CNRS Nantes University UFIP UFIP
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***  3pf9  ***

elNémo ID: 21072802491088046

Job options:

ID        	=	 21072802491088046
JOBID     	=	 3pf9
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 3pf9

HEADER    HYDROLASE                               28-OCT-10   3PF9              
TITLE     CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE   
TITLE    2 LJ0536 S106A MUTANT                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CINNAMOYL ESTERASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS JOHNSONII;                        
SOURCE   3 ORGANISM_TAXID: 33959;                                               
SOURCE   4 GENE: LJ0536;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: P15TV-L                                   
KEYWDS    ALPHA/BETA HYDROLASE FOLD, ESTERASE, HYDROLASE, CINNAMOYL/FERULOYL    
KEYWDS   2 ESTERASE, HYDROXYCINAMMATES, EXTRACELLULAR                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.STOGIOS,K.K.LAI,C.VU,X.XU,H.CUI,S.MOLLOY,C.F.GONZALEZ,A.YAKUNIN,  
AUTHOR   2 A.SAVCHENKO                                                          
REVDAT   2   24-OCT-12 3PF9    1       JRNL                                     
REVDAT   1   31-AUG-11 3PF9    0                                                
JRNL        AUTH   K.K.LAI,P.J.STOGIOS,C.VU,X.XU,H.CUI,S.MOLLOY,A.SAVCHENKO,    
JRNL        AUTH 2 A.YAKUNIN,C.F.GONZALEZ                                       
JRNL        TITL   AN INSERTED ALPHA/BETA SUBDOMAIN SHAPES THE CATALYTIC POCKET 
JRNL        TITL 2 OF LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE                
JRNL        REF    PLOS ONE                      V.   6 23269 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21876742                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0023269                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24675                          
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) : 0.145                           
REMARK   3   R VALUE            (WORKING SET) : 0.142                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1310                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1762                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1962                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 275                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.22000                                              
REMARK   3    B22 (A**2) : -1.08000                                             
REMARK   3    B33 (A**2) : -0.13000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.108         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.133         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2033 ; 0.025 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2772 ; 1.843 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   260 ; 6.039 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   102 ;35.642 ;25.196       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   334 ;13.779 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;20.923 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   316 ; 0.142 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1573 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1260 ; 1.909 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2041 ; 2.872 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   773 ; 4.773 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   726 ; 6.696 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2033 ; 2.602 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -5        A   179                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.0564 -11.2655  -7.8493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0000 T22:   0.0000                                     
REMARK   3      T33:   0.0000 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   180        A   245                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.6832 -18.7138 -13.8719              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0000 T22:   0.0000                                     
REMARK   3      T33:   0.0000 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3PF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062306.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26002                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200   FOR THE DATA SET  : 37.8700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46000                            
REMARK 200   FOR SHELL         : 3.750                              
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: CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII     
REMARK 200  CINNAMOYL ESTERASE LJ0536                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE PH 6.5, 0.2 M    
REMARK 280  CALCIUM ACETATE, 9% PEG8K, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.94450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.94450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       36.37000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.85100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.37000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.85100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.94450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.37000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.85100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       40.94450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.37000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.85100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     ARG A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A   246                                                      
REMARK 465     ASN A   247                                                      
REMARK 465     ALA A   248                                                      
REMARK 465     PHE A   249                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  98      -85.18    -90.26                                   
REMARK 500    ALA A 106     -124.85     64.66                                   
REMARK 500    ALA A 132       48.06    -79.88                                   
REMARK 500    HIS A 153       73.98   -152.41                                   
REMARK 500    LYS A 161     -115.34     49.52                                   
REMARK 500    ASP A 229     -114.01     56.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 250  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  66   O                                                      
REMARK 620 2 HOH A 293   O    75.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 253  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 212   O                                                      
REMARK 620 2 SER A 215   OG  106.7                                              
REMARK 620 3 HOH A 435   O    67.6 140.7                                        
REMARK 620 4 ASP A 209   O    99.0  74.1  68.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 251  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 326   O                                                      
REMARK 620 2 HOH A 316   O    88.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 252  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 457   O                                                      
REMARK 620 2 HOH A 366   O   101.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 250                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 251                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 252                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 253                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PF8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536                                                      
REMARK 900 RELATED ID: 3PFA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH CAFFEIC ACID            
REMARK 900 RELATED ID: 3PFB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE           
REMARK 900 RELATED ID: 3PFC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL           
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH FERULIC ACID            
DBREF  3PF9 A    1   249  UNP    D3YEX6   D3YEX6_LACJO     1    249             
SEQADV 3PF9 MET A  -20  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 GLY A  -19  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 SER A  -18  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 SER A  -17  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 HIS A  -16  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 HIS A  -15  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 HIS A  -14  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 HIS A  -13  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 HIS A  -12  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 HIS A  -11  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 SER A  -10  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 SER A   -9  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 GLY A   -8  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 ARG A   -7  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 GLU A   -6  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 ASN A   -5  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 LEU A   -4  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 TYR A   -3  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 PHE A   -2  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 GLN A   -1  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 GLY A    0  UNP  D3YEX6              EXPRESSION TAG                 
SEQADV 3PF9 ALA A  106  UNP  D3YEX6    SER   106 ENGINEERED MUTATION            
SEQRES   1 A  270  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  270  ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR          
SEQRES   3 A  270  LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU          
SEQRES   4 A  270  GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE          
SEQRES   5 A  270  HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG          
SEQRES   6 A  270  GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER          
SEQRES   7 A  270  VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY          
SEQRES   8 A  270  LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP          
SEQRES   9 A  270  ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS          
SEQRES  10 A  270  VAL ARG ASN ILE TYR LEU VAL GLY HIS ALA GLN GLY GLY          
SEQRES  11 A  270  VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU          
SEQRES  12 A  270  ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU          
SEQRES  13 A  270  LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR          
SEQRES  14 A  270  TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS          
SEQRES  15 A  270  ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN          
SEQRES  16 A  270  GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS          
SEQRES  17 A  270  PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL          
SEQRES  18 A  270  SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN          
SEQRES  19 A  270  ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS          
SEQRES  20 A  270  PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR          
SEQRES  21 A  270  THR ASP PHE LEU GLN ASN ASN ASN ALA PHE                      
HET     NA  A 250       1                                                       
HET     NA  A 251       1                                                       
HET     NA  A 252       1                                                       
HET     NA  A 253       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   2   NA    4(NA 1+)                                                     
FORMUL   6  HOH   *275(H2 O)                                                    
HELIX    1   1 THR A   40  GLU A   53  1                                  14    
HELIX    2   2 LYS A   71  MET A   75  5                                   5    
HELIX    3   3 THR A   76  THR A   93  1                                  18    
HELIX    4   4 GLN A  107  TYR A  119  1                                  13    
HELIX    5   5 ALA A  133  GLY A  142  1                                  10    
HELIX    6   6 GLY A  167  GLN A  175  1                                   9    
HELIX    7   7 PRO A  177  ALA A  183  1                                   7    
HELIX    8   8 PRO A  202  TYR A  212  1                                  11    
HELIX    9   9 SER A  228  SER A  230  5                                   3    
HELIX   10  10 TYR A  231  ASN A  245  1                                  15    
SHEET    1   A 8 GLY A   0  ARG A   8  0                                        
SHEET    2   A 8 LEU A  11  GLU A  19 -1  O  GLY A  15   N  ILE A   4           
SHEET    3   A 8 ALA A  56  PHE A  60 -1  O  SER A  57   N  GLU A  18           
SHEET    4   A 8 TYR A  25  PHE A  31  1  N  ILE A  30   O  VAL A  58           
SHEET    5   A 8 VAL A  97  HIS A 105  1  O  VAL A 103   N  PHE A  31           
SHEET    6   A 8 ILE A 123  LEU A 129  1  O  LYS A 124   N  ILE A 100           
SHEET    7   A 8 VAL A 189  GLY A 194  1  O  CYS A 190   N  LEU A 128           
SHEET    8   A 8 SER A 215  ILE A 220  1  O  THR A 216   N  LEU A 191           
SHEET    1   B 2 ASN A 143  THR A 144  0                                        
SHEET    2   B 2 VAL A 147  THR A 148 -1  O  VAL A 147   N  THR A 144           
SHEET    1   C 2 ARG A 157  PHE A 160  0                                        
SHEET    2   C 2 LEU A 163  GLY A 166 -1  O  LEU A 163   N  PHE A 160           
LINK         O   GLY A  66                NA    NA A 250     1555   1555  2.27  
LINK        NA    NA A 250                 O   HOH A 293     1555   1555  2.42  
LINK         O   TYR A 212                NA    NA A 253     1555   1555  2.51  
LINK         OG  SER A 215                NA    NA A 253     1555   1555  2.65  
LINK        NA    NA A 251                 O   HOH A 326     1555   1555  2.70  
LINK        NA    NA A 253                 O   HOH A 435     1555   1555  2.72  
LINK        NA    NA A 252                 O   HOH A 457     1555   1555  2.76  
LINK         O   ASP A 209                NA    NA A 253     1555   1555  2.79  
LINK        NA    NA A 251                 O   HOH A 316     1555   1555  2.80  
LINK        NA    NA A 252                 O   HOH A 366     1555   1555  2.88  
SITE     1 AC1  4 GLY A  66  HOH A 256  HOH A 293  HOH A 295                    
SITE     1 AC2  2 HOH A 316  HOH A 326                                          
SITE     1 AC3  5 GLN A 213  SER A 215   NA A 253  HOH A 366                    
SITE     2 AC3  5 HOH A 457                                                     
SITE     1 AC4  5 ASP A 209  TYR A 212  SER A 215   NA A 252                    
SITE     2 AC4  5 HOH A 435                                                     
CRYST1   72.740   85.702   81.889  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013748  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011668  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012212        0.00000                         
ATOM      1  N   ASN A  -5     -37.962 -31.460  -0.363  1.00 26.80           N  
ANISOU    1  N   ASN A  -5     3395   3539   3246   -250    176    246       N  
ATOM      2  CA  ASN A  -5     -37.905 -32.174   0.933  1.00 28.62           C  
ANISOU    2  CA  ASN A  -5     3410   3699   3763   -244     44    138       C  
ATOM      3  C   ASN A  -5     -38.381 -33.611   0.680  1.00 29.28           C  
ANISOU    3  C   ASN A  -5     3417   3818   3888   -175     23    171       C  
ATOM      4  O   ASN A  -5     -38.470 -34.055  -0.496  1.00 29.24           O  
ANISOU    4  O   ASN A  -5     3332   3928   3848   -208     68    251       O  
ATOM      5  CB  ASN A  -5     -38.642 -31.393   2.064  1.00 28.76           C  
ANISOU    5  CB  ASN A  -5     3557   3603   3765   -157     88    186       C  
ATOM      6  CG  ASN A  -5     -40.142 -31.190   1.806  1.00 32.29           C  
ANISOU    6  CG  ASN A  -5     3908   3975   4383    -96    318    -18       C  
ATOM      7  OD1 ASN A  -5     -40.833 -32.063   1.275  1.00 32.30           O  
ANISOU    7  OD1 ASN A  -5     3774   3801   4697   -112    481      1       O  
ATOM      8  ND2 ASN A  -5     -40.653 -30.022   2.192  1.00 33.52           N  
ANISOU    8  ND2 ASN A  -5     4702   3800   4232   -318    767   -328       N  
ATOM      9  N   LEU A  -4     -38.632 -34.352   1.741  1.00 30.86           N  
ANISOU    9  N   LEU A  -4     3516   3940   4268   -149    -67    193       N  
ATOM     10  CA  LEU A  -4     -39.052 -35.735   1.603  1.00 32.22           C  
ANISOU   10  CA  LEU A  -4     3834   4029   4378   -188     10    235       C  
ATOM     11  C   LEU A  -4     -40.373 -35.888   0.886  1.00 31.46           C  
ANISOU   11  C   LEU A  -4     3738   3862   4351   -211    128    156       C  
ATOM     12  O   LEU A  -4     -40.641 -36.941   0.319  1.00 32.04           O  
ANISOU   12  O   LEU A  -4     3846   3812   4514   -226      3     -4       O  
ATOM     13  CB  LEU A  -4     -39.159 -36.357   2.991  1.00 33.91           C  
ANISOU   13  CB  LEU A  -4     4125   4358   4398   -241    -12    348       C  
ATOM     14  CG  LEU A  -4     -37.960 -36.862   3.754  1.00 38.76           C  
ANISOU   14  CG  LEU A  -4     4654   4883   5191   -161    -33    402       C  
ATOM     15  CD1 LEU A  -4     -38.467 -37.105   5.198  1.00 43.06           C  
ANISOU   15  CD1 LEU A  -4     5580   5717   5061   -146   -165    467       C  
ATOM     16  CD2 LEU A  -4     -37.532 -38.112   3.085  1.00 43.59           C  
ANISOU   16  CD2 LEU A  -4     5160   5695   5705    158   -113    156       C  
ATOM     17  N   TYR A  -3     -41.202 -34.847   0.896  1.00 29.84           N  
ANISOU   17  N   TYR A  -3     3466   3686   4185   -206    224    279       N  
ATOM     18  CA  TYR A  -3     -42.610 -34.986   0.459  1.00 28.88           C  
ANISOU   18  CA  TYR A  -3     3447   3621   3903   -208    187    105       C  
ATOM     19  C   TYR A  -3     -42.939 -34.174  -0.763  1.00 28.76           C  
ANISOU   19  C   TYR A  -3     3431   3554   3940   -155    209     41       C  
ATOM     20  O   TYR A  -3     -43.708 -34.641  -1.586  1.00 27.38           O  
ANISOU   20  O   TYR A  -3     3474   3055   3873   -257    218   -125       O  
ATOM     21  CB  TYR A  -3     -43.530 -34.605   1.616  1.00 27.71           C  
ANISOU   21  CB  TYR A  -3     3166   3531   3830     62    165     28       C  
ATOM     22  CG  TYR A  -3     -43.290 -35.499   2.801  1.00 29.31           C  
ANISOU   22  CG  TYR A  -3     3338   3792   4005    110    360    -83       C  
ATOM     23  CD1 TYR A  -3     -43.746 -36.819   2.779  1.00 31.43           C  
ANISOU   23  CD1 TYR A  -3     3244   3962   4736    -87    336    194       C  
ATOM     24  CD2 TYR A  -3     -42.567 -35.040   3.947  1.00 32.32           C  
ANISOU   24  CD2 TYR A  -3     3769   4551   3959    317    374     67       C  
ATOM     25  CE1 TYR A  -3     -43.526 -37.689   3.888  1.00 32.72           C  
ANISOU   25  CE1 TYR A  -3     3585   4417   4427    -36   -293    331       C  
ATOM     26  CE2 TYR A  -3     -42.334 -35.886   5.021  1.00 33.56           C  
ANISOU   26  CE2 TYR A  -3     4181   4434   4135    300    131    -10       C  
ATOM     27  CZ  TYR A  -3     -42.853 -37.201   5.001  1.00 34.68           C  
ANISOU   27  CZ  TYR A  -3     4296   4582   4297     90     90    177       C  
ATOM     28  OH  TYR A  -3     -42.611 -38.047   6.053  1.00 38.77           O  
ANISOU   28  OH  TYR A  -3     4871   4851   5008   -326    437    873       O  
ATOM     29  N   PHE A  -2     -42.324 -32.965  -0.903  1.00 28.79           N  
ANISOU   29  N   PHE A  -2     3425   3483   4030   -136    459    -11       N  
ATOM     30  CA  PHE A  -2     -42.564 -32.109  -2.074  1.00 27.76           C  
ANISOU   30  CA  PHE A  -2     3361   3431   3752    -84    579     77       C  
ATOM     31  C   PHE A  -2     -41.256 -31.894  -2.858  1.00 29.81           C  
ANISOU   31  C   PHE A  -2     3572   3785   3967   -184    397     68       C  
ATOM     32  O   PHE A  -2     -40.251 -31.598  -2.234  1.00 29.61           O  
ANISOU   32  O   PHE A  -2     3601   3524   4124   -503    491    -84       O  
ATOM     33  CB  PHE A  -2     -43.062 -30.694  -1.669  1.00 29.03           C  
ANISOU   33  CB  PHE A  -2     3457   3514   4057   -107    635     76       C  
ATOM     34  CG  PHE A  -2     -43.137 -29.747  -2.861  1.00 28.57           C  
ANISOU   34  CG  PHE A  -2     3573   3200   4082   -133    574      0       C  
