU A  83     2798   3059   3052   -782   1036   -272       C  
ATOM    659  C   LEU A  83      12.422  21.996   9.108  1.00 19.64           C  
ANISOU  659  C   LEU A  83     2680   1906   2875   -889    881    -87       C  
ATOM    660  O   LEU A  83      11.376  21.467   8.778  1.00 20.38           O  
ANISOU  660  O   LEU A  83     2909   2117   2717   -872    690     42       O  
ATOM    661  N   ALA A  84      12.787  23.211   8.671  1.00 21.63           N  
ANISOU  661  N   ALA A  84     2645   2414   3158  -1068   1011    438       N  
ATOM    662  CA  ALA A  84      11.919  23.988   7.808  1.00 23.70           C  
ANISOU  662  CA  ALA A  84     3777   1925   3300   -850    979    323       C  
ATOM    663  CB  ALA A  84      12.558  25.320   7.501  1.00 24.38           C  
ANISOU  663  CB  ALA A  84     3377   2222   3663  -1010   1118    347       C  
ATOM    664  C   ALA A  84      11.625  23.192   6.527  1.00 24.89           C  
ANISOU  664  C   ALA A  84     4144   2097   3215  -1225    868    459       C  
ATOM    665  O   ALA A  84      12.467  22.431   6.075  1.00 27.25           O  
ANISOU  665  O   ALA A  84     3977   2883   3494  -1202    763    -84       O  
ATOM    666  N   ASP A  85      10.413  23.379   5.991  1.00 27.17           N  
ANISOU  666  N   ASP A  85     4323   2328   3671  -1020    734    247       N  
ATOM    667  CA AASP A  85       9.940  22.773   4.727  0.50 28.45           C  
ANISOU  667  CA AASP A  85     4467   2845   3494   -992    736    350       C  
ATOM    668  CA BASP A  85       9.939  22.774   4.730  0.50 27.78           C  
ANISOU  668  CA BASP A  85     4336   2808   3409   -868    782    422       C  
ATOM    669  CB AASP A  85      10.889  23.043   3.550  0.50 30.58           C  
ANISOU  669  CB AASP A  85     4672   3409   3538   -771    828    505       C  
ATOM    670  CB BASP A  85      10.889  23.058   3.559  0.50 28.98           C  
ANISOU  670  CB BASP A  85     4387   3221   3403   -509    796    716       C  
ATOM    671  CG AASP A  85      10.251  22.789   2.190  0.50 34.26           C  
ANISOU  671  CG AASP A  85     4955   4207   3854   -603    624    463       C  
ATOM    672  CG BASP A  85      11.154  24.536   3.331  0.50 30.70           C  
ANISOU  672  CG BASP A  85     4614   3200   3848   -181    914    939       C  
ATOM    673  OD1AASP A  85       9.130  23.289   1.971  0.50 35.82           O  
ANISOU  673  OD1AASP A  85     5083   4537   3990   -628    101    685       O  
ATOM    674  OD1BASP A  85      10.215  25.334   3.512  0.50 35.23           O  
ANISOU  674  OD1BASP A  85     4596   4567   4220    552    886   1246       O  
ATOM    675  OD2AASP A  85      10.866  22.074   1.363  0.50 40.66           O  
ANISOU  675  OD2AASP A  85     6297   5007   4142   -155    459     -1       O  
ATOM    676  OD2BASP A  85      12.304  24.877   2.986  0.50 34.55           O  
ANISOU  676  OD2BASP A  85     4618   3870   4638   -316    895   1051       O  
ATOM    677  C   ASP A  85       9.718  21.265   4.904  1.00 26.37           C  
ANISOU  677  C   ASP A  85     4648   2774   2594  -1012    931    228       C  
ATOM    678  O   ASP A  85       9.738  20.527   3.936  1.00 30.04           O  
ANISOU  678  O   ASP A  85     5620   2991   2800  -1364    910      3       O  
ATOM    679  N   SER A  86       9.477  20.811   6.144  1.00 22.90           N  
ANISOU  679  N   SER A  86     4078   2057   2563   -945    663    266       N  
ATOM    680  CA  SER A  86       9.148  19.401   6.388  1.00 21.47           C  
ANISOU  680  CA  SER A  86     3426   2023   2709  -1046    502     32       C  
ATOM    681  CB  SER A  86       9.414  18.983   7.811  1.00 20.75           C  
ANISOU  681  CB  SER A  86     3226   1846   2811   -979    432    218       C  
ATOM    682  OG  SER A  86      10.799  18.955   8.085  1.00 20.96           O  
ANISOU  682  OG  SER A  86     2929   2228   2805   -602    515    143       O  
ATOM    683  C   SER A  86       7.679  19.158   6.048  1.00 20.72           C  
ANISOU  683  C   SER A  86     3536   1936   2401   -961    100     15       C  
ATOM    684  O   SER A  86       6.800  19.840   6.586  1.00 21.48           O  
ANISOU  684  O   SER A  86     3155   2217   2787   -965    -36    -81       O  
ATOM    685  N   SER A  87       7.403  18.145   5.225  1.00 19.53           N  
ANISOU  685  N   SER A  87     3721   1750   1950   -834    153    225       N  
ATOM    686  CA  SER A  87       6.009  17.831   4.892  1.00 21.42           C  
ANISOU  686  CA  SER A  87     3628   2086   2422  -1069    147     46       C  
ATOM    687  CB  SER A  87       5.914  16.890   3.714  1.00 24.28           C  
ANISOU  687  CB  SER A  87     4238   2749   2236   -913      0   -201       C  
ATOM    688  OG  SER A  87       6.066  15.536   4.103  1.00 25.97           O  
ANISOU  688  OG  SER A  87     4554   2745   2569  -1283    472   -134       O  
ATOM    689  C   SER A  87       5.233  17.289   6.101  1.00 19.44           C  
ANISOU  689  C   SER A  87     3383   1893   2108   -619    -53    103       C  
ATOM    690  O   SER A  87       4.027  17.526   6.234  1.00 20.81           O  
ANISOU  690  O   SER A  87     3277   1868   2762   -792   -284    380       O  
ATOM    691  N   LEU A  88       5.932  16.532   6.955  1.00 16.64           N  
ANISOU  691  N   LEU A  88     2606   1648   2066   -598    189     62       N  
ATOM    692  CA  LEU A  88       5.363  15.782   8.097  1.00 15.96           C  
ANISOU  692  CA  LEU A  88     2379   1598   2084   -563    130     80       C  
ATOM    693  CB  LEU A  88       4.723  16.745   9.102  1.00 16.06           C  
ANISOU  693  CB  LEU A  88     2111   1652   2336   -480     95    -55       C  
ATOM    694  CG  LEU A  88       5.672  17.763   9.731  1.00 15.68           C  
ANISOU  694  CG  LEU A  88     1866   1706   2383   -393    108   -127       C  
ATOM    695  CD1 LEU A  88       4.898  18.688  10.676  1.00 17.66           C  
ANISOU  695  CD1 LEU A  88     2040   2012   2657   -217    212   -208       C  
ATOM    696  CD2 LEU A  88       6.816  17.049  10.466  1.00 16.59           C  
ANISOU  696  CD2 LEU A  88     1830   1751   2723   -524    -38   -163       C  
ATOM    697  C   LEU A  88       4.357  14.710   7.677  1.00 15.99           C  
ANISOU  697  C   LEU A  88     2328   1579   2166   -427     97    -92       C  
ATOM    698  O   LEU A  88       3.698  14.138   8.549  1.00 14.99           O  
ANISOU  698  O   LEU A  88     2157   1598   1941   -329     55   -222       O  
ATOM    699  N   LYS A  89       4.281  14.369   6.392  1.00 16.86           N  
ANISOU  699  N   LYS A  89     2646   1570   2188   -794   -130     89       N  
ATOM    700  CA ALYS A  89       3.262  13.426   5.947  0.50 16.88           C  
ANISOU  700  CA ALYS A  89     2763   1452   2196   -724   -280    179       C  
ATOM    701  CA BLYS A  89       3.293  13.410   5.912  0.50 16.83           C  
ANISOU  701  CA BLYS A  89     2799   1412   2183   -717   -236    118       C  
ATOM    702  CB ALYS A  89       3.260  13.274   4.426  0.50 20.22           C  
ANISOU  702  CB ALYS A  89     3482   1942   2257   -547   -305    426       C  
ATOM    703  CB BLYS A  89       3.435  13.218   4.398  0.50 20.40           C  
ANISOU  703  CB BLYS A  89     3485   1958   2307   -525   -124    163       C  
ATOM    704  CG ALYS A  89       2.226  12.294   3.879  0.50 20.79           C  
ANISOU  704  CG ALYS A  89     3184   2331   2382   -663   -354    626       C  
ATOM    705  CG BLYS A  89       2.537  12.153   3.782  0.50 21.55           C  
ANISOU  705  CG BLYS A  89     3430   2352   2406   -725   -140    148       C  
ATOM    706  CD ALYS A  89       0.777  12.616   4.225  0.50 22.31           C  
ANISOU  706  CD ALYS A  89     3133   2594   2747   -406   -390    740       C  
ATOM    707  CD BLYS A  89       2.890  11.756   2.353  0.50 23.81           C  
ANISOU  707  CD BLYS A  89     3463   2912   2671   -361    288    163       C  
ATOM    708  CE ALYS A  89      -0.234  11.803   3.427  0.50 23.62           C  
ANISOU  708  CE ALYS A  89     2800   3170   3002   -213   -597    689       C  
ATOM    709  CE BLYS A  89       2.114  10.526   1.925  0.50 24.95           C  
ANISOU  709  CE BLYS A  89     3466   3079   2932   -162    -25    -60       C  
ATOM    710  NZ ALYS A  89      -0.359  12.291   2.028  0.50 23.45           N  
ANISOU  710  NZ ALYS A  89     2387   3382   3139     25   -808    824       N  
ATOM    711  NZ BLYS A  89       2.052  10.410   0.460  0.50 26.88           N  
ANISOU  711  NZ BLYS A  89     3436   3870   2904   -103    323    267       N  
ATOM    712  C   LYS A  89       3.481  12.072   6.634  1.00 15.10           C  
ANISOU  712  C   LYS A  89     2446   1331   1958   -650    -69     63       C  
ATOM    713  O   LYS A  89       4.574  11.497   6.579  1.00 15.77           O  
ANISOU  713  O   LYS A  89     2341   2029   1619   -577    202    146       O  
ATOM    714  N   ASP A  90       2.402  11.566   7.250  1.00 13.54           N  
ANISOU  714  N   ASP A  90     2203   1120   1822   -434    -98   -232       N  
ATOM    715  CA  ASP A  90       2.419  10.240   7.872  1.00 12.99           C  
ANISOU  715  CA  ASP A  90     2040   1258   1637   -387     94   -157       C  
ATOM    716  CB  ASP A  90       2.554   9.146   6.812  1.00 13.68           C  
ANISOU  716  CB  ASP A  90     2280   1352   1564   -355    160   -200       C  
ATOM    717  CG  ASP A  90       1.391   9.093   5.825  1.00 14.44           C  
ANISOU  717  CG  ASP A  90     2187   1526   1772   -335    144   -283       C  
ATOM    718  OD1 ASP A  90       0.260   9.433   6.209  1.00 14.10           O  
ANISOU  718  OD1 ASP A  90     2131   1640   1585   -220    115     36       O  
ATOM    719  OD2 ASP A  90       1.623   8.694   4.653  1.00 18.57           O  
ANISOU  719  OD2 ASP A  90     2766   2462   1828   -266    352   -413       O  
ATOM    720  C   ASP A  90       3.473  10.120   8.978  1.00 12.10           C  
ANISOU  720  C   ASP A  90     1757   1181   1657   -253    218    -50       C  
ATOM    721  O   ASP A  90       3.989   9.019   9.236  1.00 12.33           O  
ANISOU  721  O   ASP A  90     2052   1206   1426   -212     91    -68       O  
ATOM    722  N   GLN A  91       3.752  11.214   9.697  1.00 12.28           N  
ANISOU  722  N   GLN A  91     1799   1265   1601   -217    158    -79       N  
ATOM    723  CA  GLN A  91       4.835  11.196  10.688  1.00 12.73           C  
ANISOU  723  CA  GLN A  91     1844   1479   1510   -298    121    -88       C  
ATOM    724  CB  GLN A  91       5.978  12.094  10.231  1.00 12.91           C  
ANISOU  724  CB  GLN A  91     1707   1634   1563   -246    267   -155       C  
ATOM    725  CG  GLN A  91       6.764  11.468   9.092  1.00 13.09           C  
ANISOU  725  CG  GLN A  91     1876   1341   1757   -200    412   -163       C  
ATOM    726  CD  GLN A  91       7.813  12.365   8.489  1.00 14.21           C  
ANISOU  726  CD  GLN A  91     1984   1672   1743   -196    448     49       C  
ATOM    727  OE1 GLN A  91       7.545  13.532   8.220  1.00 16.35           O  
ANISOU  727  OE1 GLN A  91     2479   1641   2092   -191    255    147       O  
ATOM    728  NE2 GLN A  91       9.000  11.813   8.266  1.00 15.27           N  
ANISOU  728  NE2 GLN A  91     2113   1699   1987    -53    311   -444       N  
ATOM    729  C   GLN A  91       4.410  11.600  12.109  1.00 13.03           C  
ANISOU  729  C   GLN A  91     1864   1484   1604   -212    197   -123       C  
ATOM    730  O   GLN A  91       5.216  11.413  13.031  1.00 13.45           O  
ANISOU  730  O   GLN A  91     2041   1610   1458   -166    148   -102       O  
ATOM    731  N   ILE A  92       3.197  12.118  12.319  1.00 11.63           N  
ANISOU  731  N   ILE A  92     1727   1353   1338   -213    -43    -99       N  
ATOM    732  CA AILE A  92       2.751  12.575  13.643  0.70 13.01           C  
ANISOU  732  CA AILE A  92     1934   1479   1529   -128    180   -127       C  
ATOM    733  CA BILE A  92       2.762  12.562  13.651  0.30 12.31           C  
ANISOU  733  CA BILE A  92     1910   1334   1432   -114     97    -96       C  
ATOM    734  CB AILE A  92       2.426  14.080  13.649  0.70 14.49           C  
ANISOU  734  CB AILE A  92     2250   1470   1786   -203    179   -322       C  
ATOM    735  CB BILE A  92       2.534  14.088  13.707  0.30 12.45           C  
ANISOU  735  CB BILE A  92     2018   1321   1391   -133    108   -145       C  
ATOM    736  CG1AILE A  92       3.561  14.935  13.082  0.70 17.06           C  
ANISOU  736  CG1AILE A  92     2553   1912   2016   -400    317   -281       C  
ATOM    737  CG1BILE A  92       3.832  14.834  13.390  0.30 12.42           C  
ANISOU  737  CG1BILE A  92     2069   1319   1331   -132    108    -99       C  
ATOM    738  CG2AILE A  92       2.029  14.520  15.043  0.70 15.27           C  
ANISOU  738  CG2AILE A  92     2384   1579   1839   -265    279   -318       C  
ATOM    739  CG2BILE A  92       1.989  14.515  15.056  0.30 12.73           C  
ANISOU  739  CG2BILE A  92     2067   1345   1424   -147    144   -151       C  
ATOM    740  CD1AILE A  92       4.845  14.848  13.847  0.70 18.29           C  
ANISOU  740  CD1AILE A  92     2685   2267   1994   -381    291   -375       C  
ATOM    741  CD1BILE A  92       3.672  16.305  13.138  0.30 12.80           C  
ANISOU  741  CD1BILE A  92     2198   1321   1343    -77    206    -90       C  
ATOM    742  C   ILE A  92       1.511  11.779  14.052  1.00 12.78           C  
ANISOU  742  C   ILE A  92     1993   1351   1511   -139    187   -185       C  
ATOM    743  O   ILE A  92       0.587  11.587  13.274  1.00 13.33           O  
ANISOU  743  O   ILE A  92     1913   1576   1575   -244    196    -27       O  
ATOM    744  N   GLY A  93       1.467  11.382  15.320  1.00 12.04           N  
ANISOU  744  N   GLY A  93     1693   1364   1518   -254     62    -79       N  
ATOM    745  CA  GLY A  93       0.260  10.819  15.878  1.00 11.96           C  
ANISOU  745  CA  GLY A  93     1692   1500   1352   -318     75   -240       C  
ATOM    746  C   GLY A  93       0.358  10.720  17.366  1.00 11.53           C  
ANISOU  746  C   GLY A  93     1599   1416   1366   -271    170   -213       C  
ATOM    747  O   GLY A  93       1.053  11.523  18.002  1.00 11.53           O  
ANISOU  747  O   GLY A  93     1676   1238   1466   -230    100   -231       O  
ATOM    748  N   LEU A  94      -0.343   9.737  17.912  1.00 11.14           N  
ANISOU  748  N   LEU A  94     1635   1169   1427   -249    131   -265       N  
ATOM    749  CA  LEU A  94      -0.325   9.503  19.364  1.00 11.26           C  
ANISOU  749  CA  LEU A  94     1705   1140   1433    -13    208   -286       C  
ATOM    750  CB  LEU A  94      -1.744   9.611  19.935  1.00 11.58           C  
ANISOU  750  CB  LEU A  94     1716   1249   1432     58    188   -273       C  
ATOM    751  CG  LEU A  94      -2.436  10.953  19.752  1.00 11.93           C  
ANISOU  751  CG  LEU A  94     1785   1240   1507     23    207   -131       C  
ATOM    752  CD1 LEU A  94      -3.848  10.890  20.285  1.00 12.64           C  
ANISOU  752  CD1 LEU A  94     1853   1344   1602    230    318    -62       C  
ATOM    753  CD2 LEU A  94      -1.676  12.093  20.407  1.00 12.27           C  
ANISOU  753  CD2 LEU A  94     1895   1249   1517     47     83   -120       C  
ATOM    754  C   LEU A  94       0.283   8.124  19.646  1.00 10.55           C  
ANISOU  754  C   LEU A  94     1645   1011   1352    -87    146   -268       C  
ATOM    755  O   LEU A  94       0.226   7.191  18.820  1.00 11.39           O  
ANISOU  755  O   LEU A  94     1858    958   1509   -150     59   -309       O  
ATOM    756  N   LYS A  95       0.858   7.997  20.834  1.00 10.95           N  
ANISOU  756  N   LYS A  95     1463   1226   1469   -189     67   -348       N  
ATOM    757  CA  LYS A  95       1.314   6.696  21.341  1.00 11.43           C  
ANISOU  757  CA  LYS A  95     1633   1272   1438   -166    113   -276       C  
ATOM    758  CB  LYS A  95       2.217   6.922  22.563  1.00 11.28           C  
ANISOU  758  CB  LYS A  95     1664   1146   1473   -224     51   -251       C  
ATOM    759  CG  LYS A  95       3.523   7.620  22.229  1.00 12.31           C  
ANISOU  759  CG  LYS A  95     1768   1483   1425   -412     32   -253       C  
ATOM    760  CD  LYS A  95       4.492   7.698  23.387  1.00 13.33           C  
ANISOU  760  CD  LYS A  95     1931   1660   1474   -386    -52    -96       C  
ATOM    761  CE  LYS A  95       5.816   8.301  22.978  1.00 13.36           C  
ANISOU  761  CE  LYS A  95     1874   1585   1617   -361     15   -292       C  
ATOM    762  NZ  LYS A  95       6.785   8.253  24.080  1.00 14.16           N  
ANISOU  762  NZ  LYS A  95     1962   1806   1612   -380     34   -339       N  
ATOM    763  C   LYS A  95       0.107   5.809  21.652  1.00 11.65           C  
ANISOU  763  C   LYS A  95     1637   1342   1446   -114    115   -165       C  
ATOM    764  O   LYS A  95      -1.013   6.263  21.728  1.00 12.71           O  
ANISOU  764  O   LYS A  95     1736   1172   1921     19    224   -105       O  
ATOM    765  N   SER A  96       0.372   4.514  21.818  1.00 11.08           N  
ANISOU  765  N   SER A  96     1581   1276   1350   -163     56   -250       N  
ATOM    766  CA ASER A  96      -0.683   3.536  22.090  0.60 11.16           C  
ANISOU  766  CA ASER A  96     1684   1253   1303   -138    156   -170       C  
ATOM    767  CA BSER A  96      -0.695   3.547  22.084  0.40 11.81           C  
ANISOU  767  CA BSER A  96     1744   1356   1387   -192    182   -199       C  
ATOM    768  CB ASER A  96      -0.112   2.129  22.078  0.60 10.46           C  
ANISOU  768  CB ASER A  96     1675   1193   1104   -162    151   -191       C  
ATOM    769  CB BSER A  96      -0.173   2.131  22.020  0.40 13.42           C  
ANISOU  769  CB BSER A  96     2052   1335   1709   -178    121   -221       C  
ATOM    770  OG ASER A  96       0.658   1.871  20.902  0.60  9.59           O  
ANISOU  770  OG ASER A  96     1388   1110   1145     27    124   -141       O  
ATOM    771  OG BSER A  96       0.598   1.809  23.149  0.40 15.76           O  
ANISOU  771  OG BSER A  96     2214   1797   1975     63     18   -199       O  
ATOM    772  C   SER A  96      -1.332   3.846  23.447  1.00 10.74           C  
ANISOU  772  C   SER A  96     1572   1200   1307   -117     97   -153       C  
ATOM    773  O   SER A  96      -0.628   4.033  24.434  1.00 12.18           O  
ANISOU  773  O   SER A  96     1666   1576   1386   -133      4   -329       O  
ATOM    774  N   PHE A  97      -2.666   3.845  23.492  1.00 10.49           N  
ANISOU  774  N   PHE A  97     1554   1334   1094    -82     64   -115       N  
ATOM    775  CA  PHE A  97      -3.415   4.046  24.747  1.00  9.96           C  
ANISOU  775  CA  PHE A  97     1515   1196   1072      1     57    -42       C  
ATOM    776  CB  PHE A  97      -3.331   2.812  25.660  1.00 10.34           C  
ANISOU  776  CB  PHE A  97     1639   1199   1091     23    -23     18       C  
ATOM    777  CG  PHE A  97      -3.678   1.553  24.892  1.00 10.58           C  
ANISOU  777  CG  PHE A  97     1716   1171   1131     48      0    -25       C  
ATOM    778  CD1 PHE A  97      -4.990   1.214  24.640  1.00 11.35           C  
ANISOU  778  CD1 PHE A  97     1774   1093   1443     -9     86    -53       C  
ATOM    779  CE1 PHE A  97      -5.294   0.130  23.826  1.00 11.41           C  
ANISOU  779  CE1 PHE A  97     1668   1052   1612     51   -102    -46       C  
ATOM    780  CZ  PHE A  97      -4.295  -0.649  23.316  1.00 12.28           C  
ANISOU  780  CZ  PHE A  97     1847   1155   1664    102    -97   -180       C  
ATOM    781  CD2 PHE A  97      -2.680   0.763  24.336  1.00 10.59           C  
ANISOU  781  CD2 PHE A  97     1652   1073   1297     81    -79     66       C  
ATOM    782  CE2 PHE A  97      -2.997  -0.322  23.543  1.00 11.35           C  
ANISOU  782  CE2 PHE A  97     1773   1098   1440    141     13     19       C  
ATOM    783  C   PHE A  97      -2.931   5.315  25.452  1.00 10.64           C  
ANISOU  783  C   PHE A  97     1535   1192   1314    -59     12    -59       C  
ATOM    784  O   PHE A  97      -2.501   5.285  26.610  1.00 10.90           O  
ANISOU  784  O   PHE A  97     1590   1246   1303    108     -8    -49       O  
ATOM    785  N   PRO A  98      -3.002   6.482  24.783  1.00 10.18           N  
ANISOU  785  N   PRO A  98     1604   1144   1120    -86    -58   -142       N  
ATOM    786  CA  PRO A  98      -2.371   7.695  25.306  1.00 10.08           C  
ANISOU  786  CA  PRO A  98     1305   1223   1302   -109    -76   -158       C  
ATOM    787  CB  PRO A  98      -2.536   8.698  24.169  1.00 11.34           C  
ANISOU  787  CB  PRO A  98     1639   1255   1412    -45     28   -152       C  
ATOM    788  CG  PRO A  98      -3.756   8.224  23.436  1.00 10.81           C  
ANISOU  788  CG  PRO A  98     1792   1099   1215      1    -20   -182       C  
ATOM    789  CD  PRO A  98      -3.659   6.715  23.485  1.00 10.20           C  
ANISOU  789  CD  PRO A  98     1678   1054   1143    -68    -98   -221       C  
ATOM    790  C   PRO A  98      -3.008   8.206  26.612  1.00 10.81           C  
ANISOU  790  C   PRO A  98     1490   1212   1403    -23    -35   -195       C  
ATOM    791  O   PRO A  98      -2.317   8.834  27.408  1.00 13.05           O  
ANISOU  791  O   PRO A  98     1799   1762   1397   -262     10   -384       O  
ATOM    792  N   VAL A  99      -4.292   7.904  26.848  1.00 10.41           N  
ANISOU  792  N   VAL A  99     1493   1197   1264    -71    102   -262       N  
ATOM    793  CA  VAL A  99      -4.930   8.319  28.088  1.00 10.83           C  
ANISOU  793  CA  VAL A  99     1628   1224   1261   -134     86   -291       C  
ATOM    794  CB  VAL A  99      -6.466   8.310  27.963  1.00 10.82           C  
ANISOU  794  CB  VAL A  99     1619   1178   1313     99    128   -147       C  
ATOM    795  CG1 VAL A  99      -7.161   8.494  29.302  1.00 12.19           C  
ANISOU  795  CG1 VAL A  99     1753   1481   1397    126    154   -244       C  
ATOM    796  CG2 VAL A  99      -6.927   9.355  26.951  1.00 11.75           C  
ANISOU  796  CG2 VAL A  99     1783   1199   1481     28   -161   -142       C  
ATOM    797  C   VAL A  99      -4.399   7.482  29.252  1.00 11.11           C  
ANISOU  797  C   VAL A  99     1580   1290   1350   -160    143   -239       C  
ATOM    798  O   VAL A  99      -3.970   8.028  30.267  1.00 11.39           O  
ANISOU  798  O   VAL A  99     1779   1354   1194    -80    180   -245       O  
ATOM    799  N   ASN A 100      -4.479   6.153  29.151  1.00  9.97           N  
ANISOU  799  N   ASN A 100     1471   1189   1125   -146     26   -158       N  
ATOM    800  CA  ASN A 100      -4.034   5.325  30.279  1.00 10.58           C  
ANISOU  800  CA  ASN A 100     1521   1175   1322   -113    -49   -112       C  
ATOM    801  CB  ASN A 100      -4.528   3.893  30.122  1.00 11.23           C  
ANISOU  801  CB  ASN A 100     1627   1231   1406   -198    -69   -100       C  
ATOM    802  CG  ASN A 100      -6.014   3.781  30.375  1.00 11.22           C  
ANISOU  802  CG  ASN A 100     1673   1363   1225   -245     33   -316       C  
ATOM    803  OD1 ASN A 100      -6.429   3.775  31.545  1.00 11.66           O  
ANISOU  803  OD1 ASN A 100     1695   1509   1223   -153     64   -272       O  
ATOM    804  ND2 ASN A 100      -6.810   3.692  29.312  1.00 11.50           N  
ANISOU  804  ND2 ASN A 100     1635   1422   1313    -19    -16    -92       N  
ATOM    805  C   ASN A 100      -2.514   5.444  30.483  1.00 10.41           C  
ANISOU  805  C   ASN A 100     1568   1204   1181   -268     23   -199       C  
ATOM    806  O   ASN A 100      -2.047   5.352  31.628  1.00 11.36           O  
ANISOU  806  O   ASN A 100     1623   1537   1155    -77     -2   -174       O  
ATOM    807  N   ARG A 101      -1.744   5.649  29.401  1.00 10.67           N  
ANISOU  807  N   ARG A 101     1469   1453   1129   -167     49   -168       N  
ATOM    808  CA  ARG A 101      -0.292   5.875  29.543  1.00 11.55           C  
ANISOU  808  CA  ARG A 101     1519   1479   1390   -276     19   -237       C  
ATOM    809  CB  ARG A 101       0.379   6.131  28.187  1.00 12.48           C  
ANISOU  809  CB  ARG A 101     1731   1629   1382   -294     56   -119       C  
ATOM    810  CG  ARG A 101       0.763   4.914  27.360  1.00 13.23           C  
ANISOU  810  CG  ARG A 101     1787   1719   1519   -368   -234   -207       C  
ATOM    811  CD  ARG A 101       1.543   5.301  26.094  1.00 15.80           C  
ANISOU  811  CD  ARG A 101     1924   2138   1941   -248     76    -39       C  
ATOM    812  NE  ARG A 101       2.728   6.106  26.341  1.00 16.79           N  
ANISOU  812  NE  ARG A 101     2074   2133   2172   -104    131   -356       N  
ATOM    813  CZ  ARG A 101       3.967   5.667  26.582  1.00 20.03           C  
ANISOU  813  CZ  ARG A 101     2282   2365   2962   -139   -168     29       C  
ATOM    814  NH1 ARG A 101       4.215   4.372  26.604  1.00 19.88           N  
ANISOU  814  NH1 ARG A 101     2322   2277   2954    403    303     84       N  
ATOM    815  NH2 ARG A 101       4.956   6.551  26.755  1.00 21.82           N  
ANISOU  815  NH2 ARG A 101     2319   2461   3509   -339    -13     99       N  
ATOM    816  C   ARG A 101       0.002   7.098  30.429  1.00 12.21           C  
ANISOU  816  C   ARG A 101     1792   1465   1380   -171     88   -282       C  
ATOM    817  O   ARG A 101       1.100   7.216  30.980  1.00 13.34           O  
ANISOU  817  O   ARG A 101     1884   1508   1676     -6    -85   -239       O  
ATOM    818  N   SER A 102      -0.951   8.032  30.478  1.00 11.30           N  
ANISOU  818  N   SER A 102     1675   1284   1333   -267    -66   -216       N  
ATOM    819  CA  SER A 102      -0.797   9.326  31.166  1.00 11.64           C  
ANISOU  819  CA  SER A 102     1883   1270   1268   -271     97   -246       C  
ATOM    820  CB  SER A 102      -1.532  10.395  30.404  1.00 11.03           C  
ANISOU  820  CB  SER A 102     1660   1178   1351   -330    137   -289       C  
ATOM    821  OG  SER A 102      -0.963  10.604  29.119  1.00 11.89           O  
ANISOU  821  OG  SER A 102     1920   1334   1263   -213    143   -219       O  
ATOM    822  C   SER A 102      -1.266   9.309  32.625  1.00 11.99           C  
ANISOU  822  C   SER A 102     1912   1292   1350   -171    150   -279       C  
ATOM    823  O   SER A 102      -1.267  10.354  33.264  1.00 13.20           O  
ANISOU  823  O   SER A 102     2137   1527   1348   -376     87   -496       O  
ATOM    824  N   ILE A 103      -1.650   8.139  33.155  1.00 11.11           N  
ANISOU  824  N   ILE A 103     1834   1151   1236   -189     62   -403       N  
ATOM    825  CA  ILE A 103      -2.221   8.064  34.506  1.00 12.13           C  
ANISOU  825  CA  ILE A 103     2071   1305   1232    -84     83   -383       C  
ATOM    826  CB  ILE A 103      -3.721   7.738  34.507  1.00 12.79           C  
ANISOU  826  CB  ILE A 103     2039   1472   1348    -44     40   -294       C  
ATOM    827  CG1 ILE A 103      -4.520   8.696  33.621  1.00 13.17           C  
ANISOU  827  CG1 ILE A 103     2211   1437   1354   -127    -90   -235       C  
ATOM    828  CG2 ILE A 103      -4.247   7.707  35.929  1.00 13.26           C  
ANISOU  828  CG2 ILE A 103     2145   1535   1359   -127      0   -114       C  
ATOM    829  CD1 ILE A 103      -5.926   8.221  33.291  1.00 13.84           C  
ANISOU  829  CD1 ILE A 103     2135   1598   1525    -89     -8   -188       C  
ATOM    830  C   ILE A 103      -1.439   7.056  35.326  1.00 11.77           C  
ANISOU  830  C   ILE A 103     1944   1361   1165   -173      7   -329       C  
ATOM    831  O   ILE A 103      -1.703   5.856  35.272  1.00 12.17           O  
ANISOU  831  O   ILE A 103     1898   1330   1393   -103    256   -276       O  
ATOM    832  N   PRO A 104      -0.416   7.490  36.091  1.00 12.17           N  
ANISOU  832  N   PRO A 104     1861   1491   1272   -182      0   -289       N  
ATOM    833  CA  PRO A 104       0.354   6.522  36.855  1.00 13.17           C  
ANISOU  833  CA  PRO A 104     1907   1513   1583   -154    -60   -206       C  
ATOM    834  CB  PRO A 104       1.469   7.372  37.478  1.00 15.74           C  
ANISOU  834  CB  PRO A 104     2302   1831   1846   -304   -411   -175       C  
ATOM    835  CG  PRO A 104       1.547   8.637  36.684  1.00 17.12           C  
ANISOU  835  CG  PRO A 104     2551   1884   2067   -141   -261   -249       C  
ATOM    836  CD  PRO A 104       0.201   8.822  36.045  1.00 14.52           C  
ANISOU  836  CD  PRO A 104     2230   1561   1725   -182    -25   -358       C  
ATOM    837  C   PRO A 104      -0.426   5.826  37.972  1.00 13.39           C  
ANISOU  837  C   PRO A 104     2026   1628   1433   -140    -66   -304       C  
ATOM    838  O   PRO A 104      -0.126   4.684  38.315  1.00 13.26           O  
ANISOU  838  O   PRO A 104     2140   1515   1384    -34    -30   -265       O  
ATOM    839  N   VAL A 105      -1.360   6.547  38.579  1.00 13.04           N  
ANISOU  839  N   VAL A 105     1880   1702   1371   -277     36   -355       N  
ATOM    840  CA AVAL A 105      -2.143   5.993  39.674  0.50 12.89           C  
ANISOU  840  CA AVAL A 105     1823   1642   1429   -233     23   -303       C  
ATOM    841  CA BVAL A 105      -2.118   6.053  39.728  0.50 13.09           C  
ANISOU  841  CA BVAL A 105     1898   1644   1430   -191     73   -281       C  
ATOM    842  CB AVAL A 105      -1.467   6.203  41.047  0.50 14.29           C  
ANISOU  842  CB AVAL A 105     1793   2096   1538   -264    -81   -236       C  
ATOM    843  CB BVAL A 105      -1.492   6.553  41.051  0.50 14.54           C  
ANISOU  843  CB BVAL A 105     2038   1990   1495   -304     -1   -270       C  
ATOM    844  CG1AVAL A 105      -1.207   7.666  41.372  0.50 15.36           C  
ANISOU  844  CG1AVAL A 105     2010   2217   1606   -230   -183   -388       C  
ATOM    845  CG1BVAL A 105      -2.174   5.933  42.266  0.50 15.30           C  
ANISOU  845  CG1BVAL A 105     2181   2302   1329   -335    -96   -270       C  
ATOM    846  CG2AVAL A 105      -2.268   5.535  42.159  0.50 14.56           C  
ANISOU  846  CG2AVAL A 105     1855   2150   1524   -433   -107   -309       C  
ATOM    847  CG2BVAL A 105       0.023   6.403  41.147  0.50 15.21           C  
ANISOU  847  CG2BVAL A 105     2114   2229   1433   -228    127   -272       C  
ATOM    848  C   VAL A 105      -3.545   6.593  39.606  1.00 12.26           C  
ANISOU  848  C   VAL A 105     1818   1532   1307   -214     22   -426       C  
ATOM    849  O   VAL A 105      -3.735   7.771  39.232  1.00 14.35           O  
ANISOU  849  O   VAL A 105     2138   1621   1692   -112      3   -285       O  
ATOM    850  N   ALA A 106      -4.521   5.745  39.928  1.00 12.05           N  
ANISOU  850  N   ALA A 106     1828   1227   1523      4     50   -234       N  
ATOM    851  CA  ALA A 106      -5.928   6.133  40.002  1.00 12.71           C  
ANISOU  851  CA  ALA A 106     1781   1623   1422    -11    107   -310       C  
ATOM    852  CB  ALA A 106      -6.700   5.613  38.805  1.00 14.06           C  
ANISOU  852  CB  ALA A 106     1881   1934   1527    139    -22   -353       C  
ATOM    853  C   ALA A 106      -6.514   5.548  41.283  1.00 11.99           C  
ANISOU  853  C   ALA A 106     1563   1492   1501    -80    203   -336       C  
ATOM    854  O   ALA A 106      -6.184   4.416  41.673  1.00 13.32           O  
ANISOU  854  O   ALA A 106     1893   1704   1462    120    269   -262       O  
ATOM    855  N   VAL A 107      -7.398   6.320  41.911  1.00 11.58           N  
ANISOU  855  N   VAL A 107     1705   1317   1378    -41    229   -270       N  
ATOM    856  CA  VAL A 107      -8.185   5.854  43.047  1.00 11.92           C  
ANISOU  856  CA  VAL A 107     1693   1435   1400     -7    186   -172       C  
ATOM    857  CB  VAL A 107      -7.833   6.581  44.351  1.00 14.20           C  
ANISOU  857  CB  VAL A 107     2016   1790   1588    -94    233   -403       C  
ATOM    858  CG1 VAL A 107      -8.697   6.070  45.496  1.00 17.11           C  
ANISOU  858  CG1 VAL A 107     2661   2434   1404   -156    332   -422       C  
ATOM    859  CG2 VAL A 107      -6.343   6.448  44.688  1.00 16.47           C  
ANISOU  859  CG2 VAL A 107     2191   2102   1962   -129    -19   -622       C  
ATOM    860  C   VAL A 107      -9.657   6.043  42.695  1.00 12.52           C  
ANISOU  860  C   VAL A 107     1741   1567   1448    160    225   -187       C  
ATOM    861  O   VAL A 107     -10.066   7.128  42.316  1.00 14.70           O  
ANISOU  861  O   VAL A 107     2006   1506   2071     98    133     52       O  
ATOM    862  N   ILE A 108     -10.430   4.954  42.780  1.00 12.59           N  
ANISOU  862  N   ILE A 108     1850   1551   1382    173     94   -197       N  
ATOM    863  CA  ILE A 108     -11.865   5.018  42.571  1.00 13.04           C  
ANISOU  863  CA  ILE A 108     1892   1558   1504     20    217   -272       C  
ATOM    864  CB  ILE A 108     -12.324   4.069  41.447  1.00 12.99           C  
ANISOU  864  CB  ILE A 108     1959   1508   1466     60    234   -213       C  
ATOM    865  CG1 ILE A 108     -11.677   4.501  40.127  1.00 12.75           C  
ANISOU  865  CG1 ILE A 108     1834   1406   1604    -22    260    -73       C  
ATOM    866  CG2 ILE A 108     -13.850   4.032  41.369  1.00 12.38           C  
ANISOU  866  CG2 ILE A 108     2009   1326   1365     47    217   -152       C  
ATOM    867  CD1 ILE A 108     -12.028   3.650  38.936  1.00 13.21           C  
ANISOU  867  CD1 ILE A 108     1908   1403   1707     -3    285   -200       C  
ATOM    868  C   ILE A 108     -12.537   4.714  43.905  1.00 12.29           C  
ANISOU  868  C   ILE A 108     1847   1481   1342    178    187   -337       C  
ATOM    869  O   ILE A 108     -12.159   3.785  44.591  1.00 13.68           O  
ANISOU  869  O   ILE A 108     2130   1654   1412    265    190   -221       O  
ATOM    870  N   ASN A 109     -13.512   5.554  44.270  1.00 12.12           N  
ANISOU  870  N   ASN A 109     1699   1476   1427    157    204   -185       N  
ATOM    871  CA  ASN A 109     -14.302   5.421  45.480  1.00 12.21           C  
ANISOU  871  CA  ASN A 109     1916   1576   1146    134     88   -187       C  
ATOM    872  CB  ASN A 109     -14.215   6.693  46.337  1.00 13.19           C  
ANISOU  872  CB  ASN A 109     2067   1774   1170     97    212   -378       C  
ATOM    873  CG  ASN A 109     -14.981   6.648  47.636  1.00 13.07           C  
ANISOU  873  CG  ASN A 109     2084   1636   1245      9    215   -470       C  
ATOM    874  OD1 ASN A 109     -16.004   5.973  47.733  1.00 14.69           O  
ANISOU  874  OD1 ASN A 109     2293   1883   1404   -205    479   -432       O  
ATOM    875  ND2 ASN A 109     -14.507   7.413  48.615  1.00 16.73           N  
ANISOU  875  ND2 ASN A 109     2755   1859   1740     17   -239   -744       N  
ATOM    876  C   ASN A 109     -15.739   5.122  45.055  1.00 11.31           C  
ANISOU  876  C   ASN A 109     1866   1563    868     36    221   -158       C  
ATOM    877  O   ASN A 109     -16.349   5.936  44.385  1.00 12.31           O  
ANISOU  877  O   ASN A 109     1783   1404   1489    -30     -7     20       O  
ATOM    878  N   MET A 110     -16.261   3.959  45.472  1.00 11.80           N  
ANISOU  878  N   MET A 110     1815   1491   1177     58    195   -176       N  
ATOM    879  CA  MET A 110     -17.656   3.621  45.328  1.00 11.76           C  
ANISOU  879  CA  MET A 110     1763   1484   1221    157    259   -204       C  
ATOM    880  CB  MET A 110     -17.856   2.374  44.457  1.00 12.20           C  
ANISOU  880  CB  MET A 110     1826   1502   1307    143    263   -227       C  
ATOM    881  CG  MET A 110     -17.513   2.630  42.998  1.00 12.52           C  
ANISOU  881  CG  MET A 110     1945   1500   1309     33    204   -290       C  
ATOM    882  SD  MET A 110     -17.859   1.212  41.969  1.00 13.63           S  
ANISOU  882  SD  MET A 110     2207   1590   1381    -17    230   -319       S  
ATOM    883  CE  MET A 110     -17.390   1.908  40.388  1.00 14.80           C  
ANISOU  883  CE  MET A 110     2218   1957   1446    -99    201   -241       C  
ATOM    884  C   MET A 110     -18.238   3.405  46.732  1.00 12.22           C  
ANISOU  884  C   MET A 110     1893   1515   1235     24    243   -251       C  
ATOM    885  O   MET A 110     -17.832   2.485  47.434  1.00 12.10           O  
ANISOU  885  O   MET A 110     1831   1627   1138    222    139   -313       O  
ATOM    886  N   ASN A 111     -19.173   4.279  47.124  1.00 12.21           N  
ANISOU  886  N   ASN A 111     1753   1587   1296     69    308   -180       N  
ATOM    887  CA  ASN A 111     -19.871   4.190  48.421  1.00 11.77           C  
ANISOU  887  CA  ASN A 111     1749   1459   1262     37    263   -284       C  
ATOM    888  CB  ASN A 111     -20.955   3.102  48.378  1.00 11.74           C  
ANISOU  888  CB  ASN A 111     1808   1301   1350     63    387   -216       C  
ATOM    889  CG  ASN A 111     -22.103   3.467  47.467  1.00 12.08           C  
ANISOU  889  CG  ASN A 111     1745   1353   1489     -6    366   -133       C  
ATOM    890  OD1 ASN A 111     -22.190   4.626  47.042  1.00 13.18           O  
ANISOU  890  OD1 ASN A 111     2051   1326   1629     -1    390    -56       O  
ATOM    891  ND2 ASN A 111     -22.977   2.503  47.180  1.00 12.67           N  
ANISOU  891  ND2 ASN A 111     1815   1397   1602    -97    605   -214       N  
ATOM    892  C   ASN A 111     -18.875   3.960  49.569  1.00 12.82           C  
ANISOU  892  C   ASN A 111     2009   1550   1311    198    206   -211       C  
ATOM    893  O   ASN A 111     -19.158   3.187  50.502  1.00 13.80           O  
ANISOU  893  O   ASN A 111     2490   1379   1372    128    141   -179       O  
ATOM    894  N   GLY A 112     -17.755   4.688  49.532  1.00 13.10           N  
ANISOU  894  N   GLY A 112     2034   1660   1281    156    270   -357       N  
ATOM    895  CA  GLY A 112     -16.790   4.703  50.608  1.00 14.05           C  
ANISOU  895  CA  GLY A 112     2075   2010   1253    182    207   -348       C  
ATOM    896  C   GLY A 112     -15.660   3.701  50.499  1.00 14.21           C  
ANISOU  896  C   GLY A 112     2057   2079   1260    183     34   -304       C  
ATOM    897  O   GLY A 112     -14.712   3.789  51.274  1.00 18.14           O  
ANISOU  897  O   GLY A 112     2529   2779   1582    414   -333   -389       O  
ATOM    898  N   LYS A 113     -15.793   2.728  49.596  1.00 13.30           N  
ANISOU  898  N   LYS A 113     1889   1690   1475    169    190   -227       N  
ATOM    899  CA  LYS A 113     -14.743   1.758  49.336  1.00 13.28           C  
ANISOU  899  CA  LYS A 113     1906   1713   1424    247    229     71       C  
ATOM    900  CB  LYS A 113     -15.338   0.428  48.879  1.00 14.03           C  
ANISOU  900  CB  LYS A 113     2157   1714   1457    251    116    156       C  
ATOM    901  CG  LYS A 113     -14.326  -0.587  48.386  1.00 16.15           C  
ANISOU  901  CG  LYS A 113     2359   1800   1975    319    264     91       C  
ATOM    902  CD  LYS A 113     -13.407  -1.074  49.479  1.00 18.10           C  
ANISOU  902  CD  LYS A 113     2448   2312   2114    235     88     91       C  
ATOM    903  CE  LYS A 113     -12.460  -2.130  48.963  1.00 21.79           C  
ANISOU  903  CE  LYS A 113     2854   2103   3319    303     99    -14       C  
ATOM    904  NZ  LYS A 113     -11.460  -2.534  49.971  1.00 26.17           N  
ANISOU  904  NZ  LYS A 113     3093   2557   4292    311   -210    549       N  
ATOM    905  C   LYS A 113     -13.800   2.310  48.264  1.00 14.01           C  
ANISOU  905  C   LYS A 113     2061   1805   1455    141    265    -25       C  
ATOM    906  O   LYS A 113     -14.234   2.639  47.178  1.00 14.88           O  
ANISOU  906  O   LYS A 113     2168   1917   1566    268     85   -137       O  
ATOM    907  N   THR A 114     -12.507   2.360  48.585  1.00 14.16           N  
ANISOU  907  N   THR A 114     2092   1960   1325    284     84   -197       N  
ATOM    908  CA  THR A 114     -11.510   2.805  47.626  1.00 13.87           C  
ANISOU  908  CA  THR A 114     1959   1952   1357    343     60    -50       C  
ATOM    909  CB  THR A 114     -10.511   3.779  48.224  1.00 15.38           C  
ANISOU  909  CB  THR A 114     2269   2050   1523    278     72   -294       C  
ATOM    910  OG1 THR A 114      -9.741   3.086  49.205  1.00 18.89           O  
ANISOU  910  OG1 THR A 114     2609   2652   1913    319   -337   -116       O  
ATOM    911  CG2 THR A 114     -11.215   4.981  48.813  1.00 17.91           C  
ANISOU  911  CG2 THR A 114     2548   2221   2033    197    232   -636       C  
ATOM    912  C   THR A 114     -10.784   1.623  46.973  1.00 14.50           C  
ANISOU  912  C   THR A 114     2199   1965   1343    383    127   -106       C  
ATOM    913  O   THR A 114     -10.496   0.597  47.589  1.00 16.88           O  
ANISOU  913  O   THR A 114     2625   2239   1548    624    283     20       O  
ATOM    914  N   PHE A 115     -10.487   1.824  45.689  1.00 12.80           N  
ANISOU  914  N   PHE A 115     1858   1620   1385    388    189    -27       N  
ATOM    915  CA  PHE A 115      -9.735   0.909  44.860  1.00 13.31           C  
ANISOU  915  CA  PHE A 115     1818   1680   1556    280    193   -192       C  
ATOM    916  CB  PHE A 115     -10.591   0.366  43.711  1.00 12.92           C  
ANISOU  916  CB  PHE A 115     1724   1537   1645    301     97    -82       C  
ATOM    917  CG  PHE A 115     -11.911  -0.242  44.117  1.00 13.31           C  
ANISOU  917  CG  PHE A 115     1927   1596   1531    104    209    -75       C  
ATOM    918  CD1 PHE A 115     -13.044   0.529  44.247  1.00 14.43           C  
ANISOU  918  CD1 PHE A 115     2234   1419   1828    173    287   -194       C  
ATOM    919  CE1 PHE A 115     -14.264  -0.019  44.596  1.00 14.53           C  
ANISOU  919  CE1 PHE A 115     1998   1674   1848    288    412   -600       C  
ATOM    920  CZ  PHE A 115     -14.369  -1.354  44.807  1.00 16.40           C  
ANISOU  920  CZ  PHE A 115     2225   1794   2212    -48    360   -237       C  
ATOM    921  CD2 PHE A 115     -12.052  -1.606  44.272  1.00 18.06           C  
ANISOU  921  CD2 PHE A 115     2371   1768   2722    170    260     35       C  
ATOM    922  CE2 PHE A 115     -13.280  -2.154  44.593  1.00 19.40           C  
ANISOU  922  CE2 PHE A 115     2425   1966   2977    105    510   -124       C  
ATOM    923  C   PHE A 115      -8.567   1.680  44.242  1.00 12.86           C  
ANISOU  923  C   PHE A 115     1957   1511   1417    286    174    -71       C  
ATOM    924  O   PHE A 115      -8.808   2.672  43.520  1.00 13.61           O  
ANISOU  924  O   PHE A 115     2073   1531   1566    327     16    -46       O  
ATOM    925  N   THR A 116      -7.338   1.277  44.568  1.00 14.01           N  
ANISOU  925  N   THR A 116     2072   1964   1287    179    -73    -85       N  
ATOM    926  CA  THR A 116      -6.149   1.939  44.075  1.00 14.13           C  
ANISOU  926  CA  THR A 116     1963   2041   1362    341     40   -223       C  
ATOM    927  CB  THR A 116      -5.176   2.245  45.221  1.00 15.26           C  
ANISOU  927  CB  THR A 116     2054   2358   1383    175    -30   -375       C  
ATOM    928  OG1 THR A 116      -5.857   3.073  46.165  1.00 16.03           O  
ANISOU  928  OG1 THR A 116     2183   2592   1313    335   -125   -438       O  
ATOM    929  CG2 THR A 116      -3.925   2.958  44.749  1.00 16.68           C  
ANISOU  929  CG2 THR A 116     1973   2668   1695    164   -161   -312       C  
ATOM    930  C   THR A 116      -5.498   1.061  43.009  1.00 13.61           C  
ANISOU  930  C   THR A 116     2200   1674   1297    286     48   -141       C  
ATOM    931  O   THR A 116      -5.227  -0.100  43.264  1.00 16.08           O  
ANISOU  931  O   THR A 116     2705   1742   1660    466    327     41       O  
ATOM    932  N   SER A 117      -5.269   1.627  41.832  1.00 13.11           N  
ANISOU  932  N   SER A 117     2080   1708   1193    351    131   -320       N  
ATOM    933  CA  SER A 117      -4.638   0.881  40.764  1.00 12.11           C  
ANISOU  933  CA  SER A 117     1942   1608   1050    277    166   -181       C  
ATOM    934  CB  SER A 117      -5.690   0.206  39.919  1.00 15.73           C  
ANISOU  934  CB  SER A 117     2646   1932   1396     85     60   -496       C  
ATOM    935  OG  SER A 117      -6.414   1.137  39.195  1.00 17.87           O  
ANISOU  935  OG  SER A 117     2440   2599   1750    104   -204   -426       O  
ATOM    936  C   SER A 117      -3.714   1.809  39.964  1.00 12.45           C  
ANISOU  936  C   SER A 117     1845   1581   1301    113     75   -236       C  
ATOM    937  O   SER A 117      -3.604   3.004  40.249  1.00 12.98           O  
ANISOU  937  O   SER A 117     1929   1595   1407     79     -1   -275       O  
ATOM    938  N   TYR A 118      -3.022   1.223  38.994  1.00 12.43           N  
ANISOU  938  N   TYR A 118     1869   1593   1260     75     85   -268       N  
ATOM    939  CA  TYR A 118      -1.895   1.862  38.289  1.00 11.82           C  
ANISOU  939  CA  TYR A 118     1872   1483   1135     51     36   -205       C  
ATOM    940  CB  TYR A 118      -0.592   1.232  38.791  1.00 13.37           C  
ANISOU  940  CB  TYR A 118     2071   1628   1380    146     14   -126       C  
ATOM    941  CG  TYR A 118      -0.471   1.350  40.291  1.00 15.08           C  
ANISOU  941  CG  TYR A 118     2201   2128   1398    -47   -124     44       C  
ATOM    942  CD1 TYR A 118      -0.077   2.536  40.878  1.00 15.23           C  
ANISOU  942  CD1 TYR A 118     2238   2166   1381    131   -260    -36       C  
ATOM    943  CE1 TYR A 118      -0.037   2.684  42.254  1.00 16.41           C  
ANISOU  943  CE1 TYR A 118     2409   2413   1411      3   -484    -11       C  
ATOM    944  CZ  TYR A 118      -0.425   1.644  43.071  1.00 17.51           C  
ANISOU  944  CZ  TYR A 118     2567   2728   1355    109   -208    143       C  
ATOM    945  OH  TYR A 118      -0.398   1.803  44.431  1.00 22.62           O  
ANISOU  945  OH  TYR A 118     2959   4188   1447    332   -233    -93       O  
ATOM    946  CE2 TYR A 118      -0.845   0.456  42.499  1.00 18.37           C  
ANISOU  946  CE2 TYR A 118     2522   2896   1560    -94      6    212       C  
ATOM    947  CD2 TYR A 118      -0.868   0.319  41.129  1.00 17.51           C  
ANISOU  947  CD2 TYR A 118     2668   2400   1583    -79    -47    212       C  
ATOM    948  C   TYR A 118      -2.117   1.736  36.784  1.00 11.27           C  
ANISOU  948  C   TYR A 118     1543   1619   1118    149    106   -335       C  
ATOM    949  O   TYR A 118      -1.579   0.831  36.148  1.00 12.32           O  
ANISOU  949  O   TYR A 118     1698   1683   1298    266    143   -349       O  
ATOM    950  N   PRO A 119      -2.927   2.629  36.170  1.00 11.63           N  
ANISOU  950  N   PRO A 119     1874   1376   1167      5      8   -290       N  
ATOM    951  CA  PRO A 119      -3.335   2.432  34.769  1.00 11.98           C  
ANISOU  951  CA  PRO A 119     1895   1423   1233    -37      0   -200       C  
ATOM    952  CB  PRO A 119      -4.233   3.644  34.507  1.00 11.20           C  
ANISOU  952  CB  PRO A 119     1462   1477   1314   -165    -32   -268       C  
ATOM    953  CG  PRO A 119      -4.824   3.923  35.874  1.00 12.02           C  
ANISOU  953  CG  PRO A 119     1829   1452   1284   -158     61   -227       C  
ATOM    954  CD  PRO A 119      -3.676   3.711  36.839  1.00 11.56           C  
ANISOU  954  CD  PRO A 119     1734   1524   1133    -57    173   -269       C  
ATOM    955  C   PRO A 119      -2.162   2.340  33.786  1.00 12.15           C  
ANISOU  955  C   PRO A 119     1864   1444   1307    -95    -43   -157       C  
ATOM    956  O   PRO A 119      -2.197   1.515  32.894  1.00 13.19           O  
ANISOU  956  O   PRO A 119     2227   1440   1343    -92    -39   -219       O  
ATOM    957  N   ALA A 120      -1.153   3.208  33.921  1.00 11.73           N  
ANISOU  957  N   ALA A 120     1471   1565   1418     -7     -1   -230       N  
ATOM    958  CA  ALA A 120      -0.046   3.178  32.948  1.00 12.59           C  
ANISOU  958  CA  ALA A 120     1873   1529   1381     15    189   -267       C  
ATOM    959  CB  ALA A 120       0.901   4.315  33.209  1.00 14.06           C  
ANISOU  959  CB  ALA A 120     1868   1719   1755     31   -140   -327       C  
ATOM    960  C   ALA A 120       0.680   1.825  33.014  1.00 13.36           C  
ANISOU  960  C   ALA A 120     2037   1584   1454     69     47   -158       C  
ATOM    961  O   ALA A 120       1.055   1.250  31.969  1.00 14.08           O  
ANISOU  961  O   ALA A 120     2214   1616   1517    207     91   -143       O  
ATOM    962  N   GLN A 121       0.886   1.307  34.243  1.00 13.01           N  
ANISOU  962  N   GLN A 121     2015   1558   1370    384    168   -268       N  
ATOM    963  CA  GLN A 121       1.537   0.024  34.417  1.00 13.77           C  
ANISOU  963  CA  GLN A 121     2151   1696   1386    465     88   -215       C  
ATOM    964  CB  GLN A 121       1.868  -0.145  35.897  1.00 15.69           C  
ANISOU  964  CB  GLN A 121     2531   2071   1356    405    119   -179       C  
ATOM    965  CG  GLN A 121       2.498  -1.485  36.268  1.00 17.57           C  
ANISOU  965  CG  GLN A 121     2768   2156   1750    395    -48   -151       C  
ATOM    966  CD  GLN A 121       2.694  -1.560  37.762  1.00 18.04           C  
ANISOU  966  CD  GLN A 121     2572   2553   1726    435    -27     80       C  
ATOM    967  OE1 GLN A 121       1.742  -1.770  38.520  1.00 18.99           O  
ANISOU  967  OE1 GLN A 121     2760   2741   1714    340     21   -210       O  
ATOM    968  NE2 GLN A 121       3.924  -1.343  38.202  1.00 18.98           N  
ANISOU  968  NE2 GLN A 121     2426   2674   2109    314     88   -235       N  
ATOM    969  C   GLN A 121       0.652  -1.095  33.853  1.00 13.58           C  
ANISOU  969  C   GLN A 121     2373   1664   1123    512     12   -252       C  
ATOM    970  O   GLN A 121       1.144  -2.031  33.192  1.00 15.18           O  
ANISOU  970  O   GLN A 121     2701   1524   1542    538    -34   -362       O  
ATOM    971  N   LEU A 122      -0.652  -1.007  34.116  1.00 13.32           N  
ANISOU  971  N   LEU A 122     2403   1506   1149    461     28   -402       N  
ATOM    972  CA  LEU A 122      -1.619  -2.027  33.699  1.00 14.35           C  
ANISOU  972  CA  LEU A 122     2627   1534   1291    460   -390   -325       C  
ATOM    973  CB  LEU A 122      -3.017  -1.732  34.250  1.00 17.73           C  
ANISOU  973  CB  LEU A 122     2890   2142   1704     52    219   -268       C  
ATOM    974  CG  LEU A 122      -3.759  -2.915  34.875  1.00 25.48           C  
ANISOU  974  CG  LEU A 122     3700   2823   3158    -73    227     63       C  
ATOM    975  CD1 LEU A 122      -4.925  -2.423  35.730  1.00 28.00           C  
ANISOU  975  CD1 LEU A 122     4073   4403   2161   -217    417    530       C  
ATOM    976  CD2 LEU A 122      -4.200  -3.885  33.792  1.00 27.82           C  
ANISOU  976  CD2 LEU A 122     4283   3749   2536    298    378   -293       C  
ATOM    977  C   LEU A 122      -1.656  -2.093  32.170  1.00 14.10           C  
ANISOU  977  C   LEU A 122     2615   1475   1264    340   -187   -333       C  
ATOM    978  O   LEU A 122      -1.590  -3.166  31.588  1.00 14.30           O  
ANISOU  978  O   LEU A 122     2450   1584   1399    596   -312   -491       O  
ATOM    979  N   ILE A 123      -1.803  -0.944  31.515  1.00 13.12           N  
ANISOU  979  N   ILE A 123     2421   1395   1168    148   -142   -360       N  
ATOM    980  CA  ILE A 123      -2.003  -0.959  30.065  1.00 12.62           C  
ANISOU  980  CA  ILE A 123     2207   1431   1155    106   -127   -397       C  
ATOM    981  CB  ILE A 123      -2.559   0.372  29.507  1.00 13.16           C  
ANISOU  981  CB  ILE A 123     2177   1438   1385    101    -41   -294       C  
ATOM    982  CG1 ILE A 123      -3.151   0.216  28.091  1.00 13.78           C  
ANISOU  982  CG1 ILE A 123     2344   1426   1462    -34   -103   -203       C  
ATOM    983  CG2 ILE A 123      -1.515   1.481  29.536  1.00 13.58           C  
ANISOU  983  CG2 ILE A 123     2395   1385   1377    112    -58   -367       C  
ATOM    984  CD1 ILE A 123      -4.196  -0.849  27.892  1.00 14.72           C  
ANISOU  984  CD1 ILE A 123     2116   1868   1606    -59   -260   -323       C  
ATOM    985  C   ILE A 123      -0.722  -1.405  29.355  1.00 13.06           C  
ANISOU  985  C   ILE A 123     2185   1493   1283     28     46   -221       C  
ATOM    986  O   ILE A 123      -0.806  -2.022  28.288  1.00 12.91           O  
ANISOU  986  O   ILE A 123     2124   1466   1313    -18    -27   -244       O  
ATOM    987  N   LYS A 124       0.452  -1.115  29.925  1.00 13.86           N  
ANISOU  987  N   LYS A 124     2217   1677   1370    294     59   -522       N  
ATOM    988  CA  LYS A 124       1.699  -1.539  29.266  1.00 14.78           C  
ANISOU  988  CA  LYS A 124     1874   2066   1672    134    -12   -375       C  
ATOM    989  CB  LYS A 124       2.938  -1.050  30.028  1.00 17.47           C  
ANISOU  989  CB  LYS A 124     1813   2514   2310    -54    -53   -434       C  
ATOM    990  CG  LYS A 124       4.277  -1.387  29.373  1.00 19.39           C  
ANISOU  990  CG  LYS A 124     2148   2658   2560    230    226   -535       C  
ATOM    991  CD  LYS A 124       5.492  -0.714  29.994  1.00 21.06           C  
ANISOU  991  CD  LYS A 124     2102   3072   2826    150    311   -503       C  
ATOM    992  CE  LYS A 124       6.765  -0.986  29.191  1.00 24.06           C  
ANISOU  992  CE  LYS A 124     2036   3522   3582     73    524   -289       C  
ATOM    993  NZ  LYS A 124       7.987  -0.443  29.845  1.00 28.10           N  
ANISOU  993  NZ  LYS A 124     2509   4146   4022   -432    597   -659       N  
ATOM    994  C   LYS A 124       1.734  -3.062  29.129  1.00 15.24           C  
ANISOU  994  C   LYS A 124     2164   2104   1520    553     36   -261       C  
ATOM    995  O   LYS A 124       2.301  -3.560  28.150  1.00 15.46           O  
ANISOU  995  O   LYS A 124     2419   1974   1479    543    207   -114       O  
ATOM    996  N   LEU A 125       1.200  -3.778  30.125  1.00 15.56           N  
ANISOU  996  N   LEU A 125     2211   2077   1624    552    109   -233       N  
ATOM    997  CA  LEU A 125       1.099  -5.251  30.061  1.00 16.63           C  
ANISOU  997  CA  LEU A 125     2666   2029   1623    526    139     80       C  
ATOM    998  CB  LEU A 125       0.882  -5.854  31.450  1.00 21.73           C  
ANISOU  998  CB  LEU A 125     3509   3082   1663    624    370    174       C  
ATOM    999  CG  LEU A 125       2.100  -5.960  32.325  1.00 25.80           C  
ANISOU  999  CG  LEU A 125     3890   3692   2219   1131    198    335       C  
ATOM   1000  CD1 LEU A 125       1.670  -6.535  33.662  1.00 28.55           C  
ANISOU 1000  CD1 LEU A 125     4164   4420   2261   1465    368    704       C  
ATOM   1001  CD2 LEU A 125       3.155  -6.831  31.659  1.00 28.36           C  
ANISOU 1001  CD2 LEU A 125     4152   4265   2358   1488    444    492       C  
ATOM   1002  C   LEU A 125      -0.100  -5.680  29.212  1.00 15.05           C  
ANISOU 1002  C   LEU A 125     2596   1345   1774    482    189     43       C  
ATOM   1003  O   LEU A 125       0.025  -6.551  28.346  1.00 16.31           O  
ANISOU 1003  O   LEU A 125     2834   1452   1911    580    265    -54       O  
ATOM   1004  N   HIS A 126      -1.269  -5.099  29.511  1.00 13.12           N  
ANISOU 1004  N   HIS A 126     2313   1296   1373    164    112   -206       N  
ATOM   1005  CA  HIS A 126      -2.526  -5.530  28.950  1.00 13.84           C  
ANISOU 1005  CA  HIS A 126     2336   1406   1514    -69    238   -217       C  
ATOM   1006  CB  HIS A 126      -3.663  -4.692  29.548  1.00 14.67           C  
ANISOU 1006  CB  HIS A 126     2644   1403   1523     44    378   -330       C  
ATOM   1007  CG  HIS A 126      -5.025  -5.096  29.115  1.00 15.81           C  
ANISOU 1007  CG  HIS A 126     2586   1698   1722   -180    392   -281       C  
ATOM   1008  ND1 HIS A 126      -5.563  -6.311  29.485  1.00 17.51           N  
ANISOU 1008  ND1 HIS A 126     2703   1910   2038   -411    382   -273       N  
ATOM   1009  CE1 HIS A 126      -6.782  -6.423  28.980  1.00 18.18           C  
ANISOU 1009  CE1 HIS A 126     2705   2199   2003   -400    450   -457       C  
ATOM   1010  NE2 HIS A 126      -7.074  -5.291  28.323  1.00 17.27           N  
ANISOU 1010  NE2 HIS A 126     2579   1970   2009   -311    386   -738       N  
ATOM   1011  CD2 HIS A 126      -5.984  -4.457  28.390  1.00 15.36           C  
ANISOU 1011  CD2 HIS A 126     2712   1350   1774   -237    380   -395       C  
ATOM   1012  C   HIS A 126      -2.522  -5.448  27.419  1.00 13.35           C  
ANISOU 1012  C   HIS A 126     2205   1409   1456    -83    324   -468       C  
ATOM   1013  O   HIS A 126      -3.123  -6.280  26.747  1.00 14.40           O  
ANISOU 1013  O   HIS A 126     2237   1359   1874   -383    330   -412       O  
ATOM   1014  N   GLN A 127      -1.848  -4.439  26.867  1.00 12.11           N  
ANISOU 1014  N   GLN A 127     2046   1332   1220     43     46   -271       N  
ATOM   1015  CA  GLN A 127      -1.831  -4.248  25.416  1.00 12.21           C  
ANISOU 1015  CA  GLN A 127     1950   1461   1226     56     29   -301       C  
ATOM   1016  CB  GLN A 127      -1.088  -2.960  25.060  1.00 12.91           C  
ANISOU 1016  CB  GLN A 127     1967   1557   1380    -11    -48   -211       C  
ATOM   1017  CG  GLN A 127       0.425  -3.015  25.312  1.00 13.60           C  
ANISOU 1017  CG  GLN A 127     1925   1598   1644   -121    -39   -364       C  
ATOM   1018  CD  GLN A 127       1.119  -1.687  25.120  1.00 14.91           C  
ANISOU 1018  CD  GLN A 127     2173   1526   1964   -139   -270   -317       C  
ATOM   1019  OE1 GLN A 127       0.562  -0.789  24.458  1.00 15.77           O  
ANISOU 1019  OE1 GLN A 127     2341   1638   2011   -162   -129    -51       O  
ATOM   1020  NE2 GLN A 127       2.319  -1.554  25.710  1.00 15.28           N  
ANISOU 1020  NE2 GLN A 127     1914   1977   1913     11      7   -450       N  
ATOM   1021  C   GLN A 127      -1.241  -5.459  24.686  1.00 12.53           C  
ANISOU 1021  C   GLN A 127     1820   1472   1466     40    166   -248       C  
ATOM   1022  O   GLN A 127      -1.523  -5.634  23.519  1.00 13.60           O  
ANISOU 1022  O   GLN A 127     2156   1414   1596    224     16   -422       O  
ATOM   1023  N   TYR A 128      -0.415  -6.264  25.368  1.00 12.30           N  
ANISOU 1023  N   TYR A 128     1831   1409   1430     46    192   -305       N  
ATOM   1024  CA  TYR A 128       0.264  -7.390  24.719  1.00 13.34           C  
ANISOU 1024  CA  TYR A 128     2186   1398   1484    134    186   -303       C  
ATOM   1025  CB  TYR A 128       1.654  -7.618  25.299  1.00 13.25           C  
ANISOU 1025  CB  TYR A 128     2156   1359   1516    314    177   -322       C  
ATOM   1026  CG  TYR A 128       2.629  -6.527  24.956  1.00 13.42           C  
ANISOU 1026  CG  TYR A 128     2015   1741   1342    243    164    -83       C  
ATOM   1027  CD1 TYR A 128       3.087  -6.370  23.655  1.00 13.76           C  
ANISOU 1027  CD1 TYR A 128     1972   1938   1317    266    135   -190       C  
ATOM   1028  CE1 TYR A 128       3.972  -5.365  23.316  1.00 14.49           C  
ANISOU 1028  CE1 TYR A 128     2024   2057   1422    335    262      0       C  
ATOM   1029  CZ  TYR A 128       4.447  -4.509  24.292  1.00 14.79           C  
ANISOU 1029  CZ  TYR A 128     2189   1994   1434     91    265    -38       C  
ATOM   1030  OH  TYR A 128       5.334  -3.512  23.990  1.00 17.75           O  
ANISOU 1030  OH  TYR A 128     2173   2429   2141    -95     35    111       O  
ATOM   1031  CE2 TYR A 128       4.000  -4.650  25.597  1.00 14.40           C  
ANISOU 1031  CE2 TYR A 128     1959   2117   1392     47    136     28       C  
ATOM   1032  CD2 TYR A 128       3.106  -5.657  25.923  1.00 13.78           C  
ANISOU 1032  CD2 TYR A 128     2138   1700   1397    161    163    -67       C  
ATOM   1033  C   TYR A 128      -0.506  -8.702  24.794  1.00 13.99           C  
ANISOU 1033  C   TYR A 128     2343   1347   1622    228    104   -158       C  
ATOM   1034  O   TYR A 128      -0.108  -9.641  24.125  1.00 15.65           O  
ANISOU 1034  O   TYR A 128     2449   1263   2232    342    -55   -338       O  
ATOM   1035  N   ASN A 129      -1.536  -8.831  25.619  1.00 15.51           N  
ANISOU 1035  N   ASN A 129     2737   1592   1562   -129    199   -213       N  
ATOM   1036  CA  ASN A 129      -2.177 -10.157  25.576  1.00 18.01           C  
ANISOU 1036  CA  ASN A 129     2793   1665   2383   -202     61    156       C  
ATOM   1037  CB  ASN A 129      -1.593 -11.146  26.583  1.00 19.62           C  
ANISOU 1037  CB  ASN A 129     3055   2212   2186     63    -20     79       C  
ATOM   1038  CG  ASN A 129      -2.131 -10.941  27.967  1.00 20.20           C  
ANISOU 1038  CG  ASN A 129     3348   2142   2185    219     83    250       C  
ATOM   1039  OD1 ASN A 129      -2.457  -9.802  28.323  1.00 19.72           O  
ANISOU 1039  OD1 ASN A 129     3053   1869   2570    -12     51    150       O  
ATOM   1040  ND2 ASN A 129      -2.121 -12.013  28.745  1.00 18.46           N  
ANISOU 1040  ND2 ASN A 129     2929   2035   2050    -76   -222    210       N  
ATOM   1041  C   ASN A 129      -3.696 -10.107  25.649  1.00 16.97           C  
ANISOU 1041  C   ASN A 129     2726   1583   2136    -60    541    291       C  
ATOM   1042  O   ASN A 129      -4.309 -11.150  25.726  1.00 18.50           O  
ANISOU 1042  O   ASN A 129     2310   1854   2862   -310    146   -192       O  
ATOM   1043  N   ALA A 130      -4.280  -8.940  25.442  1.00 17.11           N  
ANISOU 1043  N   ALA A 130     2624   1277   2598   -121    799    -54       N  
ATOM   1044  CA  ALA A 130      -5.690  -8.775  25.278  1.00 20.65           C  
ANISOU 1044  CA  ALA A 130     2799   1664   3383   -195    393   -280       C  
ATOM   1045  CB  ALA A 130      -6.090  -7.377  25.662  1.00 18.74           C  
ANISOU 1045  CB  ALA A 130     2753   1648   2717    218     52   -154       C  
ATOM   1046  C   ALA A 130      -6.105  -9.060  23.837  1.00 19.09           C  
ANISOU 1046  C   ALA A 130     2058   1696   3497   -249    470   -496       C  
ATOM   1047  O   ALA A 130      -5.311  -9.012  22.899  1.00 22.29           O  
ANISOU 1047  O   ALA A 130     2623   2428   3418   -187    848   -883       O  
ATOM   1048  N   ASP A 131      -7.395  -9.292  23.681  1.00 21.49           N  
ANISOU 1048  N   ASP A 131     1925   1670   4568    -37    350   -489       N  
ATOM   1049  CA  ASP A 131      -8.021  -9.428  22.402  1.00 23.96           C  
ANISOU 1049  CA  ASP A 131     2759   1569   4775    -91   -114   -974       C  
ATOM   1050  CB  ASP A 131      -9.466  -9.863  22.641  1.00 30.41           C  
ANISOU 1050  CB  ASP A 131     2979   2778   5797   -666   -496   -333       C  
ATOM   1051  CG  ASP A 131     -10.267 -10.042  21.368  1.00 34.13           C  
ANISOU 1051  CG  ASP A 131     3703   2957   6307   -794  -1350   -127       C  
ATOM   1052  OD1 ASP A 131      -9.753  -9.672  20.298  1.00 34.87           O  
ANISOU 1052  OD1 ASP A 131     3684   2582   6982   -955   -356   -963       O  
ATOM   1053  OD2 ASP A 131     -11.366 -10.621  21.453  1.00 44.04           O  
ANISOU 1053  OD2 ASP A 131     4970   3577   8183  -1996  -1195    565       O  
ATOM   1054  C   ASP A 131      -7.941  -8.102  21.646  1.00 22.84           C  
ANISOU 1054  C   ASP A 131     2519   1977   4180     59     68   -928       C  
ATOM   1055  O   ASP A 131      -8.435  -7.083  22.124  1.00 22.32           O  
ANISOU 1055  O   ASP A 131     2183   1747   4549     -6   -147  -1073       O  
ATOM   1056  N   PRO A 132      -7.289  -8.023  20.472  1.00 22.73           N  
ANISOU 1056  N   PRO A 132     2506   2389   3741    130    -81  -1717       N  
ATOM   1057  CA  PRO A 132      -7.178  -6.745  19.761  1.00 26.31           C  
ANISOU 1057  CA  PRO A 132     3074   2812   4110    224    321  -1293       C  
ATOM   1058  CB  PRO A 132      -6.359  -7.100  18.503  1.00 29.40           C  
ANISOU 1058  CB  PRO A 132     3568   3281   4320    419    614  -1461       C  
ATOM   1059  CG  PRO A 132      -5.641  -8.372  18.861  1.00 31.14           C  
ANISOU 1059  CG  PRO A 132     3578   3609   4645    564    918  -1425       C  
ATOM   1060  CD  PRO A 132      -6.553  -9.108  19.810  1.00 26.31           C  
ANISOU 1060  CD  PRO A 132     3128   2373   4493    384    120  -1636       C  
ATOM   1061  C   PRO A 132      -8.519  -6.078  19.392  1.00 23.38           C  
ANISOU 1061  C   PRO A 132     3109   2338   3433   -118   -370  -1453       C  
ATOM   1062  O   PRO A 132      -8.588  -4.852  19.278  1.00 22.90           O  
ANISOU 1062  O   PRO A 132     3518   2363   2818   -461    320  -1117       O  
ATOM   1063  N   LEU A 133      -9.592  -6.869  19.250  1.00 26.80           N  
ANISOU 1063  N   LEU A 133     3782   2664   3734   -556   -314  -1655       N  
ATOM   1064  CA  LEU A 133     -10.937  -6.288  19.039  1.00 26.53           C  
ANISOU 1064  CA  LEU A 133     3560   2905   3616   -522   -634  -1130       C  
ATOM   1065  CB  LEU A 133     -11.931  -7.407  18.720  1.00 30.98           C  
ANISOU 1065  CB  LEU A 133     4275   3516   3977   -720  -1507  -1404       C  
ATOM   1066  CG  LEU A 133     -11.522  -8.293  17.547  1.00 38.69           C  
ANISOU 1066  CG  LEU A 133     5477   4956   4267   -440  -1347  -1886       C  
ATOM   1067  CD1 LEU A 133     -12.478  -9.467  17.365  1.00 45.45           C  
ANISOU 1067  CD1 LEU A 133     6195   5188   5883   -803  -1840  -1295       C  
ATOM   1068  CD2 LEU A 133     -11.424  -7.468  16.271  1.00 40.92           C  
ANISOU 1068  CD2 LEU A 133     5600   5281   4664    -31  -1325  -1202       C  
ATOM   1069  C   LEU A 133     -11.384  -5.490  20.277  1.00 21.79           C  
ANISOU 1069  C   LEU A 133     2780   2272   3227   -499   -489   -503       C  
ATOM   1070  O   LEU A 133     -11.971  -4.395  20.161  1.00 21.36           O  
ANISOU 1070  O   LEU A 133     2820   2543   2751   -263   -304   -241       O  
ATOM   1071  N   GLU A 134     -11.119  -6.020  21.473  1.00 18.74           N  
ANISOU 1071  N   GLU A 134     2456   1496   3166   -281   -164   -467       N  
ATOM   1072  CA  GLU A 134     -11.458  -5.308  22.707  1.00 17.58           C  
ANISOU 1072  CA  GLU A 134     2061   1670   2946     12    -64   -174       C  
ATOM   1073  CB  GLU A 134     -11.318  -6.176  23.975  1.00 21.25           C  
ANISOU 1073  CB  GLU A 134     2518   2012   3543   -111    -70    346       C  
ATOM   1074  CG  GLU A 134     -12.532  -6.994  24.330  1.00 28.10           C  
ANISOU 1074  CG  GLU A 134     3260   3136   4281   -582    136    205       C  
ATOM   1075  CD  GLU A 134     -13.725  -6.217  24.854  1.00 27.58           C  
ANISOU 1075  CD  GLU A 134     2738   3025   4713   -471    192    845       C  
ATOM   1076  OE1 GLU A 134     -13.569  -5.132  25.466  1.00 25.21           O  
ANISOU 1076  OE1 GLU A 134     2303   2998   4277    194    748    789       O  
ATOM   1077  OE2 GLU A 134     -14.804  -6.760  24.735  1.00 37.04           O  
ANISOU 1077  OE2 GLU A 134     3528   6075   4469  -1151   -998   -178       O  
ATOM   1078  C   GLU A 134     -10.542  -4.085  22.832  1.00 14.95           C  
ANISOU 1078  C   GLU A 134     1795   1565   2318     86    206   -116       C  
ATOM   1079  O   GLU A 134     -10.994  -3.037  23.258  1.00 14.85           O  
ANISOU 1079  O   GLU A 134     1939   1475   2228    114    381     15       O  
ATOM   1080  N   LEU A 135      -9.268  -4.205  22.453  1.00 13.23           N  
ANISOU 1080  N   LEU A 135     1865   1159   2002     49    346   -201       N  
ATOM   1081  CA  LEU A 135      -8.346  -3.063  22.583  1.00 13.24           C  
ANISOU 1081  CA  LEU A 135     1861   1221   1948     25    167   -346       C  
ATOM   1082  CB  LEU A 135      -6.921  -3.476  22.215  1.00 12.55           C  
ANISOU 1082  CB  LEU A 135     1938    978   1850     31    313   -335       C  
ATOM   1083  CG  LEU A 135      -6.223  -4.431  23.182  1.00 12.54           C  
ANISOU 1083  CG  LEU A 135     1873    999   1893     62    323   -241       C  
ATOM   1084  CD1 LEU A 135      -4.822  -4.790  22.673  1.00 14.94           C  
ANISOU 1084  CD1 LEU A 135     1956   1428   2290    267    264   -344       C  
ATOM   1085  CD2 LEU A 135      -6.155  -3.847  24.584  1.00 14.23           C  
ANISOU 1085  CD2 LEU A 135     2391   1164   1848     74    189    -69       C  
ATOM   1086  C   LEU A 135      -8.813  -1.892  21.702  1.00 12.47           C  
ANISOU 1086  C   LEU A 135     1721   1505   1509    -69      3   -390       C  
ATOM   1087  O   LEU A 135      -8.693  -0.752  22.107  1.00 12.24           O  
ANISOU 1087  O   LEU A 135     1780   1361   1508    -17    142   -246       O  
ATOM   1088  N   ALA A 136      -9.383  -2.179  20.520  1.00 11.97           N  
ANISOU 1088  N   ALA A 136     1503   1589   1455   -220     62   -454       N  
ATOM   1089  CA  ALA A 136      -9.899  -1.112  19.662  1.00 13.38           C  
ANISOU 1089  CA  ALA A 136     1827   1860   1395   -224     95   -304       C  
ATOM   1090  CB  ALA A 136     -10.176  -1.649  18.272  1.00 14.86           C  
ANISOU 1090  CB  ALA A 136     1918   2331   1394   -236   -200   -183       C  
ATOM   1091  C   ALA A 136     -11.146  -0.437  20.267  1.00 12.80           C  
ANISOU 1091  C   ALA A 136     1580   1730   1550   -178   -110   -160       C  
ATOM   1092  O   ALA A 136     -11.418   0.723  19.983  1.00 15.40           O  
ANISOU 1092  O   ALA A 136     1884   1767   2199   -195   -157     27       O  
ATOM   1093  N   LEU A 137     -11.907  -1.156  21.077  1.00 11.74           N  
ANISOU 1093  N   LEU A 137     1505   1608   1347   -108     11   -243       N  
ATOM   1094  CA  LEU A 137     -13.023  -0.532  21.808  1.00 12.45           C  
ANISOU 1094  CA  LEU A 137     1627   1596   1506    -33     94   -311       C  
ATOM   1095  CB  LEU A 137     -13.995  -1.594  22.315  1.00 15.33           C  
ANISOU 1095  CB  LEU A 137     1764   1956   2105   -319    188   -340       C  
ATOM   1096  CG  LEU A 137     -14.711  -2.396  21.238  1.00 19.43           C  
ANISOU 1096  CG  LEU A 137     2174   2521   2687   -556   -272   -352       C  
ATOM   1097  CD1 LEU A 137     -15.605  -3.453  21.884  1.00 21.05           C  
ANISOU 1097  CD1 LEU A 137     1950   2513   3534   -577   -301   -311       C  
ATOM   1098  CD2 LEU A 137     -15.494  -1.458  20.309  1.00 22.74           C  
ANISOU 1098  CD2 LEU A 137     2394   3059   3187   -584   -833   -392       C  
ATOM   1099  C   LEU A 137     -12.519   0.276  23.003  1.00 11.98           C  
ANISOU 1099  C   LEU A 137     1742   1337   1472   -210    199   -202       C  
ATOM   1100  O   LEU A 137     -13.227   1.170  23.474  1.00 13.53           O  
ANISOU 1100  O   LEU A 137     1952   1493   1696    -57    244   -198       O  
ATOM   1101  N   LEU A 138     -11.344  -0.083  23.515  1.00 11.30           N  
ANISOU 1101  N   LEU A 138     1824   1204   1266   -116    287   -254       N  
ATOM   1102  CA  LEU A 138     -10.749   0.590  24.656  1.00 11.47           C  
ANISOU 1102  CA  LEU A 138     1881   1262   1214     -6    128   -169       C  
ATOM   1103  CB  LEU A 138      -9.647  -0.318  25.233  1.00 12.42           C  
ANISOU 1103  CB  LEU A 138     1899   1426   1391    111     20   -171       C  
ATOM   1104  CG  LEU A 138      -9.194  -0.084  26.670  1.00 12.55           C  
ANISOU 1104  CG  LEU A 138     1784   1465   1519    163   -104   -338       C  
ATOM   1105  CD1 LEU A 138      -8.392  -1.293  27.125  1.00 14.44           C  
ANISOU 1105  CD1 LEU A 138     2363   1662   1461    311   -158   -129       C  
ATOM   1106  CD2 LEU A 138      -8.371   1.173  26.821  1.00 12.92           C  
ANISOU 1106  CD2 LEU A 138     1827   1637   1443      3    -74    -31       C  
ATOM   1107  C   LEU A 138     -10.211   1.964  24.243  1.00 10.56           C  
ANISOU 1107  C   LEU A 138     1655   1310   1047    -28    260   -158       C  
ATOM   1108  O   LEU A 138     -10.468   2.966  24.938  1.00 11.49           O  
ANISOU 1108  O   LEU A 138     1911   1337   1116     91    181   -170       O  
ATOM   1109  N   SER A 139      -9.458   2.029  23.136  1.00 10.78           N  
ANISOU 1109  N   SER A 139     1728   1232   1135    -46    356   -213       N  
ATOM   1110  CA  SER A 139      -8.831   3.282  22.697  1.00 11.02           C  
ANISOU 1110  CA  SER A 139     1644   1376   1164   -113    289   -247       C  
ATOM   1111  CB  SER A 139      -7.375   3.330  23.139  1.00 11.98           C  
ANISOU 1111  CB  SER A 139     1737   1543   1271   -112      8   -132       C  
ATOM   1112  OG  SER A 139      -6.706   4.516  22.702  1.00 12.95           O  
ANISOU 1112  OG  SER A 139     1765   1648   1505   -242     48    -93       O  
ATOM   1113  C   SER A 139      -8.885   3.378  21.184  1.00 10.80           C  
ANISOU 1113  C   SER A 139     1505   1464   1133     18    233   -305       C  
ATOM   1114  O   SER A 139      -8.712   2.361  20.497  1.00 10.82           O  
ANISOU 1114  O   SER A 139     1675   1455    980   -121    115   -328       O  
ATOM   1115  N   PRO A 140      -8.964   4.613  20.632  1.00 11.61           N  
ANISOU 1115  N   PRO A 140     1718   1486   1206     29    305   -161       N  
ATOM   1116  CA  PRO A 140      -8.775   4.816  19.193  1.00 11.32           C  
ANISOU 1116  CA  PRO A 140     1729   1407   1165     25    200   -187       C  
ATOM   1117  CB  PRO A 140      -9.166   6.278  18.970  1.00 11.48           C  
ANISOU 1117  CB  PRO A 140     1531   1447   1383    104    300   -177       C  
ATOM   1118  CG  PRO A 140      -8.840   6.932  20.301  1.00 12.81           C  
ANISOU 1118  CG  PRO A 140     1905   1520   1441    104    149   -133       C  
ATOM   1119  CD  PRO A 140      -9.270   5.885  21.328  1.00 12.52           C  
ANISOU 1119  CD  PRO A 140     1824   1521   1411    198    339    -94       C  
ATOM   1120  C   PRO A 140      -7.342   4.541  18.734  1.00 10.95           C  
ANISOU 1120  C   PRO A 140     1625   1487   1046   -119     77   -142       C  
ATOM   1121  O   PRO A 140      -7.092   4.357  17.547  1.00 12.89           O  
ANISOU 1121  O   PRO A 140     1722   2161   1012    218    -48   -156       O  
ATOM   1122  N   CYS A 141      -6.407   4.545  19.698  1.00 10.25           N  
ANISOU 1122  N   CYS A 141     1468   1318   1107   -116    104   -194       N  
ATOM   1123  CA  CYS A 141      -4.993   4.318  19.416  1.00 10.35           C  
ANISOU 1123  CA  CYS A 141     1466   1385   1081    -96     10   -127       C  
ATOM   1124  CB  CYS A 141      -4.169   5.446  20.000  1.00 11.42           C  
ANISOU 1124  CB  CYS A 141     1602   1282   1452   -113    -56   -127       C  
ATOM   1125  SG  CYS A 141      -4.494   7.033  19.200  1.00 14.22           S  
ANISOU 1125  SG  CYS A 141     2117   1196   2089   -182   -138      1       S  
ATOM   1126  C   CYS A 141      -4.584   2.969  20.003  1.00 11.03           C  
ANISOU 1126  C   CYS A 141     1643   1245   1301    -67     88   -240       C  
ATOM   1127  O   CYS A 141      -3.871   2.898  20.998  1.00 12.84           O  
ANISOU 1127  O   CYS A 141     2025   1354   1498   -100   -195   -147       O  
ATOM   1128  N   SER A 142      -5.018   1.903  19.327  1.00 10.68           N  
ANISOU 1128  N   SER A 142     1603   1183   1270   -215     49   -146       N  
ATOM   1129  CA  SER A 142      -4.883   0.548  19.872  1.00 11.64           C  
ANISOU 1129  CA  SER A 142     1664   1184   1576    -79    300   -143       C  
ATOM   1130  CB  SER A 142      -6.178  -0.202  19.769  1.00 13.25           C  
ANISOU 1130  CB  SER A 142     1632   1486   1915   -199    457   -337       C  
ATOM   1131  OG  SER A 142      -6.571  -0.386  18.417  1.00 15.73           O  
ANISOU 1131  OG  SER A 142     2054   1878   2043   -509    322   -682       O  
ATOM   1132  C   SER A 142      -3.746  -0.252  19.236  1.00 11.18           C  
ANISOU 1132  C   SER A 142     1675   1171   1401    -32    298    -15       C  
ATOM   1133  O   SER A 142      -3.358  -1.270  19.785  1.00 12.21           O  
ANISOU 1133  O   SER A 142     1660   1206   1772    167    315    153       O  
ATOM   1134  N   ASP A 143      -3.211   0.207  18.105  1.00  9.85           N  
ANISOU 1134  N   ASP A 143     1461   1038   1244   -105    219    -86       N  
ATOM   1135  CA  ASP A 143      -2.087  -0.481  17.446  1.00 10.45           C  
ANISOU 1135  CA  ASP A 143     1485   1177   1306    -38    141   -104       C  
ATOM   1136  CB  ASP A 143      -1.810   0.139  16.082  1.00 11.34           C  
ANISOU 1136  CB  ASP A 143     1640   1350   1317     40     50     35       C  
ATOM   1137  CG  ASP A 143      -0.604  -0.450  15.380  1.00 11.40           C  
ANISOU 1137  CG  ASP A 143     1703   1421   1205     -7    103      9       C  
ATOM   1138  OD1 ASP A 143       0.539   0.071  15.638  1.00 11.66           O  
ANISOU 1138  OD1 ASP A 143     1660   1367   1402     -1     89    -69       O  
ATOM   1139  OD2 ASP A 143      -0.791  -1.430  14.621  1.00 12.71           O  
ANISOU 1139  OD2 ASP A 143     1707   1603   1517     18     50   -239       O  
ATOM   1140  C   ASP A 143      -0.862  -0.397  18.350  1.00 10.00           C  
ANISOU 1140  C   ASP A 143     1362   1211   1226    -16    188    -47       C  
ATOM   1141  O   ASP A 143      -0.562   0.696  18.853  1.00 11.22           O  
ANISOU 1141  O   ASP A 143     1749   1190   1321    -13    106    -91       O  
ATOM   1142  N   VAL A 144      -0.169  -1.523  18.514  1.00 10.35           N  
ANISOU 1142  N   VAL A 144     1532   1194   1206    -27    107   -127       N  
ATOM   1143  CA  VAL A 144       1.014  -1.618  19.364  1.00 10.86           C  
ANISOU 1143  CA  VAL A 144     1567   1247   1311     97     18   -132       C  
ATOM   1144  CB  VAL A 144       0.856  -2.785  20.353  1.00 11.61           C  
ANISOU 1144  CB  VAL A 144     1620   1375   1416    -21     60    -11       C  
ATOM   1145  CG1 VAL A 144       2.142  -3.081  21.113  1.00 12.64           C  
ANISOU 1145  CG1 VAL A 144     1765   1585   1452    231    153    118       C  
ATOM   1146  CG2 VAL A 144      -0.294  -2.537  21.320  1.00 12.09           C  
ANISOU 1146  CG2 VAL A 144     1338   1742   1511    -28    -24    189       C  
ATOM   1147  C   VAL A 144       2.260  -1.773  18.492  1.00 10.74           C  
ANISOU 1147  C   VAL A 144     1500   1145   1434      2     -4    -93       C  
ATOM   1148  O   VAL A 144       2.304  -2.590  17.587  1.00 11.48           O  
ANISOU 1148  O   VAL A 144     1709   1295   1355     21    158   -155       O  
ATOM   1149  N   ASP A 145       3.285  -0.967  18.793  1.00 11.04           N  
ANISOU 1149  N   ASP A 145     1581   1308   1303   -102     11   -182       N  
ATOM   1150  CA  ASP A 145       4.533  -0.953  18.015  1.00 11.08           C  
ANISOU 1150  CA  ASP A 145     1573   1282   1351   -116     39    -32       C  
ATOM   1151  CB  ASP A 145       5.507   0.063  18.576  1.00 11.33           C  
ANISOU 1151  CB  ASP A 145     1635   1356   1310    -94    -50    -88       C  
ATOM   1152  CG  ASP A 145       5.048   1.510  18.477  1.00 11.59           C  
ANISOU 1152  CG  ASP A 145     1611   1395   1396    -39    100    -92       C  
ATOM   1153  OD1 ASP A 145       4.355   1.860  17.505  1.00 12.10           O  
ANISOU 1153  OD1 ASP A 145     1512   1564   1520     -8     76   -143       O  
ATOM   1154  OD2 ASP A 145       5.455   2.274  19.367  1.00 12.90           O  
ANISOU 1154  OD2 ASP A 145     1980   1261   1661      3   -108   -117       O  
ATOM   1155  C   ASP A 145       5.212  -2.313  17.980  1.00 10.99           C  
ANISOU 1155  C   ASP A 145     1596   1365   1212   -102    135   -149       C  
ATOM   1156  O   ASP A 145       5.376  -2.990  19.004  1.00 12.13           O  
ANISOU 1156  O   ASP A 145     1980   1404   1223     99    163    -52       O  
ATOM   1157  N   GLU A 146       5.660  -2.697  16.780  1.00 10.55           N  
ANISOU 1157  N   GLU A 146     1496   1259   1253     40    286    -44       N  
ATOM   1158  CA  GLU A 146       6.399  -3.955  16.619  1.00 10.62           C  
ANISOU 1158  CA  GLU A 146     1431   1161   1441    -40     41    -64       C  
ATOM   1159  CB  GLU A 146       6.035  -4.614  15.299  1.00 11.09           C  
ANISOU 1159  CB  GLU A 146     1462   1356   1395     57     59   -132       C  
ATOM   1160  CG  GLU A 146       4.553  -4.983  15.222  1.00 12.03           C  
ANISOU 1160  CG  GLU A 146     1478   1455   1636     69    -49   -275       C  
ATOM   1161  CD  GLU A 146       3.582  -3.935  14.696  1.00 12.49           C  
ANISOU 1161  CD  GLU A 146     1645   1413   1684     40    -20   -162       C  
ATOM   1162  OE1 GLU A 146       4.016  -2.793  14.390  1.00 12.85           O  
ANISOU 1162  OE1 GLU A 146     1803   1507   1570    -94     32   -108       O  
ATOM   1163  OE2 GLU A 146       2.370  -4.265  14.598  1.00 12.40           O  
ANISOU 1163  OE2 GLU A 146     1677   1544   1490    150     52   -120       O  
ATOM   1164  C   GLU A 146       7.914  -3.744  16.709  1.00 11.49           C  
ANISOU 1164  C   GLU A 146     1511   1451   1403   -145    -44   -122       C  
ATOM   1165  O   GLU A 146       8.620  -4.656  17.131  1.00 11.81           O  
ANISOU 1165  O   GLU A 146     1493   1459   1534    -47    166    -23       O  
ATOM   1166  N   TYR A 147       8.388  -2.562  16.291  1.00 11.04           N  
ANISOU 1166  N   TYR A 147     1434   1390   1370     58     77     20       N  
ATOM   1167  CA  TYR A 147       9.816  -2.257  16.183  1.00 10.90           C  
ANISOU 1167  CA  TYR A 147     1451   1176   1511   -107     75    -45       C  
ATOM   1168  CB  TYR A 147      10.249  -2.184  14.714  1.00 11.86           C  
ANISOU 1168  CB  TYR A 147     1544   1472   1489    -64     63    -77       C  
ATOM   1169  CG  TYR A 147       9.843  -3.398  13.933  1.00 11.38           C  
ANISOU 1169  CG  TYR A 147     1418   1377   1529     50    112   -106       C  
ATOM   1170  CD1 TYR A 147      10.488  -4.611  14.091  1.00 10.88           C  
ANISOU 1170  CD1 TYR A 147     1285   1388   1460     78    140   -127       C  
ATOM   1171  CE1 TYR A 147      10.046  -5.757  13.435  1.00 11.41           C  
ANISOU 1171  CE1 TYR A 147     1476   1270   1589     44    -77     -2       C  
ATOM   1172  CZ  TYR A 147       8.940  -5.696  12.612  1.00 10.29           C  
ANISOU 1172  CZ  TYR A 147     1373   1361   1173    -10    101   -192       C  
ATOM   1173  OH  TYR A 147       8.447  -6.790  11.955  1.00 11.28           O  
ANISOU 1173  OH  TYR A 147     1507   1393   1385    -68    120   -265       O  
ATOM   1174  CE2 TYR A 147       8.306  -4.484  12.424  1.00 11.53           C  
ANISOU 1174  CE2 TYR A 147     1533   1423   1425     18    -45    -88       C  
ATOM   1175  CD2 TYR A 147       8.750  -3.359  13.086  1.00 11.32           C  
ANISOU 1175  CD2 TYR A 147     1672   1277   1351     97      2     22       C  
ATOM   1176  C   TYR A 147      10.135  -0.980  16.951  1.00 12.59           C  
ANISOU 1176  C   TYR A 147     1490   1409   1882   -161    281   -314       C  
ATOM   1177  O   TYR A 147       9.235  -0.220  17.310  1.00 15.27           O  
ANISOU 1177  O   TYR A 147     1718   1805   2277    143    177   -581       O  
ATOM   1178  N   ASN A 148      11.436  -0.724  17.118  1.00 12.71           N  
ANISOU 1178  N   ASN A 148     1455   1464   1910   -129    160   -338       N  
ATOM   1179  CA  ASN A 148      11.870   0.343  18.007  1.00 12.98           C  
ANISOU 1179  CA  ASN A 148     1493   1596   1840   -176     87   -399       C  
ATOM   1180  CB  ASN A 148      13.139  -0.030  18.768  1.00 14.10           C  
ANISOU 1180  CB  ASN A 148     1737   1695   1924   -122   -107   -477       C  
ATOM   1181  CG  ASN A 148      14.395  -0.040  17.921  1.00 14.31           C  
ANISOU 1181  CG  ASN A 148     1780   1763   1891     -5    -58   -383       C  
ATOM   1182  OD1 ASN A 148      14.332  -0.102  16.685  1.00 14.01           O  
ANISOU 1182  OD1 ASN A 148     1720   1874   1729    -17    112   -473       O  
ATOM   1183  ND2 ASN A 148      15.539  -0.002  18.596  1.00 16.90           N  
ANISOU 1183  ND2 ASN A 148     1829   2442   2147    -26   -146   -450       N  
ATOM   1184  C   ASN A 148      12.014   1.692  17.290  1.00 13.26           C  
ANISOU 1184  C   ASN A 148     1546   1635   1857    -62     90   -390       C  
ATOM   1185  O   ASN A 148      12.384   2.681  17.918  1.00 14.39           O  
ANISOU 1185  O   ASN A 148     1979   1666   1822   -144    -80   -387       O  
ATOM   1186  N  ALYS A 149      11.706   1.719  15.997  0.50 12.87           N  
ANISOU 1186  N  ALYS A 149     1506   1505   1876     47     -2   -399       N  
ATOM   1187  N  BLYS A 149      11.710   1.720  15.995  0.50 12.83           N  
ANISOU 1187  N  BLYS A 149     1508   1503   1862    -14    -57   -395       N  
ATOM   1188  CA ALYS A 149      11.686   2.944  15.207  0.50 14.10           C  
ANISOU 1188  CA ALYS A 149     1662   1627   2067    -77     13   -255       C  
ATOM   1189  CA BLYS A 149      11.696   2.946  15.200  0.50 13.89           C  
ANISOU 1189  CA BLYS A 149     1690   1632   1953   -172    -90   -269       C  
ATOM   1190  CB ALYS A 149      12.951   3.088  14.360  0.50 16.08           C  
ANISOU 1190  CB ALYS A 149     1920   1703   2487     -2    295   -213       C  
ATOM   1191  CB BLYS A 149      12.968   3.096  14.359  0.50 15.36           C  
ANISOU 1191  CB BLYS A 149     1908   1714   2213   -211     65   -232       C  
ATOM   1192  CG ALYS A 149      14.246   3.168  15.133  0.50 18.12           C  
ANISOU 1192  CG ALYS A 149     1777   2124   2982    -40    360   -144       C  
ATOM   1193  CG BLYS A 149      14.260   3.143  15.141  0.50 17.39           C  
ANISOU 1193  CG BLYS A 149     1838   2167   2601   -335     58   -134       C  
ATOM   1194  CD ALYS A 149      15.330   3.769  14.283  0.50 20.84           C  
ANISOU 1194  CD ALYS A 149     1983   2343   3592   -278    479    -62       C  
ATOM   1195  CD BLYS A 149      14.345   4.328  16.068  0.50 19.05           C  
ANISOU 1195  CD BLYS A 149     2028   2262   2945   -622   -149   -243       C  
ATOM   1196  CE ALYS A 149      16.702   3.670  14.885  0.50 21.76           C  
ANISOU 1196  CE ALYS A 149     2015   2288   3963   -102    530    -67       C  
ATOM   1197  CE BLYS A 149      15.279   4.074  17.224  0.50 21.90           C  
ANISOU 1197  CE BLYS A 149     2333   2769   3216   -689   -365   -340       C  
ATOM   1198  NZ ALYS A 149      17.639   3.414  13.786  0.50 18.31           N  
ANISOU 1198  NZ ALYS A 149     1484   1180   4293   -304    770    214       N  
ATOM   1199  NZ BLYS A 149      16.670   4.308  16.803  0.50 23.92           N  
ANISOU 1199  NZ BLYS A 149     2098   3144   3843   -756   -602   -447       N  
ATOM   1200  C  ALYS A 149      10.478   2.889  14.271  0.50 13.46           C  
ANISOU 1200  C  ALYS A 149     1817   1483   1812    -95      6   -308       C  
ATOM   1201  C  BLYS A 149      10.483   2.890  14.268  0.50 13.19           C  
ANISOU 1201  C  BLYS A 149     1791   1475   1745   -144    -71   -316       C  
ATOM   1202  O  ALYS A 149      10.028   1.802  13.877  0.50 14.90           O  
ANISOU 1202  O  ALYS A 149     1936   1359   2366    -40    -27   -326       O  
ATOM   1203  O  BLYS A 149      10.031   1.803  13.878  0.50 14.69           O  
ANISOU 1203  O  BLYS A 149     1915   1366   2300    -92    -75   -359       O  
ATOM   1204  N   ILE A 150       9.981   4.078  13.932  1.00 13.18           N  
ANISOU 1204  N   ILE A 150     1736   1450   1819   -126     43   -317       N  
ATOM   1205  CA  ILE A 150       8.898   4.270  12.983  1.00 13.15           C  
ANISOU 1205  CA  ILE A 150     1923   1257   1817    -66     24   -160       C  
ATOM   1206  CB  ILE A 150       7.647   4.817  13.701  1.00 12.42           C  
ANISOU 1206  CB  ILE A 150     1810   1275   1633   -213     67   -164       C  
ATOM   1207  CG1 ILE A 150       7.083   3.780  14.676  1.00 12.36           C  
ANISOU 1207  CG1 ILE A 150     1518   1411   1767   -347    -24   -176       C  
ATOM   1208  CG2 ILE A 150       6.598   5.312  12.706  1.00 13.69           C  
ANISOU 1208  CG2 ILE A 150     2068   1454   1677    -35     77    -39       C  
ATOM   1209  CD1 ILE A 150       6.146   4.360  15.711  1.00 13.61           C  
ANISOU 1209  CD1 ILE A 150     1623   1670   1878   -142    -17   -193       C  
ATOM   1210  C   ILE A 150       9.415   5.253  11.936  1.00 13.42           C  
ANISOU 1210  C   ILE A 150     1865   1282   1951   -107    178   -170       C  
ATOM   1211  O   ILE A 150       9.909   6.316  12.298  1.00 14.01           O  
ANISOU 1211  O   ILE A 150     2069   1485   1767   -227    115   -352       O  
ATOM   1212  N   LYS A 151       9.203   4.941  10.659  1.00 13.68           N  
ANISOU 1212  N   LYS A 151     2118   1198   1883   -337    257   -142       N  
ATOM   1213  CA  LYS A 151       9.628   5.806   9.572  1.00 13.75           C  
ANISOU 1213  CA  LYS A 151     2000   1262   1959   -309    275    -58       C  
ATOM   1214  CB  LYS A 151      10.905   5.294   8.906  1.00 16.07           C  
ANISOU 1214  CB  LYS A 151     2241   1823   2040   -324    345   -104       C  
ATOM   1215  CG  LYS A 151      12.116   5.176   9.816  1.00 17.82           C  
ANISOU 1215  CG  LYS A 151     2226   2140   2404    -70    326    159       C  
ATOM   1216  CD  LYS A 151      13.407   4.821   9.069  1.00 18.68           C  
ANISOU 1216  CD  LYS A 151     2383   2258   2457   -152    432    117       C  
ATOM   1217  CE  LYS A 151      13.319   3.525   8.293  1.00 20.39           C  
ANISOU 1217  CE  LYS A 151     2840   2345   2560   -100    435     28       C  
ATOM   1218  NZ  LYS A 151      14.609   3.170   7.647  1.00 22.75           N  
ANISOU 1218  NZ  LYS A 151     3136   2646   2861     67    476   -465       N  
ATOM   1219  C   LYS A 151       8.511   5.904   8.539  1.00 14.60           C  
ANISOU 1219  C   LYS A 151     2303   1570   1674   -320    345   -170       C  
ATOM   1220  O   LYS A 151       7.901   4.904   8.173  1.00 15.61           O  
ANISOU 1220  O   LYS A 151     2497   1586   1848   -334    102   -150       O  
ATOM   1221  N   ALA A 152       8.296   7.112   8.010  1.00 14.68           N  
ANISOU 1221  N   ALA A 152     2311   1383   1884   -320    272   -287       N  
ATOM   1222  CA  ALA A 152       7.252   7.304   6.997  1.00 15.67           C  
ANISOU 1222  CA  ALA A 152     2423   1794   1737   -276    323     18       C  
ATOM   1223  CB  ALA A 152       6.954   8.760   6.830  1.00 17.59           C  
ANISOU 1223  CB  ALA A 152     2865   1795   2022    -29     27   -150       C  
ATOM   1224  C   ALA A 152       7.629   6.643   5.664  1.00 16.14           C  
ANISOU 1224  C   ALA A 152     2665   1633   1831   -143    343     29       C  
ATOM   1225  O   ALA A 152       6.754   6.400   4.832  1.00 18.60           O  
ANISOU 1225  O   ALA A 152     2637   2222   2208   -282    245    -55       O  
ATOM   1226  N   VAL A 153       8.908   6.324   5.459  1.00 16.25           N  
ANISOU 1226  N   VAL A 153     2703   1804   1667   -307    566     56       N  
ATOM   1227  CA  VAL A 153       9.295   5.641   4.225  1.00 18.30           C  
ANISOU 1227  CA  VAL A 153     3096   2039   1814   -223    683    -81       C  
ATOM   1228  CB  VAL A 153      10.795   5.766   3.938  1.00 20.67           C  
ANISOU 1228  CB  VAL A 153     3287   2209   2357     32   1090   -250       C  
ATOM   1229  CG1 VAL A 153      11.154   7.210   3.610  1.00 25.34           C  
ANISOU 1229  CG1 VAL A 153     4092   2527   3006   -315   1397    -64       C  
ATOM   1230  CG2 VAL A 153      11.667   5.177   5.039  1.00 21.98           C  
ANISOU 1230  CG2 VAL A 153     3155   3104   2089    117   1287   -120       C  
ATOM   1231  C   VAL A 153       8.847   4.165   4.246  1.00 18.00           C  
ANISOU 1231  C   VAL A 153     3169   1989   1679   -270    515    -62       C  
ATOM   1232  O   VAL A 153       8.931   3.508   3.212  1.00 22.23           O  
ANISOU 1232  O   VAL A 153     4189   2169   2087   -116    382   -515       O  
ATOM   1233  N   SER A 154       8.459   3.637   5.417  1.00 16.20           N  
ANISOU 1233  N   SER A 154     2788   1649   1718   -217    449    -10       N  
ATOM   1234  CA  SER A 154       8.107   2.219   5.613  1.00 17.78           C  
ANISOU 1234  CA  SER A 154     2899   1762   2095   -369    176    168       C  
ATOM   1235  CB  SER A 154       8.716   1.706   6.901  1.00 20.21           C  
ANISOU 1235  CB  SER A 154     3002   2134   2541   -296   -168    483       C  
ATOM   1236  OG  SER A 154      10.085   1.931   6.927  1.00 25.16           O  
ANISOU 1236  OG  SER A 154     3080   2595   3883   -342   -369    664       O  
ATOM   1237  C   SER A 154       6.590   2.043   5.712  1.00 15.48           C  
ANISOU 1237  C   SER A 154     2735   1476   1670     -3    356     -9       C  
ATOM   1238  O   SER A 154       5.893   2.873   6.294  1.00 18.88           O  
ANISOU 1238  O   SER A 154     3311   1686   2175     25    779   -261       O  
ATOM   1239  N   MET A 155       6.084   0.902   5.252  1.00 14.79           N  
ANISOU 1239  N   MET A 155     2662   1199   1758    235    180    110       N  
ATOM   1240  CA  MET A 155       4.640   0.710   5.228  1.00 15.43           C  
ANISOU 1240  CA  MET A 155     2611   1497   1752    246    197    161       C  
ATOM   1241  CB  MET A 155       4.233  -0.345   4.208  1.00 17.74           C  
ANISOU 1241  CB  MET A 155     2799   1843   2097    367    166   -200       C  
ATOM   1242  CG  MET A 155       4.608   0.044   2.796  1.00 21.80           C  
ANISOU 1242  CG  MET A 155     3430   2787   2062    -27     37   -293       C  
ATOM   1243  SD  MET A 155       3.837   1.517   2.133  1.00 33.35           S  
ANISOU 1243  SD  MET A 155     5365   4050   3257    400   -252    729       S  
ATOM   1244  CE  MET A 155       2.218   1.487   2.890  1.00 35.17           C  
ANISOU 1244  CE  MET A 155     4664   4708   3991    122  -1154    617       C  
ATOM   1245  C   MET A 155       4.065   0.343   6.601  1.00 15.08           C  
ANISOU 1245  C   MET A 155     2581   1354   1794    134    141    176       C  
ATOM   1246  O   MET A 155       2.899   0.661   6.866  1.00 15.88           O  
ANISOU 1246  O   MET A 155     2610   1390   2033    122    124     51       O  
ATOM   1247  N   ASN A 156       4.851  -0.309   7.464  1.00 13.08           N  
ANISOU 1247  N   ASN A 156     2029   1328   1611    137    286     40       N  
ATOM   1248  CA  ASN A 156       4.365  -0.582   8.811  1.00 13.31           C  
ANISOU 1248  CA  ASN A 156     2134   1306   1615    129    259    102       C  
ATOM   1249  CB  ASN A 156       4.999  -1.816   9.452  1.00 13.22           C  
ANISOU 1249  CB  ASN A 156     2240   1139   1641    123    255    -18       C  
ATOM   1250  CG  ASN A 156       4.363  -2.112  10.796  1.00 13.62           C  
ANISOU 1250  CG  ASN A 156     2093   1464   1617      4    150     33       C  
ATOM   1251  OD1 ASN A 156       3.129  -2.104  10.885  1.00 13.55           O  
ANISOU 1251  OD1 ASN A 156     2014   1487   1646    -80   -116   -126       O  
ATOM   1252  ND2 ASN A 156       5.174  -2.401  11.819  1.00 13.73           N  
ANISOU 1252  ND2 ASN A 156     1996   1563   1656    106    101    -31       N  
ATOM   1253  C   ASN A 156       4.613   0.679   9.647  1.00 13.58           C  
ANISOU 1253  C   ASN A 156     2259   1194   1705    230    266    130       C  
ATOM   1254  O   ASN A 156       5.643   0.844  10.282  1.00 15.97           O  
ANISOU 1254  O   ASN A 156     2212   1398   2458    302    157    -15       O  
ATOM   1255  N   ASN A 157       3.638   1.580   9.587  1.00 11.79           N  
ANISOU 1255  N   ASN A 157     1729   1205   1542     41    -34   -141       N  
ATOM   1256  CA  ASN A 157       3.816   2.911  10.143  1.00 11.07           C  
ANISOU 1256  CA  ASN A 157     1673   1177   1355     39     63   -124       C  
ATOM   1257  CB  ASN A 157       4.243   3.902   9.056  1.00 12.26           C  
ANISOU 1257  CB  ASN A 157     1737   1396   1525    114    157     51       C  
ATOM   1258  CG  ASN A 157       4.168   5.347   9.498  1.00 11.50           C  
ANISOU 1258  CG  ASN A 157     1771   1406   1189   -199    184     -9       C  
ATOM   1259  OD1 ASN A 157       4.090   5.595  10.706  1.00 11.38           O  
ANISOU 1259  OD1 ASN A 157     1707   1422   1192   -190    217    -38       O  
ATOM   1260  ND2 ASN A 157       4.196   6.278   8.537  1.00 13.06           N  
ANISOU 1260  ND2 ASN A 157     1762   1587   1613   -287    363    272       N  
ATOM   1261  C   ASN A 157       2.497   3.332  10.769  1.00 11.38           C  
ANISOU 1261  C   ASN A 157     1697   1221   1404    111    109     13       C  
ATOM   1262  O   ASN A 157       1.559   3.687  10.054  1.00 11.12           O  
ANISOU 1262  O   ASN A 157     1569   1331   1322     19    122      0       O  
ATOM   1263  N   PRO A 158       2.389   3.325  12.111  1.00 10.74           N  
ANISOU 1263  N   PRO A 158     1431   1315   1333     58    130   -172       N  
ATOM   1264  CA  PRO A 158       1.116   3.658  12.752  1.00 11.36           C  
ANISOU 1264  CA  PRO A 158     1546   1419   1349     40    222   -225       C  
ATOM   1265  CB  PRO A 158       1.379   3.295  14.225  1.00 12.50           C  
ANISOU 1265  CB  PRO A 158     1869   1505   1374    103    266    -56       C  
ATOM   1266  CG  PRO A 158       2.847   3.535  14.398  1.00 12.60           C  
ANISOU 1266  CG  PRO A 158     1987   1440   1358    246     40      2       C  
ATOM   1267  CD  PRO A 158       3.455   3.046  13.099  1.00 11.89           C  
ANISOU 1267  CD  PRO A 158     1688   1473   1354    129     50    -64       C  
ATOM   1268  C   PRO A 158       0.734   5.135  12.596  1.00 11.35           C  
ANISOU 1268  C   PRO A 158     1469   1408   1434   -167    158    -17       C  
ATOM   1269  O   PRO A 158      -0.369   5.508  12.949  1.00 12.74           O  
ANISOU 1269  O   PRO A 158     1726   1479   1634     87    256     56       O  
ATOM   1270  N   TYR A 159       1.654   5.976  12.106  1.00 10.32           N  
ANISOU 1270  N   TYR A 159     1228   1365   1328    -68    187     30       N  
ATOM   1271  CA  TYR A 159       1.320   7.384  11.892  1.00 10.97           C  
ANISOU 1271  CA  TYR A 159     1492   1305   1367    -53    139    -61       C  
ATOM   1272  CB  TYR A 159       2.459   8.311  12.343  1.00 11.35           C  
ANISOU 1272  CB  TYR A 159     1456   1457   1397    -79    147    -38       C  
ATOM   1273  CG  TYR A 159       2.895   8.032  13.764  1.00 11.58           C  
ANISOU 1273  CG  TYR A 159     1541   1484   1374    -42    144    -74       C  
ATOM   1274  CD1 TYR A 159       1.941   7.803  14.754  1.00 11.42           C  
ANISOU 1274  CD1 TYR A 159     1683   1345   1311    -64    155    -56       C  
ATOM   1275  CE1 TYR A 159       2.315   7.480  16.049  1.00 11.45           C  
ANISOU 1275  CE1 TYR A 159     1619   1435   1293    -72    234     54       C  
ATOM   1276  CZ  TYR A 159       3.647   7.407  16.385  1.00 11.49           C  
ANISOU 1276  CZ  TYR A 159     1607   1330   1426   -156    120     17       C  
ATOM   1277  OH  TYR A 159       3.963   7.030  17.667  1.00 11.61           O  
ANISOU 1277  OH  TYR A 159     1732   1329   1348   -242     14    -94       O  
ATOM   1278  CE2 TYR A 159       4.607   7.664  15.421  1.00 11.23           C  
ANISOU 1278  CE2 TYR A 159     1449   1371   1445   -233     47    -74       C  
ATOM   1279  CD2 TYR A 159       4.223   7.990  14.132  1.00 12.61           C  
ANISOU 1279  CD2 TYR A 159     1629   1553   1608     -1    172    151       C  
ATOM   1280  C   TYR A 159       0.851   7.626  10.456  1.00 11.18           C  
ANISOU 1280  C   TYR A 159     1611   1209   1426   -172     10      0       C  
ATOM   1281  O   TYR A 159       0.582   8.774  10.096  1.00 11.80           O  
ANISOU 1281  O   TYR A 159     1724   1179   1578   -160    -73     23       O  
ATOM   1282  N   ARG A 160       0.662   6.564   9.664  1.00 11.01           N  
ANISOU 1282  N   ARG A 160     1565   1260   1358    -79    -87    -17       N  
ATOM   1283  CA  ARG A 160      -0.129   6.697   8.448  1.00 11.05           C  
ANISOU 1283  CA  ARG A 160     1713   1291   1192    -16     47    -45       C  
ATOM   1284  CB  ARG A 160      -0.321   5.347   7.761  1.00 11.99           C  
ANISOU 1284  CB  ARG A 160     1971   1254   1328    -45   -106    -54       C  
ATOM   1285  CG  ARG A 160       0.901   4.900   6.961  1.00 14.10           C  
ANISOU 1285  CG  ARG A 160     2412   1414   1528     13    202     63       C  
ATOM   1286  CD  ARG A 160       0.932   3.418   6.602  1.00 18.33           C  
ANISOU 1286  CD  ARG A 160     3297   1503   2163    168    -31   -167       C  
ATOM   1287  NE  ARG A 160       0.033   3.025   5.560  1.00 19.44           N  
ANISOU 1287  NE  ARG A 160     3907   1365   2114    244   -344      5       N  
ATOM   1288  CZ  ARG A 160      -0.258   1.769   5.155  1.00 20.24           C  
ANISOU 1288  CZ  ARG A 160     3871   1673   2145     86   -426   -346       C  
ATOM   1289  NH1 ARG A 160       0.441   0.745   5.566  1.00 23.61           N  
ANISOU 1289  NH1 ARG A 160     4890   2000   2079    446   -204   -391       N  
ATOM   1290  NH2 ARG A 160      -1.291   1.561   4.342  1.00 24.80           N  
ANISOU 1290  NH2 ARG A 160     3707   3005   2710    139   -329   -404       N  
ATOM   1291  C   ARG A 160      -1.470   7.327   8.794  1.00 11.39           C  
ANISOU 1291  C   ARG A 160     1574   1514   1238     -4    -73   -116       C  
ATOM   1292  O   ARG A 160      -2.180   6.859   9.690  1.00 13.45           O  
ANISOU 1292  O   ARG A 160     1627   2000   1483     86     52     79       O  
ATOM   1293  N   GLN A 161      -1.843   8.366   8.053  1.00 11.34           N  
ANISOU 1293  N   GLN A 161     1475   1567   1267    -27     49    -66       N  
ATOM   1294  CA  GLN A 161      -3.154   8.930   8.287  1.00 12.27           C  
ANISOU 1294  CA  GLN A 161     1522   1666   1473     42     59     47       C  
ATOM   1295  CB  GLN A 161      -3.207  10.350   7.738  1.00 15.07           C  
ANISOU 1295  CB  GLN A 161     1993   1681   2051   -167    -31    152       C  
ATOM   1296  CG  GLN A 161      -3.106  10.483   6.240  1.00 16.25           C  
ANISOU 1296  CG  GLN A 161     2113   1942   2116   -314     72    402       C  
ATOM   1297  CD  GLN A 161      -3.105  11.965   5.881  1.00 20.17           C  
ANISOU 1297  CD  GLN A 161     2974   1953   2736  -1137    397    704       C  
ATOM   1298  OE1 GLN A 161      -2.411  12.820   6.468  1.00 24.62           O  
ANISOU 1298  OE1 GLN A 161     4029   2216   3107   -850    112    446       O  
ATOM   1299  NE2 GLN A 161      -3.822  12.305   4.846  1.00 23.99           N  
ANISOU 1299  NE2 GLN A 161     3101   2252   3758   -959   -254    311       N  
ATOM   1300  C   GLN A 161      -4.259   8.018   7.731  1.00 11.23           C  
ANISOU 1300  C   GLN A 161     1558   1466   1241    143     53    -33       C  
ATOM   1301  O   GLN A 161      -3.997   7.006   7.062  1.00 11.45           O  
ANISOU 1301  O   GLN A 161     1434   1425   1490    113    118   -130       O  
ATOM   1302  N   GLY A 162      -5.511   8.388   8.002  1.00 10.62           N  
ANISOU 1302  N   GLY A 162     1479   1343   1212     31    -20      3       N  
ATOM   1303  CA  GLY A 162      -6.662   7.587   7.568  1.00 10.49           C  
ANISOU 1303  CA  GLY A 162     1331   1413   1238     44     83    -24       C  
ATOM   1304  C   GLY A 162      -6.671   7.323   6.069  1.00 11.51           C  
ANISOU 1304  C   GLY A 162     1731   1404   1238   -182    110    -40       C  
ATOM   1305  O   GLY A 162      -6.939   6.187   5.631  1.00 11.36           O  
ANISOU 1305  O   GLY A 162     1666   1425   1224   -211     86   -113       O  
ATOM   1306  N   THR A 163      -6.416   8.363   5.258  1.00 11.43           N  
ANISOU 1306  N   THR A 163     1584   1506   1252   -273     60     57       N  
ATOM   1307  CA  THR A 163      -6.434   8.175   3.805  1.00 12.54           C  
ANISOU 1307  CA  THR A 163     1767   1713   1283   -290    157     59       C  
ATOM   1308  CB  THR A 163      -6.351   9.502   3.049  1.00 13.32           C  
ANISOU 1308  CB  THR A 163     1778   1817   1466   -361     59    188       C  
ATOM   1309  OG1 THR A 163      -5.093  10.128   3.325  1.00 14.85           O  
ANISOU 1309  OG1 THR A 163     1853   1748   2040   -395    -87    175       O  
ATOM   1310  CG2 THR A 163      -7.523  10.438   3.336  1.00 13.44           C  
ANISOU 1310  CG2 THR A 163     1695   2040   1372   -338     34    315       C  
ATOM   1311  C   THR A 163      -5.294   7.261   3.328  1.00 11.99           C  
ANISOU 1311  C   THR A 163     1821   1619   1112   -325     47     69       C  
ATOM   1312  O   THR A 163      -5.296   6.848   2.150  1.00 13.13           O  
ANISOU 1312  O   THR A 163     1814   2064   1110   -370    -58    -49       O  
ATOM   1313  N   GLU A 164      -4.348   6.933   4.229  1.00 11.41           N  
ANISOU 1313  N   GLU A 164     1771   1491   1073   -206     75     -6       N  
ATOM   1314  CA  GLU A 164      -3.251   6.039   3.904  1.00 12.82           C  
ANISOU 1314  CA  GLU A 164     1771   1892   1206   -180    167   -181       C  
ATOM   1315  CB  GLU A 164      -1.920   6.663   4.309  1.00 14.27           C  
ANISOU 1315  CB  GLU A 164     1888   2151   1381   -312     17   -238       C  
ATOM   1316  CG  GLU A 164      -1.672   8.011   3.670  1.00 15.50           C  
ANISOU 1316  CG  GLU A 164     1938   2174   1777   -489    -89   -274       C  
ATOM   1317  CD  GLU A 164      -1.287   7.988   2.203  1.00 19.81           C  
ANISOU 1317  CD  GLU A 164     3051   2545   1930   -633     67    208       C  
ATOM   1318  OE1 GLU A 164      -1.245   6.934   1.627  1.00 19.33           O  
ANISOU 1318  OE1 GLU A 164     2784   3021   1538   -916    195   -265       O  
ATOM   1319  OE2 GLU A 164      -0.974   9.067   1.662  1.00 28.61           O  
ANISOU 1319  OE2 GLU A 164     4830   3148   2893  -1426    -40    810       O  
ATOM   1320  C   GLU A 164      -3.408   4.670   4.578  1.00 12.71           C  
ANISOU 1320  C   GLU A 164     1782   1740   1305   -238    199   -253       C  
ATOM   1321  O   GLU A 164      -2.492   3.852   4.527  1.00 16.49           O  
ANISOU 1321  O   GLU A 164     2217   2169   1880     87    523     32       O  
ATOM   1322  N   SER A 165      -4.551   4.427   5.238  1.00 11.93           N  
ANISOU 1322  N   SER A 165     1682   1502   1349     49    172      3       N  
ATOM   1323  CA  SER A 165      -4.748   3.228   6.091  1.00 11.62           C  
ANISOU 1323  CA  SER A 165     1780   1325   1310    103     90   -137       C  
ATOM   1324  CB  SER A 165      -4.916   3.623   7.532  1.00 12.28           C  
ANISOU 1324  CB  SER A 165     1844   1492   1330    -82    294   -146       C  
ATOM   1325  OG  SER A 165      -3.742   4.263   8.032  1.00 14.14           O  
ANISOU 1325  OG  SER A 165     2160   1773   1437   -169      0   -126       O  
ATOM   1326  C   SER A 165      -6.005   2.487   5.618  1.00 12.63           C  
ANISOU 1326  C   SER A 165     1836   1461   1499    119    -27   -104       C  
ATOM   1327  O   SER A 165      -7.102   2.979   5.754  1.00 13.49           O  
ANISOU 1327  O   SER A 165     1758   1446   1921    -43     87   -378       O  
ATOM   1328  N  ATHR A 166      -5.817   1.303   5.043  0.50 12.61           N  
ANISOU 1328  N  ATHR A 166     1819   1423   1549    216     55    -55       N  
ATOM   1329  N  BTHR A 166      -5.838   1.304   5.017  0.50 12.22           N  
ANISOU 1329  N  BTHR A 166     1618   1503   1520    416    -13    -80       N  
ATOM   1330  CA ATHR A 166      -6.927   0.468   4.590  0.50 13.30           C  
ANISOU 1330  CA ATHR A 166     2106   1410   1537     89    -21    -15       C  
ATOM   1331  CA BTHR A 166      -7.010   0.494   4.596  0.50 12.71           C  
ANISOU 1331  CA BTHR A 166     1778   1581   1468    380   -115    -92       C  
ATOM   1332  CB ATHR A 166      -6.398  -0.625   3.662  0.50 14.18           C  
ANISOU 1332  CB ATHR A 166     2432   1427   1525     92    203     89       C  
ATOM   1333  CB BTHR A 166      -6.676  -0.679   3.673  0.50 12.95           C  
ANISOU 1333  CB BTHR A 166     1739   1786   1396    610      4    -54       C  
ATOM   1334  OG1ATHR A 166      -5.814   0.011   2.518  0.50 16.39           O  
ANISOU 1334  OG1ATHR A 166     2849   1663   1714   -305    279    168       O  
ATOM   1335  OG1BTHR A 166      -5.719  -1.517   4.333  0.50 13.50           O  
ANISOU 1335  OG1BTHR A 166     1681   2093   1353    823    -85   -305       O  
ATOM   1336  CG2ATHR A 166      -7.481  -1.573   3.219  0.50 14.10           C  
ANISOU 1336  CG2ATHR A 166     2269   1534   1553     72    246    109       C  
ATOM   1337  CG2BTHR A 166      -6.178  -0.205   2.324  0.50 14.02           C  
ANISOU 1337  CG2BTHR A 166     1942   1994   1391    536     -9     -6       C  
ATOM   1338  C  ATHR A 166      -7.704  -0.095   5.790  0.50 12.18           C  
ANISOU 1338  C  ATHR A 166     1945   1241   1441    185    -53   -108       C  
ATOM   1339  C  BTHR A 166      -7.736  -0.083   5.809  0.50 12.30           C  
ANISOU 1339  C  BTHR A 166     1807   1357   1510    318    -76   -147       C  
ATOM   1340  O  ATHR A 166      -8.920  -0.286   5.727  0.50 13.05           O  
ANISOU 1340  O  ATHR A 166     1943   1490   1522    172   -106    -32       O  
ATOM   1341  O  BTHR A 166      -8.951  -0.279   5.758  0.50 13.03           O  
ANISOU 1341  O  BTHR A 166     1805   1582   1563    285   -135    -22       O  
ATOM   1342  N   ASP A 167      -6.987  -0.364   6.879  1.00 12.32           N  
ANISOU 1342  N   ASP A 167     1970   1352   1359     87   -135   -219       N  
ATOM   1343  CA  ASP A 167      -7.563  -0.931   8.104  1.00 12.89           C  
ANISOU 1343  CA  ASP A 167     2270   1234   1390     -6   -198   -137       C  
ATOM   1344  CB  ASP A 167      -6.912  -2.261   8.462  1.00 15.84           C  
ANISOU 1344  CB  ASP A 167     3172   1119   1726    171   -145   -371       C  
ATOM   1345  CG  ASP A 167      -7.472  -2.970   9.692  1.00 20.97           C  
ANISOU 1345  CG  ASP A 167     4014   1592   2361   -260    -77     49       C  
ATOM   1346  OD1 ASP A 167      -8.298  -2.347  10.471  1.00 21.16           O  
ANISOU 1346  OD1 ASP A 167     3768   1442   2826   -292   -671   -188       O  
ATOM   1347  OD2 ASP A 167      -7.051  -4.153   9.883  1.00 28.08           O  
ANISOU 1347  OD2 ASP A 167     5177   2044   3447    326   -335    250       O  
ATOM   1348  C   ASP A 167      -7.327   0.049   9.254  1.00 12.08           C  
ANISOU 1348  C   ASP A 167     2117   1261   1209     65   -208    -79       C  
ATOM   1349  O   ASP A 167      -6.163   0.230   9.697  1.00 12.54           O  
ANISOU 1349  O   ASP A 167     1867   1453   1443    238     44   -194       O  
ATOM   1350  N   SER A 168      -8.412   0.672   9.725  1.00 11.73           N  
ANISOU 1350  N   SER A 168     1890   1331   1234   -147   -200   -123       N  
ATOM   1351  CA  SER A 168      -8.318   1.710  10.728  1.00 11.83           C  
ANISOU 1351  CA  SER A 168     1839   1244   1408   -152   -110   -139       C  
ATOM   1352  CB  SER A 168      -9.674   2.264  11.062  1.00 12.31           C  
ANISOU 1352  CB  SER A 168     1904   1269   1502    -65    -37   -109       C  
ATOM   1353  OG  SER A 168     -10.487   1.275  11.671  1.00 13.55           O  
ANISOU 1353  OG  SER A 168     1718   1749   1680   -105    187    -18       O  
ATOM   1354  C   SER A 168      -7.594   1.251  12.007  1.00 11.87           C  
ANISOU 1354  C   SER A 168     1681   1308   1521      9   -156   -197       C  
ATOM   1355  O   SER A 168      -6.944   2.073  12.669  1.00 11.96           O  
ANISOU 1355  O   SER A 168     1820   1259   1462   -110   -192   -188       O  
ATOM   1356  N   ARG A 169      -7.678  -0.026  12.358  1.00 12.30           N  
ANISOU 1356  N   ARG A 169     1682   1415   1576    -36   -148      9       N  
ATOM   1357  CA  ARG A 169      -7.097  -0.468  13.652  1.00 13.84           C  
ANISOU 1357  CA  ARG A 169     2151   1558   1546    -10   -163     76       C  
ATOM   1358  CB  ARG A 169      -7.571  -1.881  14.014  1.00 19.49           C  
ANISOU 1358  CB  ARG A 169     3000   1906   2498   -335   -463    580       C  
ATOM   1359  CG  ARG A 169      -6.889  -3.012  13.277  1.00 27.09           C  
ANISOU 1359  CG  ARG A 169     3949   3096   3247   -146   -179    274       C  
ATOM   1360  CD  ARG A 169      -7.607  -4.345  13.480  1.00 35.18           C  
ANISOU 1360  CD  ARG A 169     5377   3567   4420   -615    319    939       C  
ATOM   1361  NE  ARG A 169      -6.891  -5.286  14.342  1.00 39.89           N  
ANISOU 1361  NE  ARG A 169     5916   5186   4055     48    772   1264       N  
ATOM   1362  CZ  ARG A 169      -5.941  -6.109  13.903  1.00 47.58           C  
ANISOU 1362  CZ  ARG A 169     6744   5941   5392    310    997    241       C  
ATOM   1363  NH1 ARG A 169      -5.566  -6.064  12.631  1.00 53.00           N  
ANISOU 1363  NH1 ARG A 169     7074   7267   5793  -1035   1961   -689       N  
ATOM   1364  NH2 ARG A 169      -5.394  -6.985  14.725  1.00 48.81           N  
ANISOU 1364  NH2 ARG A 169     5769   6795   5980    450   -192   -343       N  
ATOM   1365  C   ARG A 169      -5.565  -0.366  13.630  1.00 12.47           C  
ANISOU 1365  C   ARG A 169     2118   1356   1263     -4   -170    110       C  
ATOM   1366  O   ARG A 169      -4.925  -0.350  14.695  1.00 13.15           O  
ANISOU 1366  O   ARG A 169     2079   1709   1206    207   -194    -88       O  
ATOM   1367  N   MET A 170      -4.950  -0.262  12.447  1.00 11.38           N  
ANISOU 1367  N   MET A 170     1726   1245   1352    128    -33    -51       N  
ATOM   1368  CA AMET A 170      -3.475  -0.190  12.337  0.50 11.56           C  
ANISOU 1368  CA AMET A 170     1680   1207   1502    221     -8    -26       C  
ATOM   1369  CA BMET A 170      -3.476  -0.195  12.352  0.50 11.42           C  
ANISOU 1369  CA BMET A 170     1672   1190   1476    230     -9    -37       C  
ATOM   1370  CB AMET A 170      -3.016  -0.541  10.922  0.50 13.46           C  
ANISOU 1370  CB AMET A 170     2052   1475   1585    194     59   -129       C  
ATOM   1371  CB BMET A 170      -2.994  -0.595  10.960  0.50 12.92           C  
ANISOU 1371  CB BMET A 170     1994   1368   1545    189     25   -156       C  
ATOM   1372  CG AMET A 170      -3.398  -1.928  10.495  0.50 14.66           C  
ANISOU 1372  CG AMET A 170     2262   1411   1894    267    -32    -94       C  
ATOM   1373  CG BMET A 170      -3.439  -1.973  10.550  0.50 13.93           C  
ANISOU 1373  CG BMET A 170     2156   1294   1841    280    -62   -151       C  
ATOM   1374  SD AMET A 170      -2.454  -3.131  11.438  0.50 14.76           S  
ANISOU 1374  SD AMET A 170     2113   1556   1938    148   -242   -112       S  
ATOM   1375  SD BMET A 170      -2.949  -3.246  11.735  0.50 13.50           S  
ANISOU 1375  SD BMET A 170     2043   1201   1885    105   -158   -188       S  
ATOM   1376  CE AMET A 170      -3.740  -3.734  12.537  0.50 17.13           C  
ANISOU 1376  CE AMET A 170     2723   1464   2321     27    -58    127       C  
ATOM   1377  CE BMET A 170      -3.230  -4.667  10.681  0.50 13.19           C  
ANISOU 1377  CE BMET A 170     1999    961   2051     86   -491    -85       C  
ATOM   1378  C   MET A 170      -2.936   1.210  12.657  1.00 11.17           C  
ANISOU 1378  C   MET A 170     1504   1300   1439    131     58    -12       C  
ATOM   1379  O   MET A 170      -1.732   1.376  12.871  1.00 12.46           O  
ANISOU 1379  O   MET A 170     1530   1502   1700    249     50    -93       O  
ATOM   1380  N   SER A 171      -3.815   2.214  12.645  1.00 11.18           N  
ANISOU 1380  N   SER A 171     1436   1317   1494     55     31   -210       N  
ATOM   1381  CA  SER A 171      -3.384   3.613  12.669  1.00 11.22           C  
ANISOU 1381  CA  SER A 171     1467   1258   1537     88     20   -214       C  
ATOM   1382  CB  SER A 171      -4.101   4.401  11.606  1.00 11.88           C  
ANISOU 1382  CB  SER A 171     1613   1329   1572    -89    -64    -91       C  
ATOM   1383  OG  SER A 171      -3.751   5.775  11.668  1.00 11.91           O  
ANISOU 1383  OG  SER A 171     1804   1337   1383   -119   -237   -116       O  
ATOM   1384  C   SER A 171      -3.591   4.276  14.030  1.00 10.70           C  
ANISOU 1384  C   SER A 171     1460   1177   1425    -56    -97   -116       C  
ATOM   1385  O   SER A 171      -4.697   4.250  14.588  1.00 11.64           O  
ANISOU 1385  O   SER A 171     1604   1157   1662   -141     51   -142       O  
ATOM   1386  N   ARG A 172      -2.535   4.948  14.492  1.00  9.83           N  
ANISOU 1386  N   ARG A 172     1477   1103   1154    -53     -1   -188       N  
ATOM   1387  CA  ARG A 172      -2.605   5.948  15.570  1.00  9.83           C  
ANISOU 1387  CA  ARG A 172     1558   1079   1096   -116    126   -165       C  
ATOM   1388  CB  ARG A 172      -1.557   5.648  16.643  1.00 10.07           C  
ANISOU 1388  CB  ARG A 172     1489   1133   1204   -188    105   -281       C  
ATOM   1389  CG  ARG A 172      -1.593   4.232  17.191  1.00 10.69           C  
ANISOU 1389  CG  ARG A 172     1547   1159   1354   -198    177   -267       C  
ATOM   1390  CD  ARG A 172      -0.749   4.050  18.456  1.00 10.44           C  
ANISOU 1390  CD  ARG A 172     1489   1113   1364   -121    146   -416       C  
ATOM   1391  NE  ARG A 172       0.632   4.479  18.304  1.00 10.64           N  
ANISOU 1391  NE  ARG A 172     1562   1060   1420   -175    155   -297       N  
ATOM   1392  CZ  ARG A 172       1.680   3.701  18.015  1.00 10.07           C  
ANISOU 1392  CZ  ARG A 172     1538    993   1291   -118     27   -249       C  
ATOM   1393  NH1 ARG A 172       1.520   2.395  17.784  1.00 10.70           N  
ANISOU 1393  NH1 ARG A 172     1654   1048   1360   -108    -22   -407       N  
ATOM   1394  NH2 ARG A 172       2.889   4.270  17.903  1.00 11.06           N  
ANISOU 1394  NH2 ARG A 172     1715   1080   1406   -290     29    -71       N  
ATOM   1395  C   ARG A 172      -2.398   7.355  15.000  1.00 10.32           C  
ANISOU 1395  C   ARG A 172     1485   1237   1199   -178     47    -38       C  
ATOM   1396  O   ARG A 172      -2.059   8.289  15.750  1.00 11.07           O  
ANISOU 1396  O   ARG A 172     1646   1231   1327   -234     66    -49       O  
ATOM   1397  N   GLY A 173      -2.587   7.481  13.675  1.00 10.49           N  
ANISOU 1397  N   GLY A 173     1618   1184   1182   -168     39    -59       N  
ATOM   1398  CA  GLY A 173      -2.290   8.705  12.967  1.00 10.42           C  
ANISOU 1398  CA  GLY A 173     1408   1291   1260   -210    186    -18       C  
ATOM   1399  C   GLY A 173      -3.481   9.645  12.900  1.00 10.77           C  
ANISOU 1399  C   GLY A 173     1452   1257   1380   -152    147    -83       C  
ATOM   1400  O   GLY A 173      -4.557   9.367  13.428  1.00 10.73           O  
ANISOU 1400  O   GLY A 173     1254   1344   1478   -124     55    -41       O  
ATOM   1401  N   LEU A 174      -3.255  10.777  12.234  1.00 11.15           N  
ANISOU 1401  N   LEU A 174     1519   1289   1428    -24    139    -45       N  
ATOM   1402  CA  LEU A 174      -4.288  11.784  12.085  1.00 11.26           C  
ANISOU 1402  CA  LEU A 174     1635   1086   1556     11     67   -108       C  
ATOM   1403  CB  LEU A 174      -3.637  13.087  11.613  1.00 11.84           C  
ANISOU 1403  CB  LEU A 174     1747   1159   1591     29    180    -71       C  
ATOM   1404  CG  LEU A 174      -2.497  13.609  12.501  1.00 12.87           C  
ANISOU 1404  CG  LEU A 174     1757   1227   1905    -64    169   -139       C  
ATOM   1405  CD1 LEU A 174      -1.931  14.884  11.917  1.00 15.91           C  
ANISOU 1405  CD1 LEU A 174     2245   1279   2518   -282     -6   -120       C  
ATOM   1406  CD2 LEU A 174      -2.939  13.782  13.945  1.00 13.94           C  
ANISOU 1406  CD2 LEU A 174     2040   1264   1991     12    173   -207       C  
ATOM   1407  C   LEU A 174      -5.363  11.308  11.106  1.00 11.60           C  
ANISOU 1407  C   LEU A 174     1639   1246   1521      7     59    -69       C  
ATOM   1408  O   LEU A 174      -5.149  10.478  10.225  1.00 12.80           O  
ANISOU 1408  O   LEU A 174     1695   1672   1495     60     37   -260       O  
ATOM   1409  N   GLY A 175      -6.558  11.861  11.253  1.00 10.62           N  
ANISOU 1409  N   GLY A 175     1506   1154   1376   -140     98    -30       N  
ATOM   1410  CA  GLY A 175      -7.626  11.650  10.280  1.00 11.02           C  
ANISOU 1410  CA  GLY A 175     1529   1290   1365   -130     53     22       C  
ATOM   1411  C   GLY A 175      -8.047  10.203  10.131  1.00 10.93           C  
ANISOU 1411  C   GLY A 175     1526   1249   1375     -6    -40    -56       C  
ATOM   1412  O   GLY A 175      -8.422   9.777   9.036  1.00 11.67           O  
ANISOU 1412  O   GLY A 175     1818   1171   1445     -2     16   -191       O  
ATOM   1413  N   CYS A 176      -8.039   9.444  11.227  1.00 10.35           N  
ANISOU 1413  N   CYS A 176     1596   1208   1129    -91    -49   -209       N  
ATOM   1414  CA  CYS A 176      -8.379   8.028  11.152  1.00 11.28           C  
ANISOU 1414  CA  CYS A 176     1732   1130   1421    -38     68   -137       C  
ATOM   1415  CB  CYS A 176      -7.154   7.119  11.136  1.00 12.00           C  
ANISOU 1415  CB  CYS A 176     1741   1228   1589    -61    -29    -36       C  
ATOM   1416  SG  CYS A 176      -7.561   5.426  10.645  1.00 12.18           S  
ANISOU 1416  SG  CYS A 176     1825   1260   1541      2     76   -114       S  
ATOM   1417  C   CYS A 176      -9.368   7.641  12.250  1.00 10.66           C  
ANISOU 1417  C   CYS A 176     1652   1061   1334     52     31   -153       C  
ATOM   1418  O   CYS A 176     -10.579   7.485  11.946  1.00 12.31           O  
ANISOU 1418  O   CYS A 176     1590   1680   1406    -94    152    194       O  
ATOM   1419  N   ASN A 177      -8.899   7.530  13.509  1.00 10.41           N  
ANISOU 1419  N   ASN A 177     1427   1216   1311    -26     44   -192       N  
ATOM   1420  CA  ASN A 177      -9.777   7.070  14.595  1.00 10.61           C  
ANISOU 1420  CA  ASN A 177     1657   1104   1267    -31     30   -163       C  
ATOM   1421  CB  ASN A 177      -9.129   5.909  15.353  1.00 10.57           C  
ANISOU 1421  CB  ASN A 177     1814    970   1232   -164     -6    -80       C  
ATOM   1422  CG  ASN A 177      -8.836   4.740  14.434  1.00 10.01           C  
ANISOU 1422  CG  ASN A 177     1433    961   1406   -101    -47   -142       C  
ATOM   1423  OD1 ASN A 177      -9.700   4.386  13.615  1.00 12.00           O  
ANISOU 1423  OD1 ASN A 177     1447   1426   1686    -58   -179   -438       O  
ATOM   1424  ND2 ASN A 177      -7.654   4.157  14.562  1.00 11.43           N  
ANISOU 1424  ND2 ASN A 177     1616   1179   1546     68   -120    -20       N  
ATOM   1425  C   ASN A 177     -10.177   8.181  15.576  1.00 10.36           C  
ANISOU 1425  C   ASN A 177     1674   1070   1193   -141     42   -142       C  
ATOM   1426  O   ASN A 177     -11.112   7.941  16.377  1.00 11.60           O  
ANISOU 1426  O   ASN A 177     1892   1274   1242   -200    125    -31       O  
ATOM   1427  N   TYR A 178      -9.434   9.310  15.583  1.00 10.10           N  
ANISOU 1427  N   TYR A 178     1444   1100   1292   -131     99   -265       N  
ATOM   1428  CA  TYR A 178      -9.704  10.368  16.553  1.00 10.55           C  
ANISOU 1428  CA  TYR A 178     1593   1105   1310   -121    167   -258       C  
ATOM   1429  CB  TYR A 178      -8.679  10.364  17.699  1.00 10.91           C  
ANISOU 1429  CB  TYR A 178     1682   1181   1281   -244    146   -171       C  
ATOM   1430  CG  TYR A 178      -7.239  10.478  17.263  1.00 11.18           C  
ANISOU 1430  CG  TYR A 178     1676   1172   1399   -212    141   -183       C  
ATOM   1431  CD1 TYR A 178      -6.662  11.705  16.947  1.00 10.99           C  
ANISOU 1431  CD1 TYR A 178     1684   1163   1327   -242     57   -197       C  
ATOM   1432  CE1 TYR A 178      -5.358  11.803  16.487  1.00 10.21           C  
ANISOU 1432  CE1 TYR A 178     1621    963   1294   -236     31   -178       C  
ATOM   1433  CZ  TYR A 178      -4.572  10.665  16.385  1.00 10.37           C  
ANISOU 1433  CZ  TYR A 178     1671   1067   1201   -137    176   -265       C  
ATOM   1434  OH  TYR A 178      -3.270  10.759  15.952  1.00 11.64           O  
ANISOU 1434  OH  TYR A 178     1685   1282   1453   -297    107    -30       O  
ATOM   1435  CE2 TYR A 178      -5.135   9.439  16.698  1.00 10.45           C  
ANISOU 1435  CE2 TYR A 178     1583   1162   1225   -232     88   -228       C  
ATOM   1436  CD2 TYR A 178      -6.454   9.360  17.120  1.00  9.96           C  
ANISOU 1436  CD2 TYR A 178     1665    955   1163   -318     88   -113       C  
ATOM   1437  C   TYR A 178      -9.777  11.721  15.848  1.00 10.55           C  
ANISOU 1437  C   TYR A 178     1499   1169   1338    -70    155   -190       C  
ATOM   1438  O   TYR A 178      -9.152  11.949  14.800  1.00 11.23           O  
ANISOU 1438  O   TYR A 178     1708   1272   1286    -44    124   -172       O  
ATOM   1439  N   ALA A 179     -10.527  12.640  16.466  1.00 10.70           N  
ANISOU 1439  N   ALA A 179     1822   1046   1195    -88    178   -146       N  
ATOM   1440  CA  ALA A 179     -10.638  13.993  15.941  1.00 10.89           C  
ANISOU 1440  CA  ALA A 179     1732   1055   1351    -86    169   -153       C  
ATOM   1441  CB  ALA A 179     -11.794  14.690  16.626  1.00 11.36           C  
ANISOU 1441  CB  ALA A 179     1668   1201   1446    -62    207   -159       C  
ATOM   1442  C   ALA A 179      -9.340  14.778  16.149  1.00 10.83           C  
ANISOU 1442  C   ALA A 179     1683   1170   1259    -81     82   -142       C  
ATOM   1443  O   ALA A 179      -8.653  14.647  17.159  1.00 10.95           O  
ANISOU 1443  O   ALA A 179     1676   1135   1347   -161     73   -156       O  
ATOM   1444  N   TYR A 180      -9.036  15.653  15.185  1.00 10.70           N  
ANISOU 1444  N   TYR A 180     1651   1190   1222    -53    -17   -108       N  
ATOM   1445  CA  TYR A 180      -7.807  16.427  15.209  1.00 11.64           C  
ANISOU 1445  CA  TYR A 180     1808   1124   1489    -73    -70   -111       C  
ATOM   1446  CB  TYR A 180      -6.615  15.593  14.691  1.00 10.70           C  
ANISOU 1446  CB  TYR A 180     1651   1175   1236   -201     40   -250       C  
ATOM   1447  CG  TYR A 180      -6.607  15.555  13.191  1.00 11.26           C  
ANISOU 1447  CG  TYR A 180     1765   1231   1280   -147     61   -154       C  
ATOM   1448  CD1 TYR A 180      -7.606  14.876  12.512  1.00 11.25           C  
ANISOU 1448  CD1 TYR A 180     1722   1099   1451   -136    107   -108       C  
ATOM   1449  CE1 TYR A 180      -7.717  14.950  11.139  1.00 12.02           C  
ANISOU 1449  CE1 TYR A 180     1844   1274   1447    -55     98   -274       C  
ATOM   1450  CZ  TYR A 180      -6.817  15.722  10.420  1.00 12.84           C  
ANISOU 1450  CZ  TYR A 180     2137   1433   1307   -227    109   -240       C  
ATOM   1451  OH  TYR A 180      -6.987  15.856   9.066  1.00 14.02           O  
ANISOU 1451  OH  TYR A 180     2477   1490   1357   -226    -74    -84       O  
ATOM   1452  CE2 TYR A 180      -5.787  16.389  11.076  1.00 12.50           C  
ANISOU 1452  CE2 TYR A 180     2115   1382   1249    -32      1   -172       C  
ATOM   1453  CD2 TYR A 180      -5.706  16.311  12.458  1.00 11.15           C  
ANISOU 1453  CD2 TYR A 180     1834   1216   1186   -252     85   -342       C  
ATOM   1454  C   TYR A 180      -8.000  17.673  14.342  1.00 10.92           C  
ANISOU 1454  C   TYR A 180     1705   1095   1349      1    -36   -207       C  
ATOM   1455  O   TYR A 180      -8.893  17.721  13.479  1.00 11.91           O  
ANISOU 1455  O   TYR A 180     1590   1365   1569   -143    -77    -46       O  
ATOM   1456  N   TYR A 181      -7.113  18.644  14.548  1.00 11.44           N  
ANISOU 1456  N   TYR A 181     1910   1076   1357   -136     64   -245       N  
ATOM   1457  CA  TYR A 181      -7.032  19.794  13.652  1.00 12.29           C  
ANISOU 1457  CA  TYR A 181     2026   1153   1490   -182    -75   -145       C  
ATOM   1458  CB  TYR A 181      -7.998  20.907  14.056  1.00 13.73           C  
ANISOU 1458  CB  TYR A 181     2277   1098   1841   -199    -18    -92       C  
ATOM   1459  CG  TYR A 181      -7.904  22.100  13.150  1.00 15.77           C  
ANISOU 1459  CG  TYR A 181     2333   1468   2190   -269    203    183       C  
ATOM   1460  CD1 TYR A 181      -8.273  22.008  11.825  1.00 16.30           C  
ANISOU 1460  CD1 TYR A 181     2265   1621   2304   -101    -22    406       C  
ATOM   1461  CE1 TYR A 181      -8.127  23.082  10.967  1.00 18.74           C  
ANISOU 1461  CE1 TYR A 181     2490   1941   2686     56    127    791       C  
ATOM   1462  CZ  TYR A 181      -7.632  24.288  11.442  1.00 19.68           C  
ANISOU 1462  CZ  TYR A 181     2786   1527   3164    113    -69    824       C  
ATOM   1463  OH  TYR A 181      -7.468  25.375  10.608  1.00 23.81           O  
ANISOU 1463  OH  TYR A 181     2848   2461   3735   -312     10   1514       O  
ATOM   1464  CE2 TYR A 181      -7.270  24.391  12.777  1.00 18.98           C  
ANISOU 1464  CE2 TYR A 181     2664   1263   3285    -37   -118    642       C  
ATOM   1465  CD2 TYR A 181      -7.392  23.288  13.610  1.00 16.84           C  
ANISOU 1465  CD2 TYR A 181     2425   1309   2661   -289    -99    319       C  
ATOM   1466  C   TYR A 181      -5.604  20.334  13.657  1.00 11.97           C  
ANISOU 1466  C   TYR A 181     2003   1034   1511   -132    143   -167       C  
ATOM   1467  O   TYR A 181      -5.101  20.730  14.702  1.00 12.86           O  
ANISOU 1467  O   TYR A 181     2032   1393   1459   -209    -10    -93       O  
ATOM   1468  N   ILE A 182      -4.988  20.392  12.475  1.00 13.88           N  
ANISOU 1468  N   ILE A 182     2200   1623   1450   -381    164   -216       N  
ATOM   1469  CA  ILE A 182      -3.677  21.004  12.299  1.00 15.22           C  
ANISOU 1469  CA  ILE A 182     2152   1703   1928   -370    269   -224       C  
ATOM   1470  CB  ILE A 182      -2.851  20.338  11.192  1.00 19.17           C  
ANISOU 1470  CB  ILE A 182     2515   2303   2464   -430    719   -387       C  
ATOM   1471  CG1 ILE A 182      -2.695  18.845  11.411  1.00 20.91           C  
ANISOU 1471  CG1 ILE A 182     2444   2210   3290   -719    919   -518       C  
ATOM   1472  CG2 ILE A 182      -1.506  21.030  11.056  1.00 18.18           C  
ANISOU 1472  CG2 ILE A 182     2468   1989   2447   -381    732   -765       C  
ATOM   1473  CD1 ILE A 182      -2.227  18.137  10.197  1.00 25.08           C  
ANISOU 1473  CD1 ILE A 182     3224   3124   3180   -604    839   -504       C  
ATOM   1474  C   ILE A 182      -3.856  22.484  11.968  1.00 15.02           C  
ANISOU 1474  C   ILE A 182     2179   1721   1804   -518    286     -8       C  
ATOM   1475  O   ILE A 182      -4.512  22.834  10.986  1.00 17.68           O  
ANISOU 1475  O   ILE A 182     2495   2355   1864   -463    131     67       O  
ATOM   1476  N   HIS A 183      -3.268  23.348  12.797  1.00 15.11           N  
ANISOU 1476  N   HIS A 183     2392   1370   1979   -314   -102    187       N  
ATOM   1477  CA  HIS A 183      -3.335  24.764  12.541  1.00 16.09           C  
ANISOU 1477  CA  HIS A 183     2625   1441   2046   -343    231    261       C  
ATOM   1478  CB  HIS A 183      -2.748  25.526  13.720  1.00 17.05           C  
ANISOU 1478  CB  HIS A 183     2799   1427   2251   -338    240    -41       C  
ATOM   1479  CG  HIS A 183      -3.430  25.388  15.043  1.00 17.25           C  
ANISOU 1479  CG  HIS A 183     2745   1556   2251   -475    275   -120       C  
ATOM   1480  ND1 HIS A 183      -4.049  24.262  15.535  1.00 19.94           N  
ANISOU 1480  ND1 HIS A 183     2912   2213   2451   -542    322    351       N  
ATOM   1481  CE1 HIS A 183      -4.499  24.522  16.766  1.00 16.90           C  
ANISOU 1481  CE1 HIS A 183     2604   1350   2465   -701    566    769       C  
ATOM   1482  NE2 HIS A 183      -4.115  25.754  17.104  1.00 22.20           N  
ANISOU 1482  NE2 HIS A 183     3447   2149   2837   -636    262    318       N  
ATOM   1483  CD2 HIS A 183      -3.465  26.309  16.038  1.00 16.76           C  
ANISOU 1483  CD2 HIS A 183     2711   1157   2497   -574    214   -235       C  
ATOM   1484  C   HIS A 183      -2.550  25.110  11.283  1.00 16.55           C  
ANISOU 1484  C   HIS A 183     2512   1636   2140   -293    228    349       C  
ATOM   1485  O   HIS A 183      -1.528  24.485  10.983  1.00 17.09           O  
ANISOU 1485  O   HIS A 183     2459   1653   2381   -294    362    393       O  
ATOM   1486  N   PRO A 184      -2.952  26.150  10.532  1.00 20.96           N  
ANISOU 1486  N   PRO A 184     2893   2296   2772   -258    447    969       N  
ATOM   1487  CA  PRO A 184      -2.176  26.575   9.364  1.00 19.77           C  
ANISOU 1487  CA  PRO A 184     2548   2241   2721   -279    353   1011       C  
ATOM   1488  CB  PRO A 184      -2.860  27.888   8.968  1.00 23.79           C  
ANISOU 1488  CB  PRO A 184     3282   2534   3223    -76    303   1282       C  
ATOM   1489  CG  PRO A 184      -4.289  27.678   9.397  1.00 24.68           C  
ANISOU 1489  CG  PRO A 184     3212   2794   3370    105    339   1492       C  
ATOM   1490  CD  PRO A 184      -4.188  26.917  10.707  1.00 23.54           C  
ANISOU 1490  CD  PRO A 184     3225   2636   3080     77    180   1169       C  
ATOM   1491  C   PRO A 184      -0.698  26.805   9.697  1.00 18.77           C  
ANISOU 1491  C   PRO A 184     2598   1938   2593   -292    241    670       C  
ATOM   1492  O   PRO A 184      -0.367  27.328  10.775  1.00 20.42           O  
ANISOU 1492  O   PRO A 184     2819   2198   2741   -483    197    524       O  
ATOM   1493  N   ARG A 185       0.170  26.374   8.781  1.00 19.82           N  
ANISOU 1493  N   ARG A 185     3004   2252   2272   -604    310    239       N  
ATOM   1494  CA  ARG A 185       1.616  26.465   8.934  1.00 19.33           C  
ANISOU 1494  CA  ARG A 185     2829   2001   2512   -491    558    404       C  
ATOM   1495  CB  ARG A 185       2.278  25.143   8.535  1.00 19.50           C  
ANISOU 1495  CB  ARG A 185     2920   1987   2499   -562    605    364       C  
ATOM   1496  CG  ARG A 185       1.879  23.955   9.390  1.00 20.53           C  
ANISOU 1496  CG  ARG A 185     3200   2113   2485   -611    419    515       C  
ATOM   1497  CD  ARG A 185       2.401  22.640   8.844  1.00 21.04           C  
ANISOU 1497  CD  ARG A 185     2794   2281   2918   -511    297    565       C  
ATOM   1498  NE  ARG A 185       3.852  22.531   8.956  1.00 20.83           N  
ANISOU 1498  NE  ARG A 185     2656   1962   3293   -629    330    635       N  
ATOM   1499  CZ  ARG A 185       4.591  21.620   8.338  1.00 18.21           C  
ANISOU 1499  CZ  ARG A 185     2049   2281   2588   -784     96    388       C  
ATOM   1500  NH1 ARG A 185       4.034  20.746   7.499  1.00 20.83           N  
ANISOU 1500  NH1 ARG A 185     2875   2057   2982   -684   -208    391       N  
ATOM   1501  NH2 ARG A 185       5.892  21.576   8.590  1.00 20.73           N  
ANISOU 1501  NH2 ARG A 185     2157   2601   3117   -500   -270    618       N  
ATOM   1502  C   ARG A 185       2.132  27.593   8.045  1.00 21.67           C  
ANISOU 1502  C   ARG A 185     3086   2240   2905   -905    394    567       C  
ATOM   1503  O   ARG A 185       1.800  27.636   6.868  1.00 24.70           O  
ANISOU 1503  O   ARG A 185     3849   2563   2971   -651    463    765       O  
ATOM   1504  N   ALA A 186       2.963  28.478   8.620  1.00 21.33           N  
ANISOU 1504  N   ALA A 186     2895   2097   3110   -657     68    631       N  
ATOM   1505  CA  ALA A 186       3.518  29.604   7.863  1.00 24.90           C  
ANISOU 1505  CA  ALA A 186     2991   2507   3959   -867    393    879       C  
ATOM   1506  CB  ALA A 186       3.895  30.731   8.797  1.00 27.04           C  
ANISOU 1506  CB  ALA A 186     3138   2598   4537   -466    140    590       C  
ATOM   1507  C   ALA A 186       4.731  29.134   7.045  1.00 25.03           C  
ANISOU 1507  C   ALA A 186     3280   2404   3826   -783    696   1090       C  
ATOM   1508  O   ALA A 186       5.416  28.167   7.432  1.00 23.86           O  
ANISOU 1508  O   ALA A 186     3257   2467   3339   -807    595    793       O  
ATOM   1509  N   ALA A 187       5.015  29.834   5.934  1.00 27.77           N  
ANISOU 1509  N   ALA A 187     3554   3065   3929  -1243    627   1226       N  
ATOM   1510  CA  ALA A 187       6.218  29.545   5.184  1.00 30.75           C  
ANISOU 1510  CA  ALA A 187     3856   3666   4161  -1060    565    963       C  
ATOM   1511  CB  ALA A 187       6.331  30.452   3.980  1.00 32.88           C  
ANISOU 1511  CB  ALA A 187     4308   4177   4006  -1024    418   1100       C  
ATOM   1512  C   ALA A 187       7.427  29.708   6.118  1.00 28.54           C  
ANISOU 1512  C   ALA A 187     3573   3366   3902  -1016    644    939       C  
ATOM   1513  O   ALA A 187       7.491  30.645   6.899  1.00 30.74           O  
ANISOU 1513  O   ALA A 187     4019   3138   4520  -1363    844   1186       O  
ATOM   1514  N   GLY A 188       8.353  28.750   6.051  1.00 26.25           N  
ANISOU 1514  N   GLY A 188     3438   3161   3373  -1117    651    819       N  
ATOM   1515  CA  GLY A 188       9.594  28.758   6.813  1.00 24.58           C  
ANISOU 1515  CA  GLY A 188     3107   2968   3262   -982    863    551       C  
ATOM   1516  C   GLY A 188       9.440  28.259   8.244  1.00 23.79           C  
ANISOU 1516  C   GLY A 188     3111   2735   3194   -969    621    478       C  
ATOM   1517  O   GLY A 188      10.423  28.206   8.986  1.00 25.44           O  
ANISOU 1517  O   GLY A 188     3149   3197   3318  -1082    425    450       O  
ATOM   1518  N   SER A 189       8.225  27.884   8.647  1.00 22.82           N  
ANISOU 1518  N   SER A 189     3159   2506   3005  -1020    743    215       N  
ATOM   1519  CA  SER A 189       7.988  27.532  10.050  1.00 22.49           C  
ANISOU 1519  CA  SER A 189     3184   2289   3071   -700    452    507       C  
ATOM   1520  CB  SER A 189       6.517  27.487  10.390  1.00 22.68           C  
ANISOU 1520  CB  SER A 189     3236   2401   2978   -672    361    147       C  
ATOM   1521  OG  SER A 189       5.827  26.570   9.561  1.00 24.80           O  
ANISOU 1521  OG  SER A 189     3342   2662   3416   -901    546   -236       O  
ATOM   1522  C   SER A 189       8.683  26.206  10.398  1.00 21.46           C  
ANISOU 1522  C   SER A 189     3102   1921   3131   -766    798    289       C  
ATOM   1523  O   SER A 189       8.880  25.340   9.536  1.00 22.29           O  
ANISOU 1523  O   SER A 189     2802   2208   3458   -870    844    105       O  
ATOM   1524  N   THR A 190       9.084  26.102  11.664  1.00 20.83           N  
ANISOU 1524  N   THR A 190     2617   2198   3098   -442    854    182       N  
ATOM   1525  CA  THR A 190       9.751  24.953  12.223  1.00 19.06           C  
ANISOU 1525  CA  THR A 190     2253   1879   3109   -428    851    -97       C  
ATOM   1526  CB  THR A 190      11.149  25.351  12.714  1.00 18.98           C  
ANISOU 1526  CB  THR A 190     2243   1594   3374   -623    865   -272       C  
ATOM   1527  OG1 THR A 190      11.036  26.387  13.704  1.00 21.84           O  
ANISOU 1527  OG1 THR A 190     2954   1870   3474   -496    998   -437       O  
ATOM   1528  CG2 THR A 190      12.036  25.816  11.577  1.00 21.16           C  
ANISOU 1528  CG2 THR A 190     2465   1921   3651   -768   1014   -122       C  
ATOM   1529  C   THR A 190       8.956  24.345  13.382  1.00 18.38           C  
ANISOU 1529  C   THR A 190     2252   1765   2967   -495    571     14       C  
ATOM   1530  O   THR A 190       9.476  23.566  14.173  1.00 17.08           O  
ANISOU 1530  O   THR A 190     2030   1802   2654   -514    431   -261       O  
ATOM   1531  N   SER A 191       7.668  24.650  13.432  1.00 19.22           N  
ANISOU 1531  N   SER A 191     2334   1974   2994   -444    727    635       N  
ATOM   1532  CA  SER A 191       6.790  24.166  14.465  1.00 17.91           C  
ANISOU 1532  CA  SER A 191     2216   1921   2668   -330    656    378       C  
ATOM   1533  CB  SER A 191       6.710  25.136  15.616  1.00 19.60           C  
ANISOU 1533  CB  SER A 191     2829   1822   2796   -557    553    416       C  
ATOM   1534  OG  SER A 191       6.200  26.365  15.158  1.00 23.74           O  
ANISOU 1534  OG  SER A 191     3497   1991   3529   -280    383    328       O  
ATOM   1535  C   SER A 191       5.409  23.918  13.873  1.00 17.76           C  
ANISOU 1535  C   SER A 191     2425   1933   2391   -380    453    380       C  
ATOM   1536  O   SER A 191       5.054  24.490  12.844  1.00 20.15           O  
ANISOU 1536  O   SER A 191     2630   2692   2332   -649    235    545       O  
ATOM   1537  N   VAL A 192       4.648  23.066  14.557  1.00 15.54           N  
ANISOU 1537  N   VAL A 192     2176   1653   2075   -339    343    100       N  
ATOM   1538  CA  VAL A 192       3.254  22.806  14.186  1.00 15.49           C  
ANISOU 1538  CA  VAL A 192     2176   1727   1982   -284    393    143       C  
ATOM   1539  CB  VAL A 192       3.130  21.519  13.346  1.00 17.35           C  
ANISOU 1539  CB  VAL A 192     2517   1953   2121   -485    269    -39       C  
ATOM   1540  CG1 VAL A 192       3.544  20.299  14.132  1.00 16.08           C  
ANISOU 1540  CG1 VAL A 192     2359   2005   1743   -442    372   -104       C  
ATOM   1541  CG2 VAL A 192       1.755  21.336  12.739  1.00 20.44           C  
ANISOU 1541  CG2 VAL A 192     2672   2618   2474   -518    412    -21       C  
ATOM   1542  C   VAL A 192       2.421  22.764  15.459  1.00 14.86           C  
ANISOU 1542  C   VAL A 192     2298   1420   1928   -373    339     14       C  
ATOM   1543  O   VAL A 192       2.928  22.348  16.500  1.00 15.67           O  
ANISOU 1543  O   VAL A 192     2127   1991   1833   -225    310     35       O  
ATOM   1544  N   LYS A 193       1.159  23.185  15.343  1.00 14.44           N  
ANISOU 1544  N   LYS A 193     2205   1586   1692   -301    315    -18       N  
ATOM   1545  CA  LYS A 193       0.180  23.057  16.420  1.00 13.90           C  
ANISOU 1545  CA  LYS A 193     1952   1462   1866   -507    309    -49       C  
ATOM   1546  CB  LYS A 193      -0.424  24.397  16.829  1.00 15.43           C  
ANISOU 1546  CB  LYS A 193     2081   1535   2248   -454    143   -222       C  
ATOM   1547  CG  LYS A 193       0.494  25.260  17.679  1.00 18.23           C  
ANISOU 1547  CG  LYS A 193     2326   2031   2569   -399   -214   -397       C  
ATOM   1548  CD  LYS A 193      -0.147  26.554  18.108  1.00 20.89           C  
ANISOU 1548  CD  LYS A 193     2676   2242   3018     21   -368   -598       C  
ATOM   1549  CE  LYS A 193       0.771  27.404  18.939  1.00 25.91           C  
ANISOU 1549  CE  LYS A 193     2796   3061   3987   -100   -743   -807       C  
ATOM   1550  NZ  LYS A 193       0.171  28.729  19.230  1.00 30.27           N  
ANISOU 1550  NZ  LYS A 193     3456   3464   4581    318   -631  -1059       N  
ATOM   1551  C   LYS A 193      -0.951  22.142  15.957  1.00 14.05           C  
ANISOU 1551  C   LYS A 193     2010   1495   1831   -430     18    -40       C  
ATOM   1552  O   LYS A 193      -1.497  22.345  14.877  1.00 14.82           O  
ANISOU 1552  O   LYS A 193     2365   1586   1681   -351    231     61       O  
ATOM   1553  N   ILE A 194      -1.285  21.145  16.796  1.00 12.60           N  
ANISOU 1553  N   ILE A 194     1888   1388   1510   -249     24   -163       N  
ATOM   1554  CA  ILE A 194      -2.309  20.177  16.472  1.00 12.84           C  
ANISOU 1554  CA  ILE A 194     1736   1436   1703   -174     86   -131       C  
ATOM   1555  CB  ILE A 194      -1.705  18.807  16.104  1.00 13.89           C  
ANISOU 1555  CB  ILE A 194     1939   1531   1805    -58    -61   -133       C  
ATOM   1556  CG1 ILE A 194      -0.611  18.964  15.048  1.00 14.94           C  
ANISOU 1556  CG1 ILE A 194     1931   1768   1974   -207      6   -200       C  
ATOM   1557  CG2 ILE A 194      -2.792  17.844  15.658  1.00 14.56           C  
ANISOU 1557  CG2 ILE A 194     2149   1540   1840   -214     84    -62       C  
ATOM   1558  CD1 ILE A 194       0.151  17.712  14.749  1.00 17.63           C  
ANISOU 1558  CD1 ILE A 194     2297   1699   2701   -224    -28   -240       C  
ATOM   1559  C   ILE A 194      -3.253  20.057  17.662  1.00 12.59           C  
ANISOU 1559  C   ILE A 194     2020   1191   1569   -309    111    -20       C  
ATOM   1560  O   ILE A 194      -2.804  19.795  18.780  1.00 13.86           O  
ANISOU 1560  O   ILE A 194     2318   1418   1528   -335     10   -161       O  
ATOM   1561  N   ASP A 195      -4.544  20.222  17.397  1.00 11.38           N  
ANISOU 1561  N   ASP A 195     1931   1074   1318   -260    278     17       N  
ATOM   1562  CA  ASP A 195      -5.570  19.931  18.364  1.00 12.13           C  
ANISOU 1562  CA  ASP A 195     1869   1262   1475   -453    261    -94       C  
ATOM   1563  CB  ASP A 195      -6.834  20.749  18.084  1.00 12.78           C  
ANISOU 1563  CB  ASP A 195     1866   1465   1523   -309    283    -53       C  
ATOM   1564  CG  ASP A 195      -6.628  22.248  17.971  1.00 13.69           C  
ANISOU 1564  CG  ASP A 195     2237   1484   1481   -232    289    -39       C  
ATOM   1565  OD1 ASP A 195      -5.629  22.785  18.538  1.00 15.23           O  
ANISOU 1565  OD1 ASP A 195     2255   1369   2162   -165    294   -306       O  
ATOM   1566  OD2 ASP A 195      -7.455  22.874  17.315  1.00 18.07           O  
ANISOU 1566  OD2 ASP A 195     2633   1602   2627   -101   -195     86       O  
ATOM   1567  C   ASP A 195      -5.927  18.445  18.268  1.00 12.40           C  
ANISOU 1567  C   ASP A 195     1967   1337   1406   -558    292   -174       C  
ATOM   1568  O   ASP A 195      -6.026  17.904  17.165  1.00 13.13           O  
ANISOU 1568  O   ASP A 195     2200   1382   1403   -451    139   -139       O  
ATOM   1569  N   PHE A 196      -6.103  17.816  19.436  1.00 11.96           N  
ANISOU 1569  N   PHE A 196     1887   1361   1294   -420    288   -223       N  
ATOM   1570  CA  PHE A 196      -6.509  16.422  19.548  1.00 12.57           C  
ANISOU 1570  CA  PHE A 196     2018   1331   1424   -323    287   -125       C  
ATOM   1571  CB  PHE A 196      -5.370  15.606  20.169  1.00 12.77           C  
ANISOU 1571  CB  PHE A 196     2067   1299   1483   -369    152    -86       C  
ATOM   1572  CG  PHE A 196      -4.116  15.458  19.336  1.00 12.56           C  
ANISOU 1572  CG  PHE A 196     2015   1351   1403   -363     48   -238       C  
ATOM   1573  CD1 PHE A 196      -3.975  14.399  18.452  1.00 12.50           C  
ANISOU 1573  CD1 PHE A 196     2077   1325   1345   -385    126   -175       C  
ATOM   1574  CE1 PHE A 196      -2.818  14.223  17.727  1.00 12.74           C  
ANISOU 1574  CE1 PHE A 196     1952   1385   1501   -264     -4   -179       C  
ATOM   1575  CZ  PHE A 196      -1.780  15.104  17.864  1.00 13.52           C  
ANISOU 1575  CZ  PHE A 196     2094   1546   1495   -407    148   -221       C  
ATOM   1576  CD2 PHE A 196      -3.061  16.345  19.458  1.00 12.83           C  
ANISOU 1576  CD2 PHE A 196     2055   1186   1632   -285     83   -183       C  
ATOM   1577  CE2 PHE A 196      -1.902  16.172  18.721  1.00 13.11           C  
ANISOU 1577  CE2 PHE A 196     1923   1470   1586   -633     34   -299       C  
ATOM   1578  C   PHE A 196      -7.718  16.285  20.469  1.00 12.41           C  
ANISOU 1578  C   PHE A 196     1942   1209   1563   -351    221   -229       C  
ATOM   1579  O   PHE A 196      -7.833  17.042  21.453  1.00 12.89           O  
ANISOU 1579  O   PHE A 196     2301   1162   1432   -330    127   -185       O  
ATOM   1580  N   VAL A 197      -8.563  15.286  20.175  1.00 11.90           N  
ANISOU 1580  N   VAL A 197     1994   1218   1309   -364    126   -264       N  
ATOM   1581  CA  VAL A 197      -9.598  14.830  21.096  1.00 13.22           C  
ANISOU 1581  CA  VAL A 197     2222   1360   1440   -448    195   -159       C  
ATOM   1582  CB  VAL A 197     -11.001  15.268  20.687  1.00 14.25           C  
ANISOU 1582  CB  VAL A 197     2347   1521   1544   -267    183   -131       C  
ATOM   1583  CG1 VAL A 197     -12.043  14.814  21.697  1.00 14.63           C  
ANISOU 1583  CG1 VAL A 197     2079   1911   1567   -314     59   -337       C  
ATOM   1584  CG2 VAL A 197     -11.059  16.767  20.476  1.00 15.78           C  
ANISOU 1584  CG2 VAL A 197     2620   1559   1814   -115    196   -166       C  
ATOM   1585  C   VAL A 197      -9.533  13.300  21.114  1.00 12.55           C  
ANISOU 1585  C   VAL A 197     2056   1281   1429   -492    229   -194       C  
ATOM   1586  O   VAL A 197      -9.597  12.670  20.045  1.00 14.01           O  
ANISOU 1586  O   VAL A 197     2662   1219   1440   -259    422   -168       O  
ATOM   1587  N   VAL A 198      -9.427  12.711  22.308  1.00 12.18           N  
ANISOU 1587  N   VAL A 198     2041   1187   1398   -376    281   -232       N  
ATOM   1588  CA  VAL A 198      -9.392  11.257  22.469  1.00 12.46           C  
ANISOU 1588  CA  VAL A 198     2084   1164   1485   -259    372   -313       C  
ATOM   1589  CB  VAL A 198      -7.976  10.761  22.852  1.00 14.66           C  
ANISOU 1589  CB  VAL A 198     2290   1442   1837     54    413   -292       C  
ATOM   1590  CG1 VAL A 198      -7.959   9.274  23.167  1.00 14.81           C  
ANISOU 1590  CG1 VAL A 198     2392   1436   1796     50    311   -304       C  
ATOM   1591  CG2 VAL A 198      -6.989  11.067  21.756  1.00 17.58           C  
ANISOU 1591  CG2 VAL A 198     2436   2109   2132    158    539   -108       C  
ATOM   1592  C   VAL A 198     -10.388  10.845  23.549  1.00 11.51           C  
ANISOU 1592  C   VAL A 198     2030    977   1364    -53    353   -175       C  
ATOM   1593  O   VAL A 198     -10.358  11.417  24.646  1.00 12.97           O  
ANISOU 1593  O   VAL A 198     2259   1119   1549   -305    264   -318       O  
ATOM   1594  N   ASP A 199     -11.194   9.821  23.254  1.00 11.35           N  
ANISOU 1594  N   ASP A 199     2131   1096   1083   -128    312   -134       N  
ATOM   1595  CA  ASP A 199     -12.183   9.242  24.226  1.00 11.59           C  
ANISOU 1595  CA  ASP A 199     2234   1068   1099     91    390    -55       C  
ATOM   1596  CB  ASP A 199     -13.597   9.409  23.666  1.00 14.14           C  
ANISOU 1596  CB  ASP A 199     2198   1388   1785     62    276     68       C  
ATOM   1597  CG  ASP A 199     -14.755   8.925  24.496  1.00 15.08           C  
ANISOU 1597  CG  ASP A 199     2233   1758   1736    200    270    -90       C  
ATOM   1598  OD1 ASP A 199     -14.514   8.087  25.360  1.00 17.04           O  
ANISOU 1598  OD1 ASP A 199     2546   1838   2089    -44    139    167       O  
ATOM   1599  OD2 ASP A 199     -15.932   9.404  24.247  1.00 18.32           O  
ANISOU 1599  OD2 ASP A 199     2333   2228   2398    514     89    -93       O  
ATOM   1600  C   ASP A 199     -11.796   7.781  24.458  1.00 12.46           C  
ANISOU 1600  C   ASP A 199     2393    987   1354     25    207   -221       C  
ATOM   1601  O   ASP A 199     -11.974   6.976  23.546  1.00 14.59           O  
ANISOU 1601  O   ASP A 199     3056   1110   1375    -33    181   -268       O  
ATOM   1602  N   GLU A 200     -11.226   7.473  25.626  1.00 11.51           N  
ANISOU 1602  N   GLU A 200     1983   1022   1365    -64    115   -368       N  
ATOM   1603  CA  GLU A 200     -10.580   6.193  25.923  1.00 10.42           C  
ANISOU 1603  CA  GLU A 200     1646   1173   1140    -77    154   -312       C  
ATOM   1604  CB  GLU A 200      -9.062   6.420  26.009  1.00 11.72           C  
ANISOU 1604  CB  GLU A 200     1678   1316   1459   -153    100   -205       C  
ATOM   1605  CG  GLU A 200      -8.242   5.181  26.326  1.00 11.68           C  
ANISOU 1605  CG  GLU A 200     1742   1368   1325   -122     49   -143       C  
ATOM   1606  CD  GLU A 200      -6.748   5.343  26.060  1.00 11.95           C  
ANISOU 1606  CD  GLU A 200     1726   1406   1405    -30     89   -169       C  
ATOM   1607  OE1 GLU A 200      -6.403   5.965  25.036  1.00 12.98           O  
ANISOU 1607  OE1 GLU A 200     1831   1585   1515   -148     28     19       O  
ATOM   1608  OE2 GLU A 200      -5.927   4.888  26.895  1.00 11.88           O  
ANISOU 1608  OE2 GLU A 200     1747   1427   1339   -147    -15   -276       O  
ATOM   1609  C   GLU A 200     -11.137   5.645  27.245  1.00 10.50           C  
ANISOU 1609  C   GLU A 200     1660   1147   1181   -147    147   -229       C  
ATOM   1610  O   GLU A 200     -11.299   6.394  28.227  1.00 10.90           O  
ANISOU 1610  O   GLU A 200     1883   1105   1151     34     71   -214       O  
ATOM   1611  N   ALA A 201     -11.443   4.346  27.277  1.00 10.26           N  
ANISOU 1611  N   ALA A 201     1743   1138   1018   -136    161   -264       N  
ATOM   1612  CA  ALA A 201     -11.915   3.715  28.527  1.00 10.71           C  
ANISOU 1612  CA  ALA A 201     1737   1247   1084   -123    205   -164       C  
ATOM   1613  CB  ALA A 201     -12.305   2.267  28.282  1.00 11.23           C  
ANISOU 1613  CB  ALA A 201     1837   1271   1157   -305    315     81       C  
ATOM   1614  C   ALA A 201     -10.814   3.779  29.588  1.00 10.29           C  
ANISOU 1614  C   ALA A 201     1635   1091   1181   -132    212    -99       C  
ATOM   1615  O   ALA A 201      -9.659   3.516  29.297  1.00 11.07           O  
ANISOU 1615  O   ALA A 201     1600   1533   1074    -96    150   -156       O  
ATOM   1616  N   LEU A 202     -11.210   4.073  30.835  1.00 10.51           N  
ANISOU 1616  N   LEU A 202     1523   1239   1231    -39    196   -161       N  
ATOM   1617  CA  LEU A 202     -10.263   4.076  31.957  1.00 10.71           C  
ANISOU 1617  CA  LEU A 202     1763   1088   1218    -53    115   -109       C  
ATOM   1618  CB  LEU A 202     -10.856   4.880  33.116  1.00 11.11           C  
ANISOU 1618  CB  LEU A 202     1750   1083   1387    -89    142   -179       C  
ATOM   1619  CG  LEU A 202     -10.054   4.870  34.413  1.00 12.23           C  
ANISOU 1619  CG  LEU A 202     2027   1256   1364     89    108   -124       C  
ATOM   1620  CD1 LEU A 202      -8.658   5.442  34.219  1.00 12.39           C  
ANISOU 1620  CD1 LEU A 202     2130   1296   1279     23      0   -156       C  
ATOM   1621  CD2 LEU A 202     -10.813   5.630  35.476  1.00 13.79           C  
ANISOU 1621  CD2 LEU A 202     2097   1671   1468     71    109   -300       C  
ATOM   1622  C   LEU A 202      -9.989   2.640  32.398  1.00 10.48           C  
ANISOU 1622  C   LEU A 202     1666   1085   1232    -86    174   -103       C  
ATOM   1623  O   LEU A 202     -10.940   1.857  32.653  1.00 11.34           O  
ANISOU 1623  O   LEU A 202     1638   1261   1410    -79    167    -82       O  
ATOM   1624  N   VAL A 203      -8.700   2.293  32.483  1.00 10.75           N  
ANISOU 1624  N   VAL A 203     1701   1168   1215   -114     99    -30       N  
ATOM   1625  CA  VAL A 203      -8.238   0.984  32.930  1.00 11.10           C  
ANISOU 1625  CA  VAL A 203     1667   1306   1244     38     70    -16       C  
ATOM   1626  CB  VAL A 203      -7.123   0.469  32.008  1.00 11.96           C  
ANISOU 1626  CB  VAL A 203     1940   1359   1243    154     52   -133       C  
ATOM   1627  CG1 VAL A 203      -6.556  -0.864  32.493  1.00 13.13           C  
ANISOU 1627  CG1 VAL A 203     2092   1315   1582     44    -67    -59       C  
ATOM   1628  CG2 VAL A 203      -7.627   0.351  30.573  1.00 12.36           C  
ANISOU 1628  CG2 VAL A 203     1936   1323   1436    100   -164   -186       C  
ATOM   1629  C   VAL A 203      -7.797   1.103  34.386  1.00 11.18           C  
ANISOU 1629  C   VAL A 203     1597   1451   1200    144    215   -181       C  
ATOM   1630  O   VAL A 203      -6.642   1.416  34.684  1.00 13.14           O  
ANISOU 1630  O   VAL A 203     1733   1825   1433    130    144   -229       O  
ATOM   1631  N   ALA A 204      -8.768   0.902  35.283  1.00 11.39           N  
ANISOU 1631  N   ALA A 204     1520   1661   1147      5    138   -190       N  
ATOM   1632  CA  ALA A 204      -8.542   1.103  36.722  1.00 11.40           C  
ANISOU 1632  CA  ALA A 204     1671   1491   1167     34      0    -95       C  
ATOM   1633  CB  ALA A 204      -8.614   2.561  37.096  1.00 11.57           C  
ANISOU 1633  CB  ALA A 204     1561   1571   1262    -63     27   -215       C  
ATOM   1634  C   ALA A 204      -9.606   0.335  37.498  1.00 11.96           C  
ANISOU 1634  C   ALA A 204     1758   1564   1222    140    104     36       C  
ATOM   1635  O   ALA A 204     -10.783   0.527  37.267  1.00 12.82           O  
ANISOU 1635  O   ALA A 204     1773   1512   1584     -3    -36     78       O  
ATOM   1636  N   ASN A 205      -9.180  -0.514  38.433  1.00 12.03           N  
ANISOU 1636  N   ASN A 205     1812   1451   1306    145     47     70       N  
ATOM   1637  CA  ASN A 205     -10.137  -1.274  39.227  1.00 12.46           C  
ANISOU 1637  CA  ASN A 205     1933   1612   1188    233    223    -26       C  
ATOM   1638  CB  ASN A 205      -9.403  -2.058  40.309  1.00 13.62           C  
ANISOU 1638  CB  ASN A 205     2222   1701   1251    465    325    131       C  
ATOM   1639  CG  ASN A 205      -8.456  -3.119  39.777  1.00 15.77           C  
ANISOU 1639  CG  ASN A 205     2571   1716   1705    576    404     16       C  
ATOM   1640  OD1 ASN A 205      -7.573  -2.805  38.974  1.00 19.12           O  
ANISOU 1640  OD1 ASN A 205     2678   2428   2157    180    385    106       O  
ATOM   1641  ND2 ASN A 205      -8.589  -4.335  40.280  1.00 14.88           N  
ANISOU 1641  ND2 ASN A 205     2383   1695   1573    317   -157    115       N  
ATOM   1642  C   ASN A 205     -11.169  -0.336  39.854  1.00 11.47           C  
ANISOU 1642  C   ASN A 205     1781   1479   1099    135     85   -111       C  
ATOM   1643  O   ASN A 205     -10.793   0.701  40.389  1.00 12.66           O  
ANISOU 1643  O   ASN A 205     1730   1582   1497    -15     72   -258       O  
ATOM   1644  N   PRO A 206     -12.479  -0.666  39.805  1.00 11.98           N  
ANISOU 1644  N   PRO A 206     1854   1436   1259    109    203   -169       N  
ATOM   1645  CA  PRO A 206     -13.090  -1.905  39.339  1.00 12.40           C  
ANISOU 1645  CA  PRO A 206     1838   1388   1483    152    291   -130       C  
ATOM   1646  CB  PRO A 206     -14.213  -2.072  40.382  1.00 13.63           C  
ANISOU 1646  CB  PRO A 206     2033   1586   1558    159    409      3       C  
ATOM   1647  CG  PRO A 206     -14.714  -0.650  40.594  1.00 13.77           C  
ANISOU 1647  CG  PRO A 206     1989   1565   1679    206    333     87       C  
ATOM   1648  CD  PRO A 206     -13.438   0.157  40.554  1.00 12.49           C  
ANISOU 1648  CD  PRO A 206     1944   1525   1277    168    364    -14       C  
ATOM   1649  C   PRO A 206     -13.709  -1.816  37.932  1.00 11.75           C  
ANISOU 1649  C   PRO A 206     1661   1288   1512     -8    167   -190       C  
ATOM   1650  O   PRO A 206     -14.621  -2.570  37.605  1.00 12.29           O  
ANISOU 1650  O   PRO A 206     1764   1368   1535     44     91   -317       O  
ATOM   1651  N   THR A 207     -13.208  -0.910  37.082  1.00 11.67           N  
ANISOU 1651  N   THR A 207     1768   1289   1376    -31     55   -239       N  
ATOM   1652  CA  THR A 207     -13.829  -0.742  35.784  1.00 11.35           C  
ANISOU 1652  CA  THR A 207     1517   1408   1388    -76     95   -203       C  
ATOM   1653  CB  THR A 207     -13.278   0.415  34.949  1.00 11.80           C  
ANISOU 1653  CB  THR A 207     1745   1416   1319   -107    -23   -115       C  
ATOM   1654  OG1 THR A 207     -11.962   0.097  34.487  1.00 12.62           O  
ANISOU 1654  OG1 THR A 207     1818   1502   1474    -87    239    -89       O  
ATOM   1655  CG2 THR A 207     -13.303   1.741  35.675  1.00 12.39           C  
ANISOU 1655  CG2 THR A 207     1718   1375   1614   -290    -36   -187       C  
ATOM   1656  C   THR A 207     -13.743  -2.038  34.961  1.00 11.29           C  
ANISOU 1656  C   THR A 207     1561   1287   1441    -72    113   -144       C  
ATOM   1657  O   THR A 207     -12.821  -2.859  35.078  1.00 12.23           O  
ANISOU 1657  O   THR A 207     1815   1300   1528     51     44   -148       O  
ATOM   1658  N   GLN A 208     -14.743  -2.198  34.099  1.00 11.11           N  
ANISOU 1658  N   GLN A 208     1693   1221   1305   -114    116   -156       N  
ATOM   1659  CA  GLN A 208     -14.948  -3.419  33.329  1.00 11.64           C  
ANISOU 1659  CA  GLN A 208     1886   1192   1341     15    170   -195       C  
ATOM   1660  CB  GLN A 208     -16.434  -3.754  33.325  1.00 12.89           C  
ANISOU 1660  CB  GLN A 208     1943   1452   1503    -84    253   -150       C  
ATOM   1661  CG  GLN A 208     -16.978  -4.023  34.723  1.00 12.40           C  
ANISOU 1661  CG  GLN A 208     2022   1259   1429   -167     80    -64       C  
ATOM   1662  CD  GLN A 208     -16.354  -5.243  35.347  1.00 13.26           C  
ANISOU 1662  CD  GLN A 208     2048   1427   1562   -132    -60    -85       C  
ATOM   1663  OE1 GLN A 208     -16.687  -6.344  34.925  1.00 14.83           O  
ANISOU 1663  OE1 GLN A 208     2306   1386   1940   -295   -268     -3       O  
ATOM   1664  NE2 GLN A 208     -15.451  -5.087  36.318  1.00 14.01           N  
ANISOU 1664  NE2 GLN A 208     2100   1769   1452   -491     24      9       N  
ATOM   1665  C   GLN A 208     -14.322  -3.245  31.932  1.00 11.91           C  
ANISOU 1665  C   GLN A 208     1736   1580   1208     38     19   -124       C  
ATOM   1666  O   GLN A 208     -14.976  -3.467  30.900  1.00 12.31           O  
ANISOU 1666  O   GLN A 208     1843   1518   1313      9    -84   -363       O  
ATOM   1667  N   TYR A 209     -13.019  -2.920  31.915  1.00 13.31           N  
ANISOU 1667  N   TYR A 209     1895   1737   1422    -37    208     68       N  
ATOM   1668  CA  TYR A 209     -12.309  -2.583  30.697  1.00 13.09           C  
ANISOU 1668  CA  TYR A 209     1897   1787   1289     31    186    -31       C  
ATOM   1669  CB  TYR A 209     -10.999  -1.851  31.017  1.00 13.72           C  
ANISOU 1669  CB  TYR A 209     1918   1805   1489      8    281   -137       C  
ATOM   1670  CG  TYR A 209     -10.040  -2.657  31.853  1.00 13.99           C  
ANISOU 1670  CG  TYR A 209     2089   1781   1446     24    146   -111       C  
ATOM   1671  CD1 TYR A 209      -9.151  -3.555  31.282  1.00 14.76           C  
ANISOU 1671  CD1 TYR A 209     2034   2157   1417    -30    249   -247       C  
ATOM   1672  CE1 TYR A 209      -8.308  -4.334  32.066  1.00 15.37           C  
ANISOU 1672  CE1 TYR A 209     2156   2016   1667    122    204   -218       C  
ATOM   1673  CZ  TYR A 209      -8.323  -4.208  33.438  1.00 14.26           C  
ANISOU 1673  CZ  TYR A 209     1879   1892   1644    128    194   -114       C  
ATOM   1674  OH  TYR A 209      -7.479  -4.980  34.216  1.00 16.82           O  
ANISOU 1674  OH  TYR A 209     2497   2331   1559    361     75    146       O  
ATOM   1675  CE2 TYR A 209      -9.184  -3.292  34.016  1.00 13.52           C  
ANISOU 1675  CE2 TYR A 209     2117   1771   1249     11    142   -322       C  
ATOM   1676  CD2 TYR A 209     -10.029  -2.530  33.228  1.00 14.26           C  
ANISOU 1676  CD2 TYR A 209     2219   1765   1435     10    256   -168       C  
ATOM   1677  C   TYR A 209     -12.049  -3.808  29.800  1.00 13.82           C  
ANISOU 1677  C   TYR A 209     1879   1920   1450   -183    413   -187       C  
ATOM   1678  O   TYR A 209     -11.543  -3.661  28.660  1.00 17.59           O  
ANISOU 1678  O   TYR A 209     2710   2569   1403   -449    538   -354       O  
ATOM   1679  N   LYS A 210     -12.308  -5.020  30.300  1.00 15.31           N  
ANISOU 1679  N   LYS A 210     2071   1820   1926     35    526   -180       N  
ATOM   1680  CA  LYS A 210     -12.159  -6.234  29.496  1.00 18.78           C  
ANISOU 1680  CA  LYS A 210     2698   2368   2069    -25    506   -552       C  
ATOM   1681  CB  LYS A 210     -11.709  -7.381  30.398  1.00 20.83           C  
ANISOU 1681  CB  LYS A 210     2691   2347   2874    217    583   -465       C  
ATOM   1682  CG  LYS A 210     -10.319  -7.200  30.985  1.00 24.86           C  
ANISOU 1682  CG  LYS A 210     2991   2792   3660    213    237   -288       C  
ATOM   1683  CD  LYS A 210     -10.032  -8.053  32.221  1.00 28.02           C  
ANISOU 1683  CD  LYS A 210     3205   3288   4151    180    -53    -28       C  
ATOM   1684  CE  LYS A 210     -10.213  -9.540  32.035  1.00 27.33           C  
ANISOU 1684  CE  LYS A 210     3103   3268   4013     41    177   -295       C  
ATOM   1685  NZ  LYS A 210      -9.082 -10.155  31.315  1.00 30.65           N  
ANISOU 1685  NZ  LYS A 210     3398   3546   4699    218    451   -210       N  
ATOM   1686  C   LYS A 210     -13.454  -6.573  28.753  1.00 18.12           C  
ANISOU 1686  C   LYS A 210     2582   2095   2205    109    482   -633       C  
ATOM   1687  O   LYS A 210     -13.441  -7.495  27.914  1.00 22.68           O  
ANISOU 1687  O   LYS A 210     3608   2573   2435    880     72   -966       O  
ATOM   1688  N   ASN A 211     -14.547  -5.849  29.047  1.00 16.27           N  
ANISOU 1688  N   ASN A 211     2491   1769   1922   -175    687   -792       N  
ATOM   1689  CA  ASN A 211     -15.851  -6.128  28.507  1.00 17.56           C  
ANISOU 1689  CA  ASN A 211     2845   1962   1864   -292     73   -836       C  
ATOM   1690  CB  ASN A 211     -16.730  -6.846  29.540  1.00 21.47           C  
ANISOU 1690  CB  ASN A 211     2819   2590   2748   -771     59   -465       C  
ATOM   1691  CG  ASN A 211     -16.198  -8.189  29.999  1.00 29.12           C  
ANISOU 1691  CG  ASN A 211     4243   3223   3598   -200   -496   -490       C  
ATOM   1692  OD1 ASN A 211     -16.534  -9.222  29.418  1.00 39.11           O  
ANISOU 1692  OD1 ASN A 211     6295   3793   4772   -779   -257  -1088       O  
ATOM   1693  ND2 ASN A 211     -15.406  -8.194  31.058  1.00 30.18           N  
ANISOU 1693  ND2 ASN A 211     4273   3736   3456   -417   -307   -292       N  
ATOM   1694  C   ASN A 211     -16.538  -4.826  28.079  1.00 17.42           C  
ANISOU 1694  C   ASN A 211     2623   2152   1844   -283    455   -539       C  
ATOM   1695  O   ASN A 211     -17.603  -4.511  28.554  1.00 18.48           O  
ANISOU 1695  O   ASN A 211     2470   2631   1920    146    280   -332       O  
ATOM   1696  N   ILE A 212     -15.920  -4.086  27.151  1.00 15.60           N  
ANISOU 1696  N   ILE A 212     2230   1800   1898    -51    441   -408       N  
ATOM   1697  CA  ILE A 212     -16.397  -2.749  26.817  1.00 17.58           C  
ANISOU 1697  CA  ILE A 212     2866   1848   1965    -18    270   -292       C  
ATOM   1698  CB  ILE A 212     -15.294  -1.970  26.094  1.00 20.21           C  
ANISOU 1698  CB  ILE A 212     3001   2020   2658   -167    337   -264       C  
ATOM   1699  CG1 ILE A 212     -14.177  -1.670  27.106  1.00 24.32           C  
ANISOU 1699  CG1 ILE A 212     3129   2856   3254   -169     21     53       C  
ATOM   1700  CG2 ILE A 212     -15.846  -0.698  25.464  1.00 20.25           C  
ANISOU 1700  CG2 ILE A 212     3106   2118   2469   -128    492   -256       C  
ATOM   1701  CD1 ILE A 212     -12.871  -1.360  26.506  1.00 26.92           C  
ANISOU 1701  CD1 ILE A 212     3612   2996   3618   -477    361    312       C  
ATOM   1702  C   ILE A 212     -17.729  -2.785  26.054  1.00 16.26           C  
ANISOU 1702  C   ILE A 212     2477   1920   1779   -131    571    -36       C  
ATOM   1703  O   ILE A 212     -18.549  -1.870  26.190  1.00 16.93           O  
ANISOU 1703  O   ILE A 212     2605   2003   1821    -26    283   -283       O  
ATOM   1704  N   LYS A 213     -17.988  -3.816  25.256  1.00 19.59           N  
ANISOU 1704  N   LYS A 213     2974   2632   1834   -788    604   -115       N  
ATOM   1705  CA  LYS A 213     -19.245  -3.822  24.493  1.00 21.55           C  
ANISOU 1705  CA  LYS A 213     3246   3131   1809   -951    430    -94       C  
ATOM   1706  CB  LYS A 213     -19.282  -4.948  23.456  1.00 26.32           C  
ANISOU 1706  CB  LYS A 213     4084   3290   2626  -1200    419   -557       C  
ATOM   1707  CG  LYS A 213     -20.555  -4.963  22.603  1.00 34.00           C  
ANISOU 1707  CG  LYS A 213     4537   4550   3829  -1024     -1   -713       C  
ATOM   1708  CD  LYS A 213     -20.840  -6.287  21.889  1.00 42.40           C  
ANISOU 1708  CD  LYS A 213     6087   4834   5190  -1169    -72  -1091       C  
ATOM   1709  CE  LYS A 213     -22.126  -6.963  22.345  1.00 48.38           C  
ANISOU 1709  CE  LYS A 213     6053   5924   6404  -1416     -1   -835       C  
ATOM   1710  NZ  LYS A 213     -22.220  -8.367  21.877  1.00 55.64           N  
ANISOU 1710  NZ  LYS A 213     7032   6134   7973  -1031   -171   -917       N  
ATOM   1711  C   LYS A 213     -20.435  -3.965  25.444  1.00 22.07           C  
ANISOU 1711  C   LYS A 213     2933   3248   2204   -838    393    389       C  
ATOM   1712  O   LYS A 213     -21.474  -3.303  25.254  1.00 25.32           O  
ANISOU 1712  O   LYS A 213     3339   3801   2480   -614   -266    309       O  
ATOM   1713  N   ASP A 214     -20.289  -4.818  26.466  1.00 18.06           N  
ANISOU 1713  N   ASP A 214     2832   2389   1639  -1236    -68   -235       N  
ATOM   1714  CA  ASP A 214     -21.422  -5.225  27.284  1.00 17.87           C  
ANISOU 1714  CA  ASP A 214     2737   2600   1452  -1126     11   -297       C  
ATOM   1715  CB  ASP A 214     -22.019  -6.511  26.709  1.00 20.62           C  
ANISOU 1715  CB  ASP A 214     3446   2677   1711  -1193    226   -714       C  
ATOM   1716  CG  ASP A 214     -23.319  -6.970  27.336  1.00 23.74           C  
ANISOU 1716  CG  ASP A 214     3419   3387   2211  -1180    278   -631       C  
ATOM   1717  OD1 ASP A 214     -24.085  -6.108  27.808  1.00 25.76           O  
ANISOU 1717  OD1 ASP A 214     2911   4360   2517  -1033    182   -805       O  
ATOM   1718  OD2 ASP A 214     -23.546  -8.193  27.362  1.00 31.25           O  
ANISOU 1718  OD2 ASP A 214     4428   3798   3648  -1937    305   -524       O  
ATOM   1719  C   ASP A 214     -21.023  -5.434  28.748  1.00 15.96           C  
ANISOU 1719  C   ASP A 214     2575   2047   1441   -705    129   -184       C  
ATOM   1720  O   ASP A 214     -21.183  -6.512  29.325  1.00 17.44           O  
ANISOU 1720  O   ASP A 214     3049   1833   1744   -632    467   -304       O  
ATOM   1721  N   PRO A 215     -20.531  -4.384  29.422  1.00 14.18           N  
ANISOU 1721  N   PRO A 215     2229   1772   1386   -432     -1    -62       N  
ATOM   1722  CA  PRO A 215     -20.081  -4.500  30.802  1.00 12.22           C  
ANISOU 1722  CA  PRO A 215     2034   1360   1247   -106    115   -130       C  
ATOM   1723  CB  PRO A 215     -19.224  -3.251  31.011  1.00 12.94           C  
ANISOU 1723  CB  PRO A 215     1870   1704   1340   -249    164   -299       C  
ATOM   1724  CG  PRO A 215     -19.809  -2.239  30.082  1.00 13.47           C  
ANISOU 1724  CG  PRO A 215     1849   1531   1736   -142    261   -177       C  
ATOM   1725  CD  PRO A 215     -20.331  -3.021  28.899  1.00 15.26           C  
ANISOU 1725  CD  PRO A 215     2372   1885   1540   -343      7    123       C  
ATOM   1726  C   PRO A 215     -21.256  -4.511  31.778  1.00 11.57           C  
ANISOU 1726  C   PRO A 215     1902   1257   1236   -105     -8    -69       C  
ATOM   1727  O   PRO A 215     -22.267  -3.864  31.547  1.00 12.08           O  
ANISOU 1727  O   PRO A 215     1842   1263   1483   -121    -31   -145       O  
ATOM   1728  N   VAL A 216     -21.098  -5.255  32.866  1.00 11.51           N  
ANISOU 1728  N   VAL A 216     2044   1132   1195     49    256    -64       N  
ATOM   1729  CA  VAL A 216     -22.081  -5.256  33.937  1.00 11.35           C  
ANISOU 1729  CA  VAL A 216     1737   1151   1422    -64    198   -155       C  
ATOM   1730  CB  VAL A 216     -21.809  -6.371  34.964  1.00 12.65           C  
ANISOU 1730  CB  VAL A 216     2104   1071   1629     -2    287    -60       C  
ATOM   1731  CG1 VAL A 216     -22.835  -6.344  36.082  1.00 12.75           C  
ANISOU 1731  CG1 VAL A 216     2196    974   1672    284    299    -48       C  
ATOM   1732  CG2 VAL A 216     -21.813  -7.734  34.299  1.00 13.39           C  
ANISOU 1732  CG2 VAL A 216     2183   1198   1704     32    303   -175       C  
ATOM   1733  C   VAL A 216     -22.078  -3.878  34.591  1.00 10.52           C  
ANISOU 1733  C   VAL A 216     1728   1065   1203     61    151    -19       C  
ATOM   1734  O   VAL A 216     -21.035  -3.383  34.991  1.00 11.97           O  
ANISOU 1734  O   VAL A 216     1785   1295   1466     49    151   -131       O  
ATOM   1735  N   PRO A 217     -23.260  -3.242  34.746  1.00 11.91           N  
ANISOU 1735  N   PRO A 217     1939   1019   1567    225    113   -324       N  
ATOM   1736  CA  PRO A 217     -23.341  -1.920  35.359  1.00 11.78           C  
ANISOU 1736  CA  PRO A 217     2026   1220   1230    125    290   -418       C  
ATOM   1737  CB  PRO A 217     -24.786  -1.491  35.142  1.00 15.04           C  
ANISOU 1737  CB  PRO A 217     2212   2042   1459    502    198   -325       C  
ATOM   1738  CG  PRO A 217     -25.445  -2.515  34.262  1.00 17.13           C  
ANISOU 1738  CG  PRO A 217     2202   1729   2575     44    335   -125       C  
ATOM   1739  CD  PRO A 217     -24.557  -3.720  34.242  1.00 13.89           C  
ANISOU 1739  CD  PRO A 217     2027   1528   1723     52    208   -433       C  
ATOM   1740  C   PRO A 217     -23.083  -1.947  36.868  1.00 10.74           C  
ANISOU 1740  C   PRO A 217     1763   1082   1233    202    201   -214       C  
ATOM   1741  O   PRO A 217     -23.246  -2.995  37.518  1.00 11.56           O  
ANISOU 1741  O   PRO A 217     1765   1293   1333   -110    182    -93       O  
ATOM   1742  N   PHE A 218     -22.703  -0.779  37.405  1.00 10.72           N  
ANISOU 1742  N   PHE A 218     1829   1094   1150     28    282    -87       N  
ATOM   1743  CA  PHE A 218     -22.692  -0.511  38.848  1.00 11.11           C  
ANISOU 1743  CA  PHE A 218     1830   1165   1223     10    269   -238       C  
ATOM   1744  CB  PHE A 218     -21.545   0.446  39.199  1.00 11.35           C  
ANISOU 1744  CB  PHE A 218     1846   1091   1374    -20    311   -166       C  
ATOM   1745  CG  PHE A 218     -20.206  -0.181  38.894  1.00 11.94           C  
ANISOU 1745  CG  PHE A 218     1791   1323   1419    -44    278   -320       C  
ATOM   1746  CD1 PHE A 218     -19.711  -1.174  39.740  1.00 12.53           C  
ANISOU 1746  CD1 PHE A 218     1911   1484   1366    121    344   -210       C  
ATOM   1747  CE1 PHE A 218     -18.493  -1.784  39.475  1.00 12.60           C  
ANISOU 1747  CE1 PHE A 218     1648   1695   1443   -101     40   -313       C  
ATOM   1748  CZ  PHE A 218     -17.782  -1.425  38.363  1.00 13.06           C  
ANISOU 1748  CZ  PHE A 218     1644   1755   1563     48    301   -443       C  
ATOM   1749  CD2 PHE A 218     -19.470   0.171  37.773  1.00 13.23           C  
ANISOU 1749  CD2 PHE A 218     1782   1784   1458    -86    201   -136       C  
ATOM   1750  CE2 PHE A 218     -18.272  -0.468  37.512  1.00 13.73           C  
ANISOU 1750  CE2 PHE A 218     1983   1962   1269     12    419   -233       C  
ATOM   1751  C   PHE A 218     -24.043   0.056  39.262  1.00 11.24           C  
ANISOU 1751  C   PHE A 218     1840   1216   1212     38    303   -155       C  
ATOM   1752  O   PHE A 218     -24.770   0.646  38.455  1.00 13.24           O  
ANISOU 1752  O   PHE A 218     2175   1450   1405    142    408    173       O  
ATOM   1753  N   ARG A 219     -24.395  -0.147  40.534  1.00 12.00           N  
ANISOU 1753  N   ARG A 219     1980   1313   1266    133    449    -38       N  
ATOM   1754  CA  ARG A 219     -25.714   0.294  41.011  1.00 12.55           C  
ANISOU 1754  CA  ARG A 219     1950   1370   1446    112    323   -406       C  
ATOM   1755  CB  ARG A 219     -26.703  -0.856  41.198  1.00 16.00           C  
ANISOU 1755  CB  ARG A 219     2397   1592   2087    -23    439   -383       C  
ATOM   1756  CG  ARG A 219     -26.195  -2.063  41.953  1.00 16.64           C  
ANISOU 1756  CG  ARG A 219     2268   2143   1910    288    456   -258       C  
ATOM   1757  CD  ARG A 219     -26.342  -1.909  43.446  1.00 18.12           C  
ANISOU 1757  CD  ARG A 219     2823   2206   1853    321    115   -423       C  
ATOM   1758  NE  ARG A 219     -26.082  -3.143  44.145  1.00 17.94           N  
ANISOU 1758  NE  ARG A 219     2498   2302   2016    118    316   -173       N  
ATOM   1759  CZ  ARG A 219     -26.951  -4.100  44.395  1.00 16.96           C  
ANISOU 1759  CZ  ARG A 219     2565   2299   1577    463    631    -31       C  
ATOM   1760  NH1 ARG A 219     -28.236  -3.970  44.087  1.00 19.57           N  
ANISOU 1760  NH1 ARG A 219     2596   3068   1770    181    710   -145       N  
ATOM   1761  NH2 ARG A 219     -26.485  -5.180  44.980  1.00 18.83           N  
ANISOU 1761  NH2 ARG A 219     3353   2166   1635    647    989    236       N  
ATOM   1762  C   ARG A 219     -25.613   1.165  42.268  1.00 11.88           C  
ANISOU 1762  C   ARG A 219     1940   1246   1328    135    376   -305       C  
ATOM   1763  O   ARG A 219     -24.841   0.922  43.203  1.00 12.43           O  
ANISOU 1763  O   ARG A 219     2107   1199   1417    102    226   -175       O  
ATOM   1764  N   ASN A 220     -26.464   2.196  42.252  1.00 11.10           N  
ANISOU 1764  N   ASN A 220     1922   1075   1220     39    216   -185       N  
ATOM   1765  CA  ASN A 220     -26.755   3.060  43.376  1.00 11.45           C  
ANISOU 1765  CA  ASN A 220     1944   1077   1326    -17    324   -276       C  
ATOM   1766  CB  ASN A 220     -27.666   2.367  44.373  1.00 11.29           C  
ANISOU 1766  CB  ASN A 220     1830   1279   1179     88    318   -361       C  
ATOM   1767  CG  ASN A 220     -28.252   3.330  45.380  1.00 11.50           C  
ANISOU 1767  CG  ASN A 220     1936   1072   1359     -1    372   -416       C  
ATOM   1768  OD1 ASN A 220     -28.570   4.480  45.027  1.00 13.78           O  
ANISOU 1768  OD1 ASN A 220     2393   1316   1524    129    342   -289       O  
ATOM   1769  ND2 ASN A 220     -28.357   2.886  46.625  1.00 12.68           N  
ANISOU 1769  ND2 ASN A 220     1892   1526   1397   -142    453   -363       N  
ATOM   1770  C   ASN A 220     -25.487   3.614  44.059  1.00 11.38           C  
ANISOU 1770  C   ASN A 220     1853   1186   1285     76    322   -253       C  
ATOM   1771  O   ASN A 220     -25.274   3.449  45.254  1.00 12.80           O  
ANISOU 1771  O   ASN A 220     1991   1588   1282    -10    343   -243       O  
ATOM   1772  N   LEU A 221     -24.704   4.361  43.276  1.00 12.25           N  
ANISOU 1772  N   LEU A 221     1820   1381   1452   -155    281   -258       N  
ATOM   1773  CA  LEU A 221     -23.474   5.014  43.751  1.00 12.10           C  
ANISOU 1773  CA  LEU A 221     1847   1304   1444    -58    248   -318       C  
ATOM   1774  CB  LEU A 221     -22.525   5.175  42.566  1.00 12.58           C  
ANISOU 1774  CB  LEU A 221     1807   1370   1602     -9    273   -196       C  
ATOM   1775  CG  LEU A 221     -22.075   3.870  41.905  1.00 14.07           C  
ANISOU 1775  CG  LEU A 221     2254   1449   1640     30    208   -307       C  
ATOM   1776  CD1 LEU A 221     -21.130   4.163  40.778  1.00 15.10           C  
ANISOU 1776  CD1 LEU A 221     2363   1560   1811   -264    284   -308       C  
ATOM   1777  CD2 LEU A 221     -21.449   2.910  42.901  1.00 14.42           C  
ANISOU 1777  CD2 LEU A 221     2295   1550   1632    132    279   -317       C  
ATOM   1778  C   LEU A 221     -23.800   6.356  44.426  1.00 12.04           C  
ANISOU 1778  C   LEU A 221     1984   1227   1361     37    249   -158       C  
ATOM   1779  O   LEU A 221     -23.785   7.421  43.811  1.00 12.76           O  
ANISOU 1779  O   LEU A 221     1997   1060   1791    -19    295   -154       O  
ATOM   1780  N   ASN A 222     -24.049   6.294  45.731  1.00 11.78           N  
ANISOU 1780  N   ASN A 222     1977   1136   1363    -33    318   -292       N  
ATOM   1781  CA  ASN A 222     -24.215   7.493  46.547  1.00 12.48           C  
ANISOU 1781  CA  ASN A 222     1925   1271   1544     62    268   -411       C  
ATOM   1782  CB  ASN A 222     -24.596   7.174  47.989  1.00 13.41           C  
ANISOU 1782  CB  ASN A 222     2048   1456   1592    -87    318   -337       C  
ATOM   1783  CG  ASN A 222     -25.998   6.691  48.250  1.00 14.46           C  
ANISOU 1783  CG  ASN A 222     2009   1735   1749     21    402   -565       C  
ATOM   1784  OD1 ASN A 222     -26.484   6.895  49.347  1.00 14.31           O  
ANISOU 1784  OD1 ASN A 222     2069   1583   1783      9    581   -322       O  
ATOM   1785  ND2 ASN A 222     -26.640   6.031  47.291  1.00 14.26           N  
ANISOU 1785  ND2 ASN A 222     2038   1837   1540    -76    410   -492       N  
ATOM   1786  C   ASN A 222     -22.906   8.298  46.635  1.00 12.56           C  
ANISOU 1786  C   ASN A 222     1833   1410   1529     66    267   -208       C  
ATOM   1787  O   ASN A 222     -22.957   9.542  46.718  1.00 13.67           O  
ANISOU 1787  O   ASN A 222     2005   1450   1738     42    480   -307       O  
ATOM   1788  N   THR A 223     -21.762   7.592  46.670  1.00 11.39           N  
ANISOU 1788  N   THR A 223     1549   1348   1430    -86    262   -299       N  
ATOM   1789  CA  THR A 223     -20.451   8.186  46.537  1.00 12.32           C  
ANISOU 1789  CA  THR A 223     1749   1265   1666   -117    310   -218       C  
ATOM   1790  CB  THR A 223     -19.558   7.921  47.759  1.00 13.70           C  
ANISOU 1790  CB  THR A 223     2039   1582   1583    -75    271   -308       C  
ATOM   1791  OG1 THR A 223     -20.176   8.440  48.938  1.00 15.31           O  
ANISOU 1791  OG1 THR A 223     2140   2170   1505      8    257   -474       O  
ATOM   1792  CG2 THR A 223     -18.186   8.528  47.608  1.00 14.24           C  
ANISOU 1792  CG2 THR A 223     2194   1454   1762   -162    154    -31       C  
ATOM   1793  C   THR A 223     -19.786   7.571  45.304  1.00 13.01           C  
ANISOU 1793  C   THR A 223     1830   1603   1509   -176    231   -254       C  
ATOM   1794  O   THR A 223     -19.755   6.338  45.169  1.00 13.43           O  
ANISOU 1794  O   THR A 223     1917   1575   1609    -27    372   -297       O  
ATOM   1795  N   PHE A 224     -19.331   8.422  44.393  1.00 12.11           N  
ANISOU 1795  N   PHE A 224     1800   1346   1454    109    225   -296       N  
ATOM   1796  CA  PHE A 224     -18.596   7.996  43.224  1.00 11.89           C  
ANISOU 1796  CA  PHE A 224     1796   1272   1450    139    206   -247       C  
ATOM   1797  CB  PHE A 224     -19.531   7.820  42.027  1.00 11.90           C  
ANISOU 1797  CB  PHE A 224     1894   1332   1294    113    245    -36       C  
ATOM   1798  CG  PHE A 224     -18.872   7.348  40.753  1.00 13.31           C  
ANISOU 1798  CG  PHE A 224     2253   1417   1386     65    278   -261       C  
ATOM   1799  CD1 PHE A 224     -17.854   6.402  40.772  1.00 13.49           C  
ANISOU 1799  CD1 PHE A 224     2215   1463   1448     16    280     11       C  
ATOM   1800  CE1 PHE A 224     -17.293   5.939  39.600  1.00 16.25           C  
ANISOU 1800  CE1 PHE A 224     2660   1940   1571     45    314   -205       C  
ATOM   1801  CZ  PHE A 224     -17.770   6.375  38.393  1.00 15.87           C  
ANISOU 1801  CZ  PHE A 224     2832   1709   1487    301    378   -319       C  
ATOM   1802  CD2 PHE A 224     -19.343   7.771  39.530  1.00 16.01           C  
ANISOU 1802  CD2 PHE A 224     2815   1788   1479    287    238   -249       C  
ATOM   1803  CE2 PHE A 224     -18.788   7.292  38.349  1.00 16.66           C  
ANISOU 1803  CE2 PHE A 224     2811   2032   1484    416    334   -220       C  
ATOM   1804  C   PHE A 224     -17.513   9.042  42.958  1.00 12.85           C  
ANISOU 1804  C   PHE A 224     1874   1406   1599     74    342    -83       C  
ATOM   1805  O   PHE A 224     -17.829  10.157  42.535  1.00 13.21           O  
ANISOU 1805  O   PHE A 224     2003   1358   1657    100    168   -119       O  
ATOM   1806  N   LYS A 225     -16.266   8.687  43.258  1.00 13.14           N  
ANISOU 1806  N   LYS A 225     1839   1367   1784     31    348   -141       N  
ATOM   1807  CA  LYS A 225     -15.156   9.577  43.008  1.00 12.99           C  
ANISOU 1807  CA  LYS A 225     1773   1486   1673     35    342    -34       C  
ATOM   1808  CB  LYS A 225     -14.514  10.096  44.296  1.00 14.75           C  
ANISOU 1808  CB  LYS A 225     1986   1882   1735     -1    171    -17       C  
ATOM   1809  CG  LYS A 225     -15.456  10.662  45.335  1.00 17.57           C  
ANISOU 1809  CG  LYS A 225     2122   2486   2066   -168    291   -410       C  
ATOM   1810  CD  LYS A 225     -14.733  11.143  46.587  1.00 21.11           C  
ANISOU 1810  CD  LYS A 225     2739   3163   2117   -473    150   -566       C  
ATOM   1811  CE  LYS A 225     -15.700  11.615  47.645  1.00 24.78           C  
ANISOU 1811  CE  LYS A 225     3366   3902   2146   -714    466   -694       C  
ATOM   1812  NZ  LYS A 225     -14.996  12.126  48.844  1.00 28.94           N  
ANISOU 1812  NZ  LYS A 225     3452   4561   2982   -678     84   -999       N  
ATOM   1813  C   LYS A 225     -14.118   8.827  42.178  1.00 13.47           C  
ANISOU 1813  C   LYS A 225     1903   1460   1753    226    358     65       C  
ATOM   1814  O   LYS A 225     -13.842   7.659  42.427  1.00 14.12           O  
ANISOU 1814  O   LYS A 225     2137   1339   1888     88    395     38       O  
ATOM   1815  N   VAL A 226     -13.530   9.533  41.217  1.00 13.14           N  
ANISOU 1815  N   VAL A 226     1941   1536   1513    517    438    107       N  
ATOM   1816  CA  VAL A 226     -12.424   9.028  40.425  1.00 13.47           C  
ANISOU 1816  CA  VAL A 226     1974   1591   1552    477    522    266       C  
ATOM   1817  CB  VAL A 226     -12.875   8.802  38.967  1.00 14.78           C  
ANISOU 1817  CB  VAL A 226     2165   1819   1631    357    474    278       C  
ATOM   1818  CG1 VAL A 226     -11.707   8.411  38.075  1.00 15.70           C  
ANISOU 1818  CG1 VAL A 226     2330   1868   1766    299    646    210       C  
ATOM   1819  CG2 VAL A 226     -13.994   7.786  38.899  1.00 15.69           C  
ANISOU 1819  CG2 VAL A 226     2325   1815   1819    354    392    119       C  
ATOM   1820  C   VAL A 226     -11.311  10.069  40.527  1.00 13.79           C  
ANISOU 1820  C   VAL A 226     1906   1669   1665    489    510    113       C  
ATOM   1821  O   VAL A 226     -11.506  11.212  40.096  1.00 14.58           O  
ANISOU 1821  O   VAL A 226     2008   1723   1806    340    331    192       O  
ATOM   1822  N   ILE A 227     -10.202   9.676  41.153  1.00 14.40           N  
ANISOU 1822  N   ILE A 227     2115   1846   1508    358    378    166       N  
ATOM   1823  CA  ILE A 227      -9.120  10.560  41.498  1.00 15.86           C  
ANISOU 1823  CA  ILE A 227     2238   1956   1829    555    251   -313       C  
ATOM   1824  CB  ILE A 227      -8.857  10.533  43.019  1.00 20.35           C  
ANISOU 1824  CB  ILE A 227     2979   2813   1937    979    217   -299       C  
ATOM   1825  CG1 ILE A 227     -10.134  10.839  43.814  1.00 20.83           C  
ANISOU 1825  CG1 ILE A 227     2922   3216   1777   1266     15   -402       C  
ATOM   1826  CG2 ILE A 227      -7.706  11.463  43.356  1.00 23.15           C  
ANISOU 1826  CG2 ILE A 227     3119   3440   2236   1101   -254   -711       C  
ATOM   1827  CD1 ILE A 227     -10.215  10.237  45.181  1.00 26.38           C  
ANISOU 1827  CD1 ILE A 227     3894   3909   2217    817    511   -127       C  
ATOM   1828  C   ILE A 227      -7.887  10.106  40.713  1.00 13.09           C  
ANISOU 1828  C   ILE A 227     1965   1384   1623    166    125   -462       C  
ATOM   1829  O   ILE A 227      -7.388   8.998  40.935  1.00 14.81           O  
ANISOU 1829  O   ILE A 227     2139   1424   2061    172    122   -254       O  
ATOM   1830  N   LEU A 228      -7.422  10.948  39.787  1.00 13.14           N  
ANISOU 1830  N   LEU A 228     2201   1231   1558    212    -60   -359       N  
ATOM   1831  CA  LEU A 228      -6.350  10.604  38.867  1.00 13.64           C  
ANISOU 1831  CA  LEU A 228     2204   1494   1483    323    -87   -374       C  
ATOM   1832  CB  LEU A 228      -6.776  10.898  37.426  1.00 15.10           C  
ANISOU 1832  CB  LEU A 228     2262   1947   1526    483   -152   -416       C  
ATOM   1833  CG  LEU A 228      -8.104  10.320  36.971  1.00 16.91           C  
ANISOU 1833  CG  LEU A 228     2475   2015   1934    458   -315   -698       C  
ATOM   1834  CD1 LEU A 228      -8.388  10.771  35.548  1.00 20.09           C  
ANISOU 1834  CD1 LEU A 228     3095   2504   2033    621   -439   -563       C  
ATOM   1835  CD2 LEU A 228      -8.109   8.817  37.090  1.00 16.05           C  
ANISOU 1835  CD2 LEU A 228     2183   1998   1917    359   -140   -795       C  
ATOM   1836  C   LEU A 228      -5.106  11.441  39.161  1.00 13.84           C  
ANISOU 1836  C   LEU A 228     2375   1463   1417    112    113   -309       C  
ATOM   1837  O   LEU A 228      -5.177  12.656  39.364  1.00 15.25           O  
ANISOU 1837  O   LEU A 228     2519   1529   1744    135     57   -502       O  
ATOM   1838  N   ASP A 229      -3.958  10.785  39.119  1.00 13.26           N  
ANISOU 1838  N   ASP A 229     2290   1409   1338     -6     -2   -401       N  
ATOM   1839  CA  ASP A 229      -2.684  11.452  39.006  1.00 14.20           C  
ANISOU 1839  CA  ASP A 229     2213   1720   1459    -34    -28   -328       C  
ATOM   1840  CB  ASP A 229      -1.573  10.567  39.551  1.00 16.27           C  
ANISOU 1840  CB  ASP A 229     2533   1995   1653    207   -129   -402       C  
ATOM   1841  CG  ASP A 229      -0.163  11.101  39.381  1.00 17.58           C  
ANISOU 1841  CG  ASP A 229     2484   2502   1694    158   -252   -591       C  
ATOM   1842  OD1 ASP A 229       0.006  12.289  39.010  1.00 21.00           O  
ANISOU 1842  OD1 ASP A 229     2880   2597   2501    -42   -442   -666       O  
ATOM   1843  OD2 ASP A 229       0.772  10.304  39.621  1.00 23.03           O  
ANISOU 1843  OD2 ASP A 229     2715   3114   2919    536   -578   -934       O  
ATOM   1844  C   ASP A 229      -2.467  11.774  37.524  1.00 13.97           C  
ANISOU 1844  C   ASP A 229     2320   1660   1325   -115     84   -553       C  
ATOM   1845  O   ASP A 229      -2.054  10.910  36.765  1.00 14.94           O  
ANISOU 1845  O   ASP A 229     2556   1641   1477    -11    117   -489       O  
ATOM   1846  N   GLY A 230      -2.794  12.993  37.107  1.00 14.34           N  
ANISOU 1846  N   GLY A 230     2347   1525   1575   -242    121   -610       N  
ATOM   1847  CA  GLY A 230      -2.705  13.385  35.700  1.00 15.06           C  
ANISOU 1847  CA  GLY A 230     2343   1627   1750   -254    118   -403       C  
ATOM   1848  C   GLY A 230      -1.282  13.663  35.267  1.00 13.34           C  
ANISOU 1848  C   GLY A 230     2274   1311   1481   -304     61   -325       C  
ATOM   1849  O   GLY A 230      -0.630  14.541  35.832  1.00 13.82           O  
ANISOU 1849  O   GLY A 230     2387   1413   1449   -377    222   -459       O  
ATOM   1850  N   GLN A 231      -0.809  12.894  34.286  1.00 13.09           N  
ANISOU 1850  N   GLN A 231     2015   1607   1351   -383    105   -362       N  
ATOM   1851  CA AGLN A 231       0.505  13.084  33.673  0.50 13.29           C  
ANISOU 1851  CA AGLN A 231     2050   1480   1519   -374     65   -200       C  
ATOM   1852  CA BGLN A 231       0.526  13.066  33.675  0.50 13.83           C  
ANISOU 1852  CA BGLN A 231     2116   1613   1524   -422    118   -254       C  
ATOM   1853  CB AGLN A 231       1.484  12.022  34.169  0.50 13.89           C  
ANISOU 1853  CB AGLN A 231     1982   1515   1778   -342     37    -52       C  
ATOM   1854  CB BGLN A 231       1.464  11.962  34.193  0.50 15.24           C  
ANISOU 1854  CB BGLN A 231     2225   1736   1829   -312     84   -121       C  
ATOM   1855  CG AGLN A 231       1.751  12.105  35.663  0.50 15.74           C  
ANISOU 1855  CG AGLN A 231     2349   1754   1878   -226   -235   -219       C  
ATOM   1856  CG BGLN A 231       2.975  12.113  33.963  0.50 17.78           C  
ANISOU 1856  CG BGLN A 231     2367   2238   2148   -448    -65   -300       C  
ATOM   1857  CD AGLN A 231       2.527  13.334  36.055  0.50 19.45           C  
ANISOU 1857  CD AGLN A 231     2800   2208   2380   -632   -649    -35       C  
ATOM   1858  CD BGLN A 231       3.826  10.967  34.491  0.50 17.45           C  
ANISOU 1858  CD BGLN A 231     2366   2317   1946   -254   -240   -484       C  
ATOM   1859  OE1AGLN A 231       3.334  13.827  35.265  0.50 23.73           O  
ANISOU 1859  OE1AGLN A 231     3281   2765   2970  -1609   -642    -11       O  
ATOM   1860  OE1BGLN A 231       4.126   9.958  33.791  0.50 12.61           O  
ANISOU 1860  OE1BGLN A 231     1663   2187    940   -595   -497   -285       O  
ATOM   1861  NE2AGLN A 231       2.300  13.826  37.275  0.50 22.76           N  
ANISOU 1861  NE2AGLN A 231     4552   1781   2314   -794  -1349   -297       N  
ATOM   1862  NE2BGLN A 231       4.273  11.128  35.741  0.50 20.25           N  
ANISOU 1862  NE2BGLN A 231     2842   2752   2097   -332   -167   -835       N  
ATOM   1863  C   GLN A 231       0.333  13.045  32.151  1.00 13.91           C  
ANISOU 1863  C   GLN A 231     2153   1634   1498   -407    238   -353       C  
ATOM   1864  O   GLN A 231       0.995  12.289  31.434  1.00 14.11           O  
ANISOU 1864  O   GLN A 231     2107   1651   1600   -511    256   -499       O  
ATOM   1865  N   PHE A 232      -0.573  13.895  31.664  1.00 12.73           N  
ANISOU 1865  N   PHE A 232     2250   1318   1267   -425    313   -502       N  
ATOM   1866  CA  PHE A 232      -0.897  14.022  30.237  1.00 13.89           C  
ANISOU 1866  CA  PHE A 232     2481   1441   1356   -419    174   -456       C  
ATOM   1867  CB  PHE A 232      -2.323  14.512  30.039  1.00 14.13           C  
ANISOU 1867  CB  PHE A 232     2546   1337   1486   -369     12   -523       C  
ATOM   1868  CG  PHE A 232      -3.368  13.584  30.595  1.00 13.64           C  
ANISOU 1868  CG  PHE A 232     2221   1331   1627   -198    -84   -317       C  
ATOM   1869  CD1 PHE A 232      -3.788  13.667  31.918  1.00 14.26           C  
ANISOU 1869  CD1 PHE A 232     2395   1366   1656   -272   -137   -443       C  
ATOM   1870  CE1 PHE A 232      -4.729  12.779  32.419  1.00 14.25           C  
ANISOU 1870  CE1 PHE A 232     1940   1775   1699    -82   -162   -344       C  
ATOM   1871  CZ  PHE A 232      -5.317  11.856  31.590  1.00 13.77           C  
ANISOU 1871  CZ  PHE A 232     1998   1494   1740    -74   -105   -267       C  
ATOM   1872  CD2 PHE A 232      -3.952  12.630  29.788  1.00 13.76           C  
ANISOU 1872  CD2 PHE A 232     2392   1356   1478   -103     -3   -406       C  
ATOM   1873  CE2 PHE A 232      -4.906  11.768  30.288  1.00 13.05           C  
ANISOU 1873  CE2 PHE A 232     1859   1318   1782     44   -155   -501       C  
ATOM   1874  C   PHE A 232       0.126  14.950  29.583  1.00 16.21           C  
ANISOU 1874  C   PHE A 232     2701   1810   1648   -551    316   -370       C  
ATOM   1875  O   PHE A 232      -0.195  16.048  29.081  1.00 17.76           O  
ANISOU 1875  O   PHE A 232     2945   1997   1804   -541    133   -240       O  
ATOM   1876  N   LYS A 233       1.367  14.471  29.587  1.00 16.98           N  
ANISOU 1876  N   LYS A 233     2648   1732   2071   -441    706   -506       N  
ATOM   1877  CA  LYS A 233       2.480  15.208  29.081  1.00 17.84           C  
ANISOU 1877  CA  LYS A 233     2694   2123   1960   -470    692   -323       C  
ATOM   1878  CB  LYS A 233       3.624  15.174  30.089  1.00 20.13           C  
ANISOU 1878  CB  LYS A 233     2722   2848   2076   -859    458   -164       C  
ATOM   1879  CG  LYS A 233       4.247  13.814  30.347  1.00 20.94           C  
ANISOU 1879  CG  LYS A 233     2837   3011   2104   -760     56   -103       C  
ATOM   1880  CD  LYS A 233       5.255  13.840  31.476  1.00 27.21           C  
ANISOU 1880  CD  LYS A 233     3159   4175   3002  -1331   -431    390       C  
ATOM   1881  CE  LYS A 233       5.984  12.524  31.588  1.00 31.46           C  
ANISOU 1881  CE  LYS A 233     3690   4856   3408  -1014   -759    905       C  
ATOM   1882  NZ  LYS A 233       7.054  12.592  32.607  1.00 40.42           N  
ANISOU 1882  NZ  LYS A 233     4488   6604   4262  -1591  -1360   1120       N  
ATOM   1883  C   LYS A 233       2.941  14.631  27.754  1.00 14.74           C  
ANISOU 1883  C   LYS A 233     2078   1547   1974   -239    607   -204       C  
ATOM   1884  O   LYS A 233       2.572  13.517  27.385  1.00 14.84           O  
ANISOU 1884  O   LYS A 233     1940   1592   2105   -351    395   -221       O  
ATOM   1885  N   PRO A 234       3.749  15.386  26.989  1.00 13.36           N  
ANISOU 1885  N   PRO A 234     1937   1349   1787   -261    405   -171       N  
ATOM   1886  CA  PRO A 234       4.092  14.958  25.632  1.00 15.10           C  
ANISOU 1886  CA  PRO A 234     2282   1692   1762   -256    351   -254       C  
ATOM   1887  CB  PRO A 234       5.038  16.061  25.147  1.00 15.82           C  
ANISOU 1887  CB  PRO A 234     2732   1538   1740   -199    382    -24       C  
ATOM   1888  CG  PRO A 234       4.601  17.278  25.924  1.00 16.28           C  
ANISOU 1888  CG  PRO A 234     2418   1977   1791   -203    565   -190       C  
ATOM   1889  CD  PRO A 234       4.282  16.727  27.308  1.00 14.81           C  
ANISOU 1889  CD  PRO A 234     2397   1467   1763   -313    600   -359       C  
ATOM   1890  C   PRO A 234       4.697  13.543  25.557  1.00 13.16           C  
ANISOU 1890  C   PRO A 234     2095   1573   1331   -392    373   -328       C  
ATOM   1891  O   PRO A 234       4.330  12.763  24.672  1.00 13.03           O  
ANISOU 1891  O   PRO A 234     2021   1479   1450   -321     -7   -308       O  
ATOM   1892  N   GLU A 235       5.600  13.190  26.482  1.00 14.69           N  
ANISOU 1892  N   GLU A 235     2232   1679   1671   -117    296   -274       N  
ATOM   1893  CA  GLU A 235       6.266  11.871  26.393  1.00 14.07           C  
ANISOU 1893  CA  GLU A 235     1896   1774   1676   -209     70   -426       C  
ATOM   1894  CB  GLU A 235       7.406  11.807  27.416  1.00 16.67           C  
ANISOU 1894  CB  GLU A 235     1919   2296   2118    -39   -125   -127       C  
ATOM   1895  CG  GLU A 235       8.197  10.527  27.343  1.00 19.75           C  
ANISOU 1895  CG  GLU A 235     2441   2436   2625    -53    101   -230       C  
ATOM   1896  CD  GLU A 235       9.548  10.563  28.044  1.00 25.40           C  
ANISOU 1896  CD  GLU A 235     3041   3196   3411    176   -486   -421       C  
ATOM   1897  OE1 GLU A 235       9.839  11.574  28.747  1.00 31.71           O  
ANISOU 1897  OE1 GLU A 235     4047   3544   4454   -183  -1053   -784       O  
ATOM   1898  OE2 GLU A 235      10.296   9.548  27.937  1.00 28.87           O  
ANISOU 1898  OE2 GLU A 235     3656   2989   4321    426   -904   -495       O  
ATOM   1899  C   GLU A 235       5.249  10.733  26.577  1.00 13.69           C  
ANISOU 1899  C   GLU A 235     1885   1645   1669    -93    111   -271       C  
ATOM   1900  O   GLU A 235       5.492   9.629  26.158  1.00 14.57           O  
ANISOU 1900  O   GLU A 235     1953   1562   2019   -144    201   -272       O  
ATOM   1901  N   ASN A 236       4.131  10.988  27.262  1.00 13.09           N  
ANISOU 1901  N   ASN A 236     1948   1449   1576   -227     90   -324       N  
ATOM   1902  CA  ASN A 236       3.130   9.942  27.466  1.00 12.36           C  
ANISOU 1902  CA  ASN A 236     1850   1311   1535    -96     68   -106       C  
ATOM   1903  CB  ASN A 236       2.392  10.106  28.794  1.00 12.44           C  
ANISOU 1903  CB  ASN A 236     1703   1522   1502    -19    -17   -154       C  
ATOM   1904  CG  ASN A 236       3.307   9.768  29.962  1.00 12.53           C  
ANISOU 1904  CG  ASN A 236     1488   1834   1438    -37     80   -107       C  
ATOM   1905  OD1 ASN A 236       4.264   8.987  29.817  1.00 15.56           O  
ANISOU 1905  OD1 ASN A 236     1935   2319   1657    358     94   -297       O  
ATOM   1906  ND2 ASN A 236       3.019  10.330  31.128  1.00 15.29           N  
ANISOU 1906  ND2 ASN A 236     2301   1988   1517   -245    154   -324       N  
ATOM   1907  C   ASN A 236       2.174   9.834  26.275  1.00 13.91           C  
ANISOU 1907  C   ASN A 236     2296   1379   1608   -271    -38   -317       C  
ATOM   1908  O   ASN A 236       1.643   8.738  26.047  1.00 15.22           O  
ANISOU 1908  O   ASN A 236     2523   1427   1830   -467   -270   -168       O  
ATOM   1909  N   MET A 237       1.946  10.923  25.531  1.00 12.83           N  
ANISOU 1909  N   MET A 237     2141   1414   1320   -321      0   -285       N  
ATOM   1910  CA  MET A 237       0.854  10.942  24.547  1.00 12.80           C  
ANISOU 1910  CA  MET A 237     2047   1497   1317   -328     58   -408       C  
ATOM   1911  CB  MET A 237      -0.074  12.131  24.789  1.00 12.05           C  
ANISOU 1911  CB  MET A 237     1679   1570   1328   -284     33   -332       C  
ATOM   1912  CG  MET A 237      -0.754  12.078  26.148  1.00 13.54           C  
ANISOU 1912  CG  MET A 237     2118   1661   1363   -100    146   -127       C  
ATOM   1913  SD  MET A 237      -2.076  13.284  26.278  1.00 15.09           S  
ANISOU 1913  SD  MET A 237     2340   1650   1741    -40    215   -243       S  
ATOM   1914  CE  MET A 237      -1.202  14.835  26.040  1.00 15.63           C  
ANISOU 1914  CE  MET A 237     2479   1425   2032     15    218   -422       C  
ATOM   1915  C   MET A 237       1.337  11.025  23.089  1.00 12.34           C  
ANISOU 1915  C   MET A 237     1863   1512   1312   -194     49   -337       C  
ATOM   1916  O   MET A 237       0.666  10.462  22.234  1.00 12.15           O  
ANISOU 1916  O   MET A 237     1760   1462   1392   -124      4   -343       O  
ATOM   1917  N   ILE A 238       2.384  11.802  22.796  1.00 12.76           N  
ANISOU 1917  N   ILE A 238     1702   1667   1478   -108     77   -471       N  
ATOM   1918  CA  ILE A 238       2.702  12.242  21.431  1.00 12.42           C  
ANISOU 1918  CA  ILE A 238     1525   1604   1590   -394    -24   -456       C  
ATOM   1919  CB  ILE A 238       3.215  13.700  21.439  1.00 13.62           C  
ANISOU 1919  CB  ILE A 238     1840   1598   1735   -433     30   -325       C  
ATOM   1920  CG1 ILE A 238       2.205  14.640  22.106  1.00 14.70           C  
ANISOU 1920  CG1 ILE A 238     2044   1771   1770   -437    103   -480       C  
ATOM   1921  CG2 ILE A 238       3.579  14.140  20.025  1.00 15.00           C  
ANISOU 1921  CG2 ILE A 238     1978   1760   1961   -344    216   -164       C  
ATOM   1922  CD1 ILE A 238       0.887  14.764  21.422  1.00 16.63           C  
ANISOU 1922  CD1 ILE A 238     2194   2053   2072   -271     24   -445       C  
ATOM   1923  C   ILE A 238       3.733  11.306  20.787  1.00 12.35           C  
ANISOU 1923  C   ILE A 238     1680   1552   1459   -293     30   -311       C  
ATOM   1924  O   ILE A 238       4.772  11.000  21.368  1.00 12.89           O  
ANISOU 1924  O   ILE A 238     1625   1689   1582   -240     41   -323       O  
ATOM   1925  N   GLY A 239       3.419  10.871  19.567  1.00 11.63           N  
ANISOU 1925  N   GLY A 239     1669   1339   1409   -288    195   -304       N  
ATOM   1926  CA  GLY A 239       4.350  10.089  18.759  1.00 11.79           C  
ANISOU 1926  CA  GLY A 239     1783   1147   1546   -255    259   -301       C  
ATOM   1927  C   GLY A 239       4.836  10.857  17.541  1.00 11.99           C  
ANISOU 1927  C   GLY A 239     1703   1372   1480   -266    119   -199       C  
ATOM   1928  O   GLY A 239       4.046  11.498  16.848  1.00 12.92           O  
ANISOU 1928  O   GLY A 239     1697   1552   1659   -126    106    -60       O  
ATOM   1929  N   ILE A 240       6.142  10.784  17.285  1.00 12.71           N  
ANISOU 1929  N   ILE A 240     1853   1393   1581    -81    134   -177       N  
ATOM   1930  CA  ILE A 240       6.771  11.457  16.154  1.00 12.26           C  
ANISOU 1930  CA  ILE A 240     1781   1382   1496   -239     81   -217       C  
ATOM   1931  CB  ILE A 240       7.523  12.736  16.561  1.00 12.90           C  
ANISOU 1931  CB  ILE A 240     1780   1447   1674   -301     62   -252       C  
ATOM   1932  CG1 ILE A 240       6.632  13.715  17.338  1.00 13.27           C  
ANISOU 1932  CG1 ILE A 240     2011   1331   1697   -387    290   -177       C  
ATOM   1933  CG2 ILE A 240       8.172  13.376  15.339  1.00 13.83           C  
ANISOU 1933  CG2 ILE A 240     2022   1452   1779   -327     86   -187       C  
ATOM   1934  CD1 ILE A 240       7.372  14.879  17.960  1.00 14.87           C  
ANISOU 1934  CD1 ILE A 240     2314   1322   2014   -335    139   -319       C  
ATOM   1935  C   ILE A 240       7.701  10.446  15.482  1.00 11.77           C  
ANISOU 1935  C   ILE A 240     1678   1386   1407   -225     83   -154       C  
ATOM   1936  O   ILE A 240       8.574   9.877  16.108  1.00 13.33           O  
ANISOU 1936  O   ILE A 240     1672   1657   1733    -19     18   -130       O  
ATOM   1937  N   ALA A 241       7.485  10.213  14.183  1.00 11.47           N  
ANISOU 1937  N   ALA A 241     1583   1271   1501   -222   -126   -188       N  
ATOM   1938  CA  ALA A 241       8.325   9.291  13.445  1.00 11.82           C  
ANISOU 1938  CA  ALA A 241     1635   1275   1580   -241    155   -168       C  
ATOM   1939  CB  ALA A 241       7.909   9.256  12.004  1.00 12.46           C  
ANISOU 1939  CB  ALA A 241     1749   1377   1608   -143    136    -89       C  
ATOM   1940  C   ALA A 241       9.808   9.663  13.567  1.00 12.68           C  
ANISOU 1940  C   ALA A 241     1606   1468   1744    -69    246   -324       C  
ATOM   1941  O   ALA A 241      10.193  10.849  13.605  1.00 13.36           O  
ANISOU 1941  O   ALA A 241     1801   1545   1730   -176    458   -346       O  
ATOM   1942  N   ASP A 242      10.640   8.620  13.564  1.00 12.43           N  
ANISOU 1942  N   ASP A 242     1640   1202   1881   -127    321   -209       N  
ATOM   1943  CA  ASP A 242      12.084   8.732  13.745  1.00 14.15           C  
ANISOU 1943  CA  ASP A 242     1676   1553   2144   -303    259   -221       C  
ATOM   1944  CB  ASP A 242      12.621   7.373  14.191  1.00 14.31           C  
ANISOU 1944  CB  ASP A 242     1540   1581   2313   -238    116   -332       C  
ATOM   1945  CG  ASP A 242      12.026   6.996  15.531  1.00 17.10           C  
ANISOU 1945  CG  ASP A 242     2167   2046   2283   -410     -2   -238       C  
ATOM   1946  OD1 ASP A 242      12.464   7.624  16.534  1.00 20.15           O  
ANISOU 1946  OD1 ASP A 242     2854   2679   2122   -899   -173   -174       O  
ATOM   1947  OD2 ASP A 242      11.097   6.147  15.565  1.00 14.52           O  
ANISOU 1947  OD2 ASP A 242     1927   1686   1902   -198     37   -308       O  
ATOM   1948  C   ASP A 242      12.790   9.316  12.522  1.00 14.20           C  
ANISOU 1948  C   ASP A 242     1514   1788   2092   -324    288   -338       C  
ATOM   1949  O   ASP A 242      13.974   9.631  12.647  1.00 19.02           O  
ANISOU 1949  O   ASP A 242     1518   3187   2519   -645    315    -62       O  
ATOM   1950  N   ASP A 243      12.089   9.504  11.397  1.00 14.91           N  
ANISOU 1950  N   ASP A 243     1703   1871   2090   -362    277   -180       N  
ATOM   1951  CA  ASP A 243      12.698  10.120  10.223  1.00 15.59           C  
ANISOU 1951  CA  ASP A 243     1998   1736   2188   -377    303      3       C  
ATOM   1952  CB  ASP A 243      12.555   9.250   8.966  1.00 15.65           C  
ANISOU 1952  CB  ASP A 243     2181   1727   2035   -445    700      6       C  
ATOM   1953  CG  ASP A 243      11.154   8.983   8.440  1.00 16.09           C  
ANISOU 1953  CG  ASP A 243     2326   1836   1950   -545    549    -55       C  
ATOM   1954  OD1 ASP A 243      10.175   9.203   9.175  1.00 15.66           O  
ANISOU 1954  OD1 ASP A 243     2082   1832   2035   -233    375    116       O  
ATOM   1955  OD2 ASP A 243      11.061   8.501   7.282  1.00 19.85           O  
ANISOU 1955  OD2 ASP A 243     2776   2720   2043   -738    417   -206       O  
ATOM   1956  C   ASP A 243      12.215  11.554   9.991  1.00 16.12           C  
ANISOU 1956  C   ASP A 243     2083   1801   2238   -363    502    -37       C  
ATOM   1957  O   ASP A 243      12.607  12.148   8.966  1.00 20.11           O  
ANISOU 1957  O   ASP A 243     2869   2287   2484   -617    915     73       O  
ATOM   1958  N   VAL A 244      11.494  12.152  10.939  1.00 14.88           N  
ANISOU 1958  N   VAL A 244     1962   1731   1960   -610    471    -17       N  
ATOM   1959  CA  VAL A 244      11.311  13.611  10.898  1.00 14.98           C  
ANISOU 1959  CA  VAL A 244     2034   1812   1844   -424    337   -148       C  
ATOM   1960  CB  VAL A 244      10.255  14.097  11.906  1.00 14.74           C  
ANISOU 1960  CB  VAL A 244     1916   1823   1860   -294    194   -210       C  
ATOM   1961  CG1 VAL A 244      10.124  15.616  11.890  1.00 14.81           C  
ANISOU 1961  CG1 VAL A 244     2090   1809   1727   -157    281   -386       C  
ATOM   1962  CG2 VAL A 244       8.896  13.460  11.652  1.00 14.65           C  
ANISOU 1962  CG2 VAL A 244     1840   1803   1921   -199     58   -184       C  
ATOM   1963  C   VAL A 244      12.670  14.267  11.181  1.00 15.72           C  
ANISOU 1963  C   VAL A 244     2086   1865   2022   -613    577   -154       C  
ATOM   1964  O   VAL A 244      13.351  13.913  12.144  1.00 17.70           O  
ANISOU 1964  O   VAL A 244     2363   1903   2456   -370    273   -280       O  
ATOM   1965  N   LYS A 245      13.041  15.251  10.356  1.00 16.67           N  
ANISOU 1965  N   LYS A 245     2297   1985   2049   -630    492    -77       N  
ATOM   1966  CA  LYS A 245      14.324  15.930  10.516  1.00 19.01           C  
ANISOU 1966  CA  LYS A 245     2418   2206   2598   -726    460   -273       C  
ATOM   1967  CB  LYS A 245      14.841  16.387   9.150  1.00 21.18           C  
ANISOU 1967  CB  LYS A 245     2731   2449   2868   -880    972   -282       C  
ATOM   1968  CG  LYS A 245      15.113  15.246   8.174  1.00 25.13           C  
ANISOU 1968  CG  LYS A 245     3263   3083   3201   -611   1129   -621       C  
ATOM   1969  CD  LYS A 245      15.676  15.759   6.859  1.00 31.19           C  
ANISOU 1969  CD  LYS A 245     4493   3616   3738   -586   1407    -63       C  
ATOM   1970  CE  LYS A 245      16.008  14.682   5.846  1.00 38.84           C  
ANISOU 1970  CE  LYS A 245     5595   4533   4628    235   1364   -685       C  
ATOM   1971  NZ  LYS A 245      16.855  13.622   6.440  1.00 45.45           N  
ANISOU 1971  NZ  LYS A 245     5880   5729   5657    565    849   -428       N  
ATOM   1972  C   LYS A 245      14.191  17.103  11.496  1.00 18.23           C  
ANISOU 1972  C   LYS A 245     2151   2163   2612   -562    495   -184       C  
ATOM   1973  O   LYS A 245      13.154  17.777  11.566  1.00 17.90           O  
ANISOU 1973  O   LYS A 245     1946   1982   2870   -650    283   -108       O  
ATOM   1974  N   LEU A 246      15.287  17.347  12.220  1.00 18.68           N  
ANISOU 1974  N   LEU A 246     1979   2198   2918   -722    451   -233       N  
ATOM   1975  CA  LEU A 246      15.416  18.381  13.223  1.00 20.56           C  
ANISOU 1975  CA  LEU A 246     2175   2408   3226   -814    456   -436       C  
ATOM   1976  CB  LEU A 246      16.224  17.814  14.395  1.00 22.96           C  
ANISOU 1976  CB  LEU A 246     2821   2706   3196   -748    205   -521       C  
ATOM   1977  CG  LEU A 246      15.510  16.782  15.265  1.00 24.46           C  
ANISOU 1977  CG  LEU A 246     2670   3241   3381   -533    489   -221       C  
ATOM   1978  CD1 LEU A 246      16.515  15.799  15.880  1.00 28.55           C  
ANISOU 1978  CD1 LEU A 246     3338   3481   4028   -372    -14   -165       C  
ATOM   1979  CD2 LEU A 246      14.715  17.473  16.358  1.00 23.58           C  
ANISOU 1979  CD2 LEU A 246     2620   3032   3305   -585    436   -262       C  
ATOM   1980  C   LEU A 246      16.139  19.607  12.655  1.00 21.97           C  
ANISOU 1980  C   LEU A 246     2355   2622   3369   -840    753   -314       C  
ATOM   1981  O   LEU A 246      17.069  19.515  11.821  1.00 24.43           O  
ANISOU 1981  O   LEU A 246     2478   2785   4018  -1324   1047   -810       O  
ATOM   1982  N   VAL A 247      15.767  20.765  13.208  1.00 22.19           N  
ANISOU 1982  N   VAL A 247     2303   2722   3403  -1082    715   -529       N  
ATOM   1983  CA AVAL A 247      16.502  21.991  12.984  0.50 24.38           C  
ANISOU 1983  CA AVAL A 247     2386   2833   4043  -1133    570   -402       C  
ATOM   1984  CA BVAL A 247      16.499  22.013  13.027  0.50 22.07           C  
ANISOU 1984  CA BVAL A 247     2317   2463   3602   -883    757   -591       C  
ATOM   1985  CB AVAL A 247      15.801  23.172  13.677  0.50 27.63           C  
ANISOU 1985  CB AVAL A 247     2981   3145   4371   -869    551   -598       C  
ATOM   1986  CB BVAL A 247      15.825  23.148  13.826  0.50 20.94           C  
ANISOU 1986  CB BVAL A 247     2390   2229   3337   -964    774   -537       C  
ATOM   1987  CG1AVAL A 247      16.095  23.219  15.159  0.50 29.08           C  
ANISOU 1987  CG1AVAL A 247     3079   3444   4525   -726    253   -374       C  
ATOM   1988  CG1BVAL A 247      16.734  24.346  14.057  0.50 21.37           C  
ANISOU 1988  CG1BVAL A 247     2483   2245   3390  -1029    773   -371       C  
ATOM   1989  CG2AVAL A 247      16.168  24.489  13.026  0.50 29.65           C  
ANISOU 1989  CG2AVAL A 247     3282   3390   4593   -764    362   -250       C  
ATOM   1990  CG2BVAL A 247      14.517  23.571  13.176  0.50 17.22           C  
ANISOU 1990  CG2BVAL A 247     2189   1428   2923   -965    905   -607       C  
ATOM   1991  C   VAL A 247      17.952  21.801  13.467  1.00 25.39           C  
ANISOU 1991  C   VAL A 247     2471   3051   4125  -1007    522   -567       C  
ATOM   1992  O   VAL A 247      18.223  21.069  14.421  1.00 26.11           O  
ANISOU 1992  O   VAL A 247     2640   3137   4143   -782    534   -519       O  
ATOM   1993  N   ALA A 248      18.881  22.446  12.760  1.00 28.02           N  
ANISOU 1993  N   ALA A 248     2233   3445   4965  -1177    512   -308       N  
ATOM   1994  CA  ALA A 248      20.299  22.314  13.074  1.00 32.42           C  
ANISOU 1994  CA  ALA A 248     2257   4294   5766  -1201    400   -531       C  
ATOM   1995  CB  ALA A 248      21.115  23.153  12.129  1.00 36.13           C  
ANISOU 1995  CB  ALA A 248     3026   4552   6147  -1379    494   -204       C  
ATOM   1996  C   ALA A 248      20.541  22.706  14.537  1.00 33.88           C  
ANISOU 1996  C   ALA A 248     2517   4425   5929  -1387    320   -731       C  
ATOM   1997  O   ALA A 248      20.039  23.724  15.001  1.00 35.81           O  
ANISOU 1997  O   ALA A 248     3334   4885   5385  -1250    450  -1071       O  
ATOM   1998  N   GLY A 249      21.286  21.856  15.258  1.00 36.49           N  
ANISOU 1998  N   GLY A 249     2711   5040   6111  -1766   -195   -701       N  
ATOM   1999  CA  GLY A 249      21.731  22.115  16.635  1.00 37.02           C  
ANISOU 1999  CA  GLY A 249     2590   5268   6205  -1895   -235  -1109       C  
ATOM   2000  C   GLY A 249      20.761  21.618  17.697  1.00 37.11           C  
ANISOU 2000  C   GLY A 249     2463   5704   5931  -1643   -439  -1163       C  
ATOM   2001  O   GLY A 249      21.048  21.748  18.886  1.00 43.34           O  
ANISOU 2001  O   GLY A 249     3465   6694   6308  -1932   -971   -308       O  
ATOM   2002  N   LYS A 250      19.603  21.082  17.286  1.00 32.34           N  
ANISOU 2002  N   LYS A 250     1945   4917   5422  -1133    -56  -1273       N  
ATOM   2003  CA  LYS A 250      18.631  20.524  18.232  1.00 33.68           C  
ANISOU 2003  CA  LYS A 250     2373   5002   5421  -1083     46  -1218       C  
ATOM   2004  CB  LYS A 250      17.217  20.976  17.866  1.00 33.11           C  
ANISOU 2004  CB  LYS A 250     2283   4906   5388  -1102     28  -1406       C  
ATOM   2005  CG  LYS A 250      16.956  22.465  18.016  1.00 33.09           C  
ANISOU 2005  CG  LYS A 250     2092   4985   5493   -967   -349  -1709       C  
ATOM   2006  CD  LYS A 250      17.122  22.985  19.428  1.00 36.59           C  
ANISOU 2006  CD  LYS A 250     2970   5182   5747   -951   -629  -2070       C  
ATOM   2007  CE  LYS A 250      16.594  24.398  19.578  1.00 39.72           C  
ANISOU 2007  CE  LYS A 250     3851   5291   5947   -850   -924  -2478       C  
ATOM   2008  NZ  LYS A 250      16.743  24.901  20.965  1.00 44.35           N  
ANISOU 2008  NZ  LYS A 250     4712   5948   6191   -663  -1410  -2521       N  
ATOM   2009  C   LYS A 250      18.719  18.993  18.230  1.00 34.13           C  
ANISOU 2009  C   LYS A 250     2667   5093   5207   -641    381   -958       C  
ATOM   2010  O   LYS A 250      18.723  18.386  17.169  1.00 35.72           O  
ANISOU 2010  O   LYS A 250     3513   4587   5469    117    477  -1153       O  
ATOM   2011  N   ALA A 251      18.735  18.401  19.432  1.00 35.00           N  
ANISOU 2011  N   ALA A 251     2668   5477   5153   -323   -448   -779       N  
ATOM   2012  CA  ALA A 251      18.868  16.962  19.646  1.00 36.51           C  
ANISOU 2012  CA  ALA A 251     2470   5559   5839   -224   -612   -285       C  
ATOM   2013  CB  ALA A 251      19.536  16.728  20.977  1.00 41.38           C  
ANISOU 2013  CB  ALA A 251     3037   6413   6270   -630  -1236   -236       C  
ATOM   2014  C   ALA A 251      17.522  16.217  19.594  1.00 33.85           C  
ANISOU 2014  C   ALA A 251     2583   4935   5340   -291   -338   -268       C  
ATOM   2015  O   ALA A 251      17.494  15.046  19.261  1.00 36.02           O  
ANISOU 2015  O   ALA A 251     2663   4906   6117    118    398    -99       O  
ATOM   2016  N   ASP A 252      16.418  16.868  19.982  1.00 27.99           N  
ANISOU 2016  N   ASP A 252     2865   3452   4315   -420   -816   -336       N  
ATOM   2017  CA  ASP A 252      15.095  16.231  19.993  1.00 26.03           C  
ANISOU 2017  CA  ASP A 252     2194   3909   3785     16   -168     48       C  
ATOM   2018  CB  ASP A 252      14.835  15.371  21.257  1.00 27.94           C  
ANISOU 2018  CB  ASP A 252     2712   4033   3871     18   -269    280       C  
ATOM   2019  CG  ASP A 252      13.740  14.269  21.209  1.00 27.59           C  
ANISOU 2019  CG  ASP A 252     3384   3724   3373   -154   -255    360       C  
ATOM   2020  OD1 ASP A 252      13.030  14.127  20.149  1.00 21.90           O  
ANISOU 2020  OD1 ASP A 252     2449   2718   3151   -574    234    194       O  
ATOM   2021  OD2 ASP A 252      13.529  13.541  22.280  1.00 24.60           O  
ANISOU 2021  OD2 ASP A 252     2668   2554   4125   -771   -249    332       O  
ATOM   2022  C   ASP A 252      14.070  17.358  19.812  1.00 21.03           C  
ANISOU 2022  C   ASP A 252     2387   3251   2349   -311    -74   -440       C  
ATOM   2023  O   ASP A 252      14.387  18.552  19.903  1.00 24.25           O  
ANISOU 2023  O   ASP A 252     2684   3407   3122   -573    253   -892       O  
ATOM   2024  N   PHE A 253      12.839  16.950  19.517  1.00 19.40           N  
ANISOU 2024  N   PHE A 253     2211   2916   2245   -420     74   -346       N  
ATOM   2025  CA  PHE A 253      11.724  17.856  19.453  1.00 17.62           C  
ANISOU 2025  CA  PHE A 253     1932   2579   2182   -521    316   -337       C  
ATOM   2026  CB  PHE A 253      10.525  17.174  18.794  1.00 17.41           C  
ANISOU 2026  CB  PHE A 253     1925   2495   2192   -492    250   -122       C  
ATOM   2027  CG  PHE A 253      10.896  16.627  17.449  1.00 18.47           C  
ANISOU 2027  CG  PHE A 253     2192   2485   2338   -170    335   -300       C  
ATOM   2028  CD1 PHE A 253      10.999  17.458  16.344  1.00 18.83           C  
ANISOU 2028  CD1 PHE A 253     2463   2345   2347   -247    302   -383       C  
ATOM   2029  CE1 PHE A 253      11.419  16.958  15.117  1.00 18.23           C  
ANISOU 2029  CE1 PHE A 253     2541   2420   1961   -277    253   -145       C  
ATOM   2030  CZ  PHE A 253      11.742  15.629  14.995  1.00 17.64           C  
ANISOU 2030  CZ  PHE A 253     2228   2575   1896   -155    122   -473       C  
ATOM   2031  CD2 PHE A 253      11.225  15.290  17.307  1.00 18.51           C  
ANISOU 2031  CD2 PHE A 253     2371   2404   2257   -212     -3   -369       C  
ATOM   2032  CE2 PHE A 253      11.664  14.807  16.088  1.00 18.26           C  
ANISOU 2032  CE2 PHE A 253     2225   2339   2373    -89     95   -435       C  
ATOM   2033  C   PHE A 253      11.400  18.375  20.847  1.00 18.56           C  
ANISOU 2033  C   PHE A 253     2263   2816   1972   -600    -88   -347       C  
ATOM   2034  O   PHE A 253      11.625  17.696  21.839  1.00 20.11           O  
ANISOU 2034  O   PHE A 253     2761   2731   2148   -456   -151   -138       O  
ATOM   2035  N   GLU A 254      10.866  19.599  20.884  1.00 20.51           N  
ANISOU 2035  N   GLU A 254     2570   2833   2391   -425    236   -314       N  
ATOM   2036  CA  GLU A 254      10.327  20.204  22.112  1.00 20.93           C  
ANISOU 2036  CA  GLU A 254     2423   3125   2405   -250    311   -296       C  
ATOM   2037  CB  GLU A 254      10.977  21.564  22.361  1.00 24.49           C  
ANISOU 2037  CB  GLU A 254     2953   3662   2689   -659     87   -836       C  
ATOM   2038  CG  GLU A 254      10.470  22.294  23.598  1.00 30.97           C  
ANISOU 2038  CG  GLU A 254     3977   4137   3653   -440    594  -1267       C  
ATOM   2039  CD  GLU A 254      11.089  23.675  23.822  1.00 37.54           C  
ANISOU 2039  CD  GLU A 254     4738   4944   4580  -1166    838  -2082       C  
ATOM   2040  OE1 GLU A 254      12.051  24.041  23.093  1.00 44.95           O  
ANISOU 2040  OE1 GLU A 254     5456   6285   5336  -1716   1279  -1848       O  
ATOM   2041  OE2 GLU A 254      10.594  24.400  24.708  1.00 49.04           O  
ANISOU 2041  OE2 GLU A 254     6763   5962   5906     36   1508  -2373       O  
ATOM   2042  C   GLU A 254       8.820  20.331  21.904  1.00 19.26           C  
ANISOU 2042  C   GLU A 254     2329   3030   1957   -438    366   -306       C  
ATOM   2043  O   GLU A 254       8.381  20.916  20.913  1.00 21.33           O  
ANISOU 2043  O   GLU A 254     2332   3780   1990   -563    437    146       O  
ATOM   2044  N   VAL A 255       8.052  19.743  22.823  1.00 16.41           N  
ANISOU 2044  N   VAL A 255     2310   2029   1894   -314    240   -336       N  
ATOM   2045  CA  VAL A 255       6.608  19.689  22.675  1.00 16.59           C  
ANISOU 2045  CA  VAL A 255     2276   1990   2035   -388    240   -209       C  
ATOM   2046  CB  VAL A 255       6.122  18.260  22.425  1.00 16.99           C  
ANISOU 2046  CB  VAL A 255     2701   1999   1753   -447    249     13       C  
ATOM   2047  CG1 VAL A 255       4.612  18.222  22.256  1.00 17.42           C  
ANISOU 2047  CG1 VAL A 255     2696   2024   1895   -579     99     -2       C  