ATOM     35  CD1 PHE A  -2     -44.170 -29.873  -3.803  1.00 28.92           C  
ANISOU   35  CD1 PHE A  -2     3434   3447   4106     28    331    365       C  
ATOM     36  CD2 PHE A  -2     -42.123 -28.770  -3.097  1.00 27.06           C  
ANISOU   36  CD2 PHE A  -2     3458   2868   3956    -94    578    121       C  
ATOM     37  CE1 PHE A  -2     -44.252 -29.059  -4.938  1.00 31.49           C  
ANISOU   37  CE1 PHE A  -2     4032   3649   4282    -71    835    120       C  
ATOM     38  CE2 PHE A  -2     -42.202 -27.959  -4.256  1.00 30.15           C  
ANISOU   38  CE2 PHE A  -2     4329   3281   3843    246    609    -43       C  
ATOM     39  CZ  PHE A  -2     -43.275 -28.105  -5.161  1.00 30.44           C  
ANISOU   39  CZ  PHE A  -2     4331   2870   4363    -42    638   -129       C  
ATOM     40  N   GLN A  -1     -41.279 -32.082  -4.190  1.00 30.56           N  
ANISOU   40  N   GLN A  -1     3686   3911   4012   -178    479    -39       N  
ATOM     41  CA  GLN A  -1     -40.154 -31.693  -5.057  1.00 30.96           C  
ANISOU   41  CA  GLN A  -1     3813   3965   3985     37    456    -71       C  
ATOM     42  C   GLN A  -1     -40.704 -30.930  -6.232  1.00 32.56           C  
ANISOU   42  C   GLN A  -1     4056   4171   4145    -68    408   -138       C  
ATOM     43  O   GLN A  -1     -41.820 -31.257  -6.712  1.00 32.62           O  
ANISOU   43  O   GLN A  -1     3765   4339   4289     93    694    -33       O  
ATOM     44  CB  GLN A  -1     -39.307 -32.938  -5.510  1.00 31.19           C  
ANISOU   44  CB  GLN A  -1     4083   3807   3961     -9    359   -172       C  
ATOM     45  CG  GLN A  -1     -38.823 -33.808  -4.325  1.00 31.88           C  
ANISOU   45  CG  GLN A  -1     3953   3799   4358    101    509   -274       C  
ATOM     46  CD  GLN A  -1     -39.891 -34.829  -3.888  1.00 33.09           C  
ANISOU   46  CD  GLN A  -1     4001   4288   4281   -428    319   -758       C  
ATOM     47  OE1 GLN A  -1     -40.581 -35.393  -4.726  1.00 34.40           O  
ANISOU   47  OE1 GLN A  -1     3396   4482   5192   -700    -98   -893       O  
ATOM     48  NE2 GLN A  -1     -40.019 -35.066  -2.574  1.00 32.98           N  
ANISOU   48  NE2 GLN A  -1     3758   4191   4581   -439    946   -266       N  
ATOM     49  N   GLY A   0     -39.936 -29.944  -6.733  1.00 33.48           N  
ANISOU   49  N   GLY A   0     4293   4159   4269   -114    353   -123       N  
ATOM     50  CA  GLY A   0     -40.265 -29.279  -7.982  1.00 34.33           C  
ANISOU   50  CA  GLY A   0     4391   4078   4572   -237    283    -72       C  
ATOM     51  C   GLY A   0     -40.045 -27.776  -7.771  1.00 35.09           C  
ANISOU   51  C   GLY A   0     4365   4152   4814   -270    242   -142       C  
ATOM     52  O   GLY A   0     -39.329 -27.368  -6.861  1.00 32.14           O  
ANISOU   52  O   GLY A   0     4004   3663   4543   -293     22   -137       O  
ATOM     53  N   MET A   1     -40.709 -26.969  -8.573  1.00 36.39           N  
ANISOU   53  N   MET A   1     4335   4411   5080   -245    193   -143       N  
ATOM     54  CA  MET A   1     -40.456 -25.531  -8.560  1.00 39.97           C  
ANISOU   54  CA  MET A   1     4690   4885   5611   -234    206   -284       C  
ATOM     55  C   MET A   1     -41.539 -24.818  -7.735  1.00 41.72           C  
ANISOU   55  C   MET A   1     4869   4953   6030   -224    268   -343       C  
ATOM     56  O   MET A   1     -42.583 -25.429  -7.377  1.00 41.25           O  
ANISOU   56  O   MET A   1     4619   5081   5970   -300    386   -310       O  
ATOM     57  CB  MET A   1     -40.504 -25.016  -9.972  1.00 42.14           C  
ANISOU   57  CB  MET A   1     5064   5174   5773   -295    121   -111       C  
ATOM     58  CG  MET A   1     -39.376 -25.451 -10.860  1.00 47.91           C  
ANISOU   58  CG  MET A   1     5885   6340   5976   -220     22   -352       C  
ATOM     59  SD  MET A   1     -39.601 -24.809 -12.584  1.00 64.06           S  
ANISOU   59  SD  MET A   1     8523   8717   7097    -34   -373    121       S  
ATOM     60  CE  MET A   1     -38.615 -23.348 -12.670  1.00 49.46           C  
ANISOU   60  CE  MET A   1     7288   6515   4990    164   -722  -1041       C  
ATOM     61  N   ALA A   2     -41.307 -23.538  -7.454  1.00 41.27           N  
ANISOU   61  N   ALA A   2     4701   4839   6140   -302    125   -503       N  
ATOM     62  CA  ALA A   2     -42.229 -22.733  -6.653  1.00 41.94           C  
ANISOU   62  CA  ALA A   2     4884   4786   6263   -132    -11   -488       C  
ATOM     63  C   ALA A   2     -41.707 -21.318  -6.818  1.00 43.39           C  
ANISOU   63  C   ALA A   2     4983   4949   6553   -130    -83   -491       C  
ATOM     64  O   ALA A   2     -40.467 -21.115  -6.727  1.00 41.65           O  
ANISOU   64  O   ALA A   2     4575   4576   6672   -115   -326   -833       O  
ATOM     65  CB  ALA A   2     -42.178 -23.154  -5.158  1.00 42.54           C  
ANISOU   65  CB  ALA A   2     5019   4765   6379   -104    118   -426       C  
ATOM     66  N   THR A   3     -42.627 -20.374  -7.105  1.00 43.27           N  
ANISOU   66  N   THR A   3     4941   5037   6462   -159   -201   -413       N  
ATOM     67  CA  THR A   3     -42.361 -18.926  -7.086  1.00 43.52           C  
ANISOU   67  CA  THR A   3     5147   5106   6281    -45    -92   -315       C  
ATOM     68  C   THR A   3     -42.408 -18.418  -5.671  1.00 42.67           C  
ANISOU   68  C   THR A   3     5041   5065   6105   -155    123   -282       C  
ATOM     69  O   THR A   3     -43.322 -18.776  -4.952  1.00 43.20           O  
ANISOU   69  O   THR A   3     4959   4885   6567   -306    219   -342       O  
ATOM     70  CB  THR A   3     -43.387 -18.159  -7.893  1.00 44.00           C  
ANISOU   70  CB  THR A   3     5145   5291   6281    -17   -151   -343       C  
ATOM     71  OG1 THR A   3     -43.217 -18.517  -9.259  1.00 46.78           O  
ANISOU   71  OG1 THR A   3     5551   5697   6523     93   -321   -647       O  
ATOM     72  CG2 THR A   3     -43.091 -16.669  -7.811  1.00 42.61           C  
ANISOU   72  CG2 THR A   3     4801   4977   6410    423   -277   -695       C  
ATOM     73  N   ILE A   4     -41.413 -17.616  -5.246  1.00 40.09           N  
ANISOU   73  N   ILE A   4     4834   4622   5775   -188    211   -260       N  
ATOM     74  CA  ILE A   4     -41.304 -17.226  -3.848  1.00 39.82           C  
ANISOU   74  CA  ILE A   4     4957   4490   5683   -220    179    -57       C  
ATOM     75  C   ILE A   4     -41.029 -15.737  -3.856  1.00 37.58           C  
ANISOU   75  C   ILE A   4     4666   4180   5430   -263    185   -103       C  
ATOM     76  O   ILE A   4     -40.570 -15.217  -4.892  1.00 35.93           O  
ANISOU   76  O   ILE A   4     4532   3738   5379   -231     37   -312       O  
ATOM     77  CB  ILE A   4     -40.169 -17.936  -3.051  1.00 40.51           C  
ANISOU   77  CB  ILE A   4     5031   4597   5764   -300    150     69       C  
ATOM     78  CG1 ILE A   4     -38.851 -17.887  -3.798  1.00 41.18           C  
ANISOU   78  CG1 ILE A   4     5169   4876   5601    -96     29     58       C  
ATOM     79  CG2 ILE A   4     -40.539 -19.459  -2.637  1.00 41.60           C  
ANISOU   79  CG2 ILE A   4     5539   4174   6092   -180    166    -67       C  
ATOM     80  CD1 ILE A   4     -37.722 -18.418  -2.951  1.00 44.37           C  
ANISOU   80  CD1 ILE A   4     5595   5466   5795   -161   -547    282       C  
ATOM     81  N   THR A   5     -41.343 -15.080  -2.743  1.00 35.66           N  
ANISOU   81  N   THR A   5     4275   4081   5193   -281    227    -22       N  
ATOM     82  CA  THR A   5     -41.258 -13.610  -2.666  1.00 35.07           C  
ANISOU   82  CA  THR A   5     4045   4176   5104    -86    185    -27       C  
ATOM     83  C   THR A   5     -40.722 -13.191  -1.317  1.00 34.07           C  
ANISOU   83  C   THR A   5     3947   4171   4826    -45    190     14       C  
ATOM     84  O   THR A   5     -41.050 -13.790  -0.283  1.00 34.41           O  
ANISOU   84  O   THR A   5     3978   4180   4913   -336     93     85       O  
ATOM     85  CB  THR A   5     -42.632 -12.865  -2.933  1.00 36.28           C  
ANISOU   85  CB  THR A   5     4103   4599   5083   -114    281     70       C  
ATOM     86  OG1 THR A   5     -43.540 -13.209  -1.891  1.00 40.03           O  
ANISOU   86  OG1 THR A   5     4142   4953   6114   -219    605     37       O  
ATOM     87  CG2 THR A   5     -43.253 -13.220  -4.289  1.00 35.40           C  
ANISOU   87  CG2 THR A   5     4175   3860   5415     56     33   -214       C  
ATOM     88  N   LEU A   6     -39.825 -12.211  -1.348  1.00 31.74           N  
ANISOU   88  N   LEU A   6     3672   3657   4727     37     16   -244       N  
ATOM     89  CA  LEU A   6     -39.160 -11.698  -0.169  1.00 31.44           C  
ANISOU   89  CA  LEU A   6     3532   3815   4599    190      3   -242       C  
ATOM     90  C   LEU A   6     -39.299 -10.195  -0.257  1.00 30.65           C  
ANISOU   90  C   LEU A   6     3429   3758   4458     40    -27   -294       C  
ATOM     91  O   LEU A   6     -39.664  -9.660  -1.270  1.00 30.90           O  
ANISOU   91  O   LEU A   6     3481   3732   4528      3    -80   -398       O  
ATOM     92  CB  LEU A   6     -37.645 -12.018  -0.188  1.00 31.49           C  
ANISOU   92  CB  LEU A   6     3514   3843   4606    216   -175   -247       C  
ATOM     93  CG  LEU A   6     -37.392 -13.508  -0.030  1.00 32.30           C  
ANISOU   93  CG  LEU A   6     3500   4147   4624    548    -74   -173       C  
ATOM     94  CD1 LEU A   6     -35.860 -13.765  -0.089  1.00 31.52           C  
ANISOU   94  CD1 LEU A   6     3369   4127   4480    700    -11   -224       C  
ATOM     95  CD2 LEU A   6     -38.047 -14.052   1.276  1.00 35.68           C  
ANISOU   95  CD2 LEU A   6     4080   4083   5391    -56    179    409       C  
ATOM     96  N   GLU A   7     -38.963  -9.516   0.825  1.00 32.24           N  
ANISOU   96  N   GLU A   7     3664   3930   4653    130     70   -438       N  
ATOM     97  CA  GLU A   7     -39.033  -8.065   0.828  1.00 33.48           C  
ANISOU   97  CA  GLU A   7     3880   4056   4784     17     85   -350       C  
ATOM     98  C   GLU A   7     -37.682  -7.527   1.249  1.00 31.09           C  
ANISOU   98  C   GLU A   7     3643   3856   4311     51    133   -375       C  
ATOM     99  O   GLU A   7     -37.081  -8.088   2.124  1.00 31.08           O  
ANISOU   99  O   GLU A   7     3634   3721   4451    -55     22   -388       O  
ATOM    100  CB  GLU A   7     -39.977  -7.644   1.941  1.00 35.45           C  
ANISOU  100  CB  GLU A   7     4096   4399   4972     95    274   -424       C  
ATOM    101  CG  GLU A   7     -41.453  -7.585   1.596  1.00 44.49           C  
ANISOU  101  CG  GLU A   7     4962   5666   6274    363    149   -109       C  
ATOM    102  CD  GLU A   7     -42.115  -6.573   2.517  1.00 55.02           C  
ANISOU  102  CD  GLU A   7     6401   6934   7566    886    695     40       C  
ATOM    103  OE1 GLU A   7     -42.071  -5.339   2.199  1.00 59.68           O  
ANISOU  103  OE1 GLU A   7     6977   7105   8594   1102    501    435       O  
ATOM    104  OE2 GLU A   7     -42.611  -7.010   3.597  1.00 61.19           O  
ANISOU  104  OE2 GLU A   7     7333   7987   7927    935    817    593       O  
ATOM    105  N   ARG A   8     -37.247  -6.418   0.679  1.00 29.65           N  
ANISOU  105  N   ARG A   8     3491   3650   4124   -109    119   -297       N  
ATOM    106  CA  ARG A   8     -36.042  -5.729   1.167  1.00 28.23           C  
ANISOU  106  CA  ARG A   8     3324   3545   3858    -10    150   -298       C  
ATOM    107  C   ARG A   8     -36.432  -4.260   1.129  1.00 28.49           C  
ANISOU  107  C   ARG A   8     3316   3649   3860     85    210   -381       C  
ATOM    108  O   ARG A   8     -36.779  -3.763   0.062  1.00 27.15           O  
ANISOU  108  O   ARG A   8     3106   3412   3797    240    149   -468       O  
ATOM    109  CB  ARG A   8     -34.842  -5.973   0.222  1.00 27.16           C  
ANISOU  109  CB  ARG A   8     3201   3560   3559   -162    142   -339       C  
ATOM    110  CG  ARG A   8     -33.477  -5.566   0.826  1.00 27.11           C  
ANISOU  110  CG  ARG A   8     3177   3396   3725     -9    114     30       C  
ATOM    111  CD  ARG A   8     -33.090  -4.163   0.427  1.00 24.67           C  
ANISOU  111  CD  ARG A   8     3130   3222   3018     -3   -194    162       C  
ATOM    112  NE  ARG A   8     -32.995  -4.045  -1.042  1.00 25.04           N  
ANISOU  112  NE  ARG A   8     3015   3476   3022      3     77    -86       N  
ATOM    113  CZ  ARG A   8     -33.043  -2.888  -1.721  1.00 24.72           C  
ANISOU  113  CZ  ARG A   8     3071   3170   3151   -120     15   -194       C  
ATOM    114  NH1 ARG A   8     -33.133  -1.691  -1.104  1.00 24.73           N  
ANISOU  114  NH1 ARG A   8     2896   3377   3124    198    234   -551       N  
ATOM    115  NH2 ARG A   8     -32.970  -2.923  -3.040  1.00 26.19           N  
ANISOU  115  NH2 ARG A   8     2925   3740   3285    -28    -50   -311       N  
ATOM    116  N   ASP A   9     -36.342  -3.573   2.280  1.00 30.20           N  
ANISOU  116  N   ASP A   9     3508   3848   4117    101    206   -496       N  
ATOM    117  CA  ASP A   9     -36.713  -2.121   2.380  1.00 30.77           C  
ANISOU  117  CA  ASP A   9     3746   3832   4114    134    122   -471       C  
ATOM    118  C   ASP A   9     -37.969  -1.712   1.651  1.00 32.49           C  
ANISOU  118  C   ASP A   9     3922   4228   4194    200    143   -579       C  
ATOM    119  O   ASP A   9     -37.969  -0.719   0.841  1.00 34.19           O  
ANISOU  119  O   ASP A   9     4100   4367   4522    353    210   -671       O  
ATOM    120  CB  ASP A   9     -35.627  -1.229   1.812  1.00 29.94           C  
ANISOU  120  CB  ASP A   9     3691   3704   3978     98    223   -439       C  
ATOM    121  CG  ASP A   9     -34.352  -1.338   2.576  1.00 28.48           C  
ANISOU  121  CG  ASP A   9     3522   3560   3737   -125    114   -368       C  
ATOM    122  OD1 ASP A   9     -34.407  -1.668   3.812  1.00 26.99           O  
ANISOU  122  OD1 ASP A   9     3076   3478   3700   -302    201   -288       O  
ATOM    123  OD2 ASP A   9     -33.304  -1.108   1.911  1.00 30.66           O  
ANISOU  123  OD2 ASP A   9     3954   3528   4166    -92    680   -881       O  
ATOM    124  N   GLY A  10     -39.046  -2.425   1.835  1.00 33.86           N  
ANISOU  124  N   GLY A  10     3965   4569   4329    104    131   -762       N  
ATOM    125  CA  GLY A  10     -40.225  -1.909   1.055  1.00 33.79           C  
ANISOU  125  CA  GLY A  10     4043   4463   4330    290    -48   -536       C  
ATOM    126  C   GLY A  10     -40.387  -2.316  -0.420  1.00 33.89           C  
ANISOU  126  C   GLY A  10     4084   4332   4457    196   -159   -585       C  
ATOM    127  O   GLY A  10     -41.421  -1.954  -1.056  1.00 34.19           O  
ANISOU  127  O   GLY A  10     3821   4229   4938    315    -63   -849       O  
ATOM    128  N   LEU A  11     -39.387  -3.010  -0.983  1.00 31.27           N  
ANISOU  128  N   LEU A  11     3768   3770   4342     14    -83   -409       N  
ATOM    129  CA  LEU A  11     -39.444  -3.569  -2.346  1.00 31.03           C  
ANISOU  129  CA  LEU A  11     3816   3745   4227    -47    -86   -229       C  
ATOM    130  C   LEU A  11     -39.709  -5.069  -2.277  1.00 30.97           C  
ANISOU  130  C   LEU A  11     3900   3684   4181     42   -169   -275       C  
ATOM    131  O   LEU A  11     -39.116  -5.774  -1.478  1.00 32.35           O  
ANISOU  131  O   LEU A  11     3965   3773   4551     77   -339   -338       O  
ATOM    132  CB  LEU A  11     -38.121  -3.345  -3.129  1.00 29.32           C  
ANISOU  132  CB  LEU A  11     3501   3559   4078   -199   -160   -212       C  
ATOM    133  CG  LEU A  11     -37.667  -1.891  -3.237  1.00 31.32           C  
ANISOU  133  CG  LEU A  11     3580   4096   4224   -138   -109     14       C  
ATOM    134  CD1 LEU A  11     -36.303  -1.930  -3.959  1.00 29.62           C  
ANISOU  134  CD1 LEU A  11     3000   4041   4213   -832    -75    -92       C  
ATOM    135  CD2 LEU A  11     -38.688  -0.981  -3.962  1.00 31.94           C  
ANISOU  135  CD2 LEU A  11     3442   3822   4871   -169   -500   -108       C  
ATOM    136  N   GLN A  12     -40.609  -5.568  -3.097  1.00 30.32           N  
ANISOU  136  N   GLN A  12     3531   3454   4536    -51   -218   -260       N  
ATOM    137  CA  GLN A  12     -40.744  -7.013  -3.217  1.00 30.57           C  
ANISOU  137  CA  GLN A  12     3512   3596   4507    -52    -58   -333       C  
ATOM    138  C   GLN A  12     -39.730  -7.557  -4.236  1.00 29.01           C  
ANISOU  138  C   GLN A  12     3249   3475   4297   -173   -153   -388       C  
ATOM    139  O   GLN A  12     -39.525  -6.979  -5.324  1.00 28.80           O  
ANISOU  139  O   GLN A  12     3216   3569   4156     18    233   -543       O  
ATOM    140  CB  GLN A  12     -42.181  -7.384  -3.592  1.00 30.35           C  
ANISOU  140  CB  GLN A  12     3383   3454   4694   -207   -331   -405       C  
ATOM    141  CG  GLN A  12     -42.414  -8.852  -3.848  1.00 38.07           C  
ANISOU  141  CG  GLN A  12     4274   4452   5738   -322     16   -168       C  
ATOM    142  CD  GLN A  12     -43.870  -9.150  -4.307  1.00 46.01           C  
ANISOU  142  CD  GLN A  12     4764   6324   6394   -682    130   -103       C  
ATOM    143  OE1 GLN A  12     -44.726  -9.479  -3.458  1.00 50.64           O  
ANISOU  143  OE1 GLN A  12     4514   7007   7718  -1117    574     78       O  
ATOM    144  NE2 GLN A  12     -44.160  -9.010  -5.645  1.00 44.66           N  
ANISOU  144  NE2 GLN A  12     4989   5738   6240   -221    -64   -498       N  
ATOM    145  N   LEU A  13     -39.115  -8.668  -3.870  1.00 28.79           N  
ANISOU  145  N   LEU A  13     3063   3468   4407   -143   -184   -553       N  
ATOM    146  CA  LEU A  13     -38.220  -9.393  -4.766  1.00 28.68           C  
ANISOU  146  CA  LEU A  13     3306   3337   4253   -149    -54   -655       C  
ATOM    147  C   LEU A  13     -38.895 -10.741  -5.076  1.00 29.55           C  
ANISOU  147  C   LEU A  13     3406   3416   4406    -16     48   -569       C  
ATOM    148  O   LEU A  13     -39.282 -11.468  -4.155  1.00 31.10           O  
ANISOU  148  O   LEU A  13     3696   3200   4918    -77    100   -587       O  
ATOM    149  CB  LEU A  13     -36.845  -9.652  -4.080  1.00 27.96           C  
ANISOU  149  CB  LEU A  13     3221   3188   4214    166    -31   -595       C  
ATOM    150  CG  LEU A  13     -36.097  -8.426  -3.486  1.00 28.99           C  
ANISOU  150  CG  LEU A  13     3290   3540   4181   -240   -223   -409       C  
ATOM    151  CD1 LEU A  13     -34.896  -8.780  -2.594  1.00 29.76           C  
ANISOU  151  CD1 LEU A  13     3468   3532   4306    -31   -135   -909       C  
ATOM    152  CD2 LEU A  13     -35.668  -7.466  -4.613  1.00 30.14           C  
ANISOU  152  CD2 LEU A  13     4005   3670   3777   -281   -210   -439       C  
ATOM    153  N   VAL A  14     -38.900 -11.094  -6.355  1.00 30.02           N  
ANISOU  153  N   VAL A  14     3288   3530   4586    -33     -3   -640       N  
ATOM    154  CA  VAL A  14     -39.530 -12.335  -6.820  1.00 30.35           C  
ANISOU  154  CA  VAL A  14     3580   3426   4523    175     70   -719       C  
ATOM    155  C   VAL A  14     -38.467 -13.364  -7.209  1.00 31.56           C  
ANISOU  155  C   VAL A  14     3701   3690   4600    138    231   -617       C  
ATOM    156  O   VAL A  14     -37.540 -13.018  -7.958  1.00 29.91           O  
ANISOU  156  O   VAL A  14     3207   3829   4327    284    499   -707       O  
ATOM    157  CB  VAL A  14     -40.458 -12.039  -7.972  1.00 30.47           C  
ANISOU  157  CB  VAL A  14     3489   3448   4637    115    -88   -919       C  
ATOM    158  CG1 VAL A  14     -41.139 -13.375  -8.430  1.00 30.67           C  
ANISOU  158  CG1 VAL A  14     3627   3138   4885      4     -2   -831       C  
ATOM    159  CG2 VAL A  14     -41.516 -10.966  -7.490  1.00 29.14           C  
ANISOU  159  CG2 VAL A  14     3269   3331   4472    189    208   -895       C  
ATOM    160  N   GLY A  15     -38.628 -14.604  -6.722  1.00 31.03           N  
ANISOU  160  N   GLY A  15     3850   3400   4537    197    131   -592       N  
ATOM    161  CA  GLY A  15     -37.615 -15.656  -6.988  1.00 30.45           C  
ANISOU  161  CA  GLY A  15     3532   3376   4661    -36    243   -816       C  
ATOM    162  C   GLY A  15     -38.233 -16.976  -7.405  1.00 31.56           C  
ANISOU  162  C   GLY A  15     3669   3634   4686    -70    240   -725       C  
ATOM    163  O   GLY A  15     -39.442 -17.138  -7.319  1.00 30.51           O  
ANISOU  163  O   GLY A  15     3440   3514   4637   -146    363   -995       O  
ATOM    164  N   THR A  16     -37.395 -17.921  -7.826  1.00 29.21           N  