ATOM   2048  CG2 VAL A 255       6.821  17.657  21.213  1.00 18.58           C  
ANISOU 2048  CG2 VAL A 255     2851   2276   1932   -263    361   -110       C  
ATOM   2049  C   VAL A 255       5.957  20.274  23.927  1.00 15.32           C  
ANISOU 2049  C   VAL A 255     2008   1915   1897   -660    203   -214       C  
ATOM   2050  O   VAL A 255       6.384  19.985  25.045  1.00 16.31           O  
ANISOU 2050  O   VAL A 255     2380   1902   1915   -391    167   -150       O  
ATOM   2051  N   ASP A 256       4.926  21.104  23.717  1.00 16.16           N  
ANISOU 2051  N   ASP A 256     2042   2270   1826   -490    294   -293       N  
ATOM   2052  CA AASP A 256       4.168  21.756  24.782  0.50 16.04           C  
ANISOU 2052  CA AASP A 256     2011   2270   1813   -539    286   -343       C  
ATOM   2053  CA BASP A 256       4.183  21.621  24.861  0.50 16.49           C  
ANISOU 2053  CA BASP A 256     2069   2406   1789   -495    366   -251       C  
ATOM   2054  CB AASP A 256       4.335  23.271  24.696  0.50 17.72           C  
ANISOU 2054  CB AASP A 256     1955   2319   2459   -558    193   -554       C  
ATOM   2055  CB BASP A 256       4.598  23.037  25.263  0.50 18.66           C  
ANISOU 2055  CB BASP A 256     2453   2475   2159   -505    524   -381       C  
ATOM   2056  CG AASP A 256       5.774  23.721  24.861  0.50 20.65           C  
ANISOU 2056  CG AASP A 256     2116   2677   3054   -879    118   -771       C  
ATOM   2057  CG BASP A 256       4.078  24.115  24.346  0.50 21.17           C  
ANISOU 2057  CG BASP A 256     2802   2735   2506   -378    390   -200       C  
ATOM   2058  OD1AASP A 256       6.418  23.219  25.787  0.50 25.37           O  
ANISOU 2058  OD1AASP A 256     2226   3095   4315   -926   -657   -897       O  
ATOM   2059  OD1BASP A 256       4.757  24.376  23.329  0.50 23.89           O  
ANISOU 2059  OD1BASP A 256     3049   3341   2686   -298    637   -250       O  
ATOM   2060  OD2AASP A 256       6.222  24.571  24.066  0.50 27.23           O  
ANISOU 2060  OD2AASP A 256     2556   3430   4360  -1470     13   -276       O  
ATOM   2061  OD2BASP A 256       3.022  24.714  24.694  0.50 21.62           O  
ANISOU 2061  OD2BASP A 256     2976   2274   2962   -444    548   -496       O  
ATOM   2062  C   ASP A 256       2.683  21.420  24.641  1.00 15.79           C  
ANISOU 2062  C   ASP A 256     2143   2143   1714   -631    149   -287       C  
ATOM   2063  O   ASP A 256       2.152  21.552  23.539  1.00 16.87           O  
ANISOU 2063  O   ASP A 256     2225   2710   1473   -907    285   -285       O  
ATOM   2064  N   ILE A 257       2.033  21.071  25.752  1.00 15.25           N  
ANISOU 2064  N   ILE A 257     2205   2042   1546   -360     77   -175       N  
ATOM   2065  CA  ILE A 257       0.599  20.851  25.857  1.00 14.05           C  
ANISOU 2065  CA  ILE A 257     2127   1816   1395   -411     34   -307       C  
ATOM   2066  CB  ILE A 257       0.291  19.634  26.751  1.00 14.56           C  
ANISOU 2066  CB  ILE A 257     2182   1929   1420   -459      8   -260       C  
ATOM   2067  CG1 ILE A 257       1.019  18.372  26.281  1.00 16.10           C  
ANISOU 2067  CG1 ILE A 257     2208   1998   1910   -329     14   -243       C  
ATOM   2068  CG2 ILE A 257      -1.210  19.414  26.890  1.00 14.74           C  
ANISOU 2068  CG2 ILE A 257     2236   1942   1423   -477     49   -172       C  
ATOM   2069  CD1 ILE A 257       0.686  17.937  24.867  1.00 17.07           C  
ANISOU 2069  CD1 ILE A 257     2407   2051   2028   -222    -20   -366       C  
ATOM   2070  C   ILE A 257      -0.033  22.111  26.441  1.00 14.26           C  
ANISOU 2070  C   ILE A 257     1938   1805   1673   -426    240   -175       C  
ATOM   2071  O   ILE A 257       0.392  22.579  27.507  1.00 17.13           O  
ANISOU 2071  O   ILE A 257     2323   2338   1845   -479    342   -530       O  
ATOM   2072  N   THR A 258      -1.072  22.601  25.763  1.00 13.49           N  
ANISOU 2072  N   THR A 258     1930   1617   1576   -392    196   -360       N  
ATOM   2073  CA  THR A 258      -1.859  23.699  26.250  1.00 14.16           C  
ANISOU 2073  CA  THR A 258     2153   1539   1688   -436    442   -554       C  
ATOM   2074  CB  THR A 258      -1.476  25.027  25.575  1.00 16.44           C  
ANISOU 2074  CB  THR A 258     2267   1776   2203   -447    592   -312       C  
ATOM   2075  OG1 THR A 258      -1.729  24.930  24.171  1.00 17.74           O  
ANISOU 2075  OG1 THR A 258     2651   1948   2140   -389    536    -68       O  
ATOM   2076  CG2 THR A 258      -0.027  25.420  25.803  1.00 17.57           C  
ANISOU 2076  CG2 THR A 258     2464   1940   2269   -613    598   -368       C  
ATOM   2077  C   THR A 258      -3.346  23.404  26.039  1.00 13.99           C  
ANISOU 2077  C   THR A 258     2166   1354   1792   -356    368   -269       C  
ATOM   2078  O   THR A 258      -3.727  22.530  25.235  1.00 14.34           O  
ANISOU 2078  O   THR A 258     2095   1735   1618   -453    431   -427       O  
ATOM   2079  N   GLY A 259      -4.192  24.159  26.749  1.00 13.70           N  
ANISOU 2079  N   GLY A 259     2340   1169   1696   -347    246   -392       N  
ATOM   2080  CA  GLY A 259      -5.643  24.043  26.558  1.00 14.14           C  
ANISOU 2080  CA  GLY A 259     2300   1355   1714   -379    361   -343       C  
ATOM   2081  C   GLY A 259      -6.192  22.700  27.005  1.00 13.85           C  
ANISOU 2081  C   GLY A 259     2253   1264   1742   -303    260   -418       C  
ATOM   2082  O   GLY A 259      -7.262  22.288  26.549  1.00 14.92           O  
ANISOU 2082  O   GLY A 259     2223   1542   1903   -411    194    -84       O  
ATOM   2083  N   PHE A 260      -5.472  22.003  27.893  1.00 12.89           N  
ANISOU 2083  N   PHE A 260     1988   1307   1602   -520    214   -307       N  
ATOM   2084  CA  PHE A 260      -5.899  20.653  28.291  1.00 12.87           C  
ANISOU 2084  CA  PHE A 260     2149   1251   1487   -436    340   -407       C  
ATOM   2085  CB  PHE A 260      -4.823  19.982  29.146  1.00 13.68           C  
ANISOU 2085  CB  PHE A 260     1976   1562   1658   -225    415   -427       C  
ATOM   2086  CG  PHE A 260      -5.169  18.594  29.592  1.00 13.36           C  
ANISOU 2086  CG  PHE A 260     1972   1520   1581   -312    153   -458       C  
ATOM   2087  CD1 PHE A 260      -4.903  17.512  28.770  1.00 13.07           C  
ANISOU 2087  CD1 PHE A 260     2049   1258   1656   -429     69   -344       C  
ATOM   2088  CE1 PHE A 260      -5.220  16.230  29.179  1.00 13.98           C  
ANISOU 2088  CE1 PHE A 260     2376   1014   1919   -212    -20   -451       C  
ATOM   2089  CZ  PHE A 260      -5.851  16.020  30.374  1.00 14.31           C  
ANISOU 2089  CZ  PHE A 260     2149   1254   2034   -244     -6    -71       C  
ATOM   2090  CD2 PHE A 260      -5.814  18.359  30.794  1.00 12.81           C  
ANISOU 2090  CD2 PHE A 260     1864   1349   1654   -366    117   -462       C  
ATOM   2091  CE2 PHE A 260      -6.133  17.073  31.196  1.00 14.70           C  
ANISOU 2091  CE2 PHE A 260     2171   1549   1863   -389    186   -174       C  
ATOM   2092  C   PHE A 260      -7.252  20.692  29.018  1.00 13.03           C  
ANISOU 2092  C   PHE A 260     2075   1242   1633   -405    324   -295       C  
ATOM   2093  O   PHE A 260      -7.451  21.485  29.957  1.00 14.21           O  
ANISOU 2093  O   PHE A 260     2226   1600   1572   -413    344   -428       O  
ATOM   2094  N   LYS A 261      -8.149  19.788  28.588  1.00 11.65           N  
ANISOU 2094  N   LYS A 261     1915   1192   1317   -247    249   -308       N  
ATOM   2095  CA  LYS A 261      -9.443  19.567  29.204  1.00 12.07           C  
ANISOU 2095  CA  LYS A 261     1908   1215   1463   -310    259   -243       C  
ATOM   2096  CB  LYS A 261     -10.553  20.206  28.371  1.00 14.04           C  
ANISOU 2096  CB  LYS A 261     1759   1586   1988   -133    280   -184       C  
ATOM   2097  CG  LYS A 261     -10.468  21.723  28.250  1.00 17.15           C  
ANISOU 2097  CG  LYS A 261     2184   1587   2744   -178    106    -47       C  
ATOM   2098  CD  LYS A 261     -10.701  22.443  29.561  1.00 21.25           C  
ANISOU 2098  CD  LYS A 261     3013   1987   3073   -199    173   -293       C  
ATOM   2099  CE  LYS A 261     -10.548  23.949  29.502  1.00 26.49           C  
ANISOU 2099  CE  LYS A 261     3526   2045   4494   -118    498   -518       C  
ATOM   2100  NZ  LYS A 261     -10.615  24.558  30.864  1.00 32.85           N  
ANISOU 2100  NZ  LYS A 261     4342   2619   5520    160     33  -1287       N  
ATOM   2101  C   LYS A 261      -9.693  18.067  29.321  1.00 11.30           C  
ANISOU 2101  C   LYS A 261     1764   1203   1324   -207    267   -257       C  
ATOM   2102  O   LYS A 261      -9.222  17.275  28.483  1.00 11.91           O  
ANISOU 2102  O   LYS A 261     1769   1324   1433   -279    435   -321       O  
ATOM   2103  N   ILE A 262     -10.480  17.687  30.322  1.00 10.96           N  
ANISOU 2103  N   ILE A 262     1755   1122   1288   -188    330   -382       N  
ATOM   2104  CA  ILE A 262     -10.822  16.293  30.537  1.00 11.53           C  
ANISOU 2104  CA  ILE A 262     1819   1189   1370   -298    232   -354       C  
ATOM   2105  CB  ILE A 262      -9.753  15.572  31.376  1.00 12.24           C  
ANISOU 2105  CB  ILE A 262     1807   1417   1424   -313    187   -269       C  
ATOM   2106  CG1 ILE A 262     -10.031  14.075  31.485  1.00 12.23           C  
ANISOU 2106  CG1 ILE A 262     1574   1438   1635   -323    144   -210       C  
ATOM   2107  CG2 ILE A 262      -9.616  16.215  32.741  1.00 13.32           C  
ANISOU 2107  CG2 ILE A 262     1929   1676   1454   -242    107   -337       C  
ATOM   2108  CD1 ILE A 262      -8.903  13.271  32.117  1.00 13.04           C  
ANISOU 2108  CD1 ILE A 262     2027   1529   1396   -209     51    -61       C  
ATOM   2109  C   ILE A 262     -12.213  16.195  31.174  1.00 11.45           C  
ANISOU 2109  C   ILE A 262     1772   1257   1322   -175    254   -231       C  
ATOM   2110  O   ILE A 262     -12.560  16.955  32.088  1.00 13.51           O  
ANISOU 2110  O   ILE A 262     1962   1625   1546   -207    492   -418       O  
ATOM   2111  N   ASN A 263     -13.010  15.251  30.660  1.00 11.51           N  
ANISOU 2111  N   ASN A 263     1931   1197   1242   -190    330   -219       N  
ATOM   2112  CA AASN A 263     -14.295  14.918  31.225  0.50 11.92           C  
ANISOU 2112  CA AASN A 263     1862   1292   1375   -198    229   -180       C  
ATOM   2113  CA BASN A 263     -14.299  14.917  31.219  0.50 11.60           C  
ANISOU 2113  CA BASN A 263     1790   1276   1343   -212    276   -176       C  
ATOM   2114  CB AASN A 263     -15.457  15.408  30.366  0.50 13.60           C  
ANISOU 2114  CB AASN A 263     2169   1502   1494    -37    108    -19       C  
ATOM   2115  CB BASN A 263     -15.453  15.435  30.360  0.50 11.43           C  
ANISOU 2115  CB BASN A 263     1675   1302   1365   -209    403      0       C  
ATOM   2116  CG AASN A 263     -15.586  16.908  30.246  0.50 15.24           C  
ANISOU 2116  CG AASN A 263     2488   1549   1750    -15   -175    114       C  
ATOM   2117  CG BASN A 263     -15.530  16.945  30.308  0.50 11.24           C  
ANISOU 2117  CG BASN A 263     1560   1302   1406   -296    407    100       C  
ATOM   2118  OD1AASN A 263     -16.233  17.375  29.304  0.50 18.84           O  
ANISOU 2118  OD1AASN A 263     2890   2075   2194    144   -513    320       O  
ATOM   2119  OD1BASN A 263     -14.835  17.579  29.498  0.50 12.90           O  
ANISOU 2119  OD1BASN A 263     1487   1670   1745   -554    442    195       O  
ATOM   2120  ND2AASN A 263     -15.024  17.657  31.175  0.50 16.96           N  
ANISOU 2120  ND2AASN A 263     3100   1695   1647     79   -273      7       N  
ATOM   2121  ND2BASN A 263     -16.306  17.517  31.206  0.50 10.60           N  
ANISOU 2121  ND2BASN A 263     1441   1086   1498   -235    418    182       N  
ATOM   2122  C   ASN A 263     -14.412  13.394  31.330  1.00 10.99           C  
ANISOU 2122  C   ASN A 263     1627   1291   1254    -97    269   -167       C  
ATOM   2123  O   ASN A 263     -13.788  12.683  30.565  1.00 11.80           O  
ANISOU 2123  O   ASN A 263     1934   1136   1411   -236    521   -234       O  
ATOM   2124  N   MET A 264     -15.231  12.927  32.280  1.00 10.89           N  
ANISOU 2124  N   MET A 264     1627   1241   1268   -218    288   -222       N  
ATOM   2125  CA  MET A 264     -15.519  11.518  32.425  1.00 11.75           C  
ANISOU 2125  CA  MET A 264     1725   1295   1442   -174    274   -262       C  
ATOM   2126  CB  MET A 264     -15.442  11.044  33.875  1.00 12.17           C  
ANISOU 2126  CB  MET A 264     1829   1397   1398   -228    120   -304       C  
ATOM   2127  CG  MET A 264     -15.706   9.561  33.990  1.00 13.25           C  
ANISOU 2127  CG  MET A 264     2237   1413   1383   -207    256   -252       C  
ATOM   2128  SD  MET A 264     -15.277   8.851  35.586  1.00 15.03           S  
ANISOU 2128  SD  MET A 264     2602   1604   1504    -19    201     -7       S  
ATOM   2129  CE  MET A 264     -16.510   9.633  36.602  1.00 18.78           C  
ANISOU 2129  CE  MET A 264     3156   2211   1766    133    530    -50       C  
ATOM   2130  C   MET A 264     -16.921  11.281  31.860  1.00 10.67           C  
ANISOU 2130  C   MET A 264     1706   1082   1266   -176    266   -233       C  
ATOM   2131  O   MET A 264     -17.873  11.967  32.252  1.00 12.69           O  
ANISOU 2131  O   MET A 264     1632   1427   1762      2     75   -437       O  
ATOM   2132  N   LEU A 265     -17.022  10.351  30.911  1.00 10.93           N  
ANISOU 2132  N   LEU A 265     1739   1089   1322    -71    146   -277       N  
ATOM   2133  CA  LEU A 265     -18.259  10.071  30.178  1.00 11.31           C  
ANISOU 2133  CA  LEU A 265     1763   1148   1386    -95     84   -200       C  
ATOM   2134  CB  LEU A 265     -18.005  10.157  28.677  1.00 12.93           C  
ANISOU 2134  CB  LEU A 265     2014   1514   1383   -192    -91   -117       C  
ATOM   2135  CG  LEU A 265     -18.044  11.561  28.068  1.00 14.73           C  
ANISOU 2135  CG  LEU A 265     2633   1610   1351   -256    -21    -52       C  
ATOM   2136  CD1 LEU A 265     -17.052  12.515  28.694  1.00 16.40           C  
ANISOU 2136  CD1 LEU A 265     3080   1550   1599   -252   -130   -144       C  
ATOM   2137  CD2 LEU A 265     -17.829  11.476  26.570  1.00 16.48           C  
ANISOU 2137  CD2 LEU A 265     2988   1963   1309   -308     -6    206       C  
ATOM   2138  C   LEU A 265     -18.725   8.668  30.553  1.00 10.51           C  
ANISOU 2138  C   LEU A 265     1725   1221   1047   -196    122   -238       C  
ATOM   2139  O   LEU A 265     -17.963   7.701  30.415  1.00 12.33           O  
ANISOU 2139  O   LEU A 265     2072   1128   1483   -175    337   -276       O  
ATOM   2140  N   VAL A 266     -19.964   8.548  31.006  1.00 11.39           N  
ANISOU 2140  N   VAL A 266     1801   1101   1423   -145    316   -244       N  
ATOM   2141  CA  VAL A 266     -20.484   7.237  31.365  1.00 11.42           C  
ANISOU 2141  CA  VAL A 266     1850   1093   1394   -131    154   -134       C  
ATOM   2142  CB  VAL A 266     -20.017   6.831  32.781  1.00 12.44           C  
ANISOU 2142  CB  VAL A 266     1858   1360   1508   -146     70    -88       C  
ATOM   2143  CG1 VAL A 266     -20.626   7.700  33.870  1.00 13.32           C  
ANISOU 2143  CG1 VAL A 266     2150   1491   1419    -60    208     73       C  
ATOM   2144  CG2 VAL A 266     -20.269   5.354  33.057  1.00 13.35           C  
ANISOU 2144  CG2 VAL A 266     1925   1381   1763   -103     33    -54       C  
ATOM   2145  C   VAL A 266     -22.012   7.261  31.252  1.00 10.72           C  
ANISOU 2145  C   VAL A 266     1770    999   1303    -94    221   -190       C  
ATOM   2146  O   VAL A 266     -22.676   8.254  31.598  1.00 11.04           O  
ANISOU 2146  O   VAL A 266     1779   1024   1390    -72    155   -325       O  
ATOM   2147  N   GLN A 267     -22.567   6.128  30.794  1.00 11.49           N  
ANISOU 2147  N   GLN A 267     1781   1037   1545    -89     23   -165       N  
ATOM   2148  CA  GLN A 267     -24.014   5.956  30.732  1.00 12.00           C  
ANISOU 2148  CA  GLN A 267     1844   1309   1404   -189     -7   -142       C  
ATOM   2149  CB  GLN A 267     -24.361   4.703  29.938  1.00 12.83           C  
ANISOU 2149  CB  GLN A 267     2065   1318   1489   -180     56   -180       C  
ATOM   2150  CG  GLN A 267     -24.114   4.848  28.438  1.00 12.69           C  
ANISOU 2150  CG  GLN A 267     1959   1402   1460   -126     25   -104       C  
ATOM   2151  CD  GLN A 267     -23.956   3.509  27.758  1.00 11.98           C  
ANISOU 2151  CD  GLN A 267     1886   1460   1206    -61     52    -50       C  
ATOM   2152  OE1 GLN A 267     -23.020   2.764  28.056  1.00 14.03           O  
ANISOU 2152  OE1 GLN A 267     1888   1722   1718    -69   -300     13       O  
ATOM   2153  NE2 GLN A 267     -24.895   3.173  26.878  1.00 13.46           N  
ANISOU 2153  NE2 GLN A 267     2095   1801   1217   -379     59    -43       N  
ATOM   2154  C   GLN A 267     -24.576   5.883  32.153  1.00 11.85           C  
ANISOU 2154  C   GLN A 267     1645   1347   1511   -121     27   -140       C  
ATOM   2155  O   GLN A 267     -23.920   5.403  33.095  1.00 11.67           O  
ANISOU 2155  O   GLN A 267     1849   1190   1392    -38    -31   -145       O  
ATOM   2156  N   ASN A 268     -25.809   6.363  32.294  1.00 11.62           N  
ANISOU 2156  N   ASN A 268     1646   1313   1455    -83    115     -6       N  
ATOM   2157  CA  ASN A 268     -26.507   6.306  33.563  1.00 12.15           C  
ANISOU 2157  CA  ASN A 268     1676   1469   1469    102    164    -52       C  
ATOM   2158  CB  ASN A 268     -26.201   7.536  34.422  1.00 13.77           C  
ANISOU 2158  CB  ASN A 268     1886   1556   1787    124    -22   -149       C  
ATOM   2159  CG  ASN A 268     -26.957   7.566  35.731  1.00 15.12           C  
ANISOU 2159  CG  ASN A 268     2169   1880   1695    436    -77   -642       C  
ATOM   2160  OD1 ASN A 268     -27.742   8.483  35.922  1.00 24.73           O  
ANISOU 2160  OD1 ASN A 268     3905   3477   2013   2045     95   -281       O  
ATOM   2161  ND2 ASN A 268     -26.674   6.668  36.653  1.00 13.86           N  
ANISOU 2161  ND2 ASN A 268     1945   1481   1836   -311    185   -394       N  
ATOM   2162  C   ASN A 268     -27.989   6.178  33.224  1.00 11.77           C  
ANISOU 2162  C   ASN A 268     1655   1265   1552      0    169    -35       C  
ATOM   2163  O   ASN A 268     -28.484   6.932  32.396  1.00 14.74           O  
ANISOU 2163  O   ASN A 268     1950   1668   1981    110     78    224       O  
ATOM   2164  N   TRP A 269     -28.699   5.241  33.860  1.00 11.90           N  
ANISOU 2164  N   TRP A 269     1755   1244   1520     -7    252    -65       N  
ATOM   2165  CA  TRP A 269     -30.060   4.955  33.466  1.00 12.08           C  
ANISOU 2165  CA  TRP A 269     1774   1253   1559     85    179   -194       C  
ATOM   2166  CB  TRP A 269     -30.093   4.180  32.140  1.00 12.59           C  
ANISOU 2166  CB  TRP A 269     1776   1579   1426    -48    134   -123       C  
ATOM   2167  CG  TRP A 269     -29.640   2.759  32.235  1.00 12.45           C  
ANISOU 2167  CG  TRP A 269     1747   1546   1437    -34    174   -213       C  
ATOM   2168  CD1 TRP A 269     -30.434   1.644  32.276  1.00 13.01           C  
ANISOU 2168  CD1 TRP A 269     1800   1526   1615    -31    227   -200       C  
ATOM   2169  NE1 TRP A 269     -29.661   0.513  32.342  1.00 12.92           N  
ANISOU 2169  NE1 TRP A 269     1830   1381   1696   -125    365   -112       N  
ATOM   2170  CE2 TRP A 269     -28.336   0.878  32.367  1.00 12.84           C  
ANISOU 2170  CE2 TRP A 269     1833   1500   1544    -31    314   -242       C  
ATOM   2171  CD2 TRP A 269     -28.283   2.284  32.284  1.00 12.52           C  
ANISOU 2171  CD2 TRP A 269     1777   1527   1452    -48    196   -134       C  
ATOM   2172  CE3 TRP A 269     -27.030   2.898  32.255  1.00 12.08           C  
ANISOU 2172  CE3 TRP A 269     1850   1288   1450    -63    265    -86       C  
ATOM   2173  CZ3 TRP A 269     -25.893   2.126  32.300  1.00 13.16           C  
ANISOU 2173  CZ3 TRP A 269     1948   1515   1537    -21    186   -174       C  
ATOM   2174  CH2 TRP A 269     -25.969   0.742  32.402  1.00 13.43           C  
ANISOU 2174  CH2 TRP A 269     1979   1477   1644      9    256    -97       C  
ATOM   2175  CZ2 TRP A 269     -27.179   0.095  32.438  1.00 12.67           C  
ANISOU 2175  CZ2 TRP A 269     1863   1393   1558    -46    251   -223       C  
ATOM   2176  C   TRP A 269     -30.802   4.210  34.564  1.00 12.59           C  
ANISOU 2176  C   TRP A 269     1719   1592   1470   -136    170   -396       C  
ATOM   2177  O   TRP A 269     -30.190   3.599  35.441  1.00 13.25           O  
ANISOU 2177  O   TRP A 269     1845   1781   1408    -40    242   -252       O  
ATOM   2178  N   VAL A 270     -32.134   4.252  34.452  1.00 14.48           N  
ANISOU 2178  N   VAL A 270     1697   2037   1765   -102    298   -200       N  
ATOM   2179  CA  VAL A 270     -33.038   3.512  35.332  1.00 15.21           C  
ANISOU 2179  CA  VAL A 270     1756   2110   1912   -288    433   -353       C  
ATOM   2180  CB  VAL A 270     -34.412   4.194  35.405  1.00 17.39           C  
ANISOU 2180  CB  VAL A 270     1788   2301   2515   -301    450   -678       C  
ATOM   2181  CG1 VAL A 270     -35.367   3.421  36.311  1.00 19.98           C  
ANISOU 2181  CG1 VAL A 270     2209   2498   2881   -440    835   -824       C  
ATOM   2182  CG2 VAL A 270     -34.281   5.635  35.850  1.00 18.32           C  
ANISOU 2182  CG2 VAL A 270     1923   2221   2817   -112    429   -595       C  
ATOM   2183  C   VAL A 270     -33.179   2.077  34.827  1.00 15.74           C  
ANISOU 2183  C   VAL A 270     1973   2171   1833   -325    348   -321       C  
ATOM   2184  O   VAL A 270     -33.453   1.856  33.653  1.00 17.21           O  
ANISOU 2184  O   VAL A 270     2022   2686   1831   -314    334   -365       O  
ATOM   2185  N   ALA A 271     -33.064   1.116  35.755  1.00 16.52           N  
ANISOU 2185  N   ALA A 271     2191   2099   1986   -370    314   -221       N  
ATOM   2186  CA  ALA A 271     -33.218  -0.293  35.398  1.00 18.08           C  
ANISOU 2186  CA  ALA A 271     2251   2234   2384   -193    149   -390       C  
ATOM   2187  CB  ALA A 271     -33.099  -1.160  36.618  1.00 18.39           C  
ANISOU 2187  CB  ALA A 271     2491   2153   2341   -292     52   -297       C  
ATOM   2188  C   ALA A 271     -34.573  -0.491  34.728  1.00 18.32           C  
ANISOU 2188  C   ALA A 271     2287   2507   2164   -231    158   -521       C  
ATOM   2189  O   ALA A 271     -35.598   0.017  35.187  1.00 19.70           O  
ANISOU 2189  O   ALA A 271     2005   2342   3135   -316    172   -586       O  
ATOM   2190  N   PRO A 272     -34.628  -1.245  33.614  1.00 19.22           N  
ANISOU 2190  N   PRO A 272     2326   2345   2630   -114    255   -844       N  
ATOM   2191  CA  PRO A 272     -35.899  -1.535  32.959  1.00 20.60           C  
ANISOU 2191  CA  PRO A 272     2397   2566   2864   -232     86   -762       C  
ATOM   2192  CB  PRO A 272     -35.515  -2.324  31.700  1.00 23.98           C  
ANISOU 2192  CB  PRO A 272     2769   3281   3060    -71    -16  -1024       C  
ATOM   2193  CG  PRO A 272     -34.163  -2.884  32.023  1.00 27.53           C  
ANISOU 2193  CG  PRO A 272     2927   3621   3912    128   -107  -1367       C  
ATOM   2194  CD  PRO A 272     -33.491  -1.895  32.952  1.00 22.33           C  
ANISOU 2194  CD  PRO A 272     2175   3047   3262    298    -17   -934       C  
ATOM   2195  C   PRO A 272     -36.787  -2.378  33.880  1.00 20.41           C  
ANISOU 2195  C   PRO A 272     2386   2542   2826    -61    275   -740       C  
ATOM   2196  O   PRO A 272     -36.285  -3.252  34.635  1.00 19.26           O  
ANISOU 2196  O   PRO A 272     2332   2206   2780   -357     58   -727       O  
ATOM   2197  N   LEU A 273     -38.097  -2.135  33.803  1.00 21.81           N  
ANISOU 2197  N   LEU A 273     2607   2388   3289    202    239   -798       N  
ATOM   2198  CA  LEU A 273     -39.068  -2.897  34.584  1.00 24.34           C  
ANISOU 2198  CA  LEU A 273     3012   2747   3487    246    495   -424       C  
ATOM   2199  CB  LEU A 273     -40.475  -2.515  34.117  1.00 28.45           C  
ANISOU 2199  CB  LEU A 273     3163   3778   3867    850    676   -112       C  
ATOM   2200  CG  LEU A 273     -40.922  -1.091  34.439  1.00 33.53           C  
ANISOU 2200  CG  LEU A 273     4248   4133   4359   1140    444   -283       C  
ATOM   2201  CD1 LEU A 273     -42.298  -0.824  33.839  1.00 35.96           C  
ANISOU 2201  CD1 LEU A 273     3611   5210   4838   1644    871   -385       C  
ATOM   2202  CD2 LEU A 273     -40.927  -0.821  35.948  1.00 34.29           C  
ANISOU 2202  CD2 LEU A 273     4640   4184   4202   1009    413   -475       C  
ATOM   2203  C   LEU A 273     -38.861  -4.406  34.375  1.00 22.42           C  
ANISOU 2203  C   LEU A 273     2673   2630   3214     51    276   -506       C  
ATOM   2204  O   LEU A 273     -39.027  -5.188  35.294  1.00 22.70           O  
ANISOU 2204  O   LEU A 273     2560   3077   2985    111    243   -361       O  
ATOM   2205  N   GLU A 274     -38.507  -4.805  33.150  1.00 21.16           N  
ANISOU 2205  N   GLU A 274     2171   2717   3153   -230    130   -604       N  
ATOM   2206  CA  GLU A 274     -38.590  -6.208  32.752  1.00 22.50           C  
ANISOU 2206  CA  GLU A 274     2900   2686   2960   -132    149   -518       C  
ATOM   2207  CB  GLU A 274     -38.539  -6.333  31.232  1.00 22.99           C  
ANISOU 2207  CB  GLU A 274     2571   3166   2996   -280     -5   -687       C  
ATOM   2208  CG  GLU A 274     -39.688  -5.628  30.532  1.00 23.46           C  
ANISOU 2208  CG  GLU A 274     3085   2997   2830   -168    -82   -533       C  
ATOM   2209  CD  GLU A 274     -39.422  -4.221  30.019  1.00 23.72           C  
ANISOU 2209  CD  GLU A 274     3284   3071   2657    -65     61   -450       C  
ATOM   2210  OE1 GLU A 274     -38.627  -3.523  30.626  1.00 23.50           O  
ANISOU 2210  OE1 GLU A 274     2621   3422   2887    223   -401   -316       O  
ATOM   2211  OE2 GLU A 274     -40.026  -3.826  29.009  1.00 25.37           O  
ANISOU 2211  OE2 GLU A 274     4065   3052   2522    250    -46   -562       O  
ATOM   2212  C   GLU A 274     -37.489  -7.079  33.373  1.00 22.67           C  
ANISOU 2212  C   GLU A 274     2631   2743   3237   -365   -302   -658       C  
ATOM   2213  O   GLU A 274     -37.590  -8.308  33.295  1.00 26.44           O  
ANISOU 2213  O   GLU A 274     3524   2767   3753   -601   -225   -858       O  
ATOM   2214  N   ILE A 275     -36.446  -6.495  33.981  1.00 20.81           N  
ANISOU 2214  N   ILE A 275     2476   2777   2652    -74   -298   -686       N  
ATOM   2215  CA  ILE A 275     -35.416  -7.333  34.630  1.00 22.80           C  
ANISOU 2215  CA  ILE A 275     2786   2831   3044    143   -171   -484       C  
ATOM   2216  CB  ILE A 275     -33.999  -6.743  34.490  1.00 23.31           C  
ANISOU 2216  CB  ILE A 275     2741   3452   2663    211    -79   -217       C  
ATOM   2217  CG1 ILE A 275     -33.794  -5.429  35.241  1.00 22.08           C  
ANISOU 2217  CG1 ILE A 275     2556   3228   2605    -76    -19    205       C  
ATOM   2218  CG2 ILE A 275     -33.628  -6.614  33.025  1.00 25.87           C  
ANISOU 2218  CG2 ILE A 275     3006   3967   2856    133    123     32       C  
ATOM   2219  CD1 ILE A 275     -32.345  -5.027  35.374  1.00 24.28           C  
ANISOU 2219  CD1 ILE A 275     2468   3604   3153    156   -186    316       C  
ATOM   2220  C   ILE A 275     -35.774  -7.601  36.093  1.00 24.01           C  
ANISOU 2220  C   ILE A 275     2729   3152   3239     42   -177   -295       C  
ATOM   2221  O   ILE A 275     -35.043  -8.311  36.793  1.00 26.07           O  
ANISOU 2221  O   ILE A 275     2738   3348   3817     71    240    605       O  
ATOM   2222  N   GLY A 276     -36.883  -7.024  36.569  1.00 24.89           N  
ANISOU 2222  N   GLY A 276     2737   3422   3296    -89   -113   -378       N  
ATOM   2223  CA  GLY A 276     -37.353  -7.273  37.933  1.00 25.50           C  
ANISOU 2223  CA  GLY A 276     2832   3507   3350   -688    -44   -324       C  
ATOM   2224  C   GLY A 276     -36.308  -6.844  38.947  1.00 24.42           C  
ANISOU 2224  C   GLY A 276     2632   3706   2940   -489    -71    327       C  
ATOM   2225  O   GLY A 276     -35.552  -5.893  38.723  1.00 26.27           O  
ANISOU 2225  O   GLY A 276     2746   3778   3457   -543    245    262       O  
ATOM   2226  N   ASP A 277     -36.243  -7.581  40.049  1.00 24.81           N  
ANISOU 2226  N   ASP A 277     2840   3207   3377   -499    -88    591       N  
ATOM   2227  CA  ASP A 277     -35.425  -7.216  41.170  1.00 23.12           C  
ANISOU 2227  CA  ASP A 277     1623   3680   3481   -243     26    546       C  
ATOM   2228  CB  ASP A 277     -35.854  -7.965  42.431  1.00 28.39           C  
ANISOU 2228  CB  ASP A 277     2235   4944   3606   -714    283    946       C  
ATOM   2229  CG  ASP A 277     -37.234  -7.586  42.953  1.00 33.85           C  
ANISOU 2229  CG  ASP A 277     2601   5800   4456   -348    747   1477       C  
ATOM   2230  OD1 ASP A 277     -37.743  -6.521  42.578  1.00 37.53           O  
ANISOU 2230  OD1 ASP A 277     2901   7061   4297    601    754   1323       O  
ATOM   2231  OD2 ASP A 277     -37.771  -8.345  43.761  1.00 46.78           O  
ANISOU 2231  OD2 ASP A 277     4090   7873   5808  -1862    935   2309       O  
ATOM   2232  C   ASP A 277     -33.955  -7.505  40.854  1.00 20.79           C  
ANISOU 2232  C   ASP A 277     1896   2716   3284    151    175    285       C  
ATOM   2233  O   ASP A 277     -33.608  -8.538  40.308  1.00 27.72           O  
ANISOU 2233  O   ASP A 277     3232   2211   5089     11    -83    -47       O  
ATOM   2234  N   ILE A 278     -33.107  -6.546  41.189  1.00 18.19           N  
ANISOU 2234  N   ILE A 278     2104   2402   2403    201    106    350       N  
ATOM   2235  CA  ILE A 278     -31.681  -6.713  41.072  1.00 18.12           C  
ANISOU 2235  CA  ILE A 278     2136   2290   2458     76    254    255       C  
ATOM   2236  CB  ILE A 278     -31.010  -5.332  40.972  1.00 20.89           C  
ANISOU 2236  CB  ILE A 278     2560   2335   3042     -4    446    460       C  
ATOM   2237  CG1 ILE A 278     -31.477  -4.612  39.702  1.00 23.46           C  
ANISOU 2237  CG1 ILE A 278     2726   2753   3434    -30    573    748       C  
ATOM   2238  CG2 ILE A 278     -29.494  -5.438  41.071  1.00 21.91           C  
ANISOU 2238  CG2 ILE A 278     2707   2811   2805   -262    457    462       C  
ATOM   2239  CD1 ILE A 278     -30.911  -3.229  39.579  1.00 25.73           C  
ANISOU 2239  CD1 ILE A 278     3613   2255   3906    255    586    246       C  
ATOM   2240  C   ILE A 278     -31.209  -7.511  42.282  1.00 17.05           C  
ANISOU 2240  C   ILE A 278     2116   2169   2191    333    499     62       C  
ATOM   2241  O   ILE A 278     -31.663  -7.273  43.403  1.00 17.52           O  
ANISOU 2241  O   ILE A 278     2011   2461   2181    168    533    -81       O  
ATOM   2242  N   PRO A 279     -30.278  -8.470  42.102  1.00 16.28           N  
ANISOU 2242  N   PRO A 279     2217   2034   1931    368    262   -108       N  
ATOM   2243  CA  PRO A 279     -29.826  -9.287  43.218  1.00 16.37           C  
ANISOU 2243  CA  PRO A 279     2305   1913   2001    379    442    -37       C  
ATOM   2244  CB  PRO A 279     -28.772 -10.217  42.602  1.00 19.78           C  
ANISOU 2244  CB  PRO A 279     3109   2013   2392    662    428   -489       C  
ATOM   2245  CG  PRO A 279     -29.004 -10.164  41.129  1.00 22.06           C  
ANISOU 2245  CG  PRO A 279     3232   2691   2459    764    257   -310       C  
ATOM   2246  CD  PRO A 279     -29.668  -8.861  40.827  1.00 19.87           C  
ANISOU 2246  CD  PRO A 279     2767   2599   2182    641    461   -200       C  
ATOM   2247  C   PRO A 279     -29.204  -8.475  44.361  1.00 15.56           C  
ANISOU 2247  C   PRO A 279     2086   1703   2124    279    495    -11       C  
ATOM   2248  O   PRO A 279     -28.662  -7.391  44.160  1.00 16.83           O  
ANISOU 2248  O   PRO A 279     2187   1795   2412    245    569    182       O  
ATOM   2249  N   LYS A 280     -29.285  -9.041  45.561  1.00 14.97           N  
ANISOU 2249  N   LYS A 280     2108   1453   2124    185    615     28       N  
ATOM   2250  CA  LYS A 280     -28.762  -8.420  46.763  1.00 16.32           C  
ANISOU 2250  CA  LYS A 280     2340   1642   2217     55    772    -76       C  
ATOM   2251  CB  LYS A 280     -29.127  -9.270  47.985  1.00 19.39           C  
ANISOU 2251  CB  LYS A 280     2858   2260   2248   -264    848    100       C  
ATOM   2252  CG  LYS A 280     -30.622  -9.364  48.242  1.00 25.66           C  
ANISOU 2252  CG  LYS A 280     3073   3183   3492    109   1029     60       C  
ATOM   2253  CD  LYS A 280     -30.994 -10.065  49.533  1.00 30.21           C  
ANISOU 2253  CD  LYS A 280     3935   3918   3623   -356   1162    258       C  
ATOM   2254  CE  LYS A 280     -32.495 -10.137  49.738  1.00 37.73           C  
ANISOU 2254  CE  LYS A 280     3994   5022   5317    116   1064    -71       C  
ATOM   2255  NZ  LYS A 280     -33.101  -8.790  49.764  1.00 41.54           N  
ANISOU 2255  NZ  LYS A 280     3925   5627   6232     97   1137   -229       N  
ATOM   2256  C   LYS A 280     -27.247  -8.214  46.673  1.00 16.59           C  
ANISOU 2256  C   LYS A 280     2328   1555   2418    191    805     21       C  
ATOM   2257  O   LYS A 280     -26.757  -7.229  47.185  1.00 20.07           O  
ANISOU 2257  O   LYS A 280     2481   1744   3401    377    718   -314       O  
ATOM   2258  N   THR A 281     -26.507  -9.157  46.082  1.00 13.97           N  
ANISOU 2258  N   THR A 281     2023   1262   2020     96    465     37       N  
ATOM   2259  CA  THR A 281     -25.053  -9.049  45.988  1.00 14.13           C  
ANISOU 2259  CA  THR A 281     2144   1421   1804    125    527    -13       C  
ATOM   2260  CB  THR A 281     -24.328  -9.979  46.961  1.00 16.26           C  
ANISOU 2260  CB  THR A 281     2433   1803   1942    336    467     68       C  
ATOM   2261  OG1 THR A 281     -24.815  -9.740  48.283  1.00 18.18           O  
ANISOU 2261  OG1 THR A 281     2559   2304   2042    229    600     58       O  
ATOM   2262  CG2 THR A 281     -22.833  -9.779  46.894  1.00 18.62           C  
ANISOU 2262  CG2 THR A 281     2562   2153   2358    254    241    166       C  
ATOM   2263  C   THR A 281     -24.608  -9.351  44.560  1.00 13.30           C  
ANISOU 2263  C   THR A 281     2062   1327   1662     34    406     59       C  
ATOM   2264  O   THR A 281     -24.835 -10.476  44.068  1.00 17.04           O  
ANISOU 2264  O   THR A 281     2640   1659   2173   -220    754   -353       O  
ATOM   2265  N   ILE A 282     -24.007  -8.343  43.907  1.00 12.88           N  
ANISOU 2265  N   ILE A 282     2017   1253   1623    158    592    -71       N  
ATOM   2266  CA  ILE A 282     -23.503  -8.476  42.542  1.00 13.30           C  
ANISOU 2266  CA  ILE A 282     2151   1355   1546    214    453   -116       C  
ATOM   2267  CB  ILE A 282     -23.898  -7.250  41.687  1.00 13.84           C  
ANISOU 2267  CB  ILE A 282     2210   1610   1438    332    271    -45       C  
ATOM   2268  CG1 ILE A 282     -25.413  -6.997  41.726  1.00 14.81           C  
ANISOU 2268  CG1 ILE A 282     2255   1818   1554    492    138   -102       C  
ATOM   2269  CG2 ILE A 282     -23.384  -7.389  40.262  1.00 14.33           C  
ANISOU 2269  CG2 ILE A 282     2497   1454   1492    238    373   -179       C  
ATOM   2270  CD1 ILE A 282     -25.787  -5.625  41.255  1.00 16.14           C  
ANISOU 2270  CD1 ILE A 282     2519   2020   1590    845    126    -31       C  
ATOM   2271  C   ILE A 282     -21.982  -8.611  42.614  1.00 12.56           C  
ANISOU 2271  C   ILE A 282     2106   1414   1250    254    269   -179       C  
ATOM   2272  O   ILE A 282     -21.336  -7.913  43.371  1.00 13.05           O  
ANISOU 2272  O   ILE A 282     1935   1416   1607     48    430   -249       O  
ATOM   2273  N   ILE A 283     -21.446  -9.507  41.780  1.00 12.89           N  
ANISOU 2273  N   ILE A 283     1912   1515   1468    144    410   -280       N  
ATOM   2274  CA  ILE A 283     -20.029  -9.846  41.702  1.00 12.77           C  
ANISOU 2274  CA  ILE A 283     1887   1558   1407     70    344   -207       C  
ATOM   2275  CB  ILE A 283     -19.853 -11.361  41.798  1.00 14.08           C  
ANISOU 2275  CB  ILE A 283     2177   1536   1634    -13    426   -108       C  
ATOM   2276  CG1 ILE A 283     -20.481 -11.900  43.084  1.00 14.98           C  
ANISOU 2276  CG1 ILE A 283     2094   1832   1765   -256    388    -52       C  
ATOM   2277  CG2 ILE A 283     -18.385 -11.773  41.635  1.00 15.48           C  
ANISOU 2277  CG2 ILE A 283     2299   1572   2010     29    592     39       C  
ATOM   2278  CD1 ILE A 283     -20.459 -13.406  43.170  1.00 16.45           C  
ANISOU 2278  CD1 ILE A 283     2239   1843   2165    -88    374    126       C  
ATOM   2279  C   ILE A 283     -19.424  -9.298  40.413  1.00 12.28           C  
ANISOU 2279  C   ILE A 283     1956   1410   1297    144    203   -185       C  
ATOM   2280  O   ILE A 283     -20.011  -9.455  39.348  1.00 13.28           O  
ANISOU 2280  O   ILE A 283     1953   1722   1370   -253     91   -288       O  
ATOM   2281  N   TYR A 284     -18.253  -8.658  40.536  1.00 11.42           N  
ANISOU 2281  N   TYR A 284     1730   1464   1145    183    328   -170       N  
ATOM   2282  CA  TYR A 284     -17.516  -8.127  39.392  1.00 11.75           C  
ANISOU 2282  CA  TYR A 284     1827   1305   1331    142    413   -139       C  
ATOM   2283  CB  TYR A 284     -17.365  -6.607  39.473  1.00 12.33           C  
ANISOU 2283  CB  TYR A 284     1840   1290   1553    129    313    -23       C  
ATOM   2284  CG  TYR A 284     -18.671  -5.860  39.539  1.00 12.16           C  
ANISOU 2284  CG  TYR A 284     1861   1212   1544    190    224   -114       C  
ATOM   2285  CD1 TYR A 284     -19.364  -5.765  40.734  1.00 12.78           C  
ANISOU 2285  CD1 TYR A 284     2150   1253   1450    202    186   -247       C  
ATOM   2286  CE1 TYR A 284     -20.592  -5.142  40.812  1.00 11.83           C  
ANISOU 2286  CE1 TYR A 284     1982   1243   1268    200    227     31       C  
ATOM   2287  CZ  TYR A 284     -21.153  -4.568  39.682  1.00 11.98           C  
ANISOU 2287  CZ  TYR A 284     1982   1292   1274    186    303     48       C  
ATOM   2288  OH  TYR A 284     -22.369  -3.946  39.783  1.00 12.48           O  
ANISOU 2288  OH  TYR A 284     1963   1275   1504    153    373   -181       O  
ATOM   2289  CE2 TYR A 284     -20.463  -4.615  38.481  1.00 10.88           C  
ANISOU 2289  CE2 TYR A 284     1872    987   1271    146    299   -104       C  
ATOM   2290  CD2 TYR A 284     -19.233  -5.270  38.412  1.00 12.15           C  
ANISOU 2290  CD2 TYR A 284     1980   1177   1459    209    336    -88       C  
ATOM   2291  C   TYR A 284     -16.119  -8.736  39.364  1.00 12.39           C  
ANISOU 2291  C   TYR A 284     1906   1443   1359    130    343   -140       C  
ATOM   2292  O   TYR A 284     -15.424  -8.812  40.387  1.00 13.18           O  
ANISOU 2292  O   TYR A 284     1952   1712   1341    266    295   -148       O  
ATOM   2293  N  AASN A 285     -15.706  -9.146  38.164  0.50 12.38           N  
ANISOU 2293  N  AASN A 285     1816   1590   1296    124    244   -227       N  
ATOM   2294  N  BASN A 285     -15.709  -9.145  38.163  0.50 12.25           N  
ANISOU 2294  N  BASN A 285     1730   1621   1302    167    243   -200       N  
ATOM   2295  CA AASN A 285     -14.350  -9.593  37.911  0.50 12.51           C  
ANISOU 2295  CA AASN A 285     1849   1496   1408    123    282   -301       C  
ATOM   2296  CA BASN A 285     -14.356  -9.586  37.909  0.50 12.61           C  
ANISOU 2296  CA BASN A 285     1737   1574   1480    172    253   -225       C  
ATOM   2297  CB AASN A 285     -14.305 -10.430  36.634  0.50 14.32           C  
ANISOU 2297  CB AASN A 285     2085   1883   1472    139    290   -463       C  
ATOM   2298  CB BASN A 285     -14.301 -10.397  36.617  0.50 14.10           C  
ANISOU 2298  CB BASN A 285     1868   1949   1540    263    230   -359       C  
ATOM   2299  CG AASN A 285     -13.043 -11.251  36.526  0.50 16.65           C  
ANISOU 2299  CG AASN A 285     2328   2196   1799    353    291   -643       C  
ATOM   2300  CG BASN A 285     -12.935 -11.001  36.417  0.50 16.60           C  
ANISOU 2300  CG BASN A 285     1901   2406   1999    401    110   -486       C  
ATOM   2301  OD1AASN A 285     -12.017 -10.878  37.092  0.50 20.47           O  
ANISOU 2301  OD1AASN A 285     2269   2800   2707    301    305   -791       O  
ATOM   2302  OD1BASN A 285     -12.411 -11.613  37.355  0.50 17.66           O  
ANISOU 2302  OD1BASN A 285     1866   2222   2620    652     52   -292       O  
ATOM   2303  ND2AASN A 285     -13.105 -12.345  35.781  0.50 18.38           N  
ANISOU 2303  ND2AASN A 285     2702   2196   2085     69    115   -719       N  
ATOM   2304  ND2BASN A 285     -12.379 -10.832  35.220  0.50 19.93           N  
ANISOU 2304  ND2BASN A 285     2388   2901   2282    345    398   -443       N  
ATOM   2305  C  AASN A 285     -13.445  -8.350  37.826  0.50 12.04           C  
ANISOU 2305  C  AASN A 285     1704   1463   1406    162    176   -194       C  
ATOM   2306  C  BASN A 285     -13.447  -8.347  37.827  0.50 12.10           C  
ANISOU 2306  C  BASN A 285     1651   1506   1440    203    170   -154       C  
ATOM   2307  O  AASN A 285     -13.625  -7.503  36.941  0.50 13.41           O  
ANISOU 2307  O  AASN A 285     1927   1749   1416    158    -18   -124       O  
ATOM   2308  O  BASN A 285     -13.624  -7.501  36.941  0.50 13.49           O  
ANISOU 2308  O  BASN A 285     1886   1796   1442    190    -22    -80       O  
ATOM   2309  N   THR A 286     -12.483  -8.247  38.748  1.00 12.64           N  
ANISOU 2309  N   THR A 286     1860   1345   1598    160     19   -135       N  
ATOM   2310  CA  THR A 286     -11.621  -7.057  38.883  1.00 11.95           C  
ANISOU 2310  CA  THR A 286     1607   1533   1398     94    158    -64       C  
ATOM   2311  CB  THR A 286     -12.157  -6.116  39.968  1.00 12.47           C  
ANISOU 2311  CB  THR A 286     1752   1601   1382    113    229    -44       C  
ATOM   2312  OG1 THR A 286     -12.253  -6.809  41.212  1.00 12.84           O  
ANISOU 2312  OG1 THR A 286     2153   1359   1365    114    233    -43       O  
ATOM   2313  CG2 THR A 286     -13.506  -5.544  39.596  1.00 12.69           C  
ANISOU 2313  CG2 THR A 286     1832   1352   1637    256    306    -36       C  
ATOM   2314  C   THR A 286     -10.184  -7.485  39.164  1.00 13.06           C  
ANISOU 2314  C   THR A 286     1591   1663   1708     81    216   -149       C  
ATOM   2315  O   THR A 286      -9.689  -7.348  40.270  1.00 13.52           O  
ANISOU 2315  O   THR A 286     1921   1544   1672     95    148    -58       O  
ATOM   2316  N   PRO A 287      -9.487  -8.033  38.154  1.00 14.42           N  
ANISOU 2316  N   PRO A 287     1609   2139   1730    193    126   -426       N  
ATOM   2317  CA  PRO A 287      -8.155  -8.598  38.351  1.00 16.00           C  
ANISOU 2317  CA  PRO A 287     1679   2345   2053    196    257   -394       C  
ATOM   2318  CB  PRO A 287      -7.658  -8.924  36.940  1.00 18.57           C  
ANISOU 2318  CB  PRO A 287     1877   2983   2195    118    268   -800       C  
ATOM   2319  CG  PRO A 287      -8.878  -8.890  36.046  1.00 18.94           C  
ANISOU 2319  CG  PRO A 287     2074   2962   2159    400    214   -511       C  
ATOM   2320  CD  PRO A 287      -9.955  -8.107  36.758  1.00 16.34           C  
ANISOU 2320  CD  PRO A 287     2019   2400   1789    119    108   -581       C  
ATOM   2321  C   PRO A 287      -7.173  -7.617  39.001  1.00 15.13           C  
ANISOU 2321  C   PRO A 287     1771   2200   1776    208    250   -271       C  
ATOM   2322  O   PRO A 287      -7.214  -6.429  38.755  1.00 15.13           O  
ANISOU 2322  O   PRO A 287     1857   2198   1691    215    489      6       O  
ATOM   2323  N   LEU A 288      -6.272  -8.156  39.811  1.00 14.14           N  
ANISOU 2323  N   LEU A 288     1978   1656   1737    136    249     35       N  
ATOM   2324  CA  LEU A 288      -5.283  -7.366  40.526  1.00 13.94           C  
ANISOU 2324  CA  LEU A 288     2141   1443   1710    158    322   -172       C  
ATOM   2325  CB  LEU A 288      -5.300  -7.752  41.998  1.00 16.38           C  
ANISOU 2325  CB  LEU A 288     2600   1842   1779    239    164    -31       C  
ATOM   2326  CG  LEU A 288      -4.336  -6.990  42.883  1.00 20.31           C  
ANISOU 2326  CG  LEU A 288     3332   2279   2103   -100     52     61       C  
ATOM   2327  CD1 LEU A 288      -4.722  -5.528  42.923  1.00 23.38           C  
ANISOU 2327  CD1 LEU A 288     3983   2422   2478    188    153     58       C  
ATOM   2328  CD2 LEU A 288      -4.321  -7.589  44.280  1.00 22.56           C  
ANISOU 2328  CD2 LEU A 288     4110   2280   2180    -89   -199    163       C  
ATOM   2329  C   LEU A 288      -3.915  -7.625  39.915  1.00 13.13           C  
ANISOU 2329  C   LEU A 288     2053   1422   1512    175    189   -245       C  
ATOM   2330  O   LEU A 288      -3.419  -8.744  39.950  1.00 15.16           O  
ANISOU 2330  O   LEU A 288     2182   1564   2013    349    191   -154       O  
ATOM   2331  N   ILE A 289      -3.332  -6.574  39.335  1.00 13.08           N  
ANISOU 2331  N   ILE A 289     2230   1425   1314    249    228   -130       N  
ATOM   2332  CA  ILE A 289      -2.020  -6.647  38.706  1.00 14.20           C  
ANISOU 2332  CA  ILE A 289     2138   1711   1545    223    182   -244       C  
ATOM   2333  CB  ILE A 289      -2.023  -6.001  37.313  1.00 17.10           C  
ANISOU 2333  CB  ILE A 289     2435   2257   1805     19    471    110       C  
ATOM   2334  CG1 ILE A 289      -2.823  -6.814  36.290  1.00 19.06           C  
ANISOU 2334  CG1 ILE A 289     2944   2631   1666    -53    389    -41       C  
ATOM   2335  CG2 ILE A 289      -0.588  -5.790  36.840  1.00 20.02           C  
ANISOU 2335  CG2 ILE A 289     2626   2948   2029    -57    653    431       C  
ATOM   2336  CD1 ILE A 289      -4.325  -6.786  36.470  1.00 20.45           C  
ANISOU 2336  CD1 ILE A 289     3040   2859   1871   -266    431    -78       C  
ATOM   2337  C   ILE A 289      -1.023  -5.964  39.639  1.00 14.84           C  
ANISOU 2337  C   ILE A 289     2022   1714   1902     70    143   -255       C  
ATOM   2338  O   ILE A 289      -1.263  -4.822  40.039  1.00 17.29           O  
ANISOU 2338  O   ILE A 289     2242   1639   2686    110    -47   -403       O  
ATOM   2339  N   SER A 290       0.070  -6.663  39.973  1.00 14.44           N  
ANISOU 2339  N   SER A 290     1850   1771   1866     23    121   -367       N  
ATOM   2340  CA ASER A 290       1.077  -6.134  40.893  0.50 15.28           C  
ANISOU 2340  CA ASER A 290     2074   1910   1820      8     38   -509       C  
ATOM   2341  CA BSER A 290       1.075  -6.150  40.916  0.50 15.19           C  
ANISOU 2341  CA BSER A 290     2047   1897   1827      8     60   -505       C  
ATOM   2342  CB ASER A 290       0.958  -6.716  42.277  0.50 18.17           C  
ANISOU 2342  CB ASER A 290     2517   2595   1790    -60     61   -472       C  
ATOM   2343  CB BSER A 290       0.946  -6.806  42.283  0.50 17.37           C  
ANISOU 2343  CB BSER A 290     2335   2479   1784    -39    153   -489       C  
ATOM   2344  OG ASER A 290       1.694  -5.868  43.150  0.50 20.91           O  
ANISOU 2344  OG ASER A 290     3107   2678   2158   -334   -120   -498       O  
ATOM   2345  OG BSER A 290      -0.392  -6.883  42.746  0.50 18.65           O  
ANISOU 2345  OG BSER A 290     2428   2534   2123   -159    302   -435       O  
ATOM   2346  C   SER A 290       2.483  -6.414  40.373  1.00 15.66           C  
ANISOU 2346  C   SER A 290     2053   2140   1756     -2     11   -410       C  
ATOM   2347  O   SER A 290       2.731  -7.455  39.806  1.00 17.51           O  
ANISOU 2347  O   SER A 290     2190   2218   2244     -7     36   -624       O  
ATOM   2348  N   LEU A 291       3.401  -5.491  40.667  1.00 17.05           N  
ANISOU 2348  N   LEU A 291     1843   2385   2248    -64    171   -377       N  
ATOM   2349  CA  LEU A 291       4.824  -5.735  40.486  1.00 17.28           C  
ANISOU 2349  CA  LEU A 291     1856   2473   2235    -13     -7   -396       C  
ATOM   2350  CB  LEU A 291       5.572  -4.405  40.402  1.00 19.16           C  
ANISOU 2350  CB  LEU A 291     2275   2453   2552   -139   -343   -328       C  
ATOM   2351  CG  LEU A 291       7.080  -4.538  40.227  1.00 21.55           C  
ANISOU 2351  CG  LEU A 291     2379   2691   3116   -126   -217   -454       C  
ATOM   2352  CD1 LEU A 291       7.435  -5.174  38.892  1.00 18.51           C  
ANISOU 2352  CD1 LEU A 291     1449   2652   2931     38    -44   -246       C  
ATOM   2353  CD2 LEU A 291       7.721  -3.176  40.370  1.00 23.63           C  
ANISOU 2353  CD2 LEU A 291     2330   3080   3566   -503   -347   -522       C  
ATOM   2354  C   LEU A 291       5.321  -6.568  41.672  1.00 18.56           C  
ANISOU 2354  C   LEU A 291     2339   2592   2117    225   -219   -512       C  
ATOM   2355  O   LEU A 291       5.280  -6.118  42.800  1.00 21.16           O  
ANISOU 2355  O   LEU A 291     3035   2766   2238    231   -331   -693       O  
ATOM   2356  N   GLU A 292       5.764  -7.793  41.401  1.00 16.43           N  
ANISOU 2356  N   GLU A 292     1906   2481   1853    242    -75   -309       N  
ATOM   2357  CA  GLU A 292       6.219  -8.706  42.461  1.00 18.78           C  
ANISOU 2357  CA  GLU A 292     2471   2935   1729    145     39    -98       C  
ATOM   2358  CB  GLU A 292       5.970 -10.157  42.079  1.00 20.78           C  
ANISOU 2358  CB  GLU A 292     2455   3144   2294   -108   -127    -59       C  
ATOM   2359  CG  GLU A 292       4.503 -10.532  42.070  1.00 21.80           C  
ANISOU 2359  CG  GLU A 292     2403   3415   2465   -106   -386    229       C  
ATOM   2360  CD  GLU A 292       3.785 -10.473  43.414  1.00 23.54           C  
ANISOU 2360  CD  GLU A 292     2886   3411   2645   -187    -28    169       C  
ATOM   2361  OE1 GLU A 292       4.449 -10.555  44.470  1.00 25.12           O  
ANISOU 2361  OE1 GLU A 292     3266   3326   2950   -249   -251    283       O  
ATOM   2362  OE2 GLU A 292       2.539 -10.338  43.387  1.00 25.59           O  
ANISOU 2362  OE2 GLU A 292     3019   4481   2223   -199    172    102       O  
ATOM   2363  C   GLU A 292       7.704  -8.521  42.767  1.00 18.79           C  
ANISOU 2363  C   GLU A 292     2740   2636   1763     44   -155   -322       C  
ATOM   2364  O   GLU A 292       8.148  -8.752  43.893  1.00 21.68           O  
ANISOU 2364  O   GLU A 292     3001   3345   1888     -1   -207     86       O  
ATOM   2365  N   GLY A 293       8.488  -8.153  41.755  1.00 16.44           N  
ANISOU 2365  N   GLY A 293     2205   2569   1470    106   -530    -53       N  
ATOM   2366  CA  GLY A 293       9.895  -7.959  41.961  1.00 17.85           C  
ANISOU 2366  CA  GLY A 293     2226   2952   1601    -27   -488   -220       C  
ATOM   2367  C   GLY A 293      10.535  -7.294  40.779  1.00 17.01           C  
ANISOU 2367  C   GLY A 293     2088   2700   1675    162   -392   -393       C  
ATOM   2368  O   GLY A 293      10.017  -7.366  39.653  1.00 16.92           O  
ANISOU 2368  O   GLY A 293     2039   2700   1690    129   -469   -230       O  
ATOM   2369  N   ASN A 294      11.659  -6.638  41.051  1.00 17.73           N  
ANISOU 2369  N   ASN A 294     2041   3004   1692    -56   -325   -289       N  
ATOM   2370  CA  ASN A 294      12.403  -5.986  40.010  1.00 18.61           C  
ANISOU 2370  CA  ASN A 294     2187   3271   1609   -133   -454   -116       C  
ATOM   2371  CB  ASN A 294      11.842  -4.594  39.716  1.00 20.75           C  
ANISOU 2371  CB  ASN A 294     2463   3131   2288   -153   -533   -146       C  
ATOM   2372  CG  ASN A 294      12.002  -3.640  40.876  1.00 25.11           C  
ANISOU 2372  CG  ASN A 294     3418   3437   2683     36     45   -528       C  
ATOM   2373  OD1 ASN A 294      11.193  -3.620  41.806  1.00 31.46           O  
ANISOU 2373  OD1 ASN A 294     4944   3936   3070    217    710   -420       O  
ATOM   2374  ND2 ASN A 294      13.073  -2.880  40.849  1.00 28.24           N  
ANISOU 2374  ND2 ASN A 294     4086   3241   3399   -318   -185   -450       N  
ATOM   2375  C   ASN A 294      13.878  -5.904  40.403  1.00 17.79           C  
ANISOU 2375  C   ASN A 294     2131   3096   1530    -63   -380   -379       C  
ATOM   2376  O   ASN A 294      14.239  -5.943  41.595  1.00 21.68           O  
ANISOU 2376  O   ASN A 294     2493   4201   1542   -110   -456   -414       O  
ATOM   2377  N   ILE A 295      14.734  -5.831  39.385  1.00 18.46           N  
ANISOU 2377  N   ILE A 295     2097   3210   1703   -190   -349   -355       N  
ATOM   2378  CA  ILE A 295      16.165  -5.676  39.600  1.00 18.94           C  
ANISOU 2378  CA  ILE A 295     2195   3276   1724   -383   -644   -571       C  
ATOM   2379  CB  ILE A 295      16.849  -7.000  39.989  1.00 21.40           C  
ANISOU 2379  CB  ILE A 295     2461   3472   2198   -338   -794   -338       C  
ATOM   2380  CG1 ILE A 295      18.269  -6.758  40.507  1.00 24.31           C  
ANISOU 2380  CG1 ILE A 295     2606   4010   2620   -384   -879   -430       C  
ATOM   2381  CG2 ILE A 295      16.829  -8.003  38.844  1.00 21.36           C  
ANISOU 2381  CG2 ILE A 295     2455   3262   2398     10   -615   -276       C  
ATOM   2382  CD1 ILE A 295      18.838  -7.895  41.292  1.00 28.04           C  
ANISOU 2382  CD1 ILE A 295     3217   4142   3295   -205  -1185   -485       C  
ATOM   2383  C   ILE A 295      16.749  -5.085  38.317  1.00 18.54           C  
ANISOU 2383  C   ILE A 295     2114   3130   1797   -138   -486   -424       C  
ATOM   2384  O   ILE A 295      16.223  -5.368  37.222  1.00 18.66           O  
ANISOU 2384  O   ILE A 295     2076   3047   1966    -99   -711   -418       O  
ATOM   2385  N   SER A 296      17.823  -4.307  38.447  1.00 19.97           N  
ANISOU 2385  N   SER A 296     2107   3419   2059   -299   -546   -321       N  
ATOM   2386  CA ASER A 296      18.380  -3.605  37.295  0.50 21.12           C  
ANISOU 2386  CA ASER A 296     2277   3641   2104   -370   -589   -251       C  
ATOM   2387  CA BSER A 296      18.383  -3.596  37.297  0.50 20.52           C  
ANISOU 2387  CA BSER A 296     2244   3487   2063   -302   -533   -301       C  
ATOM   2388  CB ASER A 296      17.998  -2.139  37.333  0.50 22.41           C  
ANISOU 2388  CB ASER A 296     2634   3565   2317   -512   -557   -383       C  
ATOM   2389  CB BSER A 296      18.056  -2.118  37.346  0.50 20.18           C  
ANISOU 2389  CB BSER A 296     2198   3395   2074   -393   -398   -478       C  
ATOM   2390  OG ASER A 296      18.581  -1.493  38.445  0.50 24.77           O  
ANISOU 2390  OG ASER A 296     2964   3974   2474   -844   -657   -416       O  
ATOM   2391  OG BSER A 296      16.676  -1.868  37.380  0.50 19.96           O  
ANISOU 2391  OG BSER A 296     2125   3325   2131   -469   -137   -399       O  
ATOM   2392  C   SER A 296      19.900  -3.782  37.229  1.00 20.26           C  
ANISOU 2392  C   SER A 296     2230   3724   1741   -417   -459   -273       C  
ATOM   2393  O   SER A 296      20.558  -4.142  38.222  1.00 23.38           O  
ANISOU 2393  O   SER A 296     2177   4537   2169   -458   -711     -3       O  
ATOM   2394  N   SER A 297      20.454  -3.513  36.049  1.00 19.02           N  
ANISOU 2394  N   SER A 297     2209   3219   1796   -531   -439   -366       N  
ATOM   2395  CA  SER A 297      21.886  -3.451  35.878  1.00 19.67           C  
ANISOU 2395  CA  SER A 297     2156   3269   2047   -643   -540   -393       C  
ATOM   2396  CB  SER A 297      22.474  -4.807  35.602  1.00 22.21           C  
ANISOU 2396  CB  SER A 297     2460   3590   2388   -400   -429   -233       C  
ATOM   2397  OG  SER A 297      22.082  -5.256  34.313  1.00 24.13           O  
ANISOU 2397  OG  SER A 297     3087   3710   2371   -542   -163   -531       O  
ATOM   2398  C   SER A 297      22.226  -2.499  34.733  1.00 20.77           C  
ANISOU 2398  C   SER A 297     2261   3360   2268   -754   -338   -507       C  
ATOM   2399  O   SER A 297      21.389  -2.212  33.874  1.00 21.39           O  
ANISOU 2399  O   SER A 297     2135   3433   2557   -602   -413   -318       O  
ATOM   2400  N   MET A 298      23.487  -2.061  34.735  1.00 22.52           N  
ANISOU 2400  N   MET A 298     2480   3501   2573  -1117   -395   -687       N  
ATOM   2401  CA  MET A 298      24.069  -1.378  33.595  1.00 22.27           C  
ANISOU 2401  CA  MET A 298     2243   3626   2590   -904   -641   -331       C  
ATOM   2402  CB  MET A 298      25.252  -0.501  34.026  1.00 25.29           C  
ANISOU 2402  CB  MET A 298     2543   4162   2902  -1430   -557   -336       C  
ATOM   2403  CG  MET A 298      25.939   0.239  32.877  1.00 28.01           C  
ANISOU 2403  CG  MET A 298     2887   4251   3504  -1471   -429     51       C  
ATOM   2404  SD  MET A 298      24.786   1.385  32.075  1.00 31.86           S  
ANISOU 2404  SD  MET A 298     3527   4606   3969  -1493   -846    199       S  
ATOM   2405  CE  MET A 298      25.904   2.454  31.173  1.00 36.33           C  
ANISOU 2405  CE  MET A 298     3309   5325   5166   -973    -49    579       C  
ATOM   2406  C   MET A 298      24.541  -2.452  32.626  1.00 22.77           C  
ANISOU 2406  C   MET A 298     2319   3840   2490   -637   -704   -407       C  
ATOM   2407  O   MET A 298      25.444  -3.218  32.943  1.00 26.31           O  
ANISOU 2407  O   MET A 298     2621   4644   2729    -52   -492   -495       O  
ATOM   2408  N   CYS A 299      23.905  -2.496  31.457  1.00 19.68           N  
ANISOU 2408  N   CYS A 299     2165   3106   2206   -404   -446   -289       N  
ATOM   2409  CA  CYS A 299      24.188  -3.494  30.429  1.00 21.58           C  
ANISOU 2409  CA  CYS A 299     2633   3280   2283   -569   -293   -451       C  
ATOM   2410  CB  CYS A 299      22.898  -4.021  29.813  1.00 21.10           C  
ANISOU 2410  CB  CYS A 299     2738   3219   2059   -644   -194   -262       C  
ATOM   2411  SG  CYS A 299      21.894  -4.992  30.958  1.00 20.86           S  
ANISOU 2411  SG  CYS A 299     2474   3058   2394   -480   -293    -14       S  
ATOM   2412  C   CYS A 299      25.074  -2.873  29.349  1.00 20.97           C  
ANISOU 2412  C   CYS A 299     2353   3254   2359   -658   -335   -654       C  
ATOM   2413  O   CYS A 299      24.650  -1.946  28.675  1.00 22.70           O  
ANISOU 2413  O   CYS A 299     2207   3663   2755   -457   -198   -367       O  
ATOM   2414  N   LEU A 300      26.304  -3.389  29.235  1.00 21.79           N  
ANISOU 2414  N   LEU A 300     2107   3520   2650   -583   -261   -289       N  
ATOM   2415  CA  LEU A 300      27.329  -2.892  28.320  1.00 22.12           C  
ANISOU 2415  CA  LEU A 300     2034   3501   2869   -607   -277   -316       C  
ATOM   2416  CB  LEU A 300      28.689  -2.792  29.028  1.00 24.86           C  
ANISOU 2416  CB  LEU A 300     2221   3936   3286   -726   -561   -411       C  
ATOM   2417  CG  LEU A 300      28.764  -1.886  30.255  1.00 29.97           C  
ANISOU 2417  CG  LEU A 300     2866   4300   4218  -1184   -482   -797       C  
ATOM   2418  CD1 LEU A 300      30.176  -1.859  30.834  1.00 36.06           C  
ANISOU 2418  CD1 LEU A 300     3172   5298   5229  -1196   -979   -458       C  
ATOM   2419  CD2 LEU A 300      28.299  -0.479  29.912  1.00 32.81           C  
ANISOU 2419  CD2 LEU A 300     3598   4221   4645  -1054   -237   -816       C  
ATOM   2420  C   LEU A 300      27.430  -3.875  27.158  1.00 21.41           C  
ANISOU 2420  C   LEU A 300     2042   3553   2539   -471   -353   -148       C  
ATOM   2421  O   LEU A 300      27.622  -5.080  27.379  1.00 22.07           O  
ANISOU 2421  O   LEU A 300     2373   3502   2511   -312   -181    -63       O  
ATOM   2422  N   ASN A 301      27.328  -3.358  25.933  1.00 20.62           N  
ANISOU 2422  N   ASN A 301     1778   3509   2545   -501   -217   -244       N  
ATOM   2423  CA  ASN A 301      27.567  -4.158  24.757  1.00 20.03           C  
ANISOU 2423  CA  ASN A 301     1744   3422   2443   -644   -201   -239       C  
ATOM   2424  CB  ASN A 301      26.532  -3.867  23.676  1.00 19.98           C  
ANISOU 2424  CB  ASN A 301     1947   3513   2131   -688    -70   -120       C  
ATOM   2425  CG  ASN A 301      25.184  -4.486  23.979  1.00 18.65           C  
ANISOU 2425  CG  ASN A 301     1612   3382   2089   -470   -276    -92       C  
ATOM   2426  OD1 ASN A 301      25.057  -5.354  24.847  1.00 20.44           O  
ANISOU 2426  OD1 ASN A 301     1839   3497   2431   -459   -231    112       O  
ATOM   2427  ND2 ASN A 301      24.167  -4.078  23.240  1.00 17.74           N  
ANISOU 2427  ND2 ASN A 301     1453   2482   2805   -225   -320   -352       N  
ATOM   2428  C   ASN A 301      29.000  -3.929  24.267  1.00 20.95           C  
ANISOU 2428  C   ASN A 301     1704   3627   2627   -802   -387   -260       C  
ATOM   2429  O   ASN A 301      29.517  -2.800  24.268  1.00 23.91           O  
ANISOU 2429  O   ASN A 301     1978   3539   3565   -886   -435   -437       O  
ATOM   2430  N   THR A 302      29.630  -5.028  23.846  1.00 23.80           N  
ANISOU 2430  N   THR A 302     2136   3757   3147   -542   -249   -281       N  
ATOM   2431  CA  THR A 302      30.974  -5.036  23.308  1.00 25.92           C  
ANISOU 2431  CA  THR A 302     2248   4492   3106   -514   -141   -329       C  
ATOM   2432  CB  THR A 302      31.904  -5.932  24.136  1.00 26.39           C  
ANISOU 2432  CB  THR A 302     2067   4868   3090   -549   -394   -251       C  
ATOM   2433  OG1 THR A 302      31.447  -7.277  24.044  1.00 26.28           O  
ANISOU 2433  OG1 THR A 302     2287   4625   3071    -49   -368   -122       O  
ATOM   2434  CG2 THR A 302      31.965  -5.521  25.591  1.00 29.11           C  
ANISOU 2434  CG2 THR A 302     2653   5190   3216   -488   -286   -291       C  
ATOM   2435  C   THR A 302      30.988  -5.498  21.843  1.00 25.18           C  
ANISOU 2435  C   THR A 302     1914   4817   2833   -388    -44     43       C  
ATOM   2436  O   THR A 302      31.998  -5.304  21.167  1.00 30.66           O  
ANISOU 2436  O   THR A 302     2098   5847   3701   -435    378    202       O  
ATOM   2437  N   LYS A 303      29.917  -6.162  21.396  1.00 23.18           N  
ANISOU 2437  N   LYS A 303     1677   4539   2590   -332     81     73       N  
ATOM   2438  CA  LYS A 303      29.743  -6.596  20.020  1.00 24.26           C  
ANISOU 2438  CA  LYS A 303     2081   4411   2725    -20   -193     13       C  
ATOM   2439  CB  LYS A 303      29.556  -8.114  19.975  1.00 25.48           C  
ANISOU 2439  CB  LYS A 303     2376   4473   2832    100   -278    336       C  
ATOM   2440  CG  LYS A 303      30.797  -8.863  20.436  1.00 31.55           C  
ANISOU 2440  CG  LYS A 303     3276   5104   3607    512   -941    808       C  
ATOM   2441  CD  LYS A 303      30.596 -10.324  20.663  1.00 35.73           C  
ANISOU 2441  CD  LYS A 303     3847   5702   4025     68   -691    890       C  
ATOM   2442  CE  LYS A 303      30.266 -10.671  22.101  1.00 37.32           C  
ANISOU 2442  CE  LYS A 303     4066   6039   4072    138   -475    939       C  
ATOM   2443  NZ  LYS A 303      29.807 -12.078  22.232  1.00 35.00           N  
ANISOU 2443  NZ  LYS A 303     3334   5626   4337    490  -1378   1050       N  
ATOM   2444  C   LYS A 303      28.568  -5.833  19.401  1.00 21.00           C  
ANISOU 2444  C   LYS A 303     1554   3752   2674   -175    147   -137       C  
ATOM   2445  O   LYS A 303      27.676  -5.331  20.101  1.00 20.95           O  
ANISOU 2445  O   LYS A 303     1432   3839   2689    -57    -39   -349       O  
ATOM   2446  N   ASP A 304      28.579  -5.730  18.069  1.00 20.84           N  
ANISOU 2446  N   ASP A 304     1636   3652   2628   -201   -206   -151       N  
ATOM   2447  CA  ASP A 304      27.563  -4.966  17.379  1.00 19.94           C  
ANISOU 2447  CA  ASP A 304     1512   3378   2684   -218     -3   -133       C  
ATOM   2448  CB  ASP A 304      27.830  -4.875  15.878  1.00 20.62           C  
ANISOU 2448  CB  ASP A 304     1762   3584   2489   -209   -124   -127       C  
ATOM   2449  CG  ASP A 304      29.077  -4.106  15.496  1.00 22.52           C  
ANISOU 2449  CG  ASP A 304     1672   3944   2938   -220     38   -104       C  
ATOM   2450  OD1 ASP A 304      29.406  -3.145  16.206  1.00 24.70           O  
ANISOU 2450  OD1 ASP A 304     2160   4559   2666   -538    204   -417       O  
ATOM   2451  OD2 ASP A 304      29.714  -4.485  14.482  1.00 26.10           O  
ANISOU 2451  OD2 ASP A 304     1951   4600   3363   -271    574   -101       O  
ATOM   2452  C   ASP A 304      26.207  -5.619  17.590  1.00 18.72           C  
ANISOU 2452  C   ASP A 304     1546   3207   2357   -188     60   -235       C  
ATOM   2453  O   ASP A 304      26.049  -6.820  17.361  1.00 19.59           O  
ANISOU 2453  O   ASP A 304     1919   3116   2408    199    -85   -404       O  
ATOM   2454  N   PRO A 305      25.167  -4.874  18.005  1.00 17.84           N  
ANISOU 2454  N   PRO A 305     1560   2731   2486    -78    -58   -151       N  
ATOM   2455  CA  PRO A 305      23.845  -5.482  18.162  1.00 16.80           C  
ANISOU 2455  CA  PRO A 305     1619   2568   2197    -76    -21     34       C  
ATOM   2456  CB  PRO A 305      23.019  -4.363  18.817  1.00 17.07           C  
ANISOU 2456  CB  PRO A 305     1561   2805   2118    -53     56    -12       C  
ATOM   2457  CG  PRO A 305      23.699  -3.085  18.380  1.00 18.84           C  
ANISOU 2457  CG  PRO A 305     1781   3055   2320   -286    137    -62       C  
ATOM   2458  CD  PRO A 305      25.176  -3.434  18.347  1.00 17.87           C  
ANISOU 2458  CD  PRO A 305     1633   2928   2228   -442    -11   -171       C  
ATOM   2459  C   PRO A 305      23.254  -5.915  16.817  1.00 16.70           C  
ANISOU 2459  C   PRO A 305     1503   2612   2228    -47     -5     48       C  
ATOM   2460  O   PRO A 305      22.393  -6.786  16.784  1.00 15.92           O  
ANISOU 2460  O   PRO A 305     1546   2395   2108     -7     71   -111       O  
ATOM   2461  N   TYR A 306      23.742  -5.308  15.736  1.00 17.06           N  
ANISOU 2461  N   TYR A 306     1603   2560   2317   -298     69    -11       N  
ATOM   2462  CA  TYR A 306      23.311  -5.616  14.369  1.00 16.73           C  
ANISOU 2462  CA  TYR A 306     1430   2723   2201    102    -41     74       C  
ATOM   2463  CB  TYR A 306      23.264  -4.343  13.525  1.00 18.77           C  
ANISOU 2463  CB  TYR A 306     1914   2599   2616    -65    153    134       C  
ATOM   2464  CG  TYR A 306      24.557  -3.570  13.500  1.00 19.75           C  
ANISOU 2464  CG  TYR A 306     2027   2710   2765   -208    -11    538       C  
ATOM   2465  CD1 TYR A 306      25.590  -3.927  12.647  1.00 21.81           C  
ANISOU 2465  CD1 TYR A 306     2113   2798   3375   -444    140    301       C  
ATOM   2466  CE1 TYR A 306      26.783  -3.228  12.632  1.00 23.29           C  
ANISOU 2466  CE1 TYR A 306     2035   3267   3546   -530    314    635       C  
ATOM   2467  CZ  TYR A 306      26.958  -2.144  13.476  1.00 23.35           C  
ANISOU 2467  CZ  TYR A 306     2040   3295   3537  -1003     12    764       C  
ATOM   2468  OH  TYR A 306      28.132  -1.443  13.454  1.00 27.13           O  
ANISOU 2468  OH  TYR A 306     1893   3791   4624   -956   -138   1127       O  
ATOM   2469  CE2 TYR A 306      25.944  -1.764  14.330  1.00 24.47           C  
ANISOU 2469  CE2 TYR A 306     2469   3271   3557   -604   -280    539       C  
ATOM   2470  CD2 TYR A 306      24.759  -2.482  14.343  1.00 22.53           C  
ANISOU 2470  CD2 TYR A 306     2269   3221   3068   -421     -6    432       C  
ATOM   2471  C   TYR A 306      24.243  -6.635  13.704  1.00 17.06           C  
ANISOU 2471  C   TYR A 306     1758   2596   2126    -35    219     76       C  
ATOM   2472  O   TYR A 306      24.105  -6.899  12.518  1.00 19.02           O  
ANISOU 2472  O   TYR A 306     2234   2820   2173    -73    173   -148       O  
ATOM   2473  N   GLY A 307      25.180  -7.208  14.469  1.00 17.55           N  
ANISOU 2473  N   GLY A 307     1787   2847   2031    105    161   -146       N  
ATOM   2474  CA  GLY A 307      26.072  -8.263  13.945  1.00 20.08           C  
ANISOU 2474  CA  GLY A 307     1956   3165   2505    212    461   -125       C  
ATOM   2475  C   GLY A 307      25.439  -9.642  14.028  1.00 18.96           C  
ANISOU 2475  C   GLY A 307     2178   2842   2181    458    279   -207       C  
ATOM   2476  O   GLY A 307      24.240  -9.783  14.249  1.00 17.71           O  
ANISOU 2476  O   GLY A 307     2138   2688   1901    590    204     40       O  
ATOM   2477  N   ILE A 308      26.273 -10.672  13.915  1.00 19.68           N  
ANISOU 2477  N   ILE A 308     2015   2991   2471    480    564   -136       N  
ATOM   2478  CA  ILE A 308      25.842 -12.065  14.001  1.00 20.19           C  
ANISOU 2478  CA  ILE A 308     1966   2923   2781    603    584    -19       C  
ATOM   2479  CB  ILE A 308      27.079 -12.999  14.038  1.00 23.61           C  
ANISOU 2479  CB  ILE A 308     2641   2732   3596    977    795   -420       C  
ATOM   2480  CG1 ILE A 308      27.872 -12.935  12.738  1.00 29.72           C  
ANISOU 2480  CG1 ILE A 308     3515   4045   3731   1144    829    -66       C  
ATOM   2481  CG2 ILE A 308      26.662 -14.422  14.361  1.00 27.04           C  
ANISOU 2481  CG2 ILE A 308     3568   2982   3722    889    819   -378       C  
ATOM   2482  CD1 ILE A 308      29.242 -13.553  12.829  1.00 31.52           C  
ANISOU 2482  CD1 ILE A 308     3579   3726   4670   1295    848   -133       C  
ATOM   2483  C   ILE A 308      24.988 -12.215  15.262  1.00 18.19           C  
ANISOU 2483  C   ILE A 308     1891   2728   2292    619    171     18       C  
ATOM   2484  O   ILE A 308      25.434 -11.878  16.364  1.00 18.95           O  
ANISOU 2484  O   ILE A 308     2228   2772   2198    524     11      9       O  
ATOM   2485  N   PRO A 309      23.747 -12.731  15.170  1.00 17.36           N  
ANISOU 2485  N   PRO A 309     1951   2778   1863    378     -4     53       N  
ATOM   2486  CA  PRO A 309      22.873 -12.747  16.347  1.00 17.01           C  
ANISOU 2486  CA  PRO A 309     1943   2626   1892    453     65     49       C  
ATOM   2487  CB  PRO A 309      21.552 -13.342  15.830  1.00 17.61           C  
ANISOU 2487  CB  PRO A 309     1914   2686   2089    398     86     24       C  
ATOM   2488  CG  PRO A 309      21.569 -13.008  14.352  1.00 20.24           C  
ANISOU 2488  CG  PRO A 309     2354   3130   2205    308   -137      0       C  
ATOM   2489  CD  PRO A 309      23.024 -13.052  13.928  1.00 18.40           C  
ANISOU 2489  CD  PRO A 309     2302   2869   1820    325    -76    156       C  
ATOM   2490  C   PRO A 309      23.463 -13.534  17.518  1.00 16.11           C  
ANISOU 2490  C   PRO A 309     1679   2580   1861    570    101   -100       C  
ATOM   2491  O   PRO A 309      23.340 -13.098  18.674  1.00 16.39           O  
ANISOU 2491  O   PRO A 309     1877   2454   1896    366    -71   -209       O  
ATOM   2492  N   GLY A 310      24.093 -14.666  17.219  1.00 19.09           N  
ANISOU 2492  N   GLY A 310     2322   2810   2119    968     49     -1       N  
ATOM   2493  CA  GLY A 310      24.684 -15.504  18.263  1.00 19.94           C  
ANISOU 2493  CA  GLY A 310     2348   3078   2149    790    -31    100       C  
ATOM   2494  C   GLY A 310      25.825 -14.848  19.020  1.00 20.14           C  
ANISOU 2494  C   GLY A 310     2350   3263   2036    792     26    -69       C  
ATOM   2495  O   GLY A 310      26.217 -15.363  20.070  1.00 22.33           O  
ANISOU 2495  O   GLY A 310     2590   3524   2370    681   -427     23       O  
ATOM   2496  N   GLU A 311      26.386 -13.753  18.491  1.00 19.81           N  
ANISOU 2496  N   GLU A 311     2086   3356   2085    751    -14     53       N  
ATOM   2497  CA AGLU A 311      27.486 -13.049  19.142  0.50 20.84           C  
ANISOU 2497  CA AGLU A 311     1928   3548   2441    792    -95    -52       C  
ATOM   2498  CA BGLU A 311      27.489 -13.042  19.130  0.50 20.72           C  
ANISOU 2498  CA BGLU A 311     1943   3510   2420    739     -7    -29       C  
ATOM   2499  CB AGLU A 311      28.566 -12.623  18.142  0.50 22.39           C  
ANISOU 2499  CB AGLU A 311     1930   3778   2796    724    -23    -52       C  
ATOM   2500  CB BGLU A 311      28.545 -12.579  18.116  0.50 22.57           C  
ANISOU 2500  CB BGLU A 311     2089   3676   2809    660    176     -4       C  
ATOM   2501  CG AGLU A 311      29.345 -13.795  17.553  0.50 24.57           C  
ANISOU 2501  CG AGLU A 311     2061   4017   3256   1036   -173   -184       C  
ATOM   2502  CG BGLU A 311      29.320 -13.713  17.458  0.50 24.66           C  
ANISOU 2502  CG BGLU A 311     2236   3888   3242    909    198    -92       C  
ATOM   2503  CD AGLU A 311      30.307 -14.529  18.480  0.50 26.50           C  
ANISOU 2503  CD AGLU A 311     1833   4602   3630   1400   -244   -344       C  
ATOM   2504  CD BGLU A 311      30.542 -13.307  16.631  0.50 26.68           C  
ANISOU 2504  CD BGLU A 311     2403   4271   3462   1054    493   -106       C  
ATOM   2505  OE1AGLU A 311      30.967 -15.481  18.014  0.50 32.29           O  
ANISOU 2505  OE1AGLU A 311     3683   3794   4791   1536   -420   -476       O  
ATOM   2506  OE1BGLU A 311      30.831 -12.082  16.531  0.50 28.96           O  
ANISOU 2506  OE1BGLU A 311     2855   4194   3952   1600    697    -27       O  
ATOM   2507  OE2AGLU A 311      30.410 -14.157  19.662  0.50 29.66           O  
ANISOU 2507  OE2AGLU A 311     2360   5041   3868   1224   -153   -603       O  
ATOM   2508  OE2BGLU A 311      31.220 -14.214  16.084  0.50 28.73           O  
ANISOU 2508  OE2BGLU A 311     2467   4214   4235   1170    337   -176       O  
ATOM   2509  C   GLU A 311      26.978 -11.836  19.933  1.00 19.04           C  
ANISOU 2509  C   GLU A 311     1707   3412   2114    479   -107    -15       C  
ATOM   2510  O   GLU A 311      27.756 -11.212  20.652  1.00 20.24           O  
ANISOU 2510  O   GLU A 311     1899   3451   2339    325   -239   -110       O  
ATOM   2511  N   ARG A 312      25.686 -11.481  19.818  1.00 17.69           N  
ANISOU 2511  N   ARG A 312     1720   2915   2085    418    -18    -87       N  
ATOM   2512  CA  ARG A 312      25.179 -10.378  20.648  1.00 17.99           C  
ANISOU 2512  CA  ARG A 312     1807   2838   2189    273   -206   -130       C  
ATOM   2513  CB  ARG A 312      23.689 -10.124  20.417  1.00 16.60           C  
ANISOU 2513  CB  ARG A 312     1733   2683   1891    292    -16    -83       C  
ATOM   2514  CG  ARG A 312      23.370  -9.590  19.026  1.00 15.74           C  
ANISOU 2514  CG  ARG A 312     1562   2467   1951    153    -83    -54       C  
ATOM   2515  CD  ARG A 312      21.878  -9.357  18.832  1.00 15.35           C  
ANISOU 2515  CD  ARG A 312     1519   2497   1815    205     78   -128       C  
ATOM   2516  NE  ARG A 312      21.452  -8.203  19.609  1.00 14.91           N  
ANISOU 2516  NE  ARG A 312     1536   2409   1718     69   -109   -270       N  
ATOM   2517  CZ  ARG A 312      20.233  -7.688  19.582  1.00 14.85           C  
ANISOU 2517  CZ  ARG A 312     1540   2158   1944     28   -139   -259       C  
ATOM   2518  NH1 ARG A 312      19.272  -8.292  18.874  1.00 13.95           N  
ANISOU 2518  NH1 ARG A 312     1641   1979   1679    -64   -133   -152       N  
ATOM   2519  NH2 ARG A 312      19.992  -6.581  20.277  1.00 15.39           N  
ANISOU 2519  NH2 ARG A 312     1957   1996   1891      9    -34   -162       N  
ATOM   2520  C   ARG A 312      25.437 -10.700  22.127  1.00 17.63           C  
ANISOU 2520  C   ARG A 312     1724   2796   2178    334   -357    -90       C  
ATOM   2521  O   ARG A 312      25.258 -11.835  22.572  1.00 19.25           O  
ANISOU 2521  O   ARG A 312     2217   2969   2125    294   -402    242       O  
ATOM   2522  N   ASN A 313      25.820  -9.676  22.896  1.00 17.25           N  
ANISOU 2522  N   ASN A 313     1719   2836   1997    238   -312    -35       N  
ATOM   2523  CA  ASN A 313      26.116  -9.888  24.312  1.00 18.33           C  
ANISOU 2523  CA  ASN A 313     1673   3202   2086    124   -497     47       C  
ATOM   2524  CB  ASN A 313      26.573  -8.613  25.009  1.00 19.97           C  
ANISOU 2524  CB  ASN A 313     1878   3278   2431    -82   -425     55       C  
ATOM   2525  CG  ASN A 313      27.905  -8.116  24.477  1.00 22.25           C  
ANISOU 2525  CG  ASN A 313     1982   3719   2750   -348   -534    145       C  
ATOM   2526  OD1 ASN A 313      27.936  -7.289  23.562  1.00 22.02           O  
ANISOU 2526  OD1 ASN A 313     2204   3601   2560   -364   -774     97       O  
ATOM   2527  ND2 ASN A 313      28.995  -8.612  25.040  1.00 25.46           N  
ANISOU 2527  ND2 ASN A 313     1975   4256   3442   -261   -751    346       N  
ATOM   2528  C   ASN A 313      24.881 -10.418  25.036  1.00 18.65           C  
ANISOU 2528  C   ASN A 313     1692   3170   2221     -6   -580      2       C  
ATOM   2529  O   ASN A 313      23.781  -9.862  24.862  1.00 18.55           O  
ANISOU 2529  O   ASN A 313     1602   3162   2282     11   -422     16       O  
ATOM   2530  N   LYS A 314      25.058 -11.495  25.816  1.00 19.10           N  
ANISOU 2530  N   LYS A 314     1615   3307   2333    144   -355    140       N  
ATOM   2531  CA  LYS A 314      23.934 -12.104  26.542  1.00 19.74           C  
ANISOU 2531  CA  LYS A 314     2004   3258   2237    163   -180    234       C  
ATOM   2532  CB  LYS A 314      24.038 -13.632  26.489  1.00 20.49           C  
ANISOU 2532  CB  LYS A 314     2231   3194   2358    215   -269    446       C  
ATOM   2533  CG  LYS A 314      23.988 -14.229  25.086  1.00 23.04           C  
ANISOU 2533  CG  LYS A 314     2508   3403   2841    371   -127    -45       C  
ATOM   2534  CD  LYS A 314      24.181 -15.732  25.090  1.00 26.01           C  
ANISOU 2534  CD  LYS A 314     2801   3439   3641    448   -386    409       C  
ATOM   2535  CE  LYS A 314      23.908 -16.422  23.765  1.00 30.31           C  
ANISOU 2535  CE  LYS A 314     3560   4093   3860    611    -79    138       C  
ATOM   2536  NZ  LYS A 314      24.777 -15.923  22.672  1.00 35.89           N  
ANISOU 2536  NZ  LYS A 314     3925   5242   4470    464    199    306       N  
ATOM   2537  C   LYS A 314      23.957 -11.603  27.983  1.00 19.97           C  
ANISOU 2537  C   LYS A 314     1864   3539   2182    665   -222    318       C  
ATOM   2538  O   LYS A 314      24.803 -12.014  28.785  1.00 25.21           O  
ANISOU 2538  O   LYS A 314     2571   5097   1907   1151   -567     48       O  
ATOM   2539  N   HIS A 315      23.058 -10.667  28.287  1.00 17.45           N  
ANISOU 2539  N   HIS A 315     1500   3169   1961    361   -318    186       N  
ATOM   2540  CA  HIS A 315      22.958 -10.086  29.621  1.00 17.58           C  
ANISOU 2540  CA  HIS A 315     1536   3225   1919    -40   -513    128       C  
ATOM   2541  CB  HIS A 315      22.424  -8.662  29.521  1.00 17.98           C  
ANISOU 2541  CB  HIS A 315     1558   3193   2079     11   -340   -186       C  
ATOM   2542  CG  HIS A 315      23.290  -7.782  28.695  1.00 19.54           C  
ANISOU 2542  CG  HIS A 315     1869   3050   2505     88   -127    -13       C  
ATOM   2543  ND1 HIS A 315      24.519  -7.350  29.153  1.00 21.18           N  
ANISOU 2543  ND1 HIS A 315     2395   2989   2663   -409   -359     73       N  
ATOM   2544  CE1 HIS A 315      25.072  -6.581  28.230  1.00 24.81           C  
ANISOU 2544  CE1 HIS A 315     2687   3506   3230   -276    259    160       C  
ATOM   2545  NE2 HIS A 315      24.219  -6.479  27.192  1.00 24.30           N  
ANISOU 2545  NE2 HIS A 315     2627   3525   3079    -10    382     -4       N  
ATOM   2546  CD2 HIS A 315      23.110  -7.234  27.468  1.00 20.68           C  
ANISOU 2546  CD2 HIS A 315     2191   3216   2447     -5   -249   -152       C  
ATOM   2547  C   HIS A 315      22.062 -10.961  30.496  1.00 18.06           C  
ANISOU 2547  C   HIS A 315     1714   3244   1902    125   -403    229       C  
ATOM   2548  O   HIS A 315      21.061 -11.488  30.003  1.00 18.11           O  
ANISOU 2548  O   HIS A 315     1768   3364   1748     45   -271     20       O  
ATOM   2549  N   ILE A 316      22.391 -11.059  31.787  1.00 19.20           N  
ANISOU 2549  N   ILE A 316     2047   3409   1839      8   -425     95       N  
ATOM   2550  CA  ILE A 316      21.580 -11.839  32.711  1.00 18.98           C  
ANISOU 2550  CA  ILE A 316     1924   3388   1897      3   -483     44       C  
ATOM   2551  CB  ILE A 316      22.331 -13.094  33.203  1.00 21.85           C  
ANISOU 2551  CB  ILE A 316     1941   3757   2605    265   -352    300       C  
ATOM   2552  CG1 ILE A 316      22.789 -13.957  32.028  1.00 22.20           C  
ANISOU 2552  CG1 ILE A 316     2049   3919   2466    555   -190    498       C  
ATOM   2553  CG2 ILE A 316      21.463 -13.904  34.165  1.00 22.89           C  
ANISOU 2553  CG2 ILE A 316     2196   3849   2653    519   -359    595       C  
ATOM   2554  CD1 ILE A 316      23.596 -15.190  32.424  1.00 26.18           C  
ANISOU 2554  CD1 ILE A 316     2814   3982   3151    800    -85    658       C  
ATOM   2555  C   ILE A 316      21.157 -10.937  33.880  1.00 18.21           C  
ANISOU 2555  C   ILE A 316     1806   3233   1879    -51   -449    -69       C  
ATOM   2556  O   ILE A 316      22.015 -10.261  34.493  1.00 18.65           O  
ANISOU 2556  O   ILE A 316     2136   3169   1779    -79   -364   -316       O  
ATOM   2557  N   LEU A 317      19.872 -11.030  34.245  1.00 16.46           N  
ANISOU 2557  N   LEU A 317     1829   2983   1442   -144   -578   -111       N  
ATOM   2558  CA  LEU A 317      19.376 -10.459  35.488  1.00 17.02           C  
ANISOU 2558  CA  LEU A 317     1797   2982   1685   -184   -543   -296       C  
ATOM   2559  CB  LEU A 317      18.474  -9.248  35.226  1.00 17.45           C  
ANISOU 2559  CB  LEU A 317     1857   2842   1930   -253   -415   -346       C  
ATOM   2560  CG  LEU A 317      19.178  -7.959  34.820  1.00 17.74           C  
ANISOU 2560  CG  LEU A 317     1946   2735   2060   -252   -155   -354       C  
ATOM   2561  CD1 LEU A 317      18.174  -6.910  34.347  1.00 18.91           C  
ANISOU 2561  CD1 LEU A 317     2333   2694   2155   -243    -44   -197       C  
ATOM   2562  CD2 LEU A 317      20.030  -7.421  35.968  1.00 19.91           C  
ANISOU 2562  CD2 LEU A 317     2376   2919   2270   -500   -365   -205       C  
ATOM   2563  C   LEU A 317      18.599 -11.548  36.227  1.00 18.07           C  
ANISOU 2563  C   LEU A 317     2028   3167   1670    -84   -356   -122       C  
ATOM   2564  O   LEU A 317      17.822 -12.307  35.595  1.00 18.12           O  
ANISOU 2564  O   LEU A 317     2204   2824   1855    189   -571    -59       O  
ATOM   2565  N   THR A 318      18.760 -11.570  37.549  1.00 18.91           N  
ANISOU 2565  N   THR A 318     2147   3240   1796    201   -710   -109       N  
ATOM   2566  CA  THR A 318      18.012 -12.483  38.405  1.00 18.98           C  
ANISOU 2566  CA  THR A 318     2376   3073   1762    288   -455   -163       C  
ATOM   2567  CB  THR A 318      18.941 -13.559  38.977  1.00 20.65           C  
ANISOU 2567  CB  THR A 318     2538   3412   1892    452   -855   -335       C  
ATOM   2568  OG1 THR A 318      19.642 -14.196  37.911  1.00 22.17           O  
ANISOU 2568  OG1 THR A 318     2572   3667   2183    678   -406    -64       O  
ATOM   2569  CG2 THR A 318      18.197 -14.598  39.788  1.00 24.02           C  
ANISOU 2569  CG2 THR A 318     2974   3820   2331    349   -340   -185       C  
ATOM   2570  C   THR A 318      17.372 -11.698  39.548  1.00 18.63           C  
ANISOU 2570  C   THR A 318     2119   3036   1922    199   -397   -127       C  
ATOM   2571  O   THR A 318      18.062 -10.979  40.295  1.00 19.49           O  
ANISOU 2571  O   THR A 318     2146   2928   2329   -148   -346    -36       O  
ATOM   2572  N   THR A 319      16.059 -11.867  39.704  1.00 17.86           N  
ANISOU 2572  N   THR A 319     2105   2846   1835    174   -338     73       N  
ATOM   2573  CA  THR A 319      15.368 -11.214  40.811  1.00 17.94           C  
ANISOU 2573  CA  THR A 319     2459   2436   1919    289   -402    -89       C  
ATOM   2574  CB  THR A 319      13.853 -11.427  40.779  1.00 17.47           C  
ANISOU 2574  CB  THR A 319     2364   2526   1745    296   -275    -82       C  
ATOM   2575  OG1 THR A 319      13.532 -12.796  41.021  1.00 18.15           O  
ANISOU 2575  OG1 THR A 319     2322   2661   1909    -12   -415   -120       O  
ATOM   2576  CG2 THR A 319      13.202 -10.988  39.487  1.00 18.20           C  
ANISOU 2576  CG2 THR A 319     2330   2647   1936    136   -465     45       C  
ATOM   2577  C   THR A 319      15.884 -11.763  42.144  1.00 19.18           C  
ANISOU 2577  C   THR A 319     2295   3185   1807     42   -454    -98       C  
ATOM   2578  O   THR A 319      16.423 -12.868  42.205  1.00 21.12           O  
ANISOU 2578  O   THR A 319     2595   3578   1851    378   -766    -80       O  
ATOM   2579  N   HIS A 320      15.707 -10.974  43.202  1.00 19.94           N  
ANISOU 2579  N   HIS A 320     2727   3034   1812   -137   -302   -107       N  
ATOM   2580  CA  HIS A 320      15.753 -11.497  44.545  1.00 21.28           C  
ANISOU 2580  CA  HIS A 320     2726   3601   1757   -212   -597   -217       C  
ATOM   2581  CB  HIS A 320      15.663 -10.362  45.577  1.00 24.13           C  
ANISOU 2581  CB  HIS A 320     3638   3798   1730   -331   -440   -279       C  
ATOM   2582  CG  HIS A 320      16.725  -9.328  45.417  1.00 29.16           C  
ANISOU 2582  CG  HIS A 320     3913   4577   2588   -885   -737   -289       C  
ATOM   2583  ND1 HIS A 320      18.062  -9.632  45.553  1.00 34.34           N  
ANISOU 2583  ND1 HIS A 320     3855   5378   3814   -803   -553   -117       N  
ATOM   2584  CE1 HIS A 320      18.783  -8.543  45.355  1.00 34.77           C  
ANISOU 2584  CE1 HIS A 320     4352   5130   3727   -911   -766   -537       C  
ATOM   2585  NE2 HIS A 320      17.949  -7.534  45.075  1.00 36.60           N  
ANISOU 2585  NE2 HIS A 320     4670   4818   4416  -1098   -736   -413       N  
ATOM   2586  CD2 HIS A 320      16.660  -8.008  45.116  1.00 34.80           C  
ANISOU 2586  CD2 HIS A 320     4511   4766   3942   -872  -1015    -35       C  
ATOM   2587  C   HIS A 320      14.592 -12.490  44.692  1.00 19.30           C  
ANISOU 2587  C   HIS A 320     2271   3329   1734    125   -545    -90       C  
ATOM   2588  O   HIS A 320      13.677 -12.537  43.849  1.00 20.98           O  
ANISOU 2588  O   HIS A 320     2291   3979   1699    -73   -552     44       O  
ATOM   2589  N   SER A 321      14.615 -13.268  45.770  1.00 21.93           N  
ANISOU 2589  N   SER A 321     2521   3868   1941     81   -366    212       N  
ATOM   2590  CA  SER A 321      13.515 -14.166  46.055  1.00 21.50           C  
ANISOU 2590  CA  SER A 321     2649   3543   1975     72   -517    162       C  
ATOM   2591  CB  SER A 321      13.841 -15.098  47.193  1.00 25.23           C  
ANISOU 2591  CB  SER A 321     3271   3972   2342    197   -327    593       C  
ATOM   2592  OG  SER A 321      12.846 -16.106  47.322  1.00 27.86           O  
ANISOU 2592  OG  SER A 321     3538   3933   3112    169   -187    892       O  
ATOM   2593  C   SER A 321      12.254 -13.334  46.329  1.00 22.13           C  
ANISOU 2593  C   SER A 321     2567   3808   2033    -45   -285   -131       C  
ATOM   2594  O   SER A 321      12.276 -12.363  47.078  1.00 25.78           O  
ANISOU 2594  O   SER A 321     2931   4563   2300     46   -259   -667       O  
ATOM   2595  N   MET A 322      11.164 -13.714  45.674  1.00 19.85           N  
ANISOU 2595  N   MET A 322     2646   3258   1638      5   -326   -139       N  
ATOM   2596  CA  MET A 322       9.870 -13.033  45.797  1.00 19.41           C  
ANISOU 2596  CA  MET A 322     2844   2942   1587    159     30   -436       C  
ATOM   2597  CB  MET A 322       9.248 -12.744  44.423  1.00 19.36           C  
ANISOU 2597  CB  MET A 322     2679   2608   2068    189   -243    -30       C  
ATOM   2598  CG  MET A 322      10.154 -11.892  43.544  1.00 19.85           C  
ANISOU 2598  CG  MET A 322     2730   2969   1842    351      7    -61       C  
ATOM   2599  SD  MET A 322       9.542 -11.641  41.881  1.00 20.65           S  
ANISOU 2599  SD  MET A 322     2850   2928   2066    579   -133     17       S  
ATOM   2600  CE  MET A 322       9.945 -13.213  41.129  1.00 18.60           C  
ANISOU 2600  CE  MET A 322     2303   2676   2085    487   -139     96       C  
ATOM   2601  C   MET A 322       8.931 -13.929  46.609  1.00 18.82           C  
ANISOU 2601  C   MET A 322     2826   2708   1616    296   -126   -206       C  
ATOM   2602  O   MET A 322       8.549 -15.004  46.160  1.00 20.31           O  
ANISOU 2602  O   MET A 322     2887   2882   1947    122    -67   -263       O  
ATOM   2603  N   ALA A 323       8.551 -13.437  47.787  1.00 19.39           N  
ANISOU 2603  N   ALA A 323     2880   2943   1545    162    -60   -240       N  
ATOM   2604  CA  ALA A 323       7.685 -14.147  48.719  1.00 21.03           C  
ANISOU 2604  CA  ALA A 323     2895   3308   1786     59    -83   -250       C  
ATOM   2605  CB  ALA A 323       8.035 -13.791  50.141  1.00 22.68           C  
ANISOU 2605  CB  ALA A 323     2889   4008   1717    -54    -10   -355       C  
ATOM   2606  C   ALA A 323       6.235 -13.788  48.412  1.00 19.93           C  
ANISOU 2606  C   ALA A 323     2866   3021   1685    155   -135   -474       C  
ATOM   2607  O   ALA A 323       5.877 -12.622  48.419  1.00 24.85           O  
ANISOU 2607  O   ALA A 323     3103   3150   3187    220    -27   -785       O  
ATOM   2608  N   MET A 324       5.422 -14.805  48.141  1.00 20.54           N  
ANISOU 2608  N   MET A 324     2824   2875   2101    212    100   -488       N  
ATOM   2609  CA  MET A 324       4.003 -14.628  47.870  1.00 20.25           C  
ANISOU 2609  CA  MET A 324     2871   2820   2001     44    -21   -253       C  
ATOM   2610  CB  MET A 324       3.688 -15.003  46.422  1.00 19.49           C  
ANISOU 2610  CB  MET A 324     2739   2638   2027    -16   -371     13       C  
ATOM   2611  CG  MET A 324       4.371 -14.089  45.440  1.00 21.04           C  
ANISOU 2611  CG  MET A 324     3138   2816   2038   -165   -224   -107       C  
ATOM   2612  SD  MET A 324       4.161 -14.589  43.727  1.00 23.58           S  
ANISOU 2612  SD  MET A 324     3272   3789   1898     -7   -286     28       S  
ATOM   2613  CE  MET A 324       5.670 -15.506  43.501  1.00 24.43           C  
ANISOU 2613  CE  MET A 324     3394   3394   2494    129   -167     81       C  
ATOM   2614  C   MET A 324       3.204 -15.494  48.848  1.00 19.37           C  
ANISOU 2614  C   MET A 324     2916   2849   1595    192   -154   -199       C  
ATOM   2615  O   MET A 324       3.577 -16.619  49.136  1.00 21.97           O  
ANISOU 2615  O   MET A 324     2801   3125   2419    503    285    276       O  
ATOM   2616  N   ASN A 325       2.095 -14.952  49.338  1.00 18.83           N  
ANISOU 2616  N   ASN A 325     2679   2908   1568    191   -329   -298       N  
ATOM   2617  CA  ASN A 325       1.267 -15.599  50.357  1.00 20.36           C  
ANISOU 2617  CA  ASN A 325     3196   2841   1698    261   -104   -113       C  
ATOM   2618  CB  ASN A 325       0.517 -14.558  51.194  1.00 25.55           C  
ANISOU 2618  CB  ASN A 325     3819   3519   2367    338    113   -717       C  
ATOM   2619  CG  ASN A 325       1.449 -13.706  52.023  1.00 32.79           C  
ANISOU 2619  CG  ASN A 325     4432   4566   3458    177   -521   -933       C  
ATOM   2620  OD1 ASN A 325       2.507 -14.167  52.438  1.00 40.53           O  
ANISOU 2620  OD1 ASN A 325     4852   6652   3894    643   -986  -1244       O  
ATOM   2621  ND2 ASN A 325       1.054 -12.474  52.299  1.00 40.83           N  
ANISOU 2621  ND2 ASN A 325     6279   4820   4412    569   -261  -1030       N  
ATOM   2622  C   ASN A 325       0.245 -16.550  49.723  1.00 17.04           C  
ANISOU 2622  C   ASN A 325     2701   2492   1282    477    -42     24       C  
ATOM   2623  O   ASN A 325      -0.458 -17.277  50.427  1.00 21.16           O  
ANISOU 2623  O   ASN A 325     3284   3092   1663    216    197    213       O  
ATOM   2624  N   ASN A 326       0.120 -16.497  48.394  1.00 15.68           N  
ANISOU 2624  N   ASN A 326     2581   2076   1298    287   -175    155       N  
ATOM   2625  CA  ASN A 326      -0.858 -17.291  47.627  1.00 16.60           C  
ANISOU 2625  CA  ASN A 326     2669   2152   1483    278   -158     79       C  
ATOM   2626  CB  ASN A 326      -2.245 -16.671  47.733  1.00 17.18           C  
ANISOU 2626  CB  ASN A 326     2651   2439   1436    251   -140    -74       C  
ATOM   2627  CG  ASN A 326      -2.246 -15.242  47.256  1.00 18.55           C  
ANISOU 2627  CG  ASN A 326     2968   2388   1691    453      3   -149       C  
ATOM   2628  OD1 ASN A 326      -2.157 -15.013  46.041  1.00 20.42           O  
ANISOU 2628  OD1 ASN A 326     3717   2203   1835    554    -23    114       O  
ATOM   2629  ND2 ASN A 326      -2.280 -14.280  48.188  1.00 18.83           N  
ANISOU 2629  ND2 ASN A 326     2580   2383   2190    536   -184   -349       N  
ATOM   2630  C   ASN A 326      -0.330 -17.389  46.195  1.00 16.01           C  
ANISOU 2630  C   ASN A 326     2450   2152   1480    325   -211     47       C  
ATOM   2631  O   ASN A 326       0.611 -16.668  45.840  1.00 18.06           O  
ANISOU 2631  O   ASN A 326     2527   2700   1633    127   -120    -99       O  
ATOM   2632  N   VAL A 327      -0.950 -18.250  45.378  1.00 13.80           N  
ANISOU 2632  N   VAL A 327     2018   1892   1331    321    -70    145       N  
ATOM   2633  CA  VAL A 327      -0.455 -18.535  44.039  1.00 14.84           C  
ANISOU 2633  CA  VAL A 327     2179   2010   1447    499    -92     73       C  
ATOM   2634  CB  VAL A 327      -0.523 -20.040  43.759  1.00 15.44           C  
ANISOU 2634  CB  VAL A 327     2281   2064   1520    507    -99      3       C  
ATOM   2635  CG1 VAL A 327       0.033 -20.357  42.381  1.00 16.64           C  
ANISOU 2635  CG1 VAL A 327     2269   2377   1675    576    171    187       C  
ATOM   2636  CG2 VAL A 327       0.204 -20.842  44.838  1.00 16.75           C  
ANISOU 2636  CG2 VAL A 327     2507   2379   1478    428    -64    197       C  
ATOM   2637  C   VAL A 327      -1.259 -17.755  43.009  1.00 14.08           C  
ANISOU 2637  C   VAL A 327     2246   1669   1433    442     -8    117       C  
ATOM   2638  O   VAL A 327      -2.440 -18.017  42.797  1.00 15.60           O  
ANISOU 2638  O   VAL A 327     2398   1897   1631    500   -208    180       O  
ATOM   2639  N   PRO A 328      -0.639 -16.790  42.308  1.00 13.32           N  
ANISOU 2639  N   PRO A 328     2144   1774   1141    325   -119    124       N  
ATOM   2640  CA  PRO A 328      -1.336 -16.058  41.248  1.00 13.03           C  
ANISOU 2640  CA  PRO A 328     2122   1554   1273    297   -136    115       C  
ATOM   2641  CB  PRO A 328      -0.327 -15.007  40.805  1.00 14.89           C  
ANISOU 2641  CB  PRO A 328     2291   1819   1547     50    -84    167       C  
ATOM   2642  CG  PRO A 328       0.572 -14.834  42.014  1.00 15.94           C  
ANISOU 2642  CG  PRO A 328     2295   2002   1758    114   -242    278       C  
ATOM   2643  CD  PRO A 328       0.680 -16.221  42.602  1.00 15.24           C  
ANISOU 2643  CD  PRO A 328     2245   1944   1601    258    -63    132       C  
ATOM   2644  C   PRO A 328      -1.728 -16.915  40.042  1.00 12.86           C  
ANISOU 2644  C   PRO A 328     1993   1697   1194    254    -73    107       C  
ATOM   2645  O   PRO A 328      -1.141 -17.955  39.778  1.00 16.13           O  
ANISOU 2645  O   PRO A 328     2640   1833   1653    545   -284    -23       O  
ATOM   2646  N   SER A 329      -2.717 -16.415  39.310  1.00 13.10           N  
ANISOU 2646  N   SER A 329     2008   1757   1210    505     13      5       N  
ATOM   2647  CA  SER A 329      -3.171 -17.000  38.060  1.00 12.79           C  
ANISOU 2647  CA  SER A 329     1805   1754   1301    262     78    -43       C  
ATOM   2648  CB  SER A 329      -4.428 -16.312  37.626  1.00 15.28           C  
ANISOU 2648  CB  SER A 329     1594   2430   1781    299     22   -285       C  
ATOM   2649  OG  SER A 329      -4.871 -16.751  36.355  1.00 18.14           O  
ANISOU 2649  OG  SER A 329     2263   2509   2117    306   -104   -596       O  
ATOM   2650  C   SER A 329      -2.123 -16.919  36.951  1.00 12.49           C  
ANISOU 2650  C   SER A 329     1793   1681   1268    308     26     32       C  
ATOM   2651  O   SER A 329      -2.027 -17.830  36.120  1.00 13.48           O  
ANISOU 2651  O   SER A 329     2262   1456   1402    411    226     55       O  
ATOM   2652  N   MET A 330      -1.420 -15.782  36.862  1.00 12.65           N  
ANISOU 2652  N   MET A 330     1962   1654   1191    203    143   -143       N  
ATOM   2653  CA  MET A 330      -0.513 -15.577  35.758  1.00 12.33           C  
ANISOU 2653  CA  MET A 330     1765   1526   1394    181    227   -138       C  
ATOM   2654  CB  MET A 330      -1.221 -15.024  34.506  1.00 14.24           C  
ANISOU 2654  CB  MET A 330     1664   1851   1893    -90   -108     64       C  
ATOM   2655  CG  MET A 330      -0.381 -15.103  33.204  1.00 17.27           C  
ANISOU 2655  CG  MET A 330     1837   2574   2148   -113     27    607       C  
ATOM   2656  SD  MET A 330      -1.256 -14.487  31.755  1.00 19.00           S  
ANISOU 2656  SD  MET A 330     2520   2757   1942    -11   -143    136       S  
ATOM   2657  CE  MET A 330      -2.494 -15.757  31.525  1.00 18.47           C  
ANISOU 2657  CE  MET A 330     2476   2396   2144    -22   -222    193       C  
ATOM   2658  C   MET A 330       0.608 -14.641  36.205  1.00 12.48           C  
ANISOU 2658  C   MET A 330     1926   1452   1364    216    -10    -44       C  
ATOM   2659  O   MET A 330       0.426 -13.819  37.097  1.00 13.15           O  
ANISOU 2659  O   MET A 330     1975   1670   1352    286     29   -144       O  
ATOM   2660  N   PHE A 331       1.762 -14.792  35.559  1.00 12.98           N  
ANISOU 2660  N   PHE A 331     1980   1643   1308     63     17    -87       N  
ATOM   2661  CA  PHE A 331       2.911 -13.935  35.722  1.00 12.54           C  
ANISOU 2661  CA  PHE A 331     1827   1648   1289    130   -118    -56       C  
ATOM   2662  CB  PHE A 331       4.121 -14.719  36.238  1.00 14.61           C  
ANISOU 2662  CB  PHE A 331     1898   2097   1553    314    -88     80       C  
ATOM   2663  CG  PHE A 331       3.901 -15.276  37.612  1.00 16.71           C  
ANISOU 2663  CG  PHE A 331     2109   2612   1628    463   -139    242       C  
ATOM   2664  CD1 PHE A 331       4.165 -14.519  38.740  1.00 19.12           C  
ANISOU 2664  CD1 PHE A 331     2716   2906   1641    539    -47    191       C  
ATOM   2665  CE1 PHE A 331       3.961 -15.040  40.004  1.00 21.21           C  
ANISOU 2665  CE1 PHE A 331     3094   3290   1675    699   -145    419       C  
ATOM   2666  CZ  PHE A 331       3.448 -16.300  40.140  1.00 20.98           C  
ANISOU 2666  CZ  PHE A 331     2939   3533   1500    550    266    915       C  
ATOM   2667  CD2 PHE A 331       3.414 -16.555  37.769  1.00 18.72           C  
ANISOU 2667  CD2 PHE A 331     2514   2765   1834    421    -43    804       C  
ATOM   2668  CE2 PHE A 331       3.166 -17.057  39.035  1.00 21.40           C  
ANISOU 2668  CE2 PHE A 331     2790   3488   1852    456    -30    889       C  
ATOM   2669  C   PHE A 331       3.279 -13.337  34.372  1.00 12.85           C  
ANISOU 2669  C   PHE A 331     1740   1829   1312     91   -198     57       C  
ATOM   2670  O   PHE A 331       2.979 -13.934  33.318  1.00 12.54           O  
ANISOU 2670  O   PHE A 331     1700   1756   1306    225   -195     -1       O  
ATOM   2671  N   ALA A 332       3.964 -12.198  34.419  1.00 13.76           N  
ANISOU 2671  N   ALA A 332     1913   1916   1397     34   -149   -212       N  
ATOM   2672  CA  ALA A 332       4.482 -11.560  33.196  1.00 14.06           C  
ANISOU 2672  CA  ALA A 332     1848   1996   1496    -56   -108   -196       C  
ATOM   2673  CB  ALA A 332       3.623 -10.405  32.739  1.00 14.88           C  
ANISOU 2673  CB  ALA A 332     1851   2309   1491     37   -288   -100       C  
ATOM   2674  C   ALA A 332       5.904 -11.095  33.482  1.00 13.64           C  
ANISOU 2674  C   ALA A 332     1672   1981   1527    -25     -4    -39       C  
ATOM   2675  O   ALA A 332       6.143 -10.444  34.513  1.00 15.53           O  
ANISOU 2675  O   ALA A 332     1983   2161   1755   -108    -16    -97       O  
ATOM   2676  N   VAL A 333       6.816 -11.415  32.563  1.00 13.01           N  
ANISOU 2676  N   VAL A 333     1640   2039   1261   -187    -16    -22       N  
ATOM   2677  CA  VAL A 333       8.217 -11.053  32.672  1.00 13.24           C  
ANISOU 2677  CA  VAL A 333     1613   1888   1528    -91    -66   -196       C  
ATOM   2678  CB  VAL A 333       9.115 -12.304  32.612  1.00 14.04           C  
ANISOU 2678  CB  VAL A 333     1895   1788   1650    -23   -155   -126       C  
ATOM   2679  CG1 VAL A 333      10.585 -11.957  32.736  1.00 14.31           C  
ANISOU 2679  CG1 VAL A 333     1906   1757   1773     62    -41   -107       C  
ATOM   2680  CG2 VAL A 333       8.694 -13.314  33.655  1.00 15.57           C  
ANISOU 2680  CG2 VAL A 333     1990   1932   1993     73   -198    151       C  
ATOM   2681  C   VAL A 333       8.584 -10.122  31.517  1.00 13.84           C  
ANISOU 2681  C   VAL A 333     1663   1962   1630   -141   -179    -69       C  
ATOM   2682  O   VAL A 333       8.293 -10.427  30.360  1.00 15.22           O  
ANISOU 2682  O   VAL A 333     2173   2037   1571     16   -159    -18       O  
ATOM   2683  N   MET A 334       9.230  -8.994  31.835  1.00 13.79           N  
ANISOU 2683  N   MET A 334     1565   2115   1556   -195   -192   -217       N  
ATOM   2684  CA  MET A 334       9.604  -7.978  30.852  1.00 15.70           C  
ANISOU 2684  CA  MET A 334     1638   2317   2009   -383    142   -182       C  
ATOM   2685  CB  MET A 334       8.472  -6.931  30.884  1.00 21.18           C  
ANISOU 2685  CB  MET A 334     1907   2689   3449    -53   -480    457       C  
ATOM   2686  CG  MET A 334       8.590  -5.743  30.057  1.00 24.70           C  
ANISOU 2686  CG  MET A 334     2653   2881   3849   -104   -125    216       C  
ATOM   2687  SD  MET A 334       7.059  -4.816  30.234  1.00 31.91           S  
ANISOU 2687  SD  MET A 334     3324   2742   6058    498    646     76       S  
ATOM   2688  CE  MET A 334       7.266  -4.028  31.813  1.00 35.09           C  
ANISOU 2688  CE  MET A 334     4450   3518   5363    323    107    784       C  
ATOM   2689  C   MET A 334      10.931  -7.382  31.321  1.00 14.26           C  
ANISOU 2689  C   MET A 334     1738   2263   1417   -355    -55    111       C  
ATOM   2690  O   MET A 334      11.130  -7.228  32.529  1.00 17.11           O  
ANISOU 2690  O   MET A 334     2177   2952   1370   -659    -37    155       O  
ATOM   2691  N   VAL A 335      11.818  -7.036  30.389  1.00 13.55           N  
ANISOU 2691  N   VAL A 335     1716   2009   1421   -546    -62    -48       N  
ATOM   2692  CA  VAL A 335      13.057  -6.330  30.711  1.00 14.10           C  
ANISOU 2692  CA  VAL A 335     1741   1988   1628   -459   -165   -165       C  
ATOM   2693  CB  VAL A 335      14.307  -7.159  30.361  1.00 15.22           C  
ANISOU 2693  CB  VAL A 335     1935   2249   1599   -374    -69   -136       C  
ATOM   2694  CG1 VAL A 335      15.583  -6.383  30.645  1.00 16.45           C  
ANISOU 2694  CG1 VAL A 335     1962   2384   1903   -401   -123    -62       C  
ATOM   2695  CG2 VAL A 335      14.316  -8.507  31.061  1.00 14.91           C  
ANISOU 2695  CG2 VAL A 335     1803   2345   1517   -293    -86    -58       C  
ATOM   2696  C   VAL A 335      13.014  -5.002  29.940  1.00 14.25           C  
ANISOU 2696  C   VAL A 335     1729   2143   1540   -307   -156   -128       C  
ATOM   2697  O   VAL A 335      13.073  -4.995  28.696  1.00 16.34           O  
ANISOU 2697  O   VAL A 335     2326   2327   1555    -42    153   -214       O  
ATOM   2698  N   SER A 336      12.914  -3.896  30.676  1.00 15.64           N  
ANISOU 2698  N   SER A 336     2049   2229   1661   -323   -277   -325       N  
ATOM   2699  CA ASER A 336      12.643  -2.565  30.098  0.50 15.84           C  
ANISOU 2699  CA ASER A 336     2161   2193   1663   -397   -309   -355       C  
ATOM   2700  CA BSER A 336      12.654  -2.574  30.077  0.50 16.65           C  
ANISOU 2700  CA BSER A 336     2268   2260   1797   -452   -347   -233       C  
ATOM   2701  CB ASER A 336      11.568  -1.811  30.876  0.50 16.89           C  
ANISOU 2701  CB ASER A 336     2206   2497   1712   -536   -184   -579       C  
ATOM   2702  CB BSER A 336      11.546  -1.829  30.791  0.50 19.23           C  
ANISOU 2702  CB BSER A 336     2503   2670   2134   -448   -137   -391       C  
ATOM   2703  OG ASER A 336      10.279  -2.383  30.731  0.50 16.72           O  
ANISOU 2703  OG ASER A 336     2214   2230   1909   -555    -31   -568       O  
ATOM   2704  OG BSER A 336      11.715  -1.927  32.180  0.50 21.50           O  
ANISOU 2704  OG BSER A 336     3133   2765   2270   -426   -123     34       O  
ATOM   2705  C   SER A 336      13.928  -1.731  30.085  1.00 16.43           C  
ANISOU 2705  C   SER A 336     2165   2263   1814   -380   -431   -365       C  
ATOM   2706  O   SER A 336      14.661  -1.721  31.077  1.00 17.09           O  
ANISOU 2706  O   SER A 336     2520   2398   1574   -320   -463   -262       O  
ATOM   2707  N   GLN A 337      14.127  -0.974  29.001  1.00 17.05           N  
ANISOU 2707  N   GLN A 337     2293   2318   1866   -564   -464   -356       N  
ATOM   2708  CA  GLN A 337      15.100   0.097  28.986  1.00 18.02           C  
ANISOU 2708  CA  GLN A 337     2324   2463   2058   -629   -635   -248       C  
ATOM   2709  CB  GLN A 337      15.203   0.675  27.578  1.00 19.72           C  
ANISOU 2709  CB  GLN A 337     2746   2521   2226   -801   -636    -47       C  
ATOM   2710  CG  GLN A 337      16.305   1.699  27.422  1.00 22.09           C  
ANISOU 2710  CG  GLN A 337     3029   2877   2485  -1041   -564     30       C  
ATOM   2711  CD  GLN A 337      16.223   2.281  26.039  1.00 21.80           C  
ANISOU 2711  CD  GLN A 337     2945   2804   2533   -759   -458    125       C  
ATOM   2712  OE1 GLN A 337      15.281   3.005  25.722  1.00 20.89           O  
ANISOU 2712  OE1 GLN A 337     2576   2627   2732   -632   -131   -123       O  
ATOM   2713  NE2 GLN A 337      17.169   1.894  25.189  1.00 25.73           N  
ANISOU 2713  NE2 GLN A 337     2875   3585   3315   -963    -54   -135       N  
ATOM   2714  C   GLN A 337      14.631   1.163  29.982  1.00 19.09           C  
ANISOU 2714  C   GLN A 337     2285   2518   2448   -492   -637   -354       C  
ATOM   2715  O   GLN A 337      13.536   1.684  29.859  1.00 20.37           O  
ANISOU 2715  O   GLN A 337     2466   2640   2632   -258   -663   -287       O  
ATOM   2716  N   GLU A 338      15.475   1.490  30.966  1.00 19.23           N  
ANISOU 2716  N   GLU A 338     2313   2856   2136   -356   -541   -443       N  
ATOM   2717  CA AGLU A 338      15.051   2.339  32.081  0.50 20.57           C  
ANISOU 2717  CA AGLU A 338     2694   2785   2336   -303   -485   -483       C  
ATOM   2718  CA BGLU A 338      15.050   2.337  32.084  0.50 21.43           C  
ANISOU 2718  CA BGLU A 338     2907   2804   2432   -229   -452   -505       C  
ATOM   2719  CB AGLU A 338      16.038   2.250  33.246  0.50 20.85           C  
ANISOU 2719  CB AGLU A 338     2895   2898   2130   -460   -439   -504       C  
ATOM   2720  CB BGLU A 338      16.052   2.276  33.239  0.50 23.31           C  
ANISOU 2720  CB BGLU A 338     3358   3114   2385   -345   -564   -443       C  
ATOM   2721  CG AGLU A 338      15.783   1.021  34.101  0.50 22.47           C  
ANISOU 2721  CG AGLU A 338     2997   3112   2427   -583   -281   -312       C  
ATOM   2722  CG BGLU A 338      15.713   3.216  34.388  0.50 26.31           C  
ANISOU 2722  CG BGLU A 338     3956   3362   2676   -311   -340   -553       C  
ATOM   2723  CD AGLU A 338      16.445   0.965  35.469  0.50 23.03           C  
ANISOU 2723  CD AGLU A 338     2986   3269   2492   -814   -412   -621       C  
ATOM   2724  CD BGLU A 338      14.462   2.859  35.172  0.50 28.82           C  
ANISOU 2724  CD BGLU A 338     4001   3849   3100   -398   -267   -639       C  
ATOM   2725  OE1AGLU A 338      15.754   1.170  36.471  0.50 28.10           O  
ANISOU 2725  OE1AGLU A 338     3316   4234   3127   -868    170   -436       O  
ATOM   2726  OE1BGLU A 338      14.033   1.707  35.075  0.50 31.91           O  
ANISOU 2726  OE1BGLU A 338     4956   3774   3391   -766     58    160       O  
ATOM   2727  OE2AGLU A 338      17.623   0.662  35.532  0.50 27.85           O  
ANISOU 2727  OE2AGLU A 338     3398   4399   2782   -152   -686    -88       O  
ATOM   2728  OE2BGLU A 338      13.921   3.750  35.862  0.50 31.27           O  
ANISOU 2728  OE2BGLU A 338     3838   4590   3452   -138      8   -904       O  
ATOM   2729  C   GLU A 338      14.820   3.773  31.597  1.00 22.05           C  
ANISOU 2729  C   GLU A 338     2904   2948   2522   -168   -531   -403       C  
ATOM   2730  O   GLU A 338      13.847   4.421  32.019  1.00 25.99           O  
ANISOU 2730  O   GLU A 338     3359   3152   3361    277   -493   -260       O  
ATOM   2731  N   THR A 339      15.706   4.267  30.729  1.00 22.79           N  
ANISOU 2731  N   THR A 339     3234   2970   2455   -189   -438   -408       N  
ATOM   2732  CA  THR A 339      15.703   5.667  30.346  1.00 25.25           C  
ANISOU 2732  CA  THR A 339     3604   3060   2926   -241   -984   -255       C  
ATOM   2733  CB  THR A 339      16.970   6.375  30.846  1.00 28.00           C  
ANISOU 2733  CB  THR A 339     4231   2996   3409   -619  -1172   -480       C  
ATOM   2734  OG1 THR A 339      17.083   6.141  32.248  1.00 32.53           O  
ANISOU 2734  OG1 THR A 339     5204   3614   3539   -769  -1217   -292       O  
ATOM   2735  CG2 THR A 339      16.951   7.865  30.578  1.00 31.08           C  
ANISOU 2735  CG2 THR A 339     4388   3350   4071   -605  -1238    109       C  
ATOM   2736  C   THR A 339      15.591   5.790  28.831  1.00 24.80           C  
ANISOU 2736  C   THR A 339     3504   3058   2860   -248   -863   -474       C  
ATOM   2737  O   THR A 339      16.535   5.467  28.110  1.00 26.80           O  
ANISOU 2737  O   THR A 339     3641   3377   3162   -196   -593   -153       O  
ATOM   2738  N   PRO A 340      14.435   6.258  28.298  1.00 22.76           N  
ANISOU 2738  N   PRO A 340     3128   2799   2722   -336   -556   -416       N  
ATOM   2739  CA  PRO A 340      14.324   6.522  26.869  1.00 22.40           C  
ANISOU 2739  CA  PRO A 340     3153   2592   2764   -282   -612   -164       C  
ATOM   2740  CB  PRO A 340      12.902   7.075  26.718  1.00 23.19           C  
ANISOU 2740  CB  PRO A 340     3238   3018   2552   -150   -774   -351       C  
ATOM   2741  CG  PRO A 340      12.147   6.482  27.894  1.00 24.01           C  
ANISOU 2741  CG  PRO A 340     3282   3100   2741     79   -465   -493       C  
ATOM   2742  CD  PRO A 340      13.168   6.477  29.015  1.00 24.58           C  