ANISOU  164  N   THR A  16     3390   3296   4411    -39    247   -673       N  
ATOM    165  CA  THR A  16     -37.849 -19.271  -8.110  1.00 29.33           C  
ANISOU  165  CA  THR A  16     3485   3457   4201   -122    244   -464       C  
ATOM    166  C   THR A  16     -36.993 -20.203  -7.270  1.00 30.01           C  
ANISOU  166  C   THR A  16     3689   3587   4126    -67    246   -414       C  
ATOM    167  O   THR A  16     -35.745 -20.062  -7.267  1.00 30.77           O  
ANISOU  167  O   THR A  16     3619   3715   4356    -20    103   -510       O  
ATOM    168  CB  THR A  16     -37.677 -19.574  -9.605  1.00 29.43           C  
ANISOU  168  CB  THR A  16     3521   3538   4121   -108    296   -261       C  
ATOM    169  OG1 THR A  16     -38.490 -18.686 -10.364  1.00 30.11           O  
ANISOU  169  OG1 THR A  16     3199   3592   4650   -196   -111   -265       O  
ATOM    170  CG2 THR A  16     -38.001 -21.044  -9.967  1.00 30.00           C  
ANISOU  170  CG2 THR A  16     3866   3452   4081   -116    836   -391       C  
ATOM    171  N   ARG A  17     -37.645 -21.135  -6.546  1.00 29.17           N  
ANISOU  171  N   ARG A  17     3625   3379   4077    -34    242   -387       N  
ATOM    172  CA  ARG A  17     -36.964 -22.116  -5.717  1.00 29.55           C  
ANISOU  172  CA  ARG A  17     3859   3343   4024    -78    213   -448       C  
ATOM    173  C   ARG A  17     -37.086 -23.471  -6.457  1.00 29.45           C  
ANISOU  173  C   ARG A  17     3813   3243   4133    -42    179   -461       C  
ATOM    174  O   ARG A  17     -38.158 -23.823  -6.939  1.00 29.02           O  
ANISOU  174  O   ARG A  17     3757   3161   4106   -112    325   -563       O  
ATOM    175  CB  ARG A  17     -37.622 -22.241  -4.337  1.00 29.21           C  
ANISOU  175  CB  ARG A  17     3914   3262   3920     43    269   -407       C  
ATOM    176  CG  ARG A  17     -37.040 -23.339  -3.448  1.00 29.95           C  
ANISOU  176  CG  ARG A  17     3679   3990   3710   -271    289   -225       C  
ATOM    177  CD  ARG A  17     -37.382 -23.033  -2.053  1.00 30.43           C  
ANISOU  177  CD  ARG A  17     3670   4072   3818   -272    109   -539       C  
ATOM    178  NE  ARG A  17     -36.863 -24.097  -1.229  1.00 32.49           N  
ANISOU  178  NE  ARG A  17     4056   3906   4380   -490    469   -255       N  
ATOM    179  CZ  ARG A  17     -36.514 -23.972   0.038  1.00 32.34           C  
ANISOU  179  CZ  ARG A  17     3951   3975   4360   -567    134   -299       C  
ATOM    180  NH1 ARG A  17     -36.646 -22.812   0.653  1.00 36.51           N  
ANISOU  180  NH1 ARG A  17     4650   4420   4802   -882    181   -386       N  
ATOM    181  NH2 ARG A  17     -36.020 -24.991   0.681  1.00 34.02           N  
ANISOU  181  NH2 ARG A  17     4163   4108   4656   -450    387    -32       N  
ATOM    182  N   GLU A  18     -35.954 -24.154  -6.589  1.00 29.00           N  
ANISOU  182  N   GLU A  18     3599   3360   4058    -63    336   -454       N  
ATOM    183  CA  GLU A  18     -35.939 -25.536  -7.027  1.00 28.66           C  
ANISOU  183  CA  GLU A  18     3786   3221   3882   -137    234   -287       C  
ATOM    184  C   GLU A  18     -35.739 -26.418  -5.812  1.00 28.75           C  
ANISOU  184  C   GLU A  18     3684   3523   3714   -131    260   -193       C  
ATOM    185  O   GLU A  18     -34.722 -26.343  -5.195  1.00 27.60           O  
ANISOU  185  O   GLU A  18     3662   3153   3672   -200    194    -26       O  
ATOM    186  CB  GLU A  18     -34.790 -25.771  -7.987  1.00 27.80           C  
ANISOU  186  CB  GLU A  18     3603   3226   3732    -64    267   -268       C  
ATOM    187  CG  GLU A  18     -34.818 -24.872  -9.229  1.00 30.65           C  
ANISOU  187  CG  GLU A  18     4168   3371   4105     50   -165   -280       C  
ATOM    188  CD  GLU A  18     -35.885 -25.247 -10.242  1.00 36.55           C  
ANISOU  188  CD  GLU A  18     5194   3995   4697   -540   -601   -235       C  
ATOM    189  OE1 GLU A  18     -36.471 -26.411 -10.196  1.00 39.28           O  
ANISOU  189  OE1 GLU A  18     5551   4042   5332   -790   -140  -1071       O  
ATOM    190  OE2 GLU A  18     -36.120 -24.350 -11.109  1.00 36.59           O  
ANISOU  190  OE2 GLU A  18     4726   3687   5487   -482  -1282   -189       O  
ATOM    191  N   GLU A  19     -36.758 -27.220  -5.470  1.00 29.35           N  
ANISOU  191  N   GLU A  19     3816   3573   3762   -176    360   -131       N  
ATOM    192  CA  GLU A  19     -36.783 -27.992  -4.228  1.00 29.44           C  
ANISOU  192  CA  GLU A  19     3625   3744   3816   -166    439   -105       C  
ATOM    193  C   GLU A  19     -36.445 -29.455  -4.562  1.00 30.07           C  
ANISOU  193  C   GLU A  19     3719   3831   3872   -174    462   -136       C  
ATOM    194  O   GLU A  19     -37.136 -30.061  -5.374  1.00 32.39           O  
ANISOU  194  O   GLU A  19     4040   3923   4344   -199    475   -349       O  
ATOM    195  CB  GLU A  19     -38.205 -27.928  -3.603  1.00 28.72           C  
ANISOU  195  CB  GLU A  19     3461   3913   3537    -92    492   -216       C  
ATOM    196  CG  GLU A  19     -38.310 -28.780  -2.388  1.00 29.40           C  
ANISOU  196  CG  GLU A  19     3370   4005   3792   -235    502   -210       C  
ATOM    197  CD  GLU A  19     -37.561 -28.176  -1.221  1.00 29.93           C  
ANISOU  197  CD  GLU A  19     3380   4295   3694   -355    458    -67       C  
ATOM    198  OE1 GLU A  19     -37.079 -27.020  -1.358  1.00 33.38           O  
ANISOU  198  OE1 GLU A  19     4194   4147   4339   -105    114   -561       O  
ATOM    199  OE2 GLU A  19     -37.443 -28.829  -0.187  1.00 31.29           O  
ANISOU  199  OE2 GLU A  19     3275   4298   4315   -112    303    237       O  
ATOM    200  N   PRO A  20     -35.373 -29.997  -4.004  1.00 30.88           N  
ANISOU  200  N   PRO A  20     3984   3754   3992   -253    412    -44       N  
ATOM    201  CA  PRO A  20     -34.943 -31.370  -4.389  1.00 32.05           C  
ANISOU  201  CA  PRO A  20     4019   3850   4305   -183    495    -88       C  
ATOM    202  C   PRO A  20     -35.511 -32.420  -3.413  1.00 32.93           C  
ANISOU  202  C   PRO A  20     4151   3858   4500   -288    536    -56       C  
ATOM    203  O   PRO A  20     -36.258 -32.054  -2.457  1.00 32.72           O  
ANISOU  203  O   PRO A  20     4171   3581   4679   -446    785   -119       O  
ATOM    204  CB  PRO A  20     -33.440 -31.299  -4.175  1.00 32.06           C  
ANISOU  204  CB  PRO A  20     3969   3969   4241   -374    340    -70       C  
ATOM    205  CG  PRO A  20     -33.333 -30.376  -2.930  1.00 31.79           C  
ANISOU  205  CG  PRO A  20     4197   3643   4236   -146    333    -39       C  
ATOM    206  CD  PRO A  20     -34.366 -29.313  -3.163  1.00 30.96           C  
ANISOU  206  CD  PRO A  20     3770   4083   3908   -137    219   -157       C  
ATOM    207  N   PHE A  21     -35.155 -33.689  -3.598  1.00 34.18           N  
ANISOU  207  N   PHE A  21     4189   3952   4844    -89    651    -39       N  
ATOM    208  CA  PHE A  21     -35.522 -34.733  -2.603  1.00 35.38           C  
ANISOU  208  CA  PHE A  21     4246   4243   4953    -96    542     24       C  
ATOM    209  C   PHE A  21     -34.676 -34.631  -1.359  1.00 35.72           C  
ANISOU  209  C   PHE A  21     4194   4273   5103   -160    518    -60       C  
ATOM    210  O   PHE A  21     -33.514 -34.181  -1.412  1.00 36.80           O  
ANISOU  210  O   PHE A  21     4268   4288   5423   -217    714     19       O  
ATOM    211  CB  PHE A  21     -35.292 -36.156  -3.160  1.00 35.58           C  
ANISOU  211  CB  PHE A  21     4263   4202   5052   -167    529   -138       C  
ATOM    212  CG  PHE A  21     -36.129 -36.496  -4.340  1.00 40.81           C  
ANISOU  212  CG  PHE A  21     4739   5112   5653    -90    206     37       C  
ATOM    213  CD1 PHE A  21     -37.275 -37.325  -4.192  1.00 42.43           C  
ANISOU  213  CD1 PHE A  21     4741   5407   5972    -34    511    194       C  
ATOM    214  CD2 PHE A  21     -35.786 -36.041  -5.635  1.00 42.96           C  
ANISOU  214  CD2 PHE A  21     4844   5621   5856   -244    391    131       C  
ATOM    215  CE1 PHE A  21     -38.080 -37.672  -5.329  1.00 40.52           C  
ANISOU  215  CE1 PHE A  21     4713   5320   5360    192    289     54       C  
ATOM    216  CE2 PHE A  21     -36.582 -36.377  -6.775  1.00 45.31           C  
ANISOU  216  CE2 PHE A  21     5464   5863   5887   -334    249    -12       C  
ATOM    217  CZ  PHE A  21     -37.731 -37.191  -6.616  1.00 43.10           C  
ANISOU  217  CZ  PHE A  21     4908   5764   5703   -121    435     43       C  
ATOM    218  N   GLY A  22     -35.212 -35.144  -0.258  1.00 34.79           N  
ANISOU  218  N   GLY A  22     4047   4212   4958   -298    478     81       N  
ATOM    219  CA  GLY A  22     -34.514 -35.309   0.995  1.00 35.22           C  
ANISOU  219  CA  GLY A  22     4005   4345   5031   -388    311     72       C  
ATOM    220  C   GLY A  22     -34.852 -34.242   2.050  1.00 36.55           C  
ANISOU  220  C   GLY A  22     4181   4570   5136   -402    291    166       C  
ATOM    221  O   GLY A  22     -35.264 -33.108   1.720  1.00 34.36           O  
ANISOU  221  O   GLY A  22     3817   4075   5161   -640    427    212       O  
ATOM    222  N   GLU A  23     -34.658 -34.629   3.321  1.00 36.73           N  
ANISOU  222  N   GLU A  23     4244   4660   5049   -457    209    159       N  
ATOM    223  CA  GLU A  23     -34.951 -33.824   4.479  1.00 38.50           C  
ANISOU  223  CA  GLU A  23     4636   4762   5230   -462    134    128       C  
ATOM    224  C   GLU A  23     -33.886 -32.718   4.611  1.00 37.20           C  
ANISOU  224  C   GLU A  23     4572   4516   5044   -504    275    115       C  
ATOM    225  O   GLU A  23     -34.211 -31.612   5.044  1.00 37.76           O  
ANISOU  225  O   GLU A  23     4581   4370   5396   -797    465     89       O  
ATOM    226  CB  GLU A  23     -34.855 -34.710   5.706  1.00 40.35           C  
ANISOU  226  CB  GLU A  23     4949   5068   5311   -392    157    325       C  
ATOM    227  CG  GLU A  23     -35.613 -34.279   6.931  1.00 47.95           C  
ANISOU  227  CG  GLU A  23     5803   6296   6118    202    189    206       C  
ATOM    228  CD  GLU A  23     -36.026 -35.526   7.773  1.00 55.93           C  
ANISOU  228  CD  GLU A  23     6969   7537   6744    603    147    804       C  
ATOM    229  OE1 GLU A  23     -35.218 -36.515   7.808  1.00 58.17           O  
ANISOU  229  OE1 GLU A  23     7619   7842   6641   1206   -435    647       O  
ATOM    230  OE2 GLU A  23     -37.152 -35.541   8.368  1.00 59.10           O  
ANISOU  230  OE2 GLU A  23     6567   8848   7038    946     17    577       O  
ATOM    231  N   ILE A  24     -32.645 -33.044   4.253  1.00 34.53           N  
ANISOU  231  N   ILE A  24     4231   4314   4573   -540    232     45       N  
ATOM    232  CA AILE A  24     -31.491 -32.133   4.383  0.50 34.95           C  
ANISOU  232  CA AILE A  24     4426   4318   4534   -484    298    135       C  
ATOM    233  CA BILE A  24     -31.559 -32.065   4.342  0.50 34.19           C  
ANISOU  233  CA BILE A  24     4361   4226   4403   -446    344    108       C  
ATOM    234  C   ILE A  24     -30.811 -32.042   2.998  1.00 34.00           C  
ANISOU  234  C   ILE A  24     4387   4158   4371   -440    295    102       C  
ATOM    235  O   ILE A  24     -30.599 -33.060   2.350  1.00 33.40           O  
ANISOU  235  O   ILE A  24     4442   3829   4418   -517    303    191       O  
ATOM    236  CB AILE A  24     -30.484 -32.642   5.489  0.50 34.59           C  
ANISOU  236  CB AILE A  24     4279   4339   4522   -509    196     86       C  
ATOM    237  CB BILE A  24     -30.555 -32.329   5.513  0.50 33.34           C  
ANISOU  237  CB BILE A  24     4177   4222   4268   -471    295     32       C  
ATOM    238  CG1AILE A  24     -31.088 -32.449   6.890  0.50 36.46           C  
ANISOU  238  CG1AILE A  24     4510   4634   4708   -483    185    143       C  
ATOM    239  CG1BILE A  24     -31.262 -32.518   6.868  0.50 34.27           C  
ANISOU  239  CG1BILE A  24     4461   4249   4310   -332    301    106       C  
ATOM    240  CG2AILE A  24     -29.111 -31.906   5.446  0.50 36.13           C  
ANISOU  240  CG2AILE A  24     4619   4447   4661   -576    283    205       C  
ATOM    241  CG2BILE A  24     -29.582 -31.140   5.674  0.50 32.43           C  
ANISOU  241  CG2BILE A  24     4200   4096   4026   -458    527     68       C  
ATOM    242  CD1AILE A  24     -30.499 -33.312   7.973  0.50 38.21           C  
ANISOU  242  CD1AILE A  24     4550   4911   5055   -320   -240    -78       C  
ATOM    243  CD1BILE A  24     -31.883 -31.225   7.458  0.50 33.39           C  
ANISOU  243  CD1BILE A  24     4622   4064   4000   -214      2   -151       C  
ATOM    244  N   TYR A  25     -30.434 -30.842   2.568  1.00 32.47           N  
ANISOU  244  N   TYR A  25     4233   3778   4325   -393    355    213       N  
ATOM    245  CA  TYR A  25     -29.760 -30.732   1.278  1.00 30.93           C  
ANISOU  245  CA  TYR A  25     4062   3522   4167   -298    417     65       C  
ATOM    246  C   TYR A  25     -28.979 -29.406   1.307  1.00 30.76           C  
ANISOU  246  C   TYR A  25     3980   3559   4146   -359    340     23       C  
ATOM    247  O   TYR A  25     -29.249 -28.522   2.147  1.00 29.32           O  
ANISOU  247  O   TYR A  25     3804   3307   4026   -242    327    131       O  
ATOM    248  CB  TYR A  25     -30.763 -30.710   0.120  1.00 30.31           C  
ANISOU  248  CB  TYR A  25     3970   3354   4188   -363    387   -116       C  
ATOM    249  CG  TYR A  25     -32.024 -29.916   0.394  1.00 31.62           C  
ANISOU  249  CG  TYR A  25     4184   3767   4060   -245    707    -43       C  
ATOM    250  CD1 TYR A  25     -32.005 -28.508   0.343  1.00 28.75           C  
ANISOU  250  CD1 TYR A  25     3788   3640   3495   -343    703     35       C  
ATOM    251  CD2 TYR A  25     -33.247 -30.579   0.719  1.00 32.39           C  
ANISOU  251  CD2 TYR A  25     3491   4036   4777   -126    365     -4       C  
ATOM    252  CE1 TYR A  25     -33.158 -27.753   0.614  1.00 29.79           C  
ANISOU  252  CE1 TYR A  25     3747   3923   3649   -144    501    -32       C  
ATOM    253  CE2 TYR A  25     -34.410 -29.842   1.000  1.00 33.42           C  
ANISOU  253  CE2 TYR A  25     4097   4151   4448    -36    552    133       C  
ATOM    254  CZ  TYR A  25     -34.369 -28.443   0.953  1.00 32.23           C  
ANISOU  254  CZ  TYR A  25     3700   4125   4419   -153    423   -295       C  
ATOM    255  OH  TYR A  25     -35.529 -27.746   1.240  1.00 31.16           O  
ANISOU  255  OH  TYR A  25     3582   3642   4615    -44    456   -403       O  
ATOM    256  N   ASP A  26     -28.049 -29.271   0.378  1.00 30.26           N  
ANISOU  256  N   ASP A  26     3877   3493   4127   -309    389     16       N  
ATOM    257  CA  ASP A  26     -27.306 -28.001   0.234  1.00 29.80           C  
ANISOU  257  CA  ASP A  26     3715   3503   4104   -280    303   -100       C  
ATOM    258  C   ASP A  26     -28.088 -27.093  -0.673  1.00 28.58           C  
ANISOU  258  C   ASP A  26     3560   3452   3844   -197    413   -107       C  
ATOM    259  O   ASP A  26     -28.953 -27.579  -1.399  1.00 29.22           O  
ANISOU  259  O   ASP A  26     3543   3551   4008   -278    427   -129       O  
ATOM    260  CB  ASP A  26     -25.924 -28.286  -0.323  1.00 29.05           C  
ANISOU  260  CB  ASP A  26     3689   3426   3922      0    389   -139       C  
ATOM    261  CG  ASP A  26     -25.166 -29.286   0.545  1.00 32.28           C  
ANISOU  261  CG  ASP A  26     4190   3936   4138    118    -45   -158       C  
ATOM    262  OD1 ASP A  26     -25.084 -29.071   1.756  1.00 33.99           O  
ANISOU  262  OD1 ASP A  26     4262   3985   4668    -87    216   -156       O  
ATOM    263  OD2 ASP A  26     -24.668 -30.323   0.023  1.00 35.67           O  
ANISOU  263  OD2 ASP A  26     4760   3984   4807    235   -285   -363       O  
ATOM    264  N   MET A  27     -27.794 -25.784  -0.683  1.00 27.80           N  
ANISOU  264  N   MET A  27     3458   3338   3767   -314    432    -72       N  
ATOM    265  CA  MET A  27     -28.581 -24.883  -1.531  1.00 26.74           C  
ANISOU  265  CA  MET A  27     3239   3263   3658   -256    553     22       C  
ATOM    266  C   MET A  27     -27.679 -23.801  -2.118  1.00 26.69           C  
ANISOU  266  C   MET A  27     3338   3242   3560   -264    375      3       C  
ATOM    267  O   MET A  27     -26.879 -23.198  -1.381  1.00 28.39           O  
ANISOU  267  O   MET A  27     3560   3526   3700   -506    348    174       O  
ATOM    268  CB  MET A  27     -29.710 -24.154  -0.749  1.00 28.87           C  
ANISOU  268  CB  MET A  27     3277   3763   3929   -416    606    -46       C  
ATOM    269  CG  MET A  27     -30.643 -23.246  -1.745  1.00 29.11           C  
ANISOU  269  CG  MET A  27     3927   3041   4090   -228   1379    361       C  
ATOM    270  SD  MET A  27     -31.883 -22.626  -0.745  1.00 42.50           S  
ANISOU  270  SD  MET A  27     5195   4990   5962    109    522   -156       S  
ATOM    271  CE  MET A  27     -33.040 -23.942  -0.778  1.00 37.90           C  
ANISOU  271  CE  MET A  27     4799   4923   4679   -471    714   -582       C  
ATOM    272  N   ALA A  28     -27.818 -23.554  -3.415  1.00 25.94           N  
ANISOU  272  N   ALA A  28     3417   3146   3293   -185    254    -30       N  
ATOM    273  CA  ALA A  28     -27.104 -22.466  -4.078  1.00 25.27           C  
ANISOU  273  CA  ALA A  28     3104   3036   3459   -126    264    -47       C  
ATOM    274  C   ALA A  28     -28.045 -21.284  -4.262  1.00 25.78           C  
ANISOU  274  C   ALA A  28     3123   3211   3459    -66    138    -74       C  
ATOM    275  O   ALA A  28     -29.253 -21.449  -4.602  1.00 27.66           O  
ANISOU  275  O   ALA A  28     3234   3419   3853   -314     14     30       O  
ATOM    276  CB  ALA A  28     -26.597 -22.898  -5.486  1.00 26.54           C  
ANISOU  276  CB  ALA A  28     3479   3213   3391    -45    158   -219       C  
ATOM    277  N   ILE A  29     -27.505 -20.081  -4.073  1.00 24.27           N  
ANISOU  277  N   ILE A  29     2891   3084   3244     67    103   -130       N  
ATOM    278  CA  ILE A  29     -28.257 -18.868  -4.380  1.00 24.20           C  
ANISOU  278  CA  ILE A  29     2973   3144   3077     81     20   -102       C  
ATOM    279  C   ILE A  29     -27.636 -18.398  -5.699  1.00 24.25           C  
ANISOU  279  C   ILE A  29     3009   3051   3151    -46     71   -127       C  
ATOM    280  O   ILE A  29     -26.427 -18.271  -5.758  1.00 25.72           O  
ANISOU  280  O   ILE A  29     3045   3393   3334     50     93    -77       O  
ATOM    281  CB  ILE A  29     -28.110 -17.783  -3.272  1.00 22.51           C  
ANISOU  281  CB  ILE A  29     2342   3052   3158     27    160   -127       C  
ATOM    282  CG1 ILE A  29     -28.540 -18.375  -1.941  1.00 25.15           C  
ANISOU  282  CG1 ILE A  29     3348   3360   2844   -138     26   -381       C  
ATOM    283  CG2 ILE A  29     -28.912 -16.521  -3.651  1.00 26.23           C  
ANISOU  283  CG2 ILE A  29     3390   3318   3259     74   -236    -56       C  
ATOM    284  CD1 ILE A  29     -28.289 -17.380  -0.729  1.00 27.22           C  
ANISOU  284  CD1 ILE A  29     3562   4046   2731   -218    271   -747       C  
ATOM    285  N   ILE A  30     -28.448 -18.134  -6.725  1.00 23.52           N  
ANISOU  285  N   ILE A  30     3105   2892   2940   -142      2   -209       N  
ATOM    286  CA  ILE A  30     -27.920 -17.886  -8.083  1.00 23.27           C  
ANISOU  286  CA  ILE A  30     3106   2758   2978   -165    -55   -156       C  
ATOM    287  C   ILE A  30     -28.289 -16.453  -8.480  1.00 23.69           C  
ANISOU  287  C   ILE A  30     3085   2939   2976   -109   -130   -297       C  
ATOM    288  O   ILE A  30     -29.490 -16.080  -8.407  1.00 24.38           O  
ANISOU  288  O   ILE A  30     2985   3219   3059    -72    -62   -447       O  
ATOM    289  CB  ILE A  30     -28.518 -18.866  -9.121  1.00 23.94           C  
ANISOU  289  CB  ILE A  30     3284   2829   2982    -77     20   -168       C  
ATOM    290  CG1 ILE A  30     -28.229 -20.360  -8.724  1.00 24.38           C  
ANISOU  290  CG1 ILE A  30     3159   2608   3494   -339    -68   -118       C  
ATOM    291  CG2 ILE A  30     -27.999 -18.505 -10.542  1.00 27.04           C  
ANISOU  291  CG2 ILE A  30     3927   2913   3433   -366   -169    -23       C  
ATOM    292  CD1 ILE A  30     -29.105 -21.370  -9.506  1.00 25.03           C  
ANISOU  292  CD1 ILE A  30     2628   3340   3542   -691    231     -3       C  
ATOM    293  N   PHE A  31     -27.290 -15.655  -8.857  1.00 22.73           N  
ANISOU  293  N   PHE A  31     2962   2933   2741    -64    -61   -155       N  
ATOM    294  CA  PHE A  31     -27.472 -14.188  -9.149  1.00 22.86           C  
ANISOU  294  CA  PHE A  31     2918   2983   2782    -35   -229   -237       C  
ATOM    295  C   PHE A  31     -27.216 -13.890 -10.613  1.00 22.37           C  
ANISOU  295  C   PHE A  31     2922   2875   2701     22   -106   -197       C  
ATOM    296  O   PHE A  31     -26.090 -14.138 -11.127  1.00 22.26           O  
ANISOU  296  O   PHE A  31     2676   2988   2794   -188   -337   -434       O  
ATOM    297  CB  PHE A  31     -26.494 -13.322  -8.356  1.00 22.93           C  
ANISOU  297  CB  PHE A  31     2904   2874   2933     72    -83   -308       C  
ATOM    298  CG  PHE A  31     -26.562 -13.548  -6.876  1.00 24.30           C  
ANISOU  298  CG  PHE A  31     3016   3318   2896      8    -93   -192       C  
ATOM    299  CD1 PHE A  31     -27.697 -13.127  -6.180  1.00 25.19           C  
ANISOU  299  CD1 PHE A  31     3300   3190   3081    100    -15   -217       C  
ATOM    300  CD2 PHE A  31     -25.483 -14.136  -6.155  1.00 23.14           C  
ANISOU  300  CD2 PHE A  31     3075   3041   2675    165   -197    -48       C  
ATOM    301  CE1 PHE A  31     -27.804 -13.272  -4.781  1.00 23.22           C  
ANISOU  301  CE1 PHE A  31     3339   2618   2864   -241   -159    -79       C  
ATOM    302  CE2 PHE A  31     -25.586 -14.300  -4.743  1.00 24.97           C  
ANISOU  302  CE2 PHE A  31     3158   3500   2830   -124   -106   -249       C  
ATOM    303  CZ  PHE A  31     -26.774 -13.858  -4.072  1.00 24.89           C  
ANISOU  303  CZ  PHE A  31     3051   2928   3477   -378   -328   -391       C  
ATOM    304  N   HIS A  32     -28.222 -13.260 -11.234  1.00 23.27           N  
ANISOU  304  N   HIS A  32     3043   3016   2781     16   -269   -274       N  
ATOM    305  CA  HIS A  32     -28.149 -12.839 -12.670  1.00 23.61           C  
ANISOU  305  CA  HIS A  32     3040   2898   3033     40   -296     -9       C  
ATOM    306  C   HIS A  32     -27.296 -11.561 -12.843  1.00 24.25           C  
ANISOU  306  C   HIS A  32     2981   3096   3136      0   -253    -69       C  
ATOM    307  O   HIS A  32     -26.994 -10.891 -11.828  1.00 23.87           O  
ANISOU  307  O   HIS A  32     2929   2967   3171      3   -323   -153       O  
ATOM    308  CB  HIS A  32     -29.597 -12.695 -13.259  1.00 23.18           C  
ANISOU  308  CB  HIS A  32     2771   2913   3121     43   -250   -235       C  
ATOM    309  CG  HIS A  32     -30.387 -11.524 -12.727  1.00 24.79           C  
ANISOU  309  CG  HIS A  32     2994   3223   3202    232   -227    -89       C  
ATOM    310  ND1 HIS A  32     -30.167 -10.228 -13.145  1.00 25.99           N  
ANISOU  310  ND1 HIS A  32     2877   3529   3465    158   -476   -445       N  
ATOM    311  CD2 HIS A  32     -31.403 -11.462 -11.824  1.00 25.69           C  
ANISOU  311  CD2 HIS A  32     3352   3262   3144    283   -218   -489       C  
ATOM    312  CE1 HIS A  32     -31.033  -9.413 -12.537  1.00 25.89           C  
ANISOU  312  CE1 HIS A  32     3224   3758   2854    -90   -437   -501       C  
ATOM    313  NE2 HIS A  32     -31.793 -10.137 -11.730  1.00 24.57           N  
ANISOU  313  NE2 HIS A  32     3001   3094   3239   -228   -197   -470       N  
ATOM    314  N   GLY A  33     -27.040 -11.153 -14.089  1.00 23.22           N  
ANISOU  314  N   GLY A  33     2827   2966   3026    -62   -125    116       N  
ATOM    315  CA  GLY A  33     -26.216  -9.989 -14.313  1.00 24.04           C  
ANISOU  315  CA  GLY A  33     3225   2735   3170     12   -155     31       C  
ATOM    316  C   GLY A  33     -27.027  -8.728 -14.683  1.00 25.85           C  
ANISOU  316  C   GLY A  33     3432   3169   3220     92   -248     24       C  
ATOM    317  O   GLY A  33     -28.281  -8.684 -14.557  1.00 27.34           O  
ANISOU  317  O   GLY A  33     3823   3013   3552     47   -257    -45       O  
ATOM    318  N   PHE A  34     -26.293  -7.688 -15.076  1.00 25.94           N  
ANISOU  318  N   PHE A  34     3707   3095   3052    102   -306     -3       N  
ATOM    319  CA  PHE A  34     -26.848  -6.342 -15.415  1.00 27.26           C  
ANISOU  319  CA  PHE A  34     3868   3446   3042    201   -348    -59       C  
ATOM    320  C   PHE A  34     -27.861  -6.429 -16.591  1.00 28.85           C  
ANISOU  320  C   PHE A  34     3994   3682   3285    145   -350   -176       C  
ATOM    321  O   PHE A  34     -27.490  -6.945 -17.686  1.00 29.13           O  
ANISOU  321  O   PHE A  34     4286   3764   3017    202   -331   -273       O  
ATOM    322  CB  PHE A  34     -25.655  -5.507 -15.786  1.00 25.74           C  
ANISOU  322  CB  PHE A  34     3770   3390   2619    103   -369    -66       C  
ATOM    323  CG  PHE A  34     -25.934  -4.092 -16.148  1.00 27.16           C  
ANISOU  323  CG  PHE A  34     4384   3213   2722   -169   -213    -89       C  
ATOM    324  CD1 PHE A  34     -26.217  -3.117 -15.182  1.00 28.16           C  
ANISOU  324  CD1 PHE A  34     3957   3270   3472   -159     79     -2       C  
ATOM    325  CD2 PHE A  34     -25.806  -3.694 -17.490  1.00 33.29           C  
ANISOU  325  CD2 PHE A  34     5546   3655   3447     60     64    173       C  
ATOM    326  CE1 PHE A  34     -26.401  -1.774 -15.542  1.00 26.22           C  
ANISOU  326  CE1 PHE A  34     3860   3396   2704   -249   -635    276       C  
ATOM    327  CE2 PHE A  34     -25.991  -2.329 -17.861  1.00 32.40           C  
ANISOU  327  CE2 PHE A  34     5496   3608   3207    212    110    105       C  
ATOM    328  CZ  PHE A  34     -26.288  -1.389 -16.879  1.00 31.87           C  
ANISOU  328  CZ  PHE A  34     5144   3458   3505    -49     54    -21       C  
ATOM    329  N   THR A  35     -29.094  -5.954 -16.353  1.00 28.95           N  
ANISOU  329  N   THR A  35     3982   3533   3484    210   -455    -19       N  
ATOM    330  CA  THR A  35     -30.239  -6.014 -17.313  1.00 30.79           C  
ANISOU  330  CA  THR A  35     4202   3815   3680    120   -544   -181       C  
ATOM    331  C   THR A  35     -30.760  -7.428 -17.638  1.00 31.32           C  
ANISOU  331  C   THR A  35     4132   3882   3884     50   -623    -85       C  
ATOM    332  O   THR A  35     -31.652  -7.577 -18.512  1.00 33.74           O  
ANISOU  332  O   THR A  35     4371   4224   4223    100   -735   -112       O  
ATOM    333  CB  THR A  35     -29.968  -5.246 -18.658  1.00 31.71           C  
ANISOU  333  CB  THR A  35     4292   3907   3849    134   -417   -125       C  
ATOM    334  OG1 THR A  35     -29.141  -6.046 -19.552  1.00 33.37           O  
ANISOU  334  OG1 THR A  35     4868   4328   3481    324   -479   -487       O  
ATOM    335  CG2 THR A  35     -29.353  -3.820 -18.442  1.00 30.25           C  
ANISOU  335  CG2 THR A  35     4360   3924   3208    338   -571   -284       C  
ATOM    336  N   ALA A  36     -30.188  -8.464 -17.016  1.00 30.05           N  
ANISOU  336  N   ALA A  36     3968   3613   3835     98   -618   -164       N  
ATOM    337  CA  ALA A  36     -30.711  -9.849 -17.121  1.00 29.64           C  
ANISOU  337  CA  ALA A  36     3794   3528   3937    100   -663   -250       C  
ATOM    338  C   ALA A  36     -31.889 -10.091 -16.164  1.00 29.23           C  
ANISOU  338  C   ALA A  36     3834   3491   3780     91   -589   -293       C  
ATOM    339  O   ALA A  36     -32.570  -9.146 -15.699  1.00 28.42           O  
ANISOU  339  O   ALA A  36     3941   3375   3481     35   -384   -495       O  
ATOM    340  CB  ALA A  36     -29.586 -10.889 -16.846  1.00 30.67           C  
ANISOU  340  CB  ALA A  36     4019   3579   4055    233   -565   -375       C  
ATOM    341  N   ASN A  37     -32.147 -11.380 -15.883  1.00 29.82           N  
ANISOU  341  N   ASN A  37     3733   3709   3886    -40   -480   -426       N  
ATOM    342  CA  ASN A  37     -33.209 -11.780 -15.002  1.00 30.24           C  
ANISOU  342  CA  ASN A  37     3996   3719   3773    -56   -490   -507       C  
ATOM    343  C   ASN A  37     -32.956 -13.204 -14.563  1.00 28.89           C  
ANISOU  343  C   ASN A  37     3692   3665   3618    -91   -563   -545       C  
ATOM    344  O   ASN A  37     -32.048 -13.871 -15.082  1.00 31.68           O  
ANISOU  344  O   ASN A  37     4254   3742   4040   -173   -375   -719       O  
ATOM    345  CB  ASN A  37     -34.595 -11.615 -15.685  1.00 30.86           C  
ANISOU  345  CB  ASN A  37     3933   3773   4018    -30   -727   -500       C  
ATOM    346  CG  ASN A  37     -34.778 -12.586 -16.865  1.00 31.95           C  
ANISOU  346  CG  ASN A  37     4392   3906   3841     12   -571   -347       C  
ATOM    347  OD1 ASN A  37     -35.106 -13.714 -16.667  1.00 32.95           O  
ANISOU  347  OD1 ASN A  37     3695   4337   4487    -81  -1098    -69       O  
ATOM    348  ND2 ASN A  37     -34.521 -12.133 -18.086  1.00 39.68           N  
ANISOU  348  ND2 ASN A  37     5460   5082   4532   -149  -1029   -144       N  
ATOM    349  N   ARG A  38     -33.764 -13.672 -13.641  1.00 27.72           N  
ANISOU  349  N   ARG A  38     3589   3486   3457   -227   -587   -661       N  
ATOM    350  CA  ARG A  38     -33.512 -14.912 -12.944  1.00 28.09           C  
ANISOU  350  CA  ARG A  38     3498   3562   3612   -267   -412   -512       C  
ATOM    351  C   ARG A  38     -33.712 -16.117 -13.857  1.00 28.72           C  
ANISOU  351  C   ARG A  38     3620   3550   3739   -138   -136   -395       C  
ATOM    352  O   ARG A  38     -33.363 -17.205 -13.456  1.00 29.07           O  
ANISOU  352  O   ARG A  38     3686   3393   3964    -95    -66   -473       O  
ATOM    353  CB  ARG A  38     -34.424 -15.020 -11.704  1.00 28.17           C  
ANISOU  353  CB  ARG A  38     3424   3610   3668   -228   -379   -556       C  
ATOM    354  CG  ARG A  38     -35.942 -15.234 -12.020  1.00 30.64           C  
ANISOU  354  CG  ARG A  38     3409   4276   3955   -332   -568   -415       C  
ATOM    355  CD  ARG A  38     -36.754 -15.116 -10.791  1.00 31.37           C  
ANISOU  355  CD  ARG A  38     3272   4090   4557   -263   -317   -465       C  
ATOM    356  NE  ARG A  38     -38.046 -15.818 -10.848  1.00 28.62           N  
ANISOU  356  NE  ARG A  38     3697   3206   3971   -151   -329   -452       N  
ATOM    357  CZ  ARG A  38     -39.178 -15.273 -11.270  1.00 32.63           C  
ANISOU  357  CZ  ARG A  38     3547   3874   4977   -354   -490   -282       C  
ATOM    358  NH1 ARG A  38     -39.165 -14.001 -11.734  1.00 30.24           N  
ANISOU  358  NH1 ARG A  38     3210   3941   4336    170   -303   -344       N  
ATOM    359  NH2 ARG A  38     -40.325 -16.004 -11.247  1.00 30.29           N  
ANISOU  359  NH2 ARG A  38     3214   3482   4813   -234   -321   -507       N  
ATOM    360  N   ASN A  39     -34.238 -15.900 -15.078  1.00 29.50           N  
ANISOU  360  N   ASN A  39     3588   3675   3945   -207   -230   -446       N  
ATOM    361  CA  ASN A  39     -34.609 -17.012 -15.934  1.00 31.15           C  
ANISOU  361  CA  ASN A  39     3920   3745   4170   -143   -136   -417       C  
ATOM    362  C   ASN A  39     -33.951 -17.081 -17.259  1.00 31.74           C  
ANISOU  362  C   ASN A  39     3981   3794   4284    -85   -185   -434       C  
ATOM    363  O   ASN A  39     -34.530 -17.636 -18.193  1.00 31.63           O  
ANISOU  363  O   ASN A  39     3999   3917   4100   -278   -265   -510       O  
ATOM    364  CB  ASN A  39     -36.119 -17.043 -16.157  1.00 32.39           C  
ANISOU  364  CB  ASN A  39     3997   3816   4493    -61   -315   -531       C  
ATOM    365  CG  ASN A  39     -36.854 -17.643 -14.981  1.00 35.28           C  
ANISOU  365  CG  ASN A  39     4429   4291   4682    -84   -244   -500       C  
ATOM    366  OD1 ASN A  39     -37.903 -17.146 -14.553  1.00 41.22           O  
ANISOU  366  OD1 ASN A  39     4552   5459   5651    -73   -130   -899       O  
ATOM    367  ND2 ASN A  39     -36.329 -18.722 -14.458  1.00 38.46           N  
ANISOU  367  ND2 ASN A  39     4685   4618   5307     24   -669   -385       N  
ATOM    368  N   THR A  40     -32.766 -16.500 -17.362  1.00 30.08           N  
ANISOU  368  N   THR A  40     3662   3563   4201   -118   -172   -384       N  
ATOM    369  CA  THR A  40     -31.985 -16.663 -18.554  1.00 30.37           C  
ANISOU  369  CA  THR A  40     3762   3651   4123    -58   -138   -278       C  
ATOM    370  C   THR A  40     -31.722 -18.155 -18.729  1.00 28.21           C  
ANISOU  370  C   THR A  40     3426   3445   3846     43   -162   -245       C  
ATOM    371  O   THR A  40     -31.802 -18.943 -17.767  1.00 27.53           O  
ANISOU  371  O   THR A  40     3109   3470   3878    170   -219   -438       O  
ATOM    372  CB  THR A  40     -30.626 -15.892 -18.519  1.00 29.33           C  
ANISOU  372  CB  THR A  40     3656   3424   4061   -117   -335   -296       C  
ATOM    373  OG1 THR A  40     -29.832 -16.474 -17.497  1.00 32.19           O  
ANISOU  373  OG1 THR A  40     4060   3773   4396    -75   -413   -482       O  
ATOM    374  CG2 THR A  40     -30.805 -14.412 -18.249  1.00 33.18           C  
ANISOU  374  CG2 THR A  40     3970   3966   4669     58    244   -394       C  
ATOM    375  N   SER A  41     -31.415 -18.536 -19.956  1.00 28.77           N  
ANISOU  375  N   SER A  41     3525   3453   3952    176   -169   -301       N  
ATOM    376  CA  SER A  41     -31.134 -19.954 -20.272  1.00 28.97           C  
ANISOU  376  CA  SER A  41     3631   3571   3801    216   -245   -276       C  
ATOM    377  C   SER A  41     -29.993 -20.526 -19.371  1.00 28.00           C  
ANISOU  377  C   SER A  41     3636   3470   3530     78   -231   -276       C  
ATOM    378  O   SER A  41     -30.112 -21.616 -18.778  1.00 27.37           O  
ANISOU  378  O   SER A  41     3775   3257   3365    -50   -383   -381       O  
ATOM    379  CB  SER A  41     -30.746 -20.085 -21.739  1.00 28.86           C  
ANISOU  379  CB  SER A  41     3665   3508   3792    210   -150   -311       C  
ATOM    380  OG  SER A  41     -30.385 -21.439 -21.997  1.00 33.79           O  
ANISOU  380  OG  SER A  41     4025   4277   4534    206   -351   -708       O  
ATOM    381  N   LEU A  42     -28.925 -19.751 -19.245  1.00 25.86           N  
ANISOU  381  N   LEU A  42     3157   3324   3344    134    -64   -272       N  
ATOM    382  CA  LEU A  42     -27.768 -20.125 -18.407  1.00 25.82           C  
ANISOU  382  CA  LEU A  42     3205   3330   3273     86    -69   -379       C  
ATOM    383  C   LEU A  42     -28.165 -20.386 -16.966  1.00 24.87           C  
ANISOU  383  C   LEU A  42     3021   3148   3281     14   -194   -227       C  
ATOM    384  O   LEU A  42     -27.844 -21.457 -16.408  1.00 24.66           O  
ANISOU  384  O   LEU A  42     2800   3403   3165    -29   -143   -232       O  
ATOM    385  CB  LEU A  42     -26.636 -19.088 -18.549  1.00 25.00           C  
ANISOU  385  CB  LEU A  42     2815   3462   3218    111    -43   -330       C  
ATOM    386  CG  LEU A  42     -25.465 -19.312 -17.529  1.00 26.68           C  
ANISOU  386  CG  LEU A  42     3382   3383   3369    394   -109   -379       C  
ATOM    387  CD1 LEU A  42     -24.709 -20.687 -17.793  1.00 29.35           C  
ANISOU  387  CD1 LEU A  42     3356   3743   4053    535    -28  -1058       C  
ATOM    388  CD2 LEU A  42     -24.482 -18.067 -17.567  1.00 26.25           C  
ANISOU  388  CD2 LEU A  42     3234   3797   2941   -203   -420   -689       C  
ATOM    389  N   LEU A  43     -28.891 -19.440 -16.360  1.00 24.82           N  
ANISOU  389  N   LEU A  43     3047   3051   3331    -92   -153   -347       N  
ATOM    390  CA  LEU A  43     -29.306 -19.638 -14.963  1.00 26.05           C  
ANISOU  390  CA  LEU A  43     3428   2981   3487     66   -146   -238       C  
ATOM    391  C   LEU A  43     -30.316 -20.779 -14.800  1.00 26.50           C  
ANISOU  391  C   LEU A  43     3384   3197   3488    107    -68   -194       C  
ATOM    392  O   LEU A  43     -30.256 -21.501 -13.803  1.00 26.25           O  
ANISOU  392  O   LEU A  43     3686   2916   3370    133     -3   -313       O  
ATOM    393  CB  LEU A  43     -29.755 -18.334 -14.258  1.00 26.78           C  
ANISOU  393  CB  LEU A  43     3415   2969   3791    207   -213   -249       C  
ATOM    394  CG  LEU A  43     -28.670 -17.234 -14.441  1.00 28.62           C  
ANISOU  394  CG  LEU A  43     3652   2946   4273    253   -212   -352       C  
ATOM    395  CD1 LEU A  43     -29.128 -15.989 -13.816  1.00 31.77           C  
ANISOU  395  CD1 LEU A  43     4589   3106   4374     58    -49  -1069       C  
ATOM    396  CD2 LEU A  43     -27.367 -17.610 -13.800  1.00 31.54           C  
ANISOU  396  CD2 LEU A  43     3808   3503   4670    -15   -618   -298       C  
ATOM    397  N   ARG A  44     -31.235 -20.956 -15.754  1.00 26.79           N  
ANISOU  397  N   ARG A  44     3428   3240   3511    127   -177   -291       N  
ATOM    398  CA  ARG A  44     -32.186 -22.048 -15.643  1.00 28.20           C  
ANISOU  398  CA  ARG A  44     3403   3420   3890    149   -264   -188       C  
ATOM    399  C   ARG A  44     -31.434 -23.359 -15.722  1.00 28.50           C  
ANISOU  399  C   ARG A  44     3720   3313   3795     58   -246   -257       C  
ATOM    400  O   ARG A  44     -31.743 -24.266 -14.967  1.00 28.87           O  
ANISOU  400  O   ARG A  44     3657   3440   3871    136   -331   -250       O  
ATOM    401  CB  ARG A  44     -33.241 -22.003 -16.751  1.00 29.14           C  
ANISOU  401  CB  ARG A  44     3619   3607   3844     51   -387   -227       C  
ATOM    402  CG  ARG A  44     -34.277 -20.938 -16.485  1.00 33.70           C  
ANISOU  402  CG  ARG A  44     3712   4404   4689    150   -691   -330       C  
ATOM    403  CD  ARG A  44     -35.413 -20.985 -17.488  1.00 35.42           C  
ANISOU  403  CD  ARG A  44     4250   4896   4310     38   -969   -474       C  
ATOM    404  NE  ARG A  44     -35.044 -20.358 -18.761  1.00 38.12           N  
ANISOU  404  NE  ARG A  44     4410   4999   5072   -154   -724   -388       N  
ATOM    405  CZ  ARG A  44     -34.757 -21.058 -19.839  1.00 36.56           C  
ANISOU  405  CZ  ARG A  44     3680   5371   4839      0   -664    -25       C  
ATOM    406  NH1 ARG A  44     -34.797 -22.372 -19.743  1.00 38.19           N  
ANISOU  406  NH1 ARG A  44     4072   5020   5415    287  -1042   -428       N  
ATOM    407  NH2 ARG A  44     -34.464 -20.470 -20.989  1.00 38.67           N  
ANISOU  407  NH2 ARG A  44     3770   6205   4717    -67   -590    673       N  
ATOM    408  N   GLU A  45     -30.436 -23.436 -16.598  1.00 27.64           N  
ANISOU  408  N   GLU A  45     3437   3232   3833     58   -252   -173       N  
ATOM    409  CA  GLU A  45     -29.815 -24.759 -16.826  1.00 28.88           C  
ANISOU  409  CA  GLU A  45     3753   3357   3864     81   -120   -255       C  
ATOM    410  C   GLU A  45     -28.883 -25.083 -15.680  1.00 28.24           C  
ANISOU  410  C   GLU A  45     3621   3329   3779     73    -69   -240       C  
ATOM    411  O   GLU A  45     -28.737 -26.243 -15.330  1.00 28.64           O  
ANISOU  411  O   GLU A  45     3682   3338   3861     10    -40   -301       O  
ATOM    412  CB  GLU A  45     -29.128 -24.891 -18.157  1.00 29.76           C  
ANISOU  412  CB  GLU A  45     4025   3489   3794    -79   -225    -23       C  
ATOM    413  CG  GLU A  45     -30.128 -24.860 -19.279  1.00 34.45           C  
ANISOU  413  CG  GLU A  45     4476   4015   4597   -175   -413   -273       C  
ATOM    414  CD  GLU A  45     -31.145 -26.007 -19.289  1.00 36.91           C  
ANISOU  414  CD  GLU A  45     5146   3966   4910   -340   -584   -137       C  
ATOM    415  OE1 GLU A  45     -31.035 -27.017 -18.548  1.00 36.68           O  
ANISOU  415  OE1 GLU A  45     5535   3222   5177   -462   -243   -325       O  
ATOM    416  OE2 GLU A  45     -32.113 -25.863 -20.071  1.00 41.28           O  
ANISOU  416  OE2 GLU A  45     5582   4692   5408   -640   -595   -483       O  
ATOM    417  N   ILE A  46     -28.253 -24.050 -15.096  1.00 27.15           N  
ANISOU  417  N   ILE A  46     3511   3138   3666     94   -130   -373       N  
ATOM    418  CA  ILE A  46     -27.545 -24.238 -13.842  1.00 27.53           C  
ANISOU  418  CA  ILE A  46     3559   3142   3758    -67    -19   -428       C  
ATOM    419  C   ILE A  46     -28.472 -24.790 -12.740  1.00 28.79           C  
ANISOU  419  C   ILE A  46     3615   3415   3910    -90    -56   -370       C  
ATOM    420  O   ILE A  46     -28.121 -25.779 -12.084  1.00 28.77           O  
ANISOU  420  O   ILE A  46     3630   3512   3788   -255   -186   -245       O  
ATOM    421  CB  ILE A  46     -26.801 -22.984 -13.371  1.00 27.51           C  
ANISOU  421  CB  ILE A  46     3316   3367   3767   -259   -122   -353       C  
ATOM    422  CG1 ILE A  46     -25.545 -22.729 -14.260  1.00 24.74           C  
ANISOU  422  CG1 ILE A  46     3203   2808   3388    -32    264   -547       C  
ATOM    423  CG2 ILE A  46     -26.424 -23.168 -11.935  1.00 24.94           C  
ANISOU  423  CG2 ILE A  46     3381   2822   3272   -300    332   -560       C  