ANISOU 2742  CD  PRO A 340     3410   3042   2886    -14   -622   -730       C  
ATOM   2743  C   PRO A 340      15.364   7.566  26.428  1.00 23.19           C  
ANISOU 2743  C   PRO A 340     2984   2605   3221   -447   -706   -354       C  
ATOM   2744  O   PRO A 340      15.584   8.539  27.143  1.00 26.08           O  
ANISOU 2744  O   PRO A 340     3838   2815   3253   -846   -420   -479       O  
ATOM   2745  N   THR A 341      15.963   7.361  25.249  1.00 23.73           N  
ANISOU 2745  N   THR A 341     2865   2799   3350   -242   -463    185       N  
ATOM   2746  CA  THR A 341      16.905   8.321  24.687  1.00 25.72           C  
ANISOU 2746  CA  THR A 341     2706   3431   3633   -274   -673    601       C  
ATOM   2747  CB  THR A 341      18.036   7.628  23.916  1.00 29.89           C  
ANISOU 2747  CB  THR A 341     3142   4340   3872    208   -236    716       C  
ATOM   2748  OG1 THR A 341      17.488   6.831  22.872  1.00 29.40           O  
ANISOU 2748  OG1 THR A 341     2885   4322   3961     56    132    511       O  
ATOM   2749  CG2 THR A 341      18.895   6.762  24.812  1.00 32.37           C  
ANISOU 2749  CG2 THR A 341     3549   4811   3935    148   -178   1192       C  
ATOM   2750  C   THR A 341      16.200   9.360  23.807  1.00 23.93           C  
ANISOU 2750  C   THR A 341     2950   2891   3249   -597   -580    609       C  
ATOM   2751  O   THR A 341      16.789  10.380  23.487  1.00 29.55           O  
ANISOU 2751  O   THR A 341     3691   3299   4234  -1246   -871    600       O  
ATOM   2752  N   LYS A 342      14.972   9.052  23.383  1.00 22.99           N  
ANISOU 2752  N   LYS A 342     2425   3153   3156     26     -5    437       N  
ATOM   2753  CA ALYS A 342      14.124   9.935  22.601  0.30 22.56           C  
ANISOU 2753  CA ALYS A 342     2532   3001   3038   -126    -43    447       C  
ATOM   2754  CA BLYS A 342      14.128   9.941  22.602  0.70 23.34           C  
ANISOU 2754  CA BLYS A 342     2583   3108   3175    -91     -3    434       C  
ATOM   2755  CB ALYS A 342      13.997   9.392  21.174  0.30 22.64           C  
ANISOU 2755  CB ALYS A 342     2642   3105   2855     45    -44    701       C  
ATOM   2756  CB BLYS A 342      13.983   9.407  21.174  0.70 25.30           C  
ANISOU 2756  CB BLYS A 342     3006   3515   3090     45    105    604       C  
ATOM   2757  CG ALYS A 342      15.285   9.424  20.361  0.30 23.15           C  
ANISOU 2757  CG ALYS A 342     2796   3261   2737     41    -14    732       C  
ATOM   2758  CG BLYS A 342      15.272   9.287  20.370  0.70 28.06           C  
ANISOU 2758  CG BLYS A 342     3513   3943   3203    -30    386    277       C  
ATOM   2759  CD ALYS A 342      15.684  10.834  19.995  0.30 22.99           C  
ANISOU 2759  CD ALYS A 342     2875   3273   2586     52   -176    861       C  
ATOM   2760  CD BLYS A 342      15.023   8.585  19.055  0.70 31.77           C  
ANISOU 2760  CD BLYS A 342     4185   4420   3463   -426    232      3       C  
ATOM   2761  CE ALYS A 342      16.977  10.921  19.217  0.30 23.86           C  
ANISOU 2761  CE ALYS A 342     3174   3475   2418     80    -39    827       C  
ATOM   2762  CE BLYS A 342      15.540   9.324  17.836  0.70 31.95           C  
ANISOU 2762  CE BLYS A 342     4542   4377   3220   -330   -158    134       C  
ATOM   2763  NZ ALYS A 342      17.411  12.328  19.081  0.30 25.04           N  
ANISOU 2763  NZ ALYS A 342     3354   3583   2574    -98   -167    773       N  
ATOM   2764  NZ BLYS A 342      14.792   8.960  16.606  0.70 26.66           N  
ANISOU 2764  NZ BLYS A 342     3306   3938   2885   -502     88    362       N  
ATOM   2765  C   LYS A 342      12.762   9.965  23.292  1.00 21.75           C  
ANISOU 2765  C   LYS A 342     2540   2727   2996   -134     10    173       C  
ATOM   2766  O   LYS A 342      12.308   8.937  23.774  1.00 27.28           O  
ANISOU 2766  O   LYS A 342     2810   3090   4466     -4    691    831       O  
ATOM   2767  N   LYS A 343      12.098  11.116  23.315  1.00 17.70           N  
ANISOU 2767  N   LYS A 343     2162   2310   2252   -594   -326    -82       N  
ATOM   2768  CA  LYS A 343      10.860  11.213  24.102  1.00 17.70           C  
ANISOU 2768  CA  LYS A 343     2315   2331   2077   -650   -194   -366       C  
ATOM   2769  CB  LYS A 343      10.601  12.658  24.532  1.00 21.06           C  
ANISOU 2769  CB  LYS A 343     2796   2420   2787   -485   -241   -460       C  
ATOM   2770  CG  LYS A 343      11.598  13.228  25.535  1.00 26.81           C  
ANISOU 2770  CG  LYS A 343     3562   3512   3113   -402   -693   -907       C  
ATOM   2771  CD  LYS A 343      11.207  14.629  25.972  1.00 32.93           C  
ANISOU 2771  CD  LYS A 343     4759   3948   3803    -47   -589  -1321       C  
ATOM   2772  CE  LYS A 343      12.187  15.283  26.920  1.00 40.95           C  
ANISOU 2772  CE  LYS A 343     5388   5670   4497   -439  -1352   -966       C  
ATOM   2773  NZ  LYS A 343      12.230  14.588  28.227  1.00 49.04           N  
ANISOU 2773  NZ  LYS A 343     6809   6732   5092   -308   -534   -390       N  
ATOM   2774  C   LYS A 343       9.631  10.704  23.332  1.00 15.25           C  
ANISOU 2774  C   LYS A 343     2132   1846   1817   -601     11   -261       C  
ATOM   2775  O   LYS A 343       8.635  10.372  23.960  1.00 15.94           O  
ANISOU 2775  O   LYS A 343     2211   2133   1711   -566     82   -125       O  
ATOM   2776  N   PHE A 344       9.683  10.668  21.993  1.00 14.92           N  
ANISOU 2776  N   PHE A 344     1942   1948   1778   -406      0   -373       N  
ATOM   2777  CA  PHE A 344       8.459  10.481  21.190  1.00 13.09           C  
ANISOU 2777  CA  PHE A 344     1896   1553   1521   -103     27   -308       C  
ATOM   2778  CB  PHE A 344       8.156  11.750  20.381  1.00 13.44           C  
ANISOU 2778  CB  PHE A 344     2019   1531   1557   -264      0   -231       C  
ATOM   2779  CG  PHE A 344       8.211  12.978  21.249  1.00 14.02           C  
ANISOU 2779  CG  PHE A 344     2061   1484   1782   -277     85   -267       C  
ATOM   2780  CD1 PHE A 344       7.251  13.182  22.219  1.00 13.91           C  
ANISOU 2780  CD1 PHE A 344     2178   1370   1735   -125     84   -178       C  
ATOM   2781  CE1 PHE A 344       7.329  14.267  23.064  1.00 15.12           C  
ANISOU 2781  CE1 PHE A 344     2358   1518   1868   -309    176   -301       C  
ATOM   2782  CZ  PHE A 344       8.388  15.153  22.976  1.00 15.60           C  
ANISOU 2782  CZ  PHE A 344     2185   1704   2038   -326     78   -261       C  
ATOM   2783  CD2 PHE A 344       9.267  13.867  21.173  1.00 15.21           C  
ANISOU 2783  CD2 PHE A 344     1901   1857   2019   -330    122   -176       C  
ATOM   2784  CE2 PHE A 344       9.338  14.967  22.011  1.00 16.68           C  
ANISOU 2784  CE2 PHE A 344     2164   1833   2338   -622    241   -223       C  
ATOM   2785  C   PHE A 344       8.534   9.231  20.317  1.00 12.90           C  
ANISOU 2785  C   PHE A 344     1722   1455   1724   -151   -129   -317       C  
ATOM   2786  O   PHE A 344       7.754   9.117  19.391  1.00 12.95           O  
ANISOU 2786  O   PHE A 344     1790   1470   1659     15   -135   -195       O  
ATOM   2787  N   ALA A 345       9.422   8.301  20.692  1.00 13.43           N  
ANISOU 2787  N   ALA A 345     1879   1574   1650    -46   -187   -304       N  
ATOM   2788  CA  ALA A 345       9.703   7.084  19.974  1.00 13.58           C  
ANISOU 2788  CA  ALA A 345     1798   1529   1832   -207      9   -314       C  
ATOM   2789  CB  ALA A 345      11.199   6.860  19.881  1.00 15.57           C  
ANISOU 2789  CB  ALA A 345     1878   1792   2244   -116     56   -313       C  
ATOM   2790  C   ALA A 345       9.040   5.898  20.666  1.00 12.98           C  
ANISOU 2790  C   ALA A 345     1590   1553   1786    -80     57   -250       C  
ATOM   2791  O   ALA A 345       8.564   6.014  21.790  1.00 14.44           O  
ANISOU 2791  O   ALA A 345     1968   1740   1776   -136    145   -395       O  
ATOM   2792  N   PRO A 346       9.020   4.718  20.026  1.00 13.27           N  
ANISOU 2792  N   PRO A 346     1760   1517   1763   -102     10   -250       N  
ATOM   2793  CA  PRO A 346       8.515   3.521  20.684  1.00 12.08           C  
ANISOU 2793  CA  PRO A 346     1426   1629   1535   -102     68   -161       C  
ATOM   2794  CB  PRO A 346       8.753   2.420  19.636  1.00 13.35           C  
ANISOU 2794  CB  PRO A 346     1771   1592   1708    -20    -45   -224       C  
ATOM   2795  CG  PRO A 346       8.693   3.165  18.314  1.00 12.72           C  
ANISOU 2795  CG  PRO A 346     1820   1435   1576    153     -4   -357       C  
ATOM   2796  CD  PRO A 346       9.434   4.449  18.633  1.00 13.10           C  
ANISOU 2796  CD  PRO A 346     1694   1502   1780     18     86   -144       C  
ATOM   2797  C   PRO A 346       9.256   3.215  21.989  1.00 13.42           C  
ANISOU 2797  C   PRO A 346     1723   1711   1662      0    -53   -229       C  
ATOM   2798  O   PRO A 346      10.467   3.443  22.094  1.00 13.62           O  
ANISOU 2798  O   PRO A 346     1781   1660   1734    -72    -69   -138       O  
ATOM   2799  N   ASP A 347       8.527   2.613  22.921  1.00 13.61           N  
ANISOU 2799  N   ASP A 347     1682   1721   1767    -63   -190      1       N  
ATOM   2800  CA  ASP A 347       9.144   2.087  24.117  1.00 13.96           C  
ANISOU 2800  CA  ASP A 347     1509   1970   1823     94   -311    -53       C  
ATOM   2801  CB  ASP A 347       8.083   1.627  25.111  1.00 15.78           C  
ANISOU 2801  CB  ASP A 347     1952   2128   1915     66    -92     78       C  
ATOM   2802  CG  ASP A 347       7.485   2.767  25.930  1.00 19.36           C  
ANISOU 2802  CG  ASP A 347     2268   2445   2639    321    525     22       C  
ATOM   2803  OD1 ASP A 347       8.123   3.853  26.045  1.00 21.64           O  
ANISOU 2803  OD1 ASP A 347     3387   2340   2496    283    580    -58       O  
ATOM   2804  OD2 ASP A 347       6.493   2.517  26.550  1.00 24.73           O  
ANISOU 2804  OD2 ASP A 347     2126   3511   3757    683    679    421       O  
ATOM   2805  C   ASP A 347      10.057   0.909  23.751  1.00 13.13           C  
ANISOU 2805  C   ASP A 347     1679   1758   1550    -63   -166   -204       C  
ATOM   2806  O   ASP A 347       9.766   0.125  22.849  1.00 15.21           O  
ANISOU 2806  O   ASP A 347     1920   1846   2013    115   -444   -470       O  
ATOM   2807  N   GLN A 348      11.180   0.809  24.449  1.00 12.94           N  
ANISOU 2807  N   GLN A 348     1504   1688   1724   -118    -72    -82       N  
ATOM   2808  CA  GLN A 348      12.176  -0.223  24.190  1.00 13.25           C  
ANISOU 2808  CA  GLN A 348     1571   1875   1589     12   -233   -222       C  
ATOM   2809  CB  GLN A 348      13.573   0.395  24.048  1.00 14.60           C  
ANISOU 2809  CB  GLN A 348     1580   2235   1729     22   -150    -16       C  
ATOM   2810  CG  GLN A 348      14.640  -0.650  23.738  1.00 15.83           C  
ANISOU 2810  CG  GLN A 348     1650   2453   1910     40     93     10       C  
ATOM   2811  CD  GLN A 348      14.580  -1.075  22.290  1.00 17.02           C  
ANISOU 2811  CD  GLN A 348     2004   2559   1903     34    101     82       C  
ATOM   2812  OE1 GLN A 348      14.947  -0.302  21.386  1.00 18.62           O  
ANISOU 2812  OE1 GLN A 348     2150   2798   2124    108    202    264       O  
ATOM   2813  NE2 GLN A 348      14.122  -2.290  22.032  1.00 18.11           N  
ANISOU 2813  NE2 GLN A 348     2006   2603   2272    408    201   -126       N  
ATOM   2814  C   GLN A 348      12.189  -1.247  25.333  1.00 13.43           C  
ANISOU 2814  C   GLN A 348     1722   1849   1530    -42   -262   -280       C  
ATOM   2815  O   GLN A 348      12.391  -0.891  26.503  1.00 14.46           O  
ANISOU 2815  O   GLN A 348     1930   1957   1606   -202   -337   -353       O  
ATOM   2816  N   LEU A 349      12.034  -2.520  24.957  1.00 13.64           N  
ANISOU 2816  N   LEU A 349     1740   1893   1549     40   -209   -388       N  
ATOM   2817  CA  LEU A 349      12.259  -3.668  25.812  1.00 13.65           C  
ANISOU 2817  CA  LEU A 349     1798   1894   1494     63   -212   -326       C  
ATOM   2818  CB  LEU A 349      11.025  -4.582  25.854  1.00 13.70           C  
ANISOU 2818  CB  LEU A 349     1827   1671   1707     69   -149   -371       C  
ATOM   2819  CG  LEU A 349       9.683  -3.922  26.170  1.00 15.09           C  
ANISOU 2819  CG  LEU A 349     1626   2058   2050   -155     -3   -455       C  
ATOM   2820  CD1 LEU A 349       8.523  -4.906  26.053  1.00 16.32           C  
ANISOU 2820  CD1 LEU A 349     1809   2033   2359   -166     63   -478       C  
ATOM   2821  CD2 LEU A 349       9.683  -3.270  27.545  1.00 17.41           C  
ANISOU 2821  CD2 LEU A 349     1993   2208   2413    -84    152   -838       C  
ATOM   2822  C   LEU A 349      13.470  -4.437  25.279  1.00 14.24           C  
ANISOU 2822  C   LEU A 349     1850   1895   1662     75   -254   -315       C  
ATOM   2823  O   LEU A 349      13.870  -4.267  24.133  1.00 16.97           O  
ANISOU 2823  O   LEU A 349     2455   2241   1749    559    -19   -160       O  
ATOM   2824  N   ALA A 350      14.055  -5.275  26.130  1.00 14.22           N  
ANISOU 2824  N   ALA A 350     1837   2078   1486    -51   -432   -345       N  
ATOM   2825  CA  ALA A 350      15.093  -6.178  25.682  1.00 14.05           C  
ANISOU 2825  CA  ALA A 350     1658   1973   1705   -209   -290   -262       C  
ATOM   2826  CB  ALA A 350      15.993  -6.567  26.828  1.00 15.34           C  
ANISOU 2826  CB  ALA A 350     2117   2120   1589   -194   -349   -201       C  
ATOM   2827  C   ALA A 350      14.461  -7.405  25.015  1.00 13.15           C  
ANISOU 2827  C   ALA A 350     1629   1989   1375   -123   -363   -203       C  
ATOM   2828  O   ALA A 350      13.300  -7.718  25.244  1.00 13.85           O  
ANISOU 2828  O   ALA A 350     1588   2054   1617   -104   -330    -52       O  
ATOM   2829  N   GLY A 351      15.257  -8.092  24.191  1.00 13.94           N  
ANISOU 2829  N   GLY A 351     1720   2065   1512   -197   -220   -205       N  
ATOM   2830  CA  GLY A 351      14.859  -9.382  23.632  1.00 13.11           C  
ANISOU 2830  CA  GLY A 351     1531   1889   1561    118   -283   -152       C  
ATOM   2831  C   GLY A 351      15.276 -10.508  24.549  1.00 13.26           C  
ANISOU 2831  C   GLY A 351     1570   1912   1554    183    -68    -62       C  
ATOM   2832  O   GLY A 351      16.467 -10.740  24.719  1.00 14.51           O  
ANISOU 2832  O   GLY A 351     1569   2166   1776     77   -156   -175       O  
ATOM   2833  N   ILE A 352      14.301 -11.190  25.144  1.00 12.81           N  
ANISOU 2833  N   ILE A 352     1516   1813   1536    160   -186     24       N  
ATOM   2834  CA  ILE A 352      14.589 -12.269  26.094  1.00 13.66           C  
ANISOU 2834  CA  ILE A 352     1789   1871   1529    330   -148      0       C  
ATOM   2835  CB  ILE A 352      13.466 -12.453  27.138  1.00 13.69           C  
ANISOU 2835  CB  ILE A 352     1689   1989   1522     78   -243    -41       C  
ATOM   2836  CG1 ILE A 352      13.263 -11.170  27.956  1.00 13.99           C  
ANISOU 2836  CG1 ILE A 352     1600   2097   1619    232   -190    -23       C  
ATOM   2837  CG2 ILE A 352      13.789 -13.660  28.026  1.00 14.31           C  
ANISOU 2837  CG2 ILE A 352     1931   1966   1541    238   -154    -97       C  
ATOM   2838  CD1 ILE A 352      12.083 -11.202  28.911  1.00 14.34           C  
ANISOU 2838  CD1 ILE A 352     1654   2132   1660    389   -183    -16       C  
ATOM   2839  C   ILE A 352      14.854 -13.551  25.306  1.00 13.68           C  
ANISOU 2839  C   ILE A 352     1850   1873   1472    207   -173     16       C  
ATOM   2840  O   ILE A 352      13.995 -13.997  24.550  1.00 14.77           O  
ANISOU 2840  O   ILE A 352     1913   1911   1789    101   -284    111       O  
ATOM   2841  N   ILE A 353      16.019 -14.150  25.550  1.00 14.85           N  
ANISOU 2841  N   ILE A 353     1878   2109   1655    300   -304   -133       N  
ATOM   2842  CA  ILE A 353      16.448 -15.355  24.841  1.00 15.02           C  
ANISOU 2842  CA  ILE A 353     1982   2169   1555    511   -250    -82       C  
ATOM   2843  CB  ILE A 353      17.811 -15.161  24.152  1.00 17.90           C  
ANISOU 2843  CB  ILE A 353     2130   2705   1965    298     11    -35       C  
ATOM   2844  CG1 ILE A 353      18.960 -14.891  25.132  1.00 18.95           C  
ANISOU 2844  CG1 ILE A 353     2177   3013   2008    520    -25    346       C  
ATOM   2845  CG2 ILE A 353      17.717 -14.073  23.097  1.00 16.38           C  
ANISOU 2845  CG2 ILE A 353     1736   2789   1698    417    115    -71       C  
ATOM   2846  CD1 ILE A 353      20.314 -14.994  24.488  1.00 19.87           C  
ANISOU 2846  CD1 ILE A 353     2301   3218   2030    436    127    443       C  
ATOM   2847  C   ILE A 353      16.466 -16.586  25.753  1.00 14.90           C  
ANISOU 2847  C   ILE A 353     1996   2196   1468    429   -159    -97       C  
ATOM   2848  O   ILE A 353      16.613 -17.714  25.251  1.00 18.09           O  
ANISOU 2848  O   ILE A 353     2723   2161   1986    554   -406   -152       O  
ATOM   2849  N   GLY A 354      16.360 -16.370  27.066  1.00 15.17           N  
ANISOU 2849  N   GLY A 354     2218   2038   1507    586   -245   -100       N  
ATOM   2850  CA  GLY A 354      16.336 -17.440  28.030  1.00 15.41           C  
ANISOU 2850  CA  GLY A 354     2314   2045   1494    498   -324    -78       C  
ATOM   2851  C   GLY A 354      15.610 -17.027  29.286  1.00 15.34           C  
ANISOU 2851  C   GLY A 354     1908   2132   1788    361   -211   -123       C  
ATOM   2852  O   GLY A 354      15.662 -15.870  29.672  1.00 14.76           O  
ANISOU 2852  O   GLY A 354     1935   2012   1659    273   -122     27       O  
ATOM   2853  N   LEU A 355      14.951 -18.000  29.922  1.00 14.86           N  
ANISOU 2853  N   LEU A 355     1921   1950   1775    209   -166   -364       N  
ATOM   2854  CA  LEU A 355      14.235 -17.775  31.151  1.00 15.88           C  
ANISOU 2854  CA  LEU A 355     2121   2197   1715    192   -208   -262       C  
ATOM   2855  CB  LEU A 355      12.763 -17.603  30.764  1.00 20.42           C  
ANISOU 2855  CB  LEU A 355     2009   3142   2606    112   -176   -157       C  
ATOM   2856  CG  LEU A 355      11.831 -17.039  31.815  1.00 21.52           C  
ANISOU 2856  CG  LEU A 355     2163   3192   2821    213   -463   -434       C  
ATOM   2857  CD1 LEU A 355      12.242 -15.622  32.217  1.00 22.41           C  
ANISOU 2857  CD1 LEU A 355     2236   3120   3157    758   -848   -935       C  
ATOM   2858  CD2 LEU A 355      10.405 -17.091  31.307  1.00 18.33           C  
ANISOU 2858  CD2 LEU A 355     1927   2537   2500    447   -315     39       C  
ATOM   2859  C   LEU A 355      14.444 -18.998  32.038  1.00 17.48           C  
ANISOU 2859  C   LEU A 355     2601   2371   1667    258    -75   -247       C  
ATOM   2860  O   LEU A 355      14.336 -20.107  31.544  1.00 19.16           O  
ANISOU 2860  O   LEU A 355     2868   2306   2105    -24     32   -268       O  
ATOM   2861  N   GLU A 356      14.742 -18.768  33.325  1.00 16.42           N  
ANISOU 2861  N   GLU A 356     2364   2311   1563     99    -42   -139       N  
ATOM   2862  CA  GLU A 356      14.797 -19.847  34.294  1.00 18.43           C  
ANISOU 2862  CA  GLU A 356     2792   2489   1720    130     43     46       C  
ATOM   2863  CB  GLU A 356      16.229 -20.231  34.669  1.00 21.95           C  
ANISOU 2863  CB  GLU A 356     3013   2964   2363    415    -84     58       C  
ATOM   2864  CG  GLU A 356      17.038 -20.693  33.488  1.00 25.17           C  
ANISOU 2864  CG  GLU A 356     3484   3329   2747    652     26     57       C  
ATOM   2865  CD  GLU A 356      18.398 -21.294  33.779  1.00 28.38           C  
ANISOU 2865  CD  GLU A 356     3138   3888   3757    575    306   -144       C  
ATOM   2866  OE1 GLU A 356      18.671 -21.640  34.952  1.00 33.18           O  
ANISOU 2866  OE1 GLU A 356     3909   4261   4435   1116   -575    217       O  
ATOM   2867  OE2 GLU A 356      19.177 -21.423  32.810  1.00 34.92           O  
ANISOU 2867  OE2 GLU A 356     3898   4838   4531    593    933   -772       O  
ATOM   2868  C   GLU A 356      14.015 -19.418  35.530  1.00 18.42           C  
ANISOU 2868  C   GLU A 356     3014   2242   1744    113    123    104       C  
ATOM   2869  O   GLU A 356      14.242 -18.329  36.069  1.00 20.75           O  
ANISOU 2869  O   GLU A 356     3632   2586   1663   -166    -80   -135       O  
ATOM   2870  N   ILE A 357      13.123 -20.302  35.984  1.00 18.14           N  
ANISOU 2870  N   ILE A 357     2650   2303   1938    214    124    212       N  
ATOM   2871  CA  ILE A 357      12.242 -20.012  37.092  1.00 18.10           C  
ANISOU 2871  CA  ILE A 357     2784   2369   1723    294     60      1       C  
ATOM   2872  CB  ILE A 357      10.755 -20.127  36.681  1.00 18.87           C  
ANISOU 2872  CB  ILE A 357     2788   2609   1770    261     50    -90       C  
ATOM   2873  CG1 ILE A 357      10.406 -19.437  35.359  1.00 21.54           C  
ANISOU 2873  CG1 ILE A 357     3710   2919   1556    406    650    -65       C  
ATOM   2874  CG2 ILE A 357       9.859 -19.662  37.816  1.00 19.01           C  
ANISOU 2874  CG2 ILE A 357     2642   2793   1786    236    155     52       C  
ATOM   2875  CD1 ILE A 357      10.477 -17.965  35.367  1.00 22.38           C  
ANISOU 2875  CD1 ILE A 357     3614   3052   1838    202    667    316       C  
ATOM   2876  C   ILE A 357      12.551 -20.985  38.234  1.00 18.37           C  
ANISOU 2876  C   ILE A 357     2762   2558   1657    417     15     68       C  
ATOM   2877  O   ILE A 357      12.718 -22.179  38.020  1.00 18.81           O  
ANISOU 2877  O   ILE A 357     2692   2531   1924    449   -128    184       O  
ATOM   2878  N   LYS A 358      12.622 -20.452  39.455  1.00 17.36           N  
ANISOU 2878  N   LYS A 358     2680   2193   1721    328   -101    142       N  
ATOM   2879  CA  LYS A 358      12.673 -21.249  40.668  1.00 18.77           C  
ANISOU 2879  CA  LYS A 358     2889   2648   1593    385   -385    153       C  
ATOM   2880  CB  LYS A 358      13.885 -20.851  41.519  1.00 20.55           C  
ANISOU 2880  CB  LYS A 358     2986   2741   2081    209   -642    265       C  
ATOM   2881  CG  LYS A 358      13.891 -21.406  42.942  1.00 24.00           C  
ANISOU 2881  CG  LYS A 358     3341   3487   2291    292   -584    614       C  
ATOM   2882  CD  LYS A 358      15.080 -20.916  43.733  1.00 26.44           C  
ANISOU 2882  CD  LYS A 358     3696   4108   2242    383   -855    237       C  
ATOM   2883  CE  LYS A 358      15.184 -21.516  45.119  1.00 31.00           C  
ANISOU 2883  CE  LYS A 358     4333   4849   2597    386  -1586    555       C  
ATOM   2884  NZ  LYS A 358      16.515 -21.272  45.714  1.00 33.36           N  
ANISOU 2884  NZ  LYS A 358     4244   5007   3423    179  -1250     65       N  
ATOM   2885  C   LYS A 358      11.378 -21.002  41.435  1.00 18.78           C  
ANISOU 2885  C   LYS A 358     2825   2535   1773    267   -347    178       C  
ATOM   2886  O   LYS A 358      10.988 -19.860  41.618  1.00 19.25           O  
ANISOU 2886  O   LYS A 358     3215   2479   1621    230   -161    -45       O  
ATOM   2887  N   VAL A 359      10.723 -22.088  41.860  1.00 19.16           N  
ANISOU 2887  N   VAL A 359     2975   2671   1633    225   -193    141       N  
ATOM   2888  CA  VAL A 359       9.582 -22.000  42.766  1.00 19.27           C  
ANISOU 2888  CA  VAL A 359     3009   2654   1658    306   -192    566       C  
ATOM   2889  CB  VAL A 359       8.238 -22.319  42.089  1.00 19.46           C  
ANISOU 2889  CB  VAL A 359     2994   2759   1640    160   -138    191       C  
ATOM   2890  CG1 VAL A 359       7.104 -22.238  43.102  1.00 19.77           C  
ANISOU 2890  CG1 VAL A 359     3303   2449   1758    317    -17    492       C  
ATOM   2891  CG2 VAL A 359       7.951 -21.386  40.925  1.00 20.47           C  
ANISOU 2891  CG2 VAL A 359     3086   2650   2041    295   -456    138       C  
ATOM   2892  C   VAL A 359       9.848 -22.948  43.932  1.00 19.44           C  
ANISOU 2892  C   VAL A 359     3061   2689   1632    564   -241    524       C  
ATOM   2893  O   VAL A 359       9.968 -24.146  43.723  1.00 21.42           O  
ANISOU 2893  O   VAL A 359     3164   2727   2247    350   -352    504       O  
ATOM   2894  N   ASP A 360       9.964 -22.387  45.139  1.00 20.02           N  
ANISOU 2894  N   ASP A 360     3198   2688   1721    635    -70    467       N  
ATOM   2895  CA  ASP A 360      10.270 -23.177  46.327  1.00 21.96           C  
ANISOU 2895  CA  ASP A 360     3196   2951   2196    899   -306    657       C  
ATOM   2896  CB  ASP A 360       9.051 -24.026  46.721  1.00 24.35           C  
ANISOU 2896  CB  ASP A 360     3702   3035   2511    629   -204    449       C  
ATOM   2897  CG  ASP A 360       7.816 -23.207  47.068  1.00 23.30           C  
ANISOU 2897  CG  ASP A 360     3664   2711   2477    402    -15    517       C  
ATOM   2898  OD1 ASP A 360       7.973 -22.010  47.330  1.00 24.17           O  
ANISOU 2898  OD1 ASP A 360     3647   2636   2899    452    472    377       O  
ATOM   2899  OD2 ASP A 360       6.706 -23.776  47.103  1.00 26.42           O  
ANISOU 2899  OD2 ASP A 360     3690   3539   2807    159    186    707       O  
ATOM   2900  C   ASP A 360      11.600 -23.892  46.027  1.00 24.24           C  
ANISOU 2900  C   ASP A 360     3413   3453   2340   1102   -190    547       C  
ATOM   2901  O   ASP A 360      12.553 -23.210  45.667  1.00 26.29           O  
ANISOU 2901  O   ASP A 360     3301   4027   2660    600   -324    541       O  
ATOM   2902  N   SER A 361      11.665 -25.226  46.143  1.00 26.74           N  
ANISOU 2902  N   SER A 361     3962   3590   2605   1164   -267    918       N  
ATOM   2903  CA ASER A 361      12.934 -25.948  46.007  0.50 27.57           C  
ANISOU 2903  CA ASER A 361     3816   3568   3092   1162   -273    924       C  
ATOM   2904  CA BSER A 361      12.929 -25.955  46.008  0.50 27.91           C  
ANISOU 2904  CA BSER A 361     3726   3871   3006   1176   -319    953       C  
ATOM   2905  CB ASER A 361      12.998 -27.121  46.956  0.50 28.91           C  
ANISOU 2905  CB ASER A 361     4089   3671   3222   1188   -464   1038       C  
ATOM   2906  CB BSER A 361      12.969 -27.137  46.947  0.50 29.33           C  
ANISOU 2906  CB BSER A 361     3916   4284   2945   1222   -575   1179       C  
ATOM   2907  OG ASER A 361      12.070 -28.130  46.588  0.50 30.89           O  
ANISOU 2907  OG ASER A 361     4407   3269   4058   1139   -272    919       O  
ATOM   2908  OG BSER A 361      12.977 -26.711  48.302  0.50 31.79           O  
ANISOU 2908  OG BSER A 361     4124   4887   3066   1170   -531    997       O  
ATOM   2909  C   SER A 361      13.172 -26.406  44.561  1.00 27.87           C  
ANISOU 2909  C   SER A 361     4079   3504   3004   1414   -314   1034       C  
ATOM   2910  O   SER A 361      14.192 -27.022  44.275  1.00 31.08           O  
ANISOU 2910  O   SER A 361     4659   4212   2936   1812   -311    431       O  
ATOM   2911  N   ASP A 362      12.244 -26.086  43.655  1.00 26.10           N  
ANISOU 2911  N   ASP A 362     3714   3385   2817   1145    -40    638       N  
ATOM   2912  CA  ASP A 362      12.285 -26.508  42.269  1.00 26.50           C  
ANISOU 2912  CA  ASP A 362     4257   2726   3083    854    228    543       C  
ATOM   2913  CB  ASP A 362      10.855 -26.767  41.818  1.00 27.21           C  
ANISOU 2913  CB  ASP A 362     4201   2938   3197    647    413    465       C  
ATOM   2914  CG  ASP A 362      10.693 -27.640  40.595  1.00 30.13           C  
ANISOU 2914  CG  ASP A 362     4758   3025   3665    802    661     85       C  
ATOM   2915  OD1 ASP A 362      11.647 -27.702  39.775  1.00 34.42           O  
ANISOU 2915  OD1 ASP A 362     4784   3906   4388    863    965   -168       O  
ATOM   2916  OD2 ASP A 362       9.587 -28.234  40.468  1.00 31.47           O  
ANISOU 2916  OD2 ASP A 362     4572   3680   3704    946    -79   -326       O  
ATOM   2917  C   ASP A 362      12.975 -25.430  41.422  1.00 23.12           C  
ANISOU 2917  C   ASP A 362     3553   2697   2534    941     39    393       C  
ATOM   2918  O   ASP A 362      12.430 -24.353  41.257  1.00 23.10           O  
ANISOU 2918  O   ASP A 362     3415   2812   2546    955   -197    434       O  
ATOM   2919  N   VAL A 363      14.162 -25.748  40.881  1.00 22.23           N  
ANISOU 2919  N   VAL A 363     3216   2893   2336    800   -253    339       N  
ATOM   2920  CA  VAL A 363      15.043 -24.757  40.273  1.00 23.23           C  
ANISOU 2920  CA  VAL A 363     3104   3353   2369    644   -260    131       C  
ATOM   2921  CB  VAL A 363      16.414 -24.695  40.976  1.00 27.71           C  
ANISOU 2921  CB  VAL A 363     3586   4293   2647    650   -684   -261       C  
ATOM   2922  CG1 VAL A 363      16.265 -24.406  42.470  1.00 29.12           C  
ANISOU 2922  CG1 VAL A 363     3830   4572   2659    587   -930   -208       C  
ATOM   2923  CG2 VAL A 363      17.223 -25.955  40.742  1.00 31.30           C  
ANISOU 2923  CG2 VAL A 363     3689   4604   3599    755   -948   -301       C  
ATOM   2924  C   VAL A 363      15.211 -25.044  38.776  1.00 20.77           C  
ANISOU 2924  C   VAL A 363     2336   3250   2305    464   -261    120       C  
ATOM   2925  O   VAL A 363      15.047 -26.159  38.298  1.00 23.26           O  
ANISOU 2925  O   VAL A 363     2833   3320   2685    518   -414    -46       O  
ATOM   2926  N   GLY A 364      15.550 -23.991  38.035  1.00 20.52           N  
ANISOU 2926  N   GLY A 364     2277   3212   2306    418   -340     51       N  
ATOM   2927  CA  GLY A 364      15.967 -24.103  36.645  1.00 21.81           C  
ANISOU 2927  CA  GLY A 364     2269   3540   2477    484      6   -280       C  
ATOM   2928  C   GLY A 364      14.843 -24.416  35.668  1.00 19.73           C  
ANISOU 2928  C   GLY A 364     1939   3054   2502    354     82    -59       C  
ATOM   2929  O   GLY A 364      15.102 -24.881  34.560  1.00 20.48           O  
ANISOU 2929  O   GLY A 364     2218   3021   2542    676     11    -99       O  
ATOM   2930  N   ILE A 365      13.600 -24.132  36.048  1.00 17.09           N  
ANISOU 2930  N   ILE A 365     1830   2899   1761    341    -95     20       N  
ATOM   2931  CA  ILE A 365      12.452 -24.447  35.184  1.00 15.99           C  
ANISOU 2931  CA  ILE A 365     1817   2465   1792    219    -77     10       C  
ATOM   2932  CB  ILE A 365      11.123 -24.274  35.939  1.00 17.08           C  
ANISOU 2932  CB  ILE A 365     1929   2665   1895    289     -8    196       C  
ATOM   2933  CG1 ILE A 365      11.098 -25.060  37.252  1.00 18.71           C  
ANISOU 2933  CG1 ILE A 365     2233   2942   1933    468    -62    317       C  
ATOM   2934  CG2 ILE A 365       9.958 -24.648  35.033  1.00 17.60           C  
ANISOU 2934  CG2 ILE A 365     1773   2652   2261    197    -65    232       C  
ATOM   2935  CD1 ILE A 365      10.105 -24.537  38.249  1.00 20.11           C  
ANISOU 2935  CD1 ILE A 365     2043   3467   2130    444    119    542       C  
ATOM   2936  C   ILE A 365      12.518 -23.545  33.942  1.00 16.34           C  
ANISOU 2936  C   ILE A 365     1984   2641   1582    285     -5    -30       C  
ATOM   2937  O   ILE A 365      12.719 -22.330  34.056  1.00 18.22           O  
ANISOU 2937  O   ILE A 365     2405   2738   1776    246    -63    -97       O  
ATOM   2938  N   PHE A 366      12.311 -24.155  32.775  1.00 15.73           N  
ANISOU 2938  N   PHE A 366     2054   2151   1770    373   -100    -86       N  
ATOM   2939  CA  PHE A 366      12.352 -23.526  31.433  1.00 16.43           C  
ANISOU 2939  CA  PHE A 366     2159   2364   1719    325    -34    -68       C  
ATOM   2940  CB  PHE A 366      11.609 -22.189  31.340  1.00 15.37           C  
ANISOU 2940  CB  PHE A 366     1875   2326   1637    256   -150    -68       C  
ATOM   2941  CG  PHE A 366      10.128 -22.227  31.634  1.00 15.59           C  
ANISOU 2941  CG  PHE A 366     1868   2414   1642    235   -111   -104       C  
ATOM   2942  CD1 PHE A 366       9.376 -23.383  31.468  1.00 15.60           C  
ANISOU 2942  CD1 PHE A 366     1890   2384   1652    226      3    -28       C  
ATOM   2943  CE1 PHE A 366       8.008 -23.384  31.719  1.00 15.36           C  
ANISOU 2943  CE1 PHE A 366     1955   2411   1470    303    147   -172       C  
ATOM   2944  CZ  PHE A 366       7.377 -22.239  32.135  1.00 15.71           C  
ANISOU 2944  CZ  PHE A 366     1703   2388   1877    291     -1    -55       C  
ATOM   2945  CD2 PHE A 366       9.470 -21.080  32.042  1.00 16.30           C  
ANISOU 2945  CD2 PHE A 366     1969   2528   1693    400    -42      0       C  
ATOM   2946  CE2 PHE A 366       8.108 -21.094  32.309  1.00 16.34           C  
ANISOU 2946  CE2 PHE A 366     1954   2379   1876    324   -136      6       C  
ATOM   2947  C   PHE A 366      13.780 -23.317  30.919  1.00 16.14           C  
ANISOU 2947  C   PHE A 366     1948   2304   1879    464   -211   -142       C  
ATOM   2948  O   PHE A 366      13.947 -22.738  29.847  1.00 17.48           O  
ANISOU 2948  O   PHE A 366     2330   2433   1878    355   -159    -20       O  
ATOM   2949  N   ARG A 367      14.798 -23.844  31.606  1.00 17.67           N  
ANISOU 2949  N   ARG A 367     1935   2880   1895    511   -212    -80       N  
ATOM   2950  CA  ARG A 367      16.183 -23.697  31.133  1.00 20.14           C  
ANISOU 2950  CA  ARG A 367     1981   3358   2312    415   -115    -43       C  
ATOM   2951  CB  ARG A 367      17.174 -24.277  32.155  1.00 23.41           C  
ANISOU 2951  CB  ARG A 367     2005   4098   2789    717   -339   -184       C  
ATOM   2952  CG  ARG A 367      17.153 -25.786  32.279  1.00 29.75           C  
ANISOU 2952  CG  ARG A 367     3021   4425   3858    858   -979   -329       C  
ATOM   2953  CD  ARG A 367      17.753 -26.322  33.578  1.00 36.84           C  
ANISOU 2953  CD  ARG A 367     4435   5447   4116   1038  -1550   -473       C  
ATOM   2954  NE  ARG A 367      19.191 -26.473  33.484  1.00 42.79           N  
ANISOU 2954  NE  ARG A 367     4836   6443   4979   1776  -1306   -729       N  
ATOM   2955  CZ  ARG A 367      19.816 -27.609  33.156  1.00 52.03           C  
ANISOU 2955  CZ  ARG A 367     6478   6074   7217   1582  -1441  -1292       C  
ATOM   2956  NH1 ARG A 367      19.162 -28.578  32.536  1.00 61.13           N  
ANISOU 2956  NH1 ARG A 367     8474   6787   7963    544  -1749  -1643       N  
ATOM   2957  NH2 ARG A 367      21.090 -27.783  33.465  1.00 57.78           N  
ANISOU 2957  NH2 ARG A 367     6282   7503   8169   2274   -791  -1103       N  
ATOM   2958  C   ARG A 367      16.374 -24.310  29.729  1.00 19.46           C  
ANISOU 2958  C   ARG A 367     1912   3281   2200    449    131    128       C  
ATOM   2959  O   ARG A 367      17.254 -23.877  29.004  1.00 21.49           O  
ANISOU 2959  O   ARG A 367     2402   3418   2344    287    514    -49       O  
ATOM   2960  N   GLU A 368      15.533 -25.268  29.317  1.00 17.92           N  
ANISOU 2960  N   GLU A 368     1880   2832   2096    710     61    252       N  
ATOM   2961  CA  GLU A 368      15.702 -25.920  28.033  1.00 21.26           C  
ANISOU 2961  CA  GLU A 368     2636   3254   2185    775   -175    128       C  
ATOM   2962  CB  GLU A 368      15.264 -27.383  28.107  1.00 22.66           C  
ANISOU 2962  CB  GLU A 368     3078   3426   2103    679   -139    144       C  
ATOM   2963  CG  GLU A 368      16.099 -28.214  29.074  1.00 27.64           C  
ANISOU 2963  CG  GLU A 368     3925   3992   2585   1155   -315    322       C  
ATOM   2964  CD  GLU A 368      17.612 -28.251  28.874  1.00 33.29           C  
ANISOU 2964  CD  GLU A 368     3938   5317   3392   1543   -340    456       C  
ATOM   2965  OE1 GLU A 368      18.083 -28.123  27.721  1.00 35.94           O  
ANISOU 2965  OE1 GLU A 368     3639   5782   4232   1785    230    893       O  
ATOM   2966  OE2 GLU A 368      18.328 -28.422  29.884  1.00 39.71           O  
ANISOU 2966  OE2 GLU A 368     4232   6818   4034   1440   -963     -3       O  
ATOM   2967  C   GLU A 368      14.951 -25.192  26.907  1.00 18.02           C  
ANISOU 2967  C   GLU A 368     2626   2378   1840    648    -36    -97       C  
ATOM   2968  O   GLU A 368      14.985 -25.647  25.748  1.00 20.93           O  
ANISOU 2968  O   GLU A 368     3309   2900   1741   1156     -3   -129       O  
ATOM   2969  N   LEU A 369      14.293 -24.062  27.208  1.00 15.86           N  
ANISOU 2969  N   LEU A 369     2001   2317   1707    475   -105   -159       N  
ATOM   2970  CA  LEU A 369      13.570 -23.325  26.164  1.00 15.01           C  
ANISOU 2970  CA  LEU A 369     1915   1890   1896    265   -190   -188       C  
ATOM   2971  CB  LEU A 369      12.361 -22.621  26.777  1.00 15.07           C  
ANISOU 2971  CB  LEU A 369     2014   1894   1816    261     16    -48       C  
ATOM   2972  CG  LEU A 369      11.303 -23.520  27.414  1.00 14.82           C  
ANISOU 2972  CG  LEU A 369     1949   1887   1793    149   -124     11       C  
ATOM   2973  CD1 LEU A 369      10.091 -22.705  27.848  1.00 15.81           C  
ANISOU 2973  CD1 LEU A 369     2071   1927   2008    308   -229    181       C  
ATOM   2974  CD2 LEU A 369      10.906 -24.681  26.497  1.00 15.88           C  
ANISOU 2974  CD2 LEU A 369     2137   2083   1813    202   -159    -62       C  
ATOM   2975  C   LEU A 369      14.477 -22.293  25.505  1.00 15.14           C  
ANISOU 2975  C   LEU A 369     1745   2034   1970    341    -24   -216       C  
ATOM   2976  O   LEU A 369      15.234 -21.585  26.171  1.00 17.79           O  
ANISOU 2976  O   LEU A 369     2323   2463   1971     -6   -123   -350       O  
ATOM   2977  N   GLU A 370      14.361 -22.193  24.182  1.00 14.59           N  
ANISOU 2977  N   GLU A 370     1676   1826   2040    215   -189   -154       N  
ATOM   2978  CA  GLU A 370      15.003 -21.124  23.431  1.00 15.49           C  
ANISOU 2978  CA  GLU A 370     1763   1931   2190    284     -7     41       C  
ATOM   2979  CB  GLU A 370      15.824 -21.657  22.262  1.00 15.89           C  
ANISOU 2979  CB  GLU A 370     1651   2134   2251    438   -141      7       C  
ATOM   2980  CG  GLU A 370      15.338 -22.930  21.593  1.00 18.30           C  
ANISOU 2980  CG  GLU A 370     2288   2318   2345    388     66   -158       C  
ATOM   2981  CD  GLU A 370      14.045 -22.865  20.808  1.00 18.36           C  
ANISOU 2981  CD  GLU A 370     2412   2323   2241    469    103    -93       C  
ATOM   2982  OE1 GLU A 370      13.327 -21.839  20.940  1.00 17.10           O  
ANISOU 2982  OE1 GLU A 370     2338   1931   2226    204     59   -137       O  
ATOM   2983  OE2 GLU A 370      13.751 -23.874  20.068  1.00 20.48           O  
ANISOU 2983  OE2 GLU A 370     2306   2685   2789    387    181   -577       O  
ATOM   2984  C   GLU A 370      13.936 -20.080  23.054  1.00 13.95           C  
ANISOU 2984  C   GLU A 370     1751   1614   1932    162    -28     33       C  
ATOM   2985  O   GLU A 370      12.756 -20.154  23.466  1.00 14.71           O  
ANISOU 2985  O   GLU A 370     1600   1888   2101    416    -38      6       O  
ATOM   2986  N   GLN A 371      14.364 -19.052  22.322  1.00 15.44           N  
ANISOU 2986  N   GLN A 371     1983   1825   2059    368    221    288       N  
ATOM   2987  CA  GLN A 371      13.533 -17.849  22.179  1.00 14.36           C  
ANISOU 2987  CA  GLN A 371     1837   1685   1934    301     60     97       C  
ATOM   2988  CB  GLN A 371      14.316 -16.748  21.456  1.00 16.28           C  
ANISOU 2988  CB  GLN A 371     2260   1919   2005    214    107    154       C  
ATOM   2989  CG  GLN A 371      13.600 -15.405  21.520  1.00 15.77           C  
ANISOU 2989  CG  GLN A 371     2237   1713   2042     16   -194     12       C  
ATOM   2990  CD  GLN A 371      14.428 -14.266  20.987  1.00 15.01           C  
ANISOU 2990  CD  GLN A 371     2213   1482   2008    220   -136    129       C  
ATOM   2991  OE1 GLN A 371      15.017 -14.348  19.900  1.00 16.29           O  
ANISOU 2991  OE1 GLN A 371     2266   1860   2062    141    -65    -17       O  
ATOM   2992  NE2 GLN A 371      14.460 -13.194  21.766  1.00 14.50           N  
ANISOU 2992  NE2 GLN A 371     1893   1897   1716    178   -468   -118       N  
ATOM   2993  C   GLN A 371      12.201 -18.162  21.481  1.00 13.78           C  
ANISOU 2993  C   GLN A 371     1742   1420   2070    316    181     92       C  
ATOM   2994  O   GLN A 371      11.149 -17.627  21.851  1.00 14.99           O  
ANISOU 2994  O   GLN A 371     1677   1702   2313    446    220    170       O  
ATOM   2995  N   GLN A 372      12.220 -19.007  20.453  1.00 14.29           N  
ANISOU 2995  N   GLN A 372     1787   1583   2059    400    161     95       N  
ATOM   2996  CA  GLN A 372      10.995 -19.361  19.743  1.00 15.08           C  
ANISOU 2996  CA  GLN A 372     1914   1960   1855    237    203    223       C  
ATOM   2997  CB  GLN A 372      11.304 -20.260  18.558  1.00 16.50           C  
ANISOU 2997  CB  GLN A 372     2351   1994   1921    379    189    111       C  
ATOM   2998  CG  GLN A 372      10.078 -20.601  17.748  1.00 20.06           C  
ANISOU 2998  CG  GLN A 372     2964   2480   2177   -191    158   -662       C  
ATOM   2999  CD  GLN A 372       9.549 -19.394  17.002  1.00 22.13           C  
ANISOU 2999  CD  GLN A 372     2649   3145   2612    185   -380   -695       C  
ATOM   3000  OE1 GLN A 372      10.303 -18.598  16.427  1.00 27.71           O  
ANISOU 3000  OE1 GLN A 372     4222   3340   2966   -287   -288   -240       O  
ATOM   3001  NE2 GLN A 372       8.243 -19.233  16.999  1.00 27.58           N  
ANISOU 3001  NE2 GLN A 372     2638   5069   2773    930   -534  -1575       N  
ATOM   3002  C   GLN A 372      10.010 -20.059  20.687  1.00 13.56           C  
ANISOU 3002  C   GLN A 372     1692   1710   1749    188     37    156       C  
ATOM   3003  O   GLN A 372       8.799 -19.810  20.629  1.00 14.62           O  
ANISOU 3003  O   GLN A 372     1770   1816   1969    293    139    305       O  
ATOM   3004  N   GLN A 373      10.518 -20.946  21.542  1.00 13.52           N  
ANISOU 3004  N   GLN A 373     1663   1721   1752    336     72     66       N  
ATOM   3005  CA  GLN A 373       9.661 -21.635  22.476  1.00 13.77           C  
ANISOU 3005  CA  GLN A 373     1827   1593   1809    362     46    178       C  
ATOM   3006  CB  GLN A 373      10.421 -22.787  23.120  1.00 13.86           C  
ANISOU 3006  CB  GLN A 373     1661   1598   2006    405     37    161       C  
ATOM   3007  CG  GLN A 373      10.714 -23.930  22.153  1.00 14.42           C  
ANISOU 3007  CG  GLN A 373     1815   1830   1835    247     19     51       C  
ATOM   3008  CD  GLN A 373      11.741 -24.878  22.722  1.00 15.40           C  
ANISOU 3008  CD  GLN A 373     2229   1570   2050    459    186     23       C  
ATOM   3009  OE1 GLN A 373      12.824 -24.446  23.111  1.00 17.45           O  
ANISOU 3009  OE1 GLN A 373     2217   1921   2491    310    154   -118       O  
ATOM   3010  NE2 GLN A 373      11.401 -26.165  22.794  1.00 15.62           N  
ANISOU 3010  NE2 GLN A 373     2256   1584   2095    261    495    -52       N  
ATOM   3011  C   GLN A 373       9.112 -20.674  23.533  1.00 12.74           C  
ANISOU 3011  C   GLN A 373     1547   1543   1750    426    -73    215       C  
ATOM   3012  O   GLN A 373       7.957 -20.828  23.965  1.00 13.34           O  
ANISOU 3012  O   GLN A 373     1717   1581   1770    426    178    142       O  
ATOM   3013  N   LEU A 374       9.912 -19.685  23.948  1.00 13.19           N  
ANISOU 3013  N   LEU A 374     1624   1601   1786    333     16    126       N  
ATOM   3014  CA  LEU A 374       9.411 -18.669  24.889  1.00 12.81           C  
ANISOU 3014  CA  LEU A 374     1765   1442   1659    329    -44    149       C  
ATOM   3015  CB  LEU A 374      10.558 -17.769  25.372  1.00 13.46           C  
ANISOU 3015  CB  LEU A 374     1775   1556   1782    390   -111    -10       C  
ATOM   3016  CG  LEU A 374      11.617 -18.459  26.225  1.00 14.51           C  
ANISOU 3016  CG  LEU A 374     1942   1693   1876    415   -279     -4       C  
ATOM   3017  CD1 LEU A 374      12.796 -17.548  26.463  1.00 15.98           C  
ANISOU 3017  CD1 LEU A 374     1988   2119   1965    258   -213    167       C  
ATOM   3018  CD2 LEU A 374      11.023 -18.944  27.543  1.00 15.31           C  
ANISOU 3018  CD2 LEU A 374     2160   1703   1953    343   -326      4       C  
ATOM   3019  C   LEU A 374       8.306 -17.820  24.249  1.00 12.16           C  
ANISOU 3019  C   LEU A 374     1553   1487   1577    192    -33     49       C  
ATOM   3020  O   LEU A 374       7.334 -17.431  24.908  1.00 12.34           O  
ANISOU 3020  O   LEU A 374     1762   1438   1488     35    182    -50       O  
ATOM   3021  N   TYR A 375       8.441 -17.551  22.953  1.00 12.52           N  
ANISOU 3021  N   TYR A 375     1653   1565   1536    232     82     83       N  
ATOM   3022  CA  TYR A 375       7.382 -16.870  22.205  1.00 12.21           C  
ANISOU 3022  CA  TYR A 375     1589   1575   1472    281    185    104       C  
ATOM   3023  CB  TYR A 375       7.856 -16.573  20.785  1.00 11.10           C  
ANISOU 3023  CB  TYR A 375     1463   1323   1430    248    185    -35       C  
ATOM   3024  CG  TYR A 375       6.796 -16.027  19.861  1.00 11.05           C  
ANISOU 3024  CG  TYR A 375     1553   1267   1375    133    110     68       C  
ATOM   3025  CD1 TYR A 375       6.310 -14.738  20.026  1.00 12.21           C  
ANISOU 3025  CD1 TYR A 375     1846   1272   1519    187    -41     88       C  
ATOM   3026  CE1 TYR A 375       5.396 -14.195  19.146  1.00 13.27           C  
ANISOU 3026  CE1 TYR A 375     1804   1667   1570    393     35    -11       C  
ATOM   3027  CZ  TYR A 375       4.909 -14.949  18.104  1.00 12.53           C  
ANISOU 3027  CZ  TYR A 375     1600   1858   1302    216      1    153       C  
ATOM   3028  OH  TYR A 375       4.009 -14.387  17.240  1.00 14.39           O  
ANISOU 3028  OH  TYR A 375     1709   2254   1504    330   -110    207       O  
ATOM   3029  CE2 TYR A 375       5.370 -16.242  17.934  1.00 13.57           C  
ANISOU 3029  CE2 TYR A 375     1873   1843   1438    147   -260   -161       C  
ATOM   3030  CD2 TYR A 375       6.301 -16.770  18.812  1.00 12.63           C  
ANISOU 3030  CD2 TYR A 375     1798   1442   1556    179      4     14       C  
ATOM   3031  C   TYR A 375       6.105 -17.721  22.173  1.00 11.71           C  
ANISOU 3031  C   TYR A 375     1496   1575   1376    339     49     18       C  
ATOM   3032  O   TYR A 375       5.004 -17.208  22.380  1.00 11.21           O  
ANISOU 3032  O   TYR A 375     1378   1490   1390    174    270   -115       O  
ATOM   3033  N   GLU A 376       6.261 -19.028  21.927  1.00 11.99           N  
ANISOU 3033  N   GLU A 376     1494   1503   1557    340     10    113       N  
ATOM   3034  CA  GLU A 376       5.091 -19.944  21.912  1.00 12.29           C  
ANISOU 3034  CA  GLU A 376     1761   1490   1418    213    -28     33       C  
ATOM   3035  CB  GLU A 376       5.548 -21.334  21.459  1.00 14.74           C  
ANISOU 3035  CB  GLU A 376     2088   1637   1874    357     73    -47       C  
ATOM   3036  CG  GLU A 376       5.945 -21.363  20.002  1.00 15.19           C  
ANISOU 3036  CG  GLU A 376     1866   1936   1970    268    149   -152       C  
ATOM   3037  CD  GLU A 376       6.633 -22.612  19.516  1.00 17.64           C  
ANISOU 3037  CD  GLU A 376     1952   2322   2425    547    188   -278       C  
ATOM   3038  OE1 GLU A 376       6.848 -23.521  20.324  1.00 21.30           O  
ANISOU 3038  OE1 GLU A 376     3112   2164   2814    662    470   -268       O  
ATOM   3039  OE2 GLU A 376       6.980 -22.647  18.307  1.00 24.30           O  
ANISOU 3039  OE2 GLU A 376     3094   3444   2693   1462    353   -665       O  
ATOM   3040  C   GLU A 376       4.433 -19.985  23.298  1.00 12.50           C  
ANISOU 3040  C   GLU A 376     1712   1516   1522    236      2     -8       C  
ATOM   3041  O   GLU A 376       3.205 -19.931  23.391  1.00 12.64           O  
ANISOU 3041  O   GLU A 376     1769   1399   1633    242    222     52       O  
ATOM   3042  N   LEU A 377       5.259 -20.045  24.363  1.00 11.24           N  
ANISOU 3042  N   LEU A 377     1564   1259   1444    137     56     24       N  
ATOM   3043  CA  LEU A 377       4.737 -20.014  25.722  1.00 11.62           C  
ANISOU 3043  CA  LEU A 377     1778   1253   1382    193     34     28       C  
ATOM   3044  CB  LEU A 377       5.912 -20.057  26.712  1.00 12.25           C  
ANISOU 3044  CB  LEU A 377     1848   1284   1521    249     15     43       C  
ATOM   3045  CG  LEU A 377       5.588 -19.740  28.174  1.00 12.64           C  
ANISOU 3045  CG  LEU A 377     1933   1310   1557    283    205     88       C  
ATOM   3046  CD1 LEU A 377       4.581 -20.723  28.764  1.00 12.72           C  
ANISOU 3046  CD1 LEU A 377     1951   1370   1511    216    158    -38       C  
ATOM   3047  CD2 LEU A 377       6.865 -19.752  29.005  1.00 14.01           C  
ANISOU 3047  CD2 LEU A 377     2095   1508   1718    311     80     68       C  
ATOM   3048  C   LEU A 377       3.904 -18.740  25.925  1.00 11.83           C  
ANISOU 3048  C   LEU A 377     1794   1236   1463    180     67     19       C  
ATOM   3049  O   LEU A 377       2.769 -18.767  26.417  1.00 12.27           O  
ANISOU 3049  O   LEU A 377     1808   1316   1536    216     14    -30       O  
ATOM   3050  N   SER A 378       4.502 -17.588  25.606  1.00 11.08           N  
ANISOU 3050  N   SER A 378     1430   1301   1477    162    189   -103       N  
ATOM   3051  CA  SER A 378       3.800 -16.336  25.858  1.00 10.60           C  
ANISOU 3051  CA  SER A 378     1388   1283   1355    201    143    -44       C  
ATOM   3052  CB  SER A 378       4.695 -15.155  25.585  1.00 11.76           C  
ANISOU 3052  CB  SER A 378     1654   1169   1642    205     85     24       C  
ATOM   3053  OG  SER A 378       4.204 -13.992  26.211  1.00 11.18           O  
ANISOU 3053  OG  SER A 378     1543   1373   1328    320    -68    -97       O  
ATOM   3054  C   SER A 378       2.496 -16.277  25.028  1.00 11.06           C  
ANISOU 3054  C   SER A 378     1506   1268   1429     76     70     61       C  
ATOM   3055  O   SER A 378       1.452 -15.830  25.521  1.00 11.21           O  
ANISOU 3055  O   SER A 378     1551   1315   1393    224   -163    -70       O  
ATOM   3056  N   SER A 379       2.570 -16.716  23.769  1.00 11.25           N  
ANISOU 3056  N   SER A 379     1396   1426   1452    132    148    -45       N  
ATOM   3057  CA  SER A 379       1.432 -16.732  22.859  1.00 11.13           C  
ANISOU 3057  CA  SER A 379     1461   1347   1419    148    141     61       C  
ATOM   3058  CB  SER A 379       1.880 -17.109  21.463  1.00 12.23           C  
ANISOU 3058  CB  SER A 379     1604   1678   1365    190    175    188       C  
ATOM   3059  OG  SER A 379       2.761 -16.125  20.940  1.00 12.80           O  
ANISOU 3059  OG  SER A 379     1656   1737   1470    106    158    171       O  
ATOM   3060  C   SER A 379       0.309 -17.642  23.369  1.00 11.03           C  
ANISOU 3060  C   SER A 379     1535   1385   1268     95     15     74       C  
ATOM   3061  O   SER A 379      -0.885 -17.333  23.199  1.00 12.21           O  
ANISOU 3061  O   SER A 379     1547   1512   1580    107     77      6       O  
ATOM   3062  N   SER A 380       0.681 -18.737  24.025  1.00 10.61           N  
ANISOU 3062  N   SER A 380     1346   1303   1382    167    -33    -12       N  
ATOM   3063  CA  SER A 380      -0.324 -19.670  24.583  1.00 11.39           C  
ANISOU 3063  CA  SER A 380     1619   1343   1366     88     63    118       C  
ATOM   3064  CB  SER A 380       0.330 -20.945  25.077  1.00 13.28           C  
ANISOU 3064  CB  SER A 380     1861   1576   1609    190   -125    229       C  
ATOM   3065  OG  SER A 380       0.989 -20.763  26.324  1.00 13.29           O  
ANISOU 3065  OG  SER A 380     1855   1686   1506    315   -131    224       O  
ATOM   3066  C   SER A 380      -1.158 -18.999  25.677  1.00 11.43           C  
ANISOU 3066  C   SER A 380     1543   1398   1401    151     -3    138       C  
ATOM   3067  O   SER A 380      -2.210 -19.491  26.010  1.00 13.79           O  
ANISOU 3067  O   SER A 380     1719   1623   1897    -65    270   -240       O  
ATOM   3068  N   ASN A 381      -0.608 -17.911  26.236  1.00 11.03           N  
ANISOU 3068  N   ASN A 381     1597   1313   1280    165    159     52       N  
ATOM   3069  CA  ASN A 381      -1.220 -17.129  27.295  1.00 11.60           C  
ANISOU 3069  CA  ASN A 381     1700   1604   1102    198     86     12       C  
ATOM   3070  CB  ASN A 381      -0.276 -17.033  28.492  1.00 11.64           C  
ANISOU 3070  CB  ASN A 381     1834   1554   1032     72     65    -16       C  
ATOM   3071  CG  ASN A 381      -0.058 -18.386  29.144  1.00 12.42           C  
ANISOU 3071  CG  ASN A 381     1853   1532   1333      4    -51     47       C  
ATOM   3072  OD1 ASN A 381      -1.042 -19.084  29.436  1.00 13.36           O  
ANISOU 3072  OD1 ASN A 381     1783   1773   1518    151    167    172       O  
ATOM   3073  ND2 ASN A 381       1.191 -18.777  29.333  1.00 14.54           N  
ANISOU 3073  ND2 ASN A 381     1763   2075   1685     22     12    -35       N  
ATOM   3074  C   ASN A 381      -1.658 -15.748  26.792  1.00 12.14           C  
ANISOU 3074  C   ASN A 381     1729   1589   1294    241      2    -96       C  
ATOM   3075  O   ASN A 381      -1.889 -14.840  27.594  1.00 14.14           O  
ANISOU 3075  O   ASN A 381     2224   1623   1523    368   -114   -269       O  
ATOM   3076  N   GLY A 382      -1.810 -15.614  25.478  1.00 10.95           N  
ANISOU 3076  N   GLY A 382     1745   1175   1238    192    142    -32       N  
ATOM   3077  CA  GLY A 382      -2.478 -14.467  24.881  1.00 12.22           C  
ANISOU 3077  CA  GLY A 382     1681   1454   1505    197    -30    142       C  
ATOM   3078  C   GLY A 382      -1.551 -13.503  24.157  1.00 12.01           C  
ANISOU 3078  C   GLY A 382     1624   1482   1458    135    -15     57       C  
ATOM   3079  O   GLY A 382      -2.076 -12.592  23.520  1.00 12.22           O  
ANISOU 3079  O   GLY A 382     1517   1282   1844    271    -26    -24       O  
ATOM   3080  N   TYR A 383      -0.215 -13.661  24.253  1.00 11.15           N  
ANISOU 3080  N   TYR A 383     1621   1210   1404    121     61    171       N  
ATOM   3081  CA  TYR A 383       0.683 -12.691  23.610  1.00 10.73           C  
ANISOU 3081  CA  TYR A 383     1429   1207   1439    118      1    128       C  
ATOM   3082  CB  TYR A 383       2.146 -13.143  23.682  1.00 10.99           C  
ANISOU 3082  CB  TYR A 383     1473   1215   1487    153     98    103       C  
ATOM   3083  CG  TYR A 383       3.105 -12.096  23.178  1.00 10.87           C  
ANISOU 3083  CG  TYR A 383     1533   1184   1411    101     20    137       C  
ATOM   3084  CD1 TYR A 383       3.540 -11.053  23.985  1.00 11.41           C  
ANISOU 3084  CD1 TYR A 383     1708   1477   1148     93    -56    100       C  
ATOM   3085  CE1 TYR A 383       4.380 -10.062  23.490  1.00 11.37           C  
ANISOU 3085  CE1 TYR A 383     1741   1347   1230     62    -39    -78       C  
ATOM   3086  CZ  TYR A 383       4.875 -10.156  22.196  1.00 10.87           C  
ANISOU 3086  CZ  TYR A 383     1765   1122   1240     89     53    129       C  
ATOM   3087  OH  TYR A 383       5.723  -9.215  21.691  1.00 11.85           O  
ANISOU 3087  OH  TYR A 383     1727   1398   1377     54    160    213       O  
ATOM   3088  CE2 TYR A 383       4.449 -11.194  21.386  1.00 11.31           C  
ANISOU 3088  CE2 TYR A 383     1682   1373   1241    138    -27     20       C  
ATOM   3089  CD2 TYR A 383       3.602 -12.169  21.892  1.00 11.53           C  
ANISOU 3089  CD2 TYR A 383     1677   1285   1418     32    -33   -105       C  
ATOM   3090  C   TYR A 383       0.268 -12.541  22.142  1.00 10.52           C  
ANISOU 3090  C   TYR A 383     1379   1202   1414     78     -3    105       C  
ATOM   3091  O   TYR A 383       0.129 -13.529  21.427  1.00 12.47           O  
ANISOU 3091  O   TYR A 383     1761   1520   1455     41     10    -21       O  
ATOM   3092  N   ASN A 384       0.146 -11.292  21.682  1.00 10.90           N  
ANISOU 3092  N   ASN A 384     1497   1169   1475     66     28     81       N  
ATOM   3093  CA  ASN A 384      -0.635 -10.973  20.489  1.00 12.10           C  
ANISOU 3093  CA  ASN A 384     1551   1483   1562     68     -7    106       C  
ATOM   3094  CB  ASN A 384      -1.879 -10.146  20.856  1.00 12.66           C  
ANISOU 3094  CB  ASN A 384     1637   1620   1554    216    -70    106       C  
ATOM   3095  CG  ASN A 384      -1.564  -8.809  21.483  1.00 12.93           C  
ANISOU 3095  CG  ASN A 384     1598   1748   1567    346    134     63       C  
ATOM   3096  OD1 ASN A 384      -0.443  -8.299  21.330  1.00 14.94           O  
ANISOU 3096  OD1 ASN A 384     1616   2053   2005    292    321    -29       O  
ATOM   3097  ND2 ASN A 384      -2.554  -8.252  22.194  1.00 14.36           N  
ANISOU 3097  ND2 ASN A 384     1732   2033   1689    426    393    176       N  
ATOM   3098  C   ASN A 384       0.173 -10.265  19.390  1.00 12.04           C  
ANISOU 3098  C   ASN A 384     1612   1530   1432    171      3     74       C  
ATOM   3099  O   ASN A 384      -0.455  -9.781  18.431  1.00 14.96           O  
ANISOU 3099  O   ASN A 384     1821   2095   1766    176   -259    322       O  
ATOM   3100  N   LYS A 385       1.508 -10.299  19.454  1.00 10.91           N  
ANISOU 3100  N   LYS A 385     1597   1253   1292    145     -7    -42       N  
ATOM   3101  CA  LYS A 385       2.343  -9.666  18.437  1.00 10.45           C  
ANISOU 3101  CA  LYS A 385     1458   1237   1276    178    -53    -17       C  
ATOM   3102  CB  LYS A 385       3.196  -8.550  19.044  1.00 11.80           C  
ANISOU 3102  CB  LYS A 385     1608   1257   1615     58    132    -88       C  
ATOM   3103  CG  LYS A 385       2.407  -7.432  19.706  1.00 12.37           C  
ANISOU 3103  CG  LYS A 385     1657   1359   1683    121    232    -62       C  
ATOM   3104  CD  LYS A 385       1.398  -6.754  18.806  1.00 12.44           C  
ANISOU 3104  CD  LYS A 385     1720   1314   1691    117    230    -32       C  
ATOM   3105  CE  LYS A 385       2.048  -6.021  17.658  1.00 12.71           C  
ANISOU 3105  CE  LYS A 385     1912   1410   1504    161    189    -11       C  
ATOM   3106  NZ  LYS A 385       1.075  -5.561  16.637  1.00 13.73           N  
ANISOU 3106  NZ  LYS A 385     1959   1474   1783    280     94    -66       N  
ATOM   3107  C   LYS A 385       3.233 -10.693  17.732  1.00 10.12           C  
ANISOU 3107  C   LYS A 385     1364   1220   1258    113     -9     15       C  
ATOM   3108  O   LYS A 385       3.474 -11.807  18.213  1.00 11.70           O  
ANISOU 3108  O   LYS A 385     1715   1262   1466    251    -62     10       O  
ATOM   3109  N   ARG A 386       3.759 -10.266  16.581  1.00 10.92           N  
ANISOU 3109  N   ARG A 386     1749   1050   1350    136    171    -47       N  
ATOM   3110  CA  ARG A 386       4.604 -11.109  15.738  1.00 10.47           C  
ANISOU 3110  CA  ARG A 386     1456   1122   1400    140     82    -74       C  
ATOM   3111  CB  ARG A 386       4.869 -10.414  14.398  1.00 10.24           C  
ANISOU 3111  CB  ARG A 386     1415   1184   1290    213     33    -78       C  
ATOM   3112  CG  ARG A 386       5.719  -9.151  14.528  1.00 11.30           C  
ANISOU 3112  CG  ARG A 386     1607   1351   1332     81   -171     45       C  
ATOM   3113  CD  ARG A 386       5.851  -8.289  13.298  1.00 10.61           C  
ANISOU 3113  CD  ARG A 386     1493   1257   1278     65     20    -28       C  
ATOM   3114  NE  ARG A 386       4.568  -7.705  12.914  1.00 11.04           N  
ANISOU 3114  NE  ARG A 386     1476   1404   1312     31     -2     64       N  
ATOM   3115  CZ  ARG A 386       4.411  -6.857  11.898  1.00 10.35           C  
ANISOU 3115  CZ  ARG A 386     1335   1354   1243      9     63     14       C  
ATOM   3116  NH1 ARG A 386       5.472  -6.530  11.153  1.00 10.87           N  
ANISOU 3116  NH1 ARG A 386     1389   1390   1351     68    237    -63       N  
ATOM   3117  NH2 ARG A 386       3.204  -6.349  11.648  1.00 11.68           N  
ANISOU 3117  NH2 ARG A 386     1590   1599   1245    291    -35    -36       N  
ATOM   3118  C   ARG A 386       5.937 -11.438  16.437  1.00 10.02           C  
ANISOU 3118  C   ARG A 386     1486   1005   1316    178     57     46       C  
ATOM   3119  O   ARG A 386       6.440 -10.723  17.327  1.00 10.95           O  
ANISOU 3119  O   ARG A 386     1599   1211   1348    135     51     42       O  
ATOM   3120  N   PHE A 387       6.568 -12.505  15.956  1.00 10.01           N  
ANISOU 3120  N   PHE A 387     1494   1060   1248    192   -130   -151       N  
ATOM   3121  CA  PHE A 387       7.825 -12.975  16.540  1.00 10.56           C  
ANISOU 3121  CA  PHE A 387     1401   1201   1410    214    -77   -129       C  
ATOM   3122  CB  PHE A 387       8.243 -14.310  15.921  1.00 10.64           C  
ANISOU 3122  CB  PHE A 387     1429   1198   1413    196     -4   -156       C  
ATOM   3123  CG  PHE A 387       9.518 -14.863  16.506  1.00 11.00           C  
ANISOU 3123  CG  PHE A 387     1385   1250   1545    195     28   -168       C  
ATOM   3124  CD1 PHE A 387       9.599 -15.188  17.854  1.00 11.78           C  
ANISOU 3124  CD1 PHE A 387     1538   1290   1648    211    -13     48       C  
ATOM   3125  CE1 PHE A 387      10.769 -15.685  18.390  1.00 12.83           C  
ANISOU 3125  CE1 PHE A 387     1625   1584   1663    309    -34    -58       C  
ATOM   3126  CZ  PHE A 387      11.855 -15.900  17.596  1.00 14.24           C  
ANISOU 3126  CZ  PHE A 387     1689   1731   1991    384    101    -56       C  
ATOM   3127  CD2 PHE A 387      10.628 -15.068  15.713  1.00 13.03           C  
ANISOU 3127  CD2 PHE A 387     1535   1672   1743    342    122    -81       C  
ATOM   3128  CE2 PHE A 387      11.800 -15.570  16.258  1.00 13.99           C  
ANISOU 3128  CE2 PHE A 387     1517   1958   1838    442     40    -90       C  
ATOM   3129  C   PHE A 387       8.961 -11.942  16.422  1.00 10.25           C  
ANISOU 3129  C   PHE A 387     1382   1215   1296    241    -43   -106       C  
ATOM   3130  O   PHE A 387       9.728 -11.806  17.353  1.00 11.96           O  
ANISOU 3130  O   PHE A 387     1615   1446   1481    184   -216   -206       O  
ATOM   3131  N   SER A 388       9.040 -11.207  15.308  1.00 10.88           N  
ANISOU 3131  N   SER A 388     1475   1437   1219    109   -118    -45       N  
ATOM   3132  CA  SER A 388      10.115 -10.215  15.119  1.00 11.26           C  
ANISOU 3132  CA  SER A 388     1425   1383   1470    217    -78   -118       C  
ATOM   3133  CB  SER A 388      10.167  -9.715  13.709  1.00 11.34           C  
ANISOU 3133  CB  SER A 388     1463   1403   1439     53    -11    -77       C  
ATOM   3134  OG  SER A 388       8.926  -9.122  13.339  1.00 12.06           O  
ANISOU 3134  OG  SER A 388     1398   1697   1485    166     26     29       O  
ATOM   3135  C   SER A 388      10.004  -9.037  16.088  1.00 12.26           C  
ANISOU 3135  C   SER A 388     1648   1436   1572    156    -97   -166       C  
ATOM   3136  O   SER A 388      10.985  -8.335  16.276  1.00 13.57           O  
ANISOU 3136  O   SER A 388     1794   1595   1764    -59    142   -285       O  
ATOM   3137  N   CYS A 389       8.816  -8.806  16.660  1.00 11.91           N  
ANISOU 3137  N   CYS A 389     1618   1400   1505     78    -88   -107       N  
ATOM   3138  CA  CYS A 389       8.663  -7.844  17.745  1.00 11.45           C  
ANISOU 3138  CA  CYS A 389     1680   1220   1449     44   -143     -7       C  
ATOM   3139  CB  CYS A 389       7.183  -7.484  17.873  1.00 11.77           C  
ANISOU 3139  CB  CYS A 389     1756   1245   1468     80    -81      2       C  
ATOM   3140  SG  CYS A 389       6.757  -6.539  19.358  1.00 13.57           S  
ANISOU 3140  SG  CYS A 389     2056   1569   1529    140    102    -62       S  
ATOM   3141  C   CYS A 389       9.239  -8.441  19.031  1.00 12.39           C  
ANISOU 3141  C   CYS A 389     1730   1541   1436    -18   -120    -27       C  
ATOM   3142  O   CYS A 389      10.206  -7.927  19.619  1.00 12.56           O  
ANISOU 3142  O   CYS A 389     1891   1308   1570     78   -190   -152       O  
ATOM   3143  N   PHE A 390       8.637  -9.562  19.431  1.00 11.09           N  
ANISOU 3143  N   PHE A 390     1551   1406   1254   -109   -235    -94       N  
ATOM   3144  CA  PHE A 390       9.019 -10.296  20.632  1.00 11.83           C  
ANISOU 3144  CA  PHE A 390     1582   1565   1346    -10   -142    -34       C  
ATOM   3145  CB  PHE A 390       8.286 -11.638  20.674  1.00 11.16           C  
ANISOU 3145  CB  PHE A 390     1431   1439   1369     50    -67   -110       C  
ATOM   3146  CG  PHE A 390       8.617 -12.500  21.861  1.00 11.69           C  
ANISOU 3146  CG  PHE A 390     1522   1695   1223     81     33    -88       C  
ATOM   3147  CD2 PHE A 390       7.845 -12.457  23.017  1.00 10.75           C  
ANISOU 3147  CD2 PHE A 390     1362   1448   1272     45    -23    -90       C  
ATOM   3148  CE2 PHE A 390       8.148 -13.279  24.098  1.00 11.71           C  
ANISOU 3148  CE2 PHE A 390     1590   1596   1260     66    -32    -31       C  
ATOM   3149  CZ  PHE A 390       9.242 -14.128  24.040  1.00 12.29           C  
ANISOU 3149  CZ  PHE A 390     1569   1749   1351     52     11     28       C  
ATOM   3150  CD1 PHE A 390       9.678 -13.392  21.811  1.00 11.47           C  
ANISOU 3150  CD1 PHE A 390     1564   1603   1191     95    191    -72       C  
ATOM   3151  CE1 PHE A 390       9.997 -14.195  22.896  1.00 12.36           C  
ANISOU 3151  CE1 PHE A 390     1599   1624   1470    154     10     -8       C  
ATOM   3152  C   PHE A 390      10.532 -10.504  20.719  1.00 11.71           C  
ANISOU 3152  C   PHE A 390     1537   1641   1271    -61   -107   -150       C  
ATOM   3153  O   PHE A 390      11.151 -10.373  21.792  1.00 12.92           O  
ANISOU 3153  O   PHE A 390     1702   1920   1287    -22   -201   -173       O  
ATOM   3154  N   SER A 391      11.147 -10.878  19.592  1.00 11.59           N  
ANISOU 3154  N   SER A 391     1534   1538   1328     65    -80    -67       N  
ATOM   3155  CA  SER A 391      12.518 -11.360  19.646  1.00 11.58           C  
ANISOU 3155  CA  SER A 391     1506   1632   1260    121   -128    -67       C  
ATOM   3156  CB  SER A 391      12.895 -12.083  18.385  1.00 12.33           C  
ANISOU 3156  CB  SER A 391     1647   1735   1302    130    -61    -95       C  
ATOM   3157  OG  SER A 391      13.020 -11.164  17.321  1.00 13.04           O  
ANISOU 3157  OG  SER A 391     1763   1637   1552     24   -161    102       O  
ATOM   3158  C   SER A 391      13.549 -10.262  19.944  1.00 12.24           C  
ANISOU 3158  C   SER A 391     1569   1628   1453    128   -171   -105       C  
ATOM   3159  O   SER A 391      14.669 -10.561  20.412  1.00 12.69           O  
ANISOU 3159  O   SER A 391     1560   1718   1542     64   -194    -28       O  
ATOM   3160  N   GLY A 392      13.229  -9.010  19.600  1.00 12.02           N  
ANISOU 3160  N   GLY A 392     1331   1522   1712     38    -42   -158       N  
ATOM   3161  CA  GLY A 392      14.214  -7.933  19.699  1.00 12.29           C  
ANISOU 3161  CA  GLY A 392     1267   1697   1703     -6   -186   -100       C  
ATOM   3162  C   GLY A 392      15.348  -8.087  18.689  1.00 12.51           C  
ANISOU 3162  C   GLY A 392     1436   1687   1627     46   -144   -193       C  
ATOM   3163  O   GLY A 392      16.388  -7.428  18.833  1.00 12.99           O  
ANISOU 3163  O   GLY A 392     1372   1751   1811     -2     -4    -76       O  
ATOM   3164  N   ALA A 393      15.170  -8.943  17.660  1.00 12.48           N  
ANISOU 3164  N   ALA A 393     1358   1672   1710    141   -252   -252       N  
ATOM   3165  CA  ALA A 393      16.209  -9.148  16.655  1.00 13.31           C  
ANISOU 3165  CA  ALA A 393     1724   1644   1689     18    -33   -247       C  
ATOM   3166  CB  ALA A 393      15.941 -10.403  15.852  1.00 12.96           C  
ANISOU 3166  CB  ALA A 393     1537   1623   1762     46    -87   -245       C  
ATOM   3167  C   ALA A 393      16.325  -7.925  15.731  1.00 12.66           C  
ANISOU 3167  C   ALA A 393     1446   1706   1658    -29    -24   -242       C  
ATOM   3168  O   ALA A 393      15.457  -7.054  15.684  1.00 12.06           O  
ANISOU 3168  O   ALA A 393     1406   1711   1466    -23     26   -116       O  
ATOM   3169  N   LEU A 394      17.431  -7.896  14.982  1.00 12.65           N  
ANISOU 3169  N   LEU A 394     1493   1688   1623     20     61    -97       N  
ATOM   3170  CA  LEU A 394      17.632  -6.897  13.937  1.00 12.90           C  
ANISOU 3170  CA  LEU A 394     1476   1663   1762      5     62    -54       C  
ATOM   3171  CB  LEU A 394      19.041  -7.038  13.369  1.00 13.88           C  
ANISOU 3171  CB  LEU A 394     1656   1928   1689     88    249   -188       C  
ATOM   3172  CG  LEU A 394      19.375  -6.153  12.172  1.00 15.22           C  
ANISOU 3172  CG  LEU A 394     1986   2098   1698   -133    109   -177       C  
ATOM   3173  CD1 LEU A 394      19.406  -4.692  12.567  1.00 16.92           C  
ANISOU 3173  CD1 LEU A 394     2086   2135   2205     -6    116   -109       C  
ATOM   3174  CD2 LEU A 394      20.704  -6.618  11.556  1.00 16.13           C  
ANISOU 3174  CD2 LEU A 394     2077   2183   1866     -2    162   -338       C  
ATOM   3175  C   LEU A 394      16.594  -7.129  12.840  1.00 12.21           C  
ANISOU 3175  C   LEU A 394     1445   1515   1679    -48    113    -53       C  
ATOM   3176  O   LEU A 394      16.582  -8.188  12.192  1.00 13.31           O  
ANISOU 3176  O   LEU A 394     1617   1593   1846    394     79   -187       O  
ATOM   3177  N   ALA A 395      15.770  -6.107  12.599  1.00 12.13           N  
ANISOU 3177  N   ALA A 395     1222   1610   1776    -38    -31   -140       N  
ATOM   3178  CA  ALA A 395      14.610  -6.214  11.720  1.00 12.19           C  
ANISOU 3178  CA  ALA A 395     1395   1634   1602    -85    -99   -160       C  
ATOM   3179  CB  ALA A 395      13.499  -5.362  12.261  1.00 11.82           C  
ANISOU 3179  CB  ALA A 395     1577   1374   1540     60   -156    -36       C  
ATOM   3180  C   ALA A 395      14.913  -5.799  10.271  1.00 12.84           C  
ANISOU 3180  C   ALA A 395     1633   1508   1735   -108     23    -55       C  
ATOM   3181  O   ALA A 395      14.182  -6.232   9.359  1.00 14.24           O  
ANISOU 3181  O   ALA A 395     1818   2018   1574     54   -111    -53       O  
ATOM   3182  N   ASN A 396      15.975  -5.013  10.043  1.00 12.88           N  
ANISOU 3182  N   ASN A 396     1694   1507   1692   -148     42    -87       N  
ATOM   3183  CA  ASN A 396      16.243  -4.448   8.723  1.00 13.51           C  
ANISOU 3183  CA  ASN A 396     1781   1586   1766     37    -57     78       C  
ATOM   3184  CB  ASN A 396      15.990  -2.940   8.710  1.00 13.73           C  
ANISOU 3184  CB  ASN A 396     1917   1499   1799    -60     15    210       C  
ATOM   3185  CG  ASN A 396      16.904  -2.134   9.606  1.00 13.21           C  
ANISOU 3185  CG  ASN A 396     1666   1614   1738    173     76    102       C  
ATOM   3186  OD1 ASN A 396      17.446  -2.665  10.569  1.00 13.84           O  
ANISOU 3186  OD1 ASN A 396     1579   1958   1720    -80    -68     73       O  
ATOM   3187  ND2 ASN A 396      17.050  -0.845   9.309  1.00 16.15           N  
ANISOU 3187  ND2 ASN A 396     2167   1703   2266     63    236    133       N  
ATOM   3188  C   ASN A 396      17.663  -4.806   8.274  1.00 14.46           C  
ANISOU 3188  C   ASN A 396     1827   1693   1971     34     -6    -14       C  
ATOM   3189  O   ASN A 396      18.492  -3.936   7.935  1.00 15.11           O  
ANISOU 3189  O   ASN A 396     2039   1734   1967     21    351     64       O  
ATOM   3190  N   GLY A 397      17.946  -6.109   8.242  1.00 14.69           N  
ANISOU 3190  N   GLY A 397     1666   1611   2304    -47    -32    -12       N  
ATOM   3191  CA  GLY A 397      19.299  -6.593   7.979  1.00 15.61           C  
ANISOU 3191  CA  GLY A 397     1812   1809   2308    145     95   -114       C  
ATOM   3192  C   GLY A 397      19.872  -6.186   6.638  1.00 15.99           C  
ANISOU 3192  C   GLY A 397     1900   2064   2109    235     55   -168       C  
ATOM   3193  O   GLY A 397      21.074  -6.053   6.539  1.00 17.11           O  
ANISOU 3193  O   GLY A 397     2108   2324   2069    -95    245   -181       O  
ATOM   3194  N   LEU A 398      19.052  -6.019   5.590  1.00 18.46           N  
ANISOU 3194  N   LEU A 398     1670   3026   2316    502    123    -87       N  
ATOM   3195  CA  LEU A 398      19.644  -5.594   4.313  1.00 21.70           C  
ANISOU 3195  CA  LEU A 398     2558   3461   2224    614    447   -137       C  
ATOM   3196  CB  LEU A 398      18.611  -5.455   3.209  1.00 25.22           C  
ANISOU 3196  CB  LEU A 398     2292   3994   3294    792     43   -108       C  
ATOM   3197  CG  LEU A 398      18.250  -6.702   2.455  1.00 26.33           C  
ANISOU 3197  CG  LEU A 398     1749   4386   3870    -62   -169   -180       C  
ATOM   3198  CD1 LEU A 398      17.039  -6.380   1.583  1.00 26.13           C  
ANISOU 3198  CD1 LEU A 398     2061   4165   3702    340   -247   -112       C  
ATOM   3199  CD2 LEU A 398      19.431  -7.208   1.645  1.00 24.17           C  
ANISOU 3199  CD2 LEU A 398     1813   3775   3594   -117   -435   -476       C  
ATOM   3200  C   LEU A 398      20.285  -4.220   4.427  1.00 24.27           C  
ANISOU 3200  C   LEU A 398     3481   3314   2425    843    735     12       C  
ATOM   3201  O   LEU A 398      21.303  -3.967   3.811  1.00 26.54           O  
ANISOU 3201  O   LEU A 398     4041   3548   2493    853   1262    201       O  
ATOM   3202  N   THR A 399      19.584  -3.313   5.111  1.00 28.83           N  
ANISOU 3202  N   THR A 399     4747   3332   2873   1303   1640    542       N  
ATOM   3203  CA  THR A 399      20.026  -1.958   5.245  1.00 32.69           C  
ANISOU 3203  CA  THR A 399     6034   3303   3081   1210   1786    915       C  
ATOM   3204  CB  THR A 399      18.985  -1.158   6.029  1.00 35.94           C  
ANISOU 3204  CB  THR A 399     6888   3064   3702   1884   1960   1049       C  
ATOM   3205  OG1 THR A 399      17.775  -1.170   5.262  1.00 37.84           O  
ANISOU 3205  OG1 THR A 399     6605   4038   3733   2574   2108   1731       O  
ATOM   3206  CG2 THR A 399      19.442   0.255   6.302  1.00 42.02           C  
ANISOU 3206  CG2 THR A 399     7583   3341   5041   1807   2097    660       C  
ATOM   3207  C   THR A 399      21.431  -1.948   5.863  1.00 32.11           C  
ANISOU 3207  C   THR A 399     6422   2853   2925    343   1903    591       C  
ATOM   3208  O   THR A 399      22.327  -1.302   5.377  1.00 38.78           O  
ANISOU 3208  O   THR A 399     7660   3320   3753   -316   3019    378       O  
ATOM   3209  N   VAL A 400      21.602  -2.743   6.920  1.00 28.73           N  
ANISOU 3209  N   VAL A 400     6365   2067   2482    332   1546     14       N  
ATOM   3210  CA  VAL A 400      22.834  -2.839   7.679  1.00 26.82           C  
ANISOU 3210  CA  VAL A 400     5405   2050   2734  -1155   1445   -233       C  
ATOM   3211  CB  VAL A 400      22.518  -3.481   9.042  1.00 32.72           C  
ANISOU 3211  CB  VAL A 400     6126   3920   2386   -858   1272    -79       C  
ATOM   3212  CG1 VAL A 400      23.774  -3.862   9.795  1.00 37.78           C  
ANISOU 3212  CG1 VAL A 400     6063   4922   3367   -797   1171   -240       C  
ATOM   3213  CG2 VAL A 400      21.622  -2.564   9.867  1.00 35.25           C  
ANISOU 3213  CG2 VAL A 400     6703   3423   3267   -983   1402   -264       C  
ATOM   3214  C   VAL A 400      23.929  -3.600   6.897  1.00 26.42           C  
ANISOU 3214  C   VAL A 400     4499   2894   2644  -1065    934   -316       C  
ATOM   3215  O   VAL A 400      25.137  -3.335   7.074  1.00 29.63           O  
ANISOU 3215  O   VAL A 400     4545   3650   3061  -1418    660   -307       O  
ATOM   3216  N   ALA A 401      23.529  -4.519   6.011  1.00 22.42           N  
ANISOU 3216  N   ALA A 401     3640   2587   2291   -786    632    -42       N  
ATOM   3217  CA  ALA A 401      24.477  -5.346   5.238  1.00 22.52           C  
ANISOU 3217  CA  ALA A 401     3361   2704   2490   -818    661   -246       C  
ATOM   3218  CB  ALA A 401      23.803  -6.636   4.805  1.00 21.55           C  
ANISOU 3218  CB  ALA A 401     3217   2531   2438   -529    868   -361       C  
ATOM   3219  C   ALA A 401      25.005  -4.598   4.012  1.00 24.25           C  
ANISOU 3219  C   ALA A 401     3529   3020   2663   -651    823   -114       C  
ATOM   3220  O   ALA A 401      25.920  -5.070   3.367  1.00 24.36           O  
ANISOU 3220  O   ALA A 401     3442   2917   2897   -501    951    -50       O  
ATOM   3221  N   ASP A 402      24.390  -3.455   3.689  1.00 27.30           N  
ANISOU 3221  N   ASP A 402     4570   2954   2845   -652   1075    199       N  
ATOM   3222  CA  ASP A 402      24.744  -2.618   2.534  1.00 28.37           C  
ANISOU 3222  CA  ASP A 402     4395   3232   3149   -538   1297    412       C  
ATOM   3223  CB  ASP A 402      23.696  -1.513   2.395  1.00 29.52           C  
ANISOU 3223  CB  ASP A 402     4809   3406   2998   -170   1255    253       C  
ATOM   3224  CG  ASP A 402      23.828  -0.617   1.173  1.00 30.90           C  
ANISOU 3224  CG  ASP A 402     5021   3821   2899     14   1005    356       C  
ATOM   3225  OD1 ASP A 402      24.881  -0.657   0.501  1.00 33.09           O  
ANISOU 3225  OD1 ASP A 402     4597   4175   3799      5    947   -409       O  
ATOM   3226  OD2 ASP A 402      22.861   0.126   0.909  1.00 34.24           O  
ANISOU 3226  OD2 ASP A 402     5391   4088   3528    471    594    229       O  
ATOM   3227  C   ASP A 402      26.145  -2.038   2.719  1.00 28.24           C  
ANISOU 3227  C   ASP A 402     4594   3006   3128   -526   1488    -82       C  
ATOM   3228  O   ASP A 402      26.396  -1.298   3.669  1.00 30.36           O  
ANISOU 3228  O   ASP A 402     4633   3571   3330   -765    888   -342       O  
ATOM   3229  N   PRO A 403      27.098  -2.310   1.792  1.00 30.53           N  
ANISOU 3229  N   PRO A 403     4681   3305   3610  -1060   1973    221       N  
ATOM   3230  CA  PRO A 403      28.450  -1.758   1.910  1.00 31.91           C  
ANISOU 3230  CA  PRO A 403     4720   3452   3951   -971   1588     27       C  
ATOM   3231  CB  PRO A 403      29.211  -2.468   0.784  1.00 32.46           C  
ANISOU 3231  CB  PRO A 403     4161   3834   4337  -1033   1912     89       C  
ATOM   3232  CG  PRO A 403      28.146  -2.788  -0.251  1.00 32.52           C  
ANISOU 3232  CG  PRO A 403     4862   3672   3821  -1325   1725     73       C  
ATOM   3233  CD  PRO A 403      26.918  -3.121   0.576  1.00 30.92           C  
ANISOU 3233  CD  PRO A 403     4781   3479   3488  -1052   1617    397       C  
ATOM   3234  C   PRO A 403      28.511  -0.231   1.745  1.00 34.84           C  
ANISOU 3234  C   PRO A 403     5409   3438   4390  -1323   1333    -68       C  
ATOM   3235  O   PRO A 403      29.497   0.389   2.174  1.00 40.12           O  
ANISOU 3235  O   PRO A 403     5548   4865   4829  -1582   1117    -74       O  
ATOM   3236  N   ALA A 404      27.471   0.356   1.133  1.00 34.32           N  
ANISOU 3236  N   ALA A 404     5476   3032   4530  -1170   1547     80       N  
ATOM   3237  CA  ALA A 404      27.341   1.818   0.982  1.00 36.43           C  
ANISOU 3237  CA  ALA A 404     6120   3187   4533   -741   1692    127       C  
ATOM   3238  CB  ALA A 404      26.266   2.141  -0.028  1.00 39.63           C  
ANISOU 3238  CB  ALA A 404     7039   3739   4279   -477   1432    300       C  
ATOM   3239  C   ALA A 404      27.034   2.496   2.327  1.00 34.76           C  
ANISOU 3239  C   ALA A 404     5996   2832   4379  -1697   1524    131       C  
ATOM   3240  O   ALA A 404      27.147   3.708   2.428  1.00 43.09           O  
ANISOU 3240  O   ALA A 404     7647   2784   5941  -1288   1255    225       O  
ATOM   3241  N   VAL A 405      26.607   1.722   3.334  1.00 35.37           N  
ANISOU 3241  N   VAL A 405     5611   3583   4243   -868   2007    328       N  
ATOM   3242  CA  VAL A 405      26.399   2.254   4.682  1.00 33.01           C  
ANISOU 3242  CA  VAL A 405     4590   3503   4449   -610   1647    -79       C  
ATOM   3243  CB  VAL A 405      25.165   1.632   5.365  1.00 31.08           C  
ANISOU 3243  CB  VAL A 405     4564   2901   4343   -362   1547    137       C  
ATOM   3244  CG1 VAL A 405      24.952   2.216   6.751  1.00 33.66           C  
ANISOU 3244  CG1 VAL A 405     5049   3375   4363   -174   1297    -32       C  
ATOM   3245  CG2 VAL A 405      23.903   1.789   4.529  1.00 30.52           C  
ANISOU 3245  CG2 VAL A 405     4814   2688   4092   -596   1426   -335       C  
ATOM   3246  C   VAL A 405      27.668   2.001   5.502  1.00 35.21           C  
ANISOU 3246  C   VAL A 405     4466   3751   5158  -1483   1383     26       C  
ATOM   3247  O   VAL A 405      27.967   0.861   5.833  1.00 34.48           O  
ANISOU 3247  O   VAL A 405     3613   4399   5085   -774   1214    153       O  
ATOM   3248  N   ALA A 406      28.408   3.076   5.797  1.00 37.75           N  
ANISOU 3248  N   ALA A 406     4612   3888   5840  -1926   1006    515       N  
ATOM   3249  CA  ALA A 406      29.641   3.032   6.592  1.00 42.96           C  
ANISOU 3249  CA  ALA A 406     4082   4851   7387  -1762    805    571       C  
ATOM   3250  CB  ALA A 406      30.254   4.413   6.644  1.00 45.86           C  
ANISOU 3250  CB  ALA A 406     4918   4744   7760  -1780    627    428       C  
ATOM   3251  C   ALA A 406      29.340   2.518   8.003  1.00 43.92           C  
ANISOU 3251  C   ALA A 406     4081   5401   7204  -1474     48    980       C  
ATOM   3252  O   ALA A 406      28.219   2.670   8.500  1.00 43.03           O  
ANISOU 3252  O   ALA A 406     3984   4258   8104  -1489    100    953       O  
ATOM   3253  N   ALA A 407      30.358   1.941   8.651  1.00 47.42           N  
ANISOU 3253  N   ALA A 407     2904   6662   8449  -1531    -69    661       N  
ATOM   3254  CA  ALA A 407      30.238   1.281   9.978  1.00 52.08           C  
ANISOU 3254  CA  ALA A 407     5014   6217   8555  -1785  -1139    775       C  
ATOM   3255  CB  ALA A 407      31.613   0.885  10.470  1.00 53.90           C  
ANISOU 3255  CB  ALA A 407     5124   6402   8951  -1937  -1587    361       C  
ATOM   3256  C   ALA A 407      29.531   2.185  11.003  1.00 53.23           C  
ANISOU 3256  C   ALA A 407     6535   5155   8534  -2293  -2143   -163       C  
ATOM   3257  O   ALA A 407      28.663   1.717  11.748  1.00 53.07           O  
ANISOU 3257  O   ALA A 407     7858   4153   8153  -2186  -2698    159       O  
ATOM   3258  N   GLY A 408      29.908   3.471  11.044  1.00 56.47           N  
ANISOU 3258  N   GLY A 408     7461   5485   8510  -2808  -2315   -322       N  
ATOM   3259  CA  GLY A 408      29.311   4.468  11.962  1.00 50.15           C  
ANISOU 3259  CA  GLY A 408     7596   4181   7276  -3513  -2752   -132       C  
ATOM   3260  C   GLY A 408      27.810   4.619  11.756  1.00 53.64           C  
ANISOU 3260  C   GLY A 408     8627   5230   6524   -736  -2227     87       C  
ATOM   3261  O   GLY A 408      27.032   4.780  12.718  1.00 61.35           O  
ANISOU 3261  O   GLY A 408    11498   4882   6930    957  -1818    658       O  
ATOM   3262  N   ASN A 409      27.390   4.559  10.492  1.00 43.68           N  
ANISOU 3262  N   ASN A 409     7027   3628   5940  -1076  -1434    584       N  
ATOM   3263  CA  ASN A 409      26.002   4.782  10.128  1.00 40.94           C  
ANISOU 3263  CA  ASN A 409     6493   3400   5659   -929   -235    865       C  
ATOM   3264  CB  ASN A 409      25.890   5.385   8.732  1.00 42.32           C  
ANISOU 3264  CB  ASN A 409     6648   3455   5974  -1023    359   1458       C  
ATOM   3265  CG  ASN A 409      26.356   6.823   8.711  1.00 46.68           C  
ANISOU 3265  CG  ASN A 409     8108   3219   6408   -914   -111   1124       C  
ATOM   3266  OD1 ASN A 409      26.272   7.515   9.725  1.00 50.54           O  
ANISOU 3266  OD1 ASN A 409     9123   3614   6463   -649    117   1147       O  
ATOM   3267  ND2 ASN A 409      26.858   7.275   7.573  1.00 52.17           N  
ANISOU 3267  ND2 ASN A 409     8076   4530   7214  -1675    518   1283       N  
ATOM   3268  C   ASN A 409      25.188   3.486  10.227  1.00 32.73           C  
ANISOU 3268  C   ASN A 409     4594   3116   4725   -309    -64    597       C  
ATOM   3269  O   ASN A 409      23.959   3.544  10.253  1.00 30.12           O  
ANISOU 3269  O   ASN A 409     4736   3400   3308      6   -157    632       O  
ATOM   3270  N   LYS A 410      25.854   2.327  10.282  1.00 27.60           N  
ANISOU 3270  N   LYS A 410     3561   3002   3921   -576    354    654       N  
ATOM   3271  CA  LYS A 410      25.126   1.056  10.396  1.00 24.73           C  
ANISOU 3271  CA  LYS A 410     2492   2980   3924   -352    451    397       C  
ATOM   3272  CB  LYS A 410      26.066  -0.151  10.338  1.00 25.59           C  
ANISOU 3272  CB  LYS A 410     2295   2959   4466   -602    629    450       C  
ATOM   3273  CG  LYS A 410      26.600  -0.450   8.943  1.00 27.18           C  
ANISOU 3273  CG  LYS A 410     2383   3408   4533   -732    856     87       C  
ATOM   3274  CD  LYS A 410      27.451  -1.698   8.880  1.00 29.60           C  
ANISOU 3274  CD  LYS A 410     2720   3898   4627   -549    505     64       C  
ATOM   3275  CE  LYS A 410      28.254  -1.829   7.602  1.00 32.42           C  
ANISOU 3275  CE  LYS A 410     3088   4520   4709   -472    679   -307       C  
ATOM   3276  NZ  LYS A 410      27.411  -1.840   6.376  1.00 30.64           N  
ANISOU 3276  NZ  LYS A 410     3321   4337   3982   -625   1134   -445       N  
ATOM   3277  C   LYS A 410      24.298   1.053  11.677  1.00 22.60           C  
ANISOU 3277  C   LYS A 410     1892   3025   3667   -384    -46    204       C  
ATOM   3278  O   LYS A 410      23.134   0.683  11.657  1.00 22.49           O  
ANISOU 3278  O   LYS A 410     1734   3293   3516   -380    225     55       O  
ATOM   3279  N   PHE A 411      24.901   1.493  12.779  1.00 23.01           N  
ANISOU 3279  N   PHE A 411     2379   2822   3541   -425    -31     49       N  
ATOM   3280  CA  PHE A 411      24.194   1.510  14.041  1.00 22.16           C  
ANISOU 3280  CA  PHE A 411     2291   2826   3302   -769   -212    -35       C  
ATOM   3281  CB  PHE A 411      25.110   1.930  15.193  1.00 23.56           C  
ANISOU 3281  CB  PHE A 411     2715   2947   3289   -761   -313    -55       C  
ATOM   3282  CG  PHE A 411      24.337   2.026  16.478  1.00 24.02           C  
ANISOU 3282  CG  PHE A 411     2643   3185   3298   -657   -253   -135       C  
ATOM   3283  CD1 PHE A 411      23.852   0.877  17.083  1.00 24.42           C  
ANISOU 3283  CD1 PHE A 411     3377   2830   3072   -505   -221   -253       C  
ATOM   3284  CE1 PHE A 411      23.088   0.956  18.232  1.00 25.16           C  
ANISOU 3284  CE1 PHE A 411     3529   2966   3063   -160   -195     58       C  
ATOM   3285  CZ  PHE A 411      22.783   2.179  18.778  1.00 25.86           C  
ANISOU 3285  CZ  PHE A 411     3535   2772   3516   -284   -371     97       C  
ATOM   3286  CD2 PHE A 411      23.987   3.252  17.013  1.00 25.08           C  
ANISOU 3286  CD2 PHE A 411     3154   2916   3456   -579   -424     75       C  
ATOM   3287  CE2 PHE A 411      23.239   3.326  18.176  1.00 27.53           C  
ANISOU 3287  CE2 PHE A 411     3507   3211   3739   -400   -131    199       C  
ATOM   3288  C   PHE A 411      22.987   2.455  13.974  1.00 19.95           C  
ANISOU 3288  C   PHE A 411     2223   2460   2893   -855     25   -153       C  
ATOM   3289  O   PHE A 411      21.889   2.090  14.385  1.00 22.17           O  
ANISOU 3289  O   PHE A 411     2123   3330   2968  -1058   -222    224       O  
ATOM   3290  N   LYS A 412      23.199   3.666  13.450  1.00 23.67           N  
ANISOU 3290  N   LYS A 412     2829   2701   3462   -934   -282    149       N  
ATOM   3291  CA  LYS A 412      22.151   4.698  13.409  1.00 23.73           C  
ANISOU 3291  CA  LYS A 412     2558   2872   3585   -907     72    -42       C  
ATOM   3292  CB  LYS A 412      22.703   6.001  12.818  1.00 29.34           C  
ANISOU 3292  CB  LYS A 412     3431   2740   4976  -1303    102    -49       C  
ATOM   3293  CG  LYS A 412      23.703   6.706  13.728  1.00 39.61           C  
ANISOU 3293  CG  LYS A 412     4680   4225   6142  -1559   -417   -480       C  
ATOM   3294  CD  LYS A 412      24.276   8.015  13.201  1.00 46.61           C  
ANISOU 3294  CD  LYS A 412     5815   4632   7262  -2133     79   -245       C  
ATOM   3295  CE  LYS A 412      25.077   8.734  14.270  1.00 54.34           C  
ANISOU 3295  CE  LYS A 412     6978   5832   7834  -2074   -400   -797       C  
ATOM   3296  NZ  LYS A 412      25.631  10.029  13.804  1.00 57.72           N  
ANISOU 3296  NZ  LYS A 412     7641   5790   8496  -2286   -376   -981       N  
ATOM   3297  C   LYS A 412      20.932   4.197  12.617  1.00 22.94           C  
ANISOU 3297  C   LYS A 412     2593   2597   3525   -733     58     78       C  
ATOM   3298  O   LYS A 412      19.806   4.587  12.905  1.00 24.72           O  
ANISOU 3298  O   LYS A 412     2741   2796   3854   -524    105   -264       O  
ATOM   3299  N   GLU A 413      21.177   3.366  11.596  1.00 20.97           N  
ANISOU 3299  N   GLU A 413     2268   2353   3344   -634     38    169       N  
ATOM   3300  CA  GLU A 413      20.122   2.918  10.693  1.00 21.16           C  
ANISOU 3300  CA  GLU A 413     2263   2420   3354   -845     79    146       C  
ATOM   3301  CB  GLU A 413      20.655   2.779   9.277  1.00 24.05           C  
ANISOU 3301  CB  GLU A 413     2570   3246   3319  -1067    232    449       C  
ATOM   3302  CG  GLU A 413      21.150   4.118   8.752  1.00 29.84           C  
ANISOU 3302  CG  GLU A 413     4035   3280   4021  -1270    283    518       C  
ATOM   3303  CD  GLU A 413      21.442   4.201   7.270  1.00 35.34           C  
ANISOU 3303  CD  GLU A 413     4781   4504   4140  -1082    563    556       C  
ATOM   3304  OE1 GLU A 413      20.994   3.315   6.531  1.00 41.67           O  
ANISOU 3304  OE1 GLU A 413     5673   5084   5073  -1343    280     93       O  
ATOM   3305  OE2 GLU A 413      22.114   5.169   6.867  1.00 45.32           O  
ANISOU 3305  OE2 GLU A 413     6740   4875   5602  -1461    600   1286       O  
ATOM   3306  C   GLU A 413      19.459   1.619  11.165  1.00 18.72           C  
ANISOU 3306  C   GLU A 413     2177   2205   2729   -529    189     50       C  
ATOM   3307  O   GLU A 413      18.392   1.283  10.646  1.00 18.23           O  
ANISOU 3307  O   GLU A 413     2081   2122   2723   -458     91    108       O  
ATOM   3308  N   ALA A 414      20.066   0.913  12.122  1.00 16.51           N  
ANISOU 3308  N   ALA A 414     1784   2202   2285   -511    315   -136       N  
ATOM   3309  CA  ALA A 414      19.555  -0.388  12.547  1.00 15.16           C  
ANISOU 3309  CA  ALA A 414     1663   2033   2063   -359    218   -322       C  
ATOM   3310  CB  ALA A 414      20.562  -1.093  13.417  1.00 15.78           C  
ANISOU 3310  CB  ALA A 414     1581   2366   2048   -287    383   -231       C  
ATOM   3311  C   ALA A 414      18.223  -0.224  13.278  1.00 15.01           C  
ANISOU 3311  C   ALA A 414     1788   2070   1844   -381    218   -186       C  
ATOM   3312  O   ALA A 414      18.056   0.692  14.114  1.00 16.68           O  
ANISOU 3312  O   ALA A 414     1873   2131   2331   -336    348   -474       O  
ATOM   3313  N   ILE A 415      17.312  -1.162  12.992  1.00 13.40           N  
ANISOU 3313  N   ILE A 415     1394   1658   2038    -60    180   -144       N  
ATOM   3314  CA  ILE A 415      15.996  -1.221  13.635  1.00 12.81           C  
ANISOU 3314  CA  ILE A 415     1481   1531   1853   -134    190   -211       C  
ATOM   3315  CB  ILE A 415      14.861  -0.959  12.635  1.00 13.21           C  
ANISOU 3315  CB  ILE A 415     1605   1611   1803    -51    176    -53       C  
ATOM   3316  CG1 ILE A 415      14.992   0.450  12.048  1.00 15.10           C  
ANISOU 3316  CG1 ILE A 415     1764   1756   2214     -3    235    206       C  
ATOM   3317  CG2 ILE A 415      13.490  -1.212  13.280  1.00 13.62           C  
ANISOU 3317  CG2 ILE A 415     1538   1745   1889    125    132     43       C  
ATOM   3318  CD1 ILE A 415      14.057   0.736  10.906  1.00 16.82           C  
ANISOU 3318  CD1 ILE A 415     1801   2239   2348    -30    220    447       C  
ATOM   3319  C   ILE A 415      15.867  -2.590  14.290  1.00 12.76           C  
ANISOU 3319  C   ILE A 415     1468   1589   1788    -47     45   -127       C  
ATOM   3320  O   ILE A 415      16.191  -3.578  13.661  1.00 14.13           O  
ANISOU 3320  O   ILE A 415     1839   1742   1785    -90    151   -273       O  
ATOM   3321  N   PHE A 416      15.354  -2.614  15.523  1.00 11.58           N  
ANISOU 3321  N   PHE A 416     1318   1376   1703    -93    -20   -247       N  
ATOM   3322  CA  PHE A 416      15.192  -3.845  16.291  1.00 12.17           C  
ANISOU 3322  CA  PHE A 416     1513   1306   1803     95    -64   -179       C  
ATOM   3323  CB  PHE A 416      16.054  -3.820  17.555  1.00 12.76           C  
ANISOU 3323  CB  PHE A 416     1452   1651   1745   -180    -63   -266       C  
ATOM   3324  CG  PHE A 416      17.531  -3.809  17.238  1.00 14.36           C  
ANISOU 3324  CG  PHE A 416     1396   1995   2064   -186   -194   -336       C  
ATOM   3325  CD1 PHE A 416      18.203  -2.616  17.037  1.00 15.61           C  
ANISOU 3325  CD1 PHE A 416     1805   2017   2107   -254   -379   -214       C  
ATOM   3326  CE1 PHE A 416      19.542  -2.612  16.688  1.00 16.08           C  
ANISOU 3326  CE1 PHE A 416     1794   2056   2258   -419   -241   -305       C  
ATOM   3327  CZ  PHE A 416      20.224  -3.800  16.525  1.00 16.09           C  
ANISOU 3327  CZ  PHE A 416     1409   2420   2283   -290     44   -206       C  
ATOM   3328  CD2 PHE A 416      18.229  -4.997  17.089  1.00 14.13           C  
ANISOU 3328  CD2 PHE A 416     1406   2121   1840    -66   -155   -149       C  
ATOM   3329  CE2 PHE A 416      19.575  -4.989  16.748  1.00 15.64           C  
ANISOU 3329  CE2 PHE A 416     1453   2186   2303    -21   -154   -237       C  
ATOM   3330  C   PHE A 416      13.729  -4.061  16.673  1.00 12.85           C  
ANISOU 3330  C   PHE A 416     1641   1506   1733    -52     16    -27       C  
ATOM   3331  O   PHE A 416      12.934  -3.114  16.781  1.00 12.94           O  
ANISOU 3331  O   PHE A 416     1540   1491   1886   -152    221   -139       O  
ATOM   3332  N   GLY A 417      13.362  -5.320  16.900  1.00 12.00           N  
ANISOU 3332  N   GLY A 417     1518   1279   1761    144    128   -322       N  
ATOM   3333  CA  GLY A 417      12.079  -5.591  17.528  1.00 12.51           C  
ANISOU 3333  CA  GLY A 417     1544   1454   1753    211     73   -119       C  
ATOM   3334  C   GLY A 417      11.956  -4.851  18.851  1.00 12.78           C  
ANISOU 3334  C   GLY A 417     1614   1531   1710    -89    -94   -125       C  
ATOM   3335  O   GLY A 417      12.949  -4.628  19.557  1.00 13.58           O  
ANISOU 3335  O   GLY A 417     1529   1967   1663   -145    -56     38       O  
ATOM   3336  N   ALA A 418      10.727  -4.477  19.208  1.00 12.31           N  
ANISOU 3336  N   ALA A 418     1475   1747   1453    -86   -174   -162       N  
ATOM   3337  CA  ALA A 418      10.473  -3.750  20.453  1.00 13.63           C  
ANISOU 3337  CA  ALA A 418     1830   1839   1508    -94   -250   -180       C  
ATOM   3338  CB  ALA A 418       9.020  -3.333  20.531  1.00 15.30           C  
ANISOU 3338  CB  ALA A 418     1892   2370   1549    129   -258   -122       C  
ATOM   3339  C   ALA A 418      10.870  -4.579  21.678  1.00 13.04           C  
ANISOU 3339  C   ALA A 418     1748   1731   1473   -143   -183   -174       C  
ATOM   3340  O   ALA A 418      11.199  -3.995  22.695  1.00 15.20           O  
ANISOU 3340  O   ALA A 418     2406   1791   1577    -94   -331   -221       O  
ATOM   3341  N   GLY A 419      10.830  -5.918  21.570  1.00 12.51           N  
ANISOU 3341  N   GLY A 419     1752   1756   1243      6   -158   -193       N  
ATOM   3342  CA  GLY A 419      11.306  -6.811  22.616  1.00 12.74           C  
ANISOU 3342  CA  GLY A 419     1584   1789   1464    -51   -112    -88       C  
ATOM   3343  C   GLY A 419      10.158  -7.545  23.314  1.00 12.28           C  
ANISOU 3343  C   GLY A 419     1739   1551   1374    -88    -66   -116       C  
ATOM   3344  O   GLY A 419       9.012  -7.516  22.853  1.00 12.70           O  
ANISOU 3344  O   GLY A 419     1616   1780   1429    -58     86   -123       O  
ATOM   3345  N   SER A 420      10.508  -8.313  24.354  1.00 12.49           N  
ANISOU 3345  N   SER A 420     1529   1925   1290   -225   -231   -103       N  
ATOM   3346  CA  SER A 420       9.683  -9.423  24.846  1.00 12.50           C  
ANISOU 3346  CA  SER A 420     1614   1748   1385    -33    -99    -44       C  
ATOM   3347  CB  SER A 420      10.566 -10.580  25.271  1.00 12.17           C  
ANISOU 3347  CB  SER A 420     1486   1693   1443    -51   -113     46       C  
ATOM   3348  OG  SER A 420      11.601 -10.867  24.359  1.00 12.46           O  
ANISOU 3348  OG  SER A 420     1501   1679   1554    -29   -130    112       O  
ATOM   3349  C   SER A 420       8.788  -9.056  26.033  1.00 11.81           C  
ANISOU 3349  C   SER A 420     1264   1845   1378   -101   -198    -80       C  
ATOM   3350  O   SER A 420       9.201  -8.362  26.962  1.00 13.14           O  
ANISOU 3350  O   SER A 420     1717   1788   1488   -291    -43   -207       O  
ATOM   3351  N   VAL A 421       7.624  -9.703  26.081  1.00 11.66           N  
ANISOU 3351  N   VAL A 421     1406   1562   1462   -108   -214   -148       N  
ATOM   3352  CA  VAL A 421       6.865  -9.901  27.321  1.00 12.20           C  
ANISOU 3352  CA  VAL A 421     1603   1617   1413      5   -253   -105       C  
ATOM   3353  CB  VAL A 421       5.599  -9.028  27.437  1.00 12.62           C  
ANISOU 3353  CB  VAL A 421     1656   1520   1619     24   -188   -241       C  
ATOM   3354  CG1 VAL A 421       4.900  -9.269  28.766  1.00 13.19           C  
ANISOU 3354  CG1 VAL A 421     1628   1637   1745    264   -126   -310       C  
ATOM   3355  CG2 VAL A 421       5.934  -7.567  27.229  1.00 13.25           C  
ANISOU 3355  CG2 VAL A 421     1683   1515   1834     55   -335   -262       C  
ATOM   3356  C   VAL A 421       6.499 -11.381  27.330  1.00 12.13           C  
ANISOU 3356  C   VAL A 421     1616   1600   1393     70   -129     49       C  
ATOM   3357  O   VAL A 421       5.906 -11.883  26.359  1.00 12.57           O  
ANISOU 3357  O   VAL A 421     1814   1558   1404     75    -19    -51       O  
ATOM   3358  N   ILE A 422       6.887 -12.059  28.410  1.00 11.88           N  
ANISOU 3358  N   ILE A 422     1724   1606   1182    161    -97    -41       N  
ATOM   3359  CA  ILE A 422       6.606 -13.485  28.550  1.00 11.83           C  
ANISOU 3359  CA  ILE A 422     1532   1607   1356    135    -81    -12       C  
ATOM   3360  CB  ILE A 422       7.870 -14.305  28.842  1.00 12.18           C  
ANISOU 3360  CB  ILE A 422     1635   1493   1496    221    -64   -141       C  
ATOM   3361  CG1 ILE A 422       8.912 -14.099  27.738  1.00 12.65           C  
ANISOU 3361  CG1 ILE A 422     1769   1610   1425    477      4     28       C  
ATOM   3362  CG2 ILE A 422       7.494 -15.773  29.022  1.00 12.92           C  
ANISOU 3362  CG2 ILE A 422     1744   1595   1568    225   -118     92       C  
ATOM   3363  CD1 ILE A 422      10.277 -14.675  28.068  1.00 13.72           C  
ANISOU 3363  CD1 ILE A 422     1921   1749   1540    540    -32    106       C  
ATOM   3364  C   ILE A 422       5.546 -13.687  29.636  1.00 11.45           C  
ANISOU 3364  C   ILE A 422     1550   1552   1245    218   -121     37       C  
ATOM   3365  O   ILE A 422       5.813 -13.468  30.822  1.00 12.70           O  
ANISOU 3365  O   ILE A 422     1771   1853   1198     78   -135    198       O  
ATOM   3366  N   PHE A 423       4.356 -14.116  29.197  1.00 10.91           N  
ANISOU 3366  N   PHE A 423     1522   1503   1120    114    -20     31       N  
ATOM   3367  CA  PHE A 423       3.256 -14.478  30.096  1.00 11.12           C  
ANISOU 3367  CA  PHE A 423     1553   1535   1136    132    -78     -2       C  
ATOM   3368  CB  PHE A 423       1.929 -14.138  29.421  1.00 11.48           C  
ANISOU 3368  CB  PHE A 423     1415   1558   1388    310     78     78       C  
ATOM   3369  CG  PHE A 423       1.687 -12.656  29.223  1.00 11.50           C  
ANISOU 3369  CG  PHE A 423     1559   1424   1383    167     99   -105       C  
ATOM   3370  CD1 PHE A 423       1.175 -11.878  30.250  1.00 12.90           C  
ANISOU 3370  CD1 PHE A 423     1967   1649   1285    402     15    -77       C  
ATOM   3371  CE1 PHE A 423       0.958 -10.525  30.073  1.00 13.17           C  
ANISOU 3371  CE1 PHE A 423     2056   1590   1357    303     52   -107       C  
ATOM   3372  CZ  PHE A 423       1.201  -9.940  28.851  1.00 12.28           C  
ANISOU 3372  CZ  PHE A 423     1805   1441   1416    234    263   -139       C  
ATOM   3373  CD2 PHE A 423       1.936 -12.050  28.007  1.00 12.12           C  
ANISOU 3373  CD2 PHE A 423     1630   1580   1393    368     29    -99       C  
ATOM   3374  CE2 PHE A 423       1.677 -10.706  27.815  1.00 12.76           C  
ANISOU 3374  CE2 PHE A 423     1993   1541   1315    269    214   -108       C  
ATOM   3375  C   PHE A 423       3.331 -15.977  30.370  1.00 12.03           C  
ANISOU 3375  C   PHE A 423     1757   1559   1254    129      2     48       C  
ATOM   3376  O   PHE A 423       3.425 -16.775  29.430  1.00 12.66           O  
ANISOU 3376  O   PHE A 423     1931   1501   1375    111    -43     41       O  
ATOM   3377  N   PHE A 424       3.278 -16.372  31.649  1.00 11.72           N  
ANISOU 3377  N   PHE A 424     1891   1317   1243    262    -15    -71       N  
ATOM   3378  CA  PHE A 424       3.241 -17.787  32.006  1.00 12.43           C  
ANISOU 3378  CA  PHE A 424     1962   1406   1354    213     94     49       C  
ATOM   3379  CB  PHE A 424       4.643 -18.385  32.187  1.00 13.13           C  
ANISOU 3379  CB  PHE A 424     2019   1378   1588    340    167     92       C  
ATOM   3380  CG  PHE A 424       5.387 -17.986  33.432  1.00 13.89           C  
ANISOU 3380  CG  PHE A 424     2046   1454   1777    312    -99    192       C  
ATOM   3381  CD1 PHE A 424       5.231 -18.695  34.604  1.00 15.81           C  
ANISOU 3381  CD1 PHE A 424     2398   1873   1734    148    -75    227       C  
ATOM   3382  CE1 PHE A 424       5.918 -18.345  35.756  1.00 16.42           C  
ANISOU 3382  CE1 PHE A 424     2332   2169   1735    220   -209    284       C  
ATOM   3383  CZ  PHE A 424       6.740 -17.257  35.765  1.00 15.56           C  
ANISOU 3383  CZ  PHE A 424     2003   2355   1553    162   -270    165       C  
ATOM   3384  CD2 PHE A 424       6.256 -16.907  33.441  1.00 15.38           C  
ANISOU 3384  CD2 PHE A 424     2285   1780   1775    172    -35     58       C  
ATOM   3385  CE2 PHE A 424       6.904 -16.525  34.608  1.00 15.67           C  
ANISOU 3385  CE2 PHE A 424     2029   1959   1964    120   -263    291       C  
ATOM   3386  C   PHE A 424       2.386 -17.981  33.251  1.00 11.86           C  
ANISOU 3386  C   PHE A 424     1721   1343   1439    392     92     32       C  
ATOM   3387  O   PHE A 424       2.291 -17.093  34.095  1.00 13.01           O  
ANISOU 3387  O   PHE A 424     2058   1565   1320    400     48    -22       O  
ATOM   3388  N   ARG A 425       1.752 -19.158  33.308  1.00 12.79           N  
ANISOU 3388  N   ARG A 425     1948   1340   1570    248    164    -90       N  
ATOM   3389  CA  ARG A 425       0.894 -19.560  34.391  1.00 12.94           C  
ANISOU 3389  CA  ARG A 425     2042   1463   1410    370     45    -41       C  
ATOM   3390  CB  ARG A 425      -0.371 -20.221  33.847  1.00 12.71           C  
ANISOU 3390  CB  ARG A 425     2020   1480   1325    251    125     78       C  
ATOM   3391  CG  ARG A 425      -1.220 -19.333  32.956  1.00 13.69           C  
ANISOU 3391  CG  ARG A 425     1995   1737   1470    330     33     84       C  
ATOM   3392  CD  ARG A 425      -2.371 -20.134  32.352  1.00 13.92           C  
ANISOU 3392  CD  ARG A 425     1921   1880   1488    295     25    143       C  
ATOM   3393  NE  ARG A 425      -3.193 -19.383  31.426  1.00 15.36           N  
ANISOU 3393  NE  ARG A 425     2148   2209   1479    407     67    237       N  
ATOM   3394  CZ  ARG A 425      -4.230 -18.616  31.736  1.00 14.89           C  
ANISOU 3394  CZ  ARG A 425     1993   1864   1798    237   -208    381       C  
ATOM   3395  NH1 ARG A 425      -4.599 -18.463  32.994  1.00 17.93           N  
ANISOU 3395  NH1 ARG A 425     2543   2446   1822    153    192    529       N  
ATOM   3396  NH2 ARG A 425      -4.896 -18.020  30.769  1.00 17.74           N  
ANISOU 3396  NH2 ARG A 425     2430   2334   1977     41   -450    784       N  
ATOM   3397  C   ARG A 425       1.632 -20.556  35.276  1.00 12.43           C  
ANISOU 3397  C   ARG A 425     2075   1390   1257    315     24   -110       C  
ATOM   3398  O   ARG A 425       2.525 -21.274  34.817  1.00 13.26           O  
ANISOU 3398  O   ARG A 425     2145   1421   1472    485     36     65       O  
ATOM   3399  N   PRO A 426       1.201 -20.740  36.533  1.00 13.13           N  
ANISOU 3399  N   PRO A 426     2220   1511   1256    647    111     77       N  
ATOM   3400  CA  PRO A 426       1.800 -21.783  37.356  1.00 13.43           C  
ANISOU 3400  CA  PRO A 426     2024   1663   1414    677     82    178       C  
ATOM   3401  CB  PRO A 426       1.071 -21.702  38.696  1.00 16.19           C  
ANISOU 3401  CB  PRO A 426     2457   2296   1398    709    177     97       C  
ATOM   3402  CG  PRO A 426      -0.046 -20.745  38.503  1.00 16.82           C  
ANISOU 3402  CG  PRO A 426     2546   2234   1609    737    428    168       C  
ATOM   3403  CD  PRO A 426       0.204 -19.939  37.255  1.00 13.77           C  
ANISOU 3403  CD  PRO A 426     2205   1641   1387    729     19    -26       C  
ATOM   3404  C   PRO A 426       1.674 -23.174  36.719  1.00 13.04           C  
ANISOU 3404  C   PRO A 426     1993   1668   1292    540    109    166       C  
ATOM   3405  O   PRO A 426       2.614 -23.980  36.848  1.00 14.43           O  
ANISOU 3405  O   PRO A 426     1885   1900   1695    563    -23    242       O  
ATOM   3406  N   SER A 427       0.577 -23.420  35.988  1.00 13.03           N  
ANISOU 3406  N   SER A 427     2032   1380   1537    342    122    232       N  
ATOM   3407  CA  SER A 427       0.397 -24.719  35.330  1.00 13.68           C  
ANISOU 3407  CA  SER A 427     2236   1401   1557     80    269    278       C  
ATOM   3408  CB  SER A 427      -1.033 -24.907  34.827  1.00 14.82           C  
ANISOU 3408  CB  SER A 427     2357   1593   1679     65    256    147       C  
ATOM   3409  OG  SER A 427      -1.470 -23.796  34.073  1.00 16.87           O  
ANISOU 3409  OG  SER A 427     2720   1809   1881    145     77    301       O  
ATOM   3410  C   SER A 427       1.422 -24.942  34.214  1.00 13.58           C  
ANISOU 3410  C   SER A 427     2245   1370   1543    238    196    127       C  
ATOM   3411  O   SER A 427       1.748 -26.090  33.889  1.00 17.01           O  
ANISOU 3411  O   SER A 427     2937   1537   1989    193    535   -101       O  
ATOM   3412  N   ASP A 428       1.978 -23.871  33.656  1.00 12.44           N  
ANISOU 3412  N   ASP A 428     1977   1306   1444    412    130    241       N  
ATOM   3413  CA  ASP A 428       2.986 -24.007  32.591  1.00 12.97           C  
ANISOU 3413  CA  ASP A 428     2003   1487   1438    355    134     58       C  
ATOM   3414  CB  ASP A 428       3.258 -22.663  31.911  1.00 12.90           C  
ANISOU 3414  CB  ASP A 428     1933   1451   1515    108    -17    -17       C  
ATOM   3415  CG  ASP A 428       2.077 -22.150  31.096  1.00 13.55           C  
ANISOU 3415  CG  ASP A 428     2349   1371   1426    204   -205    -41       C  
ATOM   3416  OD1 ASP A 428       1.349 -22.978  30.517  1.00 16.27           O  
ANISOU 3416  OD1 ASP A 428     2486   1762   1933     60   -447   -189       O  
ATOM   3417  OD2 ASP A 428       1.863 -20.931  31.090  1.00 13.57           O  
ANISOU 3417  OD2 ASP A 428     2269   1390   1497    274    170     68       O  
ATOM   3418  C   ASP A 428       4.304 -24.574  33.126  1.00 12.80           C  
ANISOU 3418  C   ASP A 428     2033   1470   1359    370    162    135       C  
ATOM   3419  O   ASP A 428       5.137 -25.054  32.354  1.00 14.20           O  
ANISOU 3419  O   ASP A 428     2096   1747   1551    241    350    -34       O  
ATOM   3420  N   LEU A 429       4.509 -24.481  34.440  1.00 13.60           N  
ANISOU 3420  N   LEU A 429     1979   1824   1362    576    138    -45       N  
ATOM   3421  CA  LEU A 429       5.801 -24.836  35.065  1.00 15.02           C  
ANISOU 3421  CA  LEU A 429     2003   1990   1714    740    167    179       C  
ATOM   3422  CB  LEU A 429       5.920 -24.145  36.423  1.00 15.35           C  
ANISOU 3422  CB  LEU A 429     2022   1938   1872    726     91     -4       C  
ATOM   3423  CG  LEU A 429       5.946 -22.624  36.415  1.00 16.14           C  
ANISOU 3423  CG  LEU A 429     2284   1989   1860    757    -70     57       C  
ATOM   3424  CD1 LEU A 429       5.780 -22.115  37.837  1.00 17.16           C  
ANISOU 3424  CD1 LEU A 429     2312   2318   1888    620    -83     -6       C  
ATOM   3425  CD2 LEU A 429       7.233 -22.114  35.792  1.00 17.38           C  
ANISOU 3425  CD2 LEU A 429     2410   2070   2124    609    -35    -21       C  
ATOM   3426  C   LEU A 429       5.959 -26.343  35.269  1.00 15.21           C  
ANISOU 3426  C   LEU A 429     2013   1958   1805    592    339    247       C  
ATOM   3427  O   LEU A 429       7.058 -26.777  35.512  1.00 16.51           O  
ANISOU 3427  O   LEU A 429     2270   2125   1877    876    187    232       O  
ATOM   3428  N   GLY A 430       4.866 -27.118  35.212  1.00 14.77           N  
ANISOU 3428  N   GLY A 430     1905   2005   1702    575    299    348       N  
ATOM   3429  CA  GLY A 430       4.931 -28.565  35.380  1.00 16.38           C  
ANISOU 3429  CA  GLY A 430     2268   2072   1882    863    376    384       C  
ATOM   3430  C   GLY A 430       5.531 -28.974  36.719  1.00 17.13           C  
ANISOU 3430  C   GLY A 430     2577   2276   1654    907    613    447       C  
ATOM   3431  O   GLY A 430       6.321 -29.948  36.797  1.00 20.18           O  
ANISOU 3431  O   GLY A 430     3175   2351   2141   1117    537    318       O  
ATOM   3432  N   LEU A 431       5.153 -28.257  37.778  1.00 16.82           N  
ANISOU 3432  N   LEU A 431     2325   2466   1598    885    506    398       N  
ATOM   3433  CA  LEU A 431       5.779 -28.450  39.084  1.00 18.28           C  
ANISOU 3433  CA  LEU A 431     2563   2550   1832    934    277    484       C  
ATOM   3434  CB  LEU A 431       5.291 -27.389  40.071  1.00 17.04           C  
ANISOU 3434  CB  LEU A 431     2322   2543   1607    888     21    405       C  
ATOM   3435  CG  LEU A 431       5.692 -25.953  39.742  1.00 19.31           C  
ANISOU 3435  CG  LEU A 431     2827   2615   1893    771    313    596       C  
ATOM   3436  CD1 LEU A 431       4.988 -24.993  40.685  1.00 21.79           C  
ANISOU 3436  CD1 LEU A 431     3095   2848   2334    556    462    201       C  