ATOM    424  CD1 ILE A  46     -24.881 -21.346 -13.947  1.00 28.67           C  
ANISOU  424  CD1 ILE A  46     3773   3225   3894   -326    643   -689       C  
ATOM    425  N   ALA A  47     -29.635 -24.157 -12.523  1.00 28.24           N  
ANISOU  425  N   ALA A  47     3301   3547   3880   -265    -99   -513       N  
ATOM    426  CA  ALA A  47     -30.523 -24.616 -11.451  1.00 28.87           C  
ANISOU  426  CA  ALA A  47     3492   3500   3975    -96     15   -460       C  
ATOM    427  C   ALA A  47     -31.003 -26.055 -11.723  1.00 28.36           C  
ANISOU  427  C   ALA A  47     3329   3518   3927    -46     59   -324       C  
ATOM    428  O   ALA A  47     -31.099 -26.873 -10.780  1.00 28.95           O  
ANISOU  428  O   ALA A  47     3557   3442   4000     32     53   -292       O  
ATOM    429  CB  ALA A  47     -31.714 -23.631 -11.269  1.00 28.07           C  
ANISOU  429  CB  ALA A  47     3132   3614   3918    -82    127   -404       C  
ATOM    430  N   ASN A  48     -31.296 -26.338 -13.008  1.00 27.23           N  
ANISOU  430  N   ASN A  48     3029   3467   3849   -121    -80   -480       N  
ATOM    431  CA  ASN A  48     -31.821 -27.671 -13.399  1.00 29.59           C  
ANISOU  431  CA  ASN A  48     3777   3485   3979     47    -71   -326       C  
ATOM    432  C   ASN A  48     -30.787 -28.749 -13.086  1.00 28.88           C  
ANISOU  432  C   ASN A  48     3593   3534   3844    -19    -73   -161       C  
ATOM    433  O   ASN A  48     -31.132 -29.796 -12.555  1.00 28.71           O  
ANISOU  433  O   ASN A  48     3561   3492   3854     45     33      0       O  
ATOM    434  CB  ASN A  48     -32.194 -27.722 -14.923  1.00 29.54           C  
ANISOU  434  CB  ASN A  48     3836   3509   3875     15   -139   -414       C  
ATOM    435  CG  ASN A  48     -33.470 -26.895 -15.292  1.00 35.20           C  
ANISOU  435  CG  ASN A  48     4494   4427   4454    -97   -162   -483       C  
ATOM    436  OD1 ASN A  48     -34.202 -26.425 -14.436  1.00 38.84           O  
ANISOU  436  OD1 ASN A  48     4493   5562   4699     14      0   -691       O  
ATOM    437  ND2 ASN A  48     -33.695 -26.700 -16.592  1.00 39.85           N  
ANISOU  437  ND2 ASN A  48     5735   4749   4655   -399    -49   -549       N  
ATOM    438  N   SER A  49     -29.525 -28.480 -13.449  1.00 28.51           N  
ANISOU  438  N   SER A  49     3512   3401   3916    -19    -18   -156       N  
ATOM    439  CA  SER A  49     -28.407 -29.434 -13.303  1.00 27.71           C  
ANISOU  439  CA  SER A  49     3364   3474   3688    -88    -10    -92       C  
ATOM    440  C   SER A  49     -28.120 -29.665 -11.799  1.00 27.41           C  
ANISOU  440  C   SER A  49     3301   3434   3680   -160    -30   -155       C  
ATOM    441  O   SER A  49     -27.937 -30.802 -11.360  1.00 27.88           O  
ANISOU  441  O   SER A  49     3524   3420   3648   -265    -52   -298       O  
ATOM    442  CB  SER A  49     -27.157 -28.975 -14.076  1.00 26.47           C  
ANISOU  442  CB  SER A  49     3165   3345   3547    105    -78    -11       C  
ATOM    443  OG  SER A  49     -26.062 -29.863 -13.800  1.00 28.63           O  
ANISOU  443  OG  SER A  49     3412   3679   3785     77     -6   -265       O  
ATOM    444  N   LEU A  50     -28.118 -28.583 -11.009  1.00 26.57           N  
ANISOU  444  N   LEU A  50     3069   3257   3769   -299    160   -232       N  
ATOM    445  CA  LEU A  50     -27.999 -28.690  -9.568  1.00 26.52           C  
ANISOU  445  CA  LEU A  50     3144   3182   3747   -310    228   -139       C  
ATOM    446  C   LEU A  50     -29.126 -29.545  -8.988  1.00 27.88           C  
ANISOU  446  C   LEU A  50     3426   3300   3867   -320    280   -163       C  
ATOM    447  O   LEU A  50     -28.865 -30.414  -8.140  1.00 29.12           O  
ANISOU  447  O   LEU A  50     3616   3349   4099   -328    367   -167       O  
ATOM    448  CB  LEU A  50     -27.954 -27.298  -8.862  1.00 25.74           C  
ANISOU  448  CB  LEU A  50     2932   3164   3681   -191    308   -298       C  
ATOM    449  CG  LEU A  50     -26.673 -26.508  -9.176  1.00 25.70           C  
ANISOU  449  CG  LEU A  50     3145   2931   3688   -179     99   -141       C  
ATOM    450  CD1 LEU A  50     -26.791 -25.085  -8.702  1.00 23.69           C  
ANISOU  450  CD1 LEU A  50     3049   2698   3252   -148    170   -180       C  
ATOM    451  CD2 LEU A  50     -25.411 -27.224  -8.547  1.00 28.09           C  
ANISOU  451  CD2 LEU A  50     3399   3226   4045    333    321     -4       C  
ATOM    452  N   ARG A  51     -30.349 -29.323  -9.455  1.00 30.46           N  
ANISOU  452  N   ARG A  51     3748   3510   4314   -289    282    -81       N  
ATOM    453  CA  ARG A  51     -31.503 -30.066  -8.854  1.00 33.34           C  
ANISOU  453  CA  ARG A  51     4052   3890   4722   -416    227    -16       C  
ATOM    454  C   ARG A  51     -31.385 -31.577  -9.187  1.00 33.37           C  
ANISOU  454  C   ARG A  51     4207   3858   4612   -309    206    -37       C  
ATOM    455  O   ARG A  51     -31.766 -32.404  -8.363  1.00 33.11           O  
ANISOU  455  O   ARG A  51     4118   3902   4561   -383    339    149       O  
ATOM    456  CB  ARG A  51     -32.845 -29.485  -9.289  1.00 35.29           C  
ANISOU  456  CB  ARG A  51     4280   3995   5133   -323    165     27       C  
ATOM    457  CG  ARG A  51     -34.167 -29.876  -8.436  1.00 40.10           C  
ANISOU  457  CG  ARG A  51     5103   4935   5198   -657    190     92       C  
ATOM    458  CD  ARG A  51     -35.427 -29.635  -9.352  1.00 46.55           C  
ANISOU  458  CD  ARG A  51     5927   6113   5646   -844   -314    -97       C  
ATOM    459  NE  ARG A  51     -35.089 -30.296 -10.635  1.00 50.69           N  
ANISOU  459  NE  ARG A  51     6993   5829   6437   -834    -69   -487       N  
ATOM    460  CZ  ARG A  51     -35.017 -29.740 -11.855  1.00 50.36           C  
ANISOU  460  CZ  ARG A  51     6775   6000   6358   -863    -99   -431       C  
ATOM    461  NH1 ARG A  51     -35.323 -28.447 -12.063  1.00 49.25           N  
ANISOU  461  NH1 ARG A  51     6285   6011   6415   -564    -76  -1021       N  
ATOM    462  NH2 ARG A  51     -34.642 -30.503 -12.894  1.00 51.90           N  
ANISOU  462  NH2 ARG A  51     7087   5622   7010   -894    210   -473       N  
ATOM    463  N   ASP A  52     -30.869 -31.911 -10.387  1.00 33.77           N  
ANISOU  463  N   ASP A  52     4149   3978   4704   -327    150    -73       N  
ATOM    464  CA  ASP A  52     -30.593 -33.326 -10.747  1.00 34.67           C  
ANISOU  464  CA  ASP A  52     4399   4117   4654   -276    117   -275       C  
ATOM    465  C   ASP A  52     -29.670 -34.012  -9.731  1.00 33.99           C  
ANISOU  465  C   ASP A  52     4443   4002   4470   -259    220   -123       C  
ATOM    466  O   ASP A  52     -29.725 -35.226  -9.573  1.00 35.12           O  
ANISOU  466  O   ASP A  52     4777   4158   4406   -344    306   -328       O  
ATOM    467  CB  ASP A  52     -29.989 -33.421 -12.132  1.00 35.51           C  
ANISOU  467  CB  ASP A  52     4602   4164   4724   -340     81   -431       C  
ATOM    468  CG  ASP A  52     -30.967 -33.014 -13.232  1.00 41.23           C  
ANISOU  468  CG  ASP A  52     5356   4854   5453   -236     -9   -564       C  
ATOM    469  OD1 ASP A  52     -32.188 -32.889 -12.951  1.00 48.22           O  
ANISOU  469  OD1 ASP A  52     5739   5822   6759   -432    -29   -894       O  
ATOM    470  OD2 ASP A  52     -30.529 -32.808 -14.386  1.00 47.56           O  
ANISOU  470  OD2 ASP A  52     6803   5833   5432   -240     36   -907       O  
ATOM    471  N   GLU A  53     -28.814 -33.228  -9.063  1.00 32.74           N  
ANISOU  471  N   GLU A  53     4404   3862   4173   -212    227   -125       N  
ATOM    472  CA  GLU A  53     -27.817 -33.684  -8.061  1.00 32.51           C  
ANISOU  472  CA  GLU A  53     4255   3703   4391   -115    303    -58       C  
ATOM    473  C   GLU A  53     -28.353 -33.527  -6.648  1.00 32.16           C  
ANISOU  473  C   GLU A  53     4231   3688   4301   -119    254    -67       C  
ATOM    474  O   GLU A  53     -27.604 -33.645  -5.650  1.00 32.08           O  
ANISOU  474  O   GLU A  53     4171   3567   4451    -36    267   -192       O  
ATOM    475  CB  GLU A  53     -26.466 -32.916  -8.215  1.00 32.57           C  
ANISOU  475  CB  GLU A  53     4254   3728   4393   -162    312    -50       C  
ATOM    476  CG  GLU A  53     -25.826 -33.083  -9.622  1.00 36.03           C  
ANISOU  476  CG  GLU A  53     4769   4025   4893    138    417     82       C  
ATOM    477  CD  GLU A  53     -25.685 -34.537 -10.061  1.00 42.19           C  
ANISOU  477  CD  GLU A  53     6117   4856   5057    583    314   -204       C  
ATOM    478  OE1 GLU A  53     -25.400 -35.399  -9.204  1.00 44.02           O  
ANISOU  478  OE1 GLU A  53     6505   4537   5682    853    859    324       O  
ATOM    479  OE2 GLU A  53     -25.859 -34.825 -11.261  1.00 43.40           O  
ANISOU  479  OE2 GLU A  53     6828   4968   4694    746    781   -448       O  
ATOM    480  N   ASN A  54     -29.662 -33.242  -6.574  1.00 32.13           N  
ANISOU  480  N   ASN A  54     4305   3615   4287   -237    329    -76       N  
ATOM    481  CA  ASN A  54     -30.327 -32.874  -5.287  1.00 32.10           C  
ANISOU  481  CA  ASN A  54     4301   3661   4235   -202    358     78       C  
ATOM    482  C   ASN A  54     -29.744 -31.694  -4.539  1.00 30.76           C  
ANISOU  482  C   ASN A  54     3984   3698   4004    -72    302     36       C  
ATOM    483  O   ASN A  54     -29.738 -31.668  -3.330  1.00 31.42           O  
ANISOU  483  O   ASN A  54     4175   3940   3822   -168    381    -79       O  
ATOM    484  CB  ASN A  54     -30.427 -34.088  -4.342  1.00 34.37           C  
ANISOU  484  CB  ASN A  54     4612   3860   4587   -129    235    105       C  
ATOM    485  CG  ASN A  54     -31.532 -34.982  -4.747  1.00 37.54           C  
ANISOU  485  CG  ASN A  54     4959   4036   5267   -187    224    213       C  
ATOM    486  OD1 ASN A  54     -32.632 -34.517  -5.121  1.00 38.39           O  
ANISOU  486  OD1 ASN A  54     4940   4418   5228    -42     87   -299       O  
ATOM    487  ND2 ASN A  54     -31.263 -36.277  -4.734  1.00 42.71           N  
ANISOU  487  ND2 ASN A  54     5984   4102   6141    196    409   -445       N  
ATOM    488  N   ILE A  55     -29.208 -30.722  -5.263  1.00 29.22           N  
ANISOU  488  N   ILE A  55     3651   3311   4140    -65    252      8       N  
ATOM    489  CA  ILE A  55     -28.793 -29.481  -4.628  1.00 27.25           C  
ANISOU  489  CA  ILE A  55     3303   3201   3847    -50    124    -76       C  
ATOM    490  C   ILE A  55     -29.919 -28.456  -4.945  1.00 26.65           C  
ANISOU  490  C   ILE A  55     3221   3149   3756   -152     81   -103       C  
ATOM    491  O   ILE A  55     -30.251 -28.217  -6.123  1.00 28.20           O  
ANISOU  491  O   ILE A  55     3598   3239   3876   -119    262   -247       O  
ATOM    492  CB  ILE A  55     -27.432 -28.990  -5.235  1.00 27.28           C  
ANISOU  492  CB  ILE A  55     3222   3142   3998    -55    115    -97       C  
ATOM    493  CG1 ILE A  55     -26.322 -30.077  -4.969  1.00 28.88           C  
ANISOU  493  CG1 ILE A  55     3303   3654   4013    110    185    -39       C  
ATOM    494  CG2 ILE A  55     -27.087 -27.592  -4.699  1.00 25.17           C  
ANISOU  494  CG2 ILE A  55     3552   2781   3229    -86    -58    -82       C  
ATOM    495  CD1 ILE A  55     -24.958 -29.823  -5.664  1.00 32.24           C  
ANISOU  495  CD1 ILE A  55     3681   4616   3952     70    667    -39       C  
ATOM    496  N   ALA A  56     -30.483 -27.855  -3.900  1.00 26.24           N  
ANISOU  496  N   ALA A  56     3116   3128   3723   -278     65    -50       N  
ATOM    497  CA  ALA A  56     -31.620 -26.948  -4.071  1.00 26.01           C  
ANISOU  497  CA  ALA A  56     3362   3066   3455   -205     95    -98       C  
ATOM    498  C   ALA A  56     -31.054 -25.664  -4.601  1.00 26.08           C  
ANISOU  498  C   ALA A  56     3191   3337   3382   -229    194     71       C  
ATOM    499  O   ALA A  56     -29.848 -25.453  -4.502  1.00 24.60           O  
ANISOU  499  O   ALA A  56     2865   3075   3404    -55    310   -132       O  
ATOM    500  CB  ALA A  56     -32.317 -26.668  -2.715  1.00 26.19           C  
ANISOU  500  CB  ALA A  56     3420   3364   3166   -259    180     64       C  
ATOM    501  N   SER A  57     -31.908 -24.788  -5.116  1.00 26.44           N  
ANISOU  501  N   SER A  57     3207   3196   3642   -104    279    -10       N  
ATOM    502  CA  SER A  57     -31.442 -23.463  -5.422  1.00 26.83           C  
ANISOU  502  CA  SER A  57     3151   3283   3760    -86    229    -36       C  
ATOM    503  C   SER A  57     -32.532 -22.479  -5.353  1.00 27.19           C  
ANISOU  503  C   SER A  57     3249   3374   3706   -140    262   -190       C  
ATOM    504  O   SER A  57     -33.715 -22.818  -5.501  1.00 27.41           O  
ANISOU  504  O   SER A  57     3051   3429   3935     27    182   -372       O  
ATOM    505  CB  SER A  57     -30.811 -23.404  -6.824  1.00 27.22           C  
ANISOU  505  CB  SER A  57     3222   3421   3700    -10    222   -108       C  
ATOM    506  OG  SER A  57     -31.674 -23.758  -7.891  1.00 26.39           O  
ANISOU  506  OG  SER A  57     3130   3190   3707   -275    416   -327       O  
ATOM    507  N   VAL A  58     -32.141 -21.230  -5.179  1.00 26.08           N  
ANISOU  507  N   VAL A  58     3087   3306   3514    -69    243   -160       N  
ATOM    508  CA AVAL A  58     -33.067 -20.169  -5.373  0.50 26.46           C  
ANISOU  508  CA AVAL A  58     3232   3339   3481    -89    101   -139       C  
ATOM    509  CA BVAL A  58     -33.064 -20.147  -5.354  0.50 26.44           C  
ANISOU  509  CA BVAL A  58     3201   3419   3424   -172     60    -60       C  
ATOM    510  C   VAL A  58     -32.431 -19.123  -6.302  1.00 26.12           C  
ANISOU  510  C   VAL A  58     3190   3395   3338    -89     99    -73       C  
ATOM    511  O   VAL A  58     -31.212 -18.909  -6.273  1.00 25.84           O  
ANISOU  511  O   VAL A  58     2998   3446   3371   -170   -114    -80       O  
ATOM    512  CB AVAL A  58     -33.522 -19.618  -3.987  0.50 25.71           C  
ANISOU  512  CB AVAL A  58     3100   3286   3381    -35     29   -239       C  
ATOM    513  CB BVAL A  58     -33.371 -19.460  -4.005  0.50 25.62           C  
ANISOU  513  CB BVAL A  58     3074   3371   3289   -111    126    -47       C  
ATOM    514  CG1AVAL A  58     -32.411 -18.684  -3.287  0.50 20.10           C  
ANISOU  514  CG1AVAL A  58     2507   2109   3021    -52    174   -236       C  
ATOM    515  CG1BVAL A  58     -33.997 -18.186  -4.247  0.50 27.22           C  
ANISOU  515  CG1BVAL A  58     3165   3584   3594   -608    -67     91       C  
ATOM    516  CG2AVAL A  58     -34.953 -19.105  -4.058  0.50 29.45           C  
ANISOU  516  CG2AVAL A  58     3676   3667   3846   -121    229   -257       C  
ATOM    517  CG2BVAL A  58     -34.243 -20.364  -3.070  0.50 22.30           C  
ANISOU  517  CG2BVAL A  58     2783   2939   2749   -412    -96    -54       C  
ATOM    518  N   ARG A  59     -33.244 -18.480  -7.108  1.00 26.02           N  
ANISOU  518  N   ARG A  59     3109   3328   3448    -78     -2   -360       N  
ATOM    519  CA  ARG A  59     -32.777 -17.470  -8.044  1.00 25.12           C  
ANISOU  519  CA  ARG A  59     3067   3014   3460     80     11   -311       C  
ATOM    520  C   ARG A  59     -33.837 -16.341  -8.076  1.00 26.45           C  
ANISOU  520  C   ARG A  59     3102   3188   3758     52    -19   -396       C  
ATOM    521  O   ARG A  59     -35.005 -16.597  -8.327  1.00 26.60           O  
ANISOU  521  O   ARG A  59     3047   2960   4100    -12     47   -352       O  
ATOM    522  CB  ARG A  59     -32.444 -18.046  -9.442  1.00 27.04           C  
ANISOU  522  CB  ARG A  59     3210   3396   3666   -117    -58   -470       C  
ATOM    523  CG  ARG A  59     -33.617 -18.678 -10.199  1.00 27.80           C  
ANISOU  523  CG  ARG A  59     3354   3525   3683   -234    -58   -542       C  
ATOM    524  CD  ARG A  59     -33.108 -19.510 -11.412  1.00 28.16           C  
ANISOU  524  CD  ARG A  59     3417   3514   3769   -126    189   -522       C  
ATOM    525  NE  ARG A  59     -34.194 -19.907 -12.331  1.00 31.30           N  
ANISOU  525  NE  ARG A  59     3776   3702   4415   -118    168   -796       N  
ATOM    526  CZ  ARG A  59     -34.927 -21.009 -12.192  1.00 31.07           C  
ANISOU  526  CZ  ARG A  59     3827   3932   4046   -186     76   -477       C  
ATOM    527  NH1 ARG A  59     -34.725 -21.851 -11.174  1.00 31.97           N  
ANISOU  527  NH1 ARG A  59     4217   3825   4103   -340   -277   -542       N  
ATOM    528  NH2 ARG A  59     -35.874 -21.268 -13.074  1.00 34.11           N  
ANISOU  528  NH2 ARG A  59     4788   4018   4153   -214   -146   -760       N  
ATOM    529  N   PHE A  60     -33.407 -15.127  -7.716  1.00 25.23           N  
ANISOU  529  N   PHE A  60     3056   2942   3586     59     93   -463       N  
ATOM    530  CA  PHE A  60     -34.338 -13.971  -7.614  1.00 26.01           C  
ANISOU  530  CA  PHE A  60     3202   3192   3486    -19    -38   -391       C  
ATOM    531  C   PHE A  60     -34.007 -12.953  -8.675  1.00 26.66           C  
ANISOU  531  C   PHE A  60     3294   3261   3571    -35    -84   -468       C  
ATOM    532  O   PHE A  60     -32.818 -12.784  -9.092  1.00 26.17           O  
ANISOU  532  O   PHE A  60     3122   3328   3494     69   -103   -589       O  
ATOM    533  CB  PHE A  60     -34.214 -13.310  -6.221  1.00 26.40           C  
ANISOU  533  CB  PHE A  60     3088   3418   3523   -100     57   -373       C  
ATOM    534  CG  PHE A  60     -34.977 -14.009  -5.141  1.00 28.30           C  
ANISOU  534  CG  PHE A  60     3518   3792   3442    -72     40   -259       C  
ATOM    535  CD1 PHE A  60     -36.239 -13.533  -4.749  1.00 28.30           C  
ANISOU  535  CD1 PHE A  60     3227   3875   3649   -525    112   -697       C  
ATOM    536  CD2 PHE A  60     -34.472 -15.137  -4.535  1.00 27.80           C  
ANISOU  536  CD2 PHE A  60     3607   3559   3396   -121    183   -335       C  
ATOM    537  CE1 PHE A  60     -36.984 -14.183  -3.729  1.00 26.31           C  
ANISOU  537  CE1 PHE A  60     2903   3904   3190   -130    184   -419       C  
ATOM    538  CE2 PHE A  60     -35.211 -15.791  -3.500  1.00 28.51           C  
ANISOU  538  CE2 PHE A  60     3667   3191   3973   -334    582   -170       C  
ATOM    539  CZ  PHE A  60     -36.500 -15.301  -3.126  1.00 28.73           C  
ANISOU  539  CZ  PHE A  60     3277   3534   4104   -432    -53   -363       C  
ATOM    540  N   ASP A  61     -35.019 -12.211  -9.099  1.00 26.10           N  
ANISOU  540  N   ASP A  61     3049   3379   3486    -16   -255   -297       N  
ATOM    541  CA  ASP A  61     -34.759 -10.979  -9.814  1.00 26.99           C  
ANISOU  541  CA  ASP A  61     3264   3412   3577   -127   -373   -311       C  
ATOM    542  C   ASP A  61     -34.307  -9.904  -8.883  1.00 26.90           C  
ANISOU  542  C   ASP A  61     3223   3345   3650    -94   -303   -205       C  
ATOM    543  O   ASP A  61     -34.927  -9.682  -7.831  1.00 27.31           O  
ANISOU  543  O   ASP A  61     3255   3382   3737   -378   -217   -417       O  
ATOM    544  CB  ASP A  61     -36.032 -10.519 -10.533  1.00 28.13           C  
ANISOU  544  CB  ASP A  61     3387   3540   3762    -24   -454   -416       C  
ATOM    545  CG  ASP A  61     -36.348 -11.408 -11.725  1.00 30.42           C  
ANISOU  545  CG  ASP A  61     3745   3666   4147      0   -258   -659       C  
ATOM    546  OD1 ASP A  61     -35.381 -11.803 -12.424  1.00 31.84           O  
ANISOU  546  OD1 ASP A  61     4007   3936   4154    309   -143   -759       O  
ATOM    547  OD2 ASP A  61     -37.539 -11.726 -11.939  1.00 30.97           O  
ANISOU  547  OD2 ASP A  61     3701   3444   4620   -205   -455   -947       O  
ATOM    548  N   PHE A  62     -33.190  -9.250  -9.243  1.00 27.16           N  
ANISOU  548  N   PHE A  62     3414   3163   3739    -97   -384   -197       N  
ATOM    549  CA  PHE A  62     -32.728  -8.093  -8.442  1.00 25.74           C  
ANISOU  549  CA  PHE A  62     3105   3085   3589     -8   -336   -279       C  
ATOM    550  C   PHE A  62     -33.720  -6.947  -8.551  1.00 25.32           C  
ANISOU  550  C   PHE A  62     3146   3026   3446     75   -276   -373       C  
ATOM    551  O   PHE A  62     -34.503  -6.877  -9.502  1.00 27.13           O  
ANISOU  551  O   PHE A  62     3372   3090   3844    114   -287   -493       O  
ATOM    552  CB  PHE A  62     -31.349  -7.584  -8.939  1.00 25.00           C  
ANISOU  552  CB  PHE A  62     2942   2937   3617     36   -259   -128       C  
ATOM    553  CG  PHE A  62     -30.197  -8.413  -8.421  1.00 23.05           C  