ATOM   3437  CD2 LEU A 431       7.192 -25.752  39.772  1.00 22.17           C  
ANISOU 3437  CD2 LEU A 431     3152   3076   2194    476    206    470       C  
ATOM   3438  C   LEU A 431       5.429 -29.826  39.627  1.00 19.99           C  
ANISOU 3438  C   LEU A 431     2886   2412   2297   1160    291    527       C  
ATOM   3439  O   LEU A 431       4.290 -30.263  39.548  1.00 21.50           O  
ANISOU 3439  O   LEU A 431     3425   2233   2510    785    246    605       O  
ATOM   3440  N   LYS A 432       6.428 -30.462  40.243  1.00 24.07           N  
ANISOU 3440  N   LYS A 432     3420   2932   2793   1500    385   1161       N  
ATOM   3441  CA  LYS A 432       6.179 -31.705  40.971  1.00 26.25           C  
ANISOU 3441  CA  LYS A 432     4129   2905   2937   1398    857   1035       C  
ATOM   3442  CB  LYS A 432       7.498 -32.390  41.336  1.00 34.11           C  
ANISOU 3442  CB  LYS A 432     4357   4609   3993   1758    524   1167       C  
ATOM   3443  CG  LYS A 432       8.417 -31.663  42.310  1.00 40.96           C  
ANISOU 3443  CG  LYS A 432     4438   5287   5837   1825    140    542       C  
ATOM   3444  CD  LYS A 432       9.666 -32.464  42.672  1.00 49.77           C  
ANISOU 3444  CD  LYS A 432     5256   6374   7279   2560   -341    817       C  
ATOM   3445  CE  LYS A 432       9.338 -33.755  43.395  1.00 55.82           C  
ANISOU 3445  CE  LYS A 432     5886   6850   8473   1931     44    841       C  
ATOM   3446  NZ  LYS A 432      10.498 -34.301  44.140  1.00 60.94           N  
ANISOU 3446  NZ  LYS A 432     6287   7911   8956   1929   -459    730       N  
ATOM   3447  C   LYS A 432       5.233 -31.444  42.155  1.00 23.11           C  
ANISOU 3447  C   LYS A 432     3814   2483   2483   1365    484   1130       C  
ATOM   3448  O   LYS A 432       4.468 -32.333  42.519  1.00 24.50           O  
ANISOU 3448  O   LYS A 432     3967   2673   2668   1263    802    961       O  
ATOM   3449  N   ASP A 433       5.291 -30.245  42.755  1.00 22.31           N  
ANISOU 3449  N   ASP A 433     3307   2545   2625   1107    457   1209       N  
ATOM   3450  CA  ASP A 433       4.391 -29.897  43.850  1.00 20.09           C  
ANISOU 3450  CA  ASP A 433     2981   2158   2494   1148    165    977       C  
ATOM   3451  CB  ASP A 433       4.959 -28.770  44.713  1.00 19.80           C  
ANISOU 3451  CB  ASP A 433     2498   2494   2532   1173    106    767       C  
ATOM   3452  CG  ASP A 433       4.118 -28.472  45.944  1.00 21.69           C  
ANISOU 3452  CG  ASP A 433     3060   2702   2479    943    197    595       C  
ATOM   3453  OD1 ASP A 433       3.020 -29.059  46.063  1.00 22.70           O  
ANISOU 3453  OD1 ASP A 433     3043   3010   2570   1003     51    714       O  
ATOM   3454  OD2 ASP A 433       4.573 -27.660  46.785  1.00 25.57           O  
ANISOU 3454  OD2 ASP A 433     3020   3397   3295    536   -138    207       O  
ATOM   3455  C   ASP A 433       3.014 -29.540  43.269  1.00 20.16           C  
ANISOU 3455  C   ASP A 433     2685   2287   2687    958    212    697       C  
ATOM   3456  O   ASP A 433       2.777 -28.415  42.830  1.00 19.96           O  
ANISOU 3456  O   ASP A 433     2747   2442   2394   1070     34    655       O  
ATOM   3457  N   TYR A 434       2.099 -30.518  43.271  1.00 20.75           N  
ANISOU 3457  N   TYR A 434     2752   2280   2851   1031    175    668       N  
ATOM   3458  CA  TYR A 434       0.754 -30.370  42.688  1.00 20.26           C  
ANISOU 3458  CA  TYR A 434     2790   2036   2871    716    169    568       C  
ATOM   3459  CB  TYR A 434       0.067 -31.733  42.591  1.00 23.30           C  
ANISOU 3459  CB  TYR A 434     3184   2077   3591    569     94    270       C  
ATOM   3460  CG  TYR A 434       0.162 -32.564  43.848  1.00 26.70           C  
ANISOU 3460  CG  TYR A 434     3927   1851   4364    802    135    698       C  
ATOM   3461  CD1 TYR A 434      -0.622 -32.276  44.958  1.00 27.91           C  
ANISOU 3461  CD1 TYR A 434     3976   2206   4421    479    167    480       C  
ATOM   3462  CE1 TYR A 434      -0.531 -33.019  46.121  1.00 29.93           C  
ANISOU 3462  CE1 TYR A 434     4319   1954   5095    604    314   1037       C  
ATOM   3463  CZ  TYR A 434       0.336 -34.100  46.176  1.00 29.31           C  
ANISOU 3463  CZ  TYR A 434     4095   2176   4865    658    374   1154       C  
ATOM   3464  OH  TYR A 434       0.418 -34.841  47.317  1.00 36.88           O  
ANISOU 3464  OH  TYR A 434     6022   3150   4837    333   -237   1391       O  
ATOM   3465  CE2 TYR A 434       1.119 -34.415  45.074  1.00 30.94           C  
ANISOU 3465  CE2 TYR A 434     4709   2045   4999    759    340    616       C  
ATOM   3466  CD2 TYR A 434       1.036 -33.640  43.926  1.00 28.33           C  
ANISOU 3466  CD2 TYR A 434     3844   2163   4758   1001    552    486       C  
ATOM   3467  C   TYR A 434      -0.103 -29.394  43.511  1.00 19.86           C  
ANISOU 3467  C   TYR A 434     2929   2079   2536    555    -18    226       C  
ATOM   3468  O   TYR A 434      -1.192 -29.013  43.067  1.00 21.69           O  
ANISOU 3468  O   TYR A 434     3200   2228   2812    682   -350    -93       O  
ATOM   3469  N   ASN A 435       0.366 -28.981  44.699  1.00 17.99           N  
ANISOU 3469  N   ASN A 435     2488   2009   2335    513    -45    439       N  
ATOM   3470  CA  ASN A 435      -0.401 -28.002  45.511  1.00 18.32           C  
ANISOU 3470  CA  ASN A 435     2500   2131   2330    577     21    489       C  
ATOM   3471  CB  ASN A 435       0.033 -28.033  46.977  1.00 19.14           C  
ANISOU 3471  CB  ASN A 435     2569   2388   2313    376    -44    547       C  
ATOM   3472  CG  ASN A 435      -0.316 -29.339  47.649  1.00 23.46           C  
ANISOU 3472  CG  ASN A 435     3203   2480   3231    516    105    790       C  
ATOM   3473  OD1 ASN A 435      -1.427 -29.830  47.474  1.00 23.84           O  
ANISOU 3473  OD1 ASN A 435     3133   2450   3473    711    137    935       O  
ATOM   3474  ND2 ASN A 435       0.607 -29.883  48.425  1.00 30.26           N  
ANISOU 3474  ND2 ASN A 435     4119   3640   3738    997   -250   1089       N  
ATOM   3475  C   ASN A 435      -0.261 -26.568  44.985  1.00 17.30           C  
ANISOU 3475  C   ASN A 435     2456   2160   1955    562     35    411       C  
ATOM   3476  O   ASN A 435      -1.053 -25.701  45.372  1.00 17.59           O  
ANISOU 3476  O   ASN A 435     2611   1996   2075    564     31    482       O  
ATOM   3477  N   VAL A 436       0.746 -26.307  44.146  1.00 15.95           N  
ANISOU 3477  N   VAL A 436     2156   1878   2027    766    -90    445       N  
ATOM   3478  CA  VAL A 436       0.957 -24.984  43.595  1.00 15.65           C  
ANISOU 3478  CA  VAL A 436     2362   1923   1659    646    -68    348       C  
ATOM   3479  CB  VAL A 436       2.435 -24.729  43.246  1.00 16.08           C  
ANISOU 3479  CB  VAL A 436     2343   1994   1771    689    -61    435       C  
ATOM   3480  CG1 VAL A 436       2.615 -23.345  42.634  1.00 16.47           C  
ANISOU 3480  CG1 VAL A 436     2505   2044   1706    679     57    421       C  
ATOM   3481  CG2 VAL A 436       3.342 -24.906  44.453  1.00 17.45           C  
ANISOU 3481  CG2 VAL A 436     2414   2216   1998   1009   -112    554       C  
ATOM   3482  C   VAL A 436       0.028 -24.809  42.388  1.00 15.24           C  
ANISOU 3482  C   VAL A 436     2238   1824   1728    610    -86    181       C  
ATOM   3483  O   VAL A 436       0.347 -25.183  41.275  1.00 17.20           O  
ANISOU 3483  O   VAL A 436     2506   2106   1921    605    181      0       O  
ATOM   3484  N   MET A 437      -1.148 -24.263  42.683  1.00 14.78           N  
ANISOU 3484  N   MET A 437     2332   1794   1486    673     13   -111       N  
ATOM   3485  CA  MET A 437      -2.245 -24.105  41.731  1.00 14.26           C  
ANISOU 3485  CA  MET A 437     2050   1814   1550    723     84    162       C  
ATOM   3486  CB  MET A 437      -3.400 -25.069  42.038  1.00 16.98           C  
ANISOU 3486  CB  MET A 437     2455   1975   2022    540    -94    342       C  
ATOM   3487  CG  MET A 437      -3.043 -26.530  41.903  1.00 19.22           C  
ANISOU 3487  CG  MET A 437     2601   2043   2656    687      1    425       C  
ATOM   3488  SD  MET A 437      -4.399 -27.616  42.408  1.00 22.91           S  
ANISOU 3488  SD  MET A 437     3198   2233   3274    345     68    403       S  
ATOM   3489  CE  MET A 437      -5.497 -27.418  41.014  1.00 25.94           C  
ANISOU 3489  CE  MET A 437     3524   2826   3506    676   -281    119       C  
ATOM   3490  C   MET A 437      -2.757 -22.670  41.815  1.00 14.43           C  
ANISOU 3490  C   MET A 437     2230   1767   1484    649     70    -20       C  
ATOM   3491  O   MET A 437      -2.831 -22.093  42.905  1.00 14.90           O  
ANISOU 3491  O   MET A 437     2326   1898   1435    600     78     37       O  
ATOM   3492  N   ALA A 438      -3.192 -22.115  40.678  1.00 13.19           N  
ANISOU 3492  N   ALA A 438     2020   1615   1374    447    158   -126       N  
ATOM   3493  CA  ALA A 438      -3.796 -20.789  40.669  1.00 12.91           C  
ANISOU 3493  CA  ALA A 438     1762   1543   1597    346     17     44       C  
ATOM   3494  CB  ALA A 438      -4.354 -20.488  39.305  1.00 14.45           C  
ANISOU 3494  CB  ALA A 438     2027   1752   1710    460    -38    103       C  
ATOM   3495  C   ALA A 438      -4.892 -20.722  41.733  1.00 12.97           C  
ANISOU 3495  C   ALA A 438     2023   1598   1307    340    -16    102       C  
ATOM   3496  O   ALA A 438      -5.758 -21.607  41.799  1.00 14.01           O  
ANISOU 3496  O   ALA A 438     2211   1677   1433    330     93    215       O  
ATOM   3497  N   ASN A 439      -4.843 -19.654  42.539  1.00 13.06           N  
ANISOU 3497  N   ASN A 439     2092   1470   1399    310    129    117       N  
ATOM   3498  CA  ASN A 439      -5.820 -19.331  43.590  1.00 13.82           C  
ANISOU 3498  CA  ASN A 439     2219   1621   1408    249    157     33       C  
ATOM   3499  CB  ASN A 439      -7.250 -19.435  43.064  1.00 14.78           C  
ANISOU 3499  CB  ASN A 439     2302   1847   1464    333      3    -31       C  
ATOM   3500  CG  ASN A 439      -7.514 -18.412  41.987  1.00 15.22           C  
ANISOU 3500  CG  ASN A 439     2218   1939   1624    480    -46     50       C  
ATOM   3501  OD1 ASN A 439      -7.035 -17.285  42.116  1.00 16.21           O  
ANISOU 3501  OD1 ASN A 439     2277   2026   1855    369     67    220       O  
ATOM   3502  ND2 ASN A 439      -8.277 -18.787  40.964  1.00 15.95           N  
ANISOU 3502  ND2 ASN A 439     2245   1930   1884    482   -265    -40       N  
ATOM   3503  C   ASN A 439      -5.643 -20.191  44.849  1.00 14.99           C  
ANISOU 3503  C   ASN A 439     2387   1665   1642    366    134    167       C  
ATOM   3504  O   ASN A 439      -6.474 -20.102  45.778  1.00 16.85           O  
ANISOU 3504  O   ASN A 439     2854   1801   1745    373    482    430       O  
ATOM   3505  N   ALA A 440      -4.568 -20.986  44.922  1.00 14.37           N  
ANISOU 3505  N   ALA A 440     2556   1742   1161    585    163     54       N  
ATOM   3506  CA  ALA A 440      -4.294 -21.713  46.171  1.00 14.91           C  
ANISOU 3506  CA  ALA A 440     2479   1814   1370    396    137    281       C  
ATOM   3507  CB  ALA A 440      -3.277 -22.793  45.956  1.00 16.35           C  
ANISOU 3507  CB  ALA A 440     2793   1997   1421    535     92    157       C  
ATOM   3508  C   ALA A 440      -3.794 -20.722  47.222  1.00 15.99           C  
ANISOU 3508  C   ALA A 440     2528   2011   1535    498    116     15       C  
ATOM   3509  O   ALA A 440      -2.946 -19.864  46.922  1.00 17.38           O  
ANISOU 3509  O   ALA A 440     2634   2312   1655    501    388    197       O  
ATOM   3510  N   ASN A 441      -4.263 -20.895  48.460  1.00 17.42           N  
ANISOU 3510  N   ASN A 441     2779   2072   1765    498    420    142       N  
ATOM   3511  CA AASN A 441      -3.819 -20.078  49.591  0.50 18.50           C  
ANISOU 3511  CA AASN A 441     2796   2526   1705    559    154    119       C  
ATOM   3512  CA BASN A 441      -3.834 -20.089  49.612  0.50 18.34           C  
ANISOU 3512  CA BASN A 441     2815   2399   1752    475    117    208       C  
ATOM   3513  CB AASN A 441      -4.898 -19.938  50.657  0.50 19.86           C  
ANISOU 3513  CB AASN A 441     2965   2806   1776    580    234   -187       C  
ATOM   3514  CB BASN A 441      -4.934 -19.988  50.675  0.50 19.60           C  
ANISOU 3514  CB BASN A 441     2957   2570   1919    437    236      9       C  
ATOM   3515  CG AASN A 441      -4.507 -18.893  51.678  0.50 23.91           C  
ANISOU 3515  CG AASN A 441     3555   3467   2060    560    211   -678       C  
ATOM   3516  CG BASN A 441      -5.204 -21.278  51.430  0.50 22.96           C  
ANISOU 3516  CG BASN A 441     3606   2866   2251     28    210    138       C  
ATOM   3517  OD1AASN A 441      -3.586 -18.106  51.435  0.50 26.89           O  
ANISOU 3517  OD1AASN A 441     3518   4246   2452    602    177   -848       O  
ATOM   3518  OD1BASN A 441      -4.810 -22.348  50.990  0.50 22.38           O  
ANISOU 3518  OD1BASN A 441     3269   3038   2196    -61    241     76       O  
ATOM   3519  ND2AASN A 441      -5.191 -18.885  52.808  0.50 27.87           N  
ANISOU 3519  ND2AASN A 441     3964   4397   2228    271    408   -232       N  
ATOM   3520  ND2BASN A 441      -5.845 -21.192  52.589  0.50 28.81           N  
ANISOU 3520  ND2BASN A 441     3977   3997   2971    410    647   -164       N  
ATOM   3521  C   ASN A 441      -2.538 -20.669  50.199  1.00 19.48           C  
ANISOU 3521  C   ASN A 441     2730   2907   1761    595    286    313       C  
ATOM   3522  O   ASN A 441      -2.402 -20.809  51.398  1.00 27.65           O  
ANISOU 3522  O   ASN A 441     3652   4914   1937   1084    263    432       O  
ATOM   3523  N   LYS A 442      -1.589 -20.989  49.340  1.00 19.36           N  
ANISOU 3523  N   LYS A 442     2484   3076   1796    554    188    218       N  
ATOM   3524  CA  LYS A 442      -0.340 -21.597  49.710  1.00 19.71           C  
ANISOU 3524  CA  LYS A 442     2765   2590   2133    519     34    370       C  
ATOM   3525  CB  LYS A 442      -0.060 -22.816  48.831  1.00 20.27           C  
ANISOU 3525  CB  LYS A 442     3163   2427   2110    356     47    458       C  
ATOM   3526  CG  LYS A 442       1.282 -23.479  49.130  1.00 23.55           C  
ANISOU 3526  CG  LYS A 442     3349   2940   2656    573    -53    564       C  
ATOM   3527  CD  LYS A 442       1.604 -24.638  48.226  1.00 25.38           C  
ANISOU 3527  CD  LYS A 442     3904   2904   2835    771   -194    466       C  
ATOM   3528  CE  LYS A 442       3.058 -25.043  48.311  1.00 27.07           C  
ANISOU 3528  CE  LYS A 442     4090   3250   2945   1127   -427    679       C  
ATOM   3529  NZ  LYS A 442       3.443 -25.512  49.663  1.00 30.69           N  
ANISOU 3529  NZ  LYS A 442     4938   3805   2914    975   -508    760       N  
ATOM   3530  C   LYS A 442       0.778 -20.581  49.464  1.00 19.17           C  
ANISOU 3530  C   LYS A 442     2960   2635   1686    404      7    311       C  
ATOM   3531  O   LYS A 442       0.845 -20.013  48.375  1.00 20.47           O  
ANISOU 3531  O   LYS A 442     3388   2772   1615    728    176    318       O  
ATOM   3532  N   SER A 443       1.623 -20.358  50.481  1.00 20.56           N  
ANISOU 3532  N   SER A 443     3161   2996   1655    351   -177    198       N  
ATOM   3533  CA ASER A 443       2.781 -19.483  50.341  0.50 21.29           C  
ANISOU 3533  CA ASER A 443     3072   3133   1882    358   -175    182       C  
ATOM   3534  CA BSER A 443       2.777 -19.480  50.335  0.50 22.36           C  
ANISOU 3534  CA BSER A 443     3080   3312   2100    361   -100    265       C  
ATOM   3535  CB ASER A 443       3.373 -19.145  51.684  0.50 21.88           C  
ANISOU 3535  CB ASER A 443     3098   3233   1983    395   -160   -114       C  
ATOM   3536  CB BSER A 443       3.358 -19.109  51.675  0.50 25.67           C  
ANISOU 3536  CB BSER A 443     3440   3906   2406    219   -356     51       C  
ATOM   3537  OG ASER A 443       2.416 -18.493  52.505  0.50 20.55           O  
ANISOU 3537  OG ASER A 443     2893   3492   1422    320   -292   -213       O  
ATOM   3538  OG BSER A 443       3.837 -20.250  52.359  0.50 28.18           O  
ANISOU 3538  OG BSER A 443     3431   4666   2607    554   -425    363       O  
ATOM   3539  C   SER A 443       3.826 -20.136  49.425  1.00 21.09           C  
ANISOU 3539  C   SER A 443     3038   3105   1868    272   -179    306       C  
ATOM   3540  O   SER A 443       4.144 -21.347  49.561  1.00 23.03           O  
ANISOU 3540  O   SER A 443     3210   3218   2321    609    -84    402       O  
ATOM   3541  N   ILE A 444       4.385 -19.337  48.511  1.00 19.99           N  
ANISOU 3541  N   ILE A 444     2514   3112   1966    276   -121    234       N  
ATOM   3542  CA  ILE A 444       5.475 -19.778  47.652  1.00 18.90           C  
ANISOU 3542  CA  ILE A 444     2528   2818   1832    345   -137    278       C  
ATOM   3543  CB  ILE A 444       4.981 -20.113  46.237  1.00 20.22           C  
ANISOU 3543  CB  ILE A 444     2657   3135   1890    345   -171    156       C  
ATOM   3544  CG1 ILE A 444       4.383 -18.896  45.512  1.00 20.59           C  
ANISOU 3544  CG1 ILE A 444     2941   3134   1746    352   -180    235       C  
ATOM   3545  CG2 ILE A 444       4.038 -21.302  46.281  1.00 21.37           C  
ANISOU 3545  CG2 ILE A 444     2864   3363   1889    211   -436    206       C  
ATOM   3546  CD1 ILE A 444       4.159 -19.089  44.028  1.00 21.84           C  
ANISOU 3546  CD1 ILE A 444     3346   3182   1770    -41   -146    255       C  
ATOM   3547  C   ILE A 444       6.561 -18.698  47.612  1.00 19.69           C  
ANISOU 3547  C   ILE A 444     2508   3070   1903    341   -243     67       C  
ATOM   3548  O   ILE A 444       6.328 -17.533  47.942  1.00 22.77           O  
ANISOU 3548  O   ILE A 444     2890   3131   2630    544     23     57       O  
ATOM   3549  N   ASN A 445       7.766 -19.125  47.223  1.00 20.24           N  
ANISOU 3549  N   ASN A 445     2743   3088   1858    476    -37     35       N  
ATOM   3550  CA  ASN A 445       8.874 -18.216  46.927  1.00 21.01           C  
ANISOU 3550  CA  ASN A 445     2991   3077   1914    450    194    322       C  
ATOM   3551  CB  ASN A 445      10.060 -18.449  47.865  1.00 26.22           C  
ANISOU 3551  CB  ASN A 445     3874   3950   2136    165   -384    342       C  
ATOM   3552  CG  ASN A 445       9.735 -18.171  49.320  1.00 31.22           C  
ANISOU 3552  CG  ASN A 445     5049   4573   2240    330   -684     24       C  
ATOM   3553  OD1 ASN A 445       9.336 -17.069  49.674  1.00 40.00           O  
ANISOU 3553  OD1 ASN A 445     6293   5123   3781   1044  -1232   -287       O  
ATOM   3554  ND2 ASN A 445       9.931 -19.160  50.175  1.00 40.54           N  
ANISOU 3554  ND2 ASN A 445     5819   5428   4154    453   -935   1020       N  
ATOM   3555  C   ASN A 445       9.269 -18.453  45.467  1.00 20.23           C  
ANISOU 3555  C   ASN A 445     3125   2700   1858    570     86    338       C  
ATOM   3556  O   ASN A 445       9.365 -19.592  45.047  1.00 22.94           O  
ANISOU 3556  O   ASN A 445     4195   2703   1818    500    342    298       O  
ATOM   3557  N   MET A 446       9.445 -17.375  44.693  1.00 18.73           N  
ANISOU 3557  N   MET A 446     2829   2561   1728    524   -145    208       N  
ATOM   3558  CA  MET A 446       9.833 -17.477  43.294  1.00 18.80           C  
ANISOU 3558  CA  MET A 446     2674   2682   1785    524    -43    247       C  
ATOM   3559  CB  MET A 446       8.687 -17.010  42.377  1.00 19.17           C  
ANISOU 3559  CB  MET A 446     2420   2783   2077    654    -92    153       C  
ATOM   3560  CG  MET A 446       8.993 -17.057  40.884  1.00 20.81           C  
ANISOU 3560  CG  MET A 446     2165   3587   2155    453   -127    112       C  
ATOM   3561  SD  MET A 446       7.651 -16.418  39.798  1.00 22.98           S  
ANISOU 3561  SD  MET A 446     2728   3734   2270    545   -313    232       S  
ATOM   3562  CE  MET A 446       6.612 -17.864  39.873  1.00 22.34           C  
ANISOU 3562  CE  MET A 446     3274   3114   2098    516   -368    875       C  
ATOM   3563  C   MET A 446      11.057 -16.601  43.024  1.00 17.70           C  
ANISOU 3563  C   MET A 446     2282   2648   1793    586   -252     -7       C  
ATOM   3564  O   MET A 446      11.189 -15.508  43.569  1.00 19.26           O  
ANISOU 3564  O   MET A 446     2579   2729   2009    527   -141     87       O  
ATOM   3565  N   GLN A 447      11.929 -17.085  42.136  1.00 16.75           N  
ANISOU 3565  N   GLN A 447     2467   2409   1486    458   -163    264       N  
ATOM   3566  CA  GLN A 447      13.031 -16.313  41.610  1.00 16.92           C  
ANISOU 3566  CA  GLN A 447     2390   2430   1606    414   -219    -21       C  
ATOM   3567  CB  GLN A 447      14.334 -16.796  42.249  1.00 20.40           C  
ANISOU 3567  CB  GLN A 447     2294   2919   2536    622   -206    -51       C  
ATOM   3568  CG  GLN A 447      15.557 -15.938  41.940  1.00 23.75           C  
ANISOU 3568  CG  GLN A 447     2747   3329   2946    325   -690    609       C  
ATOM   3569  CD  GLN A 447      16.682 -16.265  42.903  1.00 25.60           C  
ANISOU 3569  CD  GLN A 447     3288   3458   2977    536  -1091    373       C  
ATOM   3570  OE1 GLN A 447      17.018 -17.419  43.116  1.00 30.85           O  
ANISOU 3570  OE1 GLN A 447     3959   3635   4127    679  -1657    308       O  
ATOM   3571  NE2 GLN A 447      17.283 -15.253  43.505  1.00 28.12           N  
ANISOU 3571  NE2 GLN A 447     3268   4236   3180   -102   -853    388       N  
ATOM   3572  C   GLN A 447      13.013 -16.481  40.093  1.00 18.34           C  
ANISOU 3572  C   GLN A 447     2725   2605   1636    305   -371     34       C  
ATOM   3573  O   GLN A 447      12.759 -17.582  39.592  1.00 20.41           O  
ANISOU 3573  O   GLN A 447     3541   2181   2032    230     88     74       O  
ATOM   3574  N   VAL A 448      13.268 -15.387  39.382  1.00 17.20           N  
ANISOU 3574  N   VAL A 448     2286   2478   1769    211   -268    -56       N  
ATOM   3575  CA  VAL A 448      13.252 -15.379  37.919  1.00 16.64           C  
ANISOU 3575  CA  VAL A 448     2290   2319   1712    231   -284      0       C  
ATOM   3576  CB  VAL A 448      12.103 -14.519  37.364  1.00 16.84           C  
ANISOU 3576  CB  VAL A 448     2242   2443   1710    322    -81     -6       C  
ATOM   3577  CG1 VAL A 448      12.182 -14.384  35.839  1.00 17.23           C  
ANISOU 3577  CG1 VAL A 448     2256   2594   1695    361   -395    -46       C  
ATOM   3578  CG2 VAL A 448      10.764 -15.091  37.803  1.00 16.80           C  
ANISOU 3578  CG2 VAL A 448     2334   2497   1550    302    -30     53       C  
ATOM   3579  C   VAL A 448      14.606 -14.882  37.414  1.00 16.15           C  
ANISOU 3579  C   VAL A 448     1931   2437   1765    320   -481    -60       C  
ATOM   3580  O   VAL A 448      15.063 -13.802  37.817  1.00 17.24           O  
ANISOU 3580  O   VAL A 448     2379   2419   1752    181   -416    -90       O  
ATOM   3581  N   GLN A 449      15.204 -15.667  36.514  1.00 16.48           N  
ANISOU 3581  N   GLN A 449     2014   2520   1728    111   -430   -125       N  
ATOM   3582  CA  GLN A 449      16.435 -15.326  35.808  1.00 17.34           C  
ANISOU 3582  CA  GLN A 449     2141   2568   1878    402   -248     73       C  
ATOM   3583  CB  GLN A 449      17.468 -16.449  35.926  1.00 18.89           C  
ANISOU 3583  CB  GLN A 449     2227   2942   2007    572   -272     31       C  
ATOM   3584  CG  GLN A 449      18.747 -16.160  35.159  1.00 20.64           C  
ANISOU 3584  CG  GLN A 449     2298   3270   2273    533    -99   -124       C  
ATOM   3585  CD  GLN A 449      19.599 -17.393  34.956  1.00 23.29           C  
ANISOU 3585  CD  GLN A 449     2446   3608   2795    983   -310    256       C  
ATOM   3586  OE1 GLN A 449      19.541 -18.042  33.908  1.00 27.00           O  
ANISOU 3586  OE1 GLN A 449     3529   3764   2965   1014     87    132       O  
ATOM   3587  NE2 GLN A 449      20.365 -17.748  35.968  1.00 25.96           N  
ANISOU 3587  NE2 GLN A 449     2277   4541   3045    815   -402    581       N  
ATOM   3588  C   GLN A 449      16.052 -15.122  34.340  1.00 16.50           C  
ANISOU 3588  C   GLN A 449     2133   2407   1728     57   -104    -23       C  
ATOM   3589  O   GLN A 449      15.448 -16.006  33.738  1.00 18.45           O  
ANISOU 3589  O   GLN A 449     3038   2071   1899    -19   -382     43       O  
ATOM   3590  N   ALA A 450      16.436 -13.979  33.769  1.00 15.38           N  
ANISOU 3590  N   ALA A 450     1971   2172   1701    154   -267    -93       N  
ATOM   3591  CA  ALA A 450      16.200 -13.680  32.349  1.00 15.16           C  
ANISOU 3591  CA  ALA A 450     1838   2338   1580    245   -240   -171       C  
ATOM   3592  CB  ALA A 450      15.287 -12.486  32.179  1.00 16.40           C  
ANISOU 3592  CB  ALA A 450     1916   2416   1898    243   -211    -53       C  
ATOM   3593  C   ALA A 450      17.543 -13.403  31.688  1.00 14.71           C  
ANISOU 3593  C   ALA A 450     1738   2093   1755    233   -335   -161       C  
ATOM   3594  O   ALA A 450      18.365 -12.644  32.246  1.00 15.78           O  
ANISOU 3594  O   ALA A 450     1631   2728   1633    -70   -198   -160       O  
ATOM   3595  N   THR A 451      17.749 -14.028  30.518  1.00 14.78           N  
ANISOU 3595  N   THR A 451     1596   2398   1621      6   -295   -130       N  
ATOM   3596  CA  THR A 451      18.896 -13.771  29.685  1.00 15.42           C  
ANISOU 3596  CA  THR A 451     1640   2577   1642    229   -304     -3       C  
ATOM   3597  CB  THR A 451      19.588 -15.077  29.278  1.00 15.56           C  
ANISOU 3597  CB  THR A 451     1648   2497   1768    319   -303    151       C  
ATOM   3598  OG1 THR A 451      19.884 -15.838  30.451  1.00 17.96           O  
ANISOU 3598  OG1 THR A 451     2096   2657   2069    648   -458    311       O  
ATOM   3599  CG2 THR A 451      20.838 -14.846  28.466  1.00 16.65           C  
ANISOU 3599  CG2 THR A 451     1470   2821   2035    698   -215     65       C  
ATOM   3600  C   THR A 451      18.372 -12.999  28.469  1.00 14.63           C  
ANISOU 3600  C   THR A 451     1754   2196   1606    309   -330   -137       C  
ATOM   3601  O   THR A 451      17.383 -13.412  27.856  1.00 14.73           O  
ANISOU 3601  O   THR A 451     1666   2285   1645    234   -313    -72       O  
ATOM   3602  N   PHE A 452      19.035 -11.902  28.099  1.00 14.61           N  
ANISOU 3602  N   PHE A 452     1683   2326   1542    236   -259   -286       N  
ATOM   3603  CA  PHE A 452      18.439 -10.996  27.119  1.00 14.50           C  
ANISOU 3603  CA  PHE A 452     1671   2268   1567    229   -255   -216       C  
ATOM   3604  CB  PHE A 452      17.471 -10.029  27.807  1.00 14.27           C  
ANISOU 3604  CB  PHE A 452     1405   2357   1659     56   -217   -215       C  
ATOM   3605  CG  PHE A 452      18.076  -9.187  28.896  1.00 15.46           C  
ANISOU 3605  CG  PHE A 452     1674   2535   1662     -3   -253   -221       C  
ATOM   3606  CD1 PHE A 452      18.688  -7.984  28.592  1.00 15.91           C  
ANISOU 3606  CD1 PHE A 452     1738   2596   1710     70   -388    -28       C  
ATOM   3607  CE1 PHE A 452      19.208  -7.199  29.608  1.00 17.04           C  
ANISOU 3607  CE1 PHE A 452     1833   2800   1840   -238   -248   -143       C  
ATOM   3608  CZ  PHE A 452      19.225  -7.652  30.913  1.00 18.39           C  
ANISOU 3608  CZ  PHE A 452     2106   2937   1942    -83   -194    -13       C  
ATOM   3609  CD2 PHE A 452      18.115  -9.643  30.207  1.00 16.13           C  
ANISOU 3609  CD2 PHE A 452     1935   2455   1739     -2   -293    -60       C  
ATOM   3610  CE2 PHE A 452      18.646  -8.857  31.222  1.00 16.69           C  
ANISOU 3610  CE2 PHE A 452     1820   2933   1587    -37   -236    -67       C  
ATOM   3611  C   PHE A 452      19.519 -10.237  26.347  1.00 15.56           C  
ANISOU 3611  C   PHE A 452     1633   2372   1905    156   -299    -71       C  
ATOM   3612  O   PHE A 452      20.663 -10.112  26.795  1.00 15.72           O  
ANISOU 3612  O   PHE A 452     1507   2398   2068     94   -131   -141       O  
ATOM   3613  N   VAL A 453      19.106  -9.717  25.176  1.00 14.66           N  
ANISOU 3613  N   VAL A 453     1362   2369   1837     18   -307    -98       N  
ATOM   3614  CA  VAL A 453      19.941  -8.911  24.321  1.00 16.39           C  
ANISOU 3614  CA  VAL A 453     1708   2515   2002    -15      3   -168       C  
ATOM   3615  CB  VAL A 453      20.128  -9.531  22.928  1.00 15.75           C  
ANISOU 3615  CB  VAL A 453     1925   2256   1804    -66     -6    -21       C  
ATOM   3616  CG1 VAL A 453      20.867 -10.863  23.015  1.00 16.51           C  
ANISOU 3616  CG1 VAL A 453     2103   2395   1775      0     46    -85       C  
ATOM   3617  CG2 VAL A 453      18.823  -9.680  22.157  1.00 16.43           C  
ANISOU 3617  CG2 VAL A 453     2035   2341   1863   -100     41   -118       C  
ATOM   3618  C   VAL A 453      19.362  -7.495  24.235  1.00 15.99           C  
ANISOU 3618  C   VAL A 453     1796   2277   2000   -308    -39   -120       C  
ATOM   3619  O   VAL A 453      18.127  -7.305  24.313  1.00 17.16           O  
ANISOU 3619  O   VAL A 453     1844   2456   2221   -361     74   -255       O  
ATOM   3620  N   THR A 454      20.280  -6.516  24.114  1.00 14.73           N  
ANISOU 3620  N   THR A 454     1505   2041   2047   -129    -22   -286       N  
ATOM   3621  CA  THR A 454      19.911  -5.107  24.129  1.00 15.35           C  
ANISOU 3621  CA  THR A 454     1865   2106   1858   -154   -140   -174       C  
ATOM   3622  CB  THR A 454      20.526  -4.427  25.359  1.00 16.60           C  
ANISOU 3622  CB  THR A 454     1927   2416   1961   -235   -391   -129       C  
ATOM   3623  OG1 THR A 454      21.939  -4.635  25.266  1.00 17.52           O  
ANISOU 3623  OG1 THR A 454     1852   2750   2051   -301   -424    -19       O  
ATOM   3624  CG2 THR A 454      19.973  -4.984  26.652  1.00 18.41           C  
ANISOU 3624  CG2 THR A 454     2161   2776   2056   -402   -388    -27       C  
ATOM   3625  C   THR A 454      20.403  -4.413  22.863  1.00 14.67           C  
ANISOU 3625  C   THR A 454     1502   2215   1855   -112    -90   -285       C  
ATOM   3626  O   THR A 454      21.344  -4.840  22.222  1.00 16.39           O  
ANISOU 3626  O   THR A 454     1739   2207   2281      5     78   -383       O  
ATOM   3627  N   PRO A 455      19.737  -3.322  22.448  1.00 16.45           N  
ANISOU 3627  N   PRO A 455     1688   2510   2049     85    -11    -84       N  
ATOM   3628  CA  PRO A 455      20.074  -2.679  21.178  1.00 17.43           C  
ANISOU 3628  CA  PRO A 455     1871   2534   2216   -118     53     -5       C  
ATOM   3629  CB  PRO A 455      18.732  -2.020  20.825  1.00 17.42           C  
ANISOU 3629  CB  PRO A 455     1947   2550   2119   -103   -115    140       C  
ATOM   3630  CG  PRO A 455      18.186  -1.616  22.179  1.00 18.43           C  
ANISOU 3630  CG  PRO A 455     2022   2607   2370     44     46    -55       C  
ATOM   3631  CD  PRO A 455      18.483  -2.811  23.054  1.00 17.14           C  
ANISOU 3631  CD  PRO A 455     1598   2810   2105     18    -26    -62       C  
ATOM   3632  C   PRO A 455      21.219  -1.652  21.165  1.00 17.81           C  
ANISOU 3632  C   PRO A 455     2011   2510   2245   -223   -117   -113       C  
ATOM   3633  O   PRO A 455      21.513  -1.091  20.119  1.00 20.75           O  
ANISOU 3633  O   PRO A 455     2477   3024   2381   -168     14     46       O  
ATOM   3634  N   GLU A 456      21.891  -1.427  22.294  1.00 18.75           N  
ANISOU 3634  N   GLU A 456     2071   2609   2442   -357   -159   -134       N  
ATOM   3635  CA  GLU A 456      22.933  -0.395  22.342  1.00 20.18           C  
ANISOU 3635  CA  GLU A 456     2275   2937   2452   -475     -7   -245       C  
ATOM   3636  CB  GLU A 456      23.344  -0.129  23.792  1.00 21.30           C  
ANISOU 3636  CB  GLU A 456     2428   3226   2439   -490   -201   -154       C  
ATOM   3637  CG  GLU A 456      22.402   0.823  24.506  1.00 23.44           C  
ANISOU 3637  CG  GLU A 456     3019   3083   2801   -453   -134   -298       C  
ATOM   3638  CD  GLU A 456      21.064   0.216  24.875  1.00 23.53           C  
ANISOU 3638  CD  GLU A 456     2880   3531   2526   -510   -179   -664       C  
ATOM   3639  OE1 GLU A 456      21.029  -0.989  25.161  1.00 23.08           O  
ANISOU 3639  OE1 GLU A 456     2674   3618   2478   -747    -79   -524       O  
ATOM   3640  OE2 GLU A 456      20.060   0.954  24.867  1.00 26.70           O  
ANISOU 3640  OE2 GLU A 456     3107   3501   3535   -503   -540   -316       O  
ATOM   3641  C   GLU A 456      24.148  -0.794  21.493  1.00 18.95           C  
ANISOU 3641  C   GLU A 456     1967   2755   2477   -454   -136    -71       C  
ATOM   3642  O   GLU A 456      24.485  -1.981  21.340  1.00 19.12           O  
ANISOU 3642  O   GLU A 456     2206   2648   2410   -426   -215   -215       O  
ATOM   3643  N   ALA A 457      24.794   0.231  20.927  1.00 20.44           N  
ANISOU 3643  N   ALA A 457     2258   2854   2652   -615    139   -134       N  
ATOM   3644  CA  ALA A 457      25.979   0.074  20.117  1.00 20.15           C  
ANISOU 3644  CA  ALA A 457     2261   3027   2367   -628     94   -129       C  
ATOM   3645  CB  ALA A 457      26.435   1.420  19.611  1.00 21.25           C  
ANISOU 3645  CB  ALA A 457     2281   3122   2669   -673    144    -46       C  
ATOM   3646  C   ALA A 457      27.104  -0.578  20.926  1.00 21.77           C  
ANISOU 3646  C   ALA A 457     2099   3314   2859   -611    118     39       C  
ATOM   3647  O   ALA A 457      27.209  -0.383  22.146  1.00 23.27           O  
ANISOU 3647  O   ALA A 457     2504   3334   3003   -721   -192   -168       O  
ATOM   3648  N   ALA A 458      27.972  -1.305  20.219  1.00 21.66           N  
ANISOU 3648  N   ALA A 458     1947   3545   2737   -576    -42   -248       N  
ATOM   3649  CA  ALA A 458      29.242  -1.772  20.797  1.00 22.56           C  
ANISOU 3649  CA  ALA A 458     1736   3791   3042   -632    128   -269       C  
ATOM   3650  CB  ALA A 458      30.099  -2.437  19.737  1.00 23.88           C  
ANISOU 3650  CB  ALA A 458     1855   3950   3268   -415    206   -390       C  
ATOM   3651  C   ALA A 458      29.983  -0.576  21.400  1.00 23.95           C  
ANISOU 3651  C   ALA A 458     2171   3750   3177   -721   -161   -255       C  
ATOM   3652  O   ALA A 458      30.098   0.503  20.775  1.00 26.61           O  
ANISOU 3652  O   ALA A 458     2554   4279   3276  -1334   -122    159       O  
ATOM   3653  N   GLY A 459      30.485  -0.776  22.614  1.00 24.58           N  
ANISOU 3653  N   GLY A 459     2256   3946   3134  -1153    -78    -51       N  
ATOM   3654  CA  GLY A 459      31.247   0.233  23.321  1.00 25.32           C  
ANISOU 3654  CA  GLY A 459     2059   4214   3344   -979   -258   -386       C  
ATOM   3655  C   GLY A 459      30.381   1.191  24.123  1.00 23.91           C  
ANISOU 3655  C   GLY A 459     2313   3780   2991  -1148   -348   -488       C  
ATOM   3656  O   GLY A 459      30.904   2.149  24.674  1.00 28.53           O  
ANISOU 3656  O   GLY A 459     2730   4387   3724  -1435   -260  -1163       O  
ATOM   3657  N   THR A 460      29.065   0.949  24.149  1.00 25.96           N  
ANISOU 3657  N   THR A 460     2270   3950   3644   -996   -268   -572       N  
ATOM   3658  CA  THR A 460      28.096   1.736  24.928  1.00 23.81           C  
ANISOU 3658  CA  THR A 460     2226   3391   3427  -1292   -172   -264       C  
ATOM   3659  CB  THR A 460      27.214   2.623  24.035  1.00 25.16           C  
ANISOU 3659  CB  THR A 460     2548   3823   3186  -1088   -247   -369       C  
ATOM   3660  OG1 THR A 460      26.241   1.808  23.368  1.00 24.76           O  
ANISOU 3660  OG1 THR A 460     2607   3306   3494  -1099   -124   -196       O  
ATOM   3661  CG2 THR A 460      28.040   3.416  23.042  1.00 28.76           C  
ANISOU 3661  CG2 THR A 460     3165   4340   3421  -1288   -270   -129       C  
ATOM   3662  C   THR A 460      27.227   0.784  25.754  1.00 23.11           C  
ANISOU 3662  C   THR A 460     2198   3379   3201   -898     68   -271       C  
ATOM   3663  O   THR A 460      27.256  -0.423  25.594  1.00 25.79           O  
ANISOU 3663  O   THR A 460     2761   3381   3656   -767   -187   -174       O  
ATOM   3664  N   GLY A 461      26.441   1.370  26.643  1.00 23.70           N  
ANISOU 3664  N   GLY A 461     2610   3532   2863   -791    267   -253       N  
ATOM   3665  CA  GLY A 461      25.504   0.616  27.417  1.00 24.51           C  
ANISOU 3665  CA  GLY A 461     2574   3609   3128   -775     91   -160       C  
ATOM   3666  C   GLY A 461      24.396   1.493  27.946  1.00 23.61           C  
ANISOU 3666  C   GLY A 461     2657   3497   2816   -744    213   -125       C  
ATOM   3667  O   GLY A 461      24.347   2.693  27.685  1.00 28.28           O  
ANISOU 3667  O   GLY A 461     3209   3357   4176   -805    550   -245       O  
ATOM   3668  N   ALA A 462      23.494   0.863  28.691  1.00 20.99           N  
ANISOU 3668  N   ALA A 462     2635   2986   2353   -735     76   -172       N  
ATOM   3669  CA  ALA A 462      22.373   1.536  29.301  1.00 21.64           C  
ANISOU 3669  CA  ALA A 462     2636   3208   2375   -639     12   -396       C  
ATOM   3670  CB  ALA A 462      21.335   1.854  28.261  1.00 23.30           C  
ANISOU 3670  CB  ALA A 462     2877   3442   2534   -586    113     27       C  
ATOM   3671  C   ALA A 462      21.793   0.628  30.383  1.00 20.15           C  
ANISOU 3671  C   ALA A 462     2607   2861   2187   -594   -192   -457       C  
ATOM   3672  O   ALA A 462      22.034  -0.577  30.385  1.00 19.91           O  
ANISOU 3672  O   ALA A 462     2166   2935   2462   -574   -260   -561       O  
ATOM   3673  N   HIS A 463      21.018   1.217  31.296  1.00 19.82           N  
ANISOU 3673  N   HIS A 463     2570   2601   2356   -709    -89   -470       N  
ATOM   3674  CA  HIS A 463      20.381   0.475  32.348  1.00 20.12           C  
ANISOU 3674  CA  HIS A 463     2494   2915   2233   -862   -324   -431       C  
ATOM   3675  CB  HIS A 463      20.073   1.393  33.529  1.00 22.70           C  
ANISOU 3675  CB  HIS A 463     2939   3515   2169   -928   -324   -684       C  
ATOM   3676  CG  HIS A 463      21.258   1.773  34.357  1.00 25.84           C  
ANISOU 3676  CG  HIS A 463     2871   4309   2635   -873   -451   -816       C  
ATOM   3677  ND1 HIS A 463      21.997   2.910  34.116  1.00 29.93           N  
ANISOU 3677  ND1 HIS A 463     3381   4724   3265  -1097   -319   -763       N  
ATOM   3678  CE1 HIS A 463      22.961   3.015  35.012  1.00 31.05           C  
ANISOU 3678  CE1 HIS A 463     3962   4459   3378  -1235   -628   -933       C  
ATOM   3679  NE2 HIS A 463      22.864   1.961  35.841  1.00 31.25           N  
ANISOU 3679  NE2 HIS A 463     3767   4931   3176  -1044   -523   -975       N  
ATOM   3680  CD2 HIS A 463      21.815   1.175  35.427  1.00 28.91           C  
ANISOU 3680  CD2 HIS A 463     3382   4854   2746   -904   -478   -722       C  
ATOM   3681  C   HIS A 463      19.092  -0.199  31.848  1.00 18.00           C  
ANISOU 3681  C   HIS A 463     2244   2954   1639   -426   -456   -555       C  
ATOM   3682  O   HIS A 463      18.256   0.427  31.161  1.00 18.80           O  
ANISOU 3682  O   HIS A 463     2188   2903   2050   -512   -578   -365       O  
ATOM   3683  N   TYR A 464      18.935  -1.464  32.242  1.00 18.60           N  
ANISOU 3683  N   TYR A 464     2172   2941   1952   -339   -560   -532       N  
ATOM   3684  CA  TYR A 464      17.767  -2.297  31.978  1.00 17.41           C  
ANISOU 3684  CA  TYR A 464     2140   2870   1604   -388   -380   -457       C  
ATOM   3685  CB  TYR A 464      18.057  -3.428  30.975  1.00 17.52           C  
ANISOU 3685  CB  TYR A 464     2192   2775   1689   -522   -508   -476       C  
ATOM   3686  CG  TYR A 464      18.134  -2.910  29.564  1.00 17.94           C  
ANISOU 3686  CG  TYR A 464     2495   2619   1700   -829   -337   -405       C  
ATOM   3687  CD1 TYR A 464      19.249  -2.209  29.121  1.00 19.39           C  
ANISOU 3687  CD1 TYR A 464     2372   3076   1918   -724   -190   -590       C  
ATOM   3688  CE1 TYR A 464      19.291  -1.643  27.859  1.00 18.89           C  
ANISOU 3688  CE1 TYR A 464     2165   2885   2125   -697     43   -252       C  
ATOM   3689  CZ  TYR A 464      18.194  -1.735  27.022  1.00 19.03           C  
ANISOU 3689  CZ  TYR A 464     2404   2741   2085   -582    -62   -315       C  
ATOM   3690  OH  TYR A 464      18.228  -1.163  25.787  1.00 20.94           O  
ANISOU 3690  OH  TYR A 464     2914   3029   2014   -704    -78   -198       O  
ATOM   3691  CE2 TYR A 464      17.079  -2.430  27.441  1.00 18.26           C  
ANISOU 3691  CE2 TYR A 464     2494   2523   1920   -638   -237   -190       C  
ATOM   3692  CD2 TYR A 464      17.054  -3.000  28.704  1.00 17.83           C  
ANISOU 3692  CD2 TYR A 464     2374   2622   1779   -687   -287   -376       C  
ATOM   3693  C   TYR A 464      17.246  -2.839  33.315  1.00 17.20           C  
ANISOU 3693  C   TYR A 464     2029   2922   1582   -325   -453   -354       C  
ATOM   3694  O   TYR A 464      18.021  -3.162  34.215  1.00 17.68           O  
ANISOU 3694  O   TYR A 464     2279   2656   1783   -110   -528   -289       O  
ATOM   3695  N   LYS A 465      15.921  -2.954  33.395  1.00 17.09           N  
ANISOU 3695  N   LYS A 465     2024   2649   1819   -366   -439   -344       N  
ATOM   3696  CA ALYS A 465      15.228  -3.413  34.582  0.30 16.65           C  
ANISOU 3696  CA ALYS A 465     2122   2553   1651   -223   -410   -391       C  
ATOM   3697  CA BLYS A 465      15.229  -3.414  34.580  0.70 16.93           C  
ANISOU 3697  CA BLYS A 465     2208   2621   1600   -253   -416   -418       C  
ATOM   3698  CB ALYS A 465      14.353  -2.292  35.142  0.30 17.27           C  
ANISOU 3698  CB ALYS A 465     2210   2540   1810   -190   -321   -424       C  
ATOM   3699  CB BLYS A 465      14.338  -2.303  35.134  0.70 19.66           C  
ANISOU 3699  CB BLYS A 465     2568   2796   2103    -65   -155   -523       C  
ATOM   3700  CG ALYS A 465      13.568  -2.643  36.395  0.30 17.38           C  
ANISOU 3700  CG ALYS A 465     2136   2518   1946   -225   -259   -453       C  
ATOM   3701  CG BLYS A 465      13.567  -2.662  36.395  0.70 21.85           C  
ANISOU 3701  CG BLYS A 465     2634   3120   2546   -210     81   -485       C  
ATOM   3702  CD ALYS A 465      12.907  -1.421  36.993  0.30 18.24           C  
ANISOU 3702  CD ALYS A 465     2232   2579   2118   -201    -68   -482       C  
ATOM   3703  CD BLYS A 465      12.546  -1.624  36.782  0.70 25.76           C  
ANISOU 3703  CD BLYS A 465     3089   3543   3153      3    687   -541       C  
ATOM   3704  CE ALYS A 465      12.043  -0.692  35.982  0.30 18.24           C  
ANISOU 3704  CE ALYS A 465     2201   2541   2188   -201    -50   -447       C  
ATOM   3705  CE BLYS A 465      13.149  -0.350  37.322  0.70 27.53           C  
ANISOU 3705  CE BLYS A 465     3371   3640   3447    -79    781   -704       C  
ATOM   3706  NZ ALYS A 465      11.310   0.434  36.606  0.30 19.37           N  
ANISOU 3706  NZ ALYS A 465     2547   2560   2251   -238     24   -568       N  
ATOM   3707  NZ BLYS A 465      12.146   0.431  38.075  0.70 31.37           N  
ANISOU 3707  NZ BLYS A 465     4092   4178   3645    402   1009   -709       N  
ATOM   3708  C   LYS A 465      14.361  -4.631  34.248  1.00 16.66           C  
ANISOU 3708  C   LYS A 465     2263   2453   1612   -235   -334   -320       C  
ATOM   3709  O   LYS A 465      13.438  -4.548  33.423  1.00 17.29           O  
ANISOU 3709  O   LYS A 465     2190   2703   1675   -264   -380   -406       O  
ATOM   3710  N   LEU A 466      14.674  -5.748  34.909  1.00 15.63           N  
ANISOU 3710  N   LEU A 466     1984   2445   1509   -247   -300   -157       N  
ATOM   3711  CA  LEU A 466      13.827  -6.944  34.890  1.00 15.28           C  
ANISOU 3711  CA  LEU A 466     1843   2370   1592   -204   -239   -158       C  
ATOM   3712  CB  LEU A 466      14.662  -8.170  35.281  1.00 16.25           C  
ANISOU 3712  CB  LEU A 466     1990   2451   1732   -151   -360    -22       C  
ATOM   3713  CG  LEU A 466      13.895  -9.449  35.628  1.00 15.70           C  
ANISOU 3713  CG  LEU A 466     1549   2641   1773   -192   -295    -55       C  
ATOM   3714  CD1 LEU A 466      13.093  -9.968  34.446  1.00 16.70           C  
ANISOU 3714  CD1 LEU A 466     2035   2448   1861   -163   -446    -50       C  
ATOM   3715  CD2 LEU A 466      14.836 -10.532  36.130  1.00 17.50           C  
ANISOU 3715  CD2 LEU A 466     1716   3020   1914   -198   -639    -30       C  
ATOM   3716  C   LEU A 466      12.675  -6.716  35.857  1.00 15.34           C  
ANISOU 3716  C   LEU A 466     1764   2435   1629   -313   -331   -177       C  
ATOM   3717  O   LEU A 466      12.909  -6.400  37.036  1.00 16.21           O  
ANISOU 3717  O   LEU A 466     1721   2823   1614    -98   -368   -184       O  
ATOM   3718  N   GLU A 467      11.447  -6.887  35.341  1.00 15.17           N  
ANISOU 3718  N   GLU A 467     1683   2390   1688   -215   -351    103       N  
ATOM   3719  CA  GLU A 467      10.233  -6.778  36.137  1.00 15.41           C  
ANISOU 3719  CA  GLU A 467     1806   2357   1690   -174   -430   -155       C  
ATOM   3720  CB  GLU A 467       9.372  -5.614  35.655  1.00 17.66           C  
ANISOU 3720  CB  GLU A 467     1970   2437   2302   -158   -674    -56       C  
ATOM   3721  CG  GLU A 467       9.941  -4.246  35.994  1.00 20.71           C  
ANISOU 3721  CG  GLU A 467     2389   2570   2907   -295   -769    107       C  
ATOM   3722  CD  GLU A 467       9.034  -3.099  35.586  1.00 23.50           C  
ANISOU 3722  CD  GLU A 467     3132   2554   3242     84   -820   -155       C  
ATOM   3723  OE1 GLU A 467       8.762  -3.001  34.395  1.00 26.13           O  
ANISOU 3723  OE1 GLU A 467     3540   3060   3326    -48   -892    183       O  
ATOM   3724  OE2 GLU A 467       8.564  -2.321  36.480  1.00 27.50           O  
ANISOU 3724  OE2 GLU A 467     3415   3384   3647    250   -366   -322       O  
ATOM   3725  C   GLU A 467       9.459  -8.088  36.026  1.00 14.67           C  
ANISOU 3725  C   GLU A 467     1844   2143   1587     15   -259   -170       C  
ATOM   3726  O   GLU A 467       9.297  -8.613  34.915  1.00 15.34           O  
ANISOU 3726  O   GLU A 467     2094   2387   1346    -39   -116    -83       O  
ATOM   3727  N   VAL A 468       8.971  -8.572  37.169  1.00 14.09           N  
ANISOU 3727  N   VAL A 468     1799   2053   1499     38   -218   -222       N  
ATOM   3728  CA  VAL A 468       8.051  -9.710  37.219  1.00 13.78           C  
ANISOU 3728  CA  VAL A 468     1741   2029   1465    177   -299   -141       C  
ATOM   3729  CB  VAL A 468       8.637 -10.890  38.004  1.00 14.79           C  
ANISOU 3729  CB  VAL A 468     1955   2044   1621    240   -245   -112       C  
ATOM   3730  CG1 VAL A 468       7.641 -12.044  38.050  1.00 15.90           C  
ANISOU 3730  CG1 VAL A 468     2082   2194   1764     86   -240     71       C  
ATOM   3731  CG2 VAL A 468       9.962 -11.303  37.408  1.00 15.68           C  
ANISOU 3731  CG2 VAL A 468     1969   2460   1528    335   -280   -142       C  
ATOM   3732  C   VAL A 468       6.744  -9.221  37.839  1.00 13.87           C  
ANISOU 3732  C   VAL A 468     1789   1966   1513    231   -180   -153       C  
ATOM   3733  O   VAL A 468       6.735  -8.752  38.979  1.00 16.26           O  
ANISOU 3733  O   VAL A 468     2165   2452   1561    357   -111   -248       O  
ATOM   3734  N   PHE A 469       5.669  -9.307  37.055  1.00 13.68           N  
ANISOU 3734  N   PHE A 469     1962   1831   1404    285   -203    -81       N  
ATOM   3735  CA  PHE A 469       4.331  -8.951  37.503  1.00 13.95           C  
ANISOU 3735  CA  PHE A 469     1821   1918   1559    278   -281   -120       C  
ATOM   3736  CB  PHE A 469       3.589  -8.156  36.433  1.00 14.02           C  
ANISOU 3736  CB  PHE A 469     1611   2034   1682    319   -393   -122       C  
ATOM   3737  CG  PHE A 469       4.264  -6.860  36.076  1.00 15.68           C  
ANISOU 3737  CG  PHE A 469     1898   2075   1985    280   -184      1       C  
ATOM   3738  CD1 PHE A 469       5.236  -6.819  35.089  1.00 16.31           C  
ANISOU 3738  CD1 PHE A 469     2153   1967   2077     82    -25    -22       C  
ATOM   3739  CE1 PHE A 469       5.860  -5.629  34.760  1.00 18.11           C  
ANISOU 3739  CE1 PHE A 469     2278   2240   2363    -55   -229    175       C  
ATOM   3740  CZ  PHE A 469       5.533  -4.481  35.443  1.00 19.38           C  
ANISOU 3740  CZ  PHE A 469     2480   2222   2658   -281   -255    -22       C  
ATOM   3741  CD2 PHE A 469       3.947  -5.695  36.752  1.00 17.18           C  
ANISOU 3741  CD2 PHE A 469     2430   1995   2100    277   -182     50       C  
ATOM   3742  CE2 PHE A 469       4.572  -4.502  36.428  1.00 18.11           C  
ANISOU 3742  CE2 PHE A 469     2459   2106   2313     90   -325     96       C  
ATOM   3743  C   PHE A 469       3.496 -10.198  37.781  1.00 13.62           C  
ANISOU 3743  C   PHE A 469     1925   1815   1434    282   -261    -99       C  
ATOM   3744  O   PHE A 469       3.682 -11.218  37.126  1.00 14.34           O  
ANISOU 3744  O   PHE A 469     2042   1802   1605     77   -112   -244       O  
ATOM   3745  N   SER A 470       2.605 -10.089  38.762  1.00 14.46           N  
ANISOU 3745  N   SER A 470     1749   1902   1841    187   -138   -496       N  
ATOM   3746  CA  SER A 470       1.558 -11.067  38.996  1.00 15.04           C  
ANISOU 3746  CA  SER A 470     1902   1918   1894    253    173   -267       C  
ATOM   3747  CB  SER A 470       1.463 -11.491  40.428  1.00 17.55           C  
ANISOU 3747  CB  SER A 470     2033   2451   2183    228      6    123       C  
ATOM   3748  OG  SER A 470       1.161 -10.381  41.250  1.00 19.21           O  
ANISOU 3748  OG  SER A 470     2738   2611   1949    546    156    300       O  
ATOM   3749  C   SER A 470       0.221 -10.493  38.535  1.00 13.82           C  
ANISOU 3749  C   SER A 470     1910   1664   1674    153    124   -179       C  
ATOM   3750  O   SER A 470      -0.068  -9.305  38.693  1.00 14.25           O  
ANISOU 3750  O   SER A 470     1873   1656   1883     24    102   -359       O  
ATOM   3751  N   ILE A 471      -0.618 -11.394  38.050  1.00 13.75           N  
ANISOU 3751  N   ILE A 471     1909   1593   1721    182     25   -258       N  
ATOM   3752  CA  ILE A 471      -2.007 -11.138  37.735  1.00 14.12           C  
ANISOU 3752  CA  ILE A 471     1837   1731   1796    166    106   -495       C  
ATOM   3753  CB  ILE A 471      -2.280 -11.324  36.226  1.00 17.43           C  
ANISOU 3753  CB  ILE A 471     2583   2179   1861    123   -105   -373       C  
ATOM   3754  CG1 ILE A 471      -1.353 -10.417  35.408  1.00 19.19           C  
ANISOU 3754  CG1 ILE A 471     3025   2196   2070    -78   -128   -151       C  
ATOM   3755  CG2 ILE A 471      -3.744 -11.041  35.921  1.00 22.23           C  
ANISOU 3755  CG2 ILE A 471     3029   3236   2180    165   -389   -577       C  
ATOM   3756  CD1 ILE A 471      -0.387 -11.120  34.515  1.00 22.44           C  
ANISOU 3756  CD1 ILE A 471     2969   2398   3156      1    115     29       C  
ATOM   3757  C   ILE A 471      -2.828 -12.099  38.591  1.00 15.31           C  
ANISOU 3757  C   ILE A 471     2208   1559   2048    132     92   -378       C  
ATOM   3758  O   ILE A 471      -2.751 -13.324  38.394  1.00 16.19           O  
ANISOU 3758  O   ILE A 471     2245   1530   2373    -70    582   -474       O  
ATOM   3759  N   ARG A 472      -3.551 -11.559  39.565  1.00 13.75           N  
ANISOU 3759  N   ARG A 472     2095   1243   1884    153     50   -150       N  
ATOM   3760  CA  ARG A 472      -4.316 -12.357  40.495  1.00 14.63           C  
ANISOU 3760  CA  ARG A 472     1969   1527   2062    106    197   -229       C  
ATOM   3761  CB  ARG A 472      -4.045 -11.954  41.941  1.00 15.17           C  
ANISOU 3761  CB  ARG A 472     2164   1660   1939    197     73   -131       C  
ATOM   3762  CG  ARG A 472      -2.696 -12.384  42.483  1.00 15.33           C  
ANISOU 3762  CG  ARG A 472     2276   1684   1863    303     90     -6       C  
ATOM   3763  CD  ARG A 472      -2.609 -11.989  43.935  1.00 16.22           C  
ANISOU 3763  CD  ARG A 472     2501   1738   1920    185     92   -109       C  
ATOM   3764  NE  ARG A 472      -1.550 -12.701  44.616  1.00 18.08           N  
ANISOU 3764  NE  ARG A 472     2403   2414   2052    234    -27   -120       N  
ATOM   3765  CZ  ARG A 472      -0.312 -12.248  44.760  1.00 20.43           C  
ANISOU 3765  CZ  ARG A 472     2338   2654   2770    348   -297    -34       C  
ATOM   3766  NH1 ARG A 472       0.023 -11.092  44.209  1.00 22.36           N  
ANISOU 3766  NH1 ARG A 472     2859   2916   2720    -81     97   -174       N  
ATOM   3767  NH2 ARG A 472       0.587 -12.981  45.402  1.00 22.60           N  
ANISOU 3767  NH2 ARG A 472     2791   3116   2677    575   -457    114       N  
ATOM   3768  C   ARG A 472      -5.818 -12.200  40.249  1.00 14.56           C  
ANISOU 3768  C   ARG A 472     1948   1476   2108    303    252   -189       C  
ATOM   3769  O   ARG A 472      -6.341 -11.123  39.951  1.00 15.79           O  
ANISOU 3769  O   ARG A 472     2165   1471   2360    288    311    -51       O  
ATOM   3770  N   ASP A 473      -6.504 -13.325  40.381  1.00 14.83           N  
ANISOU 3770  N   ASP A 473     2040   1409   2184    267    310   -208       N  
ATOM   3771  CA  ASP A 473      -7.956 -13.383  40.323  1.00 15.46           C  
ANISOU 3771  CA  ASP A 473     2091   1836   1945    371    215    -85       C  
ATOM   3772  CB  ASP A 473      -8.431 -14.824  40.184  1.00 16.01           C  
ANISOU 3772  CB  ASP A 473     2307   1808   1967    236    227    -62       C  
ATOM   3773  CG  ASP A 473      -7.946 -15.548  38.916  1.00 17.43           C  
ANISOU 3773  CG  ASP A 473     2606   1890   2126    423    236   -141       C  
ATOM   3774  OD1 ASP A 473      -7.536 -14.871  37.933  1.00 20.35           O  
ANISOU 3774  OD1 ASP A 473     3002   2239   2489      7    322    -86       O  
ATOM   3775  OD2 ASP A 473      -8.008 -16.801  38.898  1.00 17.95           O  
ANISOU 3775  OD2 ASP A 473     2825   1929   2066    394    -50     93       O  
ATOM   3776  C   ASP A 473      -8.490 -12.687  41.579  1.00 15.05           C  
ANISOU 3776  C   ASP A 473     2084   1739   1893    318    233    -11       C  
ATOM   3777  O   ASP A 473      -8.087 -12.980  42.698  1.00 16.43           O  
ANISOU 3777  O   ASP A 473     2520   2012   1708    357    216   -202       O  
ATOM   3778  N   ASN A 474      -9.376 -11.723  41.361  1.00 14.25           N  
ANISOU 3778  N   ASN A 474     2037   1912   1463    457    133   -112       N  
ATOM   3779  CA  ASN A 474      -9.801 -10.812  42.383  1.00 14.30           C  
ANISOU 3779  CA  ASN A 474     2086   1918   1427    318    233    -39       C  
ATOM   3780  CB  ASN A 474      -8.834  -9.641  42.465  1.00 15.15           C  
ANISOU 3780  CB  ASN A 474     2076   2023   1656    207    176     31       C  
ATOM   3781  CG  ASN A 474      -9.145  -8.683  43.587  1.00 15.80           C  
ANISOU 3781  CG  ASN A 474     2505   1803   1692     31   -272    -69       C  
ATOM   3782  OD1 ASN A 474      -9.122  -9.058  44.755  1.00 18.03           O  
ANISOU 3782  OD1 ASN A 474     2788   2477   1586    202    -46    -38       O  
ATOM   3783  ND2 ASN A 474      -9.435  -7.445  43.223  1.00 17.67           N  
ANISOU 3783  ND2 ASN A 474     3418   1591   1705    271   -462   -178       N  
ATOM   3784  C   ASN A 474     -11.216 -10.360  42.022  1.00 13.20           C  
ANISOU 3784  C   ASN A 474     2004   1649   1360    337    217     52       C  
ATOM   3785  O   ASN A 474     -11.460  -9.986  40.849  1.00 14.24           O  
ANISOU 3785  O   ASN A 474     2056   1917   1437    159    270    195       O  
ATOM   3786  N   LEU A 475     -12.111 -10.369  43.014  1.00 13.43           N  
ANISOU 3786  N   LEU A 475     2117   1564   1421    216    268     88       N  
ATOM   3787  CA  LEU A 475     -13.505 -10.025  42.787  1.00 12.80           C  
ANISOU 3787  CA  LEU A 475     2000   1190   1671    233    441    -96       C  
ATOM   3788  CB  LEU A 475     -14.420 -11.202  43.138  1.00 13.96           C  
ANISOU 3788  CB  LEU A 475     2144   1331   1827    113    235     84       C  
ATOM   3789  CG  LEU A 475     -14.216 -12.487  42.360  1.00 17.16           C  
ANISOU 3789  CG  LEU A 475     2642   1653   2224    -88    405   -246       C  
ATOM   3790  CD1 LEU A 475     -15.277 -13.503  42.735  1.00 18.02           C  
ANISOU 3790  CD1 LEU A 475     2853   1743   2251   -221    350    -30       C  
ATOM   3791  CD2 LEU A 475     -14.151 -12.279  40.876  1.00 19.48           C  
ANISOU 3791  CD2 LEU A 475     3049   2107   2242   -200   -164   -168       C  
ATOM   3792  C   LEU A 475     -13.912  -8.822  43.655  1.00 12.77           C  
ANISOU 3792  C   LEU A 475     2181   1378   1293    316    379    -86       C  
ATOM   3793  O   LEU A 475     -13.461  -8.660  44.801  1.00 14.59           O  
ANISOU 3793  O   LEU A 475     2397   1684   1459    385    209   -145       O  
ATOM   3794  N   THR A 476     -14.813  -8.011  43.096  1.00 12.08           N  
ANISOU 3794  N   THR A 476     1973   1353   1263    240    354    -60       N  
ATOM   3795  CA  THR A 476     -15.461  -6.917  43.803  1.00 12.90           C  
ANISOU 3795  CA  THR A 476     2091   1485   1322    289    365    -91       C  
ATOM   3796  CB  THR A 476     -15.300  -5.610  43.016  1.00 13.31           C  
ANISOU 3796  CB  THR A 476     2260   1359   1437    242    277   -107       C  
ATOM   3797  OG1 THR A 476     -13.907  -5.300  42.960  1.00 13.82           O  
ANISOU 3797  OG1 THR A 476     2137   1451   1661    140    153   -216       O  
ATOM   3798  CG2 THR A 476     -16.062  -4.457  43.620  1.00 13.47           C  
ANISOU 3798  CG2 THR A 476     2331   1382   1404    279    253   -139       C  
ATOM   3799  C   THR A 476     -16.930  -7.296  44.012  1.00 12.77           C  
ANISOU 3799  C   THR A 476     2012   1558   1280    363    288    -22       C  
ATOM   3800  O   THR A 476     -17.585  -7.847  43.113  1.00 13.92           O  
ANISOU 3800  O   THR A 476     2085   1842   1361    124    301   -104       O  
ATOM   3801  N   TYR A 477     -17.424  -7.011  45.211  1.00 12.53           N  
ANISOU 3801  N   TYR A 477     1953   1400   1405    408    407   -136       N  
ATOM   3802  CA  TYR A 477     -18.788  -7.363  45.634  1.00 12.88           C  
ANISOU 3802  CA  TYR A 477     2010   1495   1387    294    337   -142       C  
ATOM   3803  CB  TYR A 477     -18.747  -8.250  46.880  1.00 13.25           C  
ANISOU 3803  CB  TYR A 477     2220   1522   1292    403    501   -174       C  
ATOM   3804  CG  TYR A 477     -17.966  -9.519  46.700  1.00 13.86           C  
ANISOU 3804  CG  TYR A 477     2207   1610   1448    512    398    -79       C  
ATOM   3805  CD1 TYR A 477     -16.607  -9.563  46.939  1.00 15.52           C  
ANISOU 3805  CD1 TYR A 477     2278   1786   1832    565    235     77       C  
ATOM   3806  CE1 TYR A 477     -15.873 -10.719  46.730  1.00 15.42           C  
ANISOU 3806  CE1 TYR A 477     1898   1802   2156    464    492     23       C  
ATOM   3807  CZ  TYR A 477     -16.506 -11.863  46.276  1.00 15.81           C  
ANISOU 3807  CZ  TYR A 477     2350   1696   1960    540    329     39       C  
ATOM   3808  OH  TYR A 477     -15.811 -13.026  46.089  1.00 16.88           O  
ANISOU 3808  OH  TYR A 477     2380   1707   2324    515    518    -57       O  
ATOM   3809  CE2 TYR A 477     -17.862 -11.831  46.028  1.00 15.86           C  
ANISOU 3809  CE2 TYR A 477     2403   1690   1932    520    512     50       C  
ATOM   3810  CD2 TYR A 477     -18.581 -10.666  46.231  1.00 14.46           C  
ANISOU 3810  CD2 TYR A 477     2268   1598   1628    446    348    169       C  
ATOM   3811  C   TYR A 477     -19.560  -6.092  45.949  1.00 12.85           C  
ANISOU 3811  C   TYR A 477     1953   1674   1253    319    498   -199       C  
ATOM   3812  O   TYR A 477     -19.090  -5.261  46.725  1.00 14.58           O  
ANISOU 3812  O   TYR A 477     2351   1674   1513    484    348   -484       O  
ATOM   3813  N   SER A 478     -20.728  -5.950  45.326  1.00 11.90           N  
ANISOU 3813  N   SER A 478     1971   1361   1190    233    391   -154       N  
ATOM   3814  CA  SER A 478     -21.625  -4.840  45.557  1.00 12.66           C  
ANISOU 3814  CA  SER A 478     1923   1371   1513    198    521    -89       C  
ATOM   3815  CB  SER A 478     -22.052  -4.241  44.246  1.00 12.86           C  
ANISOU 3815  CB  SER A 478     1984   1313   1589    121    347    -57       C  
ATOM   3816  OG  SER A 478     -23.058  -3.241  44.417  1.00 12.54           O  
ANISOU 3816  OG  SER A 478     1861   1471   1432    217    425    -69       O  
ATOM   3817  C   SER A 478     -22.848  -5.349  46.329  1.00 13.86           C  
ANISOU 3817  C   SER A 478     2039   1644   1581    -17    574    -78       C  
ATOM   3818  O   SER A 478     -23.688  -6.054  45.749  1.00 13.72           O  
ANISOU 3818  O   SER A 478     1855   1718   1639     36    560   -219       O  
ATOM   3819  N   PHE A 479     -22.933  -4.979  47.611  1.00 13.47           N  
ANISOU 3819  N   PHE A 479     1956   1592   1570     40    531    -33       N  
ATOM   3820  CA  PHE A 479     -24.052  -5.373  48.466  1.00 14.54           C  
ANISOU 3820  CA  PHE A 479     2000   1792   1731    162    728   -120       C  
ATOM   3821  CB  PHE A 479     -23.573  -5.529  49.908  1.00 14.79           C  
ANISOU 3821  CB  PHE A 479     2463   1491   1664    297    703    -99       C  
ATOM   3822  CG  PHE A 479     -22.481  -6.559  50.078  1.00 15.51           C  
ANISOU 3822  CG  PHE A 479     2508   1711   1675    350    642    117       C  
ATOM   3823  CD1 PHE A 479     -22.799  -7.884  50.333  1.00 17.89           C  
ANISOU 3823  CD1 PHE A 479     2916   1765   2116    268    594     97       C  
ATOM   3824  CE1 PHE A 479     -21.801  -8.843  50.478  1.00 18.09           C  
ANISOU 3824  CE1 PHE A 479     3065   1929   1877    372    521    222       C  
ATOM   3825  CZ  PHE A 479     -20.480  -8.479  50.388  1.00 17.65           C  
ANISOU 3825  CZ  PHE A 479     2930   1996   1781    629    571     93       C  
ATOM   3826  CD2 PHE A 479     -21.148  -6.211  50.013  1.00 15.97           C  
ANISOU 3826  CD2 PHE A 479     2646   1882   1540    378    633   -165       C  
ATOM   3827  CE2 PHE A 479     -20.156  -7.164  50.151  1.00 17.45           C  
ANISOU 3827  CE2 PHE A 479     2948   1993   1689    476    644    -34       C  
ATOM   3828  C   PHE A 479     -25.175  -4.324  48.346  1.00 14.77           C  
ANISOU 3828  C   PHE A 479     2255   1511   1845    169    759   -109       C  
ATOM   3829  O   PHE A 479     -24.909  -3.150  48.195  1.00 14.43           O  
ANISOU 3829  O   PHE A 479     2293   1562   1625    159    536     35       O  
ATOM   3830  N   GLU A 480     -26.437  -4.755  48.441  1.00 16.67           N  
ANISOU 3830  N   GLU A 480     2457   1524   2351   -120    960    -30       N  
ATOM   3831  CA  GLU A 480     -27.533  -3.824  48.143  1.00 17.87           C  
ANISOU 3831  CA  GLU A 480     2398   1824   2565    -28   1130   -192       C  
ATOM   3832  CB  GLU A 480     -28.849  -4.534  47.840  1.00 21.75           C  
ANISOU 3832  CB  GLU A 480     2824   2523   2915   -243    927    -55       C  
ATOM   3833  CG  GLU A 480     -29.420  -5.213  49.044  1.00 19.85           C  
ANISOU 3833  CG  GLU A 480     2960   2377   2204    -37   1127   -426       C  
ATOM   3834  CD  GLU A 480     -30.812  -5.784  48.879  1.00 21.14           C  
ANISOU 3834  CD  GLU A 480     2730   2565   2734    234   1084    111       C  
ATOM   3835  OE1 GLU A 480     -31.329  -5.867  47.735  1.00 21.55           O  
ANISOU 3835  OE1 GLU A 480     2937   1970   3279    362    843   -246       O  
ATOM   3836  OE2 GLU A 480     -31.378  -6.163  49.915  1.00 23.64           O  
ANISOU 3836  OE2 GLU A 480     2446   3390   3143    485   1160    837       O  
ATOM   3837  C   GLU A 480     -27.642  -2.751  49.235  1.00 16.20           C  
ANISOU 3837  C   GLU A 480     2279   1654   2221     29    819     -1       C  
ATOM   3838  O   GLU A 480     -28.204  -1.706  48.955  1.00 16.53           O  
ANISOU 3838  O   GLU A 480     2529   1762   1987    188    810    -80       O  
ATOM   3839  N   ASP A 481     -27.101  -2.974  50.441  1.00 15.80           N  
ANISOU 3839  N   ASP A 481     2381   1569   2053    305    948     15       N  
ATOM   3840  CA  ASP A 481     -27.080  -1.919  51.475  1.00 16.91           C  
ANISOU 3840  CA  ASP A 481     2727   1627   2071    335    950    -12       C  
ATOM   3841  CB  ASP A 481     -26.752  -2.455  52.875  1.00 18.96           C  
ANISOU 3841  CB  ASP A 481     2969   2041   2193    418   1137    290       C  
ATOM   3842  CG  ASP A 481     -25.348  -3.008  53.091  1.00 19.45           C  
ANISOU 3842  CG  ASP A 481     3220   1990   2179    577   1054    416       C  
ATOM   3843  OD1 ASP A 481     -24.471  -2.815  52.242  1.00 20.48           O  
ANISOU 3843  OD1 ASP A 481     3239   2317   2223    933   1183    649       O  
ATOM   3844  OD2 ASP A 481     -25.148  -3.641  54.146  1.00 25.63           O  
ANISOU 3844  OD2 ASP A 481     4120   3214   2402   1101   1416   1009       O  
ATOM   3845  C   ASP A 481     -26.122  -0.763  51.121  1.00 16.77           C  
ANISOU 3845  C   ASP A 481     2650   1781   1939    266    925    -83       C  
ATOM   3846  O   ASP A 481     -26.108   0.236  51.836  1.00 17.71           O  
ANISOU 3846  O   ASP A 481     3064   1842   1821    373    870   -107       O  
ATOM   3847  N   GLY A 482     -25.345  -0.898  50.039  1.00 14.98           N  
ANISOU 3847  N   GLY A 482     2197   1605   1889    258    774     54       N  
ATOM   3848  CA  GLY A 482     -24.447   0.137  49.553  1.00 13.81           C  
ANISOU 3848  CA  GLY A 482     2242   1389   1617    154    522   -185       C  
ATOM   3849  C   GLY A 482     -22.986  -0.270  49.615  1.00 12.66           C  
ANISOU 3849  C   GLY A 482     2227   1229   1353    137    407    -13       C  
ATOM   3850  O   GLY A 482     -22.139   0.238  48.851  1.00 13.00           O  
ANISOU 3850  O   GLY A 482     2047   1551   1338     22    317     21       O  
ATOM   3851  N   THR A 483     -22.660  -1.188  50.528  1.00 12.81           N  
ANISOU 3851  N   THR A 483     2279   1234   1352    210    534     54       N  
ATOM   3852  CA  THR A 483     -21.272  -1.544  50.763  1.00 14.20           C  
ANISOU 3852  CA  THR A 483     2469   1516   1410    400    430    -67       C  
ATOM   3853  CB  THR A 483     -21.168  -2.526  51.935  1.00 15.18           C  
ANISOU 3853  CB  THR A 483     2435   1785   1546    556    461    172       C  
ATOM   3854  OG1 THR A 483     -21.735  -1.883  53.072  1.00 17.00           O  
ANISOU 3854  OG1 THR A 483     2540   2313   1605    720    497     45       O  
ATOM   3855  CG2 THR A 483     -19.746  -2.934  52.252  1.00 15.88           C  
ANISOU 3855  CG2 THR A 483     2662   2031   1341    739    297    146       C  
ATOM   3856  C   THR A 483     -20.640  -2.169  49.509  1.00 13.13           C  
ANISOU 3856  C   THR A 483     2259   1498   1231    238    397     14       C  
ATOM   3857  O   THR A 483     -21.272  -2.995  48.821  1.00 14.15           O  
ANISOU 3857  O   THR A 483     2215   1518   1641    175    290    -93       O  
ATOM   3858  N   PHE A 484     -19.382  -1.796  49.251  1.00 12.76           N  
ANISOU 3858  N   PHE A 484     2103   1587   1158    359    208   -158       N  
ATOM   3859  CA  PHE A 484     -18.511  -2.524  48.310  1.00 12.51           C  
ANISOU 3859  CA  PHE A 484     2085   1542   1124    320    234   -149       C  
ATOM   3860  CB  PHE A 484     -17.950  -1.616  47.206  1.00 12.21           C  
ANISOU 3860  CB  PHE A 484     1979   1450   1210    366    321   -192       C  
ATOM   3861  CG  PHE A 484     -18.949  -1.241  46.144  1.00 12.99           C  
ANISOU 3861  CG  PHE A 484     2082   1618   1233    323    294    -62       C  
ATOM   3862  CD1 PHE A 484     -19.934  -0.294  46.373  1.00 12.45           C  
ANISOU 3862  CD1 PHE A 484     1942   1660   1125    236    319   -185       C  
ATOM   3863  CE1 PHE A 484     -20.827   0.052  45.380  1.00 13.13           C  
ANISOU 3863  CE1 PHE A 484     1881   1650   1456    154    226    -28       C  
ATOM   3864  CZ  PHE A 484     -20.739  -0.525  44.144  1.00 12.71           C  
ANISOU 3864  CZ  PHE A 484     2018   1410   1399    -58     58     94       C  
ATOM   3865  CD2 PHE A 484     -18.863  -1.805  44.882  1.00 13.84           C  
ANISOU 3865  CD2 PHE A 484     2346   1661   1252    217    157   -103       C  
ATOM   3866  CE2 PHE A 484     -19.779  -1.469  43.897  1.00 13.61           C  
ANISOU 3866  CE2 PHE A 484     2346   1610   1215    110    232    -20       C  
ATOM   3867  C   PHE A 484     -17.334  -3.137  49.073  1.00 13.56           C  
ANISOU 3867  C   PHE A 484     2314   1547   1288    499    199    -95       C  
ATOM   3868  O   PHE A 484     -16.797  -2.537  50.009  1.00 14.85           O  
ANISOU 3868  O   PHE A 484     2277   1915   1448    287    353   -311       O  
ATOM   3869  N   MET A 485     -16.932  -4.339  48.644  1.00 14.64           N  
ANISOU 3869  N   MET A 485     2352   1654   1555    435    130   -330       N  
ATOM   3870  CA  MET A 485     -15.743  -5.029  49.161  1.00 15.43           C  
ANISOU 3870  CA  MET A 485     2574   1623   1665    595     34   -261       C  
ATOM   3871  CB  MET A 485     -16.128  -6.174  50.118  1.00 17.33           C  
ANISOU 3871  CB  MET A 485     2838   1930   1815    709    198     -3       C  
ATOM   3872  CG  MET A 485     -16.851  -5.716  51.386  1.00 18.60           C  
ANISOU 3872  CG  MET A 485     3452   1802   1813    546    199   -148       C  
ATOM   3873  SD  MET A 485     -17.311  -7.086  52.458  1.00 25.26           S  
ANISOU 3873  SD  MET A 485     4303   2903   2391   -171   -128    521       S  
ATOM   3874  CE  MET A 485     -15.703  -7.535  53.098  1.00 29.74           C  
ANISOU 3874  CE  MET A 485     4457   3922   2920     90   -432    421       C  
ATOM   3875  C   MET A 485     -14.979  -5.606  47.967  1.00 14.87           C  
ANISOU 3875  C   MET A 485     2142   1674   1831    581     35   -271       C  
ATOM   3876  O   MET A 485     -15.571  -5.781  46.904  1.00 15.58           O  
ANISOU 3876  O   MET A 485     2008   1977   1935    467     43   -417       O  
ATOM   3877  N   ASP A 486     -13.684  -5.883  48.127  1.00 14.58           N  
ANISOU 3877  N   ASP A 486     2038   1558   1943    518     14   -593       N  
ATOM   3878  CA  ASP A 486     -13.025  -6.722  47.155  1.00 15.84           C  
ANISOU 3878  CA  ASP A 486     2089   1704   2223    821     91   -503       C  
ATOM   3879  CB  ASP A 486     -12.326  -5.897  46.059  1.00 18.91           C  
ANISOU 3879  CB  ASP A 486     2518   2189   2477    647    231   -349       C  
ATOM   3880  CG  ASP A 486     -11.099  -5.123  46.464  1.00 26.62           C  
ANISOU 3880  CG  ASP A 486     2693   3541   3881    332     53   -703       C  
ATOM   3881  OD1 ASP A 486     -11.027  -4.711  47.612  1.00 30.57           O  
ANISOU 3881  OD1 ASP A 486     2714   3730   5171    466    107  -2306       O  
ATOM   3882  OD2 ASP A 486     -10.186  -5.015  45.611  1.00 37.00           O  
ANISOU 3882  OD2 ASP A 486     3752   4886   5417   -725    788   -794       O  
ATOM   3883  C   ASP A 486     -12.099  -7.694  47.893  1.00 16.64           C  
ANISOU 3883  C   ASP A 486     2564   1929   1828    924   -234   -602       C  
ATOM   3884  O   ASP A 486     -11.620  -7.441  49.009  1.00 20.85           O  
ANISOU 3884  O   ASP A 486     3297   2624   1998   1083   -625   -726       O  
ATOM   3885  N   ASP A 487     -11.833  -8.829  47.245  1.00 14.11           N  
ANISOU 3885  N   ASP A 487     2414   1677   1270    605    -40   -324       N  
ATOM   3886  CA  ASP A 487     -11.042  -9.866  47.858  1.00 15.34           C  
ANISOU 3886  CA  ASP A 487     2247   1966   1616    664     77    -84       C  
ATOM   3887  CB  ASP A 487     -11.835 -10.698  48.878  1.00 17.40           C  
ANISOU 3887  CB  ASP A 487     2674   2265   1669    617    438   -101       C  
ATOM   3888  CG  ASP A 487     -11.941 -10.064  50.253  1.00 23.03           C  
ANISOU 3888  CG  ASP A 487     3555   3195   1997    776    476   -500       C  
ATOM   3889  OD1 ASP A 487     -10.894  -9.806  50.854  1.00 27.91           O  
ANISOU 3889  OD1 ASP A 487     4165   4010   2429    745     -6   -360       O  
ATOM   3890  OD2 ASP A 487     -13.068  -9.781  50.678  1.00 31.21           O  
ANISOU 3890  OD2 ASP A 487     4083   4350   3425    607   1324  -1225       O  
ATOM   3891  C   ASP A 487     -10.534 -10.833  46.795  1.00 14.11           C  
ANISOU 3891  C   ASP A 487     2079   1772   1508    373    325     76       C  
ATOM   3892  O   ASP A 487     -11.231 -11.139  45.802  1.00 15.20           O  
ANISOU 3892  O   ASP A 487     2370   1911   1494    406    268    -85       O  
ATOM   3893  N   LEU A 488      -9.314 -11.336  47.035  1.00 14.46           N  
ANISOU 3893  N   LEU A 488     2213   1706   1574    484    215    -63       N  
ATOM   3894  CA  LEU A 488      -8.778 -12.405  46.253  1.00 14.52           C  
ANISOU 3894  CA  LEU A 488     2063   1901   1553    407    463   -186       C  
ATOM   3895  CB  LEU A 488      -7.373 -12.738  46.746  1.00 15.22           C  
ANISOU 3895  CB  LEU A 488     2322   1862   1598    466    299    -37       C  
ATOM   3896  CG  LEU A 488      -6.317 -11.644  46.637  1.00 16.72           C  
ANISOU 3896  CG  LEU A 488     2622   1789   1940    428    336    -89       C  
ATOM   3897  CD1 LEU A 488      -4.979 -12.182  47.135  1.00 17.85           C  
ANISOU 3897  CD1 LEU A 488     2733   2236   1811    354    167   -128       C  
ATOM   3898  CD2 LEU A 488      -6.197 -11.152  45.206  1.00 16.78           C  
ANISOU 3898  CD2 LEU A 488     2468   2052   1855    526    350    -90       C  
ATOM   3899  C   LEU A 488      -9.675 -13.634  46.411  1.00 14.66           C  
ANISOU 3899  C   LEU A 488     2083   1880   1605    445    179    -57       C  
ATOM   3900  O   LEU A 488     -10.300 -13.839  47.450  1.00 16.75           O  
ANISOU 3900  O   LEU A 488     2572   2210   1582    -33    265    -41       O  
ATOM   3901  N   THR A 489      -9.711 -14.458  45.365  1.00 15.36           N  
ANISOU 3901  N   THR A 489     2401   1671   1763    409    303   -123       N  
ATOM   3902  CA  THR A 489     -10.433 -15.721  45.360  1.00 16.54           C  
ANISOU 3902  CA  THR A 489     2561   1636   2087    387     60   -166       C  
ATOM   3903  CB  THR A 489     -11.042 -15.991  43.975  1.00 16.88           C  
ANISOU 3903  CB  THR A 489     2740   1514   2157    300   -181     46       C  
ATOM   3904  OG1 THR A 489     -10.012 -15.961  42.970  1.00 18.82           O  
ANISOU 3904  OG1 THR A 489     3134   2058   1959    291   -192    -57       O  
ATOM   3905  CG2 THR A 489     -12.106 -14.975  43.616  1.00 18.21           C  
ANISOU 3905  CG2 THR A 489     2692   1812   2413    337   -227    123       C  
ATOM   3906  C   THR A 489      -9.459 -16.826  45.756  1.00 17.05           C  
ANISOU 3906  C   THR A 489     2355   2057   2065    523     77    -41       C  
ATOM   3907  O   THR A 489      -8.757 -17.341  44.898  1.00 23.18           O  
ANISOU 3907  O   THR A 489     3958   2764   2083   1805    321    271       O  
ATOM   3908  N   LEU A 490      -9.403 -17.174  47.038  1.00 16.81           N  
ANISOU 3908  N   LEU A 490     2330   2003   2053    631    219    -28       N  
ATOM   3909  CA  LEU A 490      -8.400 -18.116  47.525  1.00 16.40           C  
ANISOU 3909  CA  LEU A 490     2470   1833   1928    593    222   -178       C  
ATOM   3910  CB  LEU A 490      -7.507 -17.434  48.568  1.00 16.41           C  
ANISOU 3910  CB  LEU A 490     2528   1854   1852    301    190    -15       C  
ATOM   3911  CG  LEU A 490      -6.690 -16.244  48.071  1.00 17.43           C  
ANISOU 3911  CG  LEU A 490     2764   1775   2081    268     -1     15       C  
ATOM   3912  CD1 LEU A 490      -5.850 -15.660  49.209  1.00 21.96           C  
ANISOU 3912  CD1 LEU A 490     3200   2652   2491   -139   -227   -129       C  
ATOM   3913  CD2 LEU A 490      -5.810 -16.644  46.915  1.00 19.92           C  
ANISOU 3913  CD2 LEU A 490     3177   1897   2495    461    418    194       C  
ATOM   3914  C   LEU A 490      -9.084 -19.324  48.157  1.00 15.83           C  
ANISOU 3914  C   LEU A 490     2384   2046   1582    319    163   -258       C  
ATOM   3915  O   LEU A 490     -10.114 -19.188  48.839  1.00 17.31           O  
ANISOU 3915  O   LEU A 490     2558   2096   1920    493    501    -19       O  
ATOM   3916  N   TYR A 491      -8.463 -20.488  47.949  1.00 15.70           N  
ANISOU 3916  N   TYR A 491     2364   2114   1486    459    212    -66       N  
ATOM   3917  CA  TYR A 491      -8.975 -21.794  48.396  1.00 15.90           C  
ANISOU 3917  CA  TYR A 491     2580   2037   1423    436    204    134       C  
ATOM   3918  CB  TYR A 491      -9.774 -22.483  47.283  1.00 16.30           C  
ANISOU 3918  CB  TYR A 491     2452   2075   1667    516    168     12       C  
ATOM   3919  CG  TYR A 491     -10.807 -21.566  46.684  1.00 17.81           C  
ANISOU 3919  CG  TYR A 491     2664   2047   2056    493   -118     26       C  
ATOM   3920  CD1 TYR A 491     -10.465 -20.745  45.620  1.00 18.47           C  
ANISOU 3920  CD1 TYR A 491     2722   2088   2207    319   -109     54       C  
ATOM   3921  CE1 TYR A 491     -11.359 -19.825  45.122  1.00 20.37           C  
ANISOU 3921  CE1 TYR A 491     3014   2275   2448    262   -630   -148       C  
ATOM   3922  CZ  TYR A 491     -12.611 -19.698  45.679  1.00 23.55           C  
ANISOU 3922  CZ  TYR A 491     3009   2939   2998    801   -574   -235       C  
ATOM   3923  OH  TYR A 491     -13.449 -18.760  45.138  1.00 27.83           O  
ANISOU 3923  OH  TYR A 491     4182   2832   3558   1219  -1295   -635       O  
ATOM   3924  CE2 TYR A 491     -12.977 -20.513  46.734  1.00 22.18           C  
ANISOU 3924  CE2 TYR A 491     2942   2867   2616    763   -299   -585       C  
ATOM   3925  CD2 TYR A 491     -12.071 -21.431  47.239  1.00 19.98           C  
ANISOU 3925  CD2 TYR A 491     2947   2577   2066    458   -136   -376       C  
ATOM   3926  C   TYR A 491      -7.784 -22.643  48.846  1.00 15.90           C  
ANISOU 3926  C   TYR A 491     2567   2015   1459    282    145    164       C  
ATOM   3927  O   TYR A 491      -6.654 -22.443  48.423  1.00 17.05           O  
ANISOU 3927  O   TYR A 491     2678   2034   1766    241    302    172       O  
ATOM   3928  N   THR A 492      -8.051 -23.655  49.672  1.00 16.95           N  
ANISOU 3928  N   THR A 492     2758   2035   1644    360    247    361       N  
ATOM   3929  CA  THR A 492      -6.993 -24.583  50.010  1.00 17.17           C  
ANISOU 3929  CA  THR A 492     2887   1974   1663    368     25    175       C  
ATOM   3930  CB  THR A 492      -7.368 -25.515  51.169  1.00 18.74           C  
ANISOU 3930  CB  THR A 492     3092   2227   1800    297     21    393       C  
ATOM   3931  OG1 THR A 492      -8.401 -26.409  50.745  1.00 20.71           O  
ANISOU 3931  OG1 THR A 492     3395   2515   1959    172    -11    237       O  
ATOM   3932  CG2 THR A 492      -7.783 -24.751  52.405  1.00 20.67           C  
ANISOU 3932  CG2 THR A 492     3391   2686   1775    336     -2    293       C  
ATOM   3933  C   THR A 492      -6.607 -25.426  48.801  1.00 17.23           C  
ANISOU 3933  C   THR A 492     2893   1897   1754    560     26    227       C  
ATOM   3934  O   THR A 492      -7.430 -25.705  47.939  1.00 16.11           O  
ANISOU 3934  O   THR A 492     2412   1804   1902    453    214    187       O  
ATOM   3935  N   PRO A 493      -5.335 -25.860  48.700  1.00 17.89           N  
ANISOU 3935  N   PRO A 493     2792   2075   1929    445    171    388       N  
ATOM   3936  CA  PRO A 493      -4.974 -26.840  47.682  1.00 18.84           C  
ANISOU 3936  CA  PRO A 493     3154   2027   1976    670    255    515       C  
ATOM   3937  CB  PRO A 493      -3.540 -27.218  48.044  1.00 19.60           C  
ANISOU 3937  CB  PRO A 493     2981   2072   2391    594    233    348       C  
ATOM   3938  CG  PRO A 493      -2.995 -25.955  48.707  1.00 20.02           C  
ANISOU 3938  CG  PRO A 493     2901   2108   2595    706    131    269       C  
ATOM   3939  CD  PRO A 493      -4.175 -25.390  49.479  1.00 18.69           C  
ANISOU 3939  CD  PRO A 493     2972   2228   1898    641    119    467       C  
ATOM   3940  C   PRO A 493      -5.929 -28.039  47.643  1.00 18.93           C  
ANISOU 3940  C   PRO A 493     2997   2009   2186    702    258    550       C  
ATOM   3941  O   PRO A 493      -6.336 -28.465  46.573  1.00 20.41           O  
ANISOU 3941  O   PRO A 493     3176   2378   2201    667    288    391       O  
ATOM   3942  N   ASP A 494      -6.298 -28.576  48.803  1.00 20.22           N  
ANISOU 3942  N   ASP A 494     3604   2124   1952    379    157    388       N  
ATOM   3943  CA  ASP A 494      -7.162 -29.744  48.846  1.00 21.65           C  
ANISOU 3943  CA  ASP A 494     3536   2221   2466    373    174    605       C  
ATOM   3944  CB  ASP A 494      -7.326 -30.269  50.273  1.00 24.32           C  
ANISOU 3944  CB  ASP A 494     3769   2740   2730     91     14   1057       C  
ATOM   3945  CG  ASP A 494      -6.108 -31.031  50.784  1.00 29.98           C  
ANISOU 3945  CG  ASP A 494     4457   3525   3408    686    -51   1376       C  
ATOM   3946  OD1 ASP A 494      -5.183 -31.329  49.969  1.00 33.49           O  
ANISOU 3946  OD1 ASP A 494     4271   3994   4459    607    222    995       O  
ATOM   3947  OD2 ASP A 494      -6.093 -31.327  51.997  1.00 36.78           O  
ANISOU 3947  OD2 ASP A 494     5700   4630   3644    837   -346   1898       O  
ATOM   3948  C   ASP A 494      -8.518 -29.427  48.219  1.00 20.65           C  
ANISOU 3948  C   ASP A 494     3618   1977   2249    388    174    588       C  
ATOM   3949  O   ASP A 494      -9.057 -30.270  47.507  1.00 23.01           O  
ANISOU 3949  O   ASP A 494     3975   2259   2508    300    213    523       O  
ATOM   3950  N   GLN A 495      -9.075 -28.230  48.472  1.00 18.90           N  
ANISOU 3950  N   GLN A 495     3127   2016   2038    265    228    337       N  
ATOM   3951  CA AGLN A 495     -10.347 -27.852  47.844  0.50 18.52           C  
ANISOU 3951  CA AGLN A 495     3058   1937   2039    232    448    513       C  
ATOM   3952  CA BGLN A 495     -10.330 -27.895  47.841  0.50 18.68           C  
ANISOU 3952  CA BGLN A 495     3102   1983   2012    261    406    519       C  
ATOM   3953  CB AGLN A 495     -10.831 -26.465  48.296  0.50 18.82           C  
ANISOU 3953  CB AGLN A 495     2917   2175   2057    360    645    430       C  
ATOM   3954  CB BGLN A 495     -10.908 -26.562  48.289  0.50 18.44           C  
ANISOU 3954  CB BGLN A 495     2957   2238   1808    417    519    500       C  
ATOM   3955  CG AGLN A 495     -11.258 -26.343  49.765  0.50 18.77           C  
ANISOU 3955  CG AGLN A 495     2706   2352   2073    450    664    501       C  
ATOM   3956  CG BGLN A 495     -12.175 -26.327  47.486  0.50 18.40           C  
ANISOU 3956  CG BGLN A 495     2890   2331   1769    510    546    579       C  
ATOM   3957  CD AGLN A 495     -11.691 -24.946  50.177  0.50 19.43           C  
ANISOU 3957  CD AGLN A 495     2534   2280   2565    321    704    463       C  
ATOM   3958  CD BGLN A 495     -13.025 -25.152  47.855  0.50 18.83           C  
ANISOU 3958  CD BGLN A 495     2842   2688   1625    672    553    465       C  
ATOM   3959  OE1AGLN A 495     -10.903 -23.992  50.323  0.50 16.51           O  
ANISOU 3959  OE1AGLN A 495     2086   2442   1744    250    837    670       O  
ATOM   3960  OE1BGLN A 495     -13.766 -24.677  47.001  0.50 18.64           O  
ANISOU 3960  OE1BGLN A 495     2989   2564   1529    890    737    741       O  
ATOM   3961  NE2AGLN A 495     -12.988 -24.815  50.401  0.50 21.47           N  
ANISOU 3961  NE2AGLN A 495     2677   2580   2900    584    862    300       N  
ATOM   3962  NE2BGLN A 495     -12.937 -24.727  49.111  0.50 19.36           N  
ANISOU 3962  NE2BGLN A 495     2658   3192   1504    260    385    607       N  
ATOM   3963  C   GLN A 495     -10.184 -27.876  46.315  1.00 18.94           C  
ANISOU 3963  C   GLN A 495     3170   2008   2019    239    321    354       C  
ATOM   3964  O   GLN A 495     -11.060 -28.377  45.589  1.00 21.44           O  
ANISOU 3964  O   GLN A 495     3935   2142   2068    -11    -11    416       O  
ATOM   3965  N   LEU A 496      -9.102 -27.275  45.824  1.00 18.11           N  
ANISOU 3965  N   LEU A 496     3011   1879   1989    278    232    237       N  
ATOM   3966  CA  LEU A 496      -8.899 -27.171  44.374  1.00 17.39           C  
ANISOU 3966  CA  LEU A 496     3043   1627   1937    367     -1    321       C  
ATOM   3967  CB  LEU A 496      -7.757 -26.197  44.109  1.00 17.78           C  
ANISOU 3967  CB  LEU A 496     3137   1728   1889    342    348    203       C  
ATOM   3968  CG  LEU A 496      -8.034 -24.761  44.568  1.00 16.89           C  
ANISOU 3968  CG  LEU A 496     3170   1530   1714    209    277    446       C  
ATOM   3969  CD1 LEU A 496      -6.846 -23.867  44.280  1.00 17.74           C  
ANISOU 3969  CD1 LEU A 496     3227   2079   1431     23    181    538       C  
ATOM   3970  CD2 LEU A 496      -9.307 -24.203  43.935  1.00 18.14           C  
ANISOU 3970  CD2 LEU A 496     3424   1655   1813    259    234    498       C  
ATOM   3971  C   LEU A 496      -8.634 -28.555  43.758  1.00 19.66           C  
ANISOU 3971  C   LEU A 496     3387   1653   2427    350     43    219       C  
ATOM   3972  O   LEU A 496      -9.202 -28.866  42.716  1.00 21.19           O  
ANISOU 3972  O   LEU A 496     3904   1665   2481    258    -53    193       O  
ATOM   3973  N   LEU A 497      -7.826 -29.394  44.418  1.00 20.79           N  
ANISOU 3973  N   LEU A 497     3577   1932   2389    430    -32    134       N  
ATOM   3974  CA  LEU A 497      -7.464 -30.721  43.881  1.00 21.49           C  
ANISOU 3974  CA  LEU A 497     3808   2048   2309    541    126    121       C  
ATOM   3975  CB  LEU A 497      -6.472 -31.408  44.826  1.00 21.58           C  
ANISOU 3975  CB  LEU A 497     3865   1762   2570    821    316    293       C  
ATOM   3976  CG  LEU A 497      -5.051 -30.852  44.778  1.00 23.50           C  
ANISOU 3976  CG  LEU A 497     3968   2289   2669    621    266     57       C  
ATOM   3977  CD1 LEU A 497      -4.257 -31.290  45.984  1.00 26.46           C  
ANISOU 3977  CD1 LEU A 497     3772   3136   3144    510    102    327       C  
ATOM   3978  CD2 LEU A 497      -4.346 -31.259  43.495  1.00 25.21           C  
ANISOU 3978  CD2 LEU A 497     3749   2648   3182    499    741    127       C  
ATOM   3979  C   LEU A 497      -8.711 -31.591  43.689  1.00 22.12           C  
ANISOU 3979  C   LEU A 497     4269   1760   2375    353   -107     54       C  
ATOM   3980  O   LEU A 497      -8.712 -32.466  42.806  1.00 25.19           O  
ANISOU 3980  O   LEU A 497     4722   1915   2931    406    -65   -241       O  
ATOM   3981  N   ARG A 498      -9.746 -31.385  44.515  1.00 21.57           N  
ANISOU 3981  N   ARG A 498     3614   1779   2802     97   -304    238       N  
ATOM   3982  CA  ARG A 498     -10.955 -32.215  44.463  1.00 24.11           C  
ANISOU 3982  CA  ARG A 498     3655   2106   3400    204   -380    453       C  
ATOM   3983  CB  ARG A 498     -11.417 -32.598  45.871  1.00 26.80           C  
ANISOU 3983  CB  ARG A 498     3759   2828   3594   -185    122    624       C  
ATOM   3984  CG  ARG A 498     -12.159 -31.542  46.673  1.00 29.78           C  
ANISOU 3984  CG  ARG A 498     4191   3406   3719    -87    292    698       C  
ATOM   3985  CD  ARG A 498     -12.510 -32.096  48.063  1.00 36.35           C  
ANISOU 3985  CD  ARG A 498     4839   5127   3843   -622    880    672       C  
ATOM   3986  NE  ARG A 498     -12.871 -31.034  48.995  1.00 40.16           N  
ANISOU 3986  NE  ARG A 498     4779   6396   4085   -682   1261    455       N  
ATOM   3987  CZ  ARG A 498     -12.093 -30.560  49.972  1.00 42.59           C  
ANISOU 3987  CZ  ARG A 498     5186   6914   4081   -780   1397     -1       C  
ATOM   3988  NH1 ARG A 498     -10.894 -31.066  50.211  1.00 48.51           N  
ANISOU 3988  NH1 ARG A 498     4170   8753   5506  -1378   1158    449       N  
ATOM   3989  NH2 ARG A 498     -12.527 -29.553  50.707  1.00 46.38           N  
ANISOU 3989  NH2 ARG A 498     6605   6884   4133   -620   1707    194       N  
ATOM   3990  C   ARG A 498     -12.076 -31.539  43.662  1.00 21.18           C  
ANISOU 3990  C   ARG A 498     3545   1827   2675    112   -198    371       C  
ATOM   3991  O   ARG A 498     -13.167 -32.109  43.540  1.00 26.01           O  
ANISOU 3991  O   ARG A 498     3878   2533   3470   -271   -252    578       O  
ATOM   3992  N   SER A 499     -11.804 -30.380  43.053  1.00 20.71           N  
ANISOU 3992  N   SER A 499     3550   1825   2493     75   -223    233       N  
ATOM   3993  CA  SER A 499     -12.818 -29.643  42.323  1.00 19.96           C  
ANISOU 3993  CA  SER A 499     3389   1735   2459    203   -210      7       C  
ATOM   3994  CB  SER A 499     -12.435 -28.207  42.142  1.00 18.96           C  
ANISOU 3994  CB  SER A 499     3349   1616   2238    314   -219     57       C  
ATOM   3995  OG  SER A 499     -12.380 -27.510  43.381  1.00 19.84           O  
ANISOU 3995  OG  SER A 499     3430   1925   2180    302    105    -62       O  
ATOM   3996  C   SER A 499     -13.058 -30.297  40.965  1.00 21.45           C  
ANISOU 3996  C   SER A 499     3759   1685   2703    385   -243   -133       C  
ATOM   3997  O   SER A 499     -12.139 -30.842  40.343  1.00 24.07           O  
ANISOU 3997  O   SER A 499     4648   1711   2783    729    296    -49       O  
ATOM   3998  N   PRO A 500     -14.302 -30.275  40.462  1.00 21.76           N  
ANISOU 3998  N   PRO A 500     3725   1845   2697    160   -380     92       N  
ATOM   3999  CA  PRO A 500     -14.604 -30.890  39.173  1.00 22.32           C  
ANISOU 3999  CA  PRO A 500     3888   1792   2797    223   -107   -153       C  
ATOM   4000  CB  PRO A 500     -16.119 -30.751  39.024  1.00 25.52           C  
ANISOU 4000  CB  PRO A 500     3908   2539   3248    -55    -97    102       C  
ATOM   4001  CG  PRO A 500     -16.510 -29.677  39.990  1.00 27.61           C  
ANISOU 4001  CG  PRO A 500     3972   3097   3421    252   -493   -215       C  
ATOM   4002  CD  PRO A 500     -15.486 -29.697  41.103  1.00 24.79           C  
ANISOU 4002  CD  PRO A 500     3819   2547   3052    273   -328    -94       C  
ATOM   4003  C   PRO A 500     -13.907 -30.191  38.002  1.00 19.64           C  
ANISOU 4003  C   PRO A 500     3025   1452   2985    494    -77   -124       C  
ATOM   4004  O   PRO A 500     -13.743 -28.960  38.051  1.00 19.57           O  
ANISOU 4004  O   PRO A 500     3214   1431   2788    422    345   -256       O  
ATOM   4005  N   LEU A 501     -13.521 -30.968  36.975  1.00 20.44           N  
ANISOU 4005  N   LEU A 501     3129   1365   3270    396   -235   -408       N  
ATOM   4006  CA  LEU A 501     -12.899 -30.395  35.804  1.00 22.24           C  
ANISOU 4006  CA  LEU A 501     2880   2504   3065    730     10   -682       C  
ATOM   4007  CB  LEU A 501     -12.315 -31.475  34.886  1.00 25.30           C  
ANISOU 4007  CB  LEU A 501     3488   2651   3472    668   -215  -1173       C  
ATOM   4008  CG  LEU A 501     -11.234 -32.363  35.478  1.00 27.19           C  
ANISOU 4008  CG  LEU A 501     4020   2514   3796    807   -381   -846       C  
ATOM   4009  CD1 LEU A 501     -10.850 -33.456  34.498  1.00 29.84           C  
ANISOU 4009  CD1 LEU A 501     3982   3132   4221   1154   -476  -1177       C  
ATOM   4010  CD2 LEU A 501     -10.026 -31.537  35.857  1.00 26.83           C  
ANISOU 4010  CD2 LEU A 501     3564   2507   4121   1102   -312   -740       C  
ATOM   4011  C   LEU A 501     -13.948 -29.619  35.011  1.00 20.94           C  
ANISOU 4011  C   LEU A 501     2440   2648   2867    736     52   -813       C  
ATOM   4012  O   LEU A 501     -15.106 -30.042  34.924  1.00 24.36           O  
ANISOU 4012  O   LEU A 501     2647   3535   3071    271     -5   -492       O  
ATOM   4013  N   LYS A 502     -13.498 -28.526  34.400  1.00 21.18           N  
ANISOU 4013  N   LYS A 502     2253   3251   2541    726    -61   -541       N  
ATOM   4014  CA  LYS A 502     -14.264 -27.784  33.421  1.00 21.31           C  
ANISOU 4014  CA  LYS A 502     2212   3418   2464    701   -130   -563       C  
ATOM   4015  CB  LYS A 502     -14.512 -26.343  33.866  1.00 24.07           C  
ANISOU 4015  CB  LYS A 502     2762   3675   2708   1043   -135   -530       C  
ATOM   4016  CG  LYS A 502     -15.189 -25.482  32.799  1.00 27.34           C  
ANISOU 4016  CG  LYS A 502     3580   4023   2786   1212   -148   -254       C  
ATOM   4017  CD  LYS A 502     -15.455 -24.066  33.223  1.00 30.72           C  
ANISOU 4017  CD  LYS A 502     4254   4246   3171   1409   -225   -436       C  
ATOM   4018  CE  LYS A 502     -16.089 -23.225  32.138  1.00 31.02           C  
ANISOU 4018  CE  LYS A 502     4224   3787   3775   1985    -50   -381       C  
ATOM   4019  NZ  LYS A 502     -15.109 -22.840  31.105  1.00 35.51           N  
ANISOU 4019  NZ  LYS A 502     4786   4377   4328   1045   -144    117       N  
ATOM   4020  C   LYS A 502     -13.448 -27.842  32.125  1.00 20.47           C  
ANISOU 4020  C   LYS A 502     2194   3268   2316    454   -108   -555       C  
ATOM   4021  O   LYS A 502     -12.404 -27.171  32.021  1.00 21.79           O  
ANISOU 4021  O   LYS A 502     2104   3498   2677    515     14   -781       O  
ATOM   4022  N   LEU A 503     -13.914 -28.664  31.167  1.00 19.45           N  
ANISOU 4022  N   LEU A 503     2306   2956   2126    532    215   -670       N  
ATOM   4023  CA  LEU A 503     -13.155 -28.938  29.961  1.00 21.96           C  
ANISOU 4023  CA  LEU A 503     2571   3427   2346    451    456   -785       C  
ATOM   4024  CB  LEU A 503     -13.268 -30.424  29.624  1.00 22.25           C  
ANISOU 4024  CB  LEU A 503     2464   3310   2679    263    404   -565       C  
ATOM   4025  CG  LEU A 503     -12.609 -31.363  30.620  1.00 24.33           C  
ANISOU 4025  CG  LEU A 503     2696   3447   3102    305    -52   -576       C  
ATOM   4026  CD1 LEU A 503     -13.169 -32.765  30.517  1.00 24.95           C  
ANISOU 4026  CD1 LEU A 503     2485   3634   3361    221   -106   -500       C  
ATOM   4027  CD2 LEU A 503     -11.123 -31.391  30.394  1.00 27.77           C  
ANISOU 4027  CD2 LEU A 503     2866   3773   3909    381     97   -378       C  
ATOM   4028  C   LEU A 503     -13.635 -28.084  28.776  1.00 24.91           C  
ANISOU 4028  C   LEU A 503     3646   3392   2424    570    376   -686       C  
ATOM   4029  O   LEU A 503     -12.952 -28.058  27.728  1.00 26.78           O  
ANISOU 4029  O   LEU A 503     4497   3401   2277    449    584   -468       O  
ATOM   4030  N   THR A 504     -14.780 -27.408  28.937  1.00 28.43           N  
ANISOU 4030  N   THR A 504     4104   3809   2890    928    280   -501       N  
ATOM   4031  CA  THR A 504     -15.352 -26.542  27.884  1.00 34.60           C  
ANISOU 4031  CA  THR A 504     5136   4696   3314   1322   -401   -471       C  
ATOM   4032  CB  THR A 504     -16.754 -27.022  27.514  1.00 38.12           C  
ANISOU 4032  CB  THR A 504     4662   5561   4259   1365   -209   -388       C  
ATOM   4033  OG1 THR A 504     -17.559 -26.900  28.689  1.00 44.12           O  
ANISOU 4033  OG1 THR A 504     4584   7337   4840   1742    153    179       O  
ATOM   4034  CG2 THR A 504     -16.739 -28.440  26.993  1.00 38.51           C  
ANISOU 4034  CG2 THR A 504     4597   5324   4709    719   -699   -110       C  
ATOM   4035  C   THR A 504     -15.370 -25.082  28.342  1.00 45.76           C  
ANISOU 4035  C   THR A 504     7069   4795   5522   1300   -162  -1057       C  
ATOM   4036  O   THR A 504     -14.589 -24.705  29.226  1.00 53.37           O  
ANISOU 4036  O   THR A 504     9215   5028   6033   1778  -1153   -815       O  
ATOM   4037  N   LYS A 509     -25.468 -21.473  29.948  1.00 46.82           N  
ANISOU 4037  N   LYS A 509     8200   2603   6984    646    156  -1665       N  
ATOM   4038  CA  LYS A 509     -25.014 -20.217  29.314  1.00 42.27           C  
ANISOU 4038  CA  LYS A 509     7347   3507   5203    942   -394  -1096       C  
ATOM   4039  CB  LYS A 509     -25.733 -19.975  27.979  1.00 47.31           C  
ANISOU 4039  CB  LYS A 509     8042   3627   6305   1772   -938   -991       C  
ATOM   4040  CG  LYS A 509     -25.236 -20.814  26.808  1.00 54.37           C  
ANISOU 4040  CG  LYS A 509     8770   5640   6245    856   -756  -1791       C  
ATOM   4041  CD  LYS A 509     -26.300 -21.146  25.771  1.00 60.74           C  
ANISOU 4041  CD  LYS A 509     8854   6719   7503    162  -1281  -1357       C  
ATOM   4042  CE  LYS A 509     -25.727 -21.367  24.382  1.00 62.06           C  
ANISOU 4042  CE  LYS A 509     8362   7187   8029      6   -939  -1782       C  
ATOM   4043  NZ  LYS A 509     -26.386 -22.484  23.664  1.00 63.03           N  
ANISOU 4043  NZ  LYS A 509     7836   6745   9367   -608  -1158  -1148       N  
ATOM   4044  C   LYS A 509     -25.226 -19.040  30.274  1.00 32.05           C  
ANISOU 4044  C   LYS A 509     5108   3314   3753   1073   -562   -396       C  
ATOM   4045  O   LYS A 509     -24.516 -18.040  30.192  1.00 33.71           O  
ANISOU 4045  O   LYS A 509     5382   3318   4107   1230    667    665       O  
ATOM   4046  N   LEU A 510     -26.144 -19.178  31.231  1.00 29.39           N  
ANISOU 4046  N   LEU A 510     3899   3283   3981    695   -928   -636       N  
ATOM   4047  CA  LEU A 510     -26.281 -18.149  32.264  1.00 26.22           C  
ANISOU 4047  CA  LEU A 510     3451   2819   3692    594   -745   -535       C  
ATOM   4048  CB  LEU A 510     -27.679 -18.183  32.897  1.00 29.23           C  
ANISOU 4048  CB  LEU A 510     3914   3288   3903    199   -481    -83       C  
ATOM   4049  CG  LEU A 510     -28.840 -17.751  32.004  1.00 31.47           C  
ANISOU 4049  CG  LEU A 510     3904   3342   4711    324   -596     47       C  
ATOM   4050  CD1 LEU A 510     -30.127 -17.637  32.807  1.00 35.83           C  
ANISOU 4050  CD1 LEU A 510     4482   4227   4902    -30   -337    228       C  
ATOM   4051  CD2 LEU A 510     -28.558 -16.428  31.301  1.00 29.25           C  
ANISOU 4051  CD2 LEU A 510     3323   3156   4634    369   -811    -43       C  
ATOM   4052  C   LEU A 510     -25.201 -18.309  33.348  1.00 22.60           C  
ANISOU 4052  C   LEU A 510     3673   2299   2615   1116   -131   -284       C  
ATOM   4053  O   LEU A 510     -24.957 -17.373  34.140  1.00 23.71           O  
ANISOU 4053  O   LEU A 510     3715   2191   3101    960   -248   -410       O  
ATOM   4054  N   MET A 511     -24.560 -19.476  33.407  1.00 24.81           N  
ANISOU 4054  N   MET A 511     3906   2524   2995   1292   -165   -454       N  
ATOM   4055  CA AMET A 511     -23.526 -19.688  34.394  0.50 25.48           C  
ANISOU 4055  CA AMET A 511     3962   2760   2958   1294   -170   -735       C  
ATOM   4056  CA BMET A 511     -23.501 -19.730  34.377  0.50 24.64           C  
ANISOU 4056  CA BMET A 511     4026   2553   2781   1494    -34   -858       C  
ATOM   4057  CB AMET A 511     -23.333 -21.188  34.642  0.50 28.31           C  
ANISOU 4057  CB AMET A 511     4490   2781   3483   1115   -325   -606       C  
ATOM   4058  CB BMET A 511     -23.202 -21.232  34.514  0.50 27.97           C  
ANISOU 4058  CB BMET A 511     4956   2476   3194   1578    178  -1193       C  
ATOM   4059  CG AMET A 511     -24.625 -21.893  35.145  0.50 32.09           C  
ANISOU 4059  CG AMET A 511     4730   3197   4266    654   -593   -289       C  
ATOM   4060  CG BMET A 511     -23.638 -21.859  35.849  0.50 33.03           C  
ANISOU 4060  CG BMET A 511     5787   2898   3862   1099    167   -640       C  
ATOM   4061  SD AMET A 511     -25.362 -21.254  36.718  0.50 33.48           S  
ANISOU 4061  SD AMET A 511     5078   2914   4727   -293   -378   -646       S  
ATOM   4062  SD BMET A 511     -22.732 -21.262  37.311  0.50 37.25           S  
ANISOU 4062  SD BMET A 511     6746   3124   4283   1361    -79  -1039       S  
ATOM   4063  CE AMET A 511     -26.686 -20.225  36.084  0.50 31.97           C  
ANISOU 4063  CE AMET A 511     4702   2928   4517   -671   -517   -383       C  
ATOM   4064  CE BMET A 511     -21.032 -21.456  36.787  0.50 31.21           C  
ANISOU 4064  CE BMET A 511     6135   2334   3386   1400    -85   -309       C  
ATOM   4065  C   MET A 511     -22.254 -18.988  33.897  1.00 24.44           C  
ANISOU 4065  C   MET A 511     3879   2861   2544   1543   -159   -780       C  
ATOM   4066  O   MET A 511     -21.927 -19.009  32.700  1.00 30.64           O  
ANISOU 4066  O   MET A 511     4006   4834   2799   1160     28  -1133       O  
ATOM   4067  N   ARG A 512     -21.580 -18.311  34.815  1.00 24.16           N  
ANISOU 4067  N   ARG A 512     3754   3138   2285   1361    -65   -556       N  
ATOM   4068  CA  ARG A 512     -20.366 -17.585  34.558  1.00 23.75           C  
ANISOU 4068  CA  ARG A 512     3622   3433   1967   1508   -270   -131       C  
ATOM   4069  CB  ARG A 512     -20.536 -16.129  35.005  1.00 25.56           C  
ANISOU 4069  CB  ARG A 512     3887   3489   2336   1115   -465   -284       C  
ATOM   4070  CG  ARG A 512     -21.633 -15.374  34.266  1.00 24.95           C  
ANISOU 4070  CG  ARG A 512     3729   3234   2514    924   -520   -390       C  
ATOM   4071  CD  ARG A 512     -22.006 -14.106  35.011  1.00 25.83           C  
ANISOU 4071  CD  ARG A 512     3459   3757   2597    898   -506   -837       C  
ATOM   4072  NE  ARG A 512     -22.736 -13.123  34.222  1.00 22.87           N  
ANISOU 4072  NE  ARG A 512     3188   3050   2449    311   -226   -585       N  
ATOM   4073  CZ  ARG A 512     -22.165 -12.219  33.424  1.00 22.47           C  
ANISOU 4073  CZ  ARG A 512     2869   3463   2204    476    -39   -629       C  
ATOM   4074  NH1 ARG A 512     -20.876 -12.301  33.158  1.00 24.64           N  
ANISOU 4074  NH1 ARG A 512     2623   3712   3027    627   -175  -1466       N  
ATOM   4075  NH2 ARG A 512     -22.876 -11.231  32.910  1.00 22.02           N  
ANISOU 4075  NH2 ARG A 512     3251   2810   2303    517   -131   -825       N  
ATOM   4076  C   ARG A 512     -19.243 -18.281  35.335  1.00 23.79           C  
ANISOU 4076  C   ARG A 512     3105   3982   1952   1220   -294   -221       C  
ATOM   4077  O   ARG A 512     -19.420 -18.667  36.485  1.00 30.32           O  
ANISOU 4077  O   ARG A 512     3494   5810   2214   1909    397    278       O  
ATOM   4078  N   VAL A 513     -18.101 -18.471  34.694  1.00 19.56           N  
ANISOU 4078  N   VAL A 513     2796   2537   2099    377   -218   -119       N  
ATOM   4079  CA  VAL A 513     -16.942 -18.964  35.414  1.00 19.62           C  
ANISOU 4079  CA  VAL A 513     2765   2512   2178    326   -181   -229       C  
ATOM   4080  CB  VAL A 513     -16.428 -20.295  34.839  1.00 20.77           C  
ANISOU 4080  CB  VAL A 513     3030   2517   2343    308   -247   -353       C  
ATOM   4081  CG1 VAL A 513     -15.179 -20.771  35.556  1.00 21.81           C  
ANISOU 4081  CG1 VAL A 513     3153   2627   2507    351   -318   -436       C  
ATOM   4082  CG2 VAL A 513     -17.517 -21.368  34.901  1.00 22.09           C  
ANISOU 4082  CG2 VAL A 513     2986   2733   2672    246   -106   -650       C  
ATOM   4083  C   VAL A 513     -15.899 -17.854  35.365  1.00 19.14           C  
ANISOU 4083  C   VAL A 513     2960   2384   1927    244    150    -80       C  
ATOM   4084  O   VAL A 513     -15.549 -17.394  34.285  1.00 23.54           O  
ANISOU 4084  O   VAL A 513     3444   3460   2038   -297     32    258       O  
ATOM   4085  N   MET A 514     -15.463 -17.412  36.539  1.00 16.95           N  
ANISOU 4085  N   MET A 514     2601   2023   1814    279    240     49       N  
ATOM   4086  CA  MET A 514     -14.473 -16.365  36.667  1.00 17.48           C  
ANISOU 4086  CA  MET A 514     2368   2038   2235    348    297     63       C  
ATOM   4087  CB  MET A 514     -14.953 -15.263  37.607  1.00 18.12           C  
ANISOU 4087  CB  MET A 514     2661   2049   2172    141    171    -50       C  
ATOM   4088  CG  MET A 514     -16.150 -14.522  37.068  1.00 18.45           C  
ANISOU 4088  CG  MET A 514     2821   2087   2102    230    349     40       C  
ATOM   4089  SD  MET A 514     -16.612 -13.188  38.173  1.00 19.35           S  
ANISOU 4089  SD  MET A 514     2887   1911   2553    246    116    -26       S  
ATOM   4090  CE  MET A 514     -17.999 -12.488  37.281  1.00 20.99           C  
ANISOU 4090  CE  MET A 514     2782   2361   2830    114     55    269       C  
ATOM   4091  C   MET A 514     -13.152 -16.956  37.170  1.00 18.46           C  
ANISOU 4091  C   MET A 514     2405   1793   2815    414    220     45       C  
ATOM   4092  O   MET A 514     -13.081 -18.063  37.659  1.00 19.88           O  
ANISOU 4092  O   MET A 514     2292   2430   2829    588    252    761       O  
ATOM   4093  N   GLY A 515     -12.083 -16.199  36.970  1.00 23.39           N  
ANISOU 4093  N   GLY A 515     2691   2220   3977    218     93     27       N  
ATOM   4094  CA  GLY A 515     -10.799 -16.575  37.479  1.00 23.85           C  
ANISOU 4094  CA  GLY A 515     2607   2643   3811    193    134   -387       C  
ATOM   4095  C   GLY A 515     -10.013 -17.336  36.443  1.00 22.92           C  
ANISOU 4095  C   GLY A 515     2679   2778   3251    248    170    -78       C  
ATOM   4096  O   GLY A 515      -9.775 -16.836  35.377  1.00 31.62           O  
ANISOU 4096  O   GLY A 515     4190   4193   3629    438    -87    329       O  
ATOM   4097  N   GLY A 516      -9.576 -18.543  36.814  1.00 22.26           N  
ANISOU 4097  N   GLY A 516     3131   2765   2561    391    722   -308       N  
ATOM   4098  CA  GLY A 516      -8.744 -19.391  36.000  1.00 19.51           C  
ANISOU 4098  CA  GLY A 516     2195   2568   2649     85    799     15       C  
ATOM   4099  C   GLY A 516      -7.279 -19.068  36.195  1.00 18.78           C  
ANISOU 4099  C   GLY A 516     2115   2314   2706    422    485   -211       C  
ATOM   4100  O   GLY A 516      -6.434 -19.711  35.573  1.00 19.67           O  
ANISOU 4100  O   GLY A 516     2167   2327   2980    161    684   -604       O  
ATOM   4101  OXT GLY A 516      -6.956 -18.160  36.986  1.00 21.20           O  
ANISOU 4101  OXT GLY A 516     2685   2687   2682    -40    182   -118       O  
TER    4102      GLY A 516                                                      
HETATM12270  O4  SO4 A 601       2.510  -8.114  14.976  1.00 12.91           O  
ANISOU12270  O4  SO4 A 601     1681   1544   1678    156    189     17       O  
HETATM12271  S   SO4 A 601       1.231  -8.457  14.280  1.00 12.82           S  
ANISOU12271  S   SO4 A 601     1676   1417   1775     82    153    123       S  
HETATM12272  O1  SO4 A 601       0.989  -9.890  14.285  1.00 14.08           O  
ANISOU12272  O1  SO4 A 601     1986   1394   1967    -92   -109     96       O  
HETATM12273  O2  SO4 A 601       1.257  -7.966  12.882  1.00 12.85           O  
ANISOU12273  O2  SO4 A 601     1862   1356   1663     26     -1    179       O  
HETATM12274  O3  SO4 A 601       0.154  -7.772  15.001  1.00 13.55           O  
ANISOU12274  O3  SO4 A 601     1629   1802   1715    174    176    -81       O  
HETATM12275  O4  SO4 A 602      14.488 -27.568  32.390  0.70 19.20           O  
ANISOU12275  O4  SO4 A 602     1805   2868   2619    324   -180   -525       O  
HETATM12276  S   SO4 A 602      13.170 -27.553  31.673  0.70 17.21           S  
ANISOU12276  S   SO4 A 602     1814   2214   2509    251   -184   -168       S  
HETATM12277  O1  SO4 A 602      13.292 -26.653  30.500  0.70 18.22           O  
ANISOU12277  O1  SO4 A 602     2277   2452   2193    -40     15   -205       O  
HETATM12278  O2  SO4 A 602      12.889 -28.935  31.157  0.70 20.91           O  
ANISOU12278  O2  SO4 A 602     2369   2388   3185     76   -502   -353       O  
HETATM12279  O3  SO4 A 602      12.082 -27.012  32.576  0.70 14.93           O  
ANISOU12279  O3  SO4 A 602     1656   1470   2545    514   -217    168       O  
HETATM12280  O4  SO4 A 603      15.552   0.238   7.115  1.00 35.64           O  
ANISOU12280  O4  SO4 A 603     5751   2327   5462   -217  -2223   -198       O  
HETATM12281  S   SO4 A 603      14.286  -0.256   6.526  1.00 29.97           S  
ANISOU12281  S   SO4 A 603     4577   2991   3818    555  -1157   -114       S  
HETATM12282  O1  SO4 A 603      14.562  -1.422   5.668  1.00 28.87           O  
ANISOU12282  O1  SO4 A 603     4288   2872   3807     50   -423   -261       O  
HETATM12283  O2  SO4 A 603      13.690   0.856   5.795  1.00 29.52           O  
ANISOU12283  O2  SO4 A 603     4286   3404   3523    831   -412    302       O  
HETATM12284  O3  SO4 A 603      13.325  -0.753   7.565  1.00 36.93           O  
ANISOU12284  O3  SO4 A 603     5873   3728   4429    142   -484   -419       O  
HETATM12285  O4  SO4 A 604      -3.028  13.719   2.391  1.00 26.76           O  
ANISOU12285  O4  SO4 A 604     4213   3121   2831   -204    275   -365       O  
HETATM12286  S   SO4 A 604      -3.694  13.439   1.094  1.00 30.54           S  
ANISOU12286  S   SO4 A 604     4963   3941   2700   1461    -96   -408       S  
HETATM12287  O1  SO4 A 604      -2.925  12.765   0.046  1.00 31.85           O  
ANISOU12287  O1  SO4 A 604     4769   3916   3415    295    755   -762       O  
HETATM12288  O2  SO4 A 604      -4.198  14.683   0.487  1.00 34.33           O  
ANISOU12288  O2  SO4 A 604     6036   4872   2132   2120    652    559       O  
HETATM12289  O3  SO4 A 604      -4.799  12.469   1.498  1.00 37.58           O  
ANISOU12289  O3  SO4 A 604     5708   5278   3293    645   -234    603       O  
HETATM12290  O4  SO4 A 605     -27.177  -2.650  22.440  0.50 23.46           O  
ANISOU12290  O4  SO4 A 605     3153   1743   4017    -12   -207    276       O  
HETATM12291  S   SO4 A 605     -28.210  -3.699  22.364  0.50 23.25           S  
ANISOU12291  S   SO4 A 605     3133   2410   3288   -211   -235     41       S  
HETATM12292  O1  SO4 A 605     -27.986  -4.690  21.260  0.50 25.01           O  
ANISOU12292  O1  SO4 A 605     3650   2280   3571    -24    141     26       O  
HETATM12293  O2  SO4 A 605     -29.515  -3.033  22.155  0.50 20.93           O  
ANISOU12293  O2  SO4 A 605     2720   1896   3335   -359   -318    205       O  
HETATM12294  O3  SO4 A 605     -28.221  -4.430  23.659  0.50 21.76           O  
ANISOU12294  O3  SO4 A 605     3353   2106   2808   -246    -55   -204       O  
HETATM12295  O4  SO4 A 606      19.359   4.591  32.291  1.00 44.17           O  
ANISOU12295  O4  SO4 A 606     4934   5027   6819  -1213  -2573   1817       O  
HETATM12296  S   SO4 A 606      20.752   4.996  31.891  1.00 41.53           S  
ANISOU12296  S   SO4 A 606     4438   5037   6303   -509  -2034    661       S  
HETATM12297  O1  SO4 A 606      20.769   6.235  31.126  1.00 43.47           O  
ANISOU12297  O1  SO4 A 606     6002   4790   5723  -1610  -1808    656       O  
HETATM12298  O2  SO4 A 606      21.196   3.922  30.998  1.00 47.69           O  
ANISOU12298  O2  SO4 A 606     5515   6210   6395     38   -291    512       O  
HETATM12299  O3  SO4 A 606      21.574   5.112  33.100  1.00 47.65           O  
ANISOU12299  O3  SO4 A 606     4347   6932   6825  -1096  -2177    608       O  
HETATM12300  O4  SO4 A 607      28.493 -10.895  26.811  0.70 30.59           O  
ANISOU12300  O4  SO4 A 607     2986   5164   3472    187   -234    557       O  
HETATM12301  S   SO4 A 607      28.778 -12.248  26.266  0.70 31.11           S  
ANISOU12301  S   SO4 A 607     2579   5712   3529    371   -531    159       S  
HETATM12302  O1  SO4 A 607      29.708 -12.067  25.129  0.70 34.54           O  
ANISOU12302  O1  SO4 A 607     2648   6072   4403    220    -90    419       O  
HETATM12303  O2  SO4 A 607      27.539 -12.945  25.778  0.70 23.26           O  
ANISOU12303  O2  SO4 A 607     2005   4082   2749    864   -375    499       O  
HETATM12304  O3  SO4 A 607      29.445 -13.080  27.281  0.70 35.20           O  
ANISOU12304  O3  SO4 A 607     3468   6019   3886    484   -591    518       O  
HETATM12305  O4  SO4 A 608      -0.144  -1.687   4.057  1.00 35.57           O  
ANISOU12305  O4  SO4 A 608     5338   3598   4577    161  -1396  -1707       O  
HETATM12306  S   SO4 A 608      -0.924  -1.818   2.762  1.00 28.02           S  
ANISOU12306  S   SO4 A 608     3588   3612   3445    163   -144   -946       S  
HETATM12307  O1  SO4 A 608      -0.143  -0.842   1.931  1.00 48.90           O  
ANISOU12307  O1  SO4 A 608     6872   5924   5781  -1232   -148    302       O  
HETATM12308  O2  SO4 A 608      -0.755  -3.180   2.123  1.00 33.82           O  
ANISOU12308  O2  SO4 A 608     4148   3963   4738   1445   -212  -1258       O  
HETATM12309  O3  SO4 A 608      -2.355  -1.267   2.793  1.00 38.89           O  
ANISOU12309  O3  SO4 A 608     4253   4718   5804   1080  -1222   -121       O  
HETATM12310  O3  GOL A 609       3.124   0.788  21.052  1.00 14.64           O  
ANISOU12310  O3  GOL A 609     2226   1731   1603   -201    236   -458       O  
HETATM12311  C3  GOL A 609       3.618   0.691  22.428  1.00 19.10           C  
ANISOU12311  C3  GOL A 609     2554   2710   1991   -382     39   -298       C  
HETATM12312  C2  GOL A 609       4.549   1.877  22.824  1.00 18.18           C  
ANISOU12312  C2  GOL A 609     2188   2316   2402    -82    247   -150       C  
HETATM12313  O2  GOL A 609       5.759   1.908  22.013  1.00 15.33           O  
ANISOU12313  O2  GOL A 609     1872   1995   1958   -125    199   -184       O  
HETATM12314  C1  GOL A 609       3.764   3.228  22.824  1.00 19.98           C  
ANISOU12314  C1  GOL A 609     2073   2416   3099    110     12     22       C  
HETATM12315  O1  GOL A 609       3.199   3.721  21.526  1.00 16.89           O  
ANISOU12315  O1  GOL A 609     1635   1917   2865     79    -53    -92       O  
HETATM12316  O3  GOL A 610      -3.944  -7.235  31.548  1.00 24.51           O  
ANISOU12316  O3  GOL A 610     3650   2653   3009   -319    565   -461       O  
HETATM12317  C3  GOL A 610      -4.720  -7.596  32.689  1.00 27.11           C  
ANISOU12317  C3  GOL A 610     4219   3390   2690   -498    317   -119       C  
HETATM12318  C2  GOL A 610      -5.431  -8.928  32.429  1.00 24.51           C  
ANISOU12318  C2  GOL A 610     3929   3053   2330    -87    259   -281       C  
HETATM12319  O2  GOL A 610      -6.293  -8.789  31.295  1.00 28.00           O  
ANISOU12319  O2  GOL A 610     3506   4066   3064    457    -39    -69       O  
HETATM12320  C1  GOL A 610      -6.271  -9.263  33.652  1.00 24.71           C  
ANISOU12320  C1  GOL A 610     3763   3220   2403    180    480   -536       C  
HETATM12321  O1  GOL A 610      -7.099 -10.403  33.397  1.00 30.43           O  
ANISOU12321  O1  GOL A 610     3993   3773   3793   -224    674  -1040       O  
HETATM12322  O3  GOL A 611      18.684 -16.372  20.599  1.00 37.77           O  
ANISOU12322  O3  GOL A 611     5600   4148   4601   1388    953    158       O  
HETATM12323  C3  GOL A 611      18.566 -15.796  19.292  1.00 31.18           C  
ANISOU12323  C3  GOL A 611     3112   4975   3757     21    833    249       C  
HETATM12324  C2  GOL A 611      19.735 -14.834  18.994  1.00 24.47           C  
ANISOU12324  C2  GOL A 611     2754   3192   3348    464    452    -50       C  
HETATM12325  O2  GOL A 611      21.017 -15.486  18.901  1.00 23.78           O  
ANISOU12325  O2  GOL A 611     2585   3579   2868    454    277    156       O  
HETATM12326  C1  GOL A 611      19.886 -13.683  20.006  1.00 20.62           C  
ANISOU12326  C1  GOL A 611     2085   3456   2292    216    359    276       C  
HETATM12327  O1  GOL A 611      20.711 -12.645  19.388  1.00 17.77           O  
ANISOU12327  O1  GOL A 611     1821   2678   2253    265   -145     73       O  
HETATM12437  O   HOH A 701     -12.845  18.668  25.853  1.00 27.33           O  
ANISOU12437  O   HOH A 701     3653   3565   3164   -285    418   -191       O  
HETATM12438  O   HOH A 702      -1.128  -7.939  44.756  1.00 42.63           O  
ANISOU12438  O   HOH A 702     5053   5508   5634   1894   2466   2887       O  
HETATM12439  O   HOH A 703      -3.278   0.598   3.952  1.00 31.82           O  
ANISOU12439  O   HOH A 703     2474   3920   5696    227    226  -1067       O  
HETATM12440  O   HOH A 704     -32.274  -1.249  29.960  1.00 29.10           O  
ANISOU12440  O   HOH A 704     3659   3350   4045    -29   -340    -74       O  
HETATM12441  O   HOH A 705       2.903  -3.702  42.800  1.00 38.25           O  
ANISOU12441  O   HOH A 705     4586   4034   5910    -80   1877  -1752       O  
HETATM12442  O   HOH A 706      -8.175  24.048  32.209  1.00 34.67           O  
ANISOU12442  O   HOH A 706     4187   5311   3672  -1901  -1510   2273       O  
HETATM12443  O   HOH A 707      27.106  -9.729  28.525  1.00 43.99           O  
ANISOU12443  O   HOH A 707     4884   6156   5673    452  -2093     76       O  
HETATM12444  O   HOH A 708     -29.848 -32.016   0.355  1.00 24.67           O  
ANISOU12444  O   HOH A 708     2820   3672   2879     66   -304   -599       O  
HETATM12445  O   HOH A 709       5.669  -2.567  21.671  1.00 17.53           O  
ANISOU12445  O   HOH A 709     2370   2832   1457   -333   -205   -117       O  
HETATM12446  O   HOH A 710      20.810   5.964  28.750  1.00 45.16           O  
ANISOU12446  O   HOH A 710     5768   6897   4492   -994   -461  -2138       O  
HETATM12447  O   HOH A 712      10.333  -4.032  32.675  1.00 25.91           O  
ANISOU12447  O   HOH A 712     3404   3515   2925   -241    -51    112       O  
HETATM12448  O   HOH A 713       6.435 -20.793  16.694  1.00 38.56           O  
ANISOU12448  O   HOH A 713     6303   5178   3167   -280   1008    180       O  
HETATM12449  O   HOH A 714      -3.627  26.441  23.167  1.00 41.31           O  
ANISOU12449  O   HOH A 714     4881   4618   6195    963  -1379   -786       O  
HETATM12450  O   HOH A 715      -2.138  -9.087  31.124  1.00 27.45           O  
ANISOU12450  O   HOH A 715     3372   4391   2667    732     72   -306       O  
HETATM12451  O   HOH A 716     -27.541  -2.718  25.483  1.00 23.49           O  
ANISOU12451  O   HOH A 716     3060   2398   3468    -92    678   -671       O  
HETATM12452  O   HOH A 717       2.064  26.088  22.866  1.00 24.12           O  
ANISOU12452  O   HOH A 717     3447   2113   3605   -735   1162   -436       O  
HETATM12453  O   HOH A 718      -6.948  15.737  46.724  1.00 22.20           O  
ANISOU12453  O   HOH A 718     3426   2356   2652     47    377   -419       O  
HETATM12454  O   HOH A 719       3.954   8.014   3.918  1.00 31.11           O  
ANISOU12454  O   HOH A 719     3315   5758   2747   1311    477  -1137       O  
HETATM12455  O   HOH A 720       2.243  24.002  28.452  1.00 46.60           O  
ANISOU12455  O   HOH A 720     6347   5659   5699  -4345  -2413   -477       O  
HETATM12456  O   HOH A 721     -16.346  11.856  23.478  1.00 27.43           O  
ANISOU12456  O   HOH A 721     4113   3491   2817    -32    149    -34       O  
HETATM12457  O   HOH A 723       5.785  14.904  34.611  1.00 36.28           O  
ANISOU12457  O   HOH A 723     5080   5136   3566    -21    633   -324       O  
HETATM12458  O   HOH A 724      -9.896 -11.395  38.462  1.00 24.87           O  
ANISOU12458  O   HOH A 724     2796   4727   1926   1111    245   -207       O  
HETATM12459  O   HOH A 725       6.329  -1.520  25.343  1.00 27.36           O  
ANISOU12459  O   HOH A 725     3331   3483   3582   -511   -505   -815       O  
HETATM12460  O   HOH A 726       8.056  26.350   4.284  1.00 40.70           O  
ANISOU12460  O   HOH A 726     5337   5835   4291  -1298    580  -1361       O  
HETATM12461  O   HOH A 727     -46.897 -24.191  17.043  1.00 56.62           O  
ANISOU12461  O   HOH A 727     7664   6709   7140  -1260   2580   -180       O  
HETATM12462  O   HOH A 728      -9.809 -14.469  49.974  1.00 45.17           O  
ANISOU12462  O   HOH A 728     4688   7978   4495   1165    477   1333       O  
HETATM12463  O   HOH A 729       8.744  15.568   7.086  1.00 18.51           O  
ANISOU12463  O   HOH A 729     2643   1942   2448   -550    401     84       O  
HETATM12464  O   HOH A 730      -5.204  -9.504  29.095  1.00 33.71           O  
ANISOU12464  O   HOH A 730     4740   5236   2832   1953    802    316       O  
HETATM12465  O   HOH A 731       2.600  -0.557  14.191  1.00 13.00           O  
ANISOU12465  O   HOH A 731     1781   1520   1638     34     84   -225       O  
HETATM12466  O   HOH A 732      10.116   7.544  23.869  1.00 21.70           O  
ANISOU12466  O   HOH A 732     2569   2872   2802   -121   -142   -264       O  
HETATM12467  O   HOH A 733     -23.805  13.807  36.241  1.00 46.52           O  
ANISOU12467  O   HOH A 733     4152   6037   7485   -420  -1633   2834       O  
HETATM12468  O   HOH A 734     -18.011   8.311  25.296  1.00 18.40           O  
ANISOU12468  O   HOH A 734     3146   1951   1893     58   -243   -265       O  
HETATM12469  O   HOH A 735      -5.135  19.951  39.174  1.00 25.81           O  
ANISOU12469  O   HOH A 735     4642   2654   2507   -619    452     28       O  
HETATM12470  O   HOH A 738      -1.009  -5.691  20.911  1.00 26.89           O  
ANISOU12470  O   HOH A 738     4930   2368   2918     22   1858   -279       O  
HETATM12471  O   HOH A 739     -33.786  -6.042  51.097  1.00 23.48           O  
ANISOU12471  O   HOH A 739     3080   2490   3350    -47    408    -83       O  
HETATM12472  O   HOH A 741       6.671 -26.223  46.288  1.00 26.22           O  
ANISOU12472  O   HOH A 741     3812   3287   2861    672   -594    383       O  
HETATM12473  O   HOH A 742     -27.439  -3.852  18.854  1.00 25.31           O  
ANISOU12473  O   HOH A 742     2865   2266   4484   -805   -767    523       O  
HETATM12474  O   HOH A 743       7.554   5.834  27.741  1.00 26.02           O  
ANISOU12474  O   HOH A 743     2579   4070   3236    267   -241  -1158       O  
HETATM12475  O   HOH A 744     -40.168  -1.345  28.390  1.00 29.11           O  
ANISOU12475  O   HOH A 744     3954   3806   3298    342  -1119   -581       O  
HETATM12476  O   HOH A 745      18.843   4.230  27.679  1.00 30.80           O  
ANISOU12476  O   HOH A 745     3884   3437   4378    129   -172     19       O  
HETATM12477  O   HOH A 746      19.751  18.608  14.779  1.00 42.21           O  
ANISOU12477  O   HOH A 746     1784   6078   8176   -954   -123   -111       O  
HETATM12478  O   HOH A 747     -33.789  -6.665  47.124  1.00 29.35           O  
ANISOU12478  O   HOH A 747     3193   3852   4107   -134    976   -305       O  
HETATM12479  O   HOH A 748       3.303  10.963  39.196  1.00 31.61           O  
ANISOU12479  O   HOH A 748     3571   4405   4034   -784   -554  -1730       O  
HETATM12480  O   HOH A 749     -35.946 -28.832  13.153  1.00 38.54           O  
ANISOU12480  O   HOH A 749     3669   4136   6838   -336    206    993       O  
HETATM12481  O   HOH A 750      21.965 -18.784  32.900  1.00 44.53           O  
ANISOU12481  O   HOH A 750     6810   5581   4526   1704    276   1210       O  
HETATM12482  O   HOH A 751      29.096  -6.692  13.050  1.00 37.69           O  
ANISOU12482  O   HOH A 751     5794   5213   3310  -1527    424   -551       O  
HETATM12483  O   HOH A 752     -17.380  -8.764  35.823  1.00 16.82           O  
ANISOU12483  O   HOH A 752     3314   1349   1727     -9   -374     11       O  
HETATM12484  O   HOH A 753     -26.897  -0.107  24.335  1.00 19.38           O  
ANISOU12484  O   HOH A 753     2892   2282   2189   -156    246     62       O  
HETATM12485  O   HOH A 754      -1.024 -24.094  31.511  1.00 26.95           O  
ANISOU12485  O   HOH A 754     5384   2968   1885  -1241   -844    362       O  
HETATM12486  O   HOH A 755       6.407  -7.510  23.578  1.00 14.12           O  
ANISOU12486  O   HOH A 755     1611   1908   1845    -95   -140   -275       O  
HETATM12487  O   HOH A 756      17.912 -20.007  25.813  1.00 31.93           O  
ANISOU12487  O   HOH A 756     4001   3651   4480    879    255   -404       O  
HETATM12488  O   HOH A 757       2.681  18.655   4.254  1.00 29.38           O  
ANISOU12488  O   HOH A 757     3384   4091   3687   -118    240   1008       O  
HETATM12489  O   HOH A 758      -4.250  -3.722  19.338  1.00 28.63           O  
ANISOU12489  O   HOH A 758     4719   1534   4624   -624    147   -236       O  
HETATM12490  O   HOH A 759      22.940  -7.746  33.727  1.00 31.08           O  
ANISOU12490  O   HOH A 759     3248   3825   4735    601   1141    168       O  
HETATM12491  O   HOH A 760      20.531 -16.702  38.402  1.00 36.52           O  
ANISOU12491  O   HOH A 760     5332   5312   3231   1531  -1407   -338       O  
HETATM12492  O   HOH A 761      -3.723 -19.815  35.573  1.00 14.04           O  
ANISOU12492  O   HOH A 761     2234   1738   1360    203    122     71       O  
HETATM12493  O   HOH A 762     -13.217 -13.096  46.579  1.00 21.90           O  
ANISOU12493  O   HOH A 762     2526   2403   3390    371    509     22       O  
HETATM12494  O   HOH A 763     -13.303  -3.871  17.890  1.00 35.79           O  
ANISOU12494  O   HOH A 763     4387   5699   3510   -949  -1598    534       O  
HETATM12495  O   HOH A 764     -39.593 -10.061  33.121  1.00 40.99           O  
ANISOU12495  O   HOH A 764     6897   4870   3805  -1304     -8    858       O  
HETATM12496  O   HOH A 765       5.060  29.329  19.280  1.00 54.49           O  
ANISOU12496  O   HOH A 765     8417   5498   6788  -1231   2796   -841       O  
HETATM12497  O   HOH A 766     -15.900  -2.370  52.507  1.00 22.76           O  
ANISOU12497  O   HOH A 766     3863   2937   1846     70   -377   -562       O  
HETATM12498  O   HOH A 767       7.907  -0.938  32.839  1.00 25.32           O  
ANISOU12498  O   HOH A 767     3237   3193   3187    473   -122   -116       O  
HETATM12499  O   HOH A 769      13.050  28.724   8.546  1.00 36.87           O  
ANISOU12499  O   HOH A 769     4006   3471   6533  -1581   1934   -679       O  
HETATM12500  O   HOH A 770       1.733  13.639  10.315  1.00 16.44           O  
ANISOU12500  O   HOH A 770     1977   2099   2169    -71    -33    346       O  
HETATM12501  O   HOH A 771      30.709   0.952  18.005  1.00 47.09           O  
ANISOU12501  O   HOH A 771     4735   5297   7859  -1292  -1564   1711       O  
HETATM12502  O   HOH A 772     -45.456 -21.013  18.402  1.00 31.33           O  
ANISOU12502  O   HOH A 772     4729   3825   3350   -808     24   -152       O  
HETATM12503  O   HOH A 773       6.580   6.928  18.312  1.00 13.17           O  
ANISOU12503  O   HOH A 773     1744   1533   1726   -104   -113   -479       O  
HETATM12504  O   HOH A 774      -8.864  21.483  24.558  1.00 21.83           O  
ANISOU12504  O   HOH A 774     3686   1925   2682     92   -629   -572       O  
HETATM12505  O   HOH A 776       0.675  21.698  36.073  1.00 25.10           O  
ANISOU12505  O   HOH A 776     3951   2689   2896   -972    736   -564       O  
HETATM12506  O   HOH A 777      20.002   3.507  25.349  1.00 36.21           O  
ANISOU12506  O   HOH A 777     6016   2995   4745     12    201   -542       O  
HETATM12507  O   HOH A 779      -9.430  -5.095  27.097  1.00 21.56           O  
ANISOU12507  O   HOH A 779     3009   2185   2995   -678   -231    256       O  
HETATM12508  O   HOH A 780      18.038 -17.373  31.663  1.00 22.56           O  
ANISOU12508  O   HOH A 780     2113   3405   3051    472   -648    588       O  
HETATM12509  O   HOH A 781      -9.676  14.561  45.242  1.00 23.79           O  
ANISOU12509  O   HOH A 781     3066   4086   1888   -311    424    239       O  
HETATM12510  O   HOH A 782     -10.789 -21.865  51.861  1.00 37.57           O  
ANISOU12510  O   HOH A 782     4904   5168   4200    460   1554   -660       O  
HETATM12511  O   HOH A 783      -4.610   5.038  47.529  1.00 26.87           O  
ANISOU12511  O   HOH A 783     4204   3695   2308  -1155   -659   -398       O  
HETATM12512  O   HOH A 784      14.153  25.219  16.820  1.00 35.36           O  
ANISOU12512  O   HOH A 784     4800   3638   4995  -1332   -282     12       O  
HETATM12513  O   HOH A 785      15.241  13.675  24.308  1.00 38.33           O  
ANISOU12513  O   HOH A 785     4196   5960   4403  -2118   -899    907       O  
HETATM12514  O   HOH A 786      22.019 -13.050  37.704  1.00 37.30           O  
ANISOU12514  O   HOH A 786     4021   6428   3721   -155    109     90       O  
HETATM12515  O   HOH A 787       5.341   4.861  20.026  1.00 14.24           O  
ANISOU12515  O   HOH A 787     1987   1576   1846     -7   -206    -50       O  
HETATM12516  O   HOH A 788     -20.935   2.826  52.449  1.00 21.55           O  
ANISOU12516  O   HOH A 788     2163   3877   2147    668    580    402       O  
HETATM12517  O   HOH A 789      11.181   1.104   9.268  1.00 25.23           O  
ANISOU12517  O   HOH A 789     3157   3211   3217  -1150   -937    767       O  
HETATM12518  O   HOH A 790     -20.390  15.051  45.812  1.00 37.50           O  
ANISOU12518  O   HOH A 790     2909   4279   7059   -320    608  -2787       O  
HETATM12519  O   HOH A 791     -22.014  -9.871  25.938  1.00 38.45           O  
ANISOU12519  O   HOH A 791     4981   3801   5824   -800    650     -9       O  
HETATM12520  O   HOH A 792     -14.597 -47.635  14.869  1.00 22.32           O  
ANISOU12520  O   HOH A 792     3028   2709   2742    309   -361    414       O  
HETATM12521  O   HOH A 793       1.549 -28.352  35.354  1.00 26.02           O  
ANISOU12521  O   HOH A 793     2912   2580   4391    719    382    311       O  
HETATM12522  O   HOH A 794      12.786   3.156  20.525  1.00 22.88           O  
ANISOU12522  O   HOH A 794     1747   4337   2607    522    -44  -1507       O  
HETATM12523  O   HOH A 795     -23.066  13.363  27.560  1.00 18.58           O  
ANISOU12523  O   HOH A 795     2767   2102   2188    154    221   -424       O  
HETATM12524  O   HOH A 796      22.131  -4.568   1.248  1.00 23.34           O  
ANISOU12524  O   HOH A 796     3207   3070   2588   -410    912   -345       O  
HETATM12525  O   HOH A 797     -20.916  18.456  31.772  1.00 38.37           O  
ANISOU12525  O   HOH A 797     6465   2330   5784    771    428   1185       O  
HETATM12526  O   HOH A 798      21.921 -17.633  30.423  1.00 27.61           O  
ANISOU12526  O   HOH A 798     2403   4060   4024   1008    264    756       O  
HETATM12527  O   HOH A 799       7.182  -0.470  22.385  1.00 21.79           O  
ANISOU12527  O   HOH A 799     2227   2429   3621   -176   -327   -242       O  
HETATM12528  O   HOH A 800      -1.781  -2.957  41.922  1.00 37.48           O  
ANISOU12528  O   HOH A 800     5485   4541   4213   -750    473  -2065       O  
HETATM12529  O   HOH A 801       5.782  24.011  10.299  1.00 22.66           O  
ANISOU12529  O   HOH A 801     2850   3244   2517  -1072    369   -248       O  
HETATM12530  O   HOH A 802      29.627  -6.412  28.478  1.00 44.77           O  
ANISOU12530  O   HOH A 802     4866   7146   4998    939  -1983  -1001       O  
HETATM12531  O   HOH A 803      24.969  -7.279  10.006  1.00 29.47           O  
ANISOU12531  O   HOH A 803     5230   3177   2789  -1059   1087   -458       O  
HETATM12532  O   HOH A 805     -23.105  -1.789  46.681  1.00 12.72           O  
ANISOU12532  O   HOH A 805     2021   1432   1380    302    447   -267       O  
HETATM12533  O   HOH A 806      -2.517 -31.459  49.335  1.00 34.55           O  
ANISOU12533  O   HOH A 806     4739   3722   4665   -208   1216   1121       O  
HETATM12534  O   HOH A 807       0.696   1.717  25.678  1.00 21.42           O  
ANISOU12534  O   HOH A 807     3455   1731   2951     89   -662     92       O  
HETATM12535  O   HOH A 808      -0.120 -22.110  28.482  1.00 26.20           O  
ANISOU12535  O   HOH A 808     3968   3521   2462  -1535  -1344   1212       O  
HETATM12536  O   HOH A 809      -1.712  28.791  12.548  1.00 35.10           O  
ANISOU12536  O   HOH A 809     5113   2836   5387   -765   1715     -1       O  
HETATM12537  O   HOH A 810      15.389  -2.264  39.804  1.00 36.18           O  
ANISOU12537  O   HOH A 810     5233   4732   3778    185   -259  -1498       O  
HETATM12538  O   HOH A 811      -1.311  -9.291  41.809  1.00 16.74           O  
ANISOU12538  O   HOH A 811     2387   2027   1946     97      9     41       O  
HETATM12539  O   HOH A 812      14.005 -11.249  48.724  1.00 46.56           O  
ANISOU12539  O   HOH A 812     3648   9037   5003  -1183   -638  -2138       O  
HETATM12540  O   HOH A 813      11.588   5.098  23.950  1.00 18.41           O  
ANISOU12540  O   HOH A 813     2472   2284   2236   -428   -245   -445       O  
HETATM12541  O   HOH A 814       9.821  -9.029  45.906  1.00 46.78           O  
ANISOU12541  O   HOH A 814     8002   6145   3625   2712  -2205  -1757       O  
HETATM12542  O   HOH A 815     -37.591  -2.137  22.453  1.00 14.59           O  
ANISOU12542  O   HOH A 815     1692   2047   1803   -255     64   -308       O  
HETATM12543  O   HOH A 816       8.418  25.327   6.771  1.00 31.91           O  
ANISOU12543  O   HOH A 816     5577   2830   3714   -434   1372   -282       O  
HETATM12544  O   HOH A 817      10.060   0.391  11.426  1.00 22.05           O  
ANISOU12544  O   HOH A 817     2886   2212   3278   -580    623  -1207       O  
HETATM12545  O   HOH A 818      11.753  -7.899  27.692  1.00 13.69           O  
ANISOU12545  O   HOH A 818     1808   1799   1594    -59   -248    -76       O  
HETATM12546  O   HOH A 819      19.040 -11.050  17.938  1.00 14.75           O  
ANISOU12546  O   HOH A 819     2124   1639   1838    208    -99   -120       O  
HETATM12547  O   HOH A 820     -16.671   2.341  27.406  1.00 20.29           O  
ANISOU12547  O   HOH A 820     4799   1552   1358  -1012    107    -53       O  
HETATM12548  O   HOH A 821       8.804  13.675  30.015  1.00 36.45           O  
ANISOU12548  O   HOH A 821     5764   3428   4656    364  -1857  -1063       O  
HETATM12549  O   HOH A 822     -35.309 -31.199   8.848  1.00 37.70           O  
ANISOU12549  O   HOH A 822     4967   3330   6027  -1276  -1160    484       O  
HETATM12550  O   HOH A 823     -24.229 -11.963  49.739  1.00 33.54           O  
ANISOU12550  O   HOH A 823     6033   3023   3688    131    486   1153       O  
HETATM12551  O   HOH A 824       2.790  18.757  29.676  1.00 17.98           O  
ANISOU12551  O   HOH A 824     2521   2204   2104    130    361   -253       O  
HETATM12552  O   HOH A 825      11.337 -27.171  28.719  1.00 17.33           O  
ANISOU12552  O   HOH A 825     2396   2018   2167    504     41    -20       O  
HETATM12553  O   HOH A 826      19.827   0.639  18.740  1.00 35.89           O  
ANISOU12553  O   HOH A 826     5343   4002   4290    540    223     67       O  
HETATM12554  O   HOH A 827     -10.010  21.911  16.980  1.00 23.12           O  
ANISOU12554  O   HOH A 827     2575   2587   3622    -38    224    523       O  
HETATM12555  O   HOH A 828      -4.635 -12.038  22.773  1.00 21.29           O  
ANISOU12555  O   HOH A 828     2188   2942   2958    333   -383    -55       O  
HETATM12556  O   HOH A 829      14.979  23.183   5.286  1.00 35.59           O  
ANISOU12556  O   HOH A 829     5087   4103   4330  -1192   1850    635       O  
HETATM12557  O   HOH A 830       1.001  -2.970  12.662  1.00 16.59           O  
ANISOU12557  O   HOH A 830     2500   1893   1911    417    265    -88       O  
HETATM12558  O   HOH A 831      -8.231   4.577  50.831  1.00 47.19           O  
ANISOU12558  O   HOH A 831     6618   5262   6049    208  -2516  -1564       O  
HETATM12559  O   HOH A 832     -32.547   1.446  38.643  1.00 26.66           O  
ANISOU12559  O   HOH A 832     5073   3052   2002  -2305    624   -734       O  
HETATM12560  O   HOH A 833      -8.463   2.086  40.707  1.00 14.80           O  
ANISOU12560  O   HOH A 833     1980   2024   1617     65    -50   -322       O  
HETATM12561  O   HOH A 834       4.795   0.530  26.189  1.00 26.01           O  
ANISOU12561  O   HOH A 834     3270   3329   3281    853    626    724       O  
HETATM12562  O   HOH A 835     -37.245   0.334  37.262  1.00 37.31           O  
ANISOU12562  O   HOH A 835     6373   3594   4207   -866   2734   -442       O  
HETATM12563  O   HOH A 836      30.774   3.129  20.854  1.00 45.27           O  
ANISOU12563  O   HOH A 836     5770   5630   5799     76   2093   -513       O  
HETATM12564  O   HOH A 837      -6.748 -14.947  44.016  1.00 19.93           O  
ANISOU12564  O   HOH A 837     3627   1808   2135    603    629    -72       O  
HETATM12565  O   HOH A 838       2.074  -2.586  41.095  1.00 28.45           O  
ANISOU12565  O   HOH A 838     5765   2978   2063  -1004   -605    276       O  
HETATM12566  O   HOH A 839     -11.816  11.702  18.888  1.00 14.24           O  
ANISOU12566  O   HOH A 839     2110   1544   1754   -326    604   -290       O  
HETATM12567  O   HOH A 840     -12.334   4.618  14.276  1.00 12.35           O  
ANISOU12567  O   HOH A 840     1629   1349   1715    184   -186    -76       O  
HETATM12568  O   HOH A 841      11.443  -6.187   9.286  1.00 14.24           O  
ANISOU12568  O   HOH A 841     1973   1581   1854    -45    106      5       O  
HETATM12569  O   HOH A 842      12.804  19.818   4.982  1.00 36.88           O  
ANISOU12569  O   HOH A 842     4159   4340   5512    437    179   -777       O  
HETATM12570  O   HOH A 843     -23.774  17.571  38.896  1.00 38.45           O  
ANISOU12570  O   HOH A 843     4476   3965   6167   1056   1404   1526       O  
HETATM12571  O   HOH A 844       7.191   5.492  24.084  1.00 16.31           O  
ANISOU12571  O   HOH A 844     2324   1795   2075    134    326   -109       O  
HETATM12572  O   HOH A 845      -7.151  24.133  30.022  1.00 24.58           O  
ANISOU12572  O   HOH A 845     2874   2319   4144   -238   -216  -1118       O  
HETATM12573  O   HOH A 846      -0.660  11.075  10.870  1.00 12.38           O  
ANISOU12573  O   HOH A 846     1718   1497   1487    -76     19     98       O  
HETATM12574  O   HOH A 847     -30.497  -5.884  23.876  1.00 34.08           O  
ANISOU12574  O   HOH A 847     3128   7143   2676  -1020   -226   -743       O  
HETATM12575  O   HOH A 848     -14.902 -17.699  47.083  1.00 31.82           O  
ANISOU12575  O   HOH A 848     6104   2782   3204   2105  -1221   -588       O  
HETATM12576  O   HOH A 849      23.072  -2.443  26.424  1.00 25.19           O  
ANISOU12576  O   HOH A 849     3790   2877   2902  -1512   -562   -519       O  
HETATM12577  O   HOH A 850      -9.894  -0.096  50.174  1.00 22.05           O  
ANISOU12577  O   HOH A 850     2846   3374   2155    425   -133    118       O  
HETATM12578  O   HOH A 851      13.196 -18.177  45.512  1.00 32.37           O  
ANISOU12578  O   HOH A 851     4204   5066   3026    996    249    929       O  
HETATM12579  O   HOH A 852      11.660 -28.259  34.972  1.00 24.30           O  
ANISOU12579  O   HOH A 852     2615   3460   3155    554   -455    884       O  
HETATM12580  O   HOH A 853     -22.228  11.455  48.422  1.00 33.57           O  
ANISOU12580  O   HOH A 853     2661   5383   4709    786   -705  -3335       O  
HETATM12581  O   HOH A 854     -17.033  16.102  39.434  1.00 15.67           O  
ANISOU12581  O   HOH A 854     2800   1556   1596     15    233     10       O  
HETATM12582  O   HOH A 855     -40.361 -27.566  13.492  1.00 29.86           O  
ANISOU12582  O   HOH A 855     4116   3755   3475    176    617   1096       O  
HETATM12583  O   HOH A 856       0.341  23.928  22.735  1.00 19.53           O  
ANISOU12583  O   HOH A 856     3099   2234   2087   -572    403   -140       O  
HETATM12584  O   HOH A 857      -3.670  13.816  47.283  1.00 21.27           O  
ANISOU12584  O   HOH A 857     3726   2030   2324   -283   -339   -425       O  
HETATM12585  O   HOH A 859     -26.966  12.416  41.515  1.00 21.86           O  
ANISOU12585  O   HOH A 859     2154   2465   3688    157    821    468       O  
HETATM12586  O   HOH A 860      27.230 -13.819  22.981  1.00 36.18           O  
ANISOU12586  O   HOH A 860     3513   5909   4325   1851    372    -94       O  
HETATM12587  O   HOH A 861      -7.591  25.572  17.997  1.00 30.99           O  
ANISOU12587  O   HOH A 861     4363   2155   5254    597    -62   -536       O  
HETATM12588  O   HOH A 862      14.482  22.842  22.179  1.00 42.27           O  
ANISOU12588  O   HOH A 862     5212   6513   4335  -1703   -135  -1787       O  
HETATM12589  O   HOH A 863     -32.105   7.442  30.475  1.00 21.72           O  
ANISOU12589  O   HOH A 863     2390   3442   2417   -218    365   -592       O  
HETATM12590  O   HOH A 864     -38.237 -27.620  11.699  1.00 23.24           O  
ANISOU12590  O   HOH A 864     3101   2213   3513   -340    454    416       O  
HETATM12591  O   HOH A 865     -21.024   3.862  29.629  1.00 14.14           O  
ANISOU12591  O   HOH A 865     1942   1288   2140    -89    -36   -107       O  
HETATM12592  O   HOH A 866      -5.099 -14.766  34.391  1.00 35.48           O  
ANISOU12592  O   HOH A 866     3607   6501   3374   -250   -232   1389       O  
HETATM12593  O   HOH A 867      13.112  -8.196  14.572  1.00 13.29           O  
ANISOU12593  O   HOH A 867     1544   1723   1781     83     72    -82       O  
HETATM12594  O   HOH A 869       2.691 -11.135  46.432  1.00 35.21           O  
ANISOU12594  O   HOH A 869     3172   6257   3948   -742   -259    688       O  
HETATM12595  O   HOH A 870      13.777  11.594  16.397  1.00 38.65           O  
ANISOU12595  O   HOH A 870     6478   3798   4409    744  -1783   -640       O  
HETATM12596  O   HOH A 871       9.159 -28.421  36.251  1.00 25.78           O  
ANISOU12596  O   HOH A 871     2276   3642   3876   1080    278   1578       O  
HETATM12597  O   HOH A 872       1.304   3.125  36.562  1.00 19.41           O  
ANISOU12597  O   HOH A 872     3343   1928   2102    -72    435    -39       O  
HETATM12598  O   HOH A 873     -27.203   0.445  47.544  1.00 15.54           O  
ANISOU12598  O   HOH A 873     2160   1878   1865     83    366    -82       O  
HETATM12599  O   HOH A 874     -34.763   2.516  41.125  1.00 39.38           O  
ANISOU12599  O   HOH A 874     5575   4550   4836  -2224   3024  -2438       O  
HETATM12600  O   HOH A 875     -22.106 -47.912  13.941  1.00 27.10           O  
ANISOU12600  O   HOH A 875     4399   2571   3324   -767   -820    -25       O  
HETATM12601  O   HOH A 877       3.753  -2.750  33.146  1.00 23.02           O  
ANISOU12601  O   HOH A 877     2761   3015   2969    529    107  -1001       O  
HETATM12602  O   HOH A 878       2.344   2.751  30.079  1.00 21.04           O  
ANISOU12602  O   HOH A 878     3575   2191   2226     65    579   -131       O  
HETATM12603  O   HOH A 879      21.800  -8.893  15.067  1.00 17.26           O  
ANISOU12603  O   HOH A 879     1957   2462   2139   -244    -96     33       O  
HETATM12604  O   HOH A 880      -0.795  -2.392  37.733  1.00 29.48           O  
ANISOU12604  O   HOH A 880     2309   3668   5221   -573   1092  -2408       O  
HETATM12605  O   HOH A 881      23.527 -13.706  21.531  1.00 23.19           O  
ANISOU12605  O   HOH A 881     3174   2672   2962    408    175     35       O  
HETATM12606  O   HOH A 882      16.619   3.189   9.634  1.00 26.22           O  
ANISOU12606  O   HOH A 882     2582   2820   4558   -348   -676    736       O  
HETATM12607  O   HOH A 883     -10.720   2.052  17.663  1.00 19.53           O  
ANISOU12607  O   HOH A 883     2525   2805   2089   -601    -72    159       O  
HETATM12608  O   HOH A 884       7.900   2.407  10.176  1.00 20.08           O  
ANISOU12608  O   HOH A 884     2797   1535   3297   -250   -413   -232       O  
HETATM12609  O   HOH A 885       3.438  26.457  15.767  1.00 38.22           O  
ANISOU12609  O   HOH A 885     4325   4424   5772   -785   1947   1101       O  
HETATM12610  O   HOH A 886      18.232   2.943  30.142  1.00 21.51           O  
ANISOU12610  O   HOH A 886     2638   2381   3153   -822   -475    -79       O  
HETATM12611  O   HOH A 887     -26.961   6.575  29.363  1.00 16.10           O  
ANISOU12611  O   HOH A 887     2546   1844   1724    229    302   -151       O  
HETATM12612  O   HOH A 888     -13.367  16.556  27.391  1.00 24.64           O  
ANISOU12612  O   HOH A 888     4285   2097   2979    976     12   -293       O  
HETATM12613  O   HOH A 889      -2.301 -22.116  36.105  1.00 14.24           O  
ANISOU12613  O   HOH A 889     1723   2033   1651    224    134    308       O  
HETATM12614  O   HOH A 890     -19.489  11.239  45.248  1.00 15.94           O  
ANISOU12614  O   HOH A 890     2331   1607   2117    157    760   -149       O  
HETATM12615  O   HOH A 891     -26.277 -41.716  16.530  1.00 31.31           O  
ANISOU12615  O   HOH A 891     3442   5072   3381    590    750   1480       O  
HETATM12616  O   HOH A 892       9.979  -1.357  38.846  1.00 44.47           O  
ANISOU12616  O   HOH A 892     5531   4965   6398  -1757   2779  -1541       O  
HETATM12617  O   HOH A 893       1.687 -27.387  40.354  1.00 18.84           O  
ANISOU12617  O   HOH A 893     2657   2246   2254    503    200    164       O  
HETATM12618  O   HOH A 894       2.202   7.704  33.448  1.00 19.48           O  
ANISOU12618  O   HOH A 894     2691   2861   1847   -458   -189   -570       O  
HETATM12619  O   HOH A 895      23.027  -7.398  24.064  1.00 18.11           O  
ANISOU12619  O   HOH A 895     1543   3237   2098     91   -192    150       O  
HETATM12620  O   HOH A 896      21.265 -17.060  16.597  1.00 25.03           O  
ANISOU12620  O   HOH A 896     3420   2747   3340    287   -198   -141       O  
HETATM12621  O   HOH A 897      12.678  25.209  20.512  1.00 41.36           O  
ANISOU12621  O   HOH A 897     6406   4886   4420   -279   -548  -2236       O  
HETATM12622  O   HOH A 898     -20.713   0.541  53.830  1.00 25.82           O  
ANISOU12622  O   HOH A 898     4293   3077   2440    575   -422    -99       O  
HETATM12623  O   HOH A 899      11.445  16.235   8.182  1.00 20.29           O  
ANISOU12623  O   HOH A 899     2472   2525   2712   -709    101    212       O  
HETATM12624  O   HOH A 900      -1.733 -15.540  21.188  1.00 18.72           O  
ANISOU12624  O   HOH A 900     2634   2253   2225    -45   -357   -238       O  
HETATM12625  O   HOH A 901     -33.273  -8.680  45.144  1.00 31.85           O  
ANISOU12625  O   HOH A 901     3791   4218   4092   -600    461   1181       O  
HETATM12626  O   HOH A 902       7.558  -0.574  11.725  1.00 17.51           O  
ANISOU12626  O   HOH A 902     2191   1703   2755   -136     79    317       O  
HETATM12627  O   HOH A 903     -36.100  -3.568  37.423  1.00 30.62           O  
ANISOU12627  O   HOH A 903     5309   3283   3040   -934   1033   -351       O  
HETATM12628  O   HOH A 904      -8.105  -4.669  36.876  1.00 19.14           O  
ANISOU12628  O   HOH A 904     3331   2118   1821    257   -127    -13       O  
HETATM12629  O   HOH A 905      -2.554  -7.986  18.121  1.00 32.78           O  
ANISOU12629  O   HOH A 905     4749   4014   3692   1831   1179    821       O  
HETATM12630  O   HOH A 906      -6.622  21.541  41.018  1.00 18.07           O  
ANISOU12630  O   HOH A 906     3223   2020   1623   -881     -2   -108       O  
HETATM12631  O   HOH A 907      -9.341  -4.153  50.463  1.00 55.34           O  
ANISOU12631  O   HOH A 907     8434   4643   7950   1627   1523   1851       O  
HETATM12632  O   HOH A 908      17.181 -26.675  24.518  1.00 41.83           O  
ANISOU12632  O   HOH A 908     3733   5902   6256    199    251  -2023       O  
HETATM12633  O   HOH A 909      -7.391   1.760  47.990  1.00 21.44           O  
ANISOU12633  O   HOH A 909     2900   3366   1877    148    323     18       O  
HETATM12634  O   HOH A 910     -25.188   4.388  40.050  1.00 14.16           O  
ANISOU12634  O   HOH A 910     2160   1519   1700     73    452      7       O  
HETATM12635  O   HOH A 911       6.239 -26.181  49.760  1.00 42.07           O  
ANISOU12635  O   HOH A 911     4856   6923   4204   2326   -193    175       O  
HETATM12636  O   HOH A 912     -15.988  21.728  42.673  1.00 26.59           O  
ANISOU12636  O   HOH A 912     2730   4460   2910    -59    907   -671       O  
HETATM12637  O   HOH A 913     -27.565  11.396  26.674  1.00 17.32           O  
ANISOU12637  O   HOH A 913     2583   1989   2008    -57    270   -139       O  
HETATM12638  O   HOH A 914     -18.934   0.577  27.477  1.00 16.65           O  
ANISOU12638  O   HOH A 914     3020   1653   1651   -115    177    -67       O  
HETATM12639  O   HOH A 915       6.785  11.943   5.049  1.00 28.89           O  
ANISOU12639  O   HOH A 915     3817   4412   2746  -1058   1128    -60       O  
HETATM12640  O   HOH A 916      15.938  12.920  12.178  1.00 44.56           O  
ANISOU12640  O   HOH A 916     3702   5199   8031    602   1414   2755       O  
HETATM12641  O   HOH A 917       9.128  -4.931  43.331  1.00 41.67           O  
ANISOU12641  O   HOH A 917     6477   3926   5429   1113   -577   -481       O  
HETATM12642  O   HOH A 918       4.375   5.154   5.811  1.00 17.13           O  
ANISOU12642  O   HOH A 918     2513   2241   1753     29    247   -248       O  
HETATM12643  O   HOH A 919      15.329 -20.616  28.769  1.00 20.35           O  
ANISOU12643  O   HOH A 919     2781   2707   2244   -285    606   -271       O  
HETATM12644  O   HOH A 920     -27.865   9.980  38.248  1.00 28.38           O  
ANISOU12644  O   HOH A 920     4754   3650   2377    995   -125    154       O  
HETATM12645  O   HOH A 921     -12.018 -20.350  50.462  1.00 33.81           O  
ANISOU12645  O   HOH A 921     5121   4779   2944   -724    780     74       O  
HETATM12646  O   HOH A 922      17.788   0.870  16.909  1.00 29.56           O  
ANISOU12646  O   HOH A 922     3314   3923   3992   -840    808   -409       O  
HETATM12647  O   HOH A 923     -32.414  -8.270  37.403  1.00 25.00           O  
ANISOU12647  O   HOH A 923     2519   3549   3428    143    411    780       O  
HETATM12648  O   HOH A 924       6.734 -10.715  45.990  1.00 32.09           O  
ANISOU12648  O   HOH A 924     3834   5455   2904    977    532    126       O  
HETATM12649  O   HOH A 925      27.701  -1.247  17.313  1.00 24.14           O  
ANISOU12649  O   HOH A 925     2148   3939   3083   -787    302    -21       O  
HETATM12650  O   HOH A 926       8.982   7.722  26.429  1.00 26.67           O  
ANISOU12650  O   HOH A 926     2970   3621   3540    -48   -428   -412       O  
HETATM12651  O   HOH A 927      10.284  10.193   5.278  1.00 38.63           O  
ANISOU12651  O   HOH A 927     7737   4234   2704   1129   1209    -31       O  
HETATM12652  O   HOH A 928       3.823 -23.210  51.527  1.00 30.57           O  
ANISOU12652  O   HOH A 928     4393   3963   3258    310   -243    408       O  
HETATM12653  O   HOH A 929      14.669  -5.471  21.782  1.00 17.16           O  
ANISOU12653  O   HOH A 929     2050   2593   1875    254    -86   -391       O  
HETATM12654  O   HOH A 930      17.199 -18.563  22.540  1.00 27.41           O  
ANISOU12654  O   HOH A 930     2899   2310   5203    100    173   -119       O  
HETATM12655  O   HOH A 931     -22.673  -2.071  41.827  1.00 12.49           O  
ANISOU12655  O   HOH A 931     1738   1473   1534    229    379   -184       O  
HETATM12656  O   HOH A 932      -4.987 -15.626  41.267  1.00 16.29           O  
ANISOU12656  O   HOH A 932     2311   2014   1864    680    353    -37       O  
HETATM12657  O   HOH A 933      26.004  -5.905  33.458  1.00 41.21           O  
ANISOU12657  O   HOH A 933     4681   5829   5147  -1038   -328     -7       O  
HETATM12658  O   HOH A 934      -5.503  22.290  37.536  1.00 15.23           O  
ANISOU12658  O   HOH A 934     2263   1560   1963   -356    225   -419       O  
HETATM12659  O   HOH A 935     -19.788  16.637  38.892  1.00 21.57           O  
ANISOU12659  O   HOH A 935     3252   2008   2935    155    410     31       O  
HETATM12660  O   HOH A 936     -17.466 -28.678  35.267  1.00 43.55           O  
ANISOU12660  O   HOH A 936     4222   6455   5868   1533    563    811       O  
HETATM12661  O   HOH A 937      25.988  -6.954  21.532  1.00 20.67           O  
ANISOU12661  O   HOH A 937     1805   3445   2600    270   -193     61       O  
HETATM12662  O   HOH A 938      -7.188  10.219  13.861  1.00 10.96           O  
ANISOU12662  O   HOH A 938     1497   1663   1002     -8    102   -165       O  
HETATM12663  O   HOH A 939      27.974  -2.635  33.948  1.00 44.33           O  
ANISOU12663  O   HOH A 939     4021   6742   6079  -1574  -1644    211       O  
HETATM12664  O   HOH A 940      -2.761  15.333   5.413  1.00 24.49           O  
ANISOU12664  O   HOH A 940     2462   1890   4951    -83   -442   -185       O  
HETATM12665  O   HOH A 941       8.604   7.105  16.397  1.00 13.58           O  
ANISOU12665  O   HOH A 941     2021   1479   1660   -141     65   -130       O  
HETATM12666  O   HOH A 942      -6.808 -34.522  42.233  1.00 35.91           O  
ANISOU12666  O   HOH A 942     6688   3328   3628    645    501    354       O  
HETATM12667  O   HOH A 943      -7.696  -7.848  46.821  1.00 32.45           O  
ANISOU12667  O   HOH A 943     7021   3190   2117  -1609  -1130    351       O  
HETATM12668  O   HOH A 944      15.174 -27.751  35.041  1.00 42.05           O  
ANISOU12668  O   HOH A 944     5408   4102   6468    992  -2433     91       O  
HETATM12669  O   HOH A 945      15.259   5.294   5.913  1.00 33.07           O  
ANISOU12669  O   HOH A 945     4075   4990   3497   -589    466    977       O  
HETATM12670  O   HOH A 946       6.191  -0.788  36.407  1.00 25.34           O  
ANISOU12670  O   HOH A 946     3308   3120   3199     22    111   -454       O  
HETATM12671  O   HOH A 947       2.793 -26.664  37.717  1.00 17.00           O  
ANISOU12671  O   HOH A 947     2620   2034   1804    733    125    349       O  
HETATM12672  O   HOH A 948      -0.326   4.246  45.575  1.00 37.34           O  
ANISOU12672  O   HOH A 948     6001   4998   3186  -1397   -469  -1326       O  
HETATM12673  O   HOH A 950     -18.602  -6.716  32.911  1.00 16.43           O  
ANISOU12673  O   HOH A 950     2140   1943   2158    177   -198   -230       O  
HETATM12674  O   HOH A 951     -13.636   1.715  31.809  1.00 13.41           O  
ANISOU12674  O   HOH A 951     1847   1303   1945   -281    173    -89       O  
HETATM12675  O   HOH A 952       4.810   0.799  14.998  1.00 13.63           O  
ANISOU12675  O   HOH A 952     2044   1579   1552   -118     82     79       O  
HETATM12676  O   HOH A 953      -4.449  -3.626   3.071  1.00 35.57           O  
ANISOU12676  O   HOH A 953     3807   6728   2979   2378   -988  -1140       O  
HETATM12677  O   HOH A 954     -15.695   1.917  22.220  1.00 30.06           O  
ANISOU12677  O   HOH A 954     4621   3285   3513    719  -1107   -932       O  
HETATM12678  O   HOH A 955      -8.226 -32.988  47.740  1.00 37.73           O  
ANISOU12678  O   HOH A 955     5834   2878   5621    401    742    394       O  
HETATM12679  O   HOH A 956     -11.582  17.759  12.670  1.00 13.83           O  
ANISOU12679  O   HOH A 956     2077   1343   1834    134   -211    -67       O  
HETATM12680  O   HOH A 957       7.683 -28.398  42.597  1.00 24.88           O  
ANISOU12680  O   HOH A 957     2750   3927   2775    318    -70    563       O  
HETATM12681  O   HOH A 958       0.582  24.471  12.843  1.00 21.89           O  
ANISOU12681  O   HOH A 958     2692   3588   2036   -317    549    651       O  
HETATM12682  O   HOH A 959     -12.118  19.706  31.763  1.00 16.85           O  
ANISOU12682  O   HOH A 959     2796   1573   2030    -45    590   -501       O  
HETATM12683  O   HOH A 960      24.375   3.913  25.184  1.00 43.54           O  
ANISOU12683  O   HOH A 960     3976   7783   4784   -421   -394    257       O  
HETATM12684  O   HOH A 961       0.191   1.273   9.495  1.00 24.03           O  
ANISOU12684  O   HOH A 961     3410   3253   2464  -1976  -1017   1085       O  
HETATM12685  O   HOH A 962     -18.482   0.466  50.867  1.00 15.05           O  
ANISOU12685  O   HOH A 962     2566   1459   1692    174    488   -204       O  
HETATM12686  O   HOH A 963      10.815  25.406  16.306  1.00 27.09           O  
ANISOU12686  O   HOH A 963     4379   2397   3513  -1211    201   -989       O  
HETATM12687  O   HOH A 964      11.215  13.116   6.723  1.00 33.71           O  
ANISOU12687  O   HOH A 964     3599   3321   5886   -324   1831   1079       O  
HETATM12688  O   HOH A 965      13.371 -28.095  37.267  1.00 37.14           O  
ANISOU12688  O   HOH A 965     3974   4990   5147    844   -666   -217       O  
HETATM12689  O   HOH A 966      12.624  12.124  14.200  1.00 24.19           O  
ANISOU12689  O   HOH A 966     3442   2202   3546   -395    750   -561       O  
HETATM12690  O   HOH A 967     -33.833   3.106  31.223  1.00 29.47           O  
ANISOU12690  O   HOH A 967     4116   3726   3354     78     43   -564       O  
HETATM12691  O   HOH A 968     -24.922   0.307  45.974  1.00 18.10           O  
ANISOU12691  O   HOH A 968     2347   2999   1529    539    579    427       O  
HETATM12692  O   HOH A 969      -1.732  -0.068  45.946  1.00 38.57           O  
ANISOU12692  O   HOH A 969     4435   7416   2801    -80    367    801       O  
HETATM12693  O   HOH A 970      -0.447 -25.218  38.602  1.00 17.72           O  
ANISOU12693  O   HOH A 970     2554   2339   1837    687    527    230       O  
HETATM12694  O   HOH A 971       1.375 -14.067  18.922  1.00 27.50           O  
ANISOU12694  O   HOH A 971     2910   4713   2823   -708    554  -1064       O  
HETATM12695  O   HOH A 972      -6.248  -3.041  17.878  1.00 38.12           O  
ANISOU12695  O   HOH A 972     5106   3319   6059    268  -1788  -2460       O  
HETATM12696  O   HOH A 973       3.426  31.940   5.304  1.00 49.47           O  
ANISOU12696  O   HOH A 973     7542   3095   8160    -49   -693   2488       O  
HETATM12697  O   HOH A 974      -5.400  25.782  20.349  1.00 39.55           O  
ANISOU12697  O   HOH A 974     4584   4144   6296   -590    546   -769       O  
HETATM12698  O   HOH A 975       8.720  22.437   8.979  1.00 22.52           O  
ANISOU12698  O   HOH A 975     2674   2075   3808   -765    455   -144       O  
HETATM12699  O   HOH A 976      30.571  -7.091  16.590  1.00 30.07           O  
ANISOU12699  O   HOH A 976     2882   4304   4239    714   1175    417       O  
HETATM12700  O   HOH A 977     -30.811  -5.059  45.032  1.00 23.71           O  
ANISOU12700  O   HOH A 977     2936   2376   3696    204    675   -397       O  
HETATM12701  O   HOH A 979       0.631   0.091  12.019  1.00 13.22           O  
ANISOU12701  O   HOH A 979     2239   1372   1409    138    151   -102       O  
HETATM12702  O   HOH A 980      -6.470  19.587  10.190  1.00 13.85           O  
ANISOU12702  O   HOH A 980     2051   1640   1568   -154     31   -301       O  
HETATM12703  O   HOH A 981      10.983  10.003  17.611  1.00 22.93           O  
ANISOU12703  O   HOH A 981     2044   3801   2865     95   -523  -1086       O  
HETATM12704  O   HOH A 982     -27.308  13.510  29.607  1.00 32.27           O  
ANISOU12704  O   HOH A 982     4231   3366   4663    978    866   -352       O  
HETATM12705  O   HOH A 983     -22.751  -1.111  31.947  1.00 12.70           O  
ANISOU12705  O   HOH A 983     1777   1292   1755    -48    174   -379       O  
HETATM12706  O   HOH A 984     -45.104 -23.004  11.308  1.00 30.33           O  
ANISOU12706  O   HOH A 984     3323   5443   2758    541   -276   -812       O  
HETATM12707  O   HOH A 985       4.619 -24.979  21.391  1.00 32.19           O  
ANISOU12707  O   HOH A 985     4461   2804   4964    514    412    201       O  
HETATM12708  O   HOH A 986     -34.166  -4.352  42.683  1.00 29.60           O  
ANISOU12708  O   HOH A 986     3391   2864   4991    652   -286  -1229       O  
HETATM12709  O   HOH A 987      -4.843   1.970  16.349  1.00 12.33           O  
ANISOU12709  O   HOH A 987     1846   1539   1299    -37     74   -107       O  
HETATM12710  O   HOH A 988       3.308   5.552  30.319  1.00 22.77           O  
ANISOU12710  O   HOH A 988     2336   3344   2968    666    159   -846       O  
HETATM12711  O   HOH A 989      -2.450  18.274  41.871  1.00 21.82           O  
ANISOU12711  O   HOH A 989     3680   2026   2582    222   -489   -698       O  
HETATM12712  O   HOH A 990      26.923  -9.557  17.194  1.00 20.71           O  
ANISOU12712  O   HOH A 990     1695   3225   2948    418    199    -35       O  
HETATM12713  O   HOH A 991       1.663 -20.805  21.120  1.00 24.85           O  
ANISOU12713  O   HOH A 991     3183   2798   3458   -247   -418   -154       O  
HETATM12714  O   HOH A 992     -11.269  -3.963  37.194  1.00 17.83           O  
ANISOU12714  O   HOH A 992     2554   2192   2027    240    552    319       O  
HETATM12715  O   HOH A 993      16.679 -11.982  18.966  1.00 15.55           O  
ANISOU12715  O   HOH A 993     1776   1997   2135    287     64     12       O  
HETATM12716  O   HOH A 994       3.137 -28.439  49.154  1.00 37.23           O  
ANISOU12716  O   HOH A 994     6308   4179   3657    733    127   1533       O  
HETATM12717  O   HOH A 995      14.557  13.136  17.904  1.00 38.14           O  
ANISOU12717  O   HOH A 995     4750   4501   5241   -266    909    155       O  
HETATM12718  O   HOH A 996     -37.258   1.874  33.612  1.00 37.19           O  
ANISOU12718  O   HOH A 996     4912   3898   5318    789  -1393  -1209       O  
HETATM12719  O   HOH A 997      27.230   5.830   5.321  1.00 46.46           O  
ANISOU12719  O   HOH A 997     7764   3243   6645   -598   1716    216       O  
HETATM12720  O   HOH A 998      -8.789  19.661  20.782  1.00 19.98           O  
ANISOU12720  O   HOH A 998     3331   1668   2589    141    842    258       O  
HETATM12721  O   HOH A 999      20.955  -0.833  -0.875  1.00 40.89           O  
ANISOU12721  O   HOH A 999     4476   5771   5286  -1313   -357    417       O  
HETATM12722  O   HOH A1000     -13.821  -6.181  32.464  1.00 25.17           O  
ANISOU12722  O   HOH A1000     4367   2053   3141    469    544   -175       O  
HETATM12723  O   HOH A1001       3.102  21.550  35.426  1.00 35.92           O  
ANISOU12723  O   HOH A1001     3921   4422   5305   -670    446   -314       O  
HETATM12724  O   HOH A1002      29.513  -9.616  16.368  1.00 28.99           O  
ANISOU12724  O   HOH A1002     1920   4606   4486    359   1226    358       O  
HETATM12725  O   HOH A1003      17.346 -29.105  25.017  1.00 39.97           O  
ANISOU12725  O   HOH A1003     3165   7512   4509   -565   -486  -1697       O  
HETATM12726  O   HOH A1005       1.169 -12.232  15.910  1.00 24.98           O  
ANISOU12726  O   HOH A1005     2851   3339   3301   -597   -343    323       O  
HETATM12727  O   HOH A1006      16.426 -21.300  38.782  1.00 29.75           O  
ANISOU12727  O   HOH A1006     2869   4604   3830   -434    -95   -792       O  
HETATM12728  O   HOH A1007     -25.006  -3.583  26.585  1.00 30.87           O  
ANISOU12728  O   HOH A1007     3445   3262   5019   -624    777   -496       O  
HETATM12729  O   HOH A1008      11.383   2.694  28.376  1.00 30.98           O  
ANISOU12729  O   HOH A1008     3384   4965   3418     14     76   -280       O  
HETATM12730  O   HOH A1009     -18.334 -49.041  21.445  1.00 32.77           O  
ANISOU12730  O   HOH A1009     5554   2761   4134   -252   -333    909       O  
HETATM12731  O   HOH A1010      13.637   7.828   6.148  1.00 33.21           O  
ANISOU12731  O   HOH A1010     3634   4441   4543   -967   1848  -1720       O  
HETATM12732  O   HOH A1011      -1.978  -4.018  14.877  1.00 28.43           O  
ANISOU12732  O   HOH A1011     4549   3420   2833  -1212  -1226    860       O  
HETATM12733  O   HOH A1012      13.911 -13.061  15.389  1.00 14.90           O  
ANISOU12733  O   HOH A1012     2077   1498   2083   -216    184   -318       O  
HETATM12734  O   HOH A1013      24.175   3.040  21.793  1.00 24.70           O  
ANISOU12734  O   HOH A1013     3226   2843   3314   -496   -370   -380       O  
HETATM12735  O   HOH A1015      11.529  11.500  19.987  1.00 18.36           O  
ANISOU12735  O   HOH A1015     2207   2903   1863   -190   -126   -237       O  
HETATM12736  O   HOH A1016      -5.789  -2.534  42.071  1.00 40.73           O  
ANISOU12736  O   HOH A1016    10018   2192   3264    171     63   -174       O  
HETATM12737  O   HOH A1017     -11.392  -1.637   6.333  1.00 19.65           O  
ANISOU12737  O   HOH A1017     3311   1585   2570   -247   1089   -672       O  
HETATM12738  O   HOH A1018     -21.429  -9.108  30.640  1.00 29.19           O  
ANISOU12738  O   HOH A1018     4302   3164   3625   -459   -166   -637       O  
HETATM12739  O   HOH A1019      -1.189  -4.038  17.461  1.00 13.38           O  
ANISOU12739  O   HOH A1019     1599   1288   2195     77    -33   -394       O  
HETATM12740  O   HOH A1021     -14.918 -53.567  18.786  1.00 46.87           O  
ANISOU12740  O   HOH A1021     7518   2844   7447  -1152    871    484       O  
HETATM12741  O   HOH A1022     -37.928  -9.921  40.314  1.00 44.96           O  
ANISOU12741  O   HOH A1022     4545   5583   6952  -1760     39   1751       O  
HETATM12742  O   HOH A1023      23.678 -16.404  14.932  1.00 21.50           O  
ANISOU12742  O   HOH A1023     2742   2683   2741    466    -10   -345       O  
HETATM12743  O   HOH A1024     -11.626   9.016  20.534  1.00 19.16           O  
ANISOU12743  O   HOH A1024     2567   2847   1866     18    -11   -731       O  
HETATM12744  O   HOH A1025     -12.299  -5.759  34.451  1.00 38.97           O  
ANISOU12744  O   HOH A1025     2353   3687   8767    173   -666  -3452       O  
HETATM12745  O   HOH A1026      15.325 -14.872  17.093  1.00 17.60           O  
ANISOU12745  O   HOH A1026     2124   2631   1930    330    199   -171       O  
HETATM12746  O   HOH A1027      14.086  -8.582  42.933  1.00 28.61           O  
ANISOU12746  O   HOH A1027     4998   3460   2412   1086   -713   -392       O  
HETATM12747  O   HOH A1028      23.279  -6.829  21.329  1.00 17.36           O  
ANISOU12747  O   HOH A1028     1739   2709   2144   -356   -141    -55       O  
HETATM12748  O   HOH A1029     -17.293  20.491  38.613  1.00 41.03           O  
ANISOU12748  O   HOH A1029     4101   7812   3674   2660    498   -534       O  
HETATM12749  O   HOH A1030      -8.521 -12.656  36.360  1.00 44.08           O  
ANISOU12749  O   HOH A1030     9107   4290   3350   2639   1830    922       O  
HETATM12750  O   HOH A1031      20.732   0.476   2.883  1.00 36.65           O  
ANISOU12750  O   HOH A1031     5657   3572   4696     72   1384    825       O  
HETATM12751  O   HOH A1032      -4.052 -15.127  43.800  1.00 19.42           O  
ANISOU12751  O   HOH A1032     3224   2247   1908     58    275      5       O  
HETATM12752  O   HOH A1033     -31.611   8.303  34.048  1.00 27.57           O  
ANISOU12752  O   HOH A1033     3602   3318   3556    -41    724   -544       O  
HETATM12753  O   HOH A1034     -40.309  -7.384  44.186  1.00 43.80           O  
ANISOU12753  O   HOH A1034     3718   3844   9080   -208   1853  -2108       O  
HETATM12754  O   HOH A1035      -0.432 -18.637  52.883  1.00 38.44           O  
ANISOU12754  O   HOH A1035     6673   5506   2424     12    408    287       O  
HETATM12755  O   HOH A1036     -22.588   0.248  29.397  1.00 15.08           O  
ANISOU12755  O   HOH A1036     1934   1659   2134    -62    215     54       O  
HETATM12756  O   HOH A1037     -13.174   5.851  52.276  1.00 46.37           O  
ANISOU12756  O   HOH A1037     7593   6656   3369  -3067  -2303   -478       O  
HETATM12757  O   HOH A1038      -8.910  18.174  10.658  1.00 14.43           O  
ANISOU12757  O   HOH A1038     2241   1345   1895     71    121      1       O  
HETATM12758  O   HOH A1039     -18.364   6.921  27.672  1.00 15.06           O  
ANISOU12758  O   HOH A1039     2350   1396   1974    144    186   -219       O  
HETATM12759  O   HOH A1040      -0.417  12.793   8.615  1.00 22.17           O  
ANISOU12759  O   HOH A1040     3333   2408   2681  -1086   -528    738       O  
HETATM12760  O   HOH A1041       3.392  28.627  11.521  1.00 27.87           O  
ANISOU12760  O   HOH A1041     3792   3390   3404   -274    713    487       O  
HETATM12761  O   HOH A1042       6.403  33.150   7.110  1.00 44.62           O  
ANISOU12761  O   HOH A1042     6339   3122   7491    108   -678   1562       O  
HETATM12762  O   HOH A1043       1.773 -29.786  38.158  1.00 38.77           O  
ANISOU12762  O   HOH A1043     4093   4946   5690   -275    194    341       O  
HETATM12763  O   HOH A1044      30.439  -0.949  26.436  1.00 38.53           O  
ANISOU12763  O   HOH A1044     4445   6600   3593  -1913  -1162    559       O  
HETATM12764  O   HOH A1045      29.082  -9.826  13.577  1.00 29.46           O  
ANISOU12764  O   HOH A1045     2213   5014   3963     55    744    -52       O  
HETATM12765  O   HOH A1046       5.525  14.415   1.609  1.00 54.09           O  
ANISOU12765  O   HOH A1046    11430   5363   3757  -1226    316   -152       O  
HETATM12766  O   HOH A1047      17.949  24.098  10.458  1.00 32.70           O  
ANISOU12766  O   HOH A1047     2882   3337   6203   -858   1502    615       O  
HETATM12767  O   HOH A1048     -21.097   1.746  26.151  1.00 27.71           O  
ANISOU12767  O   HOH A1048     3696   3869   2961    257    727  -1005       O  
HETATM12768  O   HOH A1049      -7.166  28.041  11.455  1.00 37.88           O  
ANISOU12768  O   HOH A1049     3822   3019   7550     60    972   1066       O  
HETATM12769  O   HOH A1050      17.318  -5.772  21.072  1.00 22.95           O  
ANISOU12769  O   HOH A1050     1790   2047   4882   -234    989   -469       O  
HETATM12770  O   HOH A1051      16.774 -29.402  32.211  1.00 47.23           O  
ANISOU12770  O   HOH A1051     5884   6612   5447   2674   -519    916       O  
HETATM12771  O   HOH A1052       2.824  26.178  12.405  1.00 29.40           O  
ANISOU12771  O   HOH A1052     4535   3165   3470   -823    -78    285       O  
HETATM12772  O   HOH A1053      -8.175 -10.593  49.651  1.00 24.94           O  
ANISOU12772  O   HOH A1053     4304   3008   2161    984   -437   -766       O  
HETATM12773  O   HOH A1054       6.409  20.002  27.928  1.00 32.06           O  
ANISOU12773  O   HOH A1054     2805   5155   4220   -416   -120  -1736       O  
HETATM12774  O   HOH A1055     -24.045  15.240  31.651  1.00 33.38           O  
ANISOU12774  O   HOH A1055     3159   1984   7540    266     65   -787       O  
HETATM12775  O   HOH A1056     -14.061 -33.806  37.175  1.00 41.09           O  
ANISOU12775  O   HOH A1056     6954   2496   6163   -530    730   -668       O  
HETATM12776  O   HOH A1057     -32.499  -6.752  16.191  1.00 38.34           O  
ANISOU12776  O   HOH A1057     7091   3055   4421    541  -1590   -817       O  
HETATM12777  O   HOH A1058      -9.431  -2.028  47.249  1.00 28.34           O  
ANISOU12777  O   HOH A1058     3949   3281   3537     17    981   -359       O  
HETATM12778  O   HOH A1059     -10.003 -11.779  34.101  1.00 47.33           O  
ANISOU12778  O   HOH A1059     3685   7758   6537    668   2901  -1170       O  
HETATM12779  O   HOH A1060     -18.187 -18.079  31.933  1.00 42.16           O  
ANISOU12779  O   HOH A1060     5060   8040   2919   1188   -228    648       O  
HETATM12780  O   HOH A1061      25.229 -18.128  20.932  1.00 42.64           O  
ANISOU12780  O   HOH A1061     7967   4847   3388    622    377    -93       O  
HETATM12781  O   HOH A1062      -6.077   7.064  14.348  1.00 10.90           O  
ANISOU12781  O   HOH A1062     1562   1256   1323    -77   -118    -61       O  
HETATM12782  O   HOH A1063      10.207   0.332  27.994  1.00 21.14           O  
ANISOU12782  O   HOH A1063     2772   2916   2343    205    345   -425       O  
HETATM12783  O   HOH A1064     -11.312  11.355  12.946  1.00 15.07           O  
ANISOU12783  O   HOH A1064     2607   1595   1522    -19   -136    -30       O  
HETATM12784  O   HOH A1065       3.540  26.031  27.374  1.00 47.66           O  
ANISOU12784  O   HOH A1065     7305   7722   3080  -1889    972  -1747       O  
HETATM12785  O   HOH A1066      17.542  15.554  11.718  1.00 30.08           O  
ANISOU12785  O   HOH A1066     2596   3851   4981   -172    635   -815       O  
HETATM12786  O   HOH A1067       3.736  20.751  28.114  1.00 17.93           O  
ANISOU12786  O   HOH A1067     2495   2586   1729   -691   -168   -227       O  
HETATM12787  O   HOH A1068       1.295 -12.219  48.532  1.00 30.42           O  
ANISOU12787  O   HOH A1068     3714   5262   2579   1685   -322    145       O  
HETATM12788  O   HOH A1069     -10.285   0.912  14.544  1.00 28.07           O  
ANISOU12788  O   HOH A1069     4839   3160   2663    680   1177    658       O  
HETATM12789  O   HOH A1070      21.680  -6.622  39.000  1.00 37.55           O  
ANISOU12789  O   HOH A1070     3635   7156   3475    938   -481    180       O  
HETATM12790  O   HOH A1071      -1.507 -11.455  48.099  1.00 21.52           O  
ANISOU12790  O   HOH A1071     3458   2308   2407     24   -204   -191       O  
HETATM12791  O   HOH A1072     -26.435  -7.978  50.115  1.00 21.96           O  
ANISOU12791  O   HOH A1072     3014   1916   3411    463   -154   -371       O  
HETATM12792  O   HOH A1073      -7.166  -1.146  46.098  1.00 25.23           O  
ANISOU12792  O   HOH A1073     3159   3163   3264    768    349   1451       O  
HETATM12793  O   HOH A1074       9.311  18.313  25.080  1.00 24.26           O  
ANISOU12793  O   HOH A1074     2991   3052   3172    -30   -527    299       O  
HETATM12794  O   HOH A1075      -9.106  24.588  26.068  1.00 34.27           O  
ANISOU12794  O   HOH A1075     4436   3675   4909    908   -699     65       O  
HETATM12795  O   HOH A1076      -3.062  -1.709  38.988  1.00 21.93           O  
ANISOU12795  O   HOH A1076     2402   1590   4338     59    792   -777       O  
HETATM12796  O   HOH A1077     -20.164  17.551  36.106  1.00 20.11           O  
ANISOU12796  O   HOH A1077     2333   2371   2934    217    552   -548       O  
HETATM12797  O   HOH A1078      -4.847  -3.879  39.452  1.00 17.62           O  
ANISOU12797  O   HOH A1078     2390   1644   2658     75   -120    -12       O  
HETATM12798  O   HOH A1079      27.040  -5.633  30.955  1.00 30.35           O  
ANISOU12798  O   HOH A1079     2961   4994   3577    158   -428    102       O  
HETATM12799  O   HOH A1080      -4.770   9.151  42.335  1.00 23.69           O  
ANISOU12799  O   HOH A1080     2407   3157   3435    423    543    401       O  
HETATM12800  O   HOH A1081      15.894 -18.181  45.751  1.00 46.05           O  
ANISOU12800  O   HOH A1081     3954   7699   5844    931   -917  -1058       O  
HETATM12801  O   HOH A1082      19.342 -10.086  15.325  1.00 14.69           O  
ANISOU12801  O   HOH A1082     1776   1898   1907    152     67    -17       O  
HETATM12802  O   HOH A1083       8.577 -31.101  35.176  1.00 31.99           O  
ANISOU12802  O   HOH A1083     4400   4939   2815  -1898     53   -808       O  
HETATM12803  O   HOH A1084     -39.009  -0.607  31.469  1.00 38.04           O  
ANISOU12803  O   HOH A1084     3614   6070   4770     90   -182   1484       O  
HETATM12804  O   HOH A1085     -12.050   3.248  21.321  1.00 16.76           O  
ANISOU12804  O   HOH A1085     2292   2059   2017    -44    690   -139       O  
HETATM12805  O   HOH A1086       7.129   2.602  29.513  1.00 26.87           O  
ANISOU12805  O   HOH A1086     3280   3422   3508   -447    414    187       O  
HETATM12806  O   HOH A1087      21.825 -20.402  36.263  1.00 45.15           O  
ANISOU12806  O   HOH A1087     4832   5509   6812    915  -1580   1182       O  
HETATM12807  O   HOH A1088      12.203   3.143  25.948  1.00 23.74           O  
ANISOU12807  O   HOH A1088     3973   2339   2706   -533   -751   -659       O  
HETATM12808  O   HOH A1089     -10.418  -4.493  42.597  1.00 26.02           O  
ANISOU12808  O   HOH A1089     5050   2459   2376   -730    888   -491       O  
HETATM12809  O   HOH A1090     -24.724  16.183  41.966  1.00 32.43           O  
ANISOU12809  O   HOH A1090     7106   1843   3370    433   2634     83       O  
HETATM12810  O   HOH A1091     -13.979  21.647  35.798  1.00 29.61           O  
ANISOU12810  O   HOH A1091     4103   2828   4320   -354    -13     47       O  
HETATM12811  O   HOH A1092     -10.123 -54.020  21.698  1.00 39.52           O  
ANISOU12811  O   HOH A1092     5798   5076   4140    791   -251   1515       O  
HETATM12812  O   HOH A1093       4.651  -0.846  41.071  1.00 30.12           O  
ANISOU12812  O   HOH A1093     3415   3474   4552   -350   -511   -478       O  
HETATM12813  O   HOH A1094      14.927  11.910   7.519  1.00 46.71           O  
ANISOU12813  O   HOH A1094     7483   3015   7249   -321   3927  -1235       O  
HETATM12814  O   HOH A1095       6.266 -17.028  50.825  1.00 28.41           O  
ANISOU12814  O   HOH A1095     4280   3974   2538   -167   -572    116       O  
HETATM12815  O   HOH A1096      14.842 -28.660  40.998  1.00 35.03           O  
ANISOU12815  O   HOH A1096     4344   3227   5738   1082    603    406       O  
HETATM12816  O   HOH A1097      -2.176   1.757   8.211  1.00 19.24           O  
ANISOU12816  O   HOH A1097     2469   2346   2494   -415   -356    340       O  
HETATM12817  O   HOH A1098     -11.808  21.771  33.531  1.00 20.08           O  
ANISOU12817  O   HOH A1098     2648   2389   2590    388   -650  -1069       O  
HETATM12818  O   HOH A1099       7.543 -25.811  43.615  1.00 27.15           O  
ANISOU12818  O   HOH A1099     3821   3649   2842    517   -874    663       O  
HETATM12819  O   HOH A1100      -4.968 -28.189  51.425  1.00 24.69           O  
ANISOU12819  O   HOH A1100     3691   2967   2720    530   -553    714       O  
HETATM12820  O   HOH A1101     -22.360  -1.721  22.915  1.00 28.55           O  
ANISOU12820  O   HOH A1101     3948   3926   2973    548    -81    490       O  
HETATM12821  O   HOH A1102     -24.570   0.558  25.550  1.00 19.20           O  
ANISOU12821  O   HOH A1102     3033   1873   2389    362   -245   -627       O  
HETATM12822  O   HOH A1103       1.730  -8.218  45.297  1.00 41.63           O  
ANISOU12822  O   HOH A1103     5886   5130   4802   -757   -374   -361       O  
HETATM12823  O   HOH A1105      20.908  -9.926  38.670  1.00 26.52           O  
ANISOU12823  O   HOH A1105     1972   5648   2453   -830   -653    291       O  
HETATM12824  O   HOH A1106     -24.977 -25.385   8.731  1.00 27.60           O  
ANISOU12824  O   HOH A1106     2867   3540   4078    394   -122    -79       O  
HETATM12825  O   HOH A1107      33.355  -3.008  22.678  1.00 51.10           O  
ANISOU12825  O   HOH A1107     3679   4683  11053   -683  -1209   -340       O  
HETATM12826  O   HOH A1108     -27.352 -11.992  45.575  1.00 26.46           O  
ANISOU12826  O   HOH A1108     3165   1864   5025   -121   -566   -107       O  
HETATM12827  O   HOH A1109      13.332 -19.080  15.909  1.00 22.73           O  
ANISOU12827  O   HOH A1109     4403   2078   2155    805    612    228       O  
HETATM12828  O   HOH A1110      -7.545  21.954  22.063  1.00 26.72           O  
ANISOU12828  O   HOH A1110     4397   2273   3479    172   -699   -353       O  
HETATM12829  O   HOH A1111     -21.193  16.342  43.140  1.00 45.42           O  
ANISOU12829  O   HOH A1111     5114   3909   8233  -1614    759   -383       O  
HETATM12830  O   HOH A1112      14.888 -19.436  19.117  1.00 26.66           O  
ANISOU12830  O   HOH A1112     3761   3230   3138    716    896    274       O  
HETATM12831  O   HOH A1113      11.982  -6.186  43.963  1.00 32.04           O  
ANISOU12831  O   HOH A1113     3853   6026   2293  -1431   -167   -205       O  
HETATM12832  O   HOH A1114     -18.531 -48.759  14.277  1.00 33.50           O  
ANISOU12832  O   HOH A1114     5454   3583   3688    772   -491   1041       O  
HETATM12833  O   HOH A1115     -29.759  -1.472  43.260  1.00 21.07           O  
ANISOU12833  O   HOH A1115     2733   2335   2936    239    922    -61       O  
HETATM12834  O   HOH A1116     -12.033 -16.769  48.467  1.00 35.07           O  
ANISOU12834  O   HOH A1116     3209   5497   4619   1328   1237   -159       O  
HETATM12835  O   HOH A1117      -3.994  -0.073   7.116  1.00 19.74           O  
ANISOU12835  O   HOH A1117     2090   2167   3243    145   -311    271       O  
HETATM12836  O   HOH A1118     -25.360 -45.519  14.955  1.00 25.96           O  
ANISOU12836  O   HOH A1118     3063   3644   3154   -679     49    547       O  
HETATM12837  O   HOH A1119       2.364  29.514  20.911  1.00 43.33           O  
ANISOU12837  O   HOH A1119     7923   3877   4663   -954   -910  -1131       O  
HETATM12838  O   HOH A1120     -26.743  -5.641  51.711  1.00 29.28           O  
ANISOU12838  O   HOH A1120     5640   1987   3495   1244   3022    902       O  
HETATM12839  O   HOH A1121       9.456 -10.722  48.555  1.00 35.61           O  
ANISOU12839  O   HOH A1121     4534   4783   4210  -1297    685  -1271       O  
HETATM12840  O   HOH A1122     -11.830   1.683  51.458  1.00 25.50           O  
ANISOU12840  O   HOH A1122     3147   4915   1626   -470   -257     85       O  
HETATM12841  O   HOH A1124      15.706 -18.783  38.739  1.00 28.71           O  
ANISOU12841  O   HOH A1124     4070   4320   2517   -848   -397    212       O  
HETATM12842  O   HOH A1125      -5.138 -12.643  32.799  1.00 34.47           O  
ANISOU12842  O   HOH A1125     4628   4048   4419      3   1087  -1194       O  
HETATM12843  O   HOH A1126     -33.356   5.564  32.039  1.00 24.55           O  
ANISOU12843  O   HOH A1126     2160   3669   3497    131     26    843       O  
HETATM12844  O   HOH A1127      25.790 -14.791  29.388  1.00 44.29           O  
ANISOU12844  O   HOH A1127     5178   8314   3336   2282     77    656       O  
HETATM12845  O   HOH A1128     -28.849  13.728  32.498  1.00 47.75           O  
ANISOU12845  O   HOH A1128     3088   5320   9734   -192   -485  -2538       O  
HETATM12846  O   HOH A1129     -19.956   1.245  30.083  1.00 11.86           O  
ANISOU12846  O   HOH A1129     1823   1277   1406    -44     39     39       O  
HETATM12847  O   HOH A1130     -14.159 -28.463  45.796  1.00 55.64           O  
ANISOU12847  O   HOH A1130     6760   7942   6438  -3326   5323   -348       O  
HETATM12848  O   HOH A1131      -7.400 -17.258  33.361  1.00 30.67           O  
ANISOU12848  O   HOH A1131     3482   4256   3916    891    134   -244       O  
HETATM12849  O   HOH A1132       1.397 -16.795  18.108  1.00 37.26           O  
ANISOU12849  O   HOH A1132     6122   5733   2300   1461    965    465       O  
HETATM12850  O   HOH A1133     -14.154  20.517  30.077  1.00 26.95           O  
ANISOU12850  O   HOH A1133     2890   2753   4596   -512   -700   -272       O  
HETATM12851  O   HOH A1134     -34.755  -0.931  27.471  1.00 28.33           O  
ANISOU12851  O   HOH A1134     3515   3023   4225    636     86   -579       O  
HETATM12852  O   HOH A1135      27.417   4.209  27.231  1.00 41.20           O  
ANISOU12852  O   HOH A1135     4632   4187   6835  -1626    990  -2172       O  
HETATM12853  O   HOH A1136     -23.118  -1.393  27.033  1.00 20.40           O  
ANISOU12853  O   HOH A1136     2727   2538   2482    215    -46    -95       O  
HETATM12854  O   HOH A1137       2.662   1.811  27.480  1.00 19.70           O  
ANISOU12854  O   HOH A1137     2493   2977   2012    422   -107   -465       O  
HETATM12855  O   HOH A1138      -2.967  15.183   8.255  1.00 29.42           O  
ANISOU12855  O   HOH A1138     4746   2824   3605    348   1029    717       O  
HETATM12856  O   HOH A1139      -3.134 -14.921  51.092  1.00 38.83           O  
ANISOU12856  O   HOH A1139     3511   8657   2583   -433    323  -1012       O  
HETATM12857  O   HOH A1140     -11.745   8.716  48.447  1.00 29.81           O  
ANISOU12857  O   HOH A1140     3362   3517   4446   -991   -477   -904       O  
HETATM12858  O   HOH A1141      15.354  24.673   9.512  1.00 27.22           O  
ANISOU12858  O   HOH A1141     2966   3355   4021  -1562   1026   -292       O  
HETATM12859  O   HOH A1142     -14.720  24.143  39.490  1.00 36.23           O  
ANISOU12859  O   HOH A1142     4876   2410   6477   -401  -1872   -126       O  
HETATM12860  O   HOH A1143     -30.752 -11.753  45.685  1.00 30.35           O  
ANISOU12860  O   HOH A1143     5281   2981   3268   -465     35    192       O  
HETATM12861  O   HOH A1144      -8.601  -6.913  49.146  1.00 47.70           O  
ANISOU12861  O   HOH A1144     3739   9449   4933    -60    559  -2726       O  
HETATM12862  O   HOH A1145      -2.897 -11.603  31.741  1.00 29.13           O  
ANISOU12862  O   HOH A1145     5192   3435   2441    612    618     82       O  
HETATM12863  O   HOH A1146      -8.411  19.143  37.647  1.00 19.23           O  
ANISOU12863  O   HOH A1146     2543   2749   2014    -95    700   -243       O  
HETATM12864  O   HOH A1147     -10.440  -3.554   8.429  1.00 42.69           O  
ANISOU12864  O   HOH A1147     7948   3145   5124    947   1012    509       O  
HETATM12865  O   HOH A1148       7.389  -0.094  14.588  1.00 18.06           O  
ANISOU12865  O   HOH A1148     1774   1927   3159    304   -213   -104       O  
HETATM12866  O   HOH A1149      21.528  -0.836  38.174  1.00 43.53           O  
ANISOU12866  O   HOH A1149     4373   5449   6715  -1601   1232  -2091       O  
HETATM12867  O   HOH A1150      -3.309  27.841  27.043  1.00 43.67           O  
ANISOU12867  O   HOH A1150     9932   2859   3800   1586   1977    764       O  
HETATM12868  O   HOH A1151     -11.023  15.017  12.799  1.00 12.82           O  
ANISOU12868  O   HOH A1151     1869   1576   1425   -153   -166   -137       O  
HETATM12869  O   HOH A1152      -7.814  -3.354  44.059  1.00 36.05           O  
ANISOU12869  O   HOH A1152     4416   4981   4299    275   -168   -903       O  
HETATM12870  O   HOH A1153     -47.682 -23.639  11.897  1.00 38.24           O  
ANISOU12870  O   HOH A1153     5009   5277   4243   -452    349   -254       O  
HETATM12871  O   HOH A1154      16.132 -29.242  38.935  1.00 50.36           O  
ANISOU12871  O   HOH A1154     5403   8334   5397    479   2034   2109       O  
HETATM12872  O   HOH A1155     -11.716  11.448  48.526  1.00 33.32           O  
ANISOU12872  O   HOH A1155     6056   3484   3120  -1024   -534     53       O  
HETATM12873  O   HOH A1156     -22.594  16.018  35.136  1.00 37.16           O  
ANISOU12873  O   HOH A1156     3692   4171   6252    142    994   -833       O  
HETATM12874  O   HOH A1157     -18.551  -9.544  32.013  1.00 50.26           O  
ANISOU12874  O   HOH A1157    10454   6158   2482   -367    919  -1484       O  
HETATM12875  O   HOH A1158      31.210  -8.642  27.578  1.00 46.21           O  
ANISOU12875  O   HOH A1158     4103   8356   5098   1576   -897   -352       O  
HETATM12876  O   HOH A1159     -14.037  16.402  45.640  1.00 43.72           O  
ANISOU12876  O   HOH A1159     3667  10411   2531    -43    221   -420       O  
HETATM12877  O   HOH A1160     -23.510 -28.850   7.721  1.00 33.31           O  
ANISOU12877  O   HOH A1160     3634   4081   4939   -303    593    125       O  
HETATM12878  O   HOH A1161     -37.655  -6.593  46.072  1.00 33.99           O  
ANISOU12878  O   HOH A1161     5581   3451   3881   -379    419   -650       O  
HETATM12879  O   HOH A1162     -35.682  -6.593  49.346  1.00 25.27           O  
ANISOU12879  O   HOH A1162     3089   2816   3694    408    -24    -81       O  
HETATM12880  O   HOH A1163       2.351 -14.055  14.477  1.00 29.48           O  
ANISOU12880  O   HOH A1163     2597   5355   3246   -107   -499  -1090       O  
HETATM12881  O   HOH A1164     -13.286 -14.391  48.943  1.00 35.29           O  
ANISOU12881  O   HOH A1164     4708   3514   5182    536    853    380       O  
HETATM12882  O   HOH A1165      17.920 -19.895  30.071  1.00 28.00           O  
ANISOU12882  O   HOH A1165     3417   3621   3600     -5   -538    194       O  
HETATM12883  O   HOH A1166      21.335  -2.052  40.531  1.00 51.46           O  
ANISOU12883  O   HOH A1166     7528   8049   3975  -1406  -1979   1241       O  
HETATM12884  O   HOH A1167      -7.820  -4.452  48.714  1.00 50.51           O  
ANISOU12884  O   HOH A1167     5810   8021   5360    275   1134   1683       O  
HETATM12885  O   HOH A1169       3.029 -18.914  18.938  1.00 34.36           O  
ANISOU12885  O   HOH A1169     4951   4390   3713   1027    467   -962       O  
HETATM12886  O   HOH A1170      16.385  10.806  10.577  1.00 55.01           O  
ANISOU12886  O   HOH A1170     3920   4712  12267   -582    726   1591       O  
HETATM12887  O   HOH A1171     -20.880  20.106  36.085  1.00 44.97           O  
ANISOU12887  O   HOH A1171     6376   3010   7697   1111   2845   -217       O  
HETATM12888  O   HOH A1172       0.570  28.271  22.646  1.00 29.49           O  
ANISOU12888  O   HOH A1172     4533   3061   3609   -658    -32   -905       O  
HETATM12889  O   HOH A1173       0.211  24.744  32.837  1.00 34.73           O  
ANISOU12889  O   HOH A1173     5269   3462   4464   -846  -1201    601       O  
HETATM12890  O   HOH A1174      -6.011  27.747  13.919  1.00 43.17           O  
ANISOU12890  O   HOH A1174     7996   3877   4528   -488   1071  -1139       O  
HETATM12891  O   HOH A1175      -6.896  -5.185  46.283  1.00 37.90           O  
ANISOU12891  O   HOH A1175     5769   4371   4259   -174     30   -246       O  
HETATM12892  O   HOH A1176      27.595 -16.895  16.923  1.00 40.79           O  
ANISOU12892  O   HOH A1176     4148   5549   5799   1824    575   -648       O  
HETATM12893  O   HOH A1177     -10.533   4.146  52.607  1.00 47.07           O  
ANISOU12893  O   HOH A1177     6093   6989   4801   -269   -494   -333       O  
HETATM12894  O   HOH A1178      -6.735  27.599  16.362  1.00 37.61           O  
ANISOU12894  O   HOH A1178     4952   3290   6046  -1040    580     70       O  
HETATM12895  O   HOH A1179     -25.989  14.742  37.586  1.00 55.95           O  
ANISOU12895  O   HOH A1179     3783  13269   4203   1765    117   -254       O  
HETATM12896  O   HOH A1180       1.070  -1.230  45.419  1.00 50.45           O  
ANISOU12896  O   HOH A1180     8214   6398   4555   1679   -739     85       O  
HETATM12897  O   HOH A1181     -19.006   4.275  27.838  1.00 29.47           O  
ANISOU12897  O   HOH A1181     2408   1448   7339   -174   1242   -898       O  
HETATM12898  O   HOH A1182      13.647 -10.341  12.805  1.00 14.58           O  
ANISOU12898  O   HOH A1182     1924   2166   1447    280    -95    171       O  
HETATM12899  O   HOH A1183     -29.877  12.335  34.619  1.00 45.34           O  
ANISOU12899  O   HOH A1183     6593   5494   5140   1826   -965  -1564       O  
HETATM12900  O   HOH A1184     -12.164   4.444  17.006  1.00 31.52           O  
ANISOU12900  O   HOH A1184     4852   4875   2248    194    190   1043       O  
HETATM12901  O   HOH A1185     -12.004   7.966  51.237  1.00 39.55           O  
ANISOU12901  O   HOH A1185     6203   5142   3682   -215  -1048   -698       O  
HETATM12902  O   HOH A1186     -13.650   0.829  53.153  1.00 45.14           O  
ANISOU12902  O   HOH A1186     5663   9108   2378  -1616    316   1173       O  
HETATM12903  O   HOH A1188      27.964  -7.769  30.090  1.00 53.42           O  
ANISOU12903  O   HOH A1188     4974   6835   8485  -1129   -770   2052       O  
HETATM12904  O   HOH A1189     -31.414   2.229  42.896  1.00 21.78           O  
ANISOU12904  O   HOH A1189     2863   2318   3094   -428    947   -602       O  
HETATM12905  O   HOH A1190      17.707  -1.918   1.608  1.00 46.28           O  
ANISOU12905  O   HOH A1190     4605   6844   6133     84   1166    115       O  
HETATM12906  O   HOH A1191     -14.367  16.846  18.562  1.00 28.41           O  
ANISOU12906  O   HOH A1191     2250   4535   4007   -106    251   1219       O  
HETATM12907  O   HOH A1192     -30.145   0.453  41.217  1.00 24.91           O  
ANISOU12907  O   HOH A1192     3548   2758   3155    655   1079    170       O  
HETATM12908  O   HOH A1193       4.557   1.820  33.374  1.00 36.95           O  
ANISOU12908  O   HOH A1193     4403   3776   5860    404   1483    722       O  
HETATM12909  O   HOH A1194      -8.297  26.293  28.036  1.00 35.45           O  
ANISOU12909  O   HOH A1194     3872   4514   5083   -165   -289   -887       O  
HETATM12910  O   HOH A1195     -14.509 -21.313  49.945  1.00 33.33           O  
ANISOU12910  O   HOH A1195     4150   4477   4034    632    238     41       O  
HETATM12911  O   HOH A1196      -2.512  -9.366  46.513  1.00 26.24           O  
ANISOU12911  O   HOH A1196     4725   2943   2302    156   -244     51       O  
HETATM12912  O   HOH A1197     -34.844  -2.172  39.529  1.00 37.43           O  
ANISOU12912  O   HOH A1197     5566   4514   4140   -128   1180    189       O  
HETATM12913  O   HOH A1198      21.364 -18.387  23.124  1.00 47.10           O  
ANISOU12913  O   HOH A1198     4882   3446   9564    509    782    246       O  
HETATM12914  O   HOH A1199      -7.526  13.103  46.629  1.00 40.12           O  
ANISOU12914  O   HOH A1199     4771   5645   4826     46    690  -1513       O  
HETATM12915  O   HOH A1200     -16.456   0.467  52.768  1.00 31.73           O  
ANISOU12915  O   HOH A1200     5435   4002   2615    494   -552     26       O  
HETATM12916  O   HOH A1201      -8.274 -34.920  45.806  1.00 41.90           O  
ANISOU12916  O   HOH A1201     6136   3351   6433    595    361    512       O  
HETATM12917  O   HOH A1202       3.865   3.592  35.477  1.00 27.28           O  
ANISOU12917  O   HOH A1202     2387   4505   3471   -132    -15    462       O  
HETATM12918  O   HOH A1203     -17.384 -10.655  33.842  1.00 39.60           O  
ANISOU12918  O   HOH A1203     6619   3050   5375  -1228    847  -1814       O  
HETATM12919  O   HOH A1204       3.992   6.084  34.485  1.00 29.14           O  
ANISOU12919  O   HOH A1204     3224   3944   3904    735    -98   -948       O  
HETATM12920  O   HOH A1206     -27.770  12.756  37.855  1.00 52.33           O  
ANISOU12920  O   HOH A1206     6850   7824   5206   2081   2320   1381       O  
HETATM12921  O   HOH A1207     -32.162  -2.979  43.731  1.00 25.19           O  
ANISOU12921  O   HOH A1207     3476   2914   3179    475    -56   -874       O  
HETATM12922  O   HOH A1208     -14.048  20.823  27.117  1.00 41.57           O  
ANISOU12922  O   HOH A1208     4998   4349   6445   -103    199    338       O  
HETATM12923  O   HOH A1209       6.555  26.755   1.650  1.00 48.70           O  
ANISOU12923  O   HOH A1209     4834   8291   5378   -548   1766    124       O  
HETATM12924  O   HOH A1210     -44.345 -10.388 -15.252  1.00 35.65           O  
ANISOU12924  O   HOH A1210     4212   4315   5017  -1572   -581   1400       O  
HETATM12925  O   HOH A1211     -11.589  13.478  46.985  1.00 33.14           O  
ANISOU12925  O   HOH A1211     4580   2987   5023   -237    623    452       O  
HETATM12926  O   HOH A1212      -9.212  23.802  20.986  1.00 46.78           O  
ANISOU12926  O   HOH A1212     5489   6101   6182   1684    788   1857       O  
HETATM12927  O   HOH A1213      28.407   1.262  16.471  1.00 30.13           O  
ANISOU12927  O   HOH A1213     3237   4012   4198   -771    314    463       O  
HETATM12928  O   HOH A1214       5.374   7.267  36.568  1.00 41.13           O  
ANISOU12928  O   HOH A1214     3332   6710   5583     60   -399  -1191       O  
HETATM12929  O   HOH A1215     -38.700   2.806  35.897  1.00 49.82           O  
ANISOU12929  O   HOH A1215     5513   5514   7901    810  -1716  -2636       O  
HETATM12930  O   HOH A1216       9.487   4.209  30.011  1.00 41.02           O  
ANISOU12930  O   HOH A1216     4923   5389   5271    189    711    621       O  
HETATM12931  O   HOH A1217       5.371  -0.739  33.774  1.00 25.09           O  
ANISOU12931  O   HOH A1217     3653   3224   2657    -77    149   -235       O  
HETATM12932  O   HOH A1218      -2.639  -5.660  19.078  1.00 26.86           O  
ANISOU12932  O   HOH A1218     3163   3327   3715    -50   1019    508       O  
HETATM12933  O   HOH A1219      25.770 -18.048  15.315  1.00 42.81           O  
ANISOU12933  O   HOH A1219     4018   3791   8454   1350    223  -1278       O  
HETATM12934  O   HOH A1220      -1.244 -17.229  19.060  1.00 27.30           O  
ANISOU12934  O   HOH A1220     4336   3016   3017    102   -555   -454       O  
HETATM12935  O   HOH A1222      16.172  24.891   6.809  1.00 37.40           O  
ANISOU12935  O   HOH A1222     4159   6141   3909  -1556    578    913       O  
HETATM12936  O   HOH A1223      30.430  -2.837  10.365  1.00 48.53           O  
ANISOU12936  O   HOH A1223     4238   6315   7884   -384  -1496    511       O  
HETATM12937  O   HOH A1224     -36.654   0.021  26.579  1.00 52.87           O  
ANISOU12937  O   HOH A1224     7697   8783   3607   1217   4087    121       O  
HETATM12938  O   HOH A1225       5.475  29.739  12.763  1.00 40.48           O  
ANISOU12938  O   HOH A1225     5861   4326   5191  -1809    603   -477       O  
HETATM12939  O   HOH A1226       6.149  30.823  23.296  1.00 44.00           O  
ANISOU12939  O   HOH A1226     8845   4459   3414     -6    284    142       O  
HETATM12940  O   HOH A1228      -5.107 -12.306  20.126  1.00 34.07           O  
ANISOU12940  O   HOH A1228     3703   5442   3799  -1018   -557     26       O  
HETATM12941  O   HOH A1230      25.524   4.976  20.376  1.00 34.72           O  
ANISOU12941  O   HOH A1230     4638   3092   5460   -838    641   -142       O  
HETATM12942  O   HOH A1231       4.850   3.137  31.091  1.00 36.66           O  
ANISOU12942  O   HOH A1231     5584   4880   3464  -1419    833  -1641       O  
HETATM12943  O   HOH A1232      15.100 -17.675  17.031  1.00 24.76           O  
ANISOU12943  O   HOH A1232     3343   3548   2515    350    -40     21       O  
HETATM12944  O   HOH A1233      29.227  -4.988   8.934  1.00 42.23           O  
ANISOU12944  O   HOH A1233     3266   7010   5768  -1623   -179    -21       O  
HETATM12945  O   HOH A1234      -6.503   6.321  49.180  1.00 43.27           O  
ANISOU12945  O   HOH A1234     7957   4854   3627    180    112  -1402       O  
HETATM12946  O   HOH A1236      -4.335 -15.250  20.835  1.00 39.41           O  
ANISOU12946  O   HOH A1236     3259   5189   6525     60  -1060  -1031       O  
HETATM12947  O   HOH A1237      -4.874  -1.487  47.445  1.00 44.71           O  
ANISOU12947  O   HOH A1237     5291   7123   4572   1297    171   2059       O  
HETATM12948  O   HOH A1238      19.561  15.909  13.482  1.00 40.99           O  
ANISOU12948  O   HOH A1238     2745   6973   5853   -106    -93    -99       O  
HETATM12949  O   HOH A1239      26.053   6.133  24.730  1.00 47.16           O  
ANISOU12949  O   HOH A1239     7538   3986   6394   -118    823   -665       O  
HETATM12950  O   HOH A1240      31.811  -5.047  29.190  1.00 48.76           O  
ANISOU12950  O   HOH A1240     4408   9782   4335    467   -683  -1281       O  
HETATM12951  O   HOH A1241      18.172 -21.450  41.334  1.00 41.39           O  
ANISOU12951  O   HOH A1241     6103   5645   3978    968   -458    352       O  
HETATM12952  O   HOH A1242      -8.469  25.612  23.734  1.00 49.02           O  
ANISOU12952  O   HOH A1242    10802   3204   4620    255  -1182    466       O  
HETATM12953  O   HOH A1243      21.750   4.155  22.058  1.00 41.10           O  
ANISOU12953  O   HOH A1243     5185   5720   4711    444   1165    327       O  
HETATM12954  O   HOH A1244      -2.651   6.438  46.079  1.00 34.91           O  
ANISOU12954  O   HOH A1244     5124   5685   2454   -551   -300   -163       O  
HETATM12955  O   HOH A1245      17.819 -14.367  15.837  1.00 21.80           O  
ANISOU12955  O   HOH A1245     2791   2720   2770   -110   -218     97       O  
HETATM12956  O   HOH A1246      18.979 -16.658  14.956  1.00 23.76           O  
ANISOU12956  O   HOH A1246     2746   2921   3361    266    683    440       O  
HETATM12957  O   HOH A1249      14.958  27.321  10.145  1.00 38.32           O  
ANISOU12957  O   HOH A1249     3842   3273   7444  -1568   1335   -370       O  
HETATM12958  O   HOH A1250      24.302 -17.174  29.076  1.00 38.60           O  
ANISOU12958  O   HOH A1250     4513   5081   5072    797    412    780       O  
HETATM12959  O   HOH A1251     -17.102  -3.291  54.816  1.00 36.67           O  
ANISOU12959  O   HOH A1251     4957   6580   2395   -511   -535    499       O  
HETATM12960  O   HOH A1252      -5.510  -9.806  49.984  1.00 34.37           O  
ANISOU12960  O   HOH A1252     3923   6029   3108   -191    127   -679       O  
HETATM12961  O   HOH A1253      -3.719   8.732  44.638  1.00 37.58           O  
ANISOU12961  O   HOH A1253     4304   6629   3342  -2444      8  -1259       O  
HETATM12962  O   HOH A1254      -4.789  -8.417  47.646  1.00 26.65           O  
ANISOU12962  O   HOH A1254     5147   2583   2395   -370    282   -304       O  
ATOM   4103  N   ASN B   2     -21.507  -7.191  56.267  1.00 31.38           N  
ANISOU 4103  N   ASN B   2     5571   3062   3288    865    -83     76       N  
ATOM   4104  CA  ASN B   2     -21.503  -7.929  54.995  1.00 25.72           C  
ANISOU 4104  CA  ASN B   2     4583   2409   2778    728    357    319       C  
ATOM   4105  CB  ASN B   2     -21.610  -6.998  53.792  1.00 22.67           C  
ANISOU 4105  CB  ASN B   2     3887   2724   2003    689    936     12       C  
ATOM   4106  CG  ASN B   2     -22.897  -6.197  53.757  1.00 22.91           C  
ANISOU 4106  CG  ASN B   2     4108   2584   2013    792   1165     77       C  
ATOM   4107  OD1 ASN B   2     -23.962  -6.735  53.477  1.00 28.94           O  
ANISOU 4107  OD1 ASN B   2     4839   3013   3144    464   1068   -434       O  
ATOM   4108  ND2 ASN B   2     -22.801  -4.910  54.006  1.00 24.61           N  
ANISOU 4108  ND2 ASN B   2     4738   2321   2291    943    680    299       N  
ATOM   4109  C   ASN B   2     -20.222  -8.759  54.864  1.00 26.04           C  
ANISOU 4109  C   ASN B   2     4747   2611   2534    749    106    -81       C  
ATOM   4110  O   ASN B   2     -19.134  -8.330  55.234  1.00 25.74           O  
ANISOU 4110  O   ASN B   2     4911   2410   2458    519     79    106       O  
ATOM   4111  N   THR B   3     -20.369  -9.938  54.262  1.00 26.08           N  
ANISOU 4111  N   THR B   3     5091   2624   2191    631    268    -66       N  
ATOM   4112  CA ATHR B   3     -19.250 -10.816  53.981  0.50 26.20           C  
ANISOU 4112  CA ATHR B   3     4995   2845   2113    763    211    -29       C  
ATOM   4113  CA BTHR B   3     -19.251 -10.827  53.982  0.50 25.64           C  
ANISOU 4113  CA BTHR B   3     5148   2687   1907    646    425     23       C  
ATOM   4114  CB ATHR B   3     -19.097 -11.847  55.107  0.50 28.61           C  
ANISOU 4114  CB ATHR B   3     5087   2920   2862   1277    -19    191       C  
ATOM   4115  CB BTHR B   3     -19.116 -11.950  55.021  0.50 26.00           C  
ANISOU 4115  CB BTHR B   3     5818   2690   1371    727    300   -323       C  
ATOM   4116  OG1ATHR B   3     -18.113 -12.814  54.739  0.50 29.48           O  
ANISOU 4116  OG1ATHR B   3     4657   3872   2670   1662   -175    -12       O  
ATOM   4117  OG1BTHR B   3     -20.033 -12.998  54.707  0.50 29.91           O  
ANISOU 4117  OG1BTHR B   3     5895   3450   2017    284    728   -306       O  
ATOM   4118  CG2ATHR B   3     -20.407 -12.515  55.463  0.50 29.35           C  
ANISOU 4118  CG2ATHR B   3     5312   3074   2765   1084     10    285       C  
ATOM   4119  CG2BTHR B   3     -19.354 -11.483  56.435  0.50 23.99           C  
ANISOU 4119  CG2BTHR B   3     5706   2210   1198    660    305   -109       C  
ATOM   4120  C   THR B   3     -19.439 -11.392  52.579  1.00 24.88           C  
ANISOU 4120  C   THR B   3     4784   2558   2108    638    128     45       C  
ATOM   4121  O   THR B   3     -20.557 -11.716  52.174  1.00 24.19           O  
ANISOU 4121  O   THR B   3     4458   2683   2050    511    468    137       O  
ATOM   4122  N   PRO B   4     -18.365 -11.515  51.775  1.00 22.24           N  
ANISOU 4122  N   PRO B   4     4687   1933   1828    434    283    274       N  
ATOM   4123  CA  PRO B   4     -18.505 -12.093  50.444  1.00 21.72           C  
ANISOU 4123  CA  PRO B   4     4427   1936   1888    119    105    274       C  
ATOM   4124  CB  PRO B   4     -17.071 -12.134  49.906  1.00 23.25           C  
ANISOU 4124  CB  PRO B   4     4306   2100   2424    401     95     53       C  
ATOM   4125  CG  PRO B   4     -16.412 -10.985  50.647  1.00 26.42           C  
ANISOU 4125  CG  PRO B   4     4863   2617   2558    168    -12     -6       C  
ATOM   4126  CD  PRO B   4     -16.990 -11.075  52.042  1.00 25.55           C  
ANISOU 4126  CD  PRO B   4     4742   2529   2435    230     30    -30       C  
ATOM   4127  C   PRO B   4     -19.098 -13.491  50.533  1.00 21.21           C  
ANISOU 4127  C   PRO B   4     4223   1885   1949    205    335    249       C  
ATOM   4128  O   PRO B   4     -18.745 -14.279  51.418  1.00 23.08           O  
ANISOU 4128  O   PRO B   4     4809   1931   2028    538    363    292       O  
ATOM   4129  N   PRO B   5     -20.013 -13.837  49.609  1.00 19.44           N  
ANISOU 4129  N   PRO B   5     3803   1803   1779    326    411    156       N  
ATOM   4130  CA  PRO B   5     -20.607 -15.170  49.604  1.00 20.22           C  
ANISOU 4130  CA  PRO B   5     3483   2058   2142    151    403     91       C  
ATOM   4131  CB  PRO B   5     -21.718 -15.038  48.558  1.00 21.93           C  
ANISOU 4131  CB  PRO B   5     3648   2313   2368    167    232    215       C  
ATOM   4132  CG  PRO B   5     -21.166 -14.007  47.596  1.00 21.08           C  
ANISOU 4132  CG  PRO B   5     3439   2144   2425     77     47    311       C  
ATOM   4133  CD  PRO B   5     -20.496 -12.995  48.501  1.00 19.60           C  
ANISOU 4133  CD  PRO B   5     3477   1824   2144    169    316    296       C  
ATOM   4134  C   PRO B   5     -19.606 -16.252  49.176  1.00 19.98           C  
ANISOU 4134  C   PRO B   5     3416   2073   2101    116    648     33       C  
ATOM   4135  O   PRO B   5     -18.700 -15.986  48.399  1.00 20.85           O  
ANISOU 4135  O   PRO B   5     3303   2251   2365    432    767    135       O  
ATOM   4136  N   GLU B   6     -19.814 -17.462  49.681  1.00 19.87           N  
ANISOU 4136  N   GLU B   6     3481   2163   1905    403    653    224       N  
ATOM   4137  CA  GLU B   6     -19.095 -18.641  49.244  1.00 21.24           C  
ANISOU 4137  CA  GLU B   6     3787   2100   2182    444    851    194       C  
ATOM   4138  CB  GLU B   6     -19.519 -19.866  50.069  1.00 24.23           C  
ANISOU 4138  CB  GLU B   6     4397   2440   2369    497   1221    452       C  
ATOM   4139  CG  GLU B   6     -18.889 -21.189  49.620  1.00 26.41           C  
ANISOU 4139  CG  GLU B   6     4781   2752   2499    764   1334    565       C  
ATOM   4140  CD  GLU B   6     -19.519 -21.932  48.434  1.00 29.33           C  
ANISOU 4140  CD  GLU B   6     4858   3188   3095    497   1044    518       C  
ATOM   4141  OE1 GLU B   6     -20.681 -21.659  48.077  1.00 32.87           O  
ANISOU 4141  OE1 GLU B   6     4915   3830   3743   1053    691    375       O  
ATOM   4142  OE2 GLU B   6     -18.831 -22.797  47.858  1.00 33.31           O  
ANISOU 4142  OE2 GLU B   6     5397   3689   3571    874   1406    637       O  
ATOM   4143  C   GLU B   6     -19.388 -18.881  47.766  1.00 21.15           C  
ANISOU 4143  C   GLU B   6     3333   2423   2279    444    841     74       C  
ATOM   4144  O   GLU B   6     -20.553 -18.773  47.311  1.00 21.22           O  
ANISOU 4144  O   GLU B   6     3204   2235   2622    457    894    144       O  
ATOM   4145  N   LEU B   7     -18.321 -19.186  47.024  1.00 17.79           N  
ANISOU 4145  N   LEU B   7     2855   1630   2272    462    587    238       N  
ATOM   4146  CA  LEU B   7     -18.407 -19.582  45.616  1.00 16.84           C  
ANISOU 4146  CA  LEU B   7     2733   1541   2120    263    610    180       C  
ATOM   4147  CB  LEU B   7     -17.662 -18.558  44.751  1.00 15.83           C  
ANISOU 4147  CB  LEU B   7     2656   1465   1894    327    480    192       C  
ATOM   4148  CG  LEU B   7     -18.191 -17.124  44.859  1.00 16.47           C  
ANISOU 4148  CG  LEU B   7     2596   1539   2122    443    538    286       C  
ATOM   4149  CD1 LEU B   7     -17.333 -16.152  44.069  1.00 16.99           C  
ANISOU 4149  CD1 LEU B   7     2508   1692   2256    386    696    164       C  
ATOM   4150  CD2 LEU B   7     -19.636 -17.040  44.391  1.00 17.52           C  
ANISOU 4150  CD2 LEU B   7     2557   1812   2286    228    555    461       C  
ATOM   4151  C   LEU B   7     -17.777 -20.964  45.442  1.00 17.37           C  
ANISOU 4151  C   LEU B   7     2752   1509   2336    182    632    179       C  
ATOM   4152  O   LEU B   7     -16.706 -21.252  45.986  1.00 19.40           O  
ANISOU 4152  O   LEU B   7     2717   1984   2668    455    723    169       O  
ATOM   4153  N   ASP B   8     -18.444 -21.795  44.639  1.00 18.06           N  
ANISOU 4153  N   ASP B   8     2802   1671   2387    176    753    -89       N  
ATOM   4154  CA  ASP B   8     -17.922 -23.116  44.313  1.00 18.05           C  
ANISOU 4154  CA  ASP B   8     2579   1851   2428    289    658   -266       C  
ATOM   4155  CB  ASP B   8     -18.999 -24.002  43.710  1.00 21.94           C  
ANISOU 4155  CB  ASP B   8     2968   2313   3054    -55    537   -457       C  
ATOM   4156  CG  ASP B   8     -20.128 -24.392  44.647  1.00 25.62           C  
ANISOU 4156  CG  ASP B   8     3404   2816   3513   -570    740   -388       C  
ATOM   4157  OD1 ASP B   8     -20.015 -24.218  45.870  1.00 27.80           O  
ANISOU 4157  OD1 ASP B   8     4283   2800   3477   -691   1307   -291       O  
ATOM   4158  OD2 ASP B   8     -21.118 -24.900  44.117  1.00 33.93           O  
ANISOU 4158  OD2 ASP B   8     2924   4691   5276   -630    519   -192       O  
ATOM   4159  C   ASP B   8     -16.767 -22.977  43.324  1.00 17.13           C  
ANISOU 4159  C   ASP B   8     2456   1791   2259    125    451   -116       C  
ATOM   4160  O   ASP B   8     -16.672 -21.991  42.594  1.00 17.51           O  
ANISOU 4160  O   ASP B   8     2556   1823   2272    232    726    -79       O  
ATOM   4161  N   THR B   9     -15.900 -23.988  43.305  1.00 17.29           N  
ANISOU 4161  N   THR B   9     2648   1791   2128    222    390   -179       N  
ATOM   4162  CA  THR B   9     -14.710 -23.985  42.450  1.00 17.08           C  
ANISOU 4162  CA  THR B   9     2718   1853   1917    239    402   -270       C  
ATOM   4163  CB  THR B   9     -13.429 -24.071  43.283  1.00 17.52           C  
ANISOU 4163  CB  THR B   9     2532   1982   2141    440    402    -48       C  
ATOM   4164  OG1 THR B   9     -13.517 -25.166  44.203  1.00 18.66           O  
ANISOU 4164  OG1 THR B   9     2983   2041   2065    378    232    -41       O  
ATOM   4165  CG2 THR B   9     -13.188 -22.799  44.064  1.00 17.74           C  
ANISOU 4165  CG2 THR B   9     2681   2122   1935    348    119     81       C  
ATOM   4166  C   THR B   9     -14.760 -25.126  41.428  1.00 17.39           C  
ANISOU 4166  C   THR B   9     2792   1816   1997    247    378   -277       C  
ATOM   4167  O   THR B   9     -15.355 -26.194  41.655  1.00 18.52           O  
ANISOU 4167  O   THR B   9     2923   2013   2100    249    284    -93       O  
ATOM   4168  N   VAL B  10     -14.120 -24.859  40.288  1.00 15.87           N  
ANISOU 4168  N   VAL B  10     2460   1518   2049    479    356   -191       N  
ATOM   4169  CA  VAL B  10     -13.866 -25.826  39.229  1.00 15.73           C  
ANISOU 4169  CA  VAL B  10     2240   1646   2087    241    165   -396       C  
ATOM   4170  CB  VAL B  10     -14.767 -25.574  38.018  1.00 16.24           C  
ANISOU 4170  CB  VAL B  10     2369   1711   2088    365    196   -280       C  
ATOM   4171  CG1 VAL B  10     -16.240 -25.647  38.408  1.00 18.69           C  
ANISOU 4171  CG1 VAL B  10     2447   2300   2353    100    188   -140       C  
ATOM   4172  CG2 VAL B  10     -14.449 -24.255  37.329  1.00 17.05           C  
ANISOU 4172  CG2 VAL B  10     2572   1944   1961    299    438   -161       C  
ATOM   4173  C   VAL B  10     -12.391 -25.746  38.826  1.00 15.79           C  
ANISOU 4173  C   VAL B  10     2076   1790   2132    343     46   -376       C  
ATOM   4174  O   VAL B  10     -11.706 -24.796  39.183  1.00 16.64           O  
ANISOU 4174  O   VAL B  10     2271   1687   2363    272    396   -441       O  
ATOM   4175  N   LEU B  11     -11.914 -26.762  38.103  1.00 17.13           N  
ANISOU 4175  N   LEU B  11     2461   1869   2177    138    -26   -626       N  
ATOM   4176  CA  LEU B  11     -10.572 -26.750  37.517  1.00 19.09           C  
ANISOU 4176  CA  LEU B  11     2404   2404   2444    309   -170   -538       C  
ATOM   4177  CB  LEU B  11      -9.841 -28.052  37.842  1.00 23.34           C  
ANISOU 4177  CB  LEU B  11     3224   2444   3199    535   -202   -670       C  
ATOM   4178  CG  LEU B  11      -9.512 -28.298  39.297  1.00 24.09           C  
ANISOU 4178  CG  LEU B  11     3431   2360   3359    481    -73    -26       C  
ATOM   4179  CD1 LEU B  11      -8.556 -29.471  39.393  1.00 25.60           C  
ANISOU 4179  CD1 LEU B  11     3227   2682   3817    479   -679    504       C  
ATOM   4180  CD2 LEU B  11      -8.918 -27.059  39.941  1.00 24.07           C  
ANISOU 4180  CD2 LEU B  11     3421   2499   3225     73   -444    373       C  
ATOM   4181  C   LEU B  11     -10.685 -26.611  36.002  1.00 18.62           C  
ANISOU 4181  C   LEU B  11     1988   2797   2288    440   -182   -904       C  
ATOM   4182  O   LEU B  11     -11.072 -27.560  35.333  1.00 22.72           O  
ANISOU 4182  O   LEU B  11     2639   2990   3003    324   -302  -1245       O  
ATOM   4183  N   GLN B  12     -10.341 -25.437  35.490  1.00 18.84           N  
ANISOU 4183  N   GLN B  12     2216   2868   2072    437     27  -1039       N  
ATOM   4184  CA  GLN B  12     -10.322 -25.218  34.045  1.00 18.73           C  
ANISOU 4184  CA  GLN B  12     2087   3009   2017    611     -2  -1101       C  
ATOM   4185  CB  GLN B  12     -10.100 -23.744  33.724  1.00 21.65           C  
ANISOU 4185  CB  GLN B  12     2771   3083   2372    756     10   -859       C  
ATOM   4186  CG  GLN B  12     -10.059 -23.418  32.243  1.00 24.62           C  
ANISOU 4186  CG  GLN B  12     3383   3540   2432    688     15  -1050       C  
ATOM   4187  CD  GLN B  12     -11.412 -23.585  31.596  1.00 28.49           C  
ANISOU 4187  CD  GLN B  12     3894   4185   2747    484   -407   -624       C  
ATOM   4188  OE1 GLN B  12     -12.414 -23.059  32.074  1.00 33.95           O  
ANISOU 4188  OE1 GLN B  12     4178   4844   3876   1119   -156     18       O  
ATOM   4189  NE2 GLN B  12     -11.446 -24.330  30.496  1.00 36.19           N  
ANISOU 4189  NE2 GLN B  12     5559   5135   3054    569   -813  -1040       N  
ATOM   4190  C   GLN B  12      -9.192 -26.090  33.481  1.00 18.23           C  
ANISOU 4190  C   GLN B  12     2136   2639   2152    434    286   -929       C  
ATOM   4191  O   GLN B  12      -8.088 -26.074  34.003  1.00 19.29           O  
ANISOU 4191  O   GLN B  12     2062   2606   2660    562    191   -837       O  
ATOM   4192  N   ALA B  13      -9.497 -26.856  32.433  1.00 18.28           N  
ANISOU 4192  N   ALA B  13     2026   2621   2297    156    399   -955       N  
ATOM   4193  CA  ALA B  13      -8.548 -27.771  31.844  1.00 17.87           C  
ANISOU 4193  CA  ALA B  13     2225   2455   2107    178    491   -769       C  
ATOM   4194  CB  ALA B  13      -8.814 -29.179  32.331  1.00 20.41           C  
ANISOU 4194  CB  ALA B  13     2871   2649   2233    112    313   -539       C  
ATOM   4195  C   ALA B  13      -8.694 -27.695  30.330  1.00 17.16           C  
ANISOU 4195  C   ALA B  13     2222   2229   2069    188    310   -797       C  
ATOM   4196  O   ALA B  13      -9.786 -27.423  29.823  1.00 19.44           O  
ANISOU 4196  O   ALA B  13     2254   2612   2517    400    356   -508       O  
ATOM   4197  N   PRO B  14      -7.618 -27.942  29.564  1.00 17.63           N  
ANISOU 4197  N   PRO B  14     2387   2253   2059    285    377   -730       N  
ATOM   4198  CA  PRO B  14      -7.733 -27.888  28.114  1.00 18.49           C  
ANISOU 4198  CA  PRO B  14     2621   2292   2109    276    403   -581       C  
ATOM   4199  CB  PRO B  14      -6.305 -28.127  27.609  1.00 21.77           C  
ANISOU 4199  CB  PRO B  14     2521   2920   2831     48    430   -475       C  
ATOM   4200  CG  PRO B  14      -5.556 -28.743  28.778  1.00 21.60           C  
ANISOU 4200  CG  PRO B  14     2574   2946   2685    421    852   -200       C  
ATOM   4201  CD  PRO B  14      -6.291 -28.342  30.041  1.00 19.35           C  
ANISOU 4201  CD  PRO B  14     2410   2544   2395    210    494   -473       C  
ATOM   4202  C   PRO B  14      -8.674 -28.977  27.586  1.00 16.89           C  
ANISOU 4202  C   PRO B  14     2209   2277   1929    347    267   -382       C  
ATOM   4203  O   PRO B  14      -8.743 -30.084  28.144  1.00 16.67           O  
ANISOU 4203  O   PRO B  14     2293   2142   1898    312    124   -465       O  
ATOM   4204  N   TYR B  15      -9.376 -28.661  26.503  1.00 16.90           N  
ANISOU 4204  N   TYR B  15     2443   2049   1926    293    224   -383       N  
ATOM   4205  CA  TYR B  15     -10.284 -29.603  25.862  1.00 16.51           C  
ANISOU 4205  CA  TYR B  15     2539   1896   1837    188     69   -153       C  
ATOM   4206  CB  TYR B  15     -11.024 -28.886  24.737  1.00 16.95           C  
ANISOU 4206  CB  TYR B  15     2527   1668   2245    237    135    163       C  
ATOM   4207  CG  TYR B  15     -12.198 -29.614  24.139  1.00 17.85           C  
ANISOU 4207  CG  TYR B  15     2730   1655   2397    442   -170    -87       C  
ATOM   4208  CD1 TYR B  15     -13.375 -29.752  24.853  1.00 20.72           C  
ANISOU 4208  CD1 TYR B  15     2913   2138   2819    301     53      0       C  
ATOM   4209  CE1 TYR B  15     -14.482 -30.385  24.313  1.00 22.14           C  
ANISOU 4209  CE1 TYR B  15     2686   2416   3308    411     58   -324       C  
ATOM   4210  CZ  TYR B  15     -14.435 -30.866  23.021  1.00 22.49           C  
ANISOU 4210  CZ  TYR B  15     3112   2099   3333    309   -410   -415       C  
ATOM   4211  OH  TYR B  15     -15.532 -31.475  22.472  1.00 26.35           O  
ANISOU 4211  OH  TYR B  15     3146   2356   4508    209   -550   -618       O  
ATOM   4212  CE2 TYR B  15     -13.286 -30.685  22.273  1.00 22.22           C  
ANISOU 4212  CE2 TYR B  15     3172   2159   3110    453   -349   -469       C  
ATOM   4213  CD2 TYR B  15     -12.172 -30.085  22.840  1.00 20.96           C  
ANISOU 4213  CD2 TYR B  15     3319   2060   2586    323   -132   -304       C  
ATOM   4214  C   TYR B  15      -9.526 -30.829  25.337  1.00 17.53           C  
ANISOU 4214  C   TYR B  15     2841   2011   1808    331   -168   -269       C  
ATOM   4215  O   TYR B  15     -10.143 -31.883  25.172  1.00 18.89           O  
ANISOU 4215  O   TYR B  15     3017   1970   2190    269   -487   -258       O  
ATOM   4216  N   ALA B  16      -8.202 -30.715  25.160  1.00 18.25           N  
ANISOU 4216  N   ALA B  16     3046   1943   1943    373     58   -327       N  
ATOM   4217  CA  ALA B  16      -7.350 -31.854  24.818  1.00 20.26           C  
ANISOU 4217  CA  ALA B  16     3195   2382   2118    757      6   -163       C  
ATOM   4218  CB  ALA B  16      -5.903 -31.409  24.786  1.00 20.34           C  
ANISOU 4218  CB  ALA B  16     3323   2055   2348    748    378    -92       C  
ATOM   4219  C   ALA B  16      -7.525 -33.004  25.825  1.00 19.82           C  
ANISOU 4219  C   ALA B  16     3313   1969   2246    294    289   -354       C  
ATOM   4220  O   ALA B  16      -7.345 -34.157  25.463  1.00 22.57           O  
ANISOU 4220  O   ALA B  16     4314   2129   2130    988    -12   -180       O  
ATOM   4221  N   TYR B  17      -7.842 -32.691  27.094  1.00 17.01           N  
ANISOU 4221  N   TYR B  17     2714   1720   2029    487     -3   -162       N  
ATOM   4222  CA  TYR B  17      -8.001 -33.709  28.117  1.00 16.86           C  
ANISOU 4222  CA  TYR B  17     2525   2060   1818    414    -51   -140       C  
ATOM   4223  CB  TYR B  17      -7.644 -33.144  29.493  1.00 17.39           C  
ANISOU 4223  CB  TYR B  17     2365   2493   1747    474   -116     44       C  
ATOM   4224  CG  TYR B  17      -6.177 -32.957  29.777  1.00 16.43           C  
ANISOU 4224  CG  TYR B  17     2156   2213   1871    493    195    -52       C  
ATOM   4225  CD1 TYR B  17      -5.212 -33.788  29.254  1.00 18.05           C  
ANISOU 4225  CD1 TYR B  17     2331   2615   1911    483    344   -294       C  
ATOM   4226  CE1 TYR B  17      -3.871 -33.623  29.558  1.00 17.72           C  
ANISOU 4226  CE1 TYR B  17     2029   2589   2113    833    611   -318       C  
ATOM   4227  CZ  TYR B  17      -3.463 -32.632  30.429  1.00 17.52           C  
ANISOU 4227  CZ  TYR B  17     2000   2819   1838    758    432   -232       C  
ATOM   4228  OH  TYR B  17      -2.136 -32.484  30.770  1.00 19.61           O  
ANISOU 4228  OH  TYR B  17     1971   3232   2247    852    388    -23       O  
ATOM   4229  CE2 TYR B  17      -4.424 -31.805  30.980  1.00 16.89           C  
ANISOU 4229  CE2 TYR B  17     1928   2195   2295    604    187   -423       C  
ATOM   4230  CD2 TYR B  17      -5.759 -31.982  30.661  1.00 17.72           C  
ANISOU 4230  CD2 TYR B  17     1946   2383   2403    481    195   -371       C  
ATOM   4231  C   TYR B  17      -9.429 -34.268  28.135  1.00 16.95           C  
ANISOU 4231  C   TYR B  17     2741   1891   1808    279   -313    -42       C  
ATOM   4232  O   TYR B  17      -9.720 -35.181  28.924  1.00 18.37           O  
ANISOU 4232  O   TYR B  17     2964   1958   2056    117   -209     95       O  
ATOM   4233  N   ASN B  18     -10.317 -33.748  27.273  1.00 17.82           N  
ANISOU 4233  N   ASN B  18     2764   1688   2319    350   -549   -232       N  
ATOM   4234  CA  ASN B  18     -11.597 -34.423  26.989  1.00 17.82           C  
ANISOU 4234  CA  ASN B  18     2827   1762   2181    301   -399   -122       C  
ATOM   4235  CB  ASN B  18     -12.674 -33.458  26.477  1.00 18.55           C  
ANISOU 4235  CB  ASN B  18     2886   1785   2375    357   -494    -76       C  
ATOM   4236  CG  ASN B  18     -13.973 -34.160  26.120  1.00 20.18           C  
ANISOU 4236  CG  ASN B  18     2994   2157   2517    296   -475   -200       C  
ATOM   4237  OD1 ASN B  18     -14.381 -35.110  26.804  1.00 21.62           O  
ANISOU 4237  OD1 ASN B  18     2938   2070   3204    503    -58   -115       O  
ATOM   4238  ND2 ASN B  18     -14.618 -33.706  25.057  1.00 18.47           N  
ANISOU 4238  ND2 ASN B  18     2578   2105   2333    562   -176   -263       N  
ATOM   4239  C   ASN B  18     -11.282 -35.521  25.973  1.00 16.13           C  
ANISOU 4239  C   ASN B  18     2681   1475   1973    271   -278    107       C  
ATOM   4240  O   ASN B  18     -11.576 -35.402  24.794  1.00 18.11           O  
ANISOU 4240  O   ASN B  18     2920   2000   1960    295   -362    116       O  
ATOM   4241  N   TRP B  19     -10.661 -36.589  26.462  1.00 15.45           N  
ANISOU 4241  N   TRP B  19     2454   1475   1939    218   -291     72       N  
ATOM   4242  CA  TRP B  19     -10.109 -37.606  25.585  1.00 15.02           C  