ANISOU  553  CG  PHE A  62     2441   3248   3068   -124   -278    165       C  
ATOM    554  CD1 PHE A  62     -29.919  -8.474  -7.025  1.00 22.84           C  
ANISOU  554  CD1 PHE A  62     2810   2905   2963     28   -364   -348       C  
ATOM    555  CD2 PHE A  62     -29.430  -9.171  -9.297  1.00 23.17           C  
ANISOU  555  CD2 PHE A  62     2770   2766   3265    -25   -470    -31       C  
ATOM    556  CE1 PHE A  62     -28.821  -9.247  -6.539  1.00 23.97           C  
ANISOU  556  CE1 PHE A  62     3043   2903   3161    149     13   -375       C  
ATOM    557  CE2 PHE A  62     -28.332  -9.966  -8.803  1.00 22.55           C  
ANISOU  557  CE2 PHE A  62     3027   2892   2646    154   -260    -22       C  
ATOM    558  CZ  PHE A  62     -28.049 -10.000  -7.423  1.00 23.70           C  
ANISOU  558  CZ  PHE A  62     2824   3225   2957   -342    -29   -431       C  
ATOM    559  N   ASN A  63     -33.640  -6.001  -7.626  1.00 25.34           N  
ANISOU  559  N   ASN A  63     3255   3149   3222     86   -369   -438       N  
ATOM    560  CA  ASN A  63     -34.439  -4.785  -7.763  1.00 24.78           C  
ANISOU  560  CA  ASN A  63     3169   3111   3136     54   -333   -362       C  
ATOM    561  C   ASN A  63     -34.202  -4.142  -9.138  1.00 24.96           C  
ANISOU  561  C   ASN A  63     3093   3189   3200    -54   -262   -355       C  
ATOM    562  O   ASN A  63     -33.077  -4.190  -9.692  1.00 23.17           O  
ANISOU  562  O   ASN A  63     2570   3183   3049    124   -377   -377       O  
ATOM    563  CB  ASN A  63     -34.210  -3.787  -6.613  1.00 24.79           C  
ANISOU  563  CB  ASN A  63     3083   3049   3287    -56   -352   -534       C  
ATOM    564  CG  ASN A  63     -32.872  -3.047  -6.734  1.00 23.83           C  
ANISOU  564  CG  ASN A  63     3065   2635   3354    -72   -406    -50       C  
ATOM    565  OD1 ASN A  63     -32.826  -1.981  -7.306  1.00 26.97           O  
ANISOU  565  OD1 ASN A  63     3578   2911   3758   -185   -378   -272       O  
ATOM    566  ND2 ASN A  63     -31.780  -3.645  -6.232  1.00 24.15           N  
ANISOU  566  ND2 ASN A  63     2718   3038   3419    216   -373   -239       N  
ATOM    567  N   GLY A  64     -35.251  -3.552  -9.700  1.00 24.75           N  
ANISOU  567  N   GLY A  64     2912   3198   3293    -39   -301   -313       N  
ATOM    568  CA  GLY A  64     -35.097  -2.888 -10.986  1.00 25.34           C  
ANISOU  568  CA  GLY A  64     3015   3211   3400     18   -239   -309       C  
ATOM    569  C   GLY A  64     -35.027  -3.840 -12.162  1.00 25.89           C  
ANISOU  569  C   GLY A  64     3065   3180   3589     46   -159   -314       C  
ATOM    570  O   GLY A  64     -34.759  -3.413 -13.303  1.00 26.59           O  
ANISOU  570  O   GLY A  64     3433   3097   3570     51   -278   -424       O  
ATOM    571  N   HIS A  65     -35.244  -5.130 -11.878  1.00 28.38           N  
ANISOU  571  N   HIS A  65     3333   3522   3927     65    -82   -314       N  
ATOM    572  CA  HIS A  65     -35.122  -6.216 -12.893  1.00 27.57           C  
ANISOU  572  CA  HIS A  65     3280   3284   3911    139   -235   -414       C  
ATOM    573  C   HIS A  65     -36.297  -7.193 -12.873  1.00 27.74           C  
ANISOU  573  C   HIS A  65     3317   3400   3821     92   -265   -324       C  
ATOM    574  O   HIS A  65     -36.873  -7.480 -11.808  1.00 26.39           O  
ANISOU  574  O   HIS A  65     3040   3236   3750     47   -409   -384       O  
ATOM    575  CB  HIS A  65     -33.814  -7.041 -12.690  1.00 27.68           C  
ANISOU  575  CB  HIS A  65     3138   3284   4095     43   -260   -312       C  
ATOM    576  CG  HIS A  65     -32.558  -6.266 -12.975  1.00 27.20           C  
ANISOU  576  CG  HIS A  65     3177   3280   3877    251   -259   -149       C  
ATOM    577  ND1 HIS A  65     -32.083  -5.287 -12.119  1.00 27.03           N  
ANISOU  577  ND1 HIS A  65     3462   3569   3237    151   -294   -412       N  
ATOM    578  CD2 HIS A  65     -31.689  -6.315 -14.019  1.00 25.05           C  
ANISOU  578  CD2 HIS A  65     3246   3140   3131    303   -492     -7       C  
ATOM    579  CE1 HIS A  65     -30.957  -4.781 -12.613  1.00 27.33           C  
ANISOU  579  CE1 HIS A  65     3873   3515   2995    216    -31   -388       C  
ATOM    580  NE2 HIS A  65     -30.695  -5.383 -13.776  1.00 27.10           N  
ANISOU  580  NE2 HIS A  65     3783   3409   3102    322   -580   -351       N  
ATOM    581  N   GLY A  66     -36.597  -7.755 -14.057  1.00 29.30           N  
ANISOU  581  N   GLY A  66     3588   3470   4075     98   -348   -408       N  
ATOM    582  CA  GLY A  66     -37.515  -8.904 -14.148  1.00 29.68           C  
ANISOU  582  CA  GLY A  66     3578   3521   4179    153   -386   -502       C  
ATOM    583  C   GLY A  66     -38.833  -8.688 -13.453  1.00 29.65           C  
ANISOU  583  C   GLY A  66     3639   3618   4007      5   -402   -495       C  
ATOM    584  O   GLY A  66     -39.519  -7.640 -13.712  1.00 30.62           O  
ANISOU  584  O   GLY A  66     3469   3993   4168    372   -619   -692       O  
ATOM    585  N   ASP A  67     -39.173  -9.580 -12.537  1.00 30.69           N  
ANISOU  585  N   ASP A  67     3648   3767   4243     84   -363   -484       N  
ATOM    586  CA  ASP A  67     -40.448  -9.473 -11.788  1.00 31.53           C  
ANISOU  586  CA  ASP A  67     3825   3862   4289   -159   -210   -389       C  
ATOM    587  C   ASP A  67     -40.400  -8.684 -10.483  1.00 30.48           C  
ANISOU  587  C   ASP A  67     3647   3809   4122   -121   -143   -332       C  
ATOM    588  O   ASP A  67     -41.398  -8.544  -9.790  1.00 31.18           O  
ANISOU  588  O   ASP A  67     3284   4018   4543   -155   -164   -389       O  
ATOM    589  CB  ASP A  67     -41.081 -10.854 -11.569  1.00 31.89           C  
ANISOU  589  CB  ASP A  67     3941   3751   4423   -174   -359   -416       C  
ATOM    590  CG  ASP A  67     -41.500 -11.485 -12.901  1.00 34.51           C  
ANISOU  590  CG  ASP A  67     4289   4046   4775   -282   -632   -479       C  
ATOM    591  OD1 ASP A  67     -41.871 -10.750 -13.864  1.00 33.95           O  
ANISOU  591  OD1 ASP A  67     3900   3781   5218   -374   -807   -450       O  
ATOM    592  OD2 ASP A  67     -41.392 -12.714 -13.008  1.00 38.03           O  
ANISOU  592  OD2 ASP A  67     4242   4031   6177   -718  -1241   -743       O  
ATOM    593  N   SER A  68     -39.240  -8.174 -10.134  1.00 28.55           N  
ANISOU  593  N   SER A  68     3231   3653   3961     69   -298   -251       N  
ATOM    594  CA  SER A  68     -39.076  -7.564  -8.835  1.00 28.23           C  
ANISOU  594  CA  SER A  68     3207   3432   4087    169   -230   -366       C  
ATOM    595  C   SER A  68     -39.440  -6.060  -8.943  1.00 28.51           C  
ANISOU  595  C   SER A  68     3283   3518   4029    120   -230   -250       C  
ATOM    596  O   SER A  68     -39.467  -5.484 -10.036  1.00 28.86           O  
ANISOU  596  O   SER A  68     3387   3285   4291    266   -311   -394       O  
ATOM    597  CB  SER A  68     -37.594  -7.736  -8.370  1.00 27.21           C  
ANISOU  597  CB  SER A  68     2928   3393   4015    242   -332   -120       C  
ATOM    598  OG  SER A  68     -37.419  -9.075  -7.882  1.00 27.12           O  
ANISOU  598  OG  SER A  68     3097   3058   4146     49   -150   -389       O  
ATOM    599  N   ASP A  69     -39.672  -5.472  -7.766  1.00 29.73           N  
ANISOU  599  N   ASP A  69     3458   3549   4286    115   -181   -490       N  
ATOM    600  CA  ASP A  69     -39.967  -4.037  -7.624  1.00 30.99           C  
ANISOU  600  CA  ASP A  69     3773   3695   4303    196   -238   -323       C  
ATOM    601  C   ASP A  69     -38.766  -3.135  -7.834  1.00 31.16           C  
ANISOU  601  C   ASP A  69     3785   3841   4211    168   -233   -284       C  
ATOM    602  O   ASP A  69     -37.606  -3.602  -7.842  1.00 31.47           O  
ANISOU  602  O   ASP A  69     3766   3964   4227    137   -356   -414       O  
ATOM    603  CB  ASP A  69     -40.510  -3.780  -6.208  1.00 30.46           C  
ANISOU  603  CB  ASP A  69     3731   3649   4192    247   -122   -233       C  
ATOM    604  CG  ASP A  69     -41.913  -4.335  -6.007  1.00 33.75           C  
ANISOU  604  CG  ASP A  69     3882   4249   4690    315   -178   -336       C  
ATOM    605  OD1 ASP A  69     -42.538  -4.767  -7.020  1.00 35.40           O  
ANISOU  605  OD1 ASP A  69     3743   4363   5342    -36   -117   -804       O  
ATOM    606  OD2 ASP A  69     -42.386  -4.319  -4.847  1.00 33.89           O  
ANISOU  606  OD2 ASP A  69     3118   4439   5318    203    269   -283       O  
ATOM    607  N   GLY A  70     -39.047  -1.834  -7.951  1.00 30.92           N  
ANISOU  607  N   GLY A  70     3815   3811   4120    130   -345   -263       N  
ATOM    608  CA  GLY A  70     -38.040  -0.815  -8.074  1.00 31.33           C  
ANISOU  608  CA  GLY A  70     3734   4035   4132    101   -472   -163       C  
ATOM    609  C   GLY A  70     -37.756  -0.492  -9.516  1.00 30.80           C  
ANISOU  609  C   GLY A  70     3745   3875   4081    222   -377   -107       C  
ATOM    610  O   GLY A  70     -37.915  -1.341 -10.407  1.00 33.32           O  
ANISOU  610  O   GLY A  70     4032   4162   4465    312   -539    -71       O  
ATOM    611  N   LYS A  71     -37.407   0.752  -9.772  1.00 30.79           N  
ANISOU  611  N   LYS A  71     3632   3944   4121    301   -429   -106       N  
ATOM    612  CA  LYS A  71     -37.032   1.179 -11.094  1.00 29.57           C  
ANISOU  612  CA  LYS A  71     3590   3679   3966    462   -304   -101       C  
ATOM    613  C   LYS A  71     -35.618   0.769 -11.371  1.00 28.59           C  
ANISOU  613  C   LYS A  71     3576   3617   3668    238   -292   -122       C  
ATOM    614  O   LYS A  71     -34.761   0.836 -10.470  1.00 27.91           O  
ANISOU  614  O   LYS A  71     3353   3557   3694    440   -323   -336       O  
ATOM    615  CB  LYS A  71     -37.061   2.711 -11.134  1.00 31.11           C  
ANISOU  615  CB  LYS A  71     3819   3842   4159    427   -391    -51       C  
ATOM    616  CG  LYS A  71     -38.418   3.269 -10.785  1.00 35.41           C  
ANISOU  616  CG  LYS A  71     4486   4186   4781    685   -113   -317       C  
ATOM    617  CD  LYS A  71     -38.352   4.825 -10.885  1.00 41.47           C  
ANISOU  617  CD  LYS A  71     5738   4204   5812   1152    -42    -73       C  
ATOM    618  CE  LYS A  71     -39.083   5.280 -12.096  1.00 48.67           C  
ANISOU  618  CE  LYS A  71     6215   5934   6341    523   -307     49       C  
ATOM    619  NZ  LYS A  71     -40.575   4.949 -12.017  1.00 50.22           N  
ANISOU  619  NZ  LYS A  71     5765   6448   6868    841    466    328       N  
ATOM    620  N   PHE A  72     -35.357   0.397 -12.614  1.00 27.96           N  
ANISOU  620  N   PHE A  72     3590   3617   3414    312   -291   -174       N  
ATOM    621  CA  PHE A  72     -34.024   0.093 -13.061  1.00 27.22           C  
ANISOU  621  CA  PHE A  72     3507   3733   3101     64   -269   -200       C  
ATOM    622  C   PHE A  72     -33.073   1.259 -12.767  1.00 27.98           C  
ANISOU  622  C   PHE A  72     3771   3640   3218    204   -285   -199       C  
ATOM    623  O   PHE A  72     -31.887   1.044 -12.387  1.00 27.57           O  
ANISOU  623  O   PHE A  72     3469   3593   3414    130   -359   -448       O  
ATOM    624  CB  PHE A  72     -34.021  -0.269 -14.575  1.00 27.98           C  
ANISOU  624  CB  PHE A  72     3774   3774   3080    194   -302   -297       C  
ATOM    625  CG  PHE A  72     -32.627  -0.587 -15.101  1.00 27.41           C  
ANISOU  625  CG  PHE A  72     3463   3982   2970     87   -533   -279       C  
ATOM    626  CD1 PHE A  72     -32.055  -1.872 -14.926  1.00 27.75           C  
ANISOU  626  CD1 PHE A  72     3594   3824   3122    276   -263   -427       C  
ATOM    627  CD2 PHE A  72     -31.862   0.412 -15.694  1.00 28.39           C  
ANISOU  627  CD2 PHE A  72     3861   3904   3021    -61   -726   -184       C  
ATOM    628  CE1 PHE A  72     -30.676  -2.136 -15.374  1.00 25.72           C  
ANISOU  628  CE1 PHE A  72     3337   3915   2517   -157    122   -273       C  
ATOM    629  CE2 PHE A  72     -30.495   0.184 -16.125  1.00 29.15           C  
ANISOU  629  CE2 PHE A  72     3854   3804   3418    -65   -577   -285       C  
ATOM    630  CZ  PHE A  72     -29.908  -1.072 -15.961  1.00 26.17           C  
ANISOU  630  CZ  PHE A  72     3368   3566   3008   -206   -641   -589       C  
ATOM    631  N   GLU A  73     -33.553   2.481 -12.946  1.00 26.95           N  
ANISOU  631  N   GLU A  73     3649   3625   2965    263   -269   -101       N  
ATOM    632  CA  GLU A  73     -32.749   3.683 -12.740  1.00 27.69           C  
ANISOU  632  CA  GLU A  73     3863   3456   3201    269   -527      2       C  
ATOM    633  C   GLU A  73     -32.234   3.840 -11.322  1.00 27.03           C  
ANISOU  633  C   GLU A  73     3706   3357   3205    331   -392    -31       C  
ATOM    634  O   GLU A  73     -31.238   4.563 -11.082  1.00 28.16           O  
ANISOU  634  O   GLU A  73     4026   3615   3058     73   -693    -75       O  
ATOM    635  CB  GLU A  73     -33.607   4.926 -13.067  1.00 29.11           C  
ANISOU  635  CB  GLU A  73     4012   3549   3498    207   -481    126       C  
ATOM    636  CG  GLU A  73     -32.727   6.172 -13.208  1.00 32.12           C  
ANISOU  636  CG  GLU A  73     4209   3933   4058     -8   -878    291       C  
ATOM    637  CD  GLU A  73     -33.540   7.442 -13.444  1.00 37.81           C  
ANISOU  637  CD  GLU A  73     4798   4302   5262    256   -885    335       C  
ATOM    638  OE1 GLU A  73     -34.725   7.348 -13.860  1.00 37.08           O  
ANISOU  638  OE1 GLU A  73     4388   4412   5286    -56  -1144    736       O  
ATOM    639  OE2 GLU A  73     -32.979   8.531 -13.180  1.00 40.77           O  
ANISOU  639  OE2 GLU A  73     5604   4631   5254    -67   -678    823       O  
ATOM    640  N   ASN A  74     -32.939   3.210 -10.396  1.00 26.89           N  
ANISOU  640  N   ASN A  74     3906   3170   3141    217   -568    -28       N  
ATOM    641  CA  ASN A  74     -32.580   3.286  -8.947  1.00 26.83           C  
ANISOU  641  CA  ASN A  74     3757   3218   3216    355   -362    -69       C  
ATOM    642  C   ASN A  74     -31.724   2.112  -8.445  1.00 25.28           C  
ANISOU  642  C   ASN A  74     3514   3060   3030    318   -311   -103       C  
ATOM    643  O   ASN A  74     -31.311   2.089  -7.308  1.00 24.46           O  
ANISOU  643  O   ASN A  74     3364   3045   2881    537   -573    -31       O  
ATOM    644  CB  ASN A  74     -33.865   3.467  -8.123  1.00 27.34           C  
ANISOU  644  CB  ASN A  74     3674   3250   3462    313   -303   -144       C  
ATOM    645  CG  ASN A  74     -34.475   4.840  -8.350  1.00 27.03           C  
ANISOU  645  CG  ASN A  74     3348   3038   3881    316    -67   -266       C  
ATOM    646  OD1 ASN A  74     -33.756   5.825  -8.631  1.00 28.68           O  
ANISOU  646  OD1 ASN A  74     3996   3020   3878     29   -201   -253       O  
ATOM    647  ND2 ASN A  74     -35.775   4.919  -8.254  1.00 25.46           N  
ANISOU  647  ND2 ASN A  74     2727   3286   3660    360    -32   -200       N  
ATOM    648  N   MET A  75     -31.486   1.132  -9.295  1.00 24.89           N  
ANISOU  648  N   MET A  75     3446   2954   3055    244   -357   -216       N  
ATOM    649  CA  MET A  75     -30.595   0.010  -8.963  1.00 22.68           C  
ANISOU  649  CA  MET A  75     3074   2834   2707    231   -361   -137       C  
ATOM    650  C   MET A  75     -29.086   0.407  -8.939  1.00 22.30           C  
ANISOU  650  C   MET A  75     2985   2905   2580     36   -416    -13       C  
ATOM    651  O   MET A  75     -28.605   1.181  -9.808  1.00 24.59           O  
ANISOU  651  O   MET A  75     3161   2994   3188   -217   -270   -212       O  
ATOM    652  CB  MET A  75     -30.869  -1.147  -9.993  1.00 21.96           C  
ANISOU  652  CB  MET A  75     2764   2789   2788    405   -607   -328       C  
ATOM    653  CG  MET A  75     -29.944  -2.376  -9.885  1.00 23.84           C  
ANISOU  653  CG  MET A  75     3377   2665   3014    255   -480   -437       C  
ATOM    654  SD  MET A  75     -28.292  -2.182 -10.699  1.00 25.65           S  
ANISOU  654  SD  MET A  75     3572   3230   2943     34   -236   -145       S  
ATOM    655  CE  MET A  75     -28.633  -1.539 -12.334  1.00 22.40           C  
ANISOU  655  CE  MET A  75     3309   2900   2301    271     64   -154       C  
ATOM    656  N   THR A  76     -28.307  -0.164  -7.991  1.00 23.28           N  
ANISOU  656  N   THR A  76     3120   3011   2712     78   -204   -186       N  
ATOM    657  CA  THR A  76     -26.851  -0.011  -8.028  1.00 21.67           C  
ANISOU  657  CA  THR A  76     2964   2762   2506     82   -391    -28       C  
ATOM    658  C   THR A  76     -26.310  -1.371  -7.623  1.00 22.27           C  
ANISOU  658  C   THR A  76     2905   2862   2691     40   -268   -125       C  
ATOM    659  O   THR A  76     -27.056  -2.239  -7.087  1.00 22.71           O  
ANISOU  659  O   THR A  76     2730   2937   2960   -146   -476   -121       O  
ATOM    660  CB  THR A  76     -26.335   1.063  -7.025  1.00 21.69           C  
ANISOU  660  CB  THR A  76     2945   2678   2616     52   -407     25       C  
ATOM    661  OG1 THR A  76     -26.467   0.552  -5.699  1.00 22.55           O  
ANISOU  661  OG1 THR A  76     3185   2831   2548     49   -414    155       O  
ATOM    662  CG2 THR A  76     -27.145   2.388  -7.048  1.00 22.53           C  
ANISOU  662  CG2 THR A  76     3198   2571   2791     15   -470   -364       C  
ATOM    663  N   VAL A  77     -24.996  -1.544  -7.708  1.00 22.37           N  
ANISOU  663  N   VAL A  77     2934   2807   2759     16      7   -123       N  
ATOM    664  CA  VAL A  77     -24.432  -2.811  -7.232  1.00 22.05           C  
ANISOU  664  CA  VAL A  77     2802   2888   2688    142   -105     45       C  
ATOM    665  C   VAL A  77     -24.643  -2.930  -5.721  1.00 22.24           C  
ANISOU  665  C   VAL A  77     2792   2829   2828     22    -65    -64       C  
ATOM    666  O   VAL A  77     -24.838  -4.047  -5.181  1.00 22.87           O  
ANISOU  666  O   VAL A  77     3150   3006   2530    -95     40    166       O  
ATOM    667  CB  VAL A  77     -22.903  -2.933  -7.620  1.00 22.30           C  
ANISOU  667  CB  VAL A  77     2842   2862   2767      7     50     78       C  
ATOM    668  CG1 VAL A  77     -22.232  -4.145  -6.931  1.00 23.40           C  
ANISOU  668  CG1 VAL A  77     3113   3087   2689    221    -50    254       C  
ATOM    669  CG2 VAL A  77     -22.785  -3.099  -9.116  1.00 23.66           C  
ANISOU  669  CG2 VAL A  77     3332   2837   2821     90     97   -173       C  
ATOM    670  N   LEU A  78     -24.583  -1.793  -5.018  1.00 21.88           N  
ANISOU  670  N   LEU A  78     2742   2810   2759    141   -268   -105       N  
ATOM    671  CA  LEU A  78     -24.760  -1.839  -3.528  1.00 22.89           C  
ANISOU  671  CA  LEU A  78     2752   3078   2863    -79     77   -183       C  
ATOM    672  C   LEU A  78     -26.156  -2.297  -3.104  1.00 23.01           C  
ANISOU  672  C   LEU A  78     2794   3022   2925     11    -59    -96       C  
ATOM    673  O   LEU A  78     -26.287  -3.160  -2.226  1.00 24.01           O  
ANISOU  673  O   LEU A  78     2378   3406   3338    -87     94     -7       O  
ATOM    674  CB  LEU A  78     -24.455  -0.484  -2.916  1.00 24.49           C  
ANISOU  674  CB  LEU A  78     2902   3191   3211    -52   -353   -266       C  
ATOM    675  CG  LEU A  78     -22.950  -0.131  -2.830  1.00 31.00           C  
ANISOU  675  CG  LEU A  78     3774   4089   3915    -54    175   -247       C  
ATOM    676  CD1 LEU A  78     -22.710   1.156  -2.061  1.00 40.25           C  
ANISOU  676  CD1 LEU A  78     5551   4721   5019   -292   -498   -603       C  
ATOM    677  CD2 LEU A  78     -21.918  -1.310  -2.359  1.00 37.15           C  
ANISOU  677  CD2 LEU A  78     4231   4637   5244    277   -152   -349       C  
ATOM    678  N   ASN A  79     -27.206  -1.759  -3.712  1.00 23.09           N  
ANISOU  678  N   ASN A  79     2960   2943   2867     65     63   -185       N  
ATOM    679  CA  ASN A  79     -28.494  -2.231  -3.314  1.00 23.15           C  
ANISOU  679  CA  ASN A  79     2912   2920   2962    139     26   -215       C  
ATOM    680  C   ASN A  79     -28.868  -3.635  -3.809  1.00 23.32           C  
ANISOU  680  C   ASN A  79     3055   2840   2964    150     52   -183       C  
ATOM    681  O   ASN A  79     -29.678  -4.289  -3.196  1.00 21.86           O  
ANISOU  681  O   ASN A  79     2861   2731   2712     -7     -8   -365       O  
ATOM    682  CB  ASN A  79     -29.600  -1.154  -3.460  1.00 23.53           C  
ANISOU  682  CB  ASN A  79     3128   2753   3056    376     43    -15       C  
ATOM    683  CG  ASN A  79     -29.795  -0.676  -4.864  1.00 26.24           C  