ANISOU 4242  CA  TRP B  19     2150   1771   1785     64   -180     22       C  
ATOM   4243  CB  TRP B  19      -9.551 -38.776  26.390  1.00 15.55           C  
ANISOU 4243  CB  TRP B  19     2068   1826   2011    131    -39    138       C  
ATOM   4244  CG  TRP B  19      -8.507 -38.416  27.393  1.00 15.88           C  
ANISOU 4244  CG  TRP B  19     2135   2004   1892    153   -103    183       C  
ATOM   4245  CD1 TRP B  19      -8.684 -38.275  28.739  1.00 16.71           C  
ANISOU 4245  CD1 TRP B  19     2257   2146   1947    -72    251    117       C  
ATOM   4246  NE1 TRP B  19      -7.494 -37.975  29.347  1.00 17.61           N  
ANISOU 4246  NE1 TRP B  19     2343   2560   1787     81    148    159       N  
ATOM   4247  CE2 TRP B  19      -6.514 -37.883  28.388  1.00 15.63           C  
ANISOU 4247  CE2 TRP B  19     2070   2107   1761    108     97     85       C  
ATOM   4248  CD2 TRP B  19      -7.121 -38.131  27.139  1.00 14.55           C  
ANISOU 4248  CD2 TRP B  19     2118   1658   1751    193      3    209       C  
ATOM   4249  CE3 TRP B  19      -6.325 -38.154  25.998  1.00 15.10           C  
ANISOU 4249  CE3 TRP B  19     2168   1934   1635    102   -130    188       C  
ATOM   4250  CZ3 TRP B  19      -4.991 -37.853  26.096  1.00 15.16           C  
ANISOU 4250  CZ3 TRP B  19     2056   1973   1732    169     59    120       C  
ATOM   4251  CH2 TRP B  19      -4.416 -37.607  27.337  1.00 16.32           C  
ANISOU 4251  CH2 TRP B  19     1925   2358   1915    138   -219    267       C  
ATOM   4252  CZ2 TRP B  19      -5.160 -37.590  28.496  1.00 16.59           C  
ANISOU 4252  CZ2 TRP B  19     2228   2480   1594     78   -293    203       C  
ATOM   4253  C   TRP B  19     -11.202 -38.128  24.668  1.00 14.11           C  
ANISOU 4253  C   TRP B  19     1884   1700   1778    187   -203    264       C  
ATOM   4254  O   TRP B  19     -12.269 -38.516  25.141  1.00 14.87           O  
ANISOU 4254  O   TRP B  19     1997   1769   1883   -117     39     64       O  
ATOM   4255  N   PRO B  20     -10.976 -38.192  23.345  1.00 14.47           N  
ANISOU 4255  N   PRO B  20     1889   1745   1863     36     78    278       N  
ATOM   4256  CA  PRO B  20     -11.957 -38.818  22.466  1.00 14.85           C  
ANISOU 4256  CA  PRO B  20     2021   1750   1869     13    -13    256       C  
ATOM   4257  CB  PRO B  20     -11.490 -38.430  21.056  1.00 15.18           C  
ANISOU 4257  CB  PRO B  20     2214   1751   1803     77      3    159       C  
ATOM   4258  CG  PRO B  20     -10.505 -37.318  21.271  1.00 15.26           C  
ANISOU 4258  CG  PRO B  20     2072   1674   2051    190    -76    256       C  
ATOM   4259  CD  PRO B  20      -9.839 -37.634  22.591  1.00 14.37           C  
ANISOU 4259  CD  PRO B  20     1916   1610   1931    108     88    368       C  
ATOM   4260  C   PRO B  20     -11.950 -40.335  22.662  1.00 15.05           C  
ANISOU 4260  C   PRO B  20     2077   1787   1852    207    115    416       C  
ATOM   4261  O   PRO B  20     -10.890 -40.960  22.596  1.00 14.53           O  
ANISOU 4261  O   PRO B  20     2117   1592   1810    244     61    271       O  
ATOM   4262  N   THR B  21     -13.131 -40.882  22.955  1.00 14.67           N  
ANISOU 4262  N   THR B  21     2084   1582   1908    153      2    319       N  
ATOM   4263  CA  THR B  21     -13.338 -42.311  23.185  1.00 15.43           C  
ANISOU 4263  CA  THR B  21     2218   1676   1968     49     71    369       C  
ATOM   4264  CB  THR B  21     -13.416 -42.639  24.678  1.00 17.58           C  
ANISOU 4264  CB  THR B  21     2668   2034   1977     37     41    365       C  
ATOM   4265  OG1 THR B  21     -14.676 -42.190  25.194  1.00 19.32           O  
ANISOU 4265  OG1 THR B  21     2817   2359   2163    -94    394    266       O  
ATOM   4266  CG2 THR B  21     -12.269 -42.060  25.481  1.00 18.00           C  
ANISOU 4266  CG2 THR B  21     2678   2190   1971    160    -71    304       C  
ATOM   4267  C   THR B  21     -14.658 -42.747  22.550  1.00 15.54           C  
ANISOU 4267  C   THR B  21     2379   1696   1827    -19     17    336       C  
ATOM   4268  O   THR B  21     -15.414 -41.951  22.054  1.00 15.31           O  
ANISOU 4268  O   THR B  21     2019   1829   1967    -67   -134    350       O  
ATOM   4269  N   SER B  22     -14.942 -44.047  22.659  1.00 17.39           N  
ANISOU 4269  N   SER B  22     2530   1642   2432   -101    -86    454       N  
ATOM   4270  CA  SER B  22     -16.190 -44.579  22.164  1.00 19.77           C  
ANISOU 4270  CA  SER B  22     2637   2166   2708   -219     -2    383       C  
ATOM   4271  CB  SER B  22     -16.177 -46.075  22.176  1.00 23.41           C  
ANISOU 4271  CB  SER B  22     3139   2158   3594   -183     14    177       C  
ATOM   4272  OG  SER B  22     -16.159 -46.568  23.499  1.00 25.68           O  
ANISOU 4272  OG  SER B  22     3601   1975   4180   -446   -328    833       O  
ATOM   4273  C   SER B  22     -17.385 -44.024  22.943  1.00 20.48           C  
ANISOU 4273  C   SER B  22     2540   2440   2798   -217    -50    356       C  
ATOM   4274  O   SER B  22     -18.509 -44.171  22.477  1.00 22.07           O  
ANISOU 4274  O   SER B  22     2803   2749   2832   -208   -415    290       O  
ATOM   4275  N   LYS B  23     -17.150 -43.415  24.110  1.00 18.97           N  
ANISOU 4275  N   LYS B  23     2574   2104   2530   -257     -1    639       N  
ATOM   4276  CA  LYS B  23     -18.244 -42.874  24.926  1.00 21.59           C  
ANISOU 4276  CA  LYS B  23     2836   2621   2745     47    181    603       C  
ATOM   4277  CB  LYS B  23     -17.844 -42.815  26.403  1.00 24.67           C  
ANISOU 4277  CB  LYS B  23     3477   3178   2718    344    411    680       C  
ATOM   4278  CG  LYS B  23     -17.678 -44.163  27.074  1.00 29.75           C  
ANISOU 4278  CG  LYS B  23     4126   3695   3483    427    315   1283       C  
ATOM   4279  CD  LYS B  23     -17.180 -44.040  28.486  1.00 36.58           C  
ANISOU 4279  CD  LYS B  23     5185   4993   3720    570      8   1221       C  
ATOM   4280  CE  LYS B  23     -17.120 -45.383  29.184  1.00 44.15           C  
ANISOU 4280  CE  LYS B  23     6362   5571   4839    504   -265   1879       C  
ATOM   4281  NZ  LYS B  23     -16.751 -45.240  30.613  1.00 51.00           N  
ANISOU 4281  NZ  LYS B  23     6858   7209   5308    513   -729   1358       N  
ATOM   4282  C   LYS B  23     -18.661 -41.474  24.461  1.00 19.37           C  
ANISOU 4282  C   LYS B  23     1994   2769   2594    -23    132    631       C  
ATOM   4283  O   LYS B  23     -19.786 -41.061  24.757  1.00 25.08           O  
ANISOU 4283  O   LYS B  23     2391   3300   3838    248    502    550       O  
ATOM   4284  N   ASN B  24     -17.775 -40.745  23.772  1.00 17.82           N  
ANISOU 4284  N   ASN B  24     2091   2255   2421    -37    112    447       N  
ATOM   4285  CA  ASN B  24     -18.058 -39.353  23.447  1.00 16.30           C  
ANISOU 4285  CA  ASN B  24     1760   2281   2152    187     -9    193       C  
ATOM   4286  CB  ASN B  24     -17.316 -38.380  24.372  1.00 16.24           C  
ANISOU 4286  CB  ASN B  24     1931   2510   1727     42    141    103       C  
ATOM   4287  CG  ASN B  24     -15.807 -38.413  24.219  1.00 16.56           C  
ANISOU 4287  CG  ASN B  24     1858   2653   1779    198   -141    -17       C  
ATOM   4288  OD1 ASN B  24     -15.292 -39.129  23.389  1.00 18.30           O  
ANISOU 4288  OD1 ASN B  24     1825   2636   2491     66     45   -297       O  
ATOM   4289  ND2 ASN B  24     -15.092 -37.605  24.985  1.00 20.85           N  
ANISOU 4289  ND2 ASN B  24     2360   3298   2264     74   -107   -540       N  
ATOM   4290  C   ASN B  24     -17.769 -39.002  21.981  1.00 17.77           C  
ANISOU 4290  C   ASN B  24     2625   2161   1962    160   -173    -32       C  
ATOM   4291  O   ASN B  24     -17.770 -37.841  21.667  1.00 22.98           O  
ANISOU 4291  O   ASN B  24     3733   2486   2511    454    240    506       O  
ATOM   4292  N   VAL B  25     -17.514 -39.982  21.105  1.00 16.46           N  
ANISOU 4292  N   VAL B  25     2505   1989   1758     79   -277    141       N  
ATOM   4293  CA  VAL B  25     -17.295 -39.733  19.693  1.00 16.80           C  
ANISOU 4293  CA  VAL B  25     2594   1985   1805    -24   -376    278       C  
ATOM   4294  CB  VAL B  25     -15.942 -40.278  19.217  1.00 16.69           C  
ANISOU 4294  CB  VAL B  25     2570   1921   1850    -15   -294    254       C  
ATOM   4295  CG1 VAL B  25     -15.820 -40.214  17.694  1.00 18.26           C  
ANISOU 4295  CG1 VAL B  25     2982   2006   1950     28   -238    382       C  
ATOM   4296  CG2 VAL B  25     -14.790 -39.538  19.873  1.00 17.63           C  
ANISOU 4296  CG2 VAL B  25     2587   2147   1963   -236   -300    262       C  
ATOM   4297  C   VAL B  25     -18.414 -40.394  18.891  1.00 16.94           C  
ANISOU 4297  C   VAL B  25     2564   2069   1802   -170   -297    235       C  
ATOM   4298  O   VAL B  25     -18.726 -41.557  19.104  1.00 19.35           O  
ANISOU 4298  O   VAL B  25     2794   2347   2211   -358    -21    592       O  
ATOM   4299  N   LYS B  26     -18.987 -39.626  17.960  1.00 16.27           N  
ANISOU 4299  N   LYS B  26     2315   2057   1808     47   -215    132       N  
ATOM   4300  CA  LYS B  26     -19.820 -40.150  16.884  1.00 16.31           C  
ANISOU 4300  CA  LYS B  26     2061   2317   1818   -205   -163    201       C  
ATOM   4301  CB  LYS B  26     -21.258 -39.622  16.993  1.00 20.27           C  
ANISOU 4301  CB  LYS B  26     2312   3183   2206     53   -187     61       C  
ATOM   4302  CG  LYS B  26     -21.975 -40.039  18.269  1.00 22.53           C  
ANISOU 4302  CG  LYS B  26     2433   3875   2251    -46    -56    180       C  
ATOM   4303  CD  LYS B  26     -23.424 -39.633  18.379  1.00 27.59           C  
ANISOU 4303  CD  LYS B  26     2752   4713   3017    110    171    509       C  
ATOM   4304  CE  LYS B  26     -23.985 -40.086  19.709  1.00 32.03           C  
ANISOU 4304  CE  LYS B  26     3625   5569   2976    -74    473    199       C  
ATOM   4305  NZ  LYS B  26     -25.341 -39.553  19.947  1.00 40.58           N  
ANISOU 4305  NZ  LYS B  26     4013   6747   4656     18    438    128       N  
ATOM   4306  C   LYS B  26     -19.193 -39.764  15.539  1.00 16.89           C  
ANISOU 4306  C   LYS B  26     2354   2198   1865     42   -131    184       C  
ATOM   4307  O   LYS B  26     -18.444 -38.785  15.440  1.00 18.13           O  
ANISOU 4307  O   LYS B  26     2453   2366   2067    -23   -152    436       O  
ATOM   4308  N   ILE B  27     -19.501 -40.559  14.514  1.00 15.67           N  
ANISOU 4308  N   ILE B  27     2553   1622   1777    202   -202    403       N  
ATOM   4309  CA  ILE B  27     -18.988 -40.324  13.168  1.00 15.18           C  
ANISOU 4309  CA  ILE B  27     2282   1663   1822    157   -142    355       C  
ATOM   4310  CB  ILE B  27     -18.328 -41.570  12.589  1.00 16.24           C  
ANISOU 4310  CB  ILE B  27     2120   1828   2222    415   -162    415       C  
ATOM   4311  CG1 ILE B  27     -17.207 -42.070  13.509  1.00 18.16           C  
ANISOU 4311  CG1 ILE B  27     2541   2238   2119    547   -341    365       C  
ATOM   4312  CG2 ILE B  27     -17.829 -41.304  11.183  1.00 18.54           C  
ANISOU 4312  CG2 ILE B  27     2613   2165   2263    522    -80    258       C  
ATOM   4313  CD1 ILE B  27     -16.146 -41.017  13.822  1.00 19.25           C  
ANISOU 4313  CD1 ILE B  27     2232   2488   2595    490    -98    534       C  
ATOM   4314  C   ILE B  27     -20.110 -39.809  12.274  1.00 14.70           C  
ANISOU 4314  C   ILE B  27     2197   1543   1845    252   -120    276       C  
ATOM   4315  O   ILE B  27     -21.172 -40.400  12.217  1.00 16.49           O  
ANISOU 4315  O   ILE B  27     2303   1696   2265    125   -401    154       O  
ATOM   4316  N   ALA B  28     -19.833 -38.694  11.579  1.00 14.27           N  
ANISOU 4316  N   ALA B  28     1881   1750   1789    109   -134    318       N  
ATOM   4317  CA  ALA B  28     -20.814 -38.121  10.668  1.00 15.29           C  
ANISOU 4317  CA  ALA B  28     2105   1944   1759    388    -86    381       C  
ATOM   4318  CB  ALA B  28     -20.752 -36.606  10.731  1.00 15.37           C  
ANISOU 4318  CB  ALA B  28     2019   1931   1887    237   -167    479       C  
ATOM   4319  C   ALA B  28     -20.605 -38.599   9.229  1.00 15.10           C  
ANISOU 4319  C   ALA B  28     2160   1709   1865    299     18    257       C  
ATOM   4320  O   ALA B  28     -19.493 -38.649   8.734  1.00 17.09           O  
ANISOU 4320  O   ALA B  28     2262   2559   1673    809     64    370       O  
ATOM   4321  N   SER B  29     -21.721 -38.904   8.565  1.00 15.36           N  
ANISOU 4321  N   SER B  29     2273   1843   1718    275    -17    318       N  
ATOM   4322  CA  SER B  29     -21.830 -38.767   7.104  1.00 14.77           C  
ANISOU 4322  CA  SER B  29     2299   1611   1703     92    -18    326       C  
ATOM   4323  CB  SER B  29     -22.576 -39.922   6.471  1.00 15.28           C  
ANISOU 4323  CB  SER B  29     2277   1720   1808    159   -170    322       C  
ATOM   4324  OG  SER B  29     -22.625 -39.823   5.047  1.00 15.01           O  
ANISOU 4324  OG  SER B  29     2193   1773   1737    -39   -106    275       O  
ATOM   4325  C   SER B  29     -22.448 -37.390   6.851  1.00 15.78           C  
ANISOU 4325  C   SER B  29     2461   1702   1831    246   -106    116       C  
ATOM   4326  O   SER B  29     -22.400 -36.532   7.726  1.00 17.53           O  
ANISOU 4326  O   SER B  29     3239   1472   1950    340   -210    187       O  
ATOM   4327  N   ARG B  30     -22.980 -37.148   5.665  1.00 15.16           N  
ANISOU 4327  N   ARG B  30     2351   1526   1881     62   -169     62       N  
ATOM   4328  CA  ARG B  30     -23.388 -35.803   5.324  1.00 15.36           C  
ANISOU 4328  CA  ARG B  30     2253   1817   1764    393    -43    302       C  
ATOM   4329  CB  ARG B  30     -22.179 -35.006   4.846  1.00 16.42           C  
ANISOU 4329  CB  ARG B  30     2205   2190   1841    331   -103    218       C  
ATOM   4330  CG  ARG B  30     -22.421 -33.518   4.717  1.00 17.14           C  
ANISOU 4330  CG  ARG B  30     2534   2199   1777    275     74    270       C  
ATOM   4331  CD  ARG B  30     -21.174 -32.807   4.263  1.00 19.14           C  
ANISOU 4331  CD  ARG B  30     2619   2368   2284    354    502    413       C  
ATOM   4332  NE  ARG B  30     -20.213 -32.762   5.355  1.00 27.83           N  
ANISOU 4332  NE  ARG B  30     3597   3076   3900    506   -181      6       N  
ATOM   4333  CZ  ARG B  30     -20.016 -31.721   6.154  1.00 23.39           C  
ANISOU 4333  CZ  ARG B  30     2878   2210   3796    264    593   -114       C  
ATOM   4334  NH1 ARG B  30     -20.698 -30.606   6.011  1.00 33.22           N  
ANISOU 4334  NH1 ARG B  30     4069   3742   4808   1433    -69   1639       N  
ATOM   4335  NH2 ARG B  30     -19.103 -31.787   7.084  1.00 31.73           N  
ANISOU 4335  NH2 ARG B  30     4171   3547   4336    201    -41    925       N  
ATOM   4336  C   ARG B  30     -24.455 -35.793   4.234  1.00 15.11           C  
ANISOU 4336  C   ARG B  30     2168   1789   1784    234     13    162       C  
ATOM   4337  O   ARG B  30     -24.422 -36.594   3.317  1.00 15.07           O  
ANISOU 4337  O   ARG B  30     2214   1681   1830    131    -22    156       O  
ATOM   4338  N   ILE B  31     -25.390 -34.846   4.377  1.00 14.40           N  
ANISOU 4338  N   ILE B  31     2129   1756   1587    247    137    299       N  
ATOM   4339  CA  ILE B  31     -26.232 -34.386   3.279  1.00 15.12           C  
ANISOU 4339  CA  ILE B  31     2163   1801   1778    141    -56    259       C  
ATOM   4340  CB  ILE B  31     -27.713 -34.737   3.515  1.00 17.92           C  
ANISOU 4340  CB  ILE B  31     2326   2178   2305     -6     15    508       C  
ATOM   4341  CG1 ILE B  31     -28.258 -34.104   4.796  1.00 18.98           C  
ANISOU 4341  CG1 ILE B  31     2505   2393   2311    115    -56    603       C  
ATOM   4342  CG2 ILE B  31     -27.914 -36.243   3.469  1.00 20.35           C  
ANISOU 4342  CG2 ILE B  31     2781   2324   2625   -315    137    599       C  
ATOM   4343  CD1 ILE B  31     -29.763 -34.249   4.959  1.00 20.77           C  
ANISOU 4343  CD1 ILE B  31     2680   2717   2492    -71     13    632       C  
ATOM   4344  C   ILE B  31     -25.993 -32.887   3.140  1.00 16.02           C  
ANISOU 4344  C   ILE B  31     2374   1900   1812     -9   -171    286       C  
ATOM   4345  O   ILE B  31     -25.559 -32.253   4.074  1.00 16.19           O  
ANISOU 4345  O   ILE B  31     2498   1858   1795     10   -245    201       O  
ATOM   4346  N   GLY B  32     -26.308 -32.324   1.970  1.00 16.25           N  
ANISOU 4346  N   GLY B  32     2321   1774   2076   -167   -243    402       N  
ATOM   4347  CA  GLY B  32     -26.040 -30.942   1.741  1.00 15.84           C  
ANISOU 4347  CA  GLY B  32     2459   1761   1797   -248   -295    398       C  
ATOM   4348  C   GLY B  32     -26.777 -30.452   0.528  1.00 16.08           C  
ANISOU 4348  C   GLY B  32     2462   1762   1886   -225   -402    418       C  
ATOM   4349  O   GLY B  32     -27.470 -31.229  -0.152  1.00 20.55           O  
ANISOU 4349  O   GLY B  32     3331   1855   2622   -722   -746    495       O  
ATOM   4350  N   ILE B  33     -26.675 -29.152   0.279  1.00 15.64           N  
ANISOU 4350  N   ILE B  33     2349   1753   1841    -94   -332    275       N  
ATOM   4351  CA  ILE B  33     -27.361 -28.549  -0.837  1.00 15.05           C  
ANISOU 4351  CA  ILE B  33     1942   2002   1775    -12   -280    258       C  
ATOM   4352  CB  ILE B  33     -27.704 -27.081  -0.531  1.00 16.07           C  
ANISOU 4352  CB  ILE B  33     2095   2018   1989    120   -346    267       C  
ATOM   4353  CG1 ILE B  33     -28.648 -26.965   0.668  1.00 19.18           C  
ANISOU 4353  CG1 ILE B  33     2681   2461   2143    379   -222    140       C  
ATOM   4354  CG2 ILE B  33     -28.243 -26.404  -1.783  1.00 15.24           C  
ANISOU 4354  CG2 ILE B  33     1917   1951   1921     83   -276    280       C  
ATOM   4355  CD1 ILE B  33     -29.070 -25.546   0.991  1.00 20.44           C  
ANISOU 4355  CD1 ILE B  33     2960   2519   2287     90   -345   -220       C  
ATOM   4356  C   ILE B  33     -26.462 -28.698  -2.064  1.00 14.42           C  
ANISOU 4356  C   ILE B  33     1795   1825   1860   -133   -227    286       C  
ATOM   4357  O   ILE B  33     -25.324 -28.257  -2.074  1.00 16.00           O  
ANISOU 4357  O   ILE B  33     1763   2098   2215   -141   -192    310       O  
ATOM   4358  N   PRO B  34     -26.942 -29.334  -3.143  1.00 13.09           N  
ANISOU 4358  N   PRO B  34     1682   1523   1768    -47   -149    304       N  
ATOM   4359  CA  PRO B  34     -26.066 -29.625  -4.260  1.00 13.34           C  
ANISOU 4359  CA  PRO B  34     1774   1640   1652    -48   -119    315       C  
ATOM   4360  CB  PRO B  34     -26.783 -30.722  -5.049  1.00 16.69           C  
ANISOU 4360  CB  PRO B  34     2209   1869   2263   -301    -83    124       C  
ATOM   4361  CG  PRO B  34     -28.198 -30.629  -4.641  1.00 18.72           C  
ANISOU 4361  CG  PRO B  34     2053   2645   2415   -295   -319   -299       C  
ATOM   4362  CD  PRO B  34     -28.268 -29.947  -3.289  1.00 14.24           C  
ANISOU 4362  CD  PRO B  34     1508   2054   1848    -13   -135    224       C  
ATOM   4363  C   PRO B  34     -25.789 -28.441  -5.195  1.00 12.68           C  
ANISOU 4363  C   PRO B  34     1607   1552   1657      9   -157    315       C  
ATOM   4364  O   PRO B  34     -26.518 -27.448  -5.191  1.00 12.24           O  
ANISOU 4364  O   PRO B  34     1509   1431   1707    -65   -182     50       O  
ATOM   4365  N   TYR B  35     -24.743 -28.629  -6.007  1.00 12.31           N  
ANISOU 4365  N   TYR B  35     1562   1358   1755     18   -120    294       N  
ATOM   4366  CA  TYR B  35     -24.369 -27.698  -7.063  1.00 12.64           C  
ANISOU 4366  CA  TYR B  35     1889   1202   1709     -9   -214    284       C  
ATOM   4367  CB  TYR B  35     -22.888 -27.345  -6.948  1.00 12.67           C  
ANISOU 4367  CB  TYR B  35     1862   1307   1644     21   -195    167       C  
ATOM   4368  CG  TYR B  35     -22.624 -26.243  -5.966  1.00 13.88           C  
ANISOU 4368  CG  TYR B  35     1625   1537   2111    -17   -399      4       C  
ATOM   4369  CD1 TYR B  35     -22.716 -26.434  -4.598  1.00 15.30           C  
ANISOU 4369  CD1 TYR B  35     1602   2066   2142   -299   -371   -369       C  
ATOM   4370  CE1 TYR B  35     -22.500 -25.382  -3.725  1.00 17.23           C  
ANISOU 4370  CE1 TYR B  35     1822   2653   2069     49   -463   -743       C  
ATOM   4371  CZ  TYR B  35     -22.187 -24.132  -4.224  1.00 18.41           C  
ANISOU 4371  CZ  TYR B  35     1938   2289   2767     79   -668  -1012       C  
ATOM   4372  OH  TYR B  35     -21.917 -23.047  -3.447  1.00 29.59           O  
ANISOU 4372  OH  TYR B  35     2861   3715   4667    443   -884  -2694       O  
ATOM   4373  CE2 TYR B  35     -22.039 -23.950  -5.571  1.00 18.56           C  
ANISOU 4373  CE2 TYR B  35     2350   1656   3044     84   -970    -99       C  
ATOM   4374  CD2 TYR B  35     -22.299 -24.989  -6.432  1.00 16.76           C  
ANISOU 4374  CD2 TYR B  35     2196   1586   2586      3   -678     93       C  
ATOM   4375  C   TYR B  35     -24.714 -28.247  -8.453  1.00 13.43           C  
ANISOU 4375  C   TYR B  35     1937   1351   1812   -282   -131    232       C  
ATOM   4376  O   TYR B  35     -24.409 -27.587  -9.449  1.00 14.31           O  
ANISOU 4376  O   TYR B  35     2230   1550   1658   -330   -320    283       O  
ATOM   4377  N   SER B  36     -25.324 -29.434  -8.497  1.00 11.89           N  
ANISOU 4377  N   SER B  36     1869   1231   1417   -259   -340    326       N  
ATOM   4378  CA  SER B  36     -25.970 -29.969  -9.696  1.00 14.17           C  
ANISOU 4378  CA  SER B  36     2286   1392   1703   -415   -353    107       C  
ATOM   4379  CB  SER B  36     -26.142 -31.449  -9.543  1.00 16.11           C  
ANISOU 4379  CB  SER B  36     2673   1422   2024   -396   -453   -200       C  
ATOM   4380  OG  SER B  36     -26.859 -31.754  -8.374  1.00 17.25           O  
ANISOU 4380  OG  SER B  36     2442   1776   2334   -330   -563    235       O  
ATOM   4381  C   SER B  36     -27.301 -29.239  -9.892  1.00 15.95           C  
ANISOU 4381  C   SER B  36     2353   1710   1997   -406   -371     81       C  
ATOM   4382  O   SER B  36     -27.908 -28.725  -8.944  1.00 17.31           O  
ANISOU 4382  O   SER B  36     2483   2001   2092     21   -141    289       O  
ATOM   4383  N   THR B  37     -27.817 -29.275 -11.112  1.00 16.67           N  
ANISOU 4383  N   THR B  37     2586   1817   1929   -214   -347    277       N  
ATOM   4384  CA  THR B  37     -29.010 -28.543 -11.528  1.00 16.36           C  
ANISOU 4384  CA  THR B  37     2411   1508   2297    -32    -84    207       C  
ATOM   4385  CB  THR B  37     -30.310 -29.322 -11.276  1.00 16.99           C  
ANISOU 4385  CB  THR B  37     2342   1781   2330   -165   -244   -184       C  
ATOM   4386  OG1 THR B  37     -30.570 -29.549  -9.888  1.00 18.21           O  
ANISOU 4386  OG1 THR B  37     2491   1945   2481    -84     68    141       O  
ATOM   4387  CG2 THR B  37     -30.302 -30.659 -11.964  1.00 18.04           C  
ANISOU 4387  CG2 THR B  37     2636   1935   2283   -344    119   -391       C  
ATOM   4388  C   THR B  37     -29.038 -27.124 -10.934  1.00 14.82           C  
ANISOU 4388  C   THR B  37     1865   1694   2069    -65   -151     19       C  
ATOM   4389  O   THR B  37     -30.114 -26.597 -10.557  1.00 15.90           O  
ANISOU 4389  O   THR B  37     2106   1715   2217     13    303    234       O  
ATOM   4390  N   PHE B  38     -27.894 -26.445 -10.998  1.00 13.70           N  
ANISOU 4390  N   PHE B  38     1842   1565   1798     -4   -421     54       N  
ATOM   4391  CA  PHE B  38     -27.791 -25.044 -10.667  1.00 13.81           C  
ANISOU 4391  CA  PHE B  38     2030   1481   1734   -115   -200    175       C  
ATOM   4392  CB  PHE B  38     -26.322 -24.690 -10.393  1.00 13.95           C  
ANISOU 4392  CB  PHE B  38     1956   1671   1670    -24   -308    230       C  
ATOM   4393  CG  PHE B  38     -26.021 -23.489  -9.513  1.00 12.15           C  
ANISOU 4393  CG  PHE B  38     1685   1483   1448      1   -116    313       C  
ATOM   4394  CD1 PHE B  38     -26.699 -22.282  -9.618  1.00 13.38           C  
ANISOU 4394  CD1 PHE B  38     1836   1460   1789    -77   -198    176       C  
ATOM   4395  CE1 PHE B  38     -26.357 -21.206  -8.820  1.00 12.96           C  
ANISOU 4395  CE1 PHE B  38     1830   1518   1572    -27   -256    200       C  
ATOM   4396  CZ  PHE B  38     -25.337 -21.310  -7.906  1.00 14.67           C  
ANISOU 4396  CZ  PHE B  38     2113   1618   1841    182   -504    170       C  
ATOM   4397  CD2 PHE B  38     -24.992 -23.568  -8.592  1.00 14.01           C  
ANISOU 4397  CD2 PHE B  38     2022   1537   1762    -59   -408     76       C  
ATOM   4398  CE2 PHE B  38     -24.667 -22.499  -7.773  1.00 14.37           C  
ANISOU 4398  CE2 PHE B  38     2001   1614   1843     90   -721     49       C  
ATOM   4399  C   PHE B  38     -28.358 -24.246 -11.849  1.00 13.53           C  
ANISOU 4399  C   PHE B  38     1982   1449   1708    -47   -195    123       C  
ATOM   4400  O   PHE B  38     -27.891 -24.405 -12.961  1.00 15.35           O  
ANISOU 4400  O   PHE B  38     2463   1714   1654    263     28    182       O  
ATOM   4401  N   GLN B  39     -29.386 -23.437 -11.626  1.00 11.72           N  
ANISOU 4401  N   GLN B  39     1874   1156   1420   -199   -195     80       N  
ATOM   4402  CA  GLN B  39     -30.109 -22.779 -12.726  1.00 12.96           C  
ANISOU 4402  CA  GLN B  39     1938   1366   1620   -111   -193    278       C  
ATOM   4403  CB  GLN B  39     -31.561 -22.498 -12.333  1.00 13.51           C  
ANISOU 4403  CB  GLN B  39     1740   1549   1843   -267   -355    359       C  
ATOM   4404  CG  GLN B  39     -32.333 -23.735 -11.924  1.00 13.83           C  
ANISOU 4404  CG  GLN B  39     1951   1544   1759   -426   -534    328       C  
ATOM   4405  CD  GLN B  39     -32.378 -24.788 -13.006  1.00 16.56           C  
ANISOU 4405  CD  GLN B  39     2331   1786   2172   -388   -735    116       C  
ATOM   4406  OE1 GLN B  39     -32.878 -24.525 -14.091  1.00 23.66           O  
ANISOU 4406  OE1 GLN B  39     3542   3007   2438   -699  -1299     99       O  
ATOM   4407  NE2 GLN B  39     -31.820 -25.963 -12.717  1.00 21.57           N  
ANISOU 4407  NE2 GLN B  39     3075   2043   3076   -264   -383    292       N  
ATOM   4408  C   GLN B  39     -29.442 -21.461 -13.108  1.00 11.38           C  
ANISOU 4408  C   GLN B  39     1769   1286   1266    -81   -278    108       C  
ATOM   4409  O   GLN B  39     -29.098 -20.650 -12.242  1.00 11.96           O  
ANISOU 4409  O   GLN B  39     1964   1268   1310   -163   -213     57       O  
ATOM   4410  N   THR B  40     -29.214 -21.292 -14.415  1.00 12.12           N  
ANISOU 4410  N   THR B  40     2023   1294   1287   -124   -177    108       N  
ATOM   4411  CA  THR B  40     -28.890 -20.022 -15.020  1.00 12.39           C  
ANISOU 4411  CA  THR B  40     2180   1440   1087     27   -207    282       C  
ATOM   4412  CB  THR B  40     -27.595 -20.090 -15.843  1.00 13.26           C  
ANISOU 4412  CB  THR B  40     2090   1584   1363      5   -282    392       C  
ATOM   4413  OG1 THR B  40     -26.477 -20.360 -14.990  1.00 15.26           O  
ANISOU 4413  OG1 THR B  40     1869   2247   1682    268   -243    157       O  
ATOM   4414  CG2 THR B  40     -27.339 -18.797 -16.590  1.00 14.38           C  
ANISOU 4414  CG2 THR B  40     2209   1602   1651     71   -112    481       C  
ATOM   4415  C   THR B  40     -30.115 -19.615 -15.842  1.00 13.25           C  
ANISOU 4415  C   THR B  40     2027   1564   1441     -5   -199    263       C  
ATOM   4416  O   THR B  40     -30.432 -20.251 -16.855  1.00 15.66           O  
ANISOU 4416  O   THR B  40     2538   1745   1664     97   -428    -14       O  
ATOM   4417  N   ILE B  41     -30.831 -18.603 -15.362  1.00 12.10           N  
ANISOU 4417  N   ILE B  41     1808   1252   1535   -160   -268    250       N  
ATOM   4418  CA  ILE B  41     -32.137 -18.224 -15.899  1.00 12.36           C  
ANISOU 4418  CA  ILE B  41     1775   1384   1536   -247   -392    167       C  
ATOM   4419  CB  ILE B  41     -33.136 -18.037 -14.749  1.00 12.57           C  
ANISOU 4419  CB  ILE B  41     1744   1451   1581   -354   -390    124       C  
ATOM   4420  CG1 ILE B  41     -33.229 -19.306 -13.906  1.00 13.82           C  
ANISOU 4420  CG1 ILE B  41     1882   1558   1808   -565   -364    146       C  
ATOM   4421  CG2 ILE B  41     -34.490 -17.625 -15.292  1.00 12.86           C  
ANISOU 4421  CG2 ILE B  41     1703   1387   1794   -317   -194    266       C  
ATOM   4422  CD1 ILE B  41     -33.977 -19.120 -12.618  1.00 13.90           C  
ANISOU 4422  CD1 ILE B  41     1781   1696   1803   -488   -368    186       C  
ATOM   4423  C   ILE B  41     -31.974 -16.948 -16.722  1.00 12.02           C  
ANISOU 4423  C   ILE B  41     1714   1327   1526    -34   -406    165       C  
ATOM   4424  O   ILE B  41     -31.485 -15.915 -16.229  1.00 13.57           O  
ANISOU 4424  O   ILE B  41     2102   1403   1648   -318   -688    391       O  
ATOM   4425  N   GLN B  42     -32.369 -17.044 -17.985  1.00 12.63           N  
ANISOU 4425  N   GLN B  42     1887   1430   1482    134   -399    192       N  
ATOM   4426  CA AGLN B  42     -32.340 -15.921 -18.909  0.50 13.98           C  
ANISOU 4426  CA AGLN B  42     2061   1475   1773     81   -347    293       C  
ATOM   4427  CA BGLN B  42     -32.352 -15.942 -18.931  0.50 14.06           C  
ANISOU 4427  CA BGLN B  42     2138   1500   1702    147   -360    303       C  
ATOM   4428  CB AGLN B  42     -32.243 -16.405 -20.356  0.50 16.16           C  
ANISOU 4428  CB AGLN B  42     2377   1879   1883    229   -232    156       C  
ATOM   4429  CB BGLN B  42     -32.362 -16.461 -20.375  0.50 16.00           C  
ANISOU 4429  CB BGLN B  42     2517   1862   1697    368   -293    278       C  
ATOM   4430  CG AGLN B  42     -30.872 -16.996 -20.653  0.50 18.22           C  
ANISOU 4430  CG AGLN B  42     2321   2372   2227    257   -190     15       C  
ATOM   4431  CG BGLN B  42     -31.298 -17.517 -20.697  0.50 17.84           C  
ANISOU 4431  CG BGLN B  42     2754   2239   1785    624   -255    197       C  
ATOM   4432  CD AGLN B  42     -30.723 -17.572 -22.037  0.50 22.36           C  
ANISOU 4432  CD AGLN B  42     2857   3069   2567    304    -56   -399       C  
ATOM   4433  CD BGLN B  42     -29.910 -16.928 -20.775  0.50 20.76           C  
ANISOU 4433  CD BGLN B  42     3042   2782   2063    390   -346    317       C  
ATOM   4434  OE1AGLN B  42     -31.691 -17.929 -22.692  0.50 25.13           O  
ANISOU 4434  OE1AGLN B  42     3087   3918   2542    591   -372   -469       O  
ATOM   4435  OE1BGLN B  42     -29.742 -15.820 -21.282  0.50 24.21           O  
ANISOU 4435  OE1BGLN B  42     3867   2911   2420    409   -259    391       O  
ATOM   4436  NE2AGLN B  42     -29.483 -17.683 -22.476  0.50 24.80           N  
ANISOU 4436  NE2AGLN B  42     3086   3199   3137     44    364   -290       N  
ATOM   4437  NE2BGLN B  42     -28.917 -17.646 -20.240  0.50 23.91           N  
ANISOU 4437  NE2BGLN B  42     4194   3064   1825   1042   -568    278       N  
ATOM   4438  C   GLN B  42     -33.603 -15.099 -18.709  1.00 13.43           C  
ANISOU 4438  C   GLN B  42     2015   1417   1670     53   -341    266       C  
ATOM   4439  O   GLN B  42     -34.658 -15.629 -18.329  1.00 13.97           O  
ANISOU 4439  O   GLN B  42     1967   1704   1634    -72   -419     71       O  
ATOM   4440  N   PRO B  43     -33.547 -13.782 -18.984  1.00 12.19           N  
ANISOU 4440  N   PRO B  43     1681   1341   1606     -7   -298    228       N  
ATOM   4441  CA  PRO B  43     -34.752 -12.968 -18.935  1.00 12.08           C  
ANISOU 4441  CA  PRO B  43     1611   1427   1551    -20   -456    310       C  
ATOM   4442  CB  PRO B  43     -34.233 -11.539 -19.081  1.00 14.74           C  
ANISOU 4442  CB  PRO B  43     2192   1356   2051    -26   -374    160       C  
ATOM   4443  CG  PRO B  43     -32.893 -11.660 -19.691  1.00 17.83           C  
ANISOU 4443  CG  PRO B  43     2371   1782   2619    -93   -165    551       C  
ATOM   4444  CD  PRO B  43     -32.357 -13.032 -19.395  1.00 15.24           C  
ANISOU 4444  CD  PRO B  43     1946   1698   2144   -129   -367    367       C  
ATOM   4445  C   PRO B  43     -35.727 -13.334 -20.062  1.00 12.08           C  
ANISOU 4445  C   PRO B  43     1801   1352   1437   -217   -414    292       C  
ATOM   4446  O   PRO B  43     -35.352 -14.004 -21.033  1.00 13.98           O  
ANISOU 4446  O   PRO B  43     1767   1872   1670     36   -372     69       O  
ATOM   4447  N   VAL B  44     -36.976 -12.910 -19.905  1.00 12.50           N  
ANISOU 4447  N   VAL B  44     1857   1470   1419   -195   -655    209       N  
ATOM   4448  CA  VAL B  44     -38.040 -13.269 -20.869  1.00 12.18           C  
ANISOU 4448  CA  VAL B  44     1656   1498   1474   -124   -620    233       C  
ATOM   4449  CB  VAL B  44     -39.428 -12.897 -20.325  1.00 14.12           C  
ANISOU 4449  CB  VAL B  44     1936   1764   1664   -147   -399    380       C  
ATOM   4450  CG1 VAL B  44     -39.710 -13.615 -19.008  1.00 14.31           C  
ANISOU 4450  CG1 VAL B  44     1864   1850   1719   -390   -220    351       C  
ATOM   4451  CG2 VAL B  44     -39.621 -11.397 -20.213  1.00 14.73           C  
ANISOU 4451  CG2 VAL B  44     1974   1856   1767    134   -517    217       C  
ATOM   4452  C   VAL B  44     -37.813 -12.635 -22.250  1.00 13.19           C  
ANISOU 4452  C   VAL B  44     1861   1533   1616   -212   -560    308       C  
ATOM   4453  O   VAL B  44     -38.397 -13.063 -23.242  1.00 14.35           O  
ANISOU 4453  O   VAL B  44     2172   1672   1606   -310   -596    255       O  
ATOM   4454  N   SER B  45     -37.031 -11.571 -22.305  1.00 12.72           N  
ANISOU 4454  N   SER B  45     1934   1564   1333   -284   -787    330       N  
ATOM   4455  CA  SER B  45     -36.789 -10.807 -23.500  1.00 13.71           C  
ANISOU 4455  CA  SER B  45     2196   1509   1503   -289   -512    348       C  
ATOM   4456  CB  SER B  45     -37.817  -9.714 -23.656  1.00 14.37           C  
ANISOU 4456  CB  SER B  45     2381   1416   1664   -258   -561    442       C  
ATOM   4457  OG  SER B  45     -37.812  -8.874 -22.499  1.00 15.33           O  
ANISOU 4457  OG  SER B  45     2535   1534   1753   -156   -578    263       O  
ATOM   4458  C   SER B  45     -35.374 -10.250 -23.417  1.00 13.25           C  
ANISOU 4458  C   SER B  45     2116   1541   1376   -212   -460    345       C  
ATOM   4459  O   SER B  45     -34.770 -10.203 -22.336  1.00 14.39           O  
ANISOU 4459  O   SER B  45     2067   1913   1487   -362   -580    465       O  
ATOM   4460  N   ASP B  46     -34.839  -9.836 -24.571  1.00 13.89           N  
ANISOU 4460  N   ASP B  46     2174   1731   1371   -123   -355    372       N  
ATOM   4461  CA AASP B  46     -33.457  -9.427 -24.655  0.70 14.99           C  
ANISOU 4461  CA AASP B  46     2148   1676   1867    -59   -411    133       C  
ATOM   4462  CA BASP B  46     -33.459  -9.396 -24.692  0.30 14.16           C  
ANISOU 4462  CA BASP B  46     2036   1688   1656     31   -357    222       C  
ATOM   4463  CB AASP B  46     -33.060  -9.092 -26.096  0.70 17.07           C  
ANISOU 4463  CB AASP B  46     2654   1795   2036     18   -370    439       C  
ATOM   4464  CB BASP B  46     -33.133  -8.961 -26.126  0.30 14.69           C  
ANISOU 4464  CB BASP B  46     2033   1790   1758    197   -305    399       C  
ATOM   4465  CG AASP B  46     -32.965 -10.300 -27.025  0.70 21.14           C  
ANISOU 4465  CG AASP B  46     3239   2249   2542    -34   -331      3       C  
ATOM   4466  CG BASP B  46     -31.660  -8.688 -26.403  0.30 15.12           C  
ANISOU 4466  CG BASP B  46     2041   1916   1788    325   -199    385       C  
ATOM   4467  OD1AASP B  46     -32.860 -11.434 -26.509  0.70 26.31           O  
ANISOU 4467  OD1AASP B  46     4462   2519   3015     84     71    218       O  
ATOM   4468  OD1BASP B  46     -30.828  -9.348 -25.774  0.30 15.72           O  
ANISOU 4468  OD1BASP B  46     1741   2117   2115    326   -237    358       O  
ATOM   4469  OD2AASP B  46     -32.967 -10.096 -28.255  0.70 26.49           O  
ANISOU 4469  OD2AASP B  46     3841   3295   2927    226   -609    771       O  
ATOM   4470  OD2BASP B  46     -31.359  -7.809 -27.261  0.30 17.27           O  
ANISOU 4470  OD2BASP B  46     2077   2429   2053    758   -169    936       O  
ATOM   4471  C   ASP B  46     -33.215  -8.241 -23.719  1.00 13.86           C  
ANISOU 4471  C   ASP B  46     1878   1785   1603    -27   -228    166       C  
ATOM   4472  O   ASP B  46     -33.933  -7.243 -23.734  1.00 16.25           O  
ANISOU 4472  O   ASP B  46     2350   1719   2105     96   -320    187       O  
ATOM   4473  N   ALA B  47     -32.158  -8.362 -22.926  1.00 14.20           N  
ANISOU 4473  N   ALA B  47     2146   1507   1740   -142   -539    156       N  
ATOM   4474  CA  ALA B  47     -31.768  -7.308 -21.991  1.00 15.38           C  
ANISOU 4474  CA  ALA B  47     2311   1589   1943   -265   -477    133       C  
ATOM   4475  CB  ALA B  47     -30.583  -7.749 -21.171  1.00 16.78           C  
ANISOU 4475  CB  ALA B  47     2485   2167   1721   -509   -639    470       C  
ATOM   4476  C   ALA B  47     -31.417  -6.042 -22.766  1.00 14.78           C  
ANISOU 4476  C   ALA B  47     2202   1548   1865   -164   -502    176       C  
ATOM   4477  O   ALA B  47     -30.837  -6.094 -23.845  1.00 14.92           O  
ANISOU 4477  O   ALA B  47     2088   1621   1958   -143   -497    158       O  
ATOM   4478  N   PRO B  48     -31.667  -4.857 -22.174  1.00 16.67           N  
ANISOU 4478  N   PRO B  48     2300   1565   2466   -259   -252    153       N  
ATOM   4479  CA  PRO B  48     -31.286  -3.601 -22.809  1.00 15.75           C  
ANISOU 4479  CA  PRO B  48     2183   1405   2394      2   -616    177       C  
ATOM   4480  CB  PRO B  48     -31.830  -2.545 -21.844  1.00 18.03           C  
ANISOU 4480  CB  PRO B  48     2425   1508   2917    430   -636     66       C  
ATOM   4481  CG  PRO B  48     -32.006  -3.256 -20.540  1.00 24.09           C  
ANISOU 4481  CG  PRO B  48     3712   2060   3380    -57     51    -49       C  
ATOM   4482  CD  PRO B  48     -32.310  -4.682 -20.865  1.00 19.19           C  
ANISOU 4482  CD  PRO B  48     2787   1944   2558    -88   -222     -6       C  
ATOM   4483  C   PRO B  48     -29.761  -3.523 -22.927  1.00 14.80           C  
ANISOU 4483  C   PRO B  48     2219   1531   1871    -44   -570    209       C  
ATOM   4484  O   PRO B  48     -29.059  -3.767 -21.968  1.00 15.26           O  
ANISOU 4484  O   PRO B  48     2261   1698   1837     29   -560    352       O  
ATOM   4485  N   ASN B  49     -29.281  -3.135 -24.113  1.00 14.70           N  
ANISOU 4485  N   ASN B  49     2109   1702   1770    -65   -646    365       N  
ATOM   4486  CA  ASN B  49     -27.863  -3.150 -24.441  1.00 15.80           C  
ANISOU 4486  CA  ASN B  49     2288   1983   1730   -168   -559    240       C  
ATOM   4487  CB  ASN B  49     -27.636  -2.710 -25.885  1.00 19.85           C  
ANISOU 4487  CB  ASN B  49     2860   3149   1530   -323   -544    130       C  
ATOM   4488  CG  ASN B  49     -26.195  -2.816 -26.332  1.00 22.01           C  
ANISOU 4488  CG  ASN B  49     3190   3321   1848    157   -785    303       C  
ATOM   4489  OD1 ASN B  49     -25.613  -3.884 -26.270  1.00 29.55           O  
ANISOU 4489  OD1 ASN B  49     3761   4221   3244   1219  -1503   -389       O  
ATOM   4490  ND2 ASN B  49     -25.613  -1.714 -26.803  1.00 28.01           N  
ANISOU 4490  ND2 ASN B  49     4505   3783   2353   -411   -315    329       N  
ATOM   4491  C   ASN B  49     -27.051  -2.244 -23.497  1.00 13.35           C  
ANISOU 4491  C   ASN B  49     1891   1814   1368      9   -647    541       C  
ATOM   4492  O   ASN B  49     -25.889  -2.532 -23.229  1.00 12.52           O  
ANISOU 4492  O   ASN B  49     1938   1363   1454   -111   -565    517       O  
ATOM   4493  N   ASN B  50     -27.660  -1.182 -22.977  1.00 14.04           N  
ANISOU 4493  N   ASN B  50     2009   1798   1527   -135   -525    393       N  
ATOM   4494  CA  ASN B  50     -26.992  -0.242 -22.100  1.00 13.40           C  
ANISOU 4494  CA  ASN B  50     2060   1590   1441    -41   -445    413       C  
ATOM   4495  CB  ASN B  50     -27.157   1.205 -22.563  1.00 14.15           C  
ANISOU 4495  CB  ASN B  50     2080   1541   1752   -167   -254    484       C  
ATOM   4496  CG  ASN B  50     -28.563   1.708 -22.358  1.00 15.34           C  
ANISOU 4496  CG  ASN B  50     2276   1544   2008    156   -471    521       C  
ATOM   4497  OD1 ASN B  50     -29.471   0.904 -22.077  1.00 15.57           O  
ANISOU 4497  OD1 ASN B  50     2162   1825   1928    125   -198    535       O  
ATOM   4498  ND2 ASN B  50     -28.731   3.023 -22.514  1.00 17.09           N  
ANISOU 4498  ND2 ASN B  50     2866   1469   2158    -71   -737    411       N  
ATOM   4499  C   ASN B  50     -27.469  -0.369 -20.651  1.00 13.31           C  
ANISOU 4499  C   ASN B  50     1781   1737   1538    -56   -373    290       C  
ATOM   4500  O   ASN B  50     -27.179   0.503 -19.824  1.00 13.72           O  
ANISOU 4500  O   ASN B  50     2117   1623   1472    -12   -375    210       O  
ATOM   4501  N   GLY B  51     -28.152  -1.457 -20.316  1.00 12.58           N  
ANISOU 4501  N   GLY B  51     1741   1622   1415    157   -344    327       N  
ATOM   4502  CA  GLY B  51     -28.551  -1.714 -18.928  1.00 13.51           C  
ANISOU 4502  CA  GLY B  51     1884   1799   1450    163   -342    405       C  
ATOM   4503  C   GLY B  51     -29.761  -0.933 -18.410  1.00 11.98           C  
ANISOU 4503  C   GLY B  51     1777   1461   1312     62   -394    387       C  
ATOM   4504  O   GLY B  51     -30.076  -1.060 -17.221  1.00 12.04           O  
ANISOU 4504  O   GLY B  51     1619   1501   1452    -18   -209    398       O  
ATOM   4505  N   ILE B  52     -30.461  -0.176 -19.271  1.00 12.60           N  
ANISOU 4505  N   ILE B  52     1753   1639   1394    121   -424    375       N  
ATOM   4506  CA  ILE B  52     -31.581   0.654 -18.817  1.00 12.59           C  
ANISOU 4506  CA  ILE B  52     1646   1489   1646     54   -444    231       C  
ATOM   4507  CB  ILE B  52     -31.430   2.108 -19.282  1.00 14.20           C  
ANISOU 4507  CB  ILE B  52     1997   1687   1710      4   -193    442       C  
ATOM   4508  CG1 ILE B  52     -30.073   2.689 -18.922  1.00 16.32           C  
ANISOU 4508  CG1 ILE B  52     2008   1944   2248    136   -275    302       C  
ATOM   4509  CG2 ILE B  52     -32.563   2.947 -18.716  1.00 15.23           C  
ANISOU 4509  CG2 ILE B  52     2264   1441   2081    103   -186    417       C  
ATOM   4510  CD1 ILE B  52     -29.776   2.690 -17.484  1.00 16.95           C  
ANISOU 4510  CD1 ILE B  52     2590   1749   2100   -102   -187    467       C  
ATOM   4511  C   ILE B  52     -32.918   0.102 -19.319  1.00 13.24           C  
ANISOU 4511  C   ILE B  52     1790   1447   1792    -63   -451    252       C  
ATOM   4512  O   ILE B  52     -33.148   0.080 -20.523  1.00 14.14           O  
ANISOU 4512  O   ILE B  52     1777   1746   1847    -35   -485    246       O  
ATOM   4513  N   GLY B  53     -33.784  -0.305 -18.384  1.00 12.55           N  
ANISOU 4513  N   GLY B  53     1812   1362   1594     87   -475    222       N  
ATOM   4514  CA  GLY B  53     -35.115  -0.746 -18.715  1.00 12.90           C  
ANISOU 4514  CA  GLY B  53     1885   1453   1561     56   -433     93       C  
ATOM   4515  C   GLY B  53     -35.614  -1.847 -17.815  1.00 12.14           C  
ANISOU 4515  C   GLY B  53     1724   1555   1331    119   -552    133       C  
ATOM   4516  O   GLY B  53     -34.852  -2.461 -17.072  1.00 13.12           O  
ANISOU 4516  O   GLY B  53     1706   1663   1615    140   -602    324       O  
ATOM   4517  N   GLN B  54     -36.917  -2.125 -17.887  1.00 11.76           N  
ANISOU 4517  N   GLN B  54     1655   1316   1495    166   -473    242       N  
ATOM   4518  CA  GLN B  54     -37.476  -3.271 -17.168  1.00 12.08           C  
ANISOU 4518  CA  GLN B  54     1644   1404   1541     64   -415    263       C  
ATOM   4519  CB  GLN B  54     -38.998  -3.298 -17.323  1.00 11.70           C  
ANISOU 4519  CB  GLN B  54     1633   1382   1428     96   -413    333       C  
ATOM   4520  CG  GLN B  54     -39.678  -4.217 -16.339  1.00 12.78           C  
ANISOU 4520  CG  GLN B  54     1767   1778   1309     95   -249    388       C  
ATOM   4521  CD  GLN B  54     -41.183  -4.162 -16.429  1.00 13.83           C  
ANISOU 4521  CD  GLN B  54     1737   1909   1607    228    -87    208       C  
ATOM   4522  OE1 GLN B  54     -41.787  -4.729 -17.332  1.00 17.76           O  
ANISOU 4522  OE1 GLN B  54     2101   2277   2368    249   -434   -192       O  
ATOM   4523  NE2 GLN B  54     -41.812  -3.463 -15.497  1.00 17.10           N  
ANISOU 4523  NE2 GLN B  54     2143   2143   2211    504    -40   -204       N  
ATOM   4524  C   GLN B  54     -36.848  -4.573 -17.666  1.00 12.30           C  
ANISOU 4524  C   GLN B  54     1750   1482   1439    168   -402    333       C  
ATOM   4525  O   GLN B  54     -36.616  -4.762 -18.864  1.00 13.21           O  
ANISOU 4525  O   GLN B  54     1986   1668   1365    -39   -504    317       O  
ATOM   4526  N   ILE B  55     -36.570  -5.466 -16.707  1.00 11.46           N  
ANISOU 4526  N   ILE B  55     1757   1409   1188     50   -464    204       N  
ATOM   4527  CA  ILE B  55     -36.004  -6.794 -16.965  1.00 12.38           C  
ANISOU 4527  CA  ILE B  55     1821   1357   1525      8   -328    194       C  
ATOM   4528  CB  ILE B  55     -34.529  -6.868 -16.542  1.00 11.87           C  
ANISOU 4528  CB  ILE B  55     1747   1146   1615    -21   -310     77       C  
ATOM   4529  CG1 ILE B  55     -33.651  -5.868 -17.306  1.00 12.21           C  
ANISOU 4529  CG1 ILE B  55     1814   1191   1631     17   -235     69       C  
ATOM   4530  CG2 ILE B  55     -33.999  -8.292 -16.630  1.00 12.70           C  
ANISOU 4530  CG2 ILE B  55     2004   1064   1755   -104   -219    121       C  
ATOM   4531  CD1 ILE B  55     -32.362  -5.495 -16.588  1.00 13.27           C  
ANISOU 4531  CD1 ILE B  55     1919   1255   1867     79   -470    198       C  
ATOM   4532  C   ILE B  55     -36.838  -7.789 -16.150  1.00 11.28           C  
ANISOU 4532  C   ILE B  55     1604   1323   1356    -39   -423    128       C  
ATOM   4533  O   ILE B  55     -37.015  -7.571 -14.975  1.00 12.58           O  
ANISOU 4533  O   ILE B  55     1882   1569   1329    -16   -294    213       O  
ATOM   4534  N   THR B  56     -37.309  -8.865 -16.785  1.00 10.79           N  
ANISOU 4534  N   THR B  56     1512   1333   1255   -111   -336    100       N  
ATOM   4535  CA  THR B  56     -38.164  -9.840 -16.115  1.00 11.22           C  
ANISOU 4535  CA  THR B  56     1563   1185   1515    -49   -296    229       C  
ATOM   4536  CB  THR B  56     -39.603  -9.814 -16.647  1.00 12.79           C  
ANISOU 4536  CB  THR B  56     1571   1462   1827    -50   -291    208       C  
ATOM   4537  OG1 THR B  56     -40.170  -8.525 -16.444  1.00 13.42           O  
ANISOU 4537  OG1 THR B  56     1491   1717   1890    195   -299    157       O  
ATOM   4538  CG2 THR B  56     -40.480 -10.862 -16.002  1.00 13.92           C  
ANISOU 4538  CG2 THR B  56     1548   1496   2243    -62   -200    164       C  
ATOM   4539  C   THR B  56     -37.614 -11.262 -16.268  1.00 11.51           C  
ANISOU 4539  C   THR B  56     1682   1253   1437    -21   -334    207       C  
ATOM   4540  O   THR B  56     -37.257 -11.694 -17.374  1.00 12.79           O  
ANISOU 4540  O   THR B  56     1963   1386   1510    -75   -283    160       O  
ATOM   4541  N   PHE B  57     -37.560 -11.964 -15.135  1.00 11.20           N  
ANISOU 4541  N   PHE B  57     1670   1162   1421    -89   -362    182       N  
ATOM   4542  CA  PHE B  57     -37.323 -13.401 -15.111  1.00 11.55           C  
ANISOU 4542  CA  PHE B  57     1737   1175   1474    -71   -269    248       C  
ATOM   4543  CB  PHE B  57     -36.222 -13.763 -14.102  1.00 12.06           C  
ANISOU 4543  CB  PHE B  57     1845   1274   1463   -179   -380    281       C  
ATOM   4544  CG  PHE B  57     -34.911 -13.074 -14.365  1.00 11.77           C  
ANISOU 4544  CG  PHE B  57     1620   1486   1363    -95   -380    196       C  
ATOM   4545  CD1 PHE B  57     -34.010 -13.593 -15.281  1.00 12.61           C  
ANISOU 4545  CD1 PHE B  57     1779   1658   1351      8   -426    288       C  
ATOM   4546  CE1 PHE B  57     -32.843 -12.918 -15.566  1.00 12.80           C  
ANISOU 4546  CE1 PHE B  57     1721   1682   1459    -19   -428    334       C  
ATOM   4547  CZ  PHE B  57     -32.543 -11.732 -14.934  1.00 13.08           C  
ANISOU 4547  CZ  PHE B  57     1762   1517   1688   -212   -349    394       C  
ATOM   4548  CD2 PHE B  57     -34.619 -11.858 -13.758  1.00 12.45           C  
ANISOU 4548  CD2 PHE B  57     1650   1494   1585   -221   -210    171       C  
ATOM   4549  CE2 PHE B  57     -33.433 -11.191 -14.036  1.00 13.73           C  
ANISOU 4549  CE2 PHE B  57     1831   1692   1691   -442   -335    214       C  
ATOM   4550  C   PHE B  57     -38.637 -14.086 -14.753  1.00 12.23           C  
ANISOU 4550  C   PHE B  57     1730   1389   1526   -115   -326    223       C  
ATOM   4551  O   PHE B  57     -39.325 -13.654 -13.818  1.00 13.52           O  
ANISOU 4551  O   PHE B  57     2032   1294   1809   -137    -74     95       O  
ATOM   4552  N   ASN B  58     -38.979 -15.138 -15.505  1.00 12.28           N  
ANISOU 4552  N   ASN B  58     1599   1382   1683   -163   -269    190       N  
ATOM   4553  CA  ASN B  58     -40.207 -15.874 -15.296  1.00 13.11           C  
ANISOU 4553  CA  ASN B  58     1644   1509   1827   -265   -290    259       C  
ATOM   4554  CB  ASN B  58     -41.297 -15.426 -16.272  1.00 13.77           C  
ANISOU 4554  CB  ASN B  58     1605   1608   2019   -254   -339    254       C  
ATOM   4555  CG  ASN B  58     -42.592 -16.196 -16.161  1.00 14.93           C  
ANISOU 4555  CG  ASN B  58     1440   2012   2218   -288   -552    534       C  
ATOM   4556  OD1 ASN B  58     -42.660 -17.226 -15.492  1.00 17.02           O  
ANISOU 4556  OD1 ASN B  58     2112   2221   2130   -749   -539    546       O  
ATOM   4557  ND2 ASN B  58     -43.597 -15.759 -16.910  1.00 21.50           N  
ANISOU 4557  ND2 ASN B  58     1915   2688   3565   -119  -1203    733       N  
ATOM   4558  C   ASN B  58     -39.875 -17.352 -15.420  1.00 12.97           C  
ANISOU 4558  C   ASN B  58     1816   1452   1657   -322   -293    237       C  
ATOM   4559  O   ASN B  58     -39.688 -17.841 -16.535  1.00 14.88           O  
ANISOU 4559  O   ASN B  58     2288   1598   1765   -398   -174    141       O  
ATOM   4560  N   GLN B  59     -39.733 -18.037 -14.274  1.00 12.12           N  
ANISOU 4560  N   GLN B  59     1893   1208   1504   -326   -302     39       N  
ATOM   4561  CA  GLN B  59     -39.246 -19.414 -14.327  1.00 12.13           C  
ANISOU 4561  CA  GLN B  59     1798   1317   1491   -251   -198    144       C  
ATOM   4562  CB  GLN B  59     -37.724 -19.427 -14.364  1.00 13.75           C  
ANISOU 4562  CB  GLN B  59     1824   1596   1801   -340   -196    138       C  
ATOM   4563  CG  GLN B  59     -37.174 -20.843 -14.477  1.00 14.42           C  
ANISOU 4563  CG  GLN B  59     1929   1577   1972   -231   -110    183       C  
ATOM   4564  CD  GLN B  59     -37.712 -21.535 -15.707  1.00 14.39           C  
ANISOU 4564  CD  GLN B  59     2380   1388   1697   -270    143    177       C  
ATOM   4565  OE1 GLN B  59     -37.372 -21.158 -16.820  1.00 18.52           O  
ANISOU 4565  OE1 GLN B  59     3053   2069   1913   -449    406    350       O  
ATOM   4566  NE2 GLN B  59     -38.578 -22.523 -15.520  1.00 15.36           N  
ANISOU 4566  NE2 GLN B  59     2667   1266   1900   -415    -45    254       N  
ATOM   4567  C   GLN B  59     -39.752 -20.197 -13.119  1.00 12.83           C  
ANISOU 4567  C   GLN B  59     1836   1511   1527   -318   -264    214       C  
ATOM   4568  O   GLN B  59     -39.134 -20.216 -12.040  1.00 12.61           O  
ANISOU 4568  O   GLN B  59     1739   1444   1605   -197   -318     41       O  
ATOM   4569  N   PRO B  60     -40.876 -20.907 -13.269  1.00 12.26           N  
ANISOU 4569  N   PRO B  60     1654   1557   1446   -242   -321    142       N  
ATOM   4570  CA  PRO B  60     -41.296 -21.860 -12.244  1.00 12.52           C  
ANISOU 4570  CA  PRO B  60     1788   1527   1439   -243   -400    122       C  
ATOM   4571  CB  PRO B  60     -42.494 -22.558 -12.883  1.00 13.57           C  
ANISOU 4571  CB  PRO B  60     1776   1550   1827   -399   -432    200       C  
ATOM   4572  CG  PRO B  60     -43.028 -21.530 -13.861  1.00 13.94           C  
ANISOU 4572  CG  PRO B  60     1755   1825   1716   -395   -552    197       C  
ATOM   4573  CD  PRO B  60     -41.783 -20.904 -14.427  1.00 13.86           C  
ANISOU 4573  CD  PRO B  60     1741   1940   1583   -289   -442    249       C  
ATOM   4574  C   PRO B  60     -40.174 -22.853 -11.943  1.00 12.23           C  
ANISOU 4574  C   PRO B  60     1680   1493   1472   -299   -490    -26       C  
ATOM   4575  O   PRO B  60     -39.500 -23.298 -12.860  1.00 12.89           O  
ANISOU 4575  O   PRO B  60     1829   1606   1462   -145   -161    229       O  
ATOM   4576  N   LEU B  61     -40.032 -23.208 -10.666  1.00 12.48           N  
ANISOU 4576  N   LEU B  61     1829   1466   1447   -227   -245      5       N  
ATOM   4577  CA  LEU B  61     -38.988 -24.145 -10.225  1.00 12.67           C  
ANISOU 4577  CA  LEU B  61     1780   1411   1622   -258   -244      2       C  
ATOM   4578  CB  LEU B  61     -37.830 -23.398  -9.576  1.00 13.44           C  
ANISOU 4578  CB  LEU B  61     1709   1685   1709   -289   -314    182       C  
ATOM   4579  CG  LEU B  61     -36.963 -22.553 -10.507  1.00 14.26           C  
ANISOU 4579  CG  LEU B  61     1797   1868   1750   -266   -170    217       C  
ATOM   4580  CD1 LEU B  61     -35.955 -21.747  -9.710  1.00 14.51           C  
ANISOU 4580  CD1 LEU B  61     1657   1933   1923   -391   -229    446       C  
ATOM   4581  CD2 LEU B  61     -36.273 -23.401 -11.553  1.00 14.88           C  
ANISOU 4581  CD2 LEU B  61     1581   2320   1751   -184   -180    201       C  
ATOM   4582  C   LEU B  61     -39.613 -25.126  -9.240  1.00 12.86           C  
ANISOU 4582  C   LEU B  61     1677   1585   1621   -221   -328    180       C  
ATOM   4583  O   LEU B  61     -40.212 -24.719  -8.240  1.00 14.68           O  
ANISOU 4583  O   LEU B  61     2108   1729   1741   -181    -64    312       O  
ATOM   4584  N   GLY B  62     -39.473 -26.427  -9.533  1.00 13.83           N  
ANISOU 4584  N   GLY B  62     2002   1637   1616   -391   -484    109       N  
ATOM   4585  CA  GLY B  62     -40.044 -27.442  -8.648  1.00 15.22           C  
ANISOU 4585  CA  GLY B  62     2048   1769   1964   -467   -610    291       C  
ATOM   4586  C   GLY B  62     -39.181 -27.660  -7.423  1.00 13.79           C  
ANISOU 4586  C   GLY B  62     2150   1388   1699   -732   -525    176       C  
ATOM   4587  O   GLY B  62     -38.022 -27.221  -7.366  1.00 13.84           O  
ANISOU 4587  O   GLY B  62     1920   1616   1722   -602   -601    222       O  
ATOM   4588  N   ASN B  63     -39.748 -28.333  -6.426  1.00 12.59           N  
ANISOU 4588  N   ASN B  63     1808   1372   1602   -382   -412    206       N  
ATOM   4589  CA  ASN B  63     -38.966 -28.796  -5.280  1.00 12.45           C  
ANISOU 4589  CA  ASN B  63     1851   1277   1599   -275   -414    178       C  
ATOM   4590  CB  ASN B  63     -38.092 -29.977  -5.702  1.00 13.10           C  
ANISOU 4590  CB  ASN B  63     1936   1291   1750   -414   -363    -27       C  
ATOM   4591  CG  ASN B  63     -38.960 -31.150  -6.102  1.00 14.41           C  
ANISOU 4591  CG  ASN B  63     2105   1527   1842   -691   -297     31       C  
ATOM   4592  OD1 ASN B  63     -39.481 -31.869  -5.241  1.00 14.36           O  
ANISOU 4592  OD1 ASN B  63     2014   1526   1913   -449   -244    169       O  
ATOM   4593  ND2 ASN B  63     -39.149 -31.339  -7.399  1.00 16.25           N  
ANISOU 4593  ND2 ASN B  63     2469   1782   1920   -488   -473    -96       N  
ATOM   4594  C   ASN B  63     -38.284 -27.590  -4.611  1.00 11.75           C  
ANISOU 4594  C   ASN B  63     1629   1352   1480   -236   -413    235       C  
ATOM   4595  O   ASN B  63     -38.976 -26.620  -4.337  1.00 12.45           O  
ANISOU 4595  O   ASN B  63     1694   1371   1664   -192   -311     97       O  
ATOM   4596  N   LEU B  64     -36.996 -27.694  -4.254  1.00 10.70           N  
ANISOU 4596  N   LEU B  64     1519   1062   1482   -161   -256    210       N  
ATOM   4597  CA  LEU B  64     -36.363 -26.661  -3.451  1.00 11.70           C  
ANISOU 4597  CA  LEU B  64     1721   1205   1518   -324   -116     76       C  
ATOM   4598  CB  LEU B  64     -35.499 -27.291  -2.366  1.00 11.45           C  
ANISOU 4598  CB  LEU B  64     1470   1313   1568   -276    -53     32       C  
ATOM   4599  CG  LEU B  64     -36.211 -28.212  -1.386  1.00 11.62           C  
ANISOU 4599  CG  LEU B  64     1655   1240   1518   -211   -130    148       C  
ATOM   4600  CD1 LEU B  64     -35.240 -28.702  -0.321  1.00 13.06           C  
ANISOU 4600  CD1 LEU B  64     1688   1409   1863   -228   -233    243       C  
ATOM   4601  CD2 LEU B  64     -37.432 -27.550  -0.762  1.00 13.37           C  
ANISOU 4601  CD2 LEU B  64     1686   1661   1731   -206    -32    169       C  
ATOM   4602  C   LEU B  64     -35.525 -25.716  -4.316  1.00 10.88           C  
ANISOU 4602  C   LEU B  64     1450   1360   1323   -217    -61     29       C  
ATOM   4603  O   LEU B  64     -34.804 -26.132  -5.222  1.00 12.14           O  
ANISOU 4603  O   LEU B  64     1737   1496   1377   -258     80     57       O  
ATOM   4604  N   THR B  65     -35.596 -24.428  -3.975  1.00 11.01           N  
ANISOU 4604  N   THR B  65     1610   1293   1277   -257     39     87       N  
ATOM   4605  CA  THR B  65     -34.877 -23.351  -4.646  1.00 10.71           C  
ANISOU 4605  CA  THR B  65     1462   1285   1323   -262     69      3       C  
ATOM   4606  CB  THR B  65     -35.854 -22.422  -5.394  1.00 11.52           C  
ANISOU 4606  CB  THR B  65     1654   1314   1408   -339    -73    100       C  
ATOM   4607  OG1 THR B  65     -36.465 -23.174  -6.449  1.00 13.66           O  
ANISOU 4607  OG1 THR B  65     2137   1539   1515   -429   -302    103       O  
ATOM   4608  CG2 THR B  65     -35.167 -21.215  -5.986  1.00 12.75           C  
ANISOU 4608  CG2 THR B  65     1736   1323   1784   -281   -182    293       C  
ATOM   4609  C   THR B  65     -34.034 -22.600  -3.609  1.00 10.71           C  
ANISOU 4609  C   THR B  65     1510   1244   1315   -312     33    105       C  
ATOM   4610  O   THR B  65     -34.494 -22.305  -2.508  1.00 11.88           O  
ANISOU 4610  O   THR B  65     1585   1503   1423   -139      4   -206       O  
ATOM   4611  N   GLY B  66     -32.805 -22.252  -3.996  1.00 10.23           N  
ANISOU 4611  N   GLY B  66     1405   1267   1213   -205    -31    108       N  
ATOM   4612  CA  GLY B  66     -31.924 -21.497  -3.113  1.00 10.72           C  
ANISOU 4612  CA  GLY B  66     1511   1178   1381   -310    -64    149       C  
ATOM   4613  C   GLY B  66     -32.563 -20.228  -2.575  1.00 11.32           C  
ANISOU 4613  C   GLY B  66     1597   1351   1351   -196   -206     60       C  
ATOM   4614  O   GLY B  66     -33.207 -19.462  -3.302  1.00 11.16           O  
ANISOU 4614  O   GLY B  66     1368   1352   1520   -150   -125    113       O  
ATOM   4615  N   GLY B  67     -32.299 -19.951  -1.287  1.00 10.48           N  
ANISOU 4615  N   GLY B  67     1440   1182   1358    -36   -318     48       N  
ATOM   4616  CA  GLY B  67     -32.888 -18.784  -0.635  1.00 10.53           C  
ANISOU 4616  CA  GLY B  67     1316   1323   1362    -30   -309    -34       C  
ATOM   4617  C   GLY B  67     -32.239 -17.467  -0.980  1.00 10.59           C  
ANISOU 4617  C   GLY B  67     1484   1329   1210     -7   -268     39       C  
ATOM   4618  O   GLY B  67     -32.834 -16.421  -0.668  1.00 11.84           O  
ANISOU 4618  O   GLY B  67     1441   1448   1610    -58    -10   -123       O  
ATOM   4619  N   ALA B  68     -31.036 -17.490  -1.545  1.00 10.50           N  
ANISOU 4619  N   ALA B  68     1486   1107   1396   -124   -226    -55       N  
ATOM   4620  CA  ALA B  68     -30.294 -16.252  -1.879  1.00 10.80           C  
ANISOU 4620  CA  ALA B  68     1548   1172   1384   -148   -197     75       C  
ATOM   4621  CB  ALA B  68     -29.097 -16.070  -0.968  1.00 10.63           C  
ANISOU 4621  CB  ALA B  68     1599   1125   1313   -309   -124    103       C  
ATOM   4622  C   ALA B  68     -29.921 -16.249  -3.354  1.00 10.55           C  
ANISOU 4622  C   ALA B  68     1393   1208   1408   -216   -215     10       C  
ATOM   4623  O   ALA B  68     -28.751 -16.369  -3.727  1.00 11.16           O  
ANISOU 4623  O   ALA B  68     1466   1342   1429    -51   -158     73       O  
ATOM   4624  N   PRO B  69     -30.905 -16.076  -4.258  1.00 10.49           N  
ANISOU 4624  N   PRO B  69     1452   1289   1243    -65   -189     15       N  
ATOM   4625  CA  PRO B  69     -30.602 -16.008  -5.693  1.00 10.05           C  
ANISOU 4625  CA  PRO B  69     1337   1193   1287    -49   -143     14       C  
ATOM   4626  CB  PRO B  69     -31.972 -15.871  -6.354  1.00 10.95           C  
ANISOU 4626  CB  PRO B  69     1536   1406   1217   -163   -357     55       C  
ATOM   4627  CG  PRO B  69     -32.838 -15.271  -5.267  1.00 12.26           C  
ANISOU 4627  CG  PRO B  69     1676   1479   1502     -6   -366   -107       C  
ATOM   4628  CD  PRO B  69     -32.332 -15.887  -3.976  1.00 11.24           C  
ANISOU 4628  CD  PRO B  69     1502   1381   1386     23   -296   -207       C  
ATOM   4629  C   PRO B  69     -29.703 -14.815  -6.022  1.00 10.26           C  
ANISOU 4629  C   PRO B  69     1303   1284   1310    -98   -143     41       C  
ATOM   4630  O   PRO B  69     -29.735 -13.774  -5.337  1.00 10.95           O  
ANISOU 4630  O   PRO B  69     1686   1072   1402   -177      3    134       O  
ATOM   4631  N   ARG B  70     -28.892 -14.991  -7.058  1.00  9.50           N  
ANISOU 4631  N   ARG B  70     1317   1131   1161   -185   -182     67       N  
ATOM   4632  CA  ARG B  70     -27.941 -13.961  -7.467  1.00  9.66           C  
ANISOU 4632  CA  ARG B  70     1464    984   1222   -188   -236     94       C  
ATOM   4633  CB  ARG B  70     -26.512 -14.504  -7.379  1.00 10.36           C  
ANISOU 4633  CB  ARG B  70     1546   1052   1338    -55   -189    103       C  
ATOM   4634  CG  ARG B  70     -26.148 -15.089  -6.027  1.00 10.47           C  
ANISOU 4634  CG  ARG B  70     1547   1009   1422    -34   -188    154       C  
ATOM   4635  CD  ARG B  70     -24.727 -15.597  -5.941  1.00 11.14           C  
ANISOU 4635  CD  ARG B  70     1535   1159   1536    -92   -182    231       C  
ATOM   4636  NE  ARG B  70     -23.759 -14.536  -5.841  1.00 11.29           N  
ANISOU 4636  NE  ARG B  70     1464   1309   1515   -148   -206    294       N  
ATOM   4637  CZ  ARG B  70     -23.339 -13.989  -4.696  1.00 11.04           C  
ANISOU 4637  CZ  ARG B  70     1589   1116   1489    -88   -110    229       C  
ATOM   4638  NH1 ARG B  70     -23.893 -14.345  -3.532  1.00 11.83           N  
ANISOU 4638  NH1 ARG B  70     1686   1296   1510     75    -80    279       N  
ATOM   4639  NH2 ARG B  70     -22.369 -13.081  -4.743  1.00 11.67           N  
ANISOU 4639  NH2 ARG B  70     1553   1074   1806    -54   -356    259       N  
ATOM   4640  C   ARG B  70     -28.226 -13.499  -8.898  1.00 10.01           C  
ANISOU 4640  C   ARG B  70     1503   1010   1288   -111   -280    144       C  
ATOM   4641  O   ARG B  70     -28.912 -14.178  -9.662  1.00 10.92           O  
ANISOU 4641  O   ARG B  70     1834   1080   1233   -144   -401    194       O  
ATOM   4642  N   LEU B  71     -27.701 -12.307  -9.224  1.00 10.07           N  
ANISOU 4642  N   LEU B  71     1578   1087   1159   -219   -359     80       N  
ATOM   4643  CA  LEU B  71     -27.722 -11.792 -10.567  1.00 10.50           C  
ANISOU 4643  CA  LEU B  71     1483   1283   1221   -168   -243    173       C  
ATOM   4644  CB  LEU B  71     -28.377 -10.410 -10.587  1.00 11.39           C  
ANISOU 4644  CB  LEU B  71     1570   1330   1428   -155   -269    141       C  
ATOM   4645  CG  LEU B  71     -29.845 -10.369 -10.138  1.00 11.26           C  
ANISOU 4645  CG  LEU B  71     1580   1363   1333   -118   -227    147       C  
ATOM   4646  CD1 LEU B  71     -30.299  -8.923  -9.965  1.00 12.00           C  
ANISOU 4646  CD1 LEU B  71     1768   1348   1442   -224   -399    -30       C  
ATOM   4647  CD2 LEU B  71     -30.763 -11.099 -11.130  1.00 12.95           C  
ANISOU 4647  CD2 LEU B  71     1507   1690   1723   -177   -276    145       C  
ATOM   4648  C   LEU B  71     -26.290 -11.732 -11.084  1.00 10.43           C  
ANISOU 4648  C   LEU B  71     1465   1290   1207   -152   -236     17       C  
ATOM   4649  O   LEU B  71     -25.413 -11.177 -10.411  1.00 10.74           O  
ANISOU 4649  O   LEU B  71     1579   1393   1107   -292   -194     43       O  
ATOM   4650  N   ARG B  72     -26.072 -12.316 -12.272  1.00 10.58           N  
ANISOU 4650  N   ARG B  72     1530   1206   1283   -124   -339    -80       N  
ATOM   4651  CA  ARG B  72     -24.812 -12.213 -12.978  1.00 11.33           C  
ANISOU 4651  CA  ARG B  72     1593   1370   1340   -282   -340    130       C  
ATOM   4652  CB  ARG B  72     -24.374 -13.576 -13.510  1.00 13.85           C  
ANISOU 4652  CB  ARG B  72     1828   1577   1857    -81   -137     31       C  
ATOM   4653  CG  ARG B  72     -23.077 -13.568 -14.317  1.00 15.77           C  
ANISOU 4653  CG  ARG B  72     1630   2015   2346    -46   -131     16       C  
ATOM   4654  CD  ARG B  72     -22.930 -14.833 -15.142  1.00 22.92           C  
ANISOU 4654  CD  ARG B  72     2796   2189   3722     50    461   -385       C  
ATOM   4655  NE  ARG B  72     -21.534 -15.189 -15.294  1.00 32.37           N  
ANISOU 4655  NE  ARG B  72     3011   3961   5327   -434    425   -989       N  
ATOM   4656  CZ  ARG B  72     -20.818 -15.004 -16.383  1.00 38.74           C  
ANISOU 4656  CZ  ARG B  72     4366   5143   5208    -54    634  -1059       C  
ATOM   4657  NH1 ARG B  72     -21.308 -14.269 -17.370  1.00 45.58           N  
ANISOU 4657  NH1 ARG B  72     6894   3932   6490   -315  -1098  -1529       N  
ATOM   4658  NH2 ARG B  72     -19.606 -15.538 -16.469  1.00 39.47           N  
ANISOU 4658  NH2 ARG B  72     3978   5028   5990    305    316  -2907       N  
ATOM   4659  C   ARG B  72     -24.983 -11.210 -14.114  1.00 10.68           C  
ANISOU 4659  C   ARG B  72     1430   1421   1205   -178   -283     67       C  
ATOM   4660  O   ARG B  72     -25.788 -11.435 -15.023  1.00 12.09           O  
ANISOU 4660  O   ARG B  72     1848   1418   1325   -249   -491     75       O  
ATOM   4661  N   VAL B  73     -24.238 -10.098 -14.026  1.00 10.39           N  
ANISOU 4661  N   VAL B  73     1375   1449   1122   -147   -281     32       N  
ATOM   4662  CA  VAL B  73     -24.302  -9.067 -15.064  1.00 11.97           C  
ANISOU 4662  CA  VAL B  73     1552   1663   1331   -245   -267    260       C  
ATOM   4663  CB  VAL B  73     -24.649  -7.675 -14.520  1.00 15.65           C  
ANISOU 4663  CB  VAL B  73     1925   2068   1954    -17   -211   -121       C  
ATOM   4664  CG1 VAL B  73     -26.026  -7.667 -13.875  1.00 16.34           C  
ANISOU 4664  CG1 VAL B  73     2214   1669   2325   -259     74   -171       C  
ATOM   4665  CG2 VAL B  73     -23.574  -7.142 -13.603  1.00 17.04           C  
ANISOU 4665  CG2 VAL B  73     2439   2016   2017     15   -279   -311       C  
ATOM   4666  C   VAL B  73     -22.953  -9.045 -15.770  1.00 11.89           C  
ANISOU 4666  C   VAL B  73     1558   1552   1406    -78   -241    353       C  
ATOM   4667  O   VAL B  73     -21.896  -9.228 -15.139  1.00 13.35           O  
ANISOU 4667  O   VAL B  73     1599   2007   1466   -170   -332    546       O  
ATOM   4668  N   SER B  74     -23.007  -8.826 -17.075  1.00 12.00           N  
ANISOU 4668  N   SER B  74     1523   1644   1393   -103   -233    346       N  
ATOM   4669  CA  SER B  74     -21.801  -8.625 -17.859  1.00 11.76           C  
ANISOU 4669  CA  SER B  74     1521   1547   1399   -189   -215    473       C  
ATOM   4670  CB  SER B  74     -21.371  -9.834 -18.604  1.00 14.32           C  
ANISOU 4670  CB  SER B  74     2122   1452   1867   -170   -157    595       C  
ATOM   4671  OG  SER B  74     -22.324 -10.220 -19.560  1.00 18.52           O  
ANISOU 4671  OG  SER B  74     2484   1980   2573    153   -427    -10       O  
ATOM   4672  C   SER B  74     -22.049  -7.442 -18.789  1.00 11.53           C  
ANISOU 4672  C   SER B  74     1598   1404   1378   -213   -122    417       C  
ATOM   4673  O   SER B  74     -23.173  -7.245 -19.263  1.00 14.41           O  
ANISOU 4673  O   SER B  74     1905   1776   1793   -313   -455    402       O  
ATOM   4674  N   PHE B  75     -20.979  -6.678 -19.045  1.00 11.30           N  
ANISOU 4674  N   PHE B  75     1569   1391   1331   -201   -167    334       N  
ATOM   4675  CA  PHE B  75     -21.085  -5.520 -19.899  1.00 11.69           C  
ANISOU 4675  CA  PHE B  75     1647   1501   1290    -42   -213    340       C  
ATOM   4676  CB  PHE B  75     -21.940  -4.434 -19.237  1.00 11.42           C  
ANISOU 4676  CB  PHE B  75     1569   1430   1337    -93    -90    277       C  
ATOM   4677  CG  PHE B  75     -21.412  -3.968 -17.902  1.00 12.23           C  
ANISOU 4677  CG  PHE B  75     1565   1565   1516      2   -241    184       C  
ATOM   4678  CD1 PHE B  75     -20.483  -2.950 -17.823  1.00 12.68           C  
ANISOU 4678  CD1 PHE B  75     1685   1627   1504    -76    -13    138       C  
ATOM   4679  CE1 PHE B  75     -19.967  -2.549 -16.603  1.00 14.04           C  
ANISOU 4679  CE1 PHE B  75     1854   1780   1700    -86   -160     42       C  
ATOM   4680  CZ  PHE B  75     -20.378  -3.142 -15.450  1.00 14.38           C  
ANISOU 4680  CZ  PHE B  75     2046   1703   1713   -174    -30    -52       C  
ATOM   4681  CD2 PHE B  75     -21.803  -4.585 -16.723  1.00 12.78           C  
ANISOU 4681  CD2 PHE B  75     1769   1595   1491   -249    -67     17       C  
ATOM   4682  CE2 PHE B  75     -21.289  -4.173 -15.498  1.00 12.83           C  
ANISOU 4682  CE2 PHE B  75     1871   1595   1407   -139     -1     33       C  
ATOM   4683  C   PHE B  75     -19.692  -4.989 -20.192  1.00 12.26           C  
ANISOU 4683  C   PHE B  75     1876   1439   1340   -192   -189    262       C  
ATOM   4684  O   PHE B  75     -18.730  -5.362 -19.557  1.00 13.02           O  
ANISOU 4684  O   PHE B  75     1870   1562   1513   -230   -212    455       O  
ATOM   4685  N   THR B  76     -19.642  -4.088 -21.165  1.00 11.95           N  
ANISOU 4685  N   THR B  76     1863   1326   1350   -177   -218    260       N  
ATOM   4686  CA  THR B  76     -18.472  -3.313 -21.487  1.00 12.55           C  
ANISOU 4686  CA  THR B  76     1760   1480   1527   -155   -177    266       C  
ATOM   4687  CB  THR B  76     -18.082  -3.478 -22.960  1.00 13.02           C  
ANISOU 4687  CB  THR B  76     2026   1405   1513     86   -240    319       C  
ATOM   4688  OG1 THR B  76     -17.856  -4.865 -23.237  1.00 14.89           O  
ANISOU 4688  OG1 THR B  76     2303   1496   1858    105    -33    105       O  
ATOM   4689  CG2 THR B  76     -16.879  -2.640 -23.325  1.00 15.08           C  
ANISOU 4689  CG2 THR B  76     2350   1803   1576    -95    -95    232       C  
ATOM   4690  C   THR B  76     -18.765  -1.857 -21.130  1.00 11.46           C  
ANISOU 4690  C   THR B  76     1549   1556   1249     23   -108    382       C  
ATOM   4691  O   THR B  76     -19.809  -1.316 -21.513  1.00 12.69           O  
ANISOU 4691  O   THR B  76     1727   1441   1652     61   -411    358       O  
ATOM   4692  N   ALA B  77     -17.830  -1.211 -20.412  1.00 12.30           N  
ANISOU 4692  N   ALA B  77     1829   1401   1441     57   -231    330       N  
ATOM   4693  CA  ALA B  77     -17.871   0.216 -20.166  1.00 12.64           C  
ANISOU 4693  CA  ALA B  77     1849   1416   1535     35   -197    264       C  
ATOM   4694  CB  ALA B  77     -17.692   0.486 -18.709  1.00 13.38           C  
ANISOU 4694  CB  ALA B  77     1744   1854   1485    -39   -290    182       C  
ATOM   4695  C   ALA B  77     -16.774   0.890 -20.970  1.00 12.67           C  
ANISOU 4695  C   ALA B  77     1956   1171   1685    -83   -185    198       C  
ATOM   4696  O   ALA B  77     -15.635   0.473 -20.913  1.00 13.74           O  
ANISOU 4696  O   ALA B  77     2077   1572   1571     57     77    369       O  
ATOM   4697  N   GLU B  78     -17.150   1.931 -21.709  1.00 12.28           N  
ANISOU 4697  N   GLU B  78     1750   1377   1540   -195   -198    365       N  
ATOM   4698  CA  GLU B  78     -16.192   2.793 -22.406  1.00 13.17           C  
ANISOU 4698  CA  GLU B  78     2079   1333   1589   -219   -134    402       C  
ATOM   4699  CB  GLU B  78     -16.599   3.013 -23.863  1.00 14.46           C  
ANISOU 4699  CB  GLU B  78     2346   1519   1629   -431   -335    425       C  
ATOM   4700  CG  GLU B  78     -15.597   3.887 -24.604  1.00 17.09           C  
ANISOU 4700  CG  GLU B  78     2730   1854   1908   -568   -108    572       C  
ATOM   4701  CD  GLU B  78     -15.833   4.104 -26.074  1.00 20.40           C  
ANISOU 4701  CD  GLU B  78     3165   2599   1985  -1037   -118    842       C  
ATOM   4702  OE1 GLU B  78     -16.886   3.725 -26.558  1.00 25.70           O  
ANISOU 4702  OE1 GLU B  78     3707   3808   2249  -1516   -548    888       O  
ATOM   4703  OE2 GLU B  78     -14.957   4.687 -26.729  1.00 27.64           O  
ANISOU 4703  OE2 GLU B  78     3942   4054   2504  -1256    622    961       O  
ATOM   4704  C   GLU B  78     -16.135   4.117 -21.650  1.00 13.43           C  
ANISOU 4704  C   GLU B  78     1897   1555   1649   -303   -185    249       C  
ATOM   4705  O   GLU B  78     -17.169   4.775 -21.528  1.00 13.84           O  
ANISOU 4705  O   GLU B  78     1838   1506   1914   -216   -256    302       O  
ATOM   4706  N   ILE B  79     -14.944   4.446 -21.145  1.00 12.67           N  
ANISOU 4706  N   ILE B  79     1792   1464   1557   -203   -138    250       N  
ATOM   4707  CA  ILE B  79     -14.682   5.656 -20.404  1.00 12.82           C  
ANISOU 4707  CA  ILE B  79     1863   1419   1587   -242    -83    315       C  
ATOM   4708  CB  ILE B  79     -13.879   5.369 -19.132  1.00 13.58           C  
ANISOU 4708  CB  ILE B  79     1908   1665   1586   -220    -91    335       C  
ATOM   4709  CG1 ILE B  79     -14.557   4.312 -18.249  1.00 14.56           C  
ANISOU 4709  CG1 ILE B  79     2049   1968   1515   -149      4    480       C  
ATOM   4710  CG2 ILE B  79     -13.607   6.657 -18.376  1.00 15.74           C  
ANISOU 4710  CG2 ILE B  79     2368   1913   1698    -40   -137    145       C  
ATOM   4711  CD1 ILE B  79     -13.694   3.829 -17.134  1.00 17.79           C  
ANISOU 4711  CD1 ILE B  79     2429   2555   1773     -3   -159    558       C  
ATOM   4712  C   ILE B  79     -13.925   6.617 -21.319  1.00 13.72           C  
ANISOU 4712  C   ILE B  79     1984   1605   1622   -332   -180    463       C  
ATOM   4713  O   ILE B  79     -12.847   6.255 -21.827  1.00 14.60           O  
ANISOU 4713  O   ILE B  79     2105   1790   1652   -406    -45    445       O  
ATOM   4714  N   LYS B  80     -14.530   7.793 -21.537  1.00 14.06           N  
ANISOU 4714  N   LYS B  80     2098   1562   1680   -209     56    313       N  
ATOM   4715  CA  LYS B  80     -13.976   8.811 -22.423  1.00 15.55           C  
ANISOU 4715  CA  LYS B  80     2714   1473   1721   -277   -236    485       C  
ATOM   4716  CB  LYS B  80     -14.989   9.187 -23.511  1.00 18.53           C  
ANISOU 4716  CB  LYS B  80     3157   1807   2074   -249   -549    706       C  
ATOM   4717  CG  LYS B  80     -15.502   8.040 -24.363  1.00 21.31           C  
ANISOU 4717  CG  LYS B  80     3696   2043   2357   -261   -672    543       C  
ATOM   4718  CD  LYS B  80     -16.623   8.476 -25.263  1.00 26.75           C  
ANISOU 4718  CD  LYS B  80     4004   3019   3139   -167  -1106    680       C  
ATOM   4719  CE  LYS B  80     -17.401   7.331 -25.861  1.00 30.23           C  
ANISOU 4719  CE  LYS B  80     4477   3360   3646   -322  -1414   1049       C  
ATOM   4720  NZ  LYS B  80     -18.653   7.834 -26.479  1.00 36.55           N  
ANISOU 4720  NZ  LYS B  80     4196   4696   4994   -194  -1547   1193       N  
ATOM   4721  C   LYS B  80     -13.590  10.071 -21.643  1.00 15.47           C  
ANISOU 4721  C   LYS B  80     2732   1426   1718   -163   -185    484       C  
ATOM   4722  O   LYS B  80     -14.027  10.278 -20.508  1.00 16.48           O  
ANISOU 4722  O   LYS B  80     2719   1735   1807   -287     77    249       O  
ATOM   4723  N   ASN B  81     -12.767  10.895 -22.295  1.00 15.99           N  
ANISOU 4723  N   ASN B  81     2774   1410   1889   -172   -156    535       N  
ATOM   4724  CA  ASN B  81     -12.298  12.216 -21.808  1.00 17.43           C  
ANISOU 4724  CA  ASN B  81     2870   1351   2400   -312   -256    553       C  
ATOM   4725  CB  ASN B  81     -13.393  13.042 -21.127  1.00 18.41           C  
ANISOU 4725  CB  ASN B  81     2942   1582   2468   -129   -323    609       C  
ATOM   4726  CG  ASN B  81     -14.595  13.317 -22.006  1.00 18.79           C  
ANISOU 4726  CG  ASN B  81     2846   1651   2642    170   -226    699       C  
ATOM   4727  OD1 ASN B  81     -14.500  13.246 -23.225  1.00 21.15           O  
ANISOU 4727  OD1 ASN B  81     3468   1896   2669     56   -306    562       O  
ATOM   4728  ND2 ASN B  81     -15.732  13.625 -21.387  1.00 18.99           N  
ANISOU 4728  ND2 ASN B  81     2932   1616   2668    357   -223    400       N  
ATOM   4729  C   ASN B  81     -11.107  12.071 -20.843  1.00 17.16           C  
ANISOU 4729  C   ASN B  81     2962   1442   2115   -302   -145    582       C  
ATOM   4730  O   ASN B  81     -10.840  12.987 -20.056  1.00 19.00           O  
ANISOU 4730  O   ASN B  81     3294   1460   2464   -401   -185    427       O  
ATOM   4731  N   ILE B  82     -10.362  10.966 -20.951  1.00 16.08           N  
ANISOU 4731  N   ILE B  82     2853   1371   1886   -374   -145    395       N  
ATOM   4732  CA  ILE B  82      -9.163  10.714 -20.162  1.00 16.12           C  
ANISOU 4732  CA  ILE B  82     2752   1626   1744   -466    -54    532       C  
ATOM   4733  CB  ILE B  82      -8.923   9.193 -20.015  1.00 15.73           C  
ANISOU 4733  CB  ILE B  82     2588   1566   1819   -621    -87    636       C  
ATOM   4734  CG1 ILE B  82     -10.142   8.476 -19.424  1.00 16.43           C  
ANISOU 4734  CG1 ILE B  82     2581   1537   2124   -547   -115    942       C  
ATOM   4735  CG2 ILE B  82      -7.662   8.928 -19.208  1.00 16.20           C  
ANISOU 4735  CG2 ILE B  82     2525   1610   2017   -466     22    418       C  
ATOM   4736  CD1 ILE B  82     -10.030   6.962 -19.505  1.00 17.37           C  
ANISOU 4736  CD1 ILE B  82     2595   1658   2345   -291    -68    724       C  
ATOM   4737  C   ILE B  82      -7.964  11.380 -20.834  1.00 17.53           C  
ANISOU 4737  C   ILE B  82     2920   1846   1894   -592    -36    639       C  
ATOM   4738  O   ILE B  82      -7.700  11.154 -22.010  1.00 18.63           O  
ANISOU 4738  O   ILE B  82     3073   2142   1862   -881    -66    645       O  
ATOM   4739  N   LEU B  83      -7.223  12.192 -20.076  1.00 18.71           N  
ANISOU 4739  N   LEU B  83     3113   2325   1670   -861     30    707       N  
ATOM   4740  CA  LEU B  83      -6.046  12.860 -20.622  1.00 19.08           C  
ANISOU 4740  CA  LEU B  83     3160   2309   1780   -833    219    698       C  
ATOM   4741  CB  LEU B  83      -5.272  13.569 -19.512  1.00 20.56           C  
ANISOU 4741  CB  LEU B  83     3217   2511   2084   -888    187    535       C  
ATOM   4742  CG  LEU B  83      -4.069  14.395 -19.971  1.00 23.73           C  
ANISOU 4742  CG  LEU B  83     3781   3068   2165  -1309    253    656       C  
ATOM   4743  CD1 LEU B  83      -4.498  15.593 -20.799  1.00 24.50           C  
ANISOU 4743  CD1 LEU B  83     4101   2678   2530  -1286    455    626       C  
ATOM   4744  CD2 LEU B  83      -3.253  14.851 -18.780  1.00 23.82           C  
ANISOU 4744  CD2 LEU B  83     3865   2691   2495  -1324    -46    599       C  
ATOM   4745  C   LEU B  83      -5.159  11.823 -21.322  1.00 18.51           C  
ANISOU 4745  C   LEU B  83     2940   2423   1668   -860    195    636       C  
ATOM   4746  O   LEU B  83      -4.903  10.767 -20.770  1.00 18.26           O  
ANISOU 4746  O   LEU B  83     2742   2305   1888   -832    305    630       O  
ATOM   4747  N   ALA B  84      -4.655  12.155 -22.514  1.00 19.73           N  
ANISOU 4747  N   ALA B  84     3144   2600   1751   -883    397    622       N  
ATOM   4748  CA  ALA B  84      -3.786  11.246 -23.235  1.00 22.28           C  
ANISOU 4748  CA  ALA B  84     3350   2931   2182   -626    650    799       C  
ATOM   4749  CB  ALA B  84      -3.361  11.861 -24.545  1.00 23.43           C  
ANISOU 4749  CB  ALA B  84     3624   3426   1852   -623    715    548       C  
ATOM   4750  C   ALA B  84      -2.577  10.882 -22.362  1.00 23.39           C  
ANISOU 4750  C   ALA B  84     3387   3398   2101   -531    718    889       C  
ATOM   4751  O   ALA B  84      -2.119  11.692 -21.546  1.00 22.81           O  
ANISOU 4751  O   ALA B  84     2766   3169   2730   -400    496    943       O  
ATOM   4752  N   ASP B  85      -2.092   9.645 -22.525  1.00 24.94           N  
ANISOU 4752  N   ASP B  85     3432   3780   2263   -263    909    615       N  
ATOM   4753  CA  ASP B  85      -0.878   9.120 -21.854  1.00 27.29           C  
ANISOU 4753  CA  ASP B  85     3174   4345   2848   -452    965    803       C  
ATOM   4754  CB  ASP B  85       0.345  10.021 -22.083  1.00 32.13           C  
ANISOU 4754  CB  ASP B  85     3441   4783   3984   -861    678    945       C  
ATOM   4755  CG  ASP B  85       0.649  10.262 -23.555  1.00 40.15           C  
ANISOU 4755  CG  ASP B  85     4733   6181   4338  -1078   1262    387       C  
ATOM   4756  OD1 ASP B  85       0.466   9.315 -24.356  1.00 48.17           O  
ANISOU 4756  OD1 ASP B  85     5618   6371   6313   -799   1377   -575       O  
ATOM   4757  OD2 ASP B  85       1.043  11.405 -23.898  1.00 55.62           O  
ANISOU 4757  OD2 ASP B  85     7510   6590   7033  -1866   1343    387       O  
ATOM   4758  C   ASP B  85      -1.147   8.877 -20.369  1.00 24.36           C  
ANISOU 4758  C   ASP B  85     2737   3843   2676   -159    359    986       C  
ATOM   4759  O   ASP B  85      -0.218   8.846 -19.583  1.00 28.29           O  
ANISOU 4759  O   ASP B  85     2576   5084   3089   -458    285    827       O  
ATOM   4760  N   SER B  86      -2.424   8.705 -19.991  1.00 20.74           N  
ANISOU 4760  N   SER B  86     2708   3001   2170   -306    254    720       N  
ATOM   4761  CA  SER B  86      -2.755   8.383 -18.593  1.00 18.62           C  
ANISOU 4761  CA  SER B  86     2481   2564   2027    -63    119    685       C  
ATOM   4762  CB  SER B  86      -4.189   8.701 -18.266  1.00 17.88           C  
ANISOU 4762  CB  SER B  86     2487   2402   1903    -22    127    629       C  
ATOM   4763  OG  SER B  86      -4.405  10.100 -18.249  1.00 19.49           O  
ANISOU 4763  OG  SER B  86     2950   2213   2241   -324    179    700       O  
ATOM   4764  C   SER B  86      -2.492   6.895 -18.338  1.00 18.51           C  
ANISOU 4764  C   SER B  86     2453   2580   1998    -33    182    822       C  
ATOM   4765  O   SER B  86      -3.005   6.038 -19.058  1.00 20.56           O  
ANISOU 4765  O   SER B  86     3121   2571   2120    155   -109    692       O  
ATOM   4766  N   SER B  87      -1.741   6.583 -17.278  1.00 19.64           N  
ANISOU 4766  N   SER B  87     2534   2930   1998    -74    187    652       N  
ATOM   4767  CA  SER B  87      -1.493   5.182 -16.931  1.00 18.38           C  
ANISOU 4767  CA  SER B  87     2177   2831   1973    118    394    679       C  
ATOM   4768  CB  SER B  87      -0.401   5.061 -15.907  1.00 21.25           C  
ANISOU 4768  CB  SER B  87     2373   3091   2610   -239    -18    804       C  
ATOM   4769  OG  SER B  87      -0.892   5.262 -14.592  1.00 24.20           O  
ANISOU 4769  OG  SER B  87     2541   4020   2630   -295     98   1030       O  
ATOM   4770  C   SER B  87      -2.776   4.466 -16.471  1.00 17.57           C  
ANISOU 4770  C   SER B  87     2211   2700   1764     52    312    445       C  
ATOM   4771  O   SER B  87      -2.960   3.271 -16.719  1.00 18.97           O  
ANISOU 4771  O   SER B  87     2673   2710   1825    103    406    525       O  
ATOM   4772  N   LEU B  88      -3.632   5.200 -15.765  1.00 16.94           N  
ANISOU 4772  N   LEU B  88     2284   2434   1715     82    267    415       N  
ATOM   4773  CA  LEU B  88      -4.858   4.693 -15.089  1.00 15.34           C  
ANISOU 4773  CA  LEU B  88     2323   1968   1535     21    200    354       C  
ATOM   4774  CB  LEU B  88      -5.813   4.104 -16.133  1.00 14.54           C  
ANISOU 4774  CB  LEU B  88     2086   1868   1570     72    144    335       C  
ATOM   4775  CG  LEU B  88      -6.339   5.102 -17.158  1.00 16.59           C  
ANISOU 4775  CG  LEU B  88     2634   1986   1681     26    -32    416       C  
ATOM   4776  CD1 LEU B  88      -7.270   4.406 -18.138  1.00 18.21           C  
ANISOU 4776  CD1 LEU B  88     3251   1896   1770   -123    -83    211       C  
ATOM   4777  CD2 LEU B  88      -7.070   6.264 -16.483  1.00 17.09           C  
ANISOU 4777  CD2 LEU B  88     2686   1865   1943     39    -28    540       C  
ATOM   4778  C   LEU B  88      -4.548   3.664 -13.987  1.00 15.98           C  
ANISOU 4778  C   LEU B  88     2355   2218   1496    162    221    408       C  
ATOM   4779  O   LEU B  88      -5.468   3.035 -13.484  1.00 15.56           O  
ANISOU 4779  O   LEU B  88     2414   1976   1522     81    163    366       O  
ATOM   4780  N   LYS B  89      -3.289   3.538 -13.571  1.00 16.77           N  
ANISOU 4780  N   LYS B  89     2290   2247   1833    158    449    564       N  
ATOM   4781  CA ALYS B  89      -2.944   2.514 -12.599  0.50 16.64           C  
ANISOU 4781  CA ALYS B  89     2254   2260   1805    257    458    533       C  
ATOM   4782  CA BLYS B  89      -2.878   2.562 -12.558  0.50 16.66           C  
ANISOU 4782  CA BLYS B  89     2183   2355   1792    211    432    554       C  
ATOM   4783  CB ALYS B  89      -1.436   2.431 -12.365  0.50 18.95           C  
ANISOU 4783  CB ALYS B  89     2313   2657   2229    253    436    508       C  
ATOM   4784  CB BLYS B  89      -1.389   2.752 -12.245  0.50 19.54           C  
ANISOU 4784  CB BLYS B  89     2236   2914   2271     99    448    475       C  
ATOM   4785  CG ALYS B  89      -1.006   1.338 -11.390  0.50 20.21           C  
ANISOU 4785  CG ALYS B  89     2673   2423   2583    341    579    532       C  
ATOM   4786  CG BLYS B  89      -0.799   1.980 -11.068  0.50 20.37           C  
ANISOU 4786  CG BLYS B  89     2299   2952   2486    327    535    517       C  
ATOM   4787  CD ALYS B  89      -1.438  -0.077 -11.752  0.50 21.14           C  
ANISOU 4787  CD ALYS B  89     2708   2406   2918    224    469    603       C  
ATOM   4788  CD BLYS B  89       0.703   2.191 -10.908  0.50 21.99           C  
ANISOU 4788  CD BLYS B  89     2344   3149   2859    119    641    375       C  
ATOM   4789  CE ALYS B  89      -0.754  -1.132 -10.903  0.50 22.33           C  
ANISOU 4789  CE ALYS B  89     2973   1924   3585    420    389    298       C  
ATOM   4790  CE BLYS B  89       1.270   1.631  -9.620  0.50 22.91           C  
ANISOU 4790  CE BLYS B  89     2372   3546   2785    -19    651    387       C  
ATOM   4791  NZ ALYS B  89       0.643  -1.339 -11.357  0.50 21.70           N  
ANISOU 4791  NZ ALYS B  89     2769   1559   3913    459    275    155       N  
ATOM   4792  NZ BLYS B  89       0.726   0.290  -9.320  0.50 26.40           N  
ANISOU 4792  NZ BLYS B  89     2982   3560   3487    184    676    336       N  
ATOM   4793  C   LYS B  89      -3.689   2.761 -11.282  1.00 15.17           C  
ANISOU 4793  C   LYS B  89     2161   2048   1552     78    248    535       C  
ATOM   4794  O   LYS B  89      -3.607   3.829 -10.702  1.00 15.09           O  
ANISOU 4794  O   LYS B  89     1885   1999   1847   -165     15    544       O  
ATOM   4795  N   ASP B  90      -4.403   1.717 -10.828  1.00 13.28           N  
ANISOU 4795  N   ASP B  90     1841   1799   1405    100    132    344       N  
ATOM   4796  CA  ASP B  90      -5.096   1.733  -9.546  1.00 11.56           C  
ANISOU 4796  CA  ASP B  90     1682   1380   1329    108     43    300       C  
ATOM   4797  CB  ASP B  90      -4.089   1.805  -8.396  1.00 11.93           C  
ANISOU 4797  CB  ASP B  90     1441   1675   1416     -2    145    287       C  
ATOM   4798  CG  ASP B  90      -3.179   0.598  -8.303  1.00 13.01           C  
ANISOU 4798  CG  ASP B  90     1710   1718   1512     84    122     67       C  
ATOM   4799  OD1 ASP B  90      -3.622  -0.506  -8.660  1.00 13.80           O  
ANISOU 4799  OD1 ASP B  90     1811   1638   1792    -14    196     28       O  
ATOM   4800  OD2 ASP B  90      -2.002   0.775  -7.847  1.00 18.21           O  
ANISOU 4800  OD2 ASP B  90     1810   2190   2918     81   -236     98       O  
ATOM   4801  C   ASP B  90      -6.148   2.849  -9.483  1.00 11.37           C  
ANISOU 4801  C   ASP B  90     1753   1378   1187     64    126    288       C  
ATOM   4802  O   ASP B  90      -6.447   3.369  -8.392  1.00 12.18           O  
ANISOU 4802  O   ASP B  90     2068   1449   1108     28    183    257       O  
ATOM   4803  N   GLN B  91      -6.796   3.142 -10.619  1.00 11.28           N  
ANISOU 4803  N   GLN B  91     1773   1377   1136    -77     27    207       N  
ATOM   4804  CA  GLN B  91      -7.720   4.274 -10.655  1.00 11.70           C  
ANISOU 4804  CA  GLN B  91     1770   1340   1333    -79     -2    134       C  
ATOM   4805  CB  GLN B  91      -7.150   5.399 -11.520  1.00 11.72           C  
ANISOU 4805  CB  GLN B  91     1726   1273   1452    -91     64    148       C  
ATOM   4806  CG  GLN B  91      -6.003   6.121 -10.834  1.00 12.19           C  
ANISOU 4806  CG  GLN B  91     1735   1435   1462   -164    122    220       C  
ATOM   4807  CD  GLN B  91      -5.317   7.146 -11.688  1.00 12.91           C  
ANISOU 4807  CD  GLN B  91     1718   1496   1688   -310    223    139       C  
ATOM   4808  OE1 GLN B  91      -4.967   6.865 -12.837  1.00 15.16           O  
ANISOU 4808  OE1 GLN B  91     2132   1987   1639   -377    249    113       O  
ATOM   4809  NE2 GLN B  91      -5.047   8.305 -11.106  1.00 13.83           N  
ANISOU 4809  NE2 GLN B  91     1922   1553   1779   -390    -22    135       N  
ATOM   4810  C   GLN B  91      -9.142   3.933 -11.134  1.00 11.58           C  
ANISOU 4810  C   GLN B  91     1808   1268   1322    -99   -122    115       C  
ATOM   4811  O   GLN B  91     -10.033   4.773 -11.000  1.00 12.87           O  
ANISOU 4811  O   GLN B  91     1866   1377   1647   -130    -99    114       O  
ATOM   4812  N   ILE B  92      -9.381   2.733 -11.661  1.00 11.35           N  
ANISOU 4812  N   ILE B  92     1756   1231   1325    -78   -141    199       N  
ATOM   4813  CA AILE B  92     -10.676   2.342 -12.221  0.70 12.05           C  
ANISOU 4813  CA AILE B  92     1829   1497   1252   -118   -169     92       C  
ATOM   4814  CA BILE B  92     -10.692   2.363 -12.199  0.30 11.68           C  
ANISOU 4814  CA BILE B  92     1771   1431   1236    -67   -121     80       C  
ATOM   4815  CB AILE B  92     -10.582   2.030 -13.729  0.70 13.99           C  
ANISOU 4815  CB AILE B  92     2170   1800   1343   -295    -53     50       C  
ATOM   4816  CB BILE B  92     -10.649   2.164 -13.728  0.30 12.49           C  
ANISOU 4816  CB BILE B  92     1950   1548   1245   -147    -55    142       C  
ATOM   4817  CG1AILE B  92      -9.912   3.155 -14.524  0.70 15.68           C  
ANISOU 4817  CG1AILE B  92     2179   2031   1748   -366    -34    222       C  
ATOM   4818  CG1BILE B  92     -10.224   3.465 -14.413  0.30 12.74           C  
ANISOU 4818  CG1BILE B  92     1962   1566   1310    -77    -29    210       C  
ATOM   4819  CG2AILE B  92     -11.976   1.702 -14.251  0.70 15.35           C  
ANISOU 4819  CG2AILE B  92     2339   1899   1593   -400   -120    -23       C  
ATOM   4820  CG2BILE B  92     -11.994   1.676 -14.246  0.30 13.09           C  
ANISOU 4820  CG2BILE B  92     2030   1589   1353   -194    -76     98       C  
ATOM   4821  CD1AILE B  92     -10.627   4.466 -14.479  0.70 16.60           C  
ANISOU 4821  CD1AILE B  92     2316   2164   1828   -232    -11    399       C  
ATOM   4822  CD1BILE B  92     -10.084   3.360 -15.897  0.30 13.40           C  
ANISOU 4822  CD1BILE B  92     2116   1699   1277    -96    -45    330       C  
ATOM   4823  C   ILE B  92     -11.200   1.119 -11.474  1.00 10.98           C  
ANISOU 4823  C   ILE B  92     1608   1402   1159    -49    -60    -21       C  
ATOM   4824  O   ILE B  92     -10.455   0.162 -11.233  1.00 12.03           O  
ANISOU 4824  O   ILE B  92     1531   1453   1588     19    -76     21       O  
ATOM   4825  N   GLY B  93     -12.486   1.142 -11.131  1.00 10.68           N  
ANISOU 4825  N   GLY B  93     1583   1221   1254   -124    -50     20       N  
ATOM   4826  CA  GLY B  93     -13.142  -0.038 -10.622  1.00 10.69           C  
ANISOU 4826  CA  GLY B  93     1621   1202   1236   -132   -143     50       C  
ATOM   4827  C   GLY B  93     -14.641   0.151 -10.602  1.00 10.48           C  
ANISOU 4827  C   GLY B  93     1633   1102   1247    -21    -75    165       C  
ATOM   4828  O   GLY B  93     -15.195   0.868 -11.461  1.00 11.33           O  
ANISOU 4828  O   GLY B  93     1764   1197   1342    112    -48    258       O  
ATOM   4829  N   LEU B  94     -15.305  -0.511  -9.655  1.00 10.34           N  
ANISOU 4829  N   LEU B  94     1643   1097   1189    -34   -110    124       N  
ATOM   4830  CA  LEU B  94     -16.743  -0.425  -9.519  1.00 10.63           C  
ANISOU 4830  CA  LEU B  94     1594   1306   1138   -143   -118     53       C  
ATOM   4831  CB  LEU B  94     -17.394  -1.804  -9.673  1.00 10.76           C  
ANISOU 4831  CB  LEU B  94     1690   1180   1215    -25   -170    129       C  
ATOM   4832  CG  LEU B  94     -17.132  -2.512 -11.015  1.00 10.70           C  
ANISOU 4832  CG  LEU B  94     1515   1263   1287    -68   -314    -53       C  
ATOM   4833  CD1 LEU B  94     -17.753  -3.897 -11.002  1.00 12.02           C  
ANISOU 4833  CD1 LEU B  94     1678   1375   1514   -138   -299    -26       C  
ATOM   4834  CD2 LEU B  94     -17.679  -1.707 -12.188  1.00 10.78           C  
ANISOU 4834  CD2 LEU B  94     1340   1315   1441   -157   -330     -8       C  
ATOM   4835  C   LEU B  94     -17.091   0.185  -8.158  1.00  9.91           C  
ANISOU 4835  C   LEU B  94     1465   1187   1110   -200   -208     39       C  
ATOM   4836  O   LEU B  94     -16.319   0.093  -7.174  1.00  9.92           O  
ANISOU 4836  O   LEU B  94     1486   1275   1008   -157   -206    -23       O  
ATOM   4837  N   LYS B  95     -18.255   0.828  -8.105  1.00 10.91           N  
ANISOU 4837  N   LYS B  95     1720   1310   1112    -15   -227     92       N  
ATOM   4838  CA  LYS B  95     -18.825   1.290  -6.860  1.00 10.18           C  
ANISOU 4838  CA  LYS B  95     1658   1173   1035   -113   -106    135       C  
ATOM   4839  CB  LYS B  95     -19.954   2.278  -7.127  1.00 10.55           C  
ANISOU 4839  CB  LYS B  95     1784   1184   1037    -47   -128     -3       C  
ATOM   4840  CG  LYS B  95     -19.480   3.562  -7.796  1.00 11.86           C  
ANISOU 4840  CG  LYS B  95     1744   1374   1386    -60     46    173       C  
ATOM   4841  CD  LYS B  95     -20.589   4.585  -7.955  1.00 12.31           C  
ANISOU 4841  CD  LYS B  95     1840   1385   1450     26   -102    292       C  
ATOM   4842  CE  LYS B  95     -20.095   5.906  -8.489  1.00 12.29           C  
ANISOU 4842  CE  LYS B  95     1701   1415   1552    -62    -74    251       C  
ATOM   4843  NZ  LYS B  95     -21.168   6.926  -8.526  1.00 12.73           N  
ANISOU 4843  NZ  LYS B  95     1997   1268   1572    -11    -91    131       N  
ATOM   4844  C   LYS B  95     -19.244   0.100  -5.996  1.00 10.58           C  
ANISOU 4844  C   LYS B  95     1642   1219   1156   -134    -13    149       C  
ATOM   4845  O   LYS B  95     -19.351  -1.018  -6.465  1.00 11.55           O  
ANISOU 4845  O   LYS B  95     1904   1302   1180   -239   -147    121       O  
ATOM   4846  N   SER B  96     -19.459   0.358  -4.701  1.00  9.90           N  
ANISOU 4846  N   SER B  96     1693    956   1109   -111   -140    137       N  
ATOM   4847  CA ASER B  96     -19.858  -0.711  -3.782  0.50 10.39           C  
ANISOU 4847  CA ASER B  96     1622   1104   1220   -175   -129    207       C  
ATOM   4848  CA BSER B  96     -19.860  -0.690  -3.764  0.50  9.82           C  
ANISOU 4848  CA BSER B  96     1559   1033   1139   -138   -146    169       C  
ATOM   4849  CB ASER B  96     -19.857  -0.208  -2.365  0.50 11.73           C  
ANISOU 4849  CB ASER B  96     1830   1472   1154   -189   -138    215       C  
ATOM   4850  CB BSER B  96     -19.897  -0.118  -2.350  0.50  9.37           C  
ANISOU 4850  CB BSER B  96     1394   1125   1040   -196   -224    210       C  
ATOM   4851  OG ASER B  96     -20.962   0.616  -2.106  0.50 14.13           O  
ANISOU 4851  OG ASER B  96     2073   1563   1730    -68    -80     31       O  
ATOM   4852  OG BSER B  96     -18.691   0.591  -1.983  0.50  8.54           O  
ANISOU 4852  OG BSER B  96     1413    829   1004   -167   -161     90       O  
ATOM   4853  C   SER B  96     -21.235  -1.259  -4.169  1.00  9.96           C  
ANISOU 4853  C   SER B  96     1487   1035   1260    -63   -108    235       C  
ATOM   4854  O   SER B  96     -22.156  -0.514  -4.440  1.00 11.73           O  
ANISOU 4854  O   SER B  96     1516   1240   1699     16   -237    249       O  
ATOM   4855  N   PHE B  97     -21.355  -2.591  -4.201  1.00 10.21           N  
ANISOU 4855  N   PHE B  97     1464    999   1415     75   -137     92       N  
ATOM   4856  CA  PHE B  97     -22.631  -3.288  -4.481  1.00  9.67           C  
ANISOU 4856  CA  PHE B  97     1443   1044   1187     -4   -119    148       C  
ATOM   4857  CB  PHE B  97     -23.607  -3.143  -3.309  1.00 10.55           C  
ANISOU 4857  CB  PHE B  97     1443   1231   1333     62    -93     23       C  
ATOM   4858  CG  PHE B  97     -22.948  -3.546  -2.010  1.00 10.63           C  
ANISOU 4858  CG  PHE B  97     1566   1212   1258      7    -67     46       C  
ATOM   4859  CD1 PHE B  97     -22.787  -4.873  -1.666  1.00 11.20           C  
ANISOU 4859  CD1 PHE B  97     1775   1169   1309   -101   -112    -63       C  
ATOM   4860  CE1 PHE B  97     -22.079  -5.240  -0.541  1.00 12.21           C  
ANISOU 4860  CE1 PHE B  97     1818   1319   1500    -56   -149     81       C  
ATOM   4861  CZ  PHE B  97     -21.530  -4.285   0.262  1.00 12.21           C  
ANISOU 4861  CZ  PHE B  97     1909   1412   1318    -34   -100    -29       C  
ATOM   4862  CD2 PHE B  97     -22.404  -2.586  -1.171  1.00 10.68           C  
ANISOU 4862  CD2 PHE B  97     1422   1265   1371    -19      5    -19       C  
ATOM   4863  CE2 PHE B  97     -21.688  -2.957  -0.047  1.00 11.44           C  
ANISOU 4863  CE2 PHE B  97     1566   1375   1403    -12   -102    -47       C  
ATOM   4864  C   PHE B  97     -23.228  -2.756  -5.790  1.00  9.75           C  
ANISOU 4864  C   PHE B  97     1415   1122   1166   -112   -158    152       C  
ATOM   4865  O   PHE B  97     -24.363  -2.272  -5.828  1.00 11.15           O  
ANISOU 4865  O   PHE B  97     1476   1477   1282   -114   -194    -50       O  
ATOM   4866  N   PRO B  98     -22.492  -2.852  -6.915  1.00  9.82           N  
ANISOU 4866  N   PRO B  98     1362   1187   1182      4   -154    225       N  
ATOM   4867  CA  PRO B  98     -22.914  -2.196  -8.149  1.00  9.72           C  
ANISOU 4867  CA  PRO B  98     1483   1141   1069     -3   -129    112       C  
ATOM   4868  CB  PRO B  98     -21.739  -2.385  -9.104  1.00 10.01           C  
ANISOU 4868  CB  PRO B  98     1359   1288   1155   -191    -76     98       C  
ATOM   4869  CG  PRO B  98     -21.063  -3.640  -8.573  1.00 10.69           C  
ANISOU 4869  CG  PRO B  98     1509   1236   1316   -143    -28     56       C  
ATOM   4870  CD  PRO B  98     -21.214  -3.564  -7.063  1.00 10.01           C  
ANISOU 4870  CD  PRO B  98     1471    979   1353    -81    -42    -14       C  
ATOM   4871  C   PRO B  98     -24.199  -2.763  -8.760  1.00 10.56           C  
ANISOU 4871  C   PRO B  98     1529   1332   1151    -65   -185    165       C  
ATOM   4872  O   PRO B  98     -24.911  -2.043  -9.433  1.00 11.24           O  
ANISOU 4872  O   PRO B  98     1588   1151   1529     57   -313     63       O  
ATOM   4873  N   VAL B  99     -24.522  -4.028  -8.474  1.00 10.14           N  
ANISOU 4873  N   VAL B  99     1431   1320   1101    -16   -192    219       N  
ATOM   4874  CA  VAL B  99     -25.748  -4.598  -9.000  1.00 10.41           C  
ANISOU 4874  CA  VAL B  99     1486   1234   1233      0   -101    119       C  
ATOM   4875  CB  VAL B  99     -25.709  -6.132  -8.991  1.00 10.46           C  
ANISOU 4875  CB  VAL B  99     1600   1193   1178     -1    -12    125       C  
ATOM   4876  CG1 VAL B  99     -27.083  -6.746  -9.265  1.00 12.41           C  
ANISOU 4876  CG1 VAL B  99     1816   1409   1489    -64   -216     -5       C  
ATOM   4877  CG2 VAL B  99     -24.674  -6.638  -9.963  1.00 11.76           C  
ANISOU 4877  CG2 VAL B  99     1640   1517   1308    -14     15     62       C  
ATOM   4878  C   VAL B  99     -26.951  -4.027  -8.234  1.00 10.62           C  
ANISOU 4878  C   VAL B  99     1334   1326   1374     18   -132    162       C  
ATOM   4879  O   VAL B  99     -27.890  -3.509  -8.851  1.00 10.55           O  
ANISOU 4879  O   VAL B  99     1540   1181   1285     37   -258    116       O  
ATOM   4880  N   ASN B 100     -26.931  -4.116  -6.898  1.00  9.86           N  
ANISOU 4880  N   ASN B 100     1297   1105   1341     27   -195    168       N  
ATOM   4881  CA  ASN B 100     -28.078  -3.601  -6.143  1.00 10.73           C  
ANISOU 4881  CA  ASN B 100     1348   1246   1480     86   -140    198       C  
ATOM   4882  CB  ASN B 100     -28.052  -4.111  -4.703  1.00 10.72           C  
ANISOU 4882  CB  ASN B 100     1396   1232   1444     19   -138    158       C  
ATOM   4883  CG  ASN B 100     -28.393  -5.583  -4.627  1.00 11.18           C  
ANISOU 4883  CG  ASN B 100     1504   1193   1550     54   -239    100       C  
ATOM   4884  OD1 ASN B 100     -29.577  -5.932  -4.693  1.00 11.59           O  
ANISOU 4884  OD1 ASN B 100     1581   1239   1582     10   -249    248       O  
ATOM   4885  ND2 ASN B 100     -27.383  -6.436  -4.495  1.00 11.05           N  
ANISOU 4885  ND2 ASN B 100     1690   1150   1356    101   -346    272       N  
ATOM   4886  C   ASN B 100     -28.189  -2.082  -6.274  1.00 10.65           C  
ANISOU 4886  C   ASN B 100     1366   1210   1470     26   -199    173       C  
ATOM   4887  O   ASN B 100     -29.314  -1.551  -6.236  1.00 10.87           O  
ANISOU 4887  O   ASN B 100     1432   1169   1526     22   -131     89       O  
ATOM   4888  N   ARG B 101     -27.059  -1.355  -6.385  1.00 10.58           N  
ANISOU 4888  N   ARG B 101     1351   1153   1514    109   -271    215       N  
ATOM   4889  CA AARG B 101     -27.110   0.112  -6.608  0.50 10.87           C  
ANISOU 4889  CA AARG B 101     1557   1148   1421     27   -215    146       C  
ATOM   4890  CA BARG B 101     -27.123   0.108  -6.605  0.50 11.47           C  
ANISOU 4890  CA BARG B 101     1683   1167   1508     67   -271    151       C  
ATOM   4891  CB AARG B 101     -25.707   0.711  -6.757  0.50 10.83           C  
ANISOU 4891  CB AARG B 101     1579   1125   1411    -29   -196    155       C  
ATOM   4892  CB BARG B 101     -25.728   0.711  -6.772  0.50 12.88           C  
ANISOU 4892  CB BARG B 101     1794   1273   1825    -50   -197    119       C  
ATOM   4893  CG AARG B 101     -24.965   1.027  -5.460  0.50 11.31           C  
ANISOU 4893  CG AARG B 101     1575   1340   1380    -43   -157    187       C  
ATOM   4894  CG BARG B 101     -24.975   1.001  -5.485  0.50 15.23           C  
ANISOU 4894  CG BARG B 101     2103   1759   1922    -25   -265     65       C  
ATOM   4895  CD AARG B 101     -23.633   1.771  -5.709  0.50 10.29           C  
ANISOU 4895  CD AARG B 101     1477   1184   1246    -36   -289    110       C  
ATOM   4896  CD BARG B 101     -23.697   1.735  -5.882  0.50 16.30           C  
ANISOU 4896  CD BARG B 101     2100   1816   2275   -136   -300    -69       C  
ATOM   4897  NE AARG B 101     -23.729   2.956  -6.560  0.50 10.06           N  
ANISOU 4897  NE AARG B 101     1467   1211   1144    -42   -108    127       N  
ATOM   4898  NE BARG B 101     -22.886   2.006  -4.729  0.50 18.60           N  
ANISOU 4898  NE BARG B 101     2565   2125   2376    -27   -454   -148       N  
ATOM   4899  CZ AARG B 101     -23.929   4.205  -6.138  0.50 11.33           C  
ANISOU 4899  CZ AARG B 101     1702   1273   1326     31   -188    144       C  
ATOM   4900  CZ BARG B 101     -22.913   3.134  -4.053  0.50 19.73           C  
ANISOU 4900  CZ BARG B 101     2911   2087   2496   -210   -576   -197       C  
ATOM   4901  NH1AARG B 101     -23.946   5.202  -7.014  0.50 12.34           N  
ANISOU 4901  NH1AARG B 101     1978   1152   1556     15   -283    177       N  
ATOM   4902  NH1BARG B 101     -22.295   3.188  -2.890  0.50 20.44           N  
ANISOU 4902  NH1BARG B 101     2762   2417   2587   -200   -624    202       N  
ATOM   4903  NH2AARG B 101     -24.136   4.457  -4.862  0.50 11.98           N  
ANISOU 4903  NH2AARG B 101     1822   1365   1363    131   -366    -91       N  
ATOM   4904  NH2BARG B 101     -23.555   4.191  -4.518  0.50 19.46           N  
ANISOU 4904  NH2BARG B 101     2510   1990   2893   -103   -512   -435       N  
ATOM   4905  C   ARG B 101     -27.901   0.458  -7.875  1.00 11.27           C  
ANISOU 4905  C   ARG B 101     1503   1344   1433     49   -192    111       C  
ATOM   4906  O   ARG B 101     -28.368   1.579  -8.003  1.00 12.05           O  
ANISOU 4906  O   ARG B 101     1749   1297   1531     18   -262     81       O  
ATOM   4907  N   SER B 102     -27.961  -0.486  -8.818  1.00 10.23           N  
ANISOU 4907  N   SER B 102     1501   1104   1280     -8   -279    257       N  
ATOM   4908  CA  SER B 102     -28.544  -0.271 -10.153  1.00 10.42           C  
ANISOU 4908  CA  SER B 102     1509   1214   1234    -20   -254    191       C  
ATOM   4909  CB  SER B 102     -27.762  -1.054 -11.179  1.00 10.81           C  
ANISOU 4909  CB  SER B 102     1587   1330   1188     63   -295    122       C  
ATOM   4910  OG  SER B 102     -26.445  -0.563 -11.317  1.00 12.20           O  
ANISOU 4910  OG  SER B 102     1679   1505   1449    -40   -209    243       O  
ATOM   4911  C   SER B 102     -30.025  -0.649 -10.230  1.00 10.57           C  
ANISOU 4911  C   SER B 102     1519   1174   1323    -61   -264    208       C  
ATOM   4912  O   SER B 102     -30.605  -0.639 -11.326  1.00 12.14           O  
ANISOU 4912  O   SER B 102     1591   1742   1277    126   -138    166       O  
ATOM   4913  N   ILE B 103     -30.648  -1.019  -9.098  1.00 11.35           N  
ANISOU 4913  N   ILE B 103     1619   1453   1240   -188   -298    231       N  
ATOM   4914  CA  ILE B 103     -32.028  -1.530  -9.119  1.00 10.94           C  
ANISOU 4914  CA  ILE B 103     1637   1197   1321    -71   -170    126       C  
ATOM   4915  CB  ILE B 103     -32.112  -3.029  -8.814  1.00 11.12           C  
ANISOU 4915  CB  ILE B 103     1695   1277   1251   -142   -108    231       C  
ATOM   4916  CG1 ILE B 103     -31.213  -3.864  -9.732  1.00 11.12           C  
ANISOU 4916  CG1 ILE B 103     1541   1268   1413   -254   -139     50       C  
ATOM   4917  CG2 ILE B 103     -33.579  -3.462  -8.894  1.00 11.52           C  
ANISOU 4917  CG2 ILE B 103     1719   1289   1366   -166   -205    176       C  
ATOM   4918  CD1 ILE B 103     -30.985  -5.287  -9.242  1.00 12.66           C  
ANISOU 4918  CD1 ILE B 103     1617   1449   1744   -162   -395     93       C  
ATOM   4919  C   ILE B 103     -32.865  -0.709  -8.141  1.00 11.37           C  
ANISOU 4919  C   ILE B 103     1616   1267   1437     20    -81    194       C  
ATOM   4920  O   ILE B 103     -32.894  -0.973  -6.946  1.00 12.62           O  
ANISOU 4920  O   ILE B 103     1904   1464   1426     77   -121    182       O  
ATOM   4921  N   PRO B 104     -33.552   0.352  -8.607  1.00 11.63           N  
ANISOU 4921  N   PRO B 104     1539   1344   1535    105    -91    172       N  
ATOM   4922  CA  PRO B 104     -34.315   1.160  -7.661  1.00 12.57           C  
ANISOU 4922  CA  PRO B 104     1658   1438   1677     98    -52     57       C  
ATOM   4923  CB  PRO B 104     -34.827   2.325  -8.519  1.00 14.72           C  
ANISOU 4923  CB  PRO B 104     2214   1305   2074     82    190    321       C  
ATOM   4924  CG  PRO B 104     -34.005   2.334  -9.763  1.00 14.33           C  
ANISOU 4924  CG  PRO B 104     2319   1558   1567    248    -94    213       C  
ATOM   4925  CD  PRO B 104     -33.403   0.981  -9.932  1.00 11.85           C  
ANISOU 4925  CD  PRO B 104     1493   1506   1500    149   -132    155       C  
ATOM   4926  C   PRO B 104     -35.526   0.445  -7.041  1.00 12.48           C  
ANISOU 4926  C   PRO B 104     1762   1220   1757     82   -118    105       C  
ATOM   4927  O   PRO B 104     -35.911   0.738  -5.936  1.00 13.04           O  
ANISOU 4927  O   PRO B 104     1833   1350   1772     37   -223      0       O  
ATOM   4928  N   VAL B 105     -36.135  -0.452  -7.813  1.00 12.09           N  
ANISOU 4928  N   VAL B 105     1684   1208   1701     20   -208    172       N  
ATOM   4929  CA AVAL B 105     -37.295  -1.188  -7.373  0.50 11.59           C  
ANISOU 4929  CA AVAL B 105     1398   1286   1719    168   -317    203       C  
ATOM   4930  CA BVAL B 105     -37.347  -1.162  -7.460  0.50 12.43           C  
ANISOU 4930  CA BVAL B 105     1557   1278   1887    135   -202    133       C  
ATOM   4931  CB AVAL B 105     -38.617  -0.440  -7.643  0.50 12.71           C  
ANISOU 4931  CB AVAL B 105     1426   1606   1797    144   -528    397       C  
ATOM   4932  CB BVAL B 105     -38.576  -0.485  -8.088  0.50 14.47           C  
ANISOU 4932  CB BVAL B 105     1810   1559   2127    216   -412    158       C  
ATOM   4933  CG1AVAL B 105     -38.832  -0.132  -9.115  0.50 13.28           C  
ANISOU 4933  CG1AVAL B 105     1633   1665   1747    204   -393    402       C  
ATOM   4934  CG1BVAL B 105     -39.866  -1.160  -7.651  0.50 15.19           C  
ANISOU 4934  CG1BVAL B 105     1908   1499   2361    255   -223    240       C  
ATOM   4935  CG2AVAL B 105     -39.784  -1.196  -7.048  0.50 12.35           C  
ANISOU 4935  CG2AVAL B 105     1096   1797   1797    252   -611    415       C  
ATOM   4936  CG2BVAL B 105     -38.617   1.005  -7.812  0.50 16.59           C  
ANISOU 4936  CG2BVAL B 105     2126   1607   2569    372   -386     93       C  
ATOM   4937  C   VAL B 105     -37.247  -2.587  -8.006  1.00 11.45           C  
ANISOU 4937  C   VAL B 105     1498   1256   1593     64   -364    223       C  
ATOM   4938  O   VAL B 105     -36.832  -2.764  -9.153  1.00 12.99           O  
ANISOU 4938  O   VAL B 105     2021   1291   1624    103   -362    194       O  
ATOM   4939  N   ALA B 106     -37.640  -3.570  -7.185  1.00 11.56           N  
ANISOU 4939  N   ALA B 106     1580   1287   1525    -97   -120     78       N  
ATOM   4940  CA  ALA B 106     -37.778  -4.945  -7.594  1.00 11.46           C  
ANISOU 4940  CA  ALA B 106     1570   1319   1465    -65   -128     35       C  
ATOM   4941  CB  ALA B 106     -36.658  -5.783  -7.036  1.00 12.51           C  
ANISOU 4941  CB  ALA B 106     1412   1522   1818    -19   -132     -5       C  
ATOM   4942  C   ALA B 106     -39.123  -5.465  -7.099  1.00 12.08           C  
ANISOU 4942  C   ALA B 106     1520   1414   1656   -128   -324     32       C  
ATOM   4943  O   ALA B 106     -39.569  -5.150  -5.982  1.00 12.86           O  
ANISOU 4943  O   ALA B 106     1573   1592   1721   -200   -201     12       O  
ATOM   4944  N   VAL B 107     -39.730  -6.294  -7.934  1.00 11.91           N  
ANISOU 4944  N   VAL B 107     1599   1384   1540   -217   -335    118       N  
ATOM   4945  CA  VAL B 107     -40.930  -7.045  -7.546  1.00 13.02           C  
ANISOU 4945  CA  VAL B 107     1696   1473   1777   -222   -152    144       C  
ATOM   4946  CB  VAL B 107     -42.157  -6.635  -8.378  1.00 15.76           C  
ANISOU 4946  CB  VAL B 107     1758   1968   2259   -171   -351    108       C  
ATOM   4947  CG1 VAL B 107     -43.378  -7.415  -7.917  1.00 16.85           C  
ANISOU 4947  CG1 VAL B 107     1358   2690   2354   -159   -350    107       C  
ATOM   4948  CG2 VAL B 107     -42.424  -5.143  -8.277  1.00 17.54           C  
ANISOU 4948  CG2 VAL B 107     2183   2078   2402    232   -484    229       C  
ATOM   4949  C   VAL B 107     -40.626  -8.528  -7.713  1.00 12.59           C  
ANISOU 4949  C   VAL B 107     1668   1494   1621   -203    -66     -1       C  
ATOM   4950  O   VAL B 107     -40.244  -8.946  -8.789  1.00 15.12           O  
ANISOU 4950  O   VAL B 107     2541   1468   1733    -16    119    -30       O  
ATOM   4951  N   ILE B 108     -40.842  -9.288  -6.642  1.00 12.56           N  
ANISOU 4951  N   ILE B 108     1632   1426   1711   -141   -107     54       N  
ATOM   4952  CA  ILE B 108     -40.729 -10.730  -6.683  1.00 12.86           C  
ANISOU 4952  CA  ILE B 108     1631   1438   1815   -177    -10     58       C  
ATOM   4953  CB  ILE B 108     -39.713 -11.246  -5.644  1.00 12.89           C  
ANISOU 4953  CB  ILE B 108     1531   1499   1865    -63     84     71       C  
ATOM   4954  CG1 ILE B 108     -38.320 -10.686  -5.936  1.00 14.67           C  
ANISOU 4954  CG1 ILE B 108     1710   1719   2143   -140    240     32       C  
ATOM   4955  CG2 ILE B 108     -39.741 -12.783  -5.604  1.00 13.66           C  
ANISOU 4955  CG2 ILE B 108     1775   1546   1867   -131    -47    233       C  
ATOM   4956  CD1 ILE B 108     -37.248 -11.139  -5.005  1.00 15.05           C  
ANISOU 4956  CD1 ILE B 108     1732   1643   2342    101    291    -42       C  
ATOM   4957  C   ILE B 108     -42.131 -11.309  -6.454  1.00 13.30           C  
ANISOU 4957  C   ILE B 108     1623   1567   1861   -248   -148    115       C  
ATOM   4958  O   ILE B 108     -42.839 -10.912  -5.543  1.00 14.27           O  
ANISOU 4958  O   ILE B 108     1591   1874   1954   -281    -82     67       O  
ATOM   4959  N   ASN B 109     -42.513 -12.252  -7.318  1.00 12.87           N  
ANISOU 4959  N   ASN B 109     1485   1569   1833   -295   -178    155       N  
ATOM   4960  CA  ASN B 109     -43.771 -12.981  -7.244  1.00 13.35           C  
ANISOU 4960  CA  ASN B 109     1422   1524   2127   -204   -253     81       C  
ATOM   4961  CB  ASN B 109     -44.552 -12.825  -8.553  1.00 14.29           C  
ANISOU 4961  CB  ASN B 109     1566   1674   2186    -58   -352    111       C  
ATOM   4962  CG  ASN B 109     -45.902 -13.503  -8.574  1.00 13.73           C  
ANISOU 4962  CG  ASN B 109     1715   1464   2036   -218   -299    118       C  
ATOM   4963  OD1 ASN B 109     -46.102 -14.519  -7.914  1.00 15.55           O  
ANISOU 4963  OD1 ASN B 109     1862   1965   2081   -491   -290    440       O  
ATOM   4964  ND2 ASN B 109     -46.798 -12.964  -9.390  1.00 17.76           N  
ANISOU 4964  ND2 ASN B 109     1920   2283   2544    176   -430    205       N  
ATOM   4965  C   ASN B 109     -43.450 -14.438  -6.942  1.00 12.76           C  
ANISOU 4965  C   ASN B 109     1131   1608   2109    -80    -63    146       C  
ATOM   4966  O   ASN B 109     -42.775 -15.076  -7.743  1.00 13.17           O  
ANISOU 4966  O   ASN B 109     1692   1305   2005   -300    175     74       O  
ATOM   4967  N   MET B 110     -43.928 -14.930  -5.796  1.00 12.19           N  
ANISOU 4967  N   MET B 110     1334   1445   1853   -173    -98    -65       N  
ATOM   4968  CA  MET B 110     -43.889 -16.355  -5.479  1.00 12.41           C  
ANISOU 4968  CA  MET B 110     1301   1525   1886   -124   -145     -5       C  
ATOM   4969  CB  MET B 110     -43.092 -16.661  -4.210  1.00 12.66           C  
ANISOU 4969  CB  MET B 110     1479   1563   1767   -170   -144   -109       C  
ATOM   4970  CG  MET B 110     -41.605 -16.310  -4.345  1.00 13.06           C  
ANISOU 4970  CG  MET B 110     1449   1670   1843    -60   -199    150       C  
ATOM   4971  SD  MET B 110     -40.705 -16.721  -2.846  1.00 14.06           S  
ANISOU 4971  SD  MET B 110     1843   1736   1762   -295   -223     44       S  
ATOM   4972  CE  MET B 110     -39.029 -16.408  -3.407  1.00 14.90           C  
ANISOU 4972  CE  MET B 110     1573   2077   2009    -74   -421    222       C  
ATOM   4973  C   MET B 110     -45.331 -16.844  -5.329  1.00 12.13           C  
ANISOU 4973  C   MET B 110     1265   1476   1866   -176   -202     28       C  
ATOM   4974  O   MET B 110     -46.060 -16.396  -4.431  1.00 12.97           O  
ANISOU 4974  O   MET B 110     1302   1718   1909   -138   -134     32       O  
ATOM   4975  N   ASN B 111     -45.752 -17.735  -6.240  1.00 13.02           N  
ANISOU 4975  N   ASN B 111     1446   1618   1880   -250    -32    -33       N  
ATOM   4976  CA  ASN B 111     -47.077 -18.358  -6.166  1.00 13.69           C  
ANISOU 4976  CA  ASN B 111     1510   1711   1977   -288    -92    107       C  
ATOM   4977  CB  ASN B 111     -47.143 -19.449  -5.083  1.00 14.25           C  
ANISOU 4977  CB  ASN B 111     1784   1635   1994   -366      1    105       C  
ATOM   4978  CG  ASN B 111     -46.288 -20.646  -5.429  1.00 13.67           C  
ANISOU 4978  CG  ASN B 111     1649   1621   1921   -532     63     38       C  
ATOM   4979  OD1 ASN B 111     -45.805 -20.750  -6.573  1.00 14.32           O  
ANISOU 4979  OD1 ASN B 111     2062   1425   1952   -378    146    234       O  
ATOM   4980  ND2 ASN B 111     -46.073 -21.523  -4.439  1.00 13.18           N  
ANISOU 4980  ND2 ASN B 111     1631   1634   1740   -461     49   -103       N  
ATOM   4981  C   ASN B 111     -48.194 -17.309  -6.008  1.00 14.07           C  
ANISOU 4981  C   ASN B 111     1566   1668   2112   -252   -238    -52       C  
ATOM   4982  O   ASN B 111     -49.178 -17.542  -5.302  1.00 16.24           O  
ANISOU 4982  O   ASN B 111     1869   1908   2392   -202   -106     91       O  
ATOM   4983  N   GLY B 112     -48.063 -16.189  -6.719  1.00 13.19           N  
ANISOU 4983  N   GLY B 112     1235   1637   2137   -294   -356    -51       N  
ATOM   4984  CA  GLY B 112     -49.080 -15.154  -6.786  1.00 15.75           C  
ANISOU 4984  CA  GLY B 112     1499   2058   2426    -65   -407   -120       C  
ATOM   4985  C   GLY B 112     -48.960 -14.059  -5.743  1.00 15.19           C  
ANISOU 4985  C   GLY B 112     1489   1780   2500    -99   -415     16       C  
ATOM   4986  O   GLY B 112     -49.702 -13.101  -5.817  1.00 19.05           O  
ANISOU 4986  O   GLY B 112     1946   2194   3097    353   -537      4       O  
ATOM   4987  N   LYS B 113     -48.074 -14.224  -4.754  1.00 14.30           N  
ANISOU 4987  N   LYS B 113     1307   1859   2266   -256   -275    -84       N  
ATOM   4988  CA  LYS B 113     -47.824 -13.206  -3.754  1.00 14.84           C  
ANISOU 4988  CA  LYS B 113     1548   1921   2169   -187     -5    -87       C  
ATOM   4989  CB  LYS B 113     -47.435 -13.831  -2.412  1.00 15.83           C  
ANISOU 4989  CB  LYS B 113     1883   2157   1972   -251    128   -147       C  
ATOM   4990  CG  LYS B 113     -46.954 -12.827  -1.361  1.00 16.30           C  
ANISOU 4990  CG  LYS B 113     2106   1980   2105   -358    166   -156       C  
ATOM   4991  CD  LYS B 113     -48.000 -11.852  -0.920  1.00 21.07           C  
ANISOU 4991  CD  LYS B 113     2961   2482   2563    -77    542   -143       C  
ATOM   4992  CE  LYS B 113     -47.445 -10.926   0.145  1.00 22.98           C  
ANISOU 4992  CE  LYS B 113     3839   2410   2481     34    398   -183       C  
ATOM   4993  NZ  LYS B 113     -48.429  -9.887   0.520  1.00 29.68           N  
ANISOU 4993  NZ  LYS B 113     4641   3392   3241    411   1029   -648       N  
ATOM   4994  C   LYS B 113     -46.685 -12.322  -4.259  1.00 15.09           C  
ANISOU 4994  C   LYS B 113     1563   1999   2171   -254   -153      8       C  
ATOM   4995  O   LYS B 113     -45.609 -12.822  -4.554  1.00 14.42           O  
ANISOU 4995  O   LYS B 113     1613   1868   1997   -150   -213     73       O  
ATOM   4996  N   THR B 114     -46.940 -11.012  -4.324  1.00 15.17           N  
ANISOU 4996  N   THR B 114     1513   1921   2330   -244     18    -32       N  
ATOM   4997  CA  THR B 114     -45.901 -10.083  -4.740  1.00 14.57           C  
ANISOU 4997  CA  THR B 114     1630   1686   2217   -218   -120     48       C  
ATOM   4998  CB  THR B 114     -46.398  -9.046  -5.740  1.00 16.63           C  
ANISOU 4998  CB  THR B 114     1816   2056   2444      1   -320    168       C  
ATOM   4999  OG1 THR B 114     -47.373  -8.233  -5.093  1.00 18.72           O  
ANISOU 4999  OG1 THR B 114     1872   2153   3087    258   -247    292       O  
ATOM   5000  CG2 THR B 114     -47.007  -9.669  -6.969  1.00 16.69           C  
ANISOU 5000  CG2 THR B 114     1755   2046   2537   -151   -588    369       C  
ATOM   5001  C   THR B 114     -45.269  -9.392  -3.530  1.00 13.85           C  
ANISOU 5001  C   THR B 114     1481   1677   2103   -160   -113     36       C  
ATOM   5002  O   THR B 114     -45.926  -9.035  -2.537  1.00 17.05           O  
ANISOU 5002  O   THR B 114     1639   2187   2651   -294    278   -360       O  
ATOM   5003  N   PHE B 115     -43.969  -9.187  -3.658  1.00 13.23           N  
ANISOU 5003  N   PHE B 115     1465   1617   1944     56    -17     71       N  
ATOM   5004  CA  PHE B 115     -43.151  -8.474  -2.688  1.00 13.05           C  
ANISOU 5004  CA  PHE B 115     1573   1574   1808   -104      9     53       C  
ATOM   5005  CB  PHE B 115     -42.085  -9.401  -2.093  1.00 13.71           C  
ANISOU 5005  CB  PHE B 115     1762   1655   1792    -93    -96     76       C  
ATOM   5006  CG  PHE B 115     -42.580 -10.687  -1.492  1.00 14.82           C  
ANISOU 5006  CG  PHE B 115     2173   1576   1882   -188   -188      0       C  
ATOM   5007  CD1 PHE B 115     -42.747 -11.828  -2.264  1.00 14.37           C  
ANISOU 5007  CD1 PHE B 115     2082   1531   1846   -146   -285     64       C  
ATOM   5008  CE1 PHE B 115     -43.185 -13.015  -1.703  1.00 14.80           C  
ANISOU 5008  CE1 PHE B 115     2008   1739   1874   -111   -417    149       C  
ATOM   5009  CZ  PHE B 115     -43.426 -13.080  -0.369  1.00 16.90           C  
ANISOU 5009  CZ  PHE B 115     2412   1968   2040   -349   -175    344       C  
ATOM   5010  CD2 PHE B 115     -42.786 -10.793  -0.132  1.00 19.75           C  
ANISOU 5010  CD2 PHE B 115     3343   2069   2090   -428      2    -89       C  
ATOM   5011  CE2 PHE B 115     -43.202 -11.991   0.422  1.00 20.39           C  
ANISOU 5011  CE2 PHE B 115     3504   2205   2036   -407     59    119       C  
ATOM   5012  C   PHE B 115     -42.437  -7.348  -3.439  1.00 12.29           C  
ANISOU 5012  C   PHE B 115     1618   1380   1671    -11   -125     83       C  
ATOM   5013  O   PHE B 115     -41.670  -7.633  -4.375  1.00 13.37           O  
ANISOU 5013  O   PHE B 115     1952   1485   1643   -118     50    -26       O  
ATOM   5014  N   THR B 116     -42.717  -6.103  -3.054  1.00 12.63           N  
ANISOU 5014  N   THR B 116     1633   1423   1742    -98    102    -36       N  
ATOM   5015  CA  THR B 116     -42.102  -4.938  -3.681  1.00 12.58           C  
ANISOU 5015  CA  THR B 116     1408   1439   1933    -57    -23     53       C  
ATOM   5016  CB  THR B 116     -43.160  -3.901  -4.078  1.00 14.85           C  
ANISOU 5016  CB  THR B 116     1606   1620   2414     92    -55    144       C  
ATOM   5017  OG1 THR B 116     -44.090  -4.526  -4.973  1.00 17.53           O  
ANISOU 5017  OG1 THR B 116     1819   2066   2774    121   -121    -72       O  
ATOM   5018  CG2 THR B 116     -42.532  -2.692  -4.731  1.00 16.92           C  
ANISOU 5018  CG2 THR B 116     1962   1699   2767    -74   -178    232       C  
ATOM   5019  C   THR B 116     -41.076  -4.357  -2.714  1.00 13.49           C  
ANISOU 5019  C   THR B 116     1632   1495   1996   -183    -10      2       C  
ATOM   5020  O   THR B 116     -41.402  -4.077  -1.553  1.00 16.63           O  
ANISOU 5020  O   THR B 116     2075   2081   2159   -383     47   -333       O  
ATOM   5021  N   SER B 117     -39.843  -4.225  -3.194  1.00 12.45           N  
ANISOU 5021  N   SER B 117     1533   1452   1742   -164   -135    -62       N  
ATOM   5022  CA ASER B 117     -38.805  -3.652  -2.371  0.50 11.82           C  
ANISOU 5022  CA ASER B 117     1403   1363   1724    -32   -169      0       C  
ATOM   5023  CA BSER B 117     -38.678  -3.795  -2.414  0.50 12.87           C  
ANISOU 5023  CA BSER B 117     1562   1547   1780   -206   -145    -30       C  
ATOM   5024  CB ASER B 117     -38.077  -4.738  -1.625  0.50 11.29           C  
ANISOU 5024  CB ASER B 117     1300   1324   1662      1   -122    -15       C  
ATOM   5025  CB BSER B 117     -37.743  -4.940  -2.078  0.50 14.16           C  
ANISOU 5025  CB BSER B 117     1808   1713   1857    -27   -261   -115       C  
ATOM   5026  OG ASER B 117     -37.352  -5.539  -2.520  0.50 11.74           O  
ANISOU 5026  OG ASER B 117     1094   1373   1993    317   -132     50       O  
ATOM   5027  OG BSER B 117     -38.376  -5.985  -1.385  0.50 17.36           O  
ANISOU 5027  OG BSER B 117     2324   1924   2347   -113    -77    -69       O  
ATOM   5028  C   SER B 117     -37.887  -2.776  -3.228  1.00 11.57           C  
ANISOU 5028  C   SER B 117     1497   1217   1680    -86   -307     43       C  
ATOM   5029  O   SER B 117     -38.090  -2.655  -4.443  1.00 11.93           O  
ANISOU 5029  O   SER B 117     1654   1145   1732    149   -214     30       O  
ATOM   5030  N   TYR B 118     -36.903  -2.149  -2.565  1.00 11.49           N  
ANISOU 5030  N   TYR B 118     1397   1223   1742   -116   -209     29       N  
ATOM   5031  CA  TYR B 118     -36.120  -1.058  -3.151  1.00 11.16           C  
ANISOU 5031  CA  TYR B 118     1425   1279   1534    -67   -148    105       C  
ATOM   5032  CB  TYR B 118     -36.591   0.269  -2.548  1.00 12.03           C  
ANISOU 5032  CB  TYR B 118     1531   1384   1654    118   -103     92       C  
ATOM   5033  CG  TYR B 118     -38.072   0.467  -2.730  1.00 13.87           C  
ANISOU 5033  CG  TYR B 118     1612   1506   2150    312    -95    -51       C  
ATOM   5034  CD1 TYR B 118     -38.617   0.841  -3.942  1.00 15.27           C  
ANISOU 5034  CD1 TYR B 118     1714   1867   2217    300    -50     47       C  
ATOM   5035  CE1 TYR B 118     -39.986   0.964  -4.111  1.00 17.51           C  
ANISOU 5035  CE1 TYR B 118     1732   2215   2703    550   -132     27       C  
ATOM   5036  CZ  TYR B 118     -40.848   0.649  -3.072  1.00 18.98           C  
ANISOU 5036  CZ  TYR B 118     1774   2470   2965    348    -54   -125       C  
ATOM   5037  OH  TYR B 118     -42.208   0.737  -3.241  1.00 23.80           O  
ANISOU 5037  OH  TYR B 118     1882   2813   4348    440   -222   -301       O  
ATOM   5038  CE2 TYR B 118     -40.321   0.206  -1.878  1.00 18.65           C  
ANISOU 5038  CE2 TYR B 118     1781   2407   2896    161    256     84       C  
ATOM   5039  CD2 TYR B 118     -38.946   0.124  -1.720  1.00 17.01           C  
ANISOU 5039  CD2 TYR B 118     1845   1982   2637    257    126    237       C  
ATOM   5040  C   TYR B 118     -34.635  -1.353  -2.939  1.00 11.50           C  
ANISOU 5040  C   TYR B 118     1528   1215   1626     -9   -237    156       C  
ATOM   5041  O   TYR B 118     -34.019  -0.863  -1.972  1.00 12.44           O  
ANISOU 5041  O   TYR B 118     1826   1271   1629    -62   -292    104       O  
ATOM   5042  N   PRO B 119     -34.021  -2.192  -3.803  1.00 11.11           N  
ANISOU 5042  N   PRO B 119     1319   1383   1518   -168   -204    105       N  
ATOM   5043  CA  PRO B 119     -32.674  -2.679  -3.532  1.00 11.17           C  
ANISOU 5043  CA  PRO B 119     1512   1323   1406     83   -165    199       C  
ATOM   5044  CB  PRO B 119     -32.392  -3.558  -4.741  1.00 10.84           C  
ANISOU 5044  CB  PRO B 119     1425   1230   1463    191   -196    200       C  
ATOM   5045  CG  PRO B 119     -33.752  -4.093  -5.122  1.00 11.29           C  
ANISOU 5045  CG  PRO B 119     1473   1360   1456     89   -161    128       C  
ATOM   5046  CD  PRO B 119     -34.662  -2.895  -4.941  1.00 11.35           C  
ANISOU 5046  CD  PRO B 119     1537   1298   1476     62   -255     65       C  
ATOM   5047  C   PRO B 119     -31.625  -1.568  -3.350  1.00 11.41           C  
ANISOU 5047  C   PRO B 119     1496   1272   1565    164   -163     84       C  
ATOM   5048  O   PRO B 119     -30.798  -1.661  -2.459  1.00 11.94           O  
ANISOU 5048  O   PRO B 119     1574   1503   1458     33   -169     84       O  
ATOM   5049  N   ALA B 120     -31.654  -0.540  -4.216  1.00 10.68           N  
ANISOU 5049  N   ALA B 120     1214   1283   1560    233   -207    106       N  
ATOM   5050  CA  ALA B 120     -30.639   0.508  -4.101  1.00 12.08           C  
ANISOU 5050  CA  ALA B 120     1487   1371   1732     86   -246    -24       C  
ATOM   5051  CB  ALA B 120     -30.763   1.472  -5.243  1.00 13.22           C  
ANISOU 5051  CB  ALA B 120     1990   1162   1869    -23   -266     10       C  
ATOM   5052  C   ALA B 120     -30.727   1.222  -2.743  1.00 12.64           C  
ANISOU 5052  C   ALA B 120     1659   1424   1718    212   -246     22       C  
ATOM   5053  O   ALA B 120     -29.701   1.526  -2.124  1.00 14.72           O  
ANISOU 5053  O   ALA B 120     1789   2008   1792     53   -250   -215       O  
ATOM   5054  N   GLN B 121     -31.949   1.500  -2.307  1.00 13.14           N  
ANISOU 5054  N   GLN B 121     1628   1600   1764     44   -253   -199       N  
ATOM   5055  CA  GLN B 121     -32.185   2.164  -1.032  1.00 13.50           C  
ANISOU 5055  CA  GLN B 121     1687   1623   1818    196   -259   -322       C  
ATOM   5056  CB  GLN B 121     -33.666   2.540  -0.912  1.00 14.86           C  
ANISOU 5056  CB  GLN B 121     1766   1775   2104    303   -221   -316       C  
ATOM   5057  CG  GLN B 121     -34.059   3.204   0.390  1.00 16.00           C  
ANISOU 5057  CG  GLN B 121     2130   1987   1961    329   -124   -118       C  
ATOM   5058  CD  GLN B 121     -35.527   3.521   0.378  1.00 16.14           C  
ANISOU 5058  CD  GLN B 121     2106   1865   2159    355     40   -417       C  
ATOM   5059  OE1 GLN B 121     -36.364   2.633   0.533  1.00 17.88           O  
ANISOU 5059  OE1 GLN B 121     1798   2094   2901    234    -98   -248       O  
ATOM   5060  NE2 GLN B 121     -35.847   4.789   0.192  1.00 18.01           N  
ANISOU 5060  NE2 GLN B 121     2600   1955   2288    640    -88   -367       N  
ATOM   5061  C   GLN B 121     -31.734   1.243   0.112  1.00 13.74           C  
ANISOU 5061  C   GLN B 121     1470   1904   1846    246   -289   -234       C  
ATOM   5062  O   GLN B 121     -31.118   1.704   1.084  1.00 15.60           O  
ANISOU 5062  O   GLN B 121     1973   2147   1807    185   -226   -535       O  
ATOM   5063  N   LEU B 122     -32.092  -0.055   0.011  1.00 13.50           N  
ANISOU 5063  N   LEU B 122     1691   1850   1589    193   -245   -179       N  
ATOM   5064  CA ALEU B 122     -31.797  -1.057   1.052  0.50 14.90           C  
ANISOU 5064  CA ALEU B 122     1764   2266   1630    319   -145    -18       C  
ATOM   5065  CA BLEU B 122     -31.791  -1.011   1.065  0.50 14.45           C  
ANISOU 5065  CA BLEU B 122     1781   2101   1607    264   -115    -71       C  
ATOM   5066  CB ALEU B 122     -32.355  -2.439   0.681  0.50 16.47           C  
ANISOU 5066  CB ALEU B 122     1794   2442   2019    142   -151    115       C  
ATOM   5067  CB BLEU B 122     -32.458  -2.350   0.751  0.50 15.89           C  
ANISOU 5067  CB BLEU B 122     1959   2186   1891    101    -42     21       C  
ATOM   5068  CG ALEU B 122     -33.844  -2.746   0.871  0.50 17.32           C  
ANISOU 5068  CG ALEU B 122     1692   2760   2128    433    -94    152       C  
ATOM   5069  CG BLEU B 122     -32.929  -3.133   1.968  0.50 16.93           C  
ANISOU 5069  CG BLEU B 122     2373   2093   1964    268     76     29       C  
ATOM   5070  CD1ALEU B 122     -34.229  -4.058   0.182  0.50 19.09           C  
ANISOU 5070  CD1ALEU B 122     2079   2592   2582    450    231    286       C  
ATOM   5071  CD1BLEU B 122     -33.833  -4.282   1.579  0.50 16.36           C  
ANISOU 5071  CD1BLEU B 122     2268   1950   1998    333     24    160       C  
ATOM   5072  CD2ALEU B 122     -34.219  -2.834   2.338  0.50 18.66           C  
ANISOU 5072  CD2ALEU B 122     1998   3051   2038    254   -241     31       C  
ATOM   5073  CD2BLEU B 122     -31.750  -3.595   2.777  0.50 18.40           C  
ANISOU 5073  CD2BLEU B 122     2219   2418   2353     64    -22     75       C  
ATOM   5074  C   LEU B 122     -30.272  -1.157   1.213  1.00 13.87           C  
ANISOU 5074  C   LEU B 122     1724   2081   1462    243    -89     65       C  
ATOM   5075  O   LEU B 122     -29.735  -1.093   2.328  1.00 14.12           O  
ANISOU 5075  O   LEU B 122     1476   2274   1611    102   -149   -177       O  
ATOM   5076  N   ILE B 123     -29.565  -1.337   0.099  1.00 12.57           N  
ANISOU 5076  N   ILE B 123     1329   1971   1474     95   -148   -132       N  
ATOM   5077  CA  ILE B 123     -28.120  -1.618   0.201  1.00 12.27           C  
ANISOU 5077  CA  ILE B 123     1346   1816   1498    214    -32     27       C  
ATOM   5078  CB  ILE B 123     -27.522  -2.201  -1.105  1.00 12.84           C  
ANISOU 5078  CB  ILE B 123     1456   1798   1623    118     31    -93       C  
ATOM   5079  CG1 ILE B 123     -26.168  -2.867  -0.860  1.00 13.56           C  
ANISOU 5079  CG1 ILE B 123     1583   1990   1576    232    149    -30       C  
ATOM   5080  CG2 ILE B 123     -27.430  -1.159  -2.210  1.00 14.21           C  
ANISOU 5080  CG2 ILE B 123     1706   2112   1580    182     94    -50       C  
ATOM   5081  CD1 ILE B 123     -26.147  -3.953   0.213  1.00 14.60           C  
ANISOU 5081  CD1 ILE B 123     1748   1931   1869    347    279    -24       C  
ATOM   5082  C   ILE B 123     -27.358  -0.385   0.698  1.00 13.56           C  
ANISOU 5082  C   ILE B 123     1390   2047   1713    195     28   -206       C  
ATOM   5083  O   ILE B 123     -26.342  -0.530   1.380  1.00 13.38           O  
ANISOU 5083  O   ILE B 123     1568   1913   1601    138     11    -53       O  
ATOM   5084  N   LYS B 124     -27.822   0.814   0.355  1.00 14.70           N  
ANISOU 5084  N   LYS B 124     1768   2009   1808    165   -356    -61       N  
ATOM   5085  CA  LYS B 124     -27.123   2.039   0.793  1.00 15.87           C  
ANISOU 5085  CA  LYS B 124     1901   1968   2159    103   -353    -95       C  
ATOM   5086  CB  LYS B 124     -27.765   3.331   0.264  1.00 19.08           C  
ANISOU 5086  CB  LYS B 124     2552   2030   2667    -43   -626    314       C  
ATOM   5087  CG  LYS B 124     -27.067   4.631   0.691  1.00 21.02           C  
ANISOU 5087  CG  LYS B 124     2814   2362   2810   -183   -582      5       C  
ATOM   5088  CD  LYS B 124     -27.635   5.924   0.102  1.00 24.53           C  
ANISOU 5088  CD  LYS B 124     3177   2251   3889   -123   -445     59       C  
ATOM   5089  CE  LYS B 124     -26.771   7.141   0.439  1.00 24.97           C  
ANISOU 5089  CE  LYS B 124     3731   2235   3518   -225   -393   -182       C  
ATOM   5090  NZ  LYS B 124     -27.311   8.424  -0.091  1.00 29.49           N  
ANISOU 5090  NZ  LYS B 124     4558   2585   4061   -366   -766    211       N  
ATOM   5091  C   LYS B 124     -27.075   2.085   2.321  1.00 15.68           C  
ANISOU 5091  C   LYS B 124     1974   1753   2228    277   -336   -210       C  
ATOM   5092  O   LYS B 124     -26.100   2.602   2.886  1.00 16.69           O  
ANISOU 5092  O   LYS B 124     1941   1980   2421    156   -195   -564       O  
ATOM   5093  N   LEU B 125     -28.136   1.606   2.980  1.00 15.13           N  
ANISOU 5093  N   LEU B 125     1745   1783   2220    257   -265   -325       N  
ATOM   5094  CA ALEU B 125     -28.182   1.561   4.436  0.50 16.88           C  
ANISOU 5094  CA ALEU B 125     2099   2150   2162    184   -154   -488       C  
ATOM   5095  CA BLEU B 125     -28.187   1.544   4.454  0.50 16.79           C  
ANISOU 5095  CA BLEU B 125     1937   2242   2197    261    -35   -502       C  
ATOM   5096  CB ALEU B 125     -29.661   1.585   4.813  0.50 17.82           C  
ANISOU 5096  CB ALEU B 125     2176   2240   2355     64   -194   -541       C  
ATOM   5097  CB BLEU B 125     -29.622   1.432   4.963  0.50 18.84           C  
ANISOU 5097  CB BLEU B 125     2041   2529   2586    186     78   -561       C  
ATOM   5098  CG ALEU B 125     -29.991   1.706   6.278  0.50 18.11           C  
ANISOU 5098  CG ALEU B 125     2457   2234   2187    177   -334   -367       C  
ATOM   5099  CG BLEU B 125     -30.407   2.715   5.021  0.50 19.42           C  
ANISOU 5099  CG BLEU B 125     2090   2714   2573    385    224   -525       C  
ATOM   5100  CD1ALEU B 125     -29.472   3.021   6.809  0.50 17.86           C  
ANISOU 5100  CD1ALEU B 125     2460   2282   2043     56   -363   -274       C  
ATOM   5101  CD1BLEU B 125     -31.823   2.393   5.416  0.50 19.94           C  
ANISOU 5101  CD1BLEU B 125     2061   2796   2717    383    236   -716       C  
ATOM   5102  CD2ALEU B 125     -31.492   1.577   6.476  0.50 18.34           C  
ANISOU 5102  CD2ALEU B 125     2475   2514   1979    106   -216   -364       C  
ATOM   5103  CD2BLEU B 125     -29.758   3.632   6.026  0.50 19.63           C  
ANISOU 5103  CD2BLEU B 125     1951   2684   2823    566    164   -667       C  
ATOM   5104  C   LEU B 125     -27.456   0.314   4.966  1.00 14.75           C  
ANISOU 5104  C   LEU B 125     1702   2079   1822     48    -24   -452       C  
ATOM   5105  O   LEU B 125     -26.649   0.415   5.895  1.00 15.52           O  
ANISOU 5105  O   LEU B 125     1672   2388   1837    -12   -106   -510       O  
ATOM   5106  N   HIS B 126     -27.793  -0.854   4.387  1.00 13.90           N  
ANISOU 5106  N   HIS B 126     1574   2159   1547      0   -120   -330       N  
ATOM   5107  CA  HIS B 126     -27.323  -2.141   4.868  1.00 13.83           C  
ANISOU 5107  CA  HIS B 126     1689   2098   1468   -176   -125    -80       C  
ATOM   5108  CB  HIS B 126     -27.916  -3.248   3.995  1.00 14.67           C  
ANISOU 5108  CB  HIS B 126     1842   2046   1684   -161   -357     39       C  
ATOM   5109  CG  HIS B 126     -27.589  -4.631   4.422  1.00 14.42           C  
ANISOU 5109  CG  HIS B 126     1784   2027   1667   -279   -301    161       C  
ATOM   5110  ND1 HIS B 126     -28.039  -5.132   5.615  1.00 17.40           N  
ANISOU 5110  ND1 HIS B 126     2096   2303   2212   -299    -37    538       N  
ATOM   5111  CE1 HIS B 126     -27.624  -6.379   5.740  1.00 18.44           C  
ANISOU 5111  CE1 HIS B 126     2647   2052   2306   -374   -117    369       C  
ATOM   5112  NE2 HIS B 126     -26.936  -6.714   4.622  1.00 17.03           N  
ANISOU 5112  NE2 HIS B 126     2028   2175   2265   -538   -393    201       N  
ATOM   5113  CD2 HIS B 126     -26.910  -5.624   3.801  1.00 15.29           C  
ANISOU 5113  CD2 HIS B 126     1912   2046   1849   -405   -310     56       C  
ATOM   5114  C   HIS B 126     -25.797  -2.215   4.880  1.00 13.16           C  
ANISOU 5114  C   HIS B 126     1755   1754   1490    -43   -230    136       C  
ATOM   5115  O   HIS B 126     -25.206  -2.849   5.724  1.00 14.35           O  
ANISOU 5115  O   HIS B 126     1792   2058   1602   -239   -407    388       O  
ATOM   5116  N   GLN B 127     -25.147  -1.574   3.909  1.00 11.85           N  
ANISOU 5116  N   GLN B 127     1535   1510   1456     99   -104     83       N  
ATOM   5117  CA  GLN B 127     -23.698  -1.659   3.798  1.00 11.96           C  
ANISOU 5117  CA  GLN B 127     1503   1540   1500     19   -235     19       C  
ATOM   5118  CB  GLN B 127     -23.218  -0.971   2.521  1.00 12.96           C  
ANISOU 5118  CB  GLN B 127     1633   1709   1580    -12    -92     64       C  
ATOM   5119  CG  GLN B 127     -23.367   0.547   2.547  1.00 13.08           C  
ANISOU 5119  CG  GLN B 127     1809   1633   1528    -25     -1     44       C  
ATOM   5120  CD  GLN B 127     -23.043   1.235   1.247  1.00 15.03           C  
ANISOU 5120  CD  GLN B 127     2199   1931   1578     69    -60     98       C  
ATOM   5121  OE1 GLN B 127     -22.365   0.667   0.396  1.00 15.26           O  
ANISOU 5121  OE1 GLN B 127     2328   1757   1713      0    129    179       O  
ATOM   5122  NE2 GLN B 127     -23.532   2.463   1.085  1.00 16.24           N  
ANISOU 5122  NE2 GLN B 127     2503   1683   1983   -188   -558    162       N  
ATOM   5123  C   GLN B 127     -22.997  -1.104   5.040  1.00 12.61           C  
ANISOU 5123  C   GLN B 127     1694   1465   1631   -134   -214    -25       C  
ATOM   5124  O   GLN B 127     -21.859  -1.467   5.279  1.00 13.04           O  
ANISOU 5124  O   GLN B 127     1874   1485   1593     47   -449     -4       O  
ATOM   5125  N   TYR B 128     -23.676  -0.237   5.793  1.00 12.21           N  
ANISOU 5125  N   TYR B 128     1457   1732   1449   -168   -114    -32       N  
ATOM   5126  CA  TYR B 128     -23.045   0.418   6.958  1.00 13.14           C  
ANISOU 5126  CA  TYR B 128     1657   1850   1483   -148   -107   -147       C  
ATOM   5127  CB  TYR B 128     -23.552   1.844   7.147  1.00 13.59           C  
ANISOU 5127  CB  TYR B 128     1693   1975   1496   -108     45   -287       C  
ATOM   5128  CG  TYR B 128     -23.090   2.784   6.072  1.00 13.58           C  
ANISOU 5128  CG  TYR B 128     1880   1726   1551    -45     77   -352       C  
ATOM   5129  CD1 TYR B 128     -21.762   3.170   5.995  1.00 14.13           C  
ANISOU 5129  CD1 TYR B 128     1937   1901   1528    -19      6   -383       C  
ATOM   5130  CE1 TYR B 128     -21.330   4.037   5.009  1.00 13.22           C  
ANISOU 5130  CE1 TYR B 128     1732   1615   1674    -38     70   -401       C  
ATOM   5131  CZ  TYR B 128     -22.239   4.554   4.098  1.00 14.54           C  
ANISOU 5131  CZ  TYR B 128     1866   1680   1975     45     -4   -216       C  
ATOM   5132  OH  TYR B 128     -21.837   5.422   3.115  1.00 16.89           O  
ANISOU 5132  OH  TYR B 128     2030   2095   2291     29    249     66       O  
ATOM   5133  CE2 TYR B 128     -23.567   4.187   4.174  1.00 15.05           C  
ANISOU 5133  CE2 TYR B 128     1987   1690   2041    -42    156   -140       C  
ATOM   5134  CD2 TYR B 128     -23.982   3.295   5.143  1.00 13.93           C  
ANISOU 5134  CD2 TYR B 128     1819   1648   1822   -141     -9   -263       C  
ATOM   5135  C   TYR B 128     -23.228  -0.333   8.265  1.00 14.28           C  
ANISOU 5135  C   TYR B 128     1748   2156   1519     79     -5   -132       C  
ATOM   5136  O   TYR B 128     -22.588   0.026   9.247  1.00 15.85           O  
ANISOU 5136  O   TYR B 128     2269   2206   1546    203   -237   -376       O  
ATOM   5137  N   ASN B 129     -24.124  -1.307   8.345  1.00 15.95           N  
ANISOU 5137  N   ASN B 129     1903   2335   1820   -193     28    275       N  
ATOM   5138  CA  ASN B 129     -24.176  -1.972   9.669  1.00 16.32           C  
ANISOU 5138  CA  ASN B 129     2013   2365   1823   -141    377    305       C  
ATOM   5139  CB  ASN B 129     -25.203  -1.380  10.624  1.00 18.15           C  
ANISOU 5139  CB  ASN B 129     2137   2401   2356     -8    438    227       C  
ATOM   5140  CG  ASN B 129     -26.593  -1.829  10.311  1.00 18.30           C  
ANISOU 5140  CG  ASN B 129     2501   2285   2166   -167    262     59       C  
ATOM   5141  OD1 ASN B 129     -26.900  -2.118   9.144  1.00 20.46           O  
ANISOU 5141  OD1 ASN B 129     3221   2460   2091    305    199    -78       O  
ATOM   5142  ND2 ASN B 129     -27.430  -1.808  11.340  1.00 18.22           N  
ANISOU 5142  ND2 ASN B 129     2718   2033   2168    387    483    413       N  
ATOM   5143  C   ASN B 129     -24.312  -3.487   9.595  1.00 15.89           C  
ANISOU 5143  C   ASN B 129     2023   2371   1643   -261    418     44       C  
ATOM   5144  O   ASN B 129     -24.480  -4.106  10.635  1.00 18.42           O  
ANISOU 5144  O   ASN B 129     3030   1966   2001   -177    217    370       O  
ATOM   5145  N   ALA B 130     -24.055  -4.067   8.433  1.00 16.64           N  
ANISOU 5145  N   ALA B 130     2679   2229   1413   -596    134     22       N  
ATOM   5146  CA  ALA B 130     -24.004  -5.493   8.274  1.00 18.56           C  
ANISOU 5146  CA  ALA B 130     3146   2265   1641   -798     69    176       C  
ATOM   5147  CB  ALA B 130     -24.336  -5.845   6.849  1.00 18.84           C  
ANISOU 5147  CB  ALA B 130     2982   2328   1846   -766   -347    148       C  
ATOM   5148  C   ALA B 130     -22.617  -6.008   8.639  1.00 19.10           C  
ANISOU 5148  C   ALA B 130     3740   2057   1458   -477   -169    306       C  
ATOM   5149  O   ALA B 130     -21.641  -5.277   8.721  1.00 21.68           O  
ANISOU 5149  O   ALA B 130     3561   2181   2493   -545   -592    143       O  
ATOM   5150  N   ASP B 131     -22.554  -7.314   8.845  1.00 21.69           N  
ANISOU 5150  N   ASP B 131     4608   2116   1515   -482   -230    134       N  
ATOM   5151  CA  ASP B 131     -21.324  -8.005   9.051  1.00 22.65           C  
ANISOU 5151  CA  ASP B 131     4774   2221   1609     29   -567    194       C  
ATOM   5152  CB  ASP B 131     -21.669  -9.430   9.462  1.00 26.49           C  
ANISOU 5152  CB  ASP B 131     5710   2192   2161    391    -76    322       C  
ATOM   5153  CG  ASP B 131     -20.445 -10.285   9.724  1.00 31.15           C  
ANISOU 5153  CG  ASP B 131     6424   2636   2772   1206   -344   1095       C  
ATOM   5154  OD1 ASP B 131     -19.319  -9.826   9.438  1.00 32.91           O  
ANISOU 5154  OD1 ASP B 131     6905   3169   2427   1013    243    761       O  
ATOM   5155  OD2 ASP B 131     -20.634 -11.389  10.236  1.00 40.98           O  
ANISOU 5155  OD2 ASP B 131     8608   2684   4278    908    344   1104       O  
ATOM   5156  C   ASP B 131     -20.482  -7.940   7.774  1.00 21.81           C  
ANISOU 5156  C   ASP B 131     4286   2137   1864     46   -821    134       C  
ATOM   5157  O   ASP B 131     -20.908  -8.405   6.741  1.00 20.06           O  
ANISOU 5157  O   ASP B 131     4065   1838   1719    -92   -747    182       O  
ATOM   5158  N   PRO B 132     -19.264  -7.353   7.771  1.00 23.53           N  
ANISOU 5158  N   PRO B 132     4124   2499   2315    -66  -1347    -82       N  
ATOM   5159  CA  PRO B 132     -18.464  -7.282   6.542  1.00 23.89           C  
ANISOU 5159  CA  PRO B 132     3664   2603   2808    111  -1002    -60       C  
ATOM   5160  CB  PRO B 132     -17.182  -6.571   6.998  1.00 29.16           C  
ANISOU 5160  CB  PRO B 132     4212   3331   3536   -117  -1204   -455       C  
ATOM   5161  CG  PRO B 132     -17.608  -5.782   8.219  1.00 31.15           C  
ANISOU 5161  CG  PRO B 132     4733   3867   3235   -527  -1381   -573       C  
ATOM   5162  CD  PRO B 132     -18.636  -6.654   8.901  1.00 25.70           C  
ANISOU 5162  CD  PRO B 132     4548   2920   2295    188  -1474   -281       C  
ATOM   5163  C   PRO B 132     -18.147  -8.646   5.896  1.00 21.09           C  
ANISOU 5163  C   PRO B 132     3263   2479   2269    247  -1002    320       C  
ATOM   5164  O   PRO B 132     -17.969  -8.717   4.664  1.00 21.51           O  
ANISOU 5164  O   PRO B 132     2776   3092   2303   -333  -1031    303       O  
ATOM   5165  N   LEU B 133     -18.116  -9.729   6.694  1.00 23.29           N  
ANISOU 5165  N   LEU B 133     3639   2856   2353    165  -1296    586       N  
ATOM   5166  CA  LEU B 133     -17.909 -11.065   6.129  1.00 24.15           C  
ANISOU 5166  CA  LEU B 133     3716   2937   2523    523   -953    580       C  
ATOM   5167  CB  LEU B 133     -17.701 -12.073   7.265  1.00 30.06           C  
ANISOU 5167  CB  LEU B 133     4673   3857   2890    871  -1017   1030       C  
ATOM   5168  CG  LEU B 133     -16.575 -11.715   8.229  1.00 38.63           C  
ANISOU 5168  CG  LEU B 133     4815   5199   4663   1170  -1699    895       C  
ATOM   5169  CD1 LEU B 133     -16.521 -12.699   9.390  1.00 44.12           C  
ANISOU 5169  CD1 LEU B 133     6566   4841   5354   1268  -1583   1107       C  
ATOM   5170  CD2 LEU B 133     -15.244 -11.649   7.487  1.00 41.61           C  
ANISOU 5170  CD2 LEU B 133     4540   5679   5589   1403  -1344    510       C  
ATOM   5171  C   LEU B 133     -19.110 -11.464   5.255  1.00 20.30           C  
ANISOU 5171  C   LEU B 133     3048   2282   2381    121   -339    584       C  
ATOM   5172  O   LEU B 133     -18.959 -12.079   4.169  1.00 21.44           O  
ANISOU 5172  O   LEU B 133     3239   2157   2750    444    -33    224       O  
ATOM   5173  N   GLU B 134     -20.319 -11.156   5.720  1.00 18.03           N  
ANISOU 5173  N   GLU B 134     3098   2055   1696     17   -326    538       N  
ATOM   5174  CA AGLU B 134     -21.504 -11.405   4.957  0.50 16.29           C  
ANISOU 5174  CA AGLU B 134     2657   1627   1903   -266      1    194       C  
ATOM   5175  CA BGLU B 134     -21.525 -11.430   4.932  0.50 17.14           C  
ANISOU 5175  CA BGLU B 134     2757   1741   2012   -241   -117    286       C  
ATOM   5176  CB AGLU B 134     -22.706 -11.150   5.862  0.50 17.43           C  
ANISOU 5176  CB AGLU B 134     2891   1743   1986   -296    254    230       C  
ATOM   5177  CB BGLU B 134     -22.835 -11.221   5.708  0.50 19.36           C  
ANISOU 5177  CB BGLU B 134     2920   2147   2288   -225     71    273       C  
ATOM   5178  CG AGLU B 134     -23.981 -11.586   5.237  0.50 17.79           C  
ANISOU 5178  CG AGLU B 134     2797   1771   2188   -252    248     20       C  
ATOM   5179  CG BGLU B 134     -23.325 -12.419   6.495  0.50 20.80           C  
ANISOU 5179  CG BGLU B 134     2950   2073   2880   -293    -89    361       C  
ATOM   5180  CD AGLU B 134     -24.051 -13.087   5.118  0.50 19.13           C  
ANISOU 5180  CD AGLU B 134     2838   1742   2686   -207    115    194       C  
ATOM   5181  CD BGLU B 134     -23.871 -13.613   5.729  0.50 21.28           C  
ANISOU 5181  CD BGLU B 134     2893   2062   3130   -347   -215    466       C  
ATOM   5182  OE1AGLU B 134     -23.282 -13.784   5.844  0.50 20.16           O  
ANISOU 5182  OE1AGLU B 134     2979   1349   3329   -245     51    492       O  
ATOM   5183  OE1BGLU B 134     -24.332 -13.480   4.549  0.50 22.49           O  
ANISOU 5183  OE1BGLU B 134     2656   2647   3240   -613   -771   -382       O  
ATOM   5184  OE2AGLU B 134     -24.879 -13.552   4.310  0.50 22.96           O  
ANISOU 5184  OE2AGLU B 134     3428   2351   2943   -576     13   -350       O  
ATOM   5185  OE2BGLU B 134     -23.895 -14.678   6.352  0.50 22.98           O  
ANISOU 5185  OE2BGLU B 134     2953   1407   4370      6   -141    334       O  
ATOM   5186  C   GLU B 134     -21.551 -10.510   3.707  1.00 14.39           C  
ANISOU 5186  C   GLU B 134     2208   1317   1939   -390    -65    119       C  
ATOM   5187  O   GLU B 134     -21.943 -10.931   2.633  1.00 14.25           O  
ANISOU 5187  O   GLU B 134     2097   1553   1763   -330    -25    154       O  
ATOM   5188  N   LEU B 135     -21.129  -9.246   3.850  1.00 12.55           N  
ANISOU 5188  N   LEU B 135     1972   1291   1504   -213   -210     49       N  
ATOM   5189  CA  LEU B 135     -21.158  -8.335   2.701  1.00 12.59           C  
ANISOU 5189  CA  LEU B 135     1905   1385   1493   -198   -219    109       C  
ATOM   5190  CB  LEU B 135     -20.769  -6.925   3.142  1.00 12.83           C  
ANISOU 5190  CB  LEU B 135     1862   1427   1585   -259   -269    112       C  
ATOM   5191  CG  LEU B 135     -21.763  -6.187   4.038  1.00 13.98           C  
ANISOU 5191  CG  LEU B 135     2141   1581   1588   -226   -134     35       C  
ATOM   5192  CD1 LEU B 135     -21.218  -4.806   4.439  1.00 15.93           C  
ANISOU 5192  CD1 LEU B 135     2570   1572   1910   -123   -209    -37       C  
ATOM   5193  CD2 LEU B 135     -23.116  -6.062   3.365  1.00 14.26           C  
ANISOU 5193  CD2 LEU B 135     2188   1477   1750    -59    -41    -24       C  
ATOM   5194  C   LEU B 135     -20.239  -8.848   1.586  1.00 12.22           C  
ANISOU 5194  C   LEU B 135     1705   1367   1571    -62   -340     78       C  
ATOM   5195  O   LEU B 135     -20.571  -8.686   0.420  1.00 11.73           O  
ANISOU 5195  O   LEU B 135     1697   1309   1451   -153   -197    116       O  
ATOM   5196  N   ALA B 136     -19.104  -9.475   1.939  1.00 11.92           N  
ANISOU 5196  N   ALA B 136     1815   1120   1595    -54   -431     66       N  
ATOM   5197  CA  ALA B 136     -18.204 -10.035   0.931  1.00 13.14           C  
ANISOU 5197  CA  ALA B 136     1770   1417   1805   -128   -312     57       C  
ATOM   5198  CB  ALA B 136     -16.876 -10.395   1.540  1.00 14.70           C  
ANISOU 5198  CB  ALA B 136     1798   1606   2178      4   -356   -111       C  
ATOM   5199  C   ALA B 136     -18.837 -11.230   0.205  1.00 11.69           C  
ANISOU 5199  C   ALA B 136     1644   1066   1730     49   -106     95       C  
ATOM   5200  O   ALA B 136     -18.487 -11.508  -0.934  1.00 14.24           O  
ANISOU 5200  O   ALA B 136     2127   1402   1879     40     38     28       O  
ATOM   5201  N   LEU B 137     -19.740 -11.962   0.867  1.00 11.87           N  
ANISOU 5201  N   LEU B 137     1630   1371   1507      7   -101    118       N  
ATOM   5202  CA  LEU B 137     -20.472 -13.037   0.193  1.00 12.50           C  
ANISOU 5202  CA  LEU B 137     1916   1284   1550     38   -165     76       C  
ATOM   5203  CB  LEU B 137     -21.073 -14.009   1.207  1.00 14.06           C  
ANISOU 5203  CB  LEU B 137     2454   1130   1757    -42   -250    139       C  
ATOM   5204  CG  LEU B 137     -20.059 -14.745   2.075  1.00 18.14           C  
ANISOU 5204  CG  LEU B 137     2948   1606   2337    261   -419    352       C  
ATOM   5205  CD1 LEU B 137     -20.794 -15.637   3.062  1.00 19.75           C  
ANISOU 5205  CD1 LEU B 137     3314   1851   2338    175   -392    524       C  
ATOM   5206  CD2 LEU B 137     -19.076 -15.535   1.209  1.00 22.45           C  
ANISOU 5206  CD2 LEU B 137     3461   2515   2551    739   -427    362       C  
ATOM   5207  C   LEU B 137     -21.588 -12.464  -0.691  1.00 11.05           C  
ANISOU 5207  C   LEU B 137     1610   1082   1506   -100    -66     94       C  
ATOM   5208  O   LEU B 137     -22.032 -13.114  -1.617  1.00 12.89           O  
ANISOU 5208  O   LEU B 137     1838   1322   1737    -28   -282    -71       O  
ATOM   5209  N   LEU B 138     -22.062 -11.270  -0.351  1.00 10.51           N  
ANISOU 5209  N   LEU B 138     1503   1187   1303    -40    -45     72       N  
ATOM   5210  CA  LEU B 138     -23.147 -10.603  -1.093  1.00 10.62           C  
ANISOU 5210  CA  LEU B 138     1441   1191   1401    -72     -9    133       C  
ATOM   5211  CB  LEU B 138     -23.714  -9.495  -0.208  1.00 11.63           C  
ANISOU 5211  CB  LEU B 138     1699   1247   1470    -48   -156      4       C  
ATOM   5212  CG  LEU B 138     -25.107  -8.963  -0.517  1.00 12.48           C  
ANISOU 5212  CG  LEU B 138     1762   1379   1600     40    -91     36       C  
ATOM   5213  CD1 LEU B 138     -25.608  -8.144   0.664  1.00 13.55           C  
ANISOU 5213  CD1 LEU B 138     1716   1924   1509    107     48     64       C  
ATOM   5214  CD2 LEU B 138     -25.151  -8.121  -1.780  1.00 13.18           C  
ANISOU 5214  CD2 LEU B 138     1873   1521   1611    -76     82     51       C  
ATOM   5215  C   LEU B 138     -22.618 -10.082  -2.432  1.00  9.93           C  
ANISOU 5215  C   LEU B 138     1411   1069   1291    -51    -98     80       C  
ATOM   5216  O   LEU B 138     -23.266 -10.303  -3.472  1.00 10.79           O  
ANISOU 5216  O   LEU B 138     1290   1547   1262     47    -74    132       O  
ATOM   5217  N   SER B 139     -21.462  -9.411  -2.434  1.00 10.54           N  
ANISOU 5217  N   SER B 139     1463   1219   1319    -67   -230    112       N  
ATOM   5218  CA  SER B 139     -20.925  -8.786  -3.650  1.00 11.16           C  
ANISOU 5218  CA  SER B 139     1487   1252   1499    -65    -49     32       C  
ATOM   5219  CB  SER B 139     -21.284  -7.315  -3.701  1.00 11.63           C  
ANISOU 5219  CB  SER B 139     1375   1321   1721     29    -90     69       C  
ATOM   5220  OG  SER B 139     -20.730  -6.661  -4.852  1.00 12.81           O  
ANISOU 5220  OG  SER B 139     1674   1215   1979     72     46    314       O  
ATOM   5221  C   SER B 139     -19.413  -8.926  -3.644  1.00 10.56           C  
ANISOU 5221  C   SER B 139     1437   1174   1401     89    -66     70       C  
ATOM   5222  O   SER B 139     -18.781  -8.785  -2.586  1.00 10.97           O  
ANISOU 5222  O   SER B 139     1416   1392   1358    -26    -49    127       O  
ATOM   5223  N   PRO B 140     -18.778  -9.036  -4.829  1.00 10.10           N  
ANISOU 5223  N   PRO B 140     1420   1164   1252    127   -158     32       N  
ATOM   5224  CA  PRO B 140     -17.323  -8.915  -4.934  1.00 10.07           C  
ANISOU 5224  CA  PRO B 140     1453   1041   1330    180   -106    116       C  
ATOM   5225  CB  PRO B 140     -17.026  -9.308  -6.389  1.00 10.68           C  
ANISOU 5225  CB  PRO B 140     1654   1057   1346     72     24    154       C  
ATOM   5226  CG  PRO B 140     -18.307  -8.920  -7.109  1.00 11.37           C  
ANISOU 5226  CG  PRO B 140     1688   1394   1238     30    -38    -32       C  
ATOM   5227  CD  PRO B 140     -19.409  -9.306  -6.137  1.00 10.71           C  
ANISOU 5227  CD  PRO B 140     1396   1383   1290     60   -114      3       C  
ATOM   5228  C   PRO B 140     -16.811  -7.506  -4.612  1.00 10.69           C  
ANISOU 5228  C   PRO B 140     1389   1168   1502     56    -70     69       C  
ATOM   5229  O   PRO B 140     -15.632  -7.331  -4.343  1.00 13.16           O  
ANISOU 5229  O   PRO B 140     1488   1280   2232    180   -176   -382       O  
ATOM   5230  N   CYS B 141     -17.719  -6.514  -4.665  1.00 10.57           N  
ANISOU 5230  N   CYS B 141     1303   1156   1555      3   -181     99       N  
ATOM   5231  CA  CYS B 141     -17.373  -5.105  -4.411  1.00 10.64           C  
ANISOU 5231  CA  CYS B 141     1496   1196   1349     65   -176     40       C  
ATOM   5232  CB  CYS B 141     -17.874  -4.263  -5.572  1.00 11.06           C  
ANISOU 5232  CB  CYS B 141     1746   1149   1307    162   -208    -74       C  
ATOM   5233  SG  CYS B 141     -16.972  -4.601  -7.101  1.00 13.90           S  
ANISOU 5233  SG  CYS B 141     2249   1565   1467    219    148    119       S  
ATOM   5234  C   CYS B 141     -18.017  -4.675  -3.092  1.00 10.44           C  
ANISOU 5234  C   CYS B 141     1421   1228   1318    -69   -204     28       C  
ATOM   5235  O   CYS B 141     -19.002  -3.938  -3.081  1.00 12.41           O  
ANISOU 5235  O   CYS B 141     1635   1794   1283    206   -132    186       O  
ATOM   5236  N   SER B 142     -17.447  -5.159  -1.989  1.00 10.40           N  
ANISOU 5236  N   SER B 142     1505   1122   1323     67    -72    168       N  
ATOM   5237  CA  SER B 142     -18.065  -5.003  -0.662  1.00 10.96           C  
ANISOU 5237  CA  SER B 142     1721   1155   1287   -162    -71     87       C  
ATOM   5238  CB  SER B 142     -18.049  -6.312   0.080  1.00 12.87           C  
ANISOU 5238  CB  SER B 142     2112   1139   1638   -520   -106    132       C  
ATOM   5239  OG  SER B 142     -16.735  -6.770   0.307  1.00 15.15           O  
ANISOU 5239  OG  SER B 142     2380   1625   1749   -383   -430    338       O  
ATOM   5240  C   SER B 142     -17.406  -3.910   0.182  1.00 10.60           C  
ANISOU 5240  C   SER B 142     1599   1120   1307   -118     34     40       C  
ATOM   5241  O   SER B 142     -17.990  -3.490   1.187  1.00 12.65           O  
ANISOU 5241  O   SER B 142     1780   1468   1556   -374    261   -290       O  
ATOM   5242  N   ASP B 143     -16.216  -3.430  -0.203  1.00  9.92           N  
ANISOU 5242  N   ASP B 143     1559   1096   1114     -7     67    -31       N  
ATOM   5243  CA  ASP B 143     -15.539  -2.361   0.554  1.00 10.79           C  
ANISOU 5243  CA  ASP B 143     1749   1041   1309    -71     12     35       C  
ATOM   5244  CB  ASP B 143     -14.128  -2.150   0.013  1.00 10.95           C  
ANISOU 5244  CB  ASP B 143     1635   1095   1428    -91    -94    -28       C  
ATOM   5245  CG  ASP B 143     -13.395  -0.990   0.635  1.00 10.90           C  
ANISOU 5245  CG  ASP B 143     1693   1101   1346   -135   -117     68       C  
ATOM   5246  OD1 ASP B 143     -12.741  -1.207   1.660  1.00 12.37           O  
ANISOU 5246  OD1 ASP B 143     2026   1304   1370   -136   -233     91       O  
ATOM   5247  OD2 ASP B 143     -13.541   0.140   0.089  1.00 11.50           O  
ANISOU 5247  OD2 ASP B 143     1840   1144   1385    -85      2    178       O  
ATOM   5248  C   ASP B 143     -16.363  -1.074   0.408  1.00 10.67           C  
ANISOU 5248  C   ASP B 143     1618   1103   1330    -74    -93   -125       C  
ATOM   5249  O   ASP B 143     -16.802  -0.744  -0.707  1.00 10.90           O  
ANISOU 5249  O   ASP B 143     1539   1291   1310   -142    -82    -75       O  
ATOM   5250  N   VAL B 144     -16.562  -0.381   1.534  1.00  9.71           N  
ANISOU 5250  N   VAL B 144     1532   1001   1154    -87    -66     28       N  
ATOM   5251  CA  VAL B 144     -17.346   0.847   1.606  1.00 10.23           C  
ANISOU 5251  CA  VAL B 144     1467   1157   1264    -19   -107     48       C  
ATOM   5252  CB  VAL B 144     -18.414   0.743   2.705  1.00 11.54           C  
ANISOU 5252  CB  VAL B 144     1482   1273   1628   -163     70     56       C  
ATOM   5253  CG1 VAL B 144     -19.090   2.076   2.962  1.00 13.09           C  
ANISOU 5253  CG1 VAL B 144     1720   1314   1939   -160    158    145       C  
ATOM   5254  CG2 VAL B 144     -19.421  -0.359   2.385  1.00 12.37           C  
ANISOU 5254  CG2 VAL B 144     1432   1343   1923   -125    157     62       C  
ATOM   5255  C   VAL B 144     -16.399   2.031   1.798  1.00 10.63           C  
ANISOU 5255  C   VAL B 144     1679   1097   1263    -60    -11     67       C  
ATOM   5256  O   VAL B 144     -15.531   2.014   2.668  1.00 11.09           O  
ANISOU 5256  O   VAL B 144     1601   1165   1446     58    -99     66       O  
ATOM   5257  N   ASP B 145     -16.607   3.078   0.978  1.00 10.33           N  
ANISOU 5257  N   ASP B 145     1529   1119   1276   -109    -65    100       N  
ATOM   5258  CA  ASP B 145     -15.728   4.252   1.028  1.00 10.77           C  
ANISOU 5258  CA  ASP B 145     1725   1021   1346   -113    -79    -16       C  
ATOM   5259  CB  ASP B 145     -16.163   5.287  -0.004  1.00 11.11           C  
ANISOU 5259  CB  ASP B 145     1751   1109   1358   -123   -216     35       C  
ATOM   5260  CG  ASP B 145     -16.021   4.840  -1.442  1.00 11.26           C  
ANISOU 5260  CG  ASP B 145     1688   1226   1364    -42   -132     98       C  
ATOM   5261  OD1 ASP B 145     -15.071   4.085  -1.730  1.00 11.93           O  
ANISOU 5261  OD1 ASP B 145     1723   1269   1540    -95    -23    234       O  
ATOM   5262  OD2 ASP B 145     -16.837   5.322  -2.268  1.00 11.98           O  
ANISOU 5262  OD2 ASP B 145     1663   1549   1339     62   -138     74       O  
ATOM   5263  C   ASP B 145     -15.744   4.932   2.397  1.00 10.33           C  
ANISOU 5263  C   ASP B 145     1502   1139   1284    -49   -168     41       C  
ATOM   5264  O   ASP B 145     -16.808   5.155   3.002  1.00 11.93           O  
ANISOU 5264  O   ASP B 145     1594   1460   1476    -12    -97   -141       O  
ATOM   5265  N   GLU B 146     -14.549   5.346   2.832  1.00 10.39           N  
ANISOU 5265  N   GLU B 146     1600   1082   1266   -196   -140   -114       N  
ATOM   5266  CA  GLU B 146     -14.420   6.069   4.085  1.00 10.77           C  
ANISOU 5266  CA  GLU B 146     1679   1210   1202   -165     -5   -139       C  
ATOM   5267  CB  GLU B 146     -13.164   5.626   4.835  1.00 11.63           C  
ANISOU 5267  CB  GLU B 146     1820   1303   1293   -167    -98     -2       C  
ATOM   5268  CG  GLU B 146     -13.161   4.151   5.214  1.00 12.37           C  
ANISOU 5268  CG  GLU B 146     1961   1386   1353    -73     20    143       C  
ATOM   5269  CD  GLU B 146     -12.616   3.173   4.196  1.00 13.02           C  
ANISOU 5269  CD  GLU B 146     1961   1361   1624     47      0    115       C  
ATOM   5270  OE1 GLU B 146     -12.241   3.618   3.073  1.00 13.08           O  
ANISOU 5270  OE1 GLU B 146     1943   1457   1568   -102    -38    -68       O  
ATOM   5271  OE2 GLU B 146     -12.651   1.960   4.523  1.00 12.71           O  
ANISOU 5271  OE2 GLU B 146     1733   1305   1791    146    -68      5       O  
ATOM   5272  C   GLU B 146     -14.412   7.578   3.892  1.00 11.57           C  
ANISOU 5272  C   GLU B 146     1904   1271   1219    -80    -65   -147       C  
ATOM   5273  O   GLU B 146     -14.857   8.308   4.801  1.00 11.02           O  
ANISOU 5273  O   GLU B 146     1972   1094   1118    -33     81     -4       O  
ATOM   5274  N   TYR B 147     -13.897   8.039   2.751  1.00 10.17           N  
ANISOU 5274  N   TYR B 147     1604    933   1327   -105    -61    -27       N  
ATOM   5275  CA  TYR B 147     -13.683   9.458   2.466  1.00 11.20           C  
ANISOU 5275  CA  TYR B 147     1775    906   1573     24   -196     24       C  
ATOM   5276  CB  TYR B 147     -12.188   9.818   2.478  1.00 11.72           C  
ANISOU 5276  CB  TYR B 147     1913    947   1591    -34    -90    130       C  
ATOM   5277  CG  TYR B 147     -11.517   9.343   3.738  1.00 10.96           C  
ANISOU 5277  CG  TYR B 147     1730    947   1484    -25   -103    -10       C  
ATOM   5278  CD1 TYR B 147     -11.700  10.003   4.940  1.00 11.10           C  
ANISOU 5278  CD1 TYR B 147     1770   1038   1409   -109   -245    -41       C  
ATOM   5279  CE1 TYR B 147     -11.133   9.538   6.118  1.00 10.16           C  
ANISOU 5279  CE1 TYR B 147     1561   1160   1140   -109   -117   -143       C  
ATOM   5280  CZ  TYR B 147     -10.381   8.379   6.106  1.00 10.37           C  
ANISOU 5280  CZ  TYR B 147     1698    977   1262   -156   -171   -120       C  
ATOM   5281  OH  TYR B 147      -9.795   7.855   7.229  1.00 11.49           O  
ANISOU 5281  OH  TYR B 147     1834   1307   1225     48    -45    -49       O  
ATOM   5282  CE2 TYR B 147     -10.162   7.734   4.907  1.00 10.84           C  
ANISOU 5282  CE2 TYR B 147     1710   1069   1338    -39    -26   -101       C  
ATOM   5283  CD2 TYR B 147     -10.709   8.216   3.731  1.00 10.82           C  
ANISOU 5283  CD2 TYR B 147     1755   1003   1352    -16     74    -10       C  
ATOM   5284  C   TYR B 147     -14.382   9.819   1.162  1.00 11.57           C  
ANISOU 5284  C   TYR B 147     1981   1088   1325    -36   -137   -111       C  
ATOM   5285  O   TYR B 147     -14.755   8.959   0.367  1.00 14.15           O  
ANISOU 5285  O   TYR B 147     2599   1050   1726   -118   -512   -125       O  
ATOM   5286  N   ASN B 148     -14.494  11.130   0.925  1.00 11.80           N  
ANISOU 5286  N   ASN B 148     1923   1080   1480    -88   -449    -35       N  
ATOM   5287  CA  ASN B 148     -15.280  11.624  -0.205  1.00 12.50           C  
ANISOU 5287  CA  ASN B 148     2079   1249   1422     85   -327     76       C  
ATOM   5288  CB  ASN B 148     -15.990  12.927   0.152  1.00 13.69           C  
ANISOU 5288  CB  ASN B 148     2050   1327   1823    173   -373    -79       C  
ATOM   5289  CG  ASN B 148     -15.083  14.139   0.218  1.00 13.56           C  
ANISOU 5289  CG  ASN B 148     2243   1245   1663     91   -376   -100       C  
ATOM   5290  OD1 ASN B 148     -13.866  14.017   0.355  1.00 13.68           O  
ANISOU 5290  OD1 ASN B 148     2301   1458   1435    142   -228    143       O  
ATOM   5291  ND2 ASN B 148     -15.672  15.330   0.130  1.00 15.84           N  
ANISOU 5291  ND2 ASN B 148     2592   1275   2149    183   -337    -99       N  
ATOM   5292  C   ASN B 148     -14.472  11.737  -1.500  1.00 12.43           C  
ANISOU 5292  C   ASN B 148     2111   1141   1469    -39   -290     39       C  
ATOM   5293  O   ASN B 148     -15.026  12.148  -2.524  1.00 14.28           O  
ANISOU 5293  O   ASN B 148     2366   1518   1541     42   -348    172       O  
ATOM   5294  N  ALYS B 149     -13.189  11.377  -1.444  0.50 12.04           N  
ANISOU 5294  N  ALYS B 149     2150   1178   1246    -42   -176     75       N  
ATOM   5295  N  BLYS B 149     -13.183  11.395  -1.446  0.50 12.36           N  
ANISOU 5295  N  BLYS B 149     2137   1290   1268     47    -80    109       N  
ATOM   5296  CA ALYS B 149     -12.335  11.320  -2.619  0.50 12.32           C  
ANISOU 5296  CA ALYS B 149     2217   1134   1328    -82    -84     82       C  
ATOM   5297  CA BLYS B 149     -12.324  11.351  -2.628  0.50 12.80           C  
ANISOU 5297  CA BLYS B 149     2134   1325   1401    103     32    131       C  
ATOM   5298  CB ALYS B 149     -11.415  12.537  -2.685  0.50 14.86           C  
ANISOU 5298  CB ALYS B 149     2694   1414   1537   -414    -81     61       C  
ATOM   5299  CB BLYS B 149     -11.416  12.583  -2.712  0.50 15.10           C  
ANISOU 5299  CB BLYS B 149     2413   1652   1671   -130    122    160       C  
ATOM   5300  CG ALYS B 149     -12.145  13.855  -2.870  0.50 16.99           C  
ANISOU 5300  CG ALYS B 149     3245   1326   1883   -402     33     67       C  
ATOM   5301  CG BLYS B 149     -12.134  13.929  -2.752  0.50 17.46           C  
ANISOU 5301  CG BLYS B 149     2761   1776   2095     27    415    190       C  
ATOM   5302  CD ALYS B 149     -11.189  14.917  -3.321  0.50 19.24           C  
ANISOU 5302  CD ALYS B 149     3885   1527   1898   -769    -70    180       C  
ATOM   5303  CD BLYS B 149     -12.893  14.224  -4.028  0.50 18.48           C  
ANISOU 5303  CD BLYS B 149     3023   1963   2033    -26    459    272       C  
ATOM   5304  CE ALYS B 149     -11.733  16.324  -3.246  0.50 20.84           C  
ANISOU 5304  CE ALYS B 149     4220   1726   1972   -635     69    -10       C  
ATOM   5305  CE BLYS B 149     -13.446  15.648  -4.082  0.50 22.51           C  
ANISOU 5305  CE BLYS B 149     3394   2454   2705    507    349    489       C  
ATOM   5306  NZ ALYS B 149     -10.628  17.256  -2.969  0.50 18.52           N  
ANISOU 5306  NZ ALYS B 149     4509   1342   1184   -947    351    201       N  
ATOM   5307  NZ BLYS B 149     -14.446  15.847  -5.157  0.50 25.00           N  
ANISOU 5307  NZ BLYS B 149     4022   2730   2747    261    311    728       N  
ATOM   5308  C  ALYS B 149     -11.471  10.065  -2.531  0.50 12.57           C  
ANISOU 5308  C  ALYS B 149     2105   1290   1378    -22   -104    109       C  
ATOM   5309  C  BLYS B 149     -11.467  10.086  -2.535  0.50 12.70           C  
ANISOU 5309  C  BLYS B 149     2046   1366   1410     79    -32    142       C  
ATOM   5310  O  ALYS B 149     -11.170   9.596  -1.430  0.50 14.21           O  
ANISOU 5310  O  ALYS B 149     2377   1828   1191     91    -46     73       O  
ATOM   5311  O  BLYS B 149     -11.184   9.616  -1.424  0.50 14.40           O  
ANISOU 5311  O  BLYS B 149     2360   1912   1199    215     61     97       O  
ATOM   5312  N   ILE B 150     -11.108   9.553  -3.703  1.00 12.07           N  
ANISOU 5312  N   ILE B 150     1955   1309   1319    -90    -51    147       N  
ATOM   5313  CA  ILE B 150     -10.199   8.412  -3.847  1.00 12.02           C  
ANISOU 5313  CA  ILE B 150     1866   1263   1435   -104   -115    184       C  
ATOM   5314  CB  ILE B 150     -10.948   7.203  -4.445  1.00 12.10           C  
ANISOU 5314  CB  ILE B 150     1797   1243   1557    -51     13    138       C  
ATOM   5315  CG1 ILE B 150     -11.998   6.686  -3.466  1.00 12.71           C  
ANISOU 5315  CG1 ILE B 150     1854   1321   1653     28     53    193       C  
ATOM   5316  CG2 ILE B 150      -9.982   6.113  -4.858  1.00 13.00           C  
ANISOU 5316  CG2 ILE B 150     1988   1161   1787    -18      3    170       C  
ATOM   5317  CD1 ILE B 150     -13.042   5.802  -4.105  1.00 12.27           C  
ANISOU 5317  CD1 ILE B 150     1895   1367   1398     25   -124    213       C  
ATOM   5318  C   ILE B 150      -9.081   8.870  -4.774  1.00 13.03           C  
ANISOU 5318  C   ILE B 150     2030   1590   1331   -202     -8     59       C  
ATOM   5319  O   ILE B 150      -9.356   9.415  -5.849  1.00 13.72           O  
ANISOU 5319  O   ILE B 150     2117   1704   1390   -208     85    253       O  
ATOM   5320  N   LYS B 151      -7.841   8.587  -4.392  1.00 13.37           N  
ANISOU 5320  N   LYS B 151     2030   1716   1334   -196    -34    375       N  
ATOM   5321  CA  LYS B 151      -6.674   8.971  -5.197  1.00 13.58           C  
ANISOU 5321  CA  LYS B 151     2021   1747   1392   -175     83    336       C  
ATOM   5322  CB  LYS B 151      -5.953  10.199  -4.611  1.00 15.61           C  
ANISOU 5322  CB  LYS B 151     2329   1854   1747   -253     38    364       C  
ATOM   5323  CG  LYS B 151      -6.821  11.452  -4.503  1.00 17.22           C  
ANISOU 5323  CG  LYS B 151     2638   1762   2143   -205    162    197       C  
ATOM   5324  CD  LYS B 151      -6.056  12.713  -4.125  1.00 17.12           C  
ANISOU 5324  CD  LYS B 151     2512   1842   2150   -169    354    177       C  
ATOM   5325  CE  LYS B 151      -5.335  12.621  -2.796  1.00 18.69           C  
ANISOU 5325  CE  LYS B 151     2619   2274   2205   -505    322    273       C  
ATOM   5326  NZ  LYS B 151      -4.705  13.910  -2.423  1.00 22.91           N  
ANISOU 5326  NZ  LYS B 151     3454   2458   2789   -473    295    -82       N  
ATOM   5327  C   LYS B 151      -5.693   7.804  -5.230  1.00 13.68           C  
ANISOU 5327  C   LYS B 151     1884   1754   1559   -319     93    242       C  
ATOM   5328  O   LYS B 151      -5.421   7.172  -4.211  1.00 15.16           O  
ANISOU 5328  O   LYS B 151     1824   2289   1646    -89     43    428       O  
ATOM   5329  N   ALA B 152      -5.117   7.563  -6.406  1.00 13.33           N  
ANISOU 5329  N   ALA B 152     1728   2005   1329   -200    -77    215       N  
ATOM   5330  CA  ALA B 152      -4.137   6.465  -6.549  1.00 15.53           C  
ANISOU 5330  CA  ALA B 152     2109   2011   1778   -188    169     93       C  
ATOM   5331  CB  ALA B 152      -3.905   6.175  -8.004  1.00 18.14           C  
ANISOU 5331  CB  ALA B 152     2449   2522   1920     35   -111   -323       C  
ATOM   5332  C   ALA B 152      -2.835   6.761  -5.795  1.00 16.09           C  
ANISOU 5332  C   ALA B 152     2073   2271   1768   -183    277      5       C  
ATOM   5333  O   ALA B 152      -2.082   5.860  -5.527  1.00 18.36           O  
ANISOU 5333  O   ALA B 152     2638   2511   1827     65     94    253       O  
ATOM   5334  N   VAL B 153      -2.575   8.024  -5.454  1.00 16.41           N  
ANISOU 5334  N   VAL B 153     1971   2447   1816   -493     88   -180       N  
ATOM   5335  CA  VAL B 153      -1.344   8.329  -4.682  1.00 18.75           C  
ANISOU 5335  CA  VAL B 153     2426   2820   1878   -676    -79    -30       C  
ATOM   5336  CB  VAL B 153      -0.964   9.819  -4.767  1.00 21.29           C  
ANISOU 5336  CB  VAL B 153     2715   2924   2449   -874     65   -145       C  
ATOM   5337  CG1 VAL B 153      -0.556  10.191  -6.189  1.00 25.67           C  
ANISOU 5337  CG1 VAL B 153     3240   3612   2899   -795    437    211       C  
ATOM   5338  CG2 VAL B 153      -2.065  10.747  -4.232  1.00 21.49           C  
ANISOU 5338  CG2 VAL B 153     2595   2901   2668  -1078    234    -79       C  
ATOM   5339  C   VAL B 153      -1.499   7.880  -3.224  1.00 17.94           C  
ANISOU 5339  C   VAL B 153     2070   2879   1866   -575    -20     23       C  
ATOM   5340  O   VAL B 153      -0.485   7.878  -2.510  1.00 22.71           O  
ANISOU 5340  O   VAL B 153     2382   3880   2366   -599   -421    111       O  
ATOM   5341  N   SER B 154      -2.733   7.555  -2.781  1.00 16.91           N  
ANISOU 5341  N   SER B 154     2189   2666   1567   -462    222     83       N  
ATOM   5342  CA  SER B 154      -3.024   7.220  -1.376  1.00 18.46           C  
ANISOU 5342  CA  SER B 154     2499   2917   1596   -297     82    280       C  
ATOM   5343  CB  SER B 154      -4.288   7.887  -0.910  1.00 21.82           C  
ANISOU 5343  CB  SER B 154     3157   2993   2139     10    444    193       C  
ATOM   5344  OG  SER B 154      -4.246   9.271  -1.148  1.00 26.36           O  
ANISOU 5344  OG  SER B 154     4382   3149   2483      8   1003    271       O  
ATOM   5345  C   SER B 154      -3.187   5.714  -1.212  1.00 15.89           C  
ANISOU 5345  C   SER B 154     1912   2804   1321   -208    -34    -70       C  
ATOM   5346  O   SER B 154      -3.741   5.042  -2.089  1.00 18.61           O  
ANISOU 5346  O   SER B 154     2386   3204   1481   -301   -275   -146       O  
ATOM   5347  N   MET B 155      -2.780   5.186  -0.056  1.00 14.30           N  
ANISOU 5347  N   MET B 155     1838   2354   1239   -203    177    -88       N  
ATOM   5348  CA  MET B 155      -2.831   3.744   0.121  1.00 15.82           C  
ANISOU 5348  CA  MET B 155     2037   2289   1682    -60    196   -217       C  
ATOM   5349  CB  MET B 155      -1.870   3.289   1.217  1.00 18.52           C  
ANISOU 5349  CB  MET B 155     2321   2784   1930    -40     41    -89       C  
ATOM   5350  CG  MET B 155      -0.434   3.629   0.929  1.00 22.16           C  
ANISOU 5350  CG  MET B 155     2322   3340   2758   -129   -299   -124       C  
ATOM   5351  SD  MET B 155       0.252   2.804  -0.512  1.00 32.99           S  
ANISOU 5351  SD  MET B 155     3867   4688   3977    444    571   -147       S  
ATOM   5352  CE  MET B 155      -0.611   1.231  -0.574  1.00 32.94           C  
ANISOU 5352  CE  MET B 155     3894   4085   4535   1098   1376   -796       C  
ATOM   5353  C   MET B 155      -4.248   3.222   0.417  1.00 14.73           C  
ANISOU 5353  C   MET B 155     2035   2220   1341    -69    199   -311       C  
ATOM   5354  O   MET B 155      -4.553   2.079   0.086  1.00 16.46           O  
ANISOU 5354  O   MET B 155     2230   2222   1799   -213    276   -300       O  
ATOM   5355  N   ASN B 156      -5.112   4.029   1.028  1.00 12.74           N  
ANISOU 5355  N   ASN B 156     1733   1999   1107   -192    166   -257       N  
ATOM   5356  CA  ASN B 156      -6.502   3.604   1.210  1.00 13.64           C  
ANISOU 5356  CA  ASN B 156     1925   1869   1388   -228    142   -178       C  
ATOM   5357  CB  ASN B 156      -7.188   4.266   2.403  1.00 12.57           C  
ANISOU 5357  CB  ASN B 156     1706   1741   1329   -169    197    -78       C  
ATOM   5358  CG  ASN B 156      -8.584   3.721   2.636  1.00 13.64           C  
ANISOU 5358  CG  ASN B 156     1756   1721   1703   -266    308   -172       C  
ATOM   5359  OD1 ASN B 156      -8.790   2.509   2.575  1.00 13.39           O  
ANISOU 5359  OD1 ASN B 156     1722   1693   1673    -98   -190   -103       O  
ATOM   5360  ND2 ASN B 156      -9.546   4.589   2.873  1.00 14.49           N  
ANISOU 5360  ND2 ASN B 156     2140   1720   1644   -182    288   -201       N  
ATOM   5361  C   ASN B 156      -7.254   3.919  -0.084  1.00 13.82           C  
ANISOU 5361  C   ASN B 156     2165   1787   1297    -74    107   -297       C  
ATOM   5362  O   ASN B 156      -7.780   5.003  -0.277  1.00 16.49           O  
ANISOU 5362  O   ASN B 156     2791   1873   1598    146     78   -289       O  
ATOM   5363  N   ASN B 157      -7.231   2.962  -0.995  1.00 11.57           N  
ANISOU 5363  N   ASN B 157     1815   1400   1181     46    134   -111       N  
ATOM   5364  CA  ASN B 157      -7.692   3.180  -2.351  1.00 11.45           C  
ANISOU 5364  CA  ASN B 157     1711   1360   1279   -122     47      4       C  
ATOM   5365  CB  ASN B 157      -6.520   3.527  -3.277  1.00 12.33           C  
ANISOU 5365  CB  ASN B 157     1839   1418   1426      9    173     81       C  
ATOM   5366  CG  ASN B 157      -6.895   3.510  -4.735  1.00 11.28           C  
ANISOU 5366  CG  ASN B 157     1657   1164   1464    -72     91    -57       C  
ATOM   5367  OD1 ASN B 157      -8.102   3.505  -5.058  1.00 11.76           O  
ANISOU 5367  OD1 ASN B 157     1720   1214   1534   -156    -18    111       O  
ATOM   5368  ND2 ASN B 157      -5.874   3.492  -5.607  1.00 11.72           N  
ANISOU 5368  ND2 ASN B 157     1638   1365   1448     10     77    165       N  
ATOM   5369  C   ASN B 157      -8.383   1.904  -2.819  1.00 11.29           C  
ANISOU 5369  C   ASN B 157     1542   1362   1384    -51    -39    -65       C  
ATOM   5370  O   ASN B 157      -7.713   0.918  -3.146  1.00 11.67           O  
ANISOU 5370  O   ASN B 157     1503   1620   1309     93    -70    -28       O  
ATOM   5371  N   PRO B 158      -9.725   1.878  -2.887  1.00 10.39           N  
ANISOU 5371  N   PRO B 158     1481   1089   1378    -95    -87    -48       N  
ATOM   5372  CA  PRO B 158     -10.421   0.654  -3.265  1.00 11.22           C  
ANISOU 5372  CA  PRO B 158     1598   1113   1550   -230    -88     52       C  
ATOM   5373  CB  PRO B 158     -11.896   0.969  -3.004  1.00 11.79           C  
ANISOU 5373  CB  PRO B 158     1646   1474   1358   -220    -16    -55       C  
ATOM   5374  CG  PRO B 158     -11.977   2.434  -3.233  1.00 13.08           C  
ANISOU 5374  CG  PRO B 158     1724   1504   1742    -36   -110   -133       C  
ATOM   5375  CD  PRO B 158     -10.669   2.988  -2.648  1.00 11.60           C  
ANISOU 5375  CD  PRO B 158     1503   1300   1605     24    -96    -76       C  
ATOM   5376  C   PRO B 158     -10.208   0.277  -4.734  1.00 10.84           C  
ANISOU 5376  C   PRO B 158     1533   1057   1526   -186    -31    142       C  
ATOM   5377  O   PRO B 158     -10.612  -0.814  -5.150  1.00 12.07           O  
ANISOU 5377  O   PRO B 158     1846   1211   1528   -363    -69    -10       O  
ATOM   5378  N   TYR B 159      -9.621   1.175  -5.535  1.00 10.03           N  
ANISOU 5378  N   TYR B 159     1561    795   1455   -130     14     64       N  
ATOM   5379  CA  TYR B 159      -9.337   0.830  -6.932  1.00 10.74           C  
ANISOU 5379  CA  TYR B 159     1660   1052   1367    -33    -99    -71       C  
ATOM   5380  CB  TYR B 159      -9.686   1.976  -7.889  1.00 10.62           C  
ANISOU 5380  CB  TYR B 159     1656   1164   1213   -146     16     12       C  
ATOM   5381  CG  TYR B 159     -11.097   2.475  -7.701  1.00 10.43           C  
ANISOU 5381  CG  TYR B 159     1558   1131   1274   -246    -64     32       C  
ATOM   5382  CD1 TYR B 159     -12.145   1.583  -7.536  1.00 10.34           C  
ANISOU 5382  CD1 TYR B 159     1437   1134   1356   -231   -187    124       C  
ATOM   5383  CE1 TYR B 159     -13.432   2.023  -7.274  1.00 10.89           C  
ANISOU 5383  CE1 TYR B 159     1590   1222   1325   -147    -66     -5       C  
ATOM   5384  CZ  TYR B 159     -13.709   3.374  -7.216  1.00 10.94           C  
ANISOU 5384  CZ  TYR B 159     1505   1263   1386   -106   -186     95       C  
ATOM   5385  OH  TYR B 159     -14.990   3.756  -6.919  1.00 10.71           O  
ANISOU 5385  OH  TYR B 159     1600   1396   1074    -17    -64    147       O  
ATOM   5386  CE2 TYR B 159     -12.679   4.281  -7.429  1.00 11.12           C  
ANISOU 5386  CE2 TYR B 159     1756   1082   1384    -97     15    142       C  
ATOM   5387  CD2 TYR B 159     -11.393   3.834  -7.650  1.00 10.95           C  
ANISOU 5387  CD2 TYR B 159     1669   1134   1357   -201     29    122       C  
ATOM   5388  C   TYR B 159      -7.918   0.282  -7.101  1.00 10.98           C  
ANISOU 5388  C   TYR B 159     1609   1085   1475   -119    -25     23       C  
ATOM   5389  O   TYR B 159      -7.520  -0.000  -8.229  1.00 12.01           O  
ANISOU 5389  O   TYR B 159     1708   1396   1458    120     66     68       O  
ATOM   5390  N   ARG B 160      -7.199   0.048  -6.002  1.00 11.15           N  
ANISOU 5390  N   ARG B 160     1752   1078   1405     14     68     50       N  
ATOM   5391  CA  ARG B 160      -6.016  -0.805  -6.070  1.00 11.42           C  
ANISOU 5391  CA  ARG B 160     1724   1196   1419     95     80     32       C  
ATOM   5392  CB  ARG B 160      -5.430  -1.046  -4.677  1.00 12.86           C  
ANISOU 5392  CB  ARG B 160     1809   1500   1574    280     -3     60       C  
ATOM   5393  CG  ARG B 160      -4.599   0.117  -4.171  1.00 15.85           C  
ANISOU 5393  CG  ARG B 160     2008   2187   1825     41    -88    -82       C  
ATOM   5394  CD  ARG B 160      -4.315   0.106  -2.674  1.00 19.73           C  
ANISOU 5394  CD  ARG B 160     2722   2978   1793    343    -15   -131       C  
ATOM   5395  NE  ARG B 160      -3.326  -0.834  -2.247  1.00 23.61           N  
ANISOU 5395  NE  ARG B 160     2935   3993   2043    838   -141    -45       N  
ATOM   5396  CZ  ARG B 160      -3.024  -1.159  -0.968  1.00 23.31           C  
ANISOU 5396  CZ  ARG B 160     3035   3550   2271   1177   -508    180       C  
ATOM   5397  NH1 ARG B 160      -3.544  -0.508   0.040  1.00 28.40           N  
ANISOU 5397  NH1 ARG B 160     3297   5107   2385   1099   -134     -1       N  
ATOM   5398  NH2 ARG B 160      -2.246  -2.206  -0.717  1.00 26.09           N  
ANISOU 5398  NH2 ARG B 160     3258   3475   3179   1089   -781    -41       N  
ATOM   5399  C   ARG B 160      -6.405  -2.129  -6.726  1.00 11.93           C  
ANISOU 5399  C   ARG B 160     1683   1291   1555    -22    -10     69       C  
ATOM   5400  O   ARG B 160      -7.361  -2.791  -6.320  1.00 13.45           O  
ANISOU 5400  O   ARG B 160     1737   1302   2069    -23    108    -35       O  
ATOM   5401  N   GLN B 161      -5.636  -2.530  -7.729  1.00 11.28           N  
ANISOU 5401  N   GLN B 161     1519   1093   1672     -2    -58     38       N  
ATOM   5402  CA  GLN B 161      -5.882  -3.822  -8.321  1.00 11.84           C  
ANISOU 5402  CA  GLN B 161     1670   1177   1649     26    -93     -9       C  
ATOM   5403  CB  GLN B 161      -5.245  -3.900  -9.702  1.00 15.30           C  
ANISOU 5403  CB  GLN B 161     2456   1492   1864    -87    171    -47       C  
ATOM   5404  CG  GLN B 161      -3.752  -3.833  -9.745  1.00 16.48           C  
ANISOU 5404  CG  GLN B 161     2541   1746   1972   -139    158    149       C  
ATOM   5405  CD  GLN B 161      -3.322  -3.867 -11.207  1.00 20.68           C  
ANISOU 5405  CD  GLN B 161     2896   2733   2228   -290    814   1044       C  
ATOM   5406  OE1 GLN B 161      -3.812  -3.111 -12.076  1.00 23.99           O  
ANISOU 5406  OE1 GLN B 161     3197   3572   2345   -295    182    807       O  
ATOM   5407  NE2 GLN B 161      -2.321  -4.644 -11.498  1.00 24.00           N  
ANISOU 5407  NE2 GLN B 161     4206   2487   2423    165   1040    862       N  
ATOM   5408  C   GLN B 161      -5.422  -4.944  -7.380  1.00 11.70           C  
ANISOU 5408  C   GLN B 161     1593   1265   1585    106    -15     17       C  
ATOM   5409  O   GLN B 161      -4.819  -4.724  -6.321  1.00 12.77           O  
ANISOU 5409  O   GLN B 161     1591   1573   1685     61   -176      3       O  
ATOM   5410  N   GLY B 162      -5.754  -6.171  -7.767  1.00 10.93           N  
ANISOU 5410  N   GLY B 162     1545   1223   1382    124    -86     39       N  
ATOM   5411  CA  GLY B 162      -5.412  -7.351  -6.961  1.00 11.08           C  
ANISOU 5411  CA  GLY B 162     1530   1181   1499     71     80    157       C  
ATOM   5412  C   GLY B 162      -3.938  -7.435  -6.602  1.00 11.70           C  
ANISOU 5412  C   GLY B 162     1593   1235   1616    -30     51     36       C  
ATOM   5413  O   GLY B 162      -3.575  -7.724  -5.450  1.00 12.10           O  
ANISOU 5413  O   GLY B 162     1656   1267   1673     61     50     83       O  
ATOM   5414  N   THR B 163      -3.061  -7.221  -7.586  1.00 11.49           N  
ANISOU 5414  N   THR B 163     1521   1248   1594    100     54    277       N  
ATOM   5415  CA  THR B 163      -1.613  -7.316  -7.323  1.00 12.69           C  
ANISOU 5415  CA  THR B 163     1537   1594   1687     67     31    182       C  
ATOM   5416  CB  THR B 163      -0.773  -7.252  -8.601  1.00 13.51           C  
ANISOU 5416  CB  THR B 163     1740   1651   1742     87    173    234       C  
ATOM   5417  OG1 THR B 163      -0.991  -5.983  -9.220  1.00 14.87           O  
ANISOU 5417  OG1 THR B 163     2121   1704   1822    103    165    374       O  
ATOM   5418  CG2 THR B 163      -1.070  -8.363  -9.581  1.00 14.65           C  
ANISOU 5418  CG2 THR B 163     1841   1839   1885    136    216     48       C  
ATOM   5419  C   THR B 163      -1.130  -6.210  -6.368  1.00 12.37           C  
ANISOU 5419  C   THR B 163     1385   1400   1915     91    -24    202       C  
ATOM   5420  O   THR B 163       0.012  -6.279  -5.894  1.00 12.93           O  
ANISOU 5420  O   THR B 163     1352   1599   1962    -21    -33    142       O  
ATOM   5421  N   GLU B 164      -1.996  -5.230  -6.071  1.00 11.98           N  
ANISOU 5421  N   GLU B 164     1336   1335   1878    137    -95    194       N  
ATOM   5422  CA  GLU B 164      -1.685  -4.152  -5.143  1.00 12.47           C  
ANISOU 5422  CA  GLU B 164     1438   1350   1950    -10    -48    184       C  
ATOM   5423  CB  GLU B 164      -2.012  -2.796  -5.797  1.00 14.46           C  
ANISOU 5423  CB  GLU B 164     1581   1483   2430    180   -282    292       C  
ATOM   5424  CG  GLU B 164      -1.289  -2.554  -7.098  1.00 16.38           C  
ANISOU 5424  CG  GLU B 164     2272   1538   2414   -194   -364    363       C  
ATOM   5425  CD  GLU B 164       0.189  -2.290  -7.033  1.00 20.13           C  
ANISOU 5425  CD  GLU B 164     2215   2956   2477    131    274    869       C  
ATOM   5426  OE1 GLU B 164       0.727  -2.251  -5.927  1.00 19.47           O  
ANISOU 5426  OE1 GLU B 164     1627   2886   2883   -235   -311   1146       O  
ATOM   5427  OE2 GLU B 164       0.800  -2.137  -8.147  1.00 26.82           O  
ANISOU 5427  OE2 GLU B 164     3088   4128   2973    527   1067   1041       O  
ATOM   5428  C   GLU B 164      -2.448  -4.283  -3.831  1.00 13.09           C  
ANISOU 5428  C   GLU B 164     1557   1364   2052   -121    -13    -64       C  
ATOM   5429  O   GLU B 164      -2.343  -3.395  -2.976  1.00 15.20           O  
ANISOU 5429  O   GLU B 164     1940   1677   2158   -242    150   -274       O  
ATOM   5430  N   SER B 165      -3.191  -5.381  -3.644  1.00 11.40           N  
ANISOU 5430  N   SER B 165     1474   1199   1656     39     -2    -30       N  
ATOM   5431  CA  SER B 165      -4.090  -5.550  -2.505  1.00 12.22           C  
ANISOU 5431  CA  SER B 165     1672   1409   1562    -44    -44     66       C  
ATOM   5432  CB  SER B 165      -5.513  -5.623  -2.968  1.00 12.68           C  
ANISOU 5432  CB  SER B 165     1692   1626   1497   -113     -6    154       C  
ATOM   5433  OG  SER B 165      -5.939  -4.448  -3.642  1.00 13.11           O  
ANISOU 5433  OG  SER B 165     1615   1652   1713    -38    -99    185       O  
ATOM   5434  C   SER B 165      -3.723  -6.820  -1.726  1.00 11.93           C  
ANISOU 5434  C   SER B 165     1620   1531   1378    207   -284    -86       C  
ATOM   5435  O   SER B 165      -3.848  -7.921  -2.247  1.00 13.78           O  
ANISOU 5435  O   SER B 165     2209   1491   1534      1   -431    -40       O  
ATOM   5436  N   THR B 166      -3.272  -6.669  -0.489  1.00 11.62           N  
ANISOU 5436  N   THR B 166     1490   1441   1484    222   -392   -276       N  
ATOM   5437  CA ATHR B 166      -2.934  -7.854   0.329  0.50 10.92           C  
ANISOU 5437  CA ATHR B 166     1406   1355   1387    352   -151   -316       C  
ATOM   5438  CA BTHR B 166      -2.932  -7.828   0.332  0.50 12.85           C  
ANISOU 5438  CA BTHR B 166     1722   1584   1576    184   -135    -69       C  
ATOM   5439  CB ATHR B 166      -2.083  -7.566   1.571  0.50 10.10           C  
ANISOU 5439  CB ATHR B 166     1096   1285   1453    522    -86   -442       C  
ATOM   5440  CB BTHR B 166      -1.992  -7.387   1.459  0.50 16.42           C  
ANISOU 5440  CB BTHR B 166     1914   2345   1979     -8   -347   -124       C  
ATOM   5441  OG1ATHR B 166      -2.761  -6.563   2.332  0.50  9.27           O  
ANISOU 5441  OG1ATHR B 166      993   1246   1281    449   -172   -493       O  
ATOM   5442  OG1BTHR B 166      -0.871  -6.696   0.886  0.50 18.62           O  
ANISOU 5442  OG1BTHR B 166     2099   2692   2282   -277   -415    -27       O  
ATOM   5443  CG2ATHR B 166      -0.650  -7.186   1.253  0.50 10.61           C  
ANISOU 5443  CG2ATHR B 166      988   1397   1645    545   -212   -432       C  
ATOM   5444  CG2BTHR B 166      -1.479  -8.547   2.276  0.50 19.22           C  
ANISOU 5444  CG2BTHR B 166     2264   2555   2483    131   -241     91       C  
ATOM   5445  C   THR B 166      -4.201  -8.555   0.802  1.00 12.14           C  
ANISOU 5445  C   THR B 166     1571   1561   1477    203   -229   -246       C  
ATOM   5446  O   THR B 166      -4.181  -9.771   1.014  1.00 12.47           O  
ANISOU 5446  O   THR B 166     1512   1509   1716    262    -97   -189       O  
ATOM   5447  N   ASP B 167      -5.264  -7.789   1.019  1.00 11.88           N  
ANISOU 5447  N   ASP B 167     1451   1742   1320    130   -164   -108       N  
ATOM   5448  CA  ASP B 167      -6.540  -8.316   1.516  1.00 12.36           C  
ANISOU 5448  CA  ASP B 167     1391   1942   1362    220   -118     -8       C  
ATOM   5449  CB  ASP B 167      -6.938  -7.674   2.844  1.00 15.58           C  
ANISOU 5449  CB  ASP B 167     1968   2644   1305    437   -130    -37       C  
ATOM   5450  CG  ASP B 167      -8.239  -8.191   3.454  1.00 20.62           C  
ANISOU 5450  CG  ASP B 167     2370   3600   1861    140    128    108       C  
ATOM   5451  OD1 ASP B 167      -9.026  -8.954   2.759  1.00 20.20           O  
ANISOU 5451  OD1 ASP B 167     2764   3028   1883    534    181    144       O  
ATOM   5452  OD2 ASP B 167      -8.477  -7.828   4.637  1.00 27.73           O  
ANISOU 5452  OD2 ASP B 167     3611   4724   2198    500    -58   -485       O  
ATOM   5453  C   ASP B 167      -7.611  -8.009   0.477  1.00 12.05           C  
ANISOU 5453  C   ASP B 167     1599   1631   1346    277   -218   -109       C  
ATOM   5454  O   ASP B 167      -7.980  -6.827   0.276  1.00 12.18           O  
ANISOU 5454  O   ASP B 167     1622   1447   1557    278   -147   -363       O  
ATOM   5455  N   SER B 168      -8.096  -9.054  -0.207  1.00 11.53           N  
ANISOU 5455  N   SER B 168     1417   1415   1549    106   -164    126       N  
ATOM   5456  CA  SER B 168      -9.037  -8.870  -1.296  1.00 11.17           C  
ANISOU 5456  CA  SER B 168     1568   1369   1306     95   -118     98       C  
ATOM   5457  CB  SER B 168      -9.426 -10.181  -1.901  1.00 10.87           C  
ANISOU 5457  CB  SER B 168     1551   1224   1354    213   -132     44       C  
ATOM   5458  OG  SER B 168     -10.089 -11.020  -0.979  1.00 13.22           O  
ANISOU 5458  OG  SER B 168     1846   1439   1737    -19      1     88       O  
ATOM   5459  C   SER B 168     -10.283  -8.105  -0.912  1.00 10.64           C  
ANISOU 5459  C   SER B 168     1549   1158   1334    124   -241    198       C  
ATOM   5460  O   SER B 168     -10.862  -7.420  -1.772  1.00 10.91           O  
ANISOU 5460  O   SER B 168     1526   1225   1393    245   -421     94       O  
ATOM   5461  N   ARG B 169     -10.730  -8.197   0.343  1.00 11.96           N  
ANISOU 5461  N   ARG B 169     1687   1405   1450    304    -50    186       N  
ATOM   5462  CA AARG B 169     -12.014  -7.571   0.717  0.50 13.50           C  
ANISOU 5462  CA AARG B 169     1717   1622   1790    317     74    208       C  
ATOM   5463  CA BARG B 169     -11.997  -7.560   0.765  0.50 13.60           C  
ANISOU 5463  CA BARG B 169     1682   1647   1836    301    122    169       C  
ATOM   5464  CB AARG B 169     -12.456  -8.058   2.102  0.50 17.30           C  
ANISOU 5464  CB AARG B 169     2254   2160   2157    258    365    555       C  
ATOM   5465  CB BARG B 169     -12.341  -7.870   2.227  0.50 16.78           C  
ANISOU 5465  CB BARG B 169     1859   2352   2164    365    635    319       C  
ATOM   5466  CG AARG B 169     -13.621  -7.300   2.722  0.50 21.91           C  
ANISOU 5466  CG AARG B 169     2783   2595   2946    617    434    402       C  
ATOM   5467  CG BARG B 169     -12.467  -9.351   2.533  0.50 21.07           C  
ANISOU 5467  CG BARG B 169     2521   2437   3047    424    698    218       C  
ATOM   5468  CD AARG B 169     -13.875  -7.738   4.158  0.50 25.73           C  
ANISOU 5468  CD AARG B 169     3354   3271   3148    295    563    628       C  
ATOM   5469  CD BARG B 169     -12.534  -9.672   4.015  0.50 24.85           C  
ANISOU 5469  CD BARG B 169     3269   3128   3043    205    647    120       C  
ATOM   5470  NE AARG B 169     -12.655  -7.732   4.945  0.50 29.38           N  
ANISOU 5470  NE AARG B 169     3615   3770   3777    327    276    494       N  
ATOM   5471  NE BARG B 169     -11.611  -8.891   4.832  0.50 30.16           N  
ANISOU 5471  NE BARG B 169     3773   4079   3604    147    171    -10       N  
ATOM   5472  CZ AARG B 169     -12.189  -6.694   5.625  0.50 30.47           C  
ANISOU 5472  CZ AARG B 169     3673   4411   3491    288    254    225       C  
ATOM   5473  CZ BARG B 169     -10.742  -9.392   5.697  0.50 28.46           C  
ANISOU 5473  CZ BARG B 169     2814   4082   3917    163    112   -389       C  
ATOM   5474  NH1AARG B 169     -10.913  -6.661   5.976  0.50 31.79           N  
ANISOU 5474  NH1AARG B 169     3178   5181   3720   -858   1079    515       N  
ATOM   5475  NH1BARG B 169     -10.108  -8.580   6.523  0.50 34.86           N  
ANISOU 5475  NH1BARG B 169     4041   4682   4521   -556     39   -648       N  
ATOM   5476  NH2AARG B 169     -12.982  -5.681   5.913  0.50 30.53           N  
ANISOU 5476  NH2AARG B 169     3184   5451   2965    317   1501   -173       N  
ATOM   5477  NH2BARG B 169     -10.517 -10.692   5.747  0.50 33.39           N  
ANISOU 5477  NH2BARG B 169     4166   4041   4478   -198    210   -602       N  
ATOM   5478  C   ARG B 169     -11.918  -6.035   0.622  1.00 12.77           C  
ANISOU 5478  C   ARG B 169     1620   1594   1638    204    113    -12       C  
ATOM   5479  O   ARG B 169     -12.944  -5.364   0.548  1.00 13.86           O  
ANISOU 5479  O   ARG B 169     1718   1767   1778    328    -50     33       O  
ATOM   5480  N   MET B 170     -10.690  -5.482   0.602  1.00 11.78           N  
ANISOU 5480  N   MET B 170     1576   1367   1530    235    -89    -42       N  
ATOM   5481  CA AMET B 170     -10.515  -4.020   0.580  0.50 12.19           C  
ANISOU 5481  CA AMET B 170     1728   1382   1521     71   -121   -207       C  
ATOM   5482  CA BMET B 170     -10.478  -4.019   0.575  0.50 12.04           C  
ANISOU 5482  CA BMET B 170     1671   1372   1530    117   -101   -234       C  
ATOM   5483  CB AMET B 170      -9.127  -3.623   1.085  0.50 13.44           C  
ANISOU 5483  CB AMET B 170     1937   1652   1515     90   -341   -273       C  
ATOM   5484  CB BMET B 170      -9.051  -3.643   0.996  0.50 13.41           C  
ANISOU 5484  CB BMET B 170     1793   1618   1682    183   -265   -376       C  
ATOM   5485  CG AMET B 170      -8.870  -4.098   2.487  0.50 14.97           C  
ANISOU 5485  CG AMET B 170     2302   1754   1631    226   -295   -107       C  
ATOM   5486  CG BMET B 170      -8.718  -4.045   2.392  0.50 14.41           C  
ANISOU 5486  CG BMET B 170     2040   1713   1722    378   -134   -296       C  
ATOM   5487  SD AMET B 170     -10.128  -3.536   3.680  0.50 15.39           S  
ANISOU 5487  SD AMET B 170     2439   1865   1543     55   -199    107       S  
ATOM   5488  SD BMET B 170      -9.688  -3.112   3.584  0.50 14.77           S  
ANISOU 5488  SD BMET B 170     2105   1691   1815    341   -153   -397       S  
ATOM   5489  CE AMET B 170      -9.194  -3.954   5.148  0.50 15.11           C  
ANISOU 5489  CE AMET B 170     2609   1747   1383    486   -130    -14       C  
ATOM   5490  CE BMET B 170     -10.830  -4.404   4.079  0.50 15.95           C  
ANISOU 5490  CE BMET B 170     2191   2164   1704    267    280   -349       C  
ATOM   5491  C   MET B 170     -10.698  -3.444  -0.829  1.00 11.24           C  
ANISOU 5491  C   MET B 170     1629   1188   1451     52   -210   -314       C  
ATOM   5492  O   MET B 170     -10.837  -2.214  -0.992  1.00 12.62           O  
ANISOU 5492  O   MET B 170     1916   1243   1635    128    -52   -293       O  
ATOM   5493  N   SER B 171     -10.693  -4.303  -1.854  1.00 10.52           N  
ANISOU 5493  N   SER B 171     1754   1001   1242     55    -80   -119       N  
ATOM   5494  CA  SER B 171     -10.603  -3.838  -3.240  1.00 10.40           C  
ANISOU 5494  CA  SER B 171     1623   1086   1239     17   -198   -110       C  
ATOM   5495  CB  SER B 171      -9.531  -4.613  -3.984  1.00 11.88           C  
ANISOU 5495  CB  SER B 171     1630   1502   1381    205   -160    -51       C  
ATOM   5496  OG  SER B 171      -9.497  -4.250  -5.366  1.00 13.01           O  
ANISOU 5496  OG  SER B 171     1724   1759   1458     46    -62    107       O  
ATOM   5497  C   SER B 171     -11.930  -3.975  -3.995  1.00 10.04           C  
ANISOU 5497  C   SER B 171     1535   1009   1271     66   -156    -40       C  
ATOM   5498  O   SER B 171     -12.531  -5.063  -4.021  1.00 11.02           O  
ANISOU 5498  O   SER B 171     1754   1057   1375    -54   -347    108       O  
ATOM   5499  N   ARG B 172     -12.302  -2.894  -4.707  1.00  9.44           N  
ANISOU 5499  N   ARG B 172     1464   1013   1107      9   -126    -70       N  
ATOM   5500  CA  ARG B 172     -13.314  -2.916  -5.760  1.00  9.66           C  
ANISOU 5500  CA  ARG B 172     1415   1104   1151    -94   -108     46       C  
ATOM   5501  CB  ARG B 172     -14.349  -1.821  -5.532  1.00  9.50           C  
ANISOU 5501  CB  ARG B 172     1339   1091   1180   -167   -121      5       C  
ATOM   5502  CG  ARG B 172     -14.989  -1.838  -4.148  1.00  9.65           C  
ANISOU 5502  CG  ARG B 172     1283   1210   1172   -139   -130    101       C  
ATOM   5503  CD  ARG B 172     -16.229  -0.942  -4.038  1.00  9.76           C  
ANISOU 5503  CD  ARG B 172     1461   1188   1059    -69   -102     38       C  
ATOM   5504  NE  ARG B 172     -15.971   0.450  -4.437  1.00  9.81           N  
ANISOU 5504  NE  ARG B 172     1569   1206    950    -31   -140    152       N  
ATOM   5505  CZ  ARG B 172     -15.651   1.464  -3.630  1.00 10.20           C  
ANISOU 5505  CZ  ARG B 172     1561   1096   1217    -24   -168    155       C  
ATOM   5506  NH1 ARG B 172     -15.514   1.262  -2.325  1.00 10.33           N  
ANISOU 5506  NH1 ARG B 172     1446   1296   1181    -25    -49    161       N  
ATOM   5507  NH2 ARG B 172     -15.423   2.665  -4.169  1.00 10.42           N  
ANISOU 5507  NH2 ARG B 172     1566   1093   1300    -24   -102    223       N  
ATOM   5508  C   ARG B 172     -12.640  -2.725  -7.128  1.00  9.41           C  
ANISOU 5508  C   ARG B 172     1321   1082   1172    -59    -63     56       C  
ATOM   5509  O   ARG B 172     -13.325  -2.354  -8.111  1.00 10.31           O  
ANISOU 5509  O   ARG B 172     1471   1182   1263    -38   -173     43       O  
ATOM   5510  N   GLY B 173     -11.318  -2.973  -7.184  1.00  9.78           N  
ANISOU 5510  N   GLY B 173     1415   1149   1149     14   -124     70       N  
ATOM   5511  CA  GLY B 173     -10.512  -2.719  -8.358  1.00 10.38           C  
ANISOU 5511  CA  GLY B 173     1353   1296   1295    -47    -67     12       C  
ATOM   5512  C   GLY B 173     -10.455  -3.911  -9.296  1.00 10.20           C  
ANISOU 5512  C   GLY B 173     1351   1228   1294    -67    -43     52       C  
ATOM   5513  O   GLY B 173     -11.066  -4.953  -9.073  1.00 10.02           O  
ANISOU 5513  O   GLY B 173     1466   1241   1099   -168   -108    -11       O  
ATOM   5514  N   LEU B 174      -9.690  -3.734 -10.372  1.00 10.45           N  
ANISOU 5514  N   LEU B 174     1570   1135   1265    -93     26     26       N  
ATOM   5515  CA  LEU B 174      -9.549  -4.743 -11.389  1.00 10.45           C  
ANISOU 5515  CA  LEU B 174     1583   1182   1206      7    -37     47       C  
ATOM   5516  CB  LEU B 174      -8.994  -4.118 -12.659  1.00 11.69           C  
ANISOU 5516  CB  LEU B 174     1689   1358   1394    -79    119     82       C  
ATOM   5517  CG  LEU B 174      -9.782  -2.928 -13.205  1.00 12.19           C  
ANISOU 5517  CG  LEU B 174     1888   1391   1351    -51     12    143       C  
ATOM   5518  CD1 LEU B 174      -9.118  -2.344 -14.435  1.00 14.66           C  
ANISOU 5518  CD1 LEU B 174     2207   1794   1570   -243     73    263       C  
ATOM   5519  CD2 LEU B 174     -11.229  -3.296 -13.479  1.00 12.77           C  
ANISOU 5519  CD2 LEU B 174     1924   1431   1494    112     11    232       C  
ATOM   5520  C   LEU B 174      -8.653  -5.871 -10.862  1.00 10.69           C  
ANISOU 5520  C   LEU B 174     1448   1317   1297     57    -41     89       C  
ATOM   5521  O   LEU B 174      -7.805  -5.686 -10.005  1.00 12.58           O  
ANISOU 5521  O   LEU B 174     1757   1285   1737     28   -321    -66       O  
ATOM   5522  N   GLY B 175      -8.841  -7.065 -11.414  1.00 11.04           N  
ANISOU 5522  N   GLY B 175     1434   1341   1417     10    -47     79       N  
ATOM   5523  CA  GLY B 175      -7.934  -8.152 -11.161  1.00 11.47           C  
ANISOU 5523  CA  GLY B 175     1575   1371   1412     79    -36     50       C  
ATOM   5524  C   GLY B 175      -7.906  -8.623  -9.723  1.00 10.92           C  
ANISOU 5524  C   GLY B 175     1487   1251   1408    122    -93     35       C  
ATOM   5525  O   GLY B 175      -6.841  -9.038  -9.254  1.00 10.86           O  
ANISOU 5525  O   GLY B 175     1463   1277   1384    107    -15    194       O  
ATOM   5526  N   CYS B 176      -9.059  -8.563  -9.025  1.00 10.48           N  
ANISOU 5526  N   CYS B 176     1329   1337   1314    125   -190    143       N  
ATOM   5527  CA  CYS B 176      -9.066  -8.910  -7.605  1.00 10.03           C  
ANISOU 5527  CA  CYS B 176     1403   1014   1394    137    -99    152       C  
ATOM   5528  CB  CYS B 176      -9.041  -7.673  -6.708  1.00  9.83           C  
ANISOU 5528  CB  CYS B 176     1446    820   1469    -54   -185    228       C  
ATOM   5529  SG  CYS B 176      -8.695  -8.095  -4.986  1.00 12.08           S  
ANISOU 5529  SG  CYS B 176     1780   1418   1392    -28   -123     14       S  
ATOM   5530  C   CYS B 176     -10.247  -9.840  -7.300  1.00 10.47           C  
ANISOU 5530  C   CYS B 176     1479   1134   1363     50   -121     96       C  
ATOM   5531  O   CYS B 176     -10.021 -11.035  -7.121  1.00 11.32           O  
ANISOU 5531  O   CYS B 176     1520   1213   1565    109     74    207       O  
ATOM   5532  N   ASN B 177     -11.475  -9.303  -7.250  1.00 10.28           N  
ANISOU 5532  N   ASN B 177     1495   1010   1398    -10     14    118       N  
ATOM   5533  CA  ASN B 177     -12.644 -10.117  -6.872  1.00  9.06           C  
ANISOU 5533  CA  ASN B 177     1395   1019   1025     54    -95    129       C  
ATOM   5534  CB  ASN B 177     -13.439  -9.425  -5.763  1.00 10.26           C  
ANISOU 5534  CB  ASN B 177     1668   1067   1161    119    -24    -47       C  
ATOM   5535  CG  ASN B 177     -12.595  -9.199  -4.531  1.00 10.61           C  
ANISOU 5535  CG  ASN B 177     1657   1093   1278    100   -122     54       C  
ATOM   5536  OD1 ASN B 177     -11.837 -10.089  -4.135  1.00 11.92           O  
ANISOU 5536  OD1 ASN B 177     1991   1038   1499    145   -349    -10       O  
ATOM   5537  ND2 ASN B 177     -12.709  -8.015  -3.935  1.00 11.26           N  
ANISOU 5537  ND2 ASN B 177     1716   1045   1515    155    -56      1       N  
ATOM   5538  C   ASN B 177     -13.575 -10.458  -8.038  1.00  9.96           C  
ANISOU 5538  C   ASN B 177     1661   1000   1123     28   -258    195       C  
ATOM   5539  O   ASN B 177     -14.386 -11.366  -7.878  1.00 10.52           O  
ANISOU 5539  O   ASN B 177     1618   1175   1203    -15    -89     70       O  
ATOM   5540  N   TYR B 178     -13.500  -9.712  -9.150  1.00  9.72           N  
ANISOU 5540  N   TYR B 178     1574   1060   1058   -131   -267    179       N  
ATOM   5541  CA  TYR B 178     -14.415  -9.936 -10.280  1.00  9.49           C  
ANISOU 5541  CA  TYR B 178     1531   1014   1059   -165   -251    147       C  
ATOM   5542  CB  TYR B 178     -15.487  -8.848 -10.364  1.00 10.38           C  
ANISOU 5542  CB  TYR B 178     1568   1184   1189    -60   -154    151       C  
ATOM   5543  CG  TYR B 178     -14.966  -7.430 -10.437  1.00 10.42           C  
ANISOU 5543  CG  TYR B 178     1570   1149   1237      9   -164    147       C  
ATOM   5544  CD1 TYR B 178     -14.528  -6.865 -11.625  1.00 10.40           C  
ANISOU 5544  CD1 TYR B 178     1591   1260   1100     59   -237     47       C  
ATOM   5545  CE1 TYR B 178     -14.001  -5.591 -11.672  1.00 11.29           C  
ANISOU 5545  CE1 TYR B 178     1779   1295   1215     49   -218    -33       C  
ATOM   5546  CZ  TYR B 178     -13.923  -4.825 -10.525  1.00 10.32           C  
ANISOU 5546  CZ  TYR B 178     1728   1000   1193    -79   -249     30       C  
ATOM   5547  OH  TYR B 178     -13.412  -3.544 -10.597  1.00 10.46           O  
ANISOU 5547  OH  TYR B 178     1707    920   1345     24    -61    182       O  
ATOM   5548  CE2 TYR B 178     -14.331  -5.381  -9.326  1.00 10.64           C  
ANISOU 5548  CE2 TYR B 178     1672   1011   1360    -11      6     -8       C  
ATOM   5549  CD2 TYR B 178     -14.852  -6.661  -9.295  1.00  9.92           C  
ANISOU 5549  CD2 TYR B 178     1554   1017   1196     16    -53    148       C  
ATOM   5550  C   TYR B 178     -13.618 -10.048 -11.579  1.00 10.03           C  
ANISOU 5550  C   TYR B 178     1530   1212   1069    128   -267    126       C  
ATOM   5551  O   TYR B 178     -12.531  -9.475 -11.727  1.00 10.98           O  
ANISOU 5551  O   TYR B 178     1696   1296   1178     62   -132     47       O  
ATOM   5552  N   ALA B 179     -14.210 -10.759 -12.538  1.00 10.31           N  
ANISOU 5552  N   ALA B 179     1549   1201   1164    104    -68    -95       N  
ATOM   5553  CA  ALA B 179     -13.602 -10.905 -13.863  1.00 10.71           C  
ANISOU 5553  CA  ALA B 179     1696   1363   1008    150   -210     -2       C  
ATOM   5554  CB  ALA B 179     -14.316 -12.017 -14.605  1.00 11.53           C  
ANISOU 5554  CB  ALA B 179     1847   1336   1197    180   -227    -87       C  
ATOM   5555  C   ALA B 179     -13.687  -9.591 -14.647  1.00 10.76           C  
ANISOU 5555  C   ALA B 179     1512   1290   1284     21   -106      0       C  
ATOM   5556  O   ALA B 179     -14.682  -8.841 -14.574  1.00 10.80           O  
ANISOU 5556  O   ALA B 179     1386   1443   1273      2    -34    156       O  
ATOM   5557  N   TYR B 180     -12.655  -9.334 -15.448  1.00 10.03           N  
ANISOU 5557  N   TYR B 180     1459   1123   1227    142    -67    -60       N  
ATOM   5558  CA  TYR B 180     -12.591  -8.095 -16.224  1.00 10.93           C  
ANISOU 5558  CA  TYR B 180     1571   1331   1251     50    -68     56       C  
ATOM   5559  CB  TYR B 180     -12.081  -6.922 -15.358  1.00 11.22           C  
ANISOU 5559  CB  TYR B 180     1617   1460   1186     32   -142    -51       C  
ATOM   5560  CG  TYR B 180     -10.584  -6.968 -15.224  1.00 11.10           C  
ANISOU 5560  CG  TYR B 180     1557   1566   1093     69   -110      0       C  
ATOM   5561  CD1 TYR B 180      -9.998  -7.997 -14.495  1.00 11.32           C  
ANISOU 5561  CD1 TYR B 180     1647   1506   1145     50   -183    -68       C  
ATOM   5562  CE1 TYR B 180      -8.630  -8.195 -14.491  1.00 11.63           C  
ANISOU 5562  CE1 TYR B 180     1584   1664   1170     94   -184      0       C  
ATOM   5563  CZ  TYR B 180      -7.812  -7.346 -15.219  1.00 12.08           C  
ANISOU 5563  CZ  TYR B 180     1604   1706   1277    -24   -271     39       C  
ATOM   5564  OH  TYR B 180      -6.455  -7.570 -15.264  1.00 13.51           O  
ANISOU 5564  OH  TYR B 180     1601   1978   1553     -9   -140    169       O  
ATOM   5565  CE2 TYR B 180      -8.372  -6.283 -15.907  1.00 11.76           C  
ANISOU 5565  CE2 TYR B 180     1638   1578   1252    -38    -74     73       C  
ATOM   5566  CD2 TYR B 180      -9.749  -6.112 -15.924  1.00 11.80           C  
ANISOU 5566  CD2 TYR B 180     1699   1556   1229     -9   -231    -23       C  
ATOM   5567  C   TYR B 180     -11.645  -8.322 -17.407  1.00 11.30           C  
ANISOU 5567  C   TYR B 180     1680   1392   1221     17    -74     86       C  
ATOM   5568  O   TYR B 180     -10.813  -9.237 -17.406  1.00 11.94           O  
ANISOU 5568  O   TYR B 180     1782   1480   1273    130     10    127       O  
ATOM   5569  N   TYR B 181     -11.741  -7.424 -18.397  1.00 10.74           N  
ANISOU 5569  N   TYR B 181     1687   1216   1174     95    -59     33       N  
ATOM   5570  CA  TYR B 181     -10.789  -7.382 -19.476  1.00 11.23           C  
ANISOU 5570  CA  TYR B 181     1623   1334   1309     55     97    -25       C  
ATOM   5571  CB  TYR B 181     -11.149  -8.352 -20.612  1.00 12.74           C  
ANISOU 5571  CB  TYR B 181     1857   1654   1326    -44     79    -71       C  
ATOM   5572  CG  TYR B 181     -10.170  -8.286 -21.747  1.00 14.40           C  
ANISOU 5572  CG  TYR B 181     2182   1795   1493   -223    323   -127       C  
ATOM   5573  CD1 TYR B 181      -8.873  -8.720 -21.583  1.00 15.91           C  
ANISOU 5573  CD1 TYR B 181     2279   2162   1603   -149    636   -188       C  
ATOM   5574  CE1 TYR B 181      -7.955  -8.651 -22.621  1.00 18.70           C  
ANISOU 5574  CE1 TYR B 181     2531   2432   2142   -268   1042   -182       C  
ATOM   5575  CZ  TYR B 181      -8.329  -8.114 -23.837  1.00 20.54           C  
ANISOU 5575  CZ  TYR B 181     3090   2681   2032   -129   1067   -332       C  
ATOM   5576  OH  TYR B 181      -7.411  -8.001 -24.857  1.00 25.47           O  
ANISOU 5576  OH  TYR B 181     4263   2483   2931     58   2027     34       O  
ATOM   5577  CE2 TYR B 181      -9.628  -7.676 -24.018  1.00 17.70           C  
ANISOU 5577  CE2 TYR B 181     3041   1970   1713   -289    766   -100       C  
ATOM   5578  CD2 TYR B 181     -10.536  -7.756 -22.972  1.00 15.80           C  
ANISOU 5578  CD2 TYR B 181     2629   1918   1456   -108    481   -108       C  
ATOM   5579  C   TYR B 181     -10.675  -5.966 -20.024  1.00 12.14           C  
ANISOU 5579  C   TYR B 181     1844   1402   1365     81     40      9       C  
ATOM   5580  O   TYR B 181     -11.661  -5.407 -20.498  1.00 11.98           O  
ANISOU 5580  O   TYR B 181     1671   1568   1312     54    163    101       O  
ATOM   5581  N   ILE B 182      -9.459  -5.416 -19.993  1.00 13.31           N  
ANISOU 5581  N   ILE B 182     1856   1587   1614     85     49    382       N  
ATOM   5582  CA  ILE B 182      -9.162  -4.102 -20.588  1.00 14.22           C  
ANISOU 5582  CA  ILE B 182     2199   1584   1618   -230     83    336       C  
ATOM   5583  CB  ILE B 182      -8.036  -3.369 -19.860  1.00 18.26           C  
ANISOU 5583  CB  ILE B 182     2949   1890   2099   -615   -135    478       C  
ATOM   5584  CG1 ILE B 182      -8.366  -3.209 -18.385  1.00 20.06           C  
ANISOU 5584  CG1 ILE B 182     3500   2169   1950   -817   -243    431       C  
ATOM   5585  CG2 ILE B 182      -7.801  -2.023 -20.529  1.00 17.38           C  
ANISOU 5585  CG2 ILE B 182     2947   1969   1686   -664   -515    569       C  
ATOM   5586  CD1 ILE B 182      -7.194  -2.826 -17.557  1.00 22.85           C  
ANISOU 5586  CD1 ILE B 182     3182   2809   2691   -608   -302    375       C  
ATOM   5587  C   ILE B 182      -8.767  -4.320 -22.055  1.00 14.21           C  
ANISOU 5587  C   ILE B 182     2242   1537   1618   -103    173    440       C  
ATOM   5588  O   ILE B 182      -7.807  -5.024 -22.359  1.00 17.12           O  
ANISOU 5588  O   ILE B 182     2300   1855   2349     66    332    602       O  
ATOM   5589  N   HIS B 183      -9.501  -3.686 -22.958  1.00 14.25           N  
ANISOU 5589  N   HIS B 183     2127   1837   1449     19    326    460       N  
ATOM   5590  CA  HIS B 183      -9.182  -3.770 -24.356  1.00 15.81           C  
ANISOU 5590  CA  HIS B 183     2377   2090   1540    -61    392    158       C  
ATOM   5591  CB  HIS B 183     -10.294  -3.170 -25.215  1.00 15.31           C  
ANISOU 5591  CB  HIS B 183     2450   2004   1363    -79    349    347       C  
ATOM   5592  CG  HIS B 183     -11.653  -3.780 -25.086  1.00 15.40           C  
ANISOU 5592  CG  HIS B 183     2383   2164   1304   -156     80    258       C  
ATOM   5593  ND1 HIS B 183     -12.572  -3.694 -26.117  1.00 18.52           N  
ANISOU 5593  ND1 HIS B 183     2317   2803   1916   -242   -238    211       N  
ATOM   5594  CE1 HIS B 183     -13.706  -4.258 -25.720  1.00 17.99           C  
ANISOU 5594  CE1 HIS B 183     2682   2460   1691   -319   -208    318       C  
ATOM   5595  NE2 HIS B 183     -13.530  -4.745 -24.471  1.00 16.98           N  
ANISOU 5595  NE2 HIS B 183     2551   2256   1643    -52   -182    213       N  
ATOM   5596  CD2 HIS B 183     -12.261  -4.431 -24.068  1.00 15.53           C  
ANISOU 5596  CD2 HIS B 183     2298   2246   1356   -147    148    238       C  
ATOM   5597  C   HIS B 183      -7.887  -3.021 -24.633  1.00 16.04           C  
ANISOU 5597  C   HIS B 183     2428   1911   1756    -21    577    222       C  
ATOM   5598  O   HIS B 183      -7.590  -2.016 -23.989  1.00 16.58           O  
ANISOU 5598  O   HIS B 183     2397   1964   1937   -235    523    283       O  
ATOM   5599  N   PRO B 184      -7.084  -3.469 -25.620  1.00 18.19           N  
ANISOU 5599  N   PRO B 184     3066   1888   1958   -257    983    -31       N  
ATOM   5600  CA  PRO B 184      -5.858  -2.755 -25.976  1.00 19.42           C  
ANISOU 5600  CA  PRO B 184     3010   2127   2241   -298    870    100       C  
ATOM   5601  CB  PRO B 184      -5.404  -3.467 -27.258  1.00 21.92           C  
ANISOU 5601  CB  PRO B 184     3302   2418   2605   -322   1106   -185       C  
ATOM   5602  CG  PRO B 184      -5.916  -4.871 -27.069  1.00 23.24           C  
ANISOU 5602  CG  PRO B 184     3501   2373   2955   -292   1262   -363       C  
ATOM   5603  CD  PRO B 184      -7.271  -4.693 -26.411  1.00 21.61           C  
ANISOU 5603  CD  PRO B 184     3420   2355   2437   -524   1078   -418       C  
ATOM   5604  C   PRO B 184      -6.091  -1.256 -26.218  1.00 19.26           C  
ANISOU 5604  C   PRO B 184     3001   2119   2195   -300    668    318       C  
ATOM   5605  O   PRO B 184      -7.096  -0.870 -26.815  1.00 19.59           O  
ANISOU 5605  O   PRO B 184     3105   2352   1987   -446    476    261       O  
ATOM   5606  N   ARG B 185      -5.151  -0.437 -25.734  1.00 19.39           N  
ANISOU 5606  N   ARG B 185     3100   2202   2065   -165    509    401       N  
ATOM   5607  CA  ARG B 185      -5.231   1.012 -25.832  1.00 19.29           C  
ANISOU 5607  CA  ARG B 185     2898   2239   2191   -184    611    610       C  
ATOM   5608  CB  ARG B 185      -4.879   1.655 -24.488  1.00 19.47           C  
ANISOU 5608  CB  ARG B 185     2868   2308   2219    -60    532    563       C  
ATOM   5609  CG  ARG B 185      -5.837   1.292 -23.359  1.00 18.91           C  
ANISOU 5609  CG  ARG B 185     2843   2142   2197    179    502    854       C  
ATOM   5610  CD  ARG B 185      -5.335   1.753 -21.993  1.00 19.13           C  
ANISOU 5610  CD  ARG B 185     2962   2008   2298    113    399    738       C  
ATOM   5611  NE  ARG B 185      -5.373   3.208 -21.882  1.00 19.65           N  
ANISOU 5611  NE  ARG B 185     3389   2023   2052    185    475    712       N  
ATOM   5612  CZ  ARG B 185      -4.783   3.929 -20.935  1.00 19.04           C  
ANISOU 5612  CZ  ARG B 185     3396   1905   1932     74    474    893       C  
ATOM   5613  NH1 ARG B 185      -4.036   3.319 -20.023  1.00 20.61           N  
ANISOU 5613  NH1 ARG B 185     3149   2259   2420    343    420    812       N  
ATOM   5614  NH2 ARG B 185      -4.986   5.248 -20.891  1.00 21.04           N  
ANISOU 5614  NH2 ARG B 185     3523   1995   2475    349    577    665       N  
ATOM   5615  C   ARG B 185      -4.254   1.495 -26.903  1.00 21.06           C  
ANISOU 5615  C   ARG B 185     3538   2418   2044   -375    812    426       C  
ATOM   5616  O   ARG B 185      -3.097   1.087 -26.907  1.00 23.74           O  
ANISOU 5616  O   ARG B 185     3549   3054   2416   -160    912    757       O  
ATOM   5617  N   ALA B 186      -4.735   2.362 -27.793  1.00 22.94           N  
ANISOU 5617  N   ALA B 186     3912   2489   2315   -190    968    685       N  
ATOM   5618  CA  ALA B 186      -3.900   2.900 -28.876  1.00 25.01           C  
ANISOU 5618  CA  ALA B 186     4238   2806   2457   -508   1093    738       C  
ATOM   5619  CB  ALA B 186      -4.767   3.354 -30.030  1.00 25.43           C  
ANISOU 5619  CB  ALA B 186     4717   2604   2338   -560    824    733       C  
ATOM   5620  C   ALA B 186      -3.046   4.059 -28.354  1.00 24.93           C  
ANISOU 5620  C   ALA B 186     3964   2811   2696   -398   1263    762       C  
ATOM   5621  O   ALA B 186      -3.435   4.750 -27.415  1.00 24.60           O  
ANISOU 5621  O   ALA B 186     4288   2535   2522   -568    986    779       O  
ATOM   5622  N   ALA B 187      -1.884   4.277 -28.971  1.00 26.72           N  
ANISOU 5622  N   ALA B 187     4018   2974   3159   -362   1358   1170       N  
ATOM   5623  CA  ALA B 187      -1.075   5.440 -28.642  1.00 28.01           C  
ANISOU 5623  CA  ALA B 187     3743   3119   3778   -386   1490   1129       C  
ATOM   5624  CB  ALA B 187       0.172   5.470 -29.493  1.00 30.96           C  
ANISOU 5624  CB  ALA B 187     3964   3560   4237   -510   1820    979       C  
ATOM   5625  C   ALA B 187      -1.931   6.697 -28.838  1.00 25.89           C  
ANISOU 5625  C   ALA B 187     3647   2844   3344   -586   1600   1030       C  
ATOM   5626  O   ALA B 187      -2.649   6.814 -29.834  1.00 28.38           O  
ANISOU 5626  O   ALA B 187     4620   2913   3249   -176   1252    996       O  
ATOM   5627  N   GLY B 188      -1.866   7.607 -27.863  1.00 27.48           N  
ANISOU 5627  N   GLY B 188     3766   2735   3940   -706   1150    738       N  
ATOM   5628  CA  GLY B 188      -2.570   8.883 -27.904  1.00 26.90           C  
ANISOU 5628  CA  GLY B 188     3850   2667   3701   -686   1029    699       C  
ATOM   5629  C   GLY B 188      -4.039   8.806 -27.513  1.00 24.38           C  
ANISOU 5629  C   GLY B 188     3714   2535   3013   -598    736    555       C  
ATOM   5630  O   GLY B 188      -4.733   9.824 -27.507  1.00 24.19           O  
ANISOU 5630  O   GLY B 188     3432   2729   3030   -335    613    592       O  
ATOM   5631  N   SER B 189      -4.530   7.614 -27.189  1.00 22.07           N  
ANISOU 5631  N   SER B 189     3425   2439   2519   -522    776