ANISOU  683  CG  ASN A  79     3596   3234   3138    274    132   -170       C  
ATOM    684  OD1 ASN A  79     -29.709  -1.473  -5.830  1.00 22.88           O  
ANISOU  684  OD1 ASN A  79     2875   2983   2836     82   -232   -142       O  
ATOM    685  ND2 ASN A  79     -30.126   0.646  -5.008  1.00 27.83           N  
ANISOU  685  ND2 ASN A  79     3819   3153   3602     87   -118     86       N  
ATOM    686  N   GLU A  80     -28.220  -4.098  -4.885  1.00 23.44           N  
ANISOU  686  N   GLU A  80     3150   2884   2870    126    -97   -144       N  
ATOM    687  CA  GLU A  80     -28.222  -5.555  -5.252  1.00 22.52           C  
ANISOU  687  CA  GLU A  80     3030   2789   2737     66   -177   -158       C  
ATOM    688  C   GLU A  80     -27.530  -6.420  -4.207  1.00 23.12           C  
ANISOU  688  C   GLU A  80     3006   2906   2871     51   -108    -88       C  
ATOM    689  O   GLU A  80     -28.044  -7.514  -3.872  1.00 22.64           O  
ANISOU  689  O   GLU A  80     3174   2685   2740    117   -163   -130       O  
ATOM    690  CB  GLU A  80     -27.625  -5.781  -6.616  1.00 22.17           C  
ANISOU  690  CB  GLU A  80     2982   2814   2626     76   -292    -81       C  
ATOM    691  CG  GLU A  80     -28.548  -5.238  -7.697  1.00 22.80           C  
ANISOU  691  CG  GLU A  80     2959   2830   2871   -115   -391   -270       C  
ATOM    692  CD  GLU A  80     -28.188  -5.790  -9.067  1.00 24.13           C  
ANISOU  692  CD  GLU A  80     3129   3139   2898    213   -242   -173       C  
ATOM    693  OE1 GLU A  80     -27.110  -6.406  -9.236  1.00 23.87           O  
ANISOU  693  OE1 GLU A  80     2725   3347   2996     48     -8   -514       O  
ATOM    694  OE2 GLU A  80     -28.990  -5.568  -9.992  1.00 25.10           O  
ANISOU  694  OE2 GLU A  80     3358   2987   3192    313   -269   -215       O  
ATOM    695  N   ILE A  81     -26.468  -5.905  -3.576  1.00 22.79           N  
ANISOU  695  N   ILE A  81     2928   3026   2703    152     -7   -111       N  
ATOM    696  CA  ILE A  81     -25.856  -6.648  -2.437  1.00 22.56           C  
ANISOU  696  CA  ILE A  81     2785   3078   2706    198    -83   -156       C  
ATOM    697  C   ILE A  81     -26.832  -6.668  -1.246  1.00 22.41           C  
ANISOU  697  C   ILE A  81     2791   2890   2833    106    -45    -51       C  
ATOM    698  O   ILE A  81     -26.984  -7.685  -0.563  1.00 21.80           O  
ANISOU  698  O   ILE A  81     2806   2662   2813    248    319   -214       O  
ATOM    699  CB  ILE A  81     -24.465  -6.004  -2.005  1.00 23.22           C  
ANISOU  699  CB  ILE A  81     2699   3302   2819    127    -35     13       C  
ATOM    700  CG1 ILE A  81     -23.420  -6.251  -3.129  1.00 24.16           C  
ANISOU  700  CG1 ILE A  81     2820   3846   2514     60     -9    -74       C  
ATOM    701  CG2 ILE A  81     -23.984  -6.617  -0.602  1.00 21.58           C  
ANISOU  701  CG2 ILE A  81     2529   3164   2503    432   -249   -140       C  
ATOM    702  CD1 ILE A  81     -22.064  -5.493  -2.964  1.00 25.69           C  
ANISOU  702  CD1 ILE A  81     3104   3609   3047   -208     42    -32       C  
ATOM    703  N   GLU A  82     -27.539  -5.546  -1.029  1.00 21.67           N  
ANISOU  703  N   GLU A  82     2799   2728   2706    132    -88   -294       N  
ATOM    704  CA  GLU A  82     -28.611  -5.521  -0.013  1.00 23.40           C  
ANISOU  704  CA  GLU A  82     2852   2870   3169     60    -19    -95       C  
ATOM    705  C   GLU A  82     -29.762  -6.548  -0.323  1.00 23.54           C  
ANISOU  705  C   GLU A  82     2969   2852   3121     85     45   -140       C  
ATOM    706  O   GLU A  82     -30.205  -7.278   0.574  1.00 23.68           O  
ANISOU  706  O   GLU A  82     2789   2966   3241    106    217    -56       O  
ATOM    707  CB  GLU A  82     -29.153  -4.114   0.161  1.00 23.28           C  
ANISOU  707  CB  GLU A  82     2859   2848   3138    -29     59   -404       C  
ATOM    708  CG  GLU A  82     -28.045  -3.191   0.638  1.00 23.80           C  
ANISOU  708  CG  GLU A  82     3257   2657   3129    154    -23   -487       C  
ATOM    709  CD  GLU A  82     -28.461  -1.740   0.727  1.00 29.56           C  
ANISOU  709  CD  GLU A  82     4160   3278   3793     29   -203   -572       C  
ATOM    710  OE1 GLU A  82     -29.377  -1.319  -0.044  1.00 30.77           O  
ANISOU  710  OE1 GLU A  82     4188   3242   4259   -121   -208   -510       O  
ATOM    711  OE2 GLU A  82     -27.835  -1.049   1.594  1.00 31.07           O  
ANISOU  711  OE2 GLU A  82     4299   3525   3982     39   -452   -998       O  
ATOM    712  N   ASP A  83     -30.221  -6.599  -1.582  1.00 24.48           N  
ANISOU  712  N   ASP A  83     3064   3166   3067    108    126    -50       N  
ATOM    713  CA  ASP A  83     -31.145  -7.694  -2.042  1.00 23.93           C  
ANISOU  713  CA  ASP A  83     2987   3040   3066     34    131   -105       C  
ATOM    714  C   ASP A  83     -30.589  -9.070  -1.699  1.00 24.41           C  
ANISOU  714  C   ASP A  83     2936   3144   3195     21    230    -14       C  
ATOM    715  O   ASP A  83     -31.317  -9.929  -1.188  1.00 25.07           O  
ANISOU  715  O   ASP A  83     3050   3317   3157     58    391    -27       O  
ATOM    716  CB  ASP A  83     -31.386  -7.716  -3.562  1.00 23.74           C  
ANISOU  716  CB  ASP A  83     3133   2942   2945    148    132    -46       C  
ATOM    717  CG  ASP A  83     -32.055  -6.448  -4.094  1.00 23.64           C  
ANISOU  717  CG  ASP A  83     2764   3218   2998      3    -33     10       C  
ATOM    718  OD1 ASP A  83     -32.758  -5.686  -3.321  1.00 25.61           O  
ANISOU  718  OD1 ASP A  83     3110   3206   3413   -390   -207   -360       O  
ATOM    719  OD2 ASP A  83     -31.865  -6.246  -5.310  1.00 26.23           O  
ANISOU  719  OD2 ASP A  83     3550   3254   3160    -16    -76   -461       O  
ATOM    720  N   ALA A  84     -29.303  -9.296  -2.060  1.00 24.27           N  
ANISOU  720  N   ALA A  84     2800   3160   3260      5    243    -13       N  
ATOM    721  CA  ALA A  84     -28.648 -10.593  -1.910  1.00 23.10           C  
ANISOU  721  CA  ALA A  84     2636   3070   3070    -65    202   -113       C  
ATOM    722  C   ALA A  84     -28.593 -10.941  -0.432  1.00 24.75           C  
ANISOU  722  C   ALA A  84     2956   3218   3227   -140    155    -98       C  
ATOM    723  O   ALA A  84     -28.772 -12.114  -0.041  1.00 24.74           O  
ANISOU  723  O   ALA A  84     3105   3136   3157   -145      5   -232       O  
ATOM    724  CB  ALA A  84     -27.200 -10.552  -2.535  1.00 22.79           C  
ANISOU  724  CB  ALA A  84     2346   3053   3259     -1    242    -66       C  
ATOM    725  N   ASN A  85     -28.329  -9.933   0.417  1.00 23.91           N  
ANISOU  725  N   ASN A  85     2913   3335   2836    -60    289   -152       N  
ATOM    726  CA  ASN A  85     -28.372 -10.225   1.864  1.00 24.09           C  
ANISOU  726  CA  ASN A  85     2876   3310   2966    -29    116   -127       C  
ATOM    727  C   ASN A  85     -29.804 -10.640   2.331  1.00 24.87           C  
ANISOU  727  C   ASN A  85     3168   3188   3091   -127    110   -111       C  
ATOM    728  O   ASN A  85     -29.893 -11.494   3.200  1.00 25.01           O  
ANISOU  728  O   ASN A  85     3013   3184   3304   -226    167    -70       O  
ATOM    729  CB  ASN A  85     -27.868  -9.023   2.649  1.00 23.53           C  
ANISOU  729  CB  ASN A  85     3052   3153   2735     18     69    -16       C  
ATOM    730  CG  ASN A  85     -27.924  -9.272   4.145  1.00 24.46           C  
ANISOU  730  CG  ASN A  85     3122   3410   2761     50    191    -84       C  
ATOM    731  OD1 ASN A  85     -27.157 -10.117   4.652  1.00 27.19           O  
ANISOU  731  OD1 ASN A  85     3839   3393   3097    -74    421    472       O  
ATOM    732  ND2 ASN A  85     -28.858  -8.599   4.845  1.00 24.23           N  
ANISOU  732  ND2 ASN A  85     2930   2987   3285   -410    463   -252       N  
ATOM    733  N   ALA A  86     -30.883  -9.983   1.833  1.00 24.37           N  
ANISOU  733  N   ALA A  86     3109   3039   3111    -80     51   -174       N  
ATOM    734  CA  ALA A  86     -32.272 -10.371   2.181  1.00 24.79           C  
ANISOU  734  CA  ALA A  86     3094   3184   3141    125    126   -146       C  
ATOM    735  C   ALA A  86     -32.552 -11.808   1.753  1.00 26.23           C  
ANISOU  735  C   ALA A  86     3225   3380   3359     86    232     52       C  
ATOM    736  O   ALA A  86     -33.209 -12.564   2.439  1.00 26.85           O  
ANISOU  736  O   ALA A  86     3218   3396   3586    -49    379    239       O  
ATOM    737  CB  ALA A  86     -33.299  -9.376   1.545  1.00 25.22           C  
ANISOU  737  CB  ALA A  86     3092   3134   3353      5    270    -46       C  
ATOM    738  N   ILE A  87     -32.018 -12.204   0.589  1.00 25.97           N  
ANISOU  738  N   ILE A  87     3362   3261   3243    -20    313   -225       N  
ATOM    739  CA  ILE A  87     -32.168 -13.604   0.112  1.00 25.66           C  
ANISOU  739  CA  ILE A  87     3305   3134   3308   -105    216   -100       C  
ATOM    740  C   ILE A  87     -31.419 -14.583   1.017  1.00 25.93           C  
ANISOU  740  C   ILE A  87     3138   3316   3397    -46    304   -192       C  
ATOM    741  O   ILE A  87     -31.947 -15.671   1.361  1.00 26.86           O  
ANISOU  741  O   ILE A  87     2999   3236   3970    118    276   -127       O  
ATOM    742  CB  ILE A  87     -31.701 -13.709  -1.336  1.00 24.02           C  
ANISOU  742  CB  ILE A  87     3099   2948   3080   -321     40   -266       C  
ATOM    743  CG1 ILE A  87     -32.637 -12.803  -2.219  1.00 25.40           C  
ANISOU  743  CG1 ILE A  87     3396   3012   3243    -82    -12     21       C  
ATOM    744  CG2 ILE A  87     -31.770 -15.126  -1.839  1.00 26.07           C  
ANISOU  744  CG2 ILE A  87     3757   2931   3216    125    487    -73       C  
ATOM    745  CD1 ILE A  87     -32.074 -12.373  -3.598  1.00 24.29           C  
ANISOU  745  CD1 ILE A  87     3196   3079   2954   -393     85    -41       C  
ATOM    746  N   LEU A  88     -30.200 -14.211   1.418  1.00 25.21           N  
ANISOU  746  N   LEU A  88     3155   3310   3112   -131    120   -167       N  
ATOM    747  CA  LEU A  88     -29.420 -15.062   2.273  1.00 25.04           C  
ANISOU  747  CA  LEU A  88     3067   3326   3117    -21    178   -119       C  
ATOM    748  C   LEU A  88     -30.086 -15.217   3.652  1.00 25.08           C  
ANISOU  748  C   LEU A  88     3029   3224   3276   -200    359      9       C  
ATOM    749  O   LEU A  88     -29.973 -16.283   4.227  1.00 26.45           O  
ANISOU  749  O   LEU A  88     3285   3369   3394   -169    309    -97       O  
ATOM    750  CB  LEU A  88     -28.032 -14.449   2.507  1.00 24.73           C  
ANISOU  750  CB  LEU A  88     3048   3177   3169   -216    118     13       C  
ATOM    751  CG  LEU A  88     -26.974 -15.250   3.337  1.00 23.85           C  
ANISOU  751  CG  LEU A  88     3007   3010   3043    135    -72   -344       C  
ATOM    752  CD1 LEU A  88     -26.870 -16.703   2.834  1.00 28.08           C  
ANISOU  752  CD1 LEU A  88     3706   2897   4064   -194    220   -130       C  
ATOM    753  CD2 LEU A  88     -25.596 -14.507   3.344  1.00 28.52           C  
ANISOU  753  CD2 LEU A  88     3474   3792   3571   -425     54    233       C  
ATOM    754  N   ASN A  89     -30.715 -14.143   4.182  1.00 26.98           N  
ANISOU  754  N   ASN A  89     3248   3456   3546   -289    281   -129       N  
ATOM    755  CA  ASN A  89     -31.574 -14.256   5.379  1.00 27.46           C  
ANISOU  755  CA  ASN A  89     3498   3346   3589   -323    371    -90       C  
ATOM    756  C   ASN A  89     -32.619 -15.392   5.249  1.00 29.35           C  
ANISOU  756  C   ASN A  89     3796   3524   3833   -293    277    -92       C  
ATOM    757  O   ASN A  89     -32.812 -16.221   6.172  1.00 29.94           O  
ANISOU  757  O   ASN A  89     3979   3545   3850   -425    476      4       O  
ATOM    758  CB  ASN A  89     -32.323 -12.941   5.653  1.00 28.70           C  
ANISOU  758  CB  ASN A  89     3542   3570   3789   -207    210   -152       C  
ATOM    759  CG  ASN A  89     -31.430 -11.891   6.276  1.00 30.23           C  
ANISOU  759  CG  ASN A  89     3849   3663   3971    -79    336   -290       C  
ATOM    760  OD1 ASN A  89     -30.390 -12.211   6.796  1.00 32.17           O  
ANISOU  760  OD1 ASN A  89     3880   4427   3914   -401    154   -189       O  
ATOM    761  ND2 ASN A  89     -31.853 -10.635   6.248  1.00 33.27           N  
ANISOU  761  ND2 ASN A  89     4404   3529   4708   -326    224    176       N  
ATOM    762  N   TYR A  90     -33.276 -15.408   4.113  1.00 29.35           N  
ANISOU  762  N   TYR A  90     3803   3574   3775   -304    301    -40       N  
ATOM    763  CA  TYR A  90     -34.284 -16.433   3.804  1.00 30.73           C  
ANISOU  763  CA  TYR A  90     3952   3827   3894   -315    406    -39       C  
ATOM    764  C   TYR A  90     -33.671 -17.833   3.766  1.00 30.73           C  
ANISOU  764  C   TYR A  90     3944   3857   3874   -230    545     16       C  
ATOM    765  O   TYR A  90     -34.219 -18.778   4.351  1.00 32.12           O  
ANISOU  765  O   TYR A  90     4145   4015   4041   -381    865    191       O  
ATOM    766  CB  TYR A  90     -35.027 -16.088   2.499  1.00 30.70           C  
ANISOU  766  CB  TYR A  90     3776   3865   4022   -241    295   -146       C  
ATOM    767  CG  TYR A  90     -35.806 -17.244   1.903  1.00 34.09           C  
ANISOU  767  CG  TYR A  90     4227   4309   4413   -320    334   -352       C  
ATOM    768  CD1 TYR A  90     -37.085 -17.563   2.374  1.00 36.20           C  
ANISOU  768  CD1 TYR A  90     4353   4678   4721   -505    385   -296       C  
ATOM    769  CD2 TYR A  90     -35.254 -18.030   0.847  1.00 34.42           C  
ANISOU  769  CD2 TYR A  90     4207   4634   4237   -264    385   -331       C  
ATOM    770  CE1 TYR A  90     -37.798 -18.656   1.824  1.00 35.47           C  
ANISOU  770  CE1 TYR A  90     4410   4666   4401   -574    115   -236       C  
ATOM    771  CE2 TYR A  90     -35.951 -19.100   0.282  1.00 34.15           C  
ANISOU  771  CE2 TYR A  90     4157   4691   4127   -154      0   -545       C  
ATOM    772  CZ  TYR A  90     -37.224 -19.406   0.779  1.00 36.40           C  
ANISOU  772  CZ  TYR A  90     4495   4648   4686   -388    132   -361       C  
ATOM    773  OH  TYR A  90     -37.933 -20.434   0.214  1.00 37.68           O  
ANISOU  773  OH  TYR A  90     4713   4232   5370   -158    291   -410       O  
ATOM    774  N   VAL A  91     -32.537 -17.988   3.073  1.00 30.14           N  
ANISOU  774  N   VAL A  91     3759   3849   3843   -144    412     12       N  
ATOM    775  CA  VAL A  91     -31.901 -19.281   2.934  1.00 29.51           C  
ANISOU  775  CA  VAL A  91     3794   3649   3767    -84    453   -100       C  
ATOM    776  C   VAL A  91     -31.312 -19.780   4.283  1.00 30.27           C  
ANISOU  776  C   VAL A  91     3838   3773   3891    -79    400    -59       C  
ATOM    777  O   VAL A  91     -31.464 -20.965   4.669  1.00 32.35           O  
ANISOU  777  O   VAL A  91     4135   4075   4080   -236    458    -76       O  
ATOM    778  CB  VAL A  91     -30.763 -19.211   1.817  1.00 28.85           C  
ANISOU  778  CB  VAL A  91     3610   3678   3673    -71    331    -79       C  
ATOM    779  CG1 VAL A  91     -29.956 -20.482   1.837  1.00 28.42           C  
ANISOU  779  CG1 VAL A  91     3533   3373   3891   -184    427   -462       C  
ATOM    780  CG2 VAL A  91     -31.411 -18.907   0.391  1.00 29.49           C  
ANISOU  780  CG2 VAL A  91     3877   3306   4020    104    106    161       C  
ATOM    781  N   LYS A  92     -30.640 -18.908   5.021  1.00 29.08           N  
ANISOU  781  N   LYS A  92     3722   3631   3695   -145    385   -114       N  
ATOM    782  CA  LYS A  92     -29.892 -19.393   6.202  1.00 30.05           C  
ANISOU  782  CA  LYS A  92     3849   3752   3814   -148    393     13       C  
ATOM    783  C   LYS A  92     -30.818 -19.772   7.343  1.00 31.55           C  
ANISOU  783  C   LYS A  92     4161   3871   3953   -179    308     52       C  
ATOM    784  O   LYS A  92     -30.381 -20.446   8.269  1.00 32.79           O  
ANISOU  784  O   LYS A  92     4285   4091   4081    -77    396    241       O  
ATOM    785  CB  LYS A  92     -28.816 -18.390   6.680  1.00 29.29           C  
ANISOU  785  CB  LYS A  92     4050   3606   3469   -215    261     13       C  
ATOM    786  CG  LYS A  92     -29.402 -17.173   7.415  1.00 29.87           C  
ANISOU  786  CG  LYS A  92     3870   3625   3852   -300    409    -14       C  
ATOM    787  CD  LYS A  92     -28.320 -16.075   7.516  1.00 29.80           C  
ANISOU  787  CD  LYS A  92     4223   3451   3648   -760    402    -61       C  
ATOM    788  CE  LYS A  92     -28.867 -14.877   8.345  1.00 31.99           C  
ANISOU  788  CE  LYS A  92     4578   3955   3620   -537    371    -46       C  
ATOM    789  NZ  LYS A  92     -27.854 -13.800   8.329  1.00 34.67           N  
ANISOU  789  NZ  LYS A  92     5018   4178   3974   -743    231     -4       N  
ATOM    790  N   THR A  93     -32.085 -19.333   7.269  1.00 31.12           N  
ANISOU  790  N   THR A  93     4074   3751   3997   -154    470    -43       N  
ATOM    791  CA  THR A  93     -33.096 -19.729   8.272  1.00 34.13           C  
ANISOU  791  CA  THR A  93     4336   4114   4518   -247    494   -135       C  
ATOM    792  C   THR A  93     -33.987 -20.913   7.837  1.00 34.22           C  
ANISOU  792  C   THR A  93     4346   4130   4525   -284    505    -74       C  
ATOM    793  O   THR A  93     -34.887 -21.272   8.570  1.00 36.72           O  
ANISOU  793  O   THR A  93     4600   4511   4841   -289    808    -30       O  
ATOM    794  CB  THR A  93     -34.016 -18.546   8.701  1.00 33.57           C  
ANISOU  794  CB  THR A  93     4244   4007   4502   -203    410    -55       C  
ATOM    795  OG1 THR A  93     -34.707 -18.006   7.553  1.00 35.19           O  
ANISOU  795  OG1 THR A  93     4325   4958   4085    -52    409    109       O  
ATOM    796  CG2 THR A  93     -33.208 -17.446   9.389  1.00 38.20           C  
ANISOU  796  CG2 THR A  93     4939   4415   5159   -278    325   -515       C  
ATOM    797  N   ASP A  94     -33.782 -21.472   6.644  1.00 33.48           N  
ANISOU  797  N   ASP A  94     4232   3917   4569   -242    391   -178       N  
ATOM    798  CA  ASP A  94     -34.533 -22.674   6.221  1.00 32.96           C  
ANISOU  798  CA  ASP A  94     4011   4210   4301   -198    197   -149       C  
ATOM    799  C   ASP A  94     -33.889 -23.904   6.934  1.00 32.92           C  
ANISOU  799  C   ASP A  94     4085   4058   4365   -192    226    -56       C  
ATOM    800  O   ASP A  94     -32.658 -24.178   6.773  1.00 30.58           O  
ANISOU  800  O   ASP A  94     3699   3799   4120   -543     76   -110       O  
ATOM    801  CB  ASP A  94     -34.497 -22.789   4.693  1.00 33.60           C  
ANISOU  801  CB  ASP A  94     4069   4417   4281   -173    215   -235       C  
ATOM    802  CG  ASP A  94     -35.334 -23.931   4.181  1.00 33.81           C  
ANISOU  802  CG  ASP A  94     4273   4196   4376    -25      8   -369       C  
ATOM    803  OD1 ASP A  94     -36.119 -23.700   3.249  1.00 37.50           O  
ANISOU  803  OD1 ASP A  94     5123   4409   4714    193   -131   -376       O  
ATOM    804  OD2 ASP A  94     -35.262 -25.037   4.726  1.00 39.90           O  
ANISOU  804  OD2 ASP A  94     4802   4974   5382     93   -471     47       O  
ATOM    805  N   PRO A  95     -34.682 -24.626   7.756  1.00 33.61           N  
ANISOU  805  N   PRO A  95     3983   4351   4433   -118    242     60       N  
ATOM    806  CA  PRO A  95     -34.043 -25.734   8.495  1.00 33.86           C  
ANISOU  806  CA  PRO A  95     4165   4370   4328   -229    302    219       C  
ATOM    807  C   PRO A  95     -33.658 -26.914   7.603  1.00 32.62           C  
ANISOU  807  C   PRO A  95     3918   4221   4255   -235    375    251       C  
ATOM    808  O   PRO A  95     -32.936 -27.771   8.051  1.00 35.18           O  
ANISOU  808  O   PRO A  95     4577   4567   4220   -279    410    291       O  
ATOM    809  CB  PRO A  95     -35.084 -26.120   9.589  1.00 35.57           C  
ANISOU  809  CB  PRO A  95     4109   4771   4632   -120    287    231       C  
ATOM    810  CG  PRO A  95     -36.438 -25.692   9.013  1.00 36.76           C  
ANISOU  810  CG  PRO A  95     4418   4898   4649    -49    150    467       C  
ATOM    811  CD  PRO A  95     -36.110 -24.431   8.125  1.00 35.94           C  
ANISOU  811  CD  PRO A  95     4197   4600   4857   -206    343    203       C  
ATOM    812  N   HIS A  96     -34.102 -26.979   6.352  1.00 31.91           N  
ANISOU  812  N   HIS A  96     3798   3986   4338   -432    416    162       N  
ATOM    813  CA  HIS A  96     -33.625 -28.056   5.472  1.00 31.70           C  
ANISOU  813  CA  HIS A  96     3815   3931   4295   -466    309     63       C  
ATOM    814  C   HIS A  96     -32.235 -27.811   4.883  1.00 32.00           C  
ANISOU  814  C   HIS A  96     3943   3839   4377   -448    370      5       C  
ATOM    815  O   HIS A  96     -31.583 -28.744   4.415  1.00 30.98           O  
ANISOU  815  O   HIS A  96     3612   3842   4315   -652    500    -11       O  
ATOM    816  CB  HIS A  96     -34.597 -28.330   4.333  1.00 33.74           C  
ANISOU  816  CB  HIS A  96     4178   4122   4517   -490    296    -34       C  
ATOM    817  CG  HIS A  96     -36.018 -28.612   4.755  1.00 34.93           C  
ANISOU  817  CG  HIS A  96     4112   4536   4623   -666    256     31       C  
ATOM    818  ND1 HIS A  96     -36.480 -29.889   5.008  1.00 35.25           N  
ANISOU  818  ND1 HIS A  96     4519   4436   4439   -724     80    198       N  
ATOM    819  CD2 HIS A  96     -37.091 -27.790   4.879  1.00 36.69           C  
ANISOU  819  CD2 HIS A  96     4291   4771   4876   -498    381    286       C  
ATOM    820  CE1 HIS A  96     -37.778 -29.832   5.301  1.00 36.81           C  
ANISOU  820  CE1 HIS A  96     4369   4441   5173   -638   -114   -160       C  
ATOM    821  NE2 HIS A  96     -38.179 -28.575   5.205  1.00 34.96           N  
ANISOU  821  NE2 HIS A  96     4135   4424   4725   -768   -262     69       N  
ATOM    822  N   VAL A  97     -31.769 -26.553   4.921  1.00 31.53           N  
ANISOU  822  N   VAL A  97     3774   3922   4284   -628    439    129       N  
ATOM    823  CA  VAL A  97     -30.529 -26.135   4.213  1.00 30.78           C  
ANISOU  823  CA  VAL A  97     3675   3875   4143   -434    372    142       C  
ATOM    824  C   VAL A  97     -29.295 -26.493   5.057  1.00 29.88           C  
ANISOU  824  C   VAL A  97     3769   3689   3892   -557    292    137       C  
ATOM    825  O   VAL A  97     -29.176 -26.077   6.212  1.00 31.93           O  
ANISOU  825  O   VAL A  97     3976   4249   3906   -525    144     85       O  
ATOM    826  CB  VAL A  97     -30.636 -24.612   3.783  1.00 29.85           C  
ANISOU  826  CB  VAL A  97     3464   3680   4196   -551    334    275       C  
ATOM    827  CG1 VAL A  97     -29.320 -24.032   3.252  1.00 32.56           C  
ANISOU  827  CG1 VAL A  97     3676   4279   4414   -548    319    238       C  
ATOM    828  CG2 VAL A  97     -31.778 -24.416   2.720  1.00 30.51           C  
ANISOU  828  CG2 VAL A  97     3689   3830   4074   -501    519    274       C  
ATOM    829  N   ARG A  98     -28.395 -27.275   4.475  1.00 29.50           N  
ANISOU  829  N   ARG A  98     3851   3462   3894   -563    160    193       N  
ATOM    830  CA  ARG A  98     -27.156 -27.667   5.076  1.00 30.63           C  
ANISOU  830  CA  ARG A  98     3695   3766   4177   -547    172     97       C  
ATOM    831  C   ARG A  98     -26.062 -26.636   4.712  1.00 30.84           C  
ANISOU  831  C   ARG A  98     3917   3655   4145   -438    231    132       C  
ATOM    832  O   ARG A  98     -25.818 -25.689   5.475  1.00 33.58           O  
ANISOU  832  O   ARG A  98     4296   4195   4265   -396    195   -100       O  
ATOM    833  CB  ARG A  98     -26.760 -29.085   4.682  1.00 29.16           C  
ANISOU  833  CB  ARG A  98     3470   3510   4097   -624    220    209       C  
ATOM    834  CG  ARG A  98     -25.490 -29.549   5.289  1.00 34.94           C  
ANISOU  834  CG  ARG A  98     4292   4341   4640   -477    181    333       C  
ATOM    835  CD  ARG A  98     -24.750 -30.381   4.279  1.00 42.34           C  
ANISOU  835  CD  ARG A  98     5021   5542   5524      0    442    331       C  
ATOM    836  NE  ARG A  98     -25.317 -31.679   4.260  1.00 45.71           N  
ANISOU  836  NE  ARG A  98     5931   4966   6467    102    233    475       N  
ATOM    837  CZ  ARG A  98     -25.775 -32.397   3.223  1.00 48.35           C  
ANISOU  837  CZ  ARG A  98     6438   5891   6041    213    266    682       C  
ATOM    838  NH1 ARG A  98     -25.697 -32.009   1.980  1.00 47.18           N  
ANISOU  838  NH1 ARG A  98     6157   5323   6443    443    403   1556       N  
ATOM    839  NH2 ARG A  98     -26.283 -33.611   3.473  1.00 47.74           N  
ANISOU  839  NH2 ARG A  98     6146   5424   6568    203    323    621       N  
ATOM    840  N   ASN A  99     -25.423 -26.788   3.564  1.00 30.12           N  
ANISOU  840  N   ASN A  99     3673   3672   4098   -399    221    161       N  
ATOM    841  CA  ASN A  99     -24.388 -25.793   3.175  1.00 29.53           C  
ANISOU  841  CA  ASN A  99     3675   3500   4044   -187    291    140       C  
ATOM    842  C   ASN A  99     -24.956 -24.826   2.192  1.00 27.41           C  
ANISOU  842  C   ASN A  99     3428   3331   3655   -171    287     40       C  
ATOM    843  O   ASN A  99     -25.810 -25.186   1.383  1.00 27.09           O  
ANISOU  843  O   ASN A  99     3380   3145   3768   -195    325     29       O  
ATOM    844  CB  ASN A  99     -23.210 -26.518   2.536  1.00 31.46           C  
ANISOU  844  CB  ASN A  99     3602   3969   4383   -163    245     51       C  
ATOM    845  CG  ASN A  99     -22.476 -27.451   3.511  1.00 31.25           C  
ANISOU  845  CG  ASN A  99     4021   3620   4231   -157    269    272       C  
ATOM    846  OD1 ASN A  99     -22.080 -27.041   4.609  1.00 34.23           O  
ANISOU  846  OD1 ASN A  99     4388   4510   4108     68    199    816       O  
ATOM    847  ND2 ASN A  99     -22.179 -28.678   3.049  1.00 37.83           N  
ANISOU  847  ND2 ASN A  99     4071   4185   6116    539     -1    122       N  
ATOM    848  N   ILE A 100     -24.470 -23.591   2.232  1.00 26.22           N  
ANISOU  848  N   ILE A 100     3379   3145   3437     19    375    -59       N  
ATOM    849  CA  ILE A 100     -24.957 -22.569   1.308  1.00 25.15           C  
ANISOU  849  CA  ILE A 100     3240   3096   3217    -49    329    -27       C  
ATOM    850  C   ILE A 100     -23.844 -22.176   0.335  1.00 25.07           C  
ANISOU  850  C   ILE A 100     3129   3229   3164    -95    166     12       C  
ATOM    851  O   ILE A 100     -22.736 -21.923   0.767  1.00 25.94           O  
ANISOU  851  O   ILE A 100     3202   3216   3437   -306     50    -52       O  
ATOM    852  CB  ILE A 100     -25.378 -21.263   2.096  1.00 26.42           C  
ANISOU  852  CB  ILE A 100     3618   3190   3227      5    473   -123       C  
ATOM    853  CG1 ILE A 100     -26.398 -21.626   3.198  1.00 27.08           C  
ANISOU  853  CG1 ILE A 100     3323   3714   3252   -152    632   -337       C  
ATOM    854  CG2 ILE A 100     -25.937 -20.163   1.096  1.00 24.54           C  
ANISOU  854  CG2 ILE A 100     3486   2779   3059   -141    396     46       C  
ATOM    855  CD1 ILE A 100     -26.740 -20.451   4.066  1.00 31.33           C  
ANISOU  855  CD1 ILE A 100     4436   3676   3789    190    676   -301       C  
ATOM    856  N   TYR A 101     -24.174 -22.105  -0.956  1.00 24.67           N  
ANISOU  856  N   TYR A 101     3006   3231   3136   -164    117      0       N  
ATOM    857  CA  TYR A 101     -23.248 -21.812  -2.043  1.00 23.98           C  
ANISOU  857  CA  TYR A 101     2972   3013   3126   -123     39     10       C  
ATOM    858  C   TYR A 101     -23.743 -20.561  -2.725  1.00 24.24           C  
ANISOU  858  C   TYR A 101     3015   3001   3194    -88      5   -101       C  
ATOM    859  O   TYR A 101     -24.986 -20.336  -2.792  1.00 24.49           O  
ANISOU  859  O   TYR A 101     3030   3115   3158   -132    -99   -300       O  
ATOM    860  CB  TYR A 101     -23.281 -22.946  -3.085  1.00 24.16           C  
ANISOU  860  CB  TYR A 101     3056   2970   3152    -46     67     26       C  
ATOM    861  CG  TYR A 101     -23.012 -24.301  -2.504  1.00 24.57           C  
ANISOU  861  CG  TYR A 101     3073   2940   3322   -162    -65     10       C  
ATOM    862  CD1 TYR A 101     -21.967 -24.494  -1.560  1.00 26.05           C  
ANISOU  862  CD1 TYR A 101     3073   2970   3854     25   -384    280       C  
ATOM    863  CD2 TYR A 101     -23.789 -25.436  -2.911  1.00 25.42           C  
ANISOU  863  CD2 TYR A 101     3397   3198   3064   -334    601     43       C  
ATOM    864  CE1 TYR A 101     -21.716 -25.790  -1.020  1.00 26.74           C  
ANISOU  864  CE1 TYR A 101     3238   3226   3696    131   -485    407       C  
ATOM    865  CE2 TYR A 101     -23.546 -26.706  -2.380  1.00 24.88           C  
ANISOU  865  CE2 TYR A 101     2928   3257   3267    110     16      8       C  
ATOM    866  CZ  TYR A 101     -22.524 -26.867  -1.436  1.00 27.67           C  
ANISOU  866  CZ  TYR A 101     3671   3429   3413     89    -41    184       C  
ATOM    867  OH  TYR A 101     -22.309 -28.100  -0.960  1.00 31.11           O  
ANISOU  867  OH  TYR A 101     4295   3260   4264   -164     78     80       O  
ATOM    868  N   LEU A 102     -22.810 -19.748  -3.247  1.00 21.33           N  
ANISOU  868  N   LEU A 102     2671   2667   2766   -249    -25   -217       N  
ATOM    869  CA  LEU A 102     -23.224 -18.617  -4.103  1.00 22.44           C  
ANISOU  869  CA  LEU A 102     2791   2803   2930     12    -43   -238       C  
ATOM    870  C   LEU A 102     -22.727 -18.824  -5.508  1.00 22.43           C  
ANISOU  870  C   LEU A 102     2699   2980   2842     11    -11    -68       C  
ATOM    871  O   LEU A 102     -21.586 -19.259  -5.685  1.00 23.15           O  
ANISOU  871  O   LEU A 102     2753   3041   3001    112     -1    -79       O  
ATOM    872  CB  LEU A 102     -22.712 -17.255  -3.592  1.00 22.11           C  
ANISOU  872  CB  LEU A 102     2543   2827   3029   -178   -135   -249       C  
ATOM    873  CG  LEU A 102     -23.060 -16.929  -2.150  1.00 22.48           C  
ANISOU  873  CG  LEU A 102     2575   2924   3042   -195     56   -414       C  
ATOM    874  CD1 LEU A 102     -22.447 -15.535  -1.796  1.00 24.22           C  
ANISOU  874  CD1 LEU A 102     3112   3040   3050   -675   -496   -499       C  
ATOM    875  CD2 LEU A 102     -24.602 -16.916  -1.896  1.00 24.87           C  
ANISOU  875  CD2 LEU A 102     2452   3350   3646    385    784   -636       C  
ATOM    876  N   VAL A 103     -23.590 -18.575  -6.487  1.00 22.25           N  
ANISOU  876  N   VAL A 103     2875   2624   2952   -108    -61    -88       N  
ATOM    877  CA  VAL A 103     -23.273 -18.676  -7.899  1.00 22.62           C  
ANISOU  877  CA  VAL A 103     2761   2799   3034      9    -33    -71       C  
ATOM    878  C   VAL A 103     -23.703 -17.363  -8.575  1.00 23.33           C  
ANISOU  878  C   VAL A 103     2923   2750   3190     -4      5   -120       C  
ATOM    879  O   VAL A 103     -24.895 -16.942  -8.494  1.00 24.83           O  
ANISOU  879  O   VAL A 103     2842   3057   3534   -104      8     25       O  
ATOM    880  CB  VAL A 103     -24.041 -19.862  -8.560  1.00 21.59           C  
ANISOU  880  CB  VAL A 103     2708   2606   2888   -122   -264    -94       C  
ATOM    881  CG1 VAL A 103     -23.799 -19.955 -10.108  1.00 23.13           C  
ANISOU  881  CG1 VAL A 103     2794   3258   2735    217    106   -368       C  
ATOM    882  CG2 VAL A 103     -23.714 -21.224  -7.869  1.00 22.07           C  
ANISOU  882  CG2 VAL A 103     2821   2616   2946    -29   -576    -65       C  
ATOM    883  N   GLY A 104     -22.766 -16.679  -9.200  1.00 23.03           N  
ANISOU  883  N   GLY A 104     3020   2719   3009     37     90     -4       N  
ATOM    884  CA  GLY A 104     -23.089 -15.374  -9.803  1.00 22.73           C  
ANISOU  884  CA  GLY A 104     2853   2787   2995    238    134    -19       C  
ATOM    885  C   GLY A 104     -22.516 -15.211 -11.178  1.00 22.34           C  
ANISOU  885  C   GLY A 104     2859   2812   2815    119     26   -103       C  
ATOM    886  O   GLY A 104     -21.330 -15.523 -11.392  1.00 25.62           O  
ANISOU  886  O   GLY A 104     3160   3360   3214     36    130    112       O  
ATOM    887  N   HIS A 105     -23.335 -14.703 -12.104  1.00 21.24           N  
ANISOU  887  N   HIS A 105     2715   2618   2738    116    278   -155       N  
ATOM    888  CA  HIS A 105     -22.891 -14.438 -13.490  1.00 22.50           C  
ANISOU  888  CA  HIS A 105     2942   2806   2801    -72     36    -21       C  
ATOM    889  C   HIS A 105     -22.803 -12.942 -13.684  1.00 22.49           C  
ANISOU  889  C   HIS A 105     2873   2932   2741     16    -28     78       C  
ATOM    890  O   HIS A 105     -23.727 -12.199 -13.310  1.00 23.29           O  
ANISOU  890  O   HIS A 105     2795   3033   3019   -149   -232    -11       O  
ATOM    891  CB  HIS A 105     -23.810 -15.097 -14.478  1.00 23.08           C  
ANISOU  891  CB  HIS A 105     2924   3018   2827    -48     63    -53       C  
ATOM    892  CG  HIS A 105     -23.611 -14.645 -15.888  1.00 23.29           C  
ANISOU  892  CG  HIS A 105     3071   2939   2836   -129    249    -15       C  
ATOM    893  ND1 HIS A 105     -22.483 -14.951 -16.652  1.00 27.55           N  
ANISOU  893  ND1 HIS A 105     3430   3969   3066   -331     10    278       N  
ATOM    894  CD2 HIS A 105     -24.374 -13.827 -16.645  1.00 21.88           C  
ANISOU  894  CD2 HIS A 105     2680   2859   2775     39    119    127       C  
ATOM    895  CE1 HIS A 105     -22.611 -14.374 -17.847  1.00 24.08           C  
ANISOU  895  CE1 HIS A 105     3453   2695   3001    179   -220    300       C  
ATOM    896  NE2 HIS A 105     -23.745 -13.680 -17.855  1.00 27.39           N  
ANISOU  896  NE2 HIS A 105     3578   3698   3130    -46    155    234       N  
ATOM    897  N   ALA A 106     -21.615 -12.507 -14.137  1.00 22.59           N  
ANISOU  897  N   ALA A 106     2860   3049   2674    -33   -139    136       N  
ATOM    898  CA  ALA A 106     -21.383 -11.135 -14.622  1.00 22.60           C  
ANISOU  898  CA  ALA A 106     2959   2813   2813     31   -104    -83       C  
ATOM    899  C   ALA A 106     -21.570 -10.178 -13.474  1.00 22.25           C  
ANISOU  899  C   ALA A 106     2877   2847   2727     56    -75   -123       C  
ATOM    900  O   ALA A 106     -20.923 -10.409 -12.448  1.00 23.02           O  
ANISOU  900  O   ALA A 106     3070   2816   2860    115    -39   -199       O  
ATOM    901  CB  ALA A 106     -22.313 -10.851 -15.899  1.00 22.37           C  
ANISOU  901  CB  ALA A 106     2750   3175   2573     30     80      7       C  
ATOM    902  N   GLN A 107     -22.435  -9.152 -13.556  1.00 23.23           N  
ANISOU  902  N   GLN A 107     3194   2876   2754    141    -86   -453       N  
ATOM    903  CA  GLN A 107     -22.620  -8.307 -12.338  1.00 22.37           C  
ANISOU  903  CA  GLN A 107     3051   2811   2634     98    -59   -299       C  
ATOM    904  C   GLN A 107     -23.132  -9.108 -11.094  1.00 22.87           C  
ANISOU  904  C   GLN A 107     2956   2898   2833    116   -116   -182       C  
ATOM    905  O   GLN A 107     -22.797  -8.805  -9.939  1.00 21.92           O  
ANISOU  905  O   GLN A 107     2756   3031   2538     78   -167   -202       O  
ATOM    906  CB  GLN A 107     -23.502  -7.116 -12.644  1.00 20.21           C  
ANISOU  906  CB  GLN A 107     2822   2489   2368    180    -74   -509       C  
ATOM    907  CG  GLN A 107     -23.677  -6.158 -11.436  1.00 22.88           C  
ANISOU  907  CG  GLN A 107     3358   2529   2804    -78    -84   -552       C  
ATOM    908  CD  GLN A 107     -24.503  -4.960 -11.841  1.00 24.23           C  
ANISOU  908  CD  GLN A 107     3193   2898   3112   -103   -260   -233       C  
ATOM    909  OE1 GLN A 107     -24.106  -4.192 -12.741  1.00 23.63           O  
ANISOU  909  OE1 GLN A 107     3150   2896   2930    -10     99   -147       O  
ATOM    910  NE2 GLN A 107     -25.643  -4.794 -11.214  1.00 24.69           N  
ANISOU  910  NE2 GLN A 107     3239   2967   3171   -323    128    -76       N  
ATOM    911  N   GLY A 108     -23.913 -10.156 -11.328  1.00 22.94           N  
ANISOU  911  N   GLY A 108     2902   2892   2921     72    -84      0       N  
ATOM    912  CA  GLY A 108     -24.227 -11.105 -10.245  1.00 22.29           C  
ANISOU  912  CA  GLY A 108     2856   2871   2743     75    -35     -4       C  
ATOM    913  C   GLY A 108     -22.998 -11.793  -9.597  1.00 22.07           C  
ANISOU  913  C   GLY A 108     2903   2706   2776    177    -14    -50       C  
ATOM    914  O   GLY A 108     -23.076 -12.224  -8.446  1.00 21.06           O  
ANISOU  914  O   GLY A 108     2668   2776   2556     29    123    -73       O  
ATOM    915  N   GLY A 109     -21.896 -11.954 -10.346  1.00 22.80           N  
ANISOU  915  N   GLY A 109     2799   2798   3066     87   -148    -14       N  
ATOM    916  CA  GLY A 109     -20.623 -12.515  -9.810  1.00 22.05           C  
ANISOU  916  CA  GLY A 109     2640   2859   2877    157   -147   -317       C  
ATOM    917  C   GLY A 109     -19.989 -11.493  -8.858  1.00 21.74           C  
ANISOU  917  C   GLY A 109     2746   2788   2724     58   -145   -240       C  
ATOM    918  O   GLY A 109     -19.393 -11.877  -7.847  1.00 23.83           O  
ANISOU  918  O   GLY A 109     2999   3187   2868     -2    -73   -242       O  
ATOM    919  N   VAL A 110     -20.109 -10.197  -9.147  1.00 20.50           N  
ANISOU  919  N   VAL A 110     2499   2770   2518     69    160   -324       N  
ATOM    920  CA  VAL A 110     -19.569  -9.187  -8.208  1.00 21.14           C  
ANISOU  920  CA  VAL A 110     2664   2760   2607   -171     10   -140       C  
ATOM    921  C   VAL A 110     -20.426  -9.194  -6.942  1.00 21.98           C  
ANISOU  921  C   VAL A 110     2591   2957   2800   -124     -5   -157       C  
ATOM    922  O   VAL A 110     -19.912  -9.095  -5.799  1.00 20.55           O  
ANISOU  922  O   VAL A 110     2435   2845   2525   -128     20     38       O  
ATOM    923  CB  VAL A 110     -19.559  -7.753  -8.866  1.00 22.39           C  
ANISOU  923  CB  VAL A 110     2832   2718   2954   -117    103   -199       C  
ATOM    924  CG1 VAL A 110     -19.239  -6.696  -7.861  1.00 22.34           C  
ANISOU  924  CG1 VAL A 110     2806   2717   2966   -288     15    -96       C  
ATOM    925  CG2 VAL A 110     -18.576  -7.733 -10.049  1.00 21.43           C  
ANISOU  925  CG2 VAL A 110     2882   2574   2685   -268      4     38       C  
ATOM    926  N   VAL A 111     -21.759  -9.277  -7.112  1.00 21.01           N  
ANISOU  926  N   VAL A 111     2357   2864   2762   -154     90   -110       N  
ATOM    927  CA  VAL A 111     -22.627  -9.350  -5.940  1.00 22.60           C  
ANISOU  927  CA  VAL A 111     2771   2959   2858    -88    110   -100       C  
ATOM    928  C   VAL A 111     -22.278 -10.598  -5.099  1.00 21.86           C  
ANISOU  928  C   VAL A 111     2597   2924   2783    -57     26    -77       C  
ATOM    929  O   VAL A 111     -22.179 -10.503  -3.899  1.00 23.18           O  
ANISOU  929  O   VAL A 111     3113   2934   2760     65    153     10       O  
ATOM    930  CB  VAL A 111     -24.124  -9.360  -6.354  1.00 21.63           C  
ANISOU  930  CB  VAL A 111     2419   2958   2841   -122    227     33       C  
ATOM    931  CG1 VAL A 111     -25.046  -9.649  -5.097  1.00 22.52           C  
ANISOU  931  CG1 VAL A 111     2773   3170   2611   -222    387    161       C  
ATOM    932  CG2 VAL A 111     -24.525  -7.983  -7.044  1.00 22.17           C  
ANISOU  932  CG2 VAL A 111     2658   2897   2869    -20   -362   -175       C  
ATOM    933  N   ALA A 112     -22.146 -11.762  -5.742  1.00 21.56           N  
ANISOU  933  N   ALA A 112     2452   2798   2939     98    268   -122       N  
ATOM    934  CA  ALA A 112     -21.772 -13.009  -5.051  1.00 22.74           C  
ANISOU  934  CA  ALA A 112     2742   2916   2982    -41     17   -122       C  
ATOM    935  C   ALA A 112     -20.431 -12.870  -4.346  1.00 23.10           C  
ANISOU  935  C   ALA A 112     2850   2940   2986    -27     45    -68       C  
ATOM    936  O   ALA A 112     -20.287 -13.303  -3.186  1.00 23.50           O  
ANISOU  936  O   ALA A 112     3131   2849   2947   -187     15    -30       O  
ATOM    937  CB  ALA A 112     -21.673 -14.159  -6.050  1.00 22.66           C  
ANISOU  937  CB  ALA A 112     2684   2743   3179      6    -15   -246       C  
ATOM    938  N   SER A 113     -19.424 -12.346  -5.079  1.00 22.28           N  
ANISOU  938  N   SER A 113     2816   2678   2968    -72    -28     99       N  
ATOM    939  CA  SER A 113     -18.037 -12.310  -4.504  1.00 21.45           C  
ANISOU  939  CA  SER A 113     2674   2685   2791     69     30    -56       C  
ATOM    940  C   SER A 113     -18.041 -11.369  -3.281  1.00 21.94           C  
ANISOU  940  C   SER A 113     2854   2810   2671     77     48     47       C  
ATOM    941  O   SER A 113     -17.463 -11.691  -2.238  1.00 22.42           O  
ANISOU  941  O   SER A 113     2669   2928   2922    383   -112    123       O  
ATOM    942  CB  SER A 113     -16.974 -11.927  -5.538  1.00 21.38           C  
ANISOU  942  CB  SER A 113     2486   2601   3035    171    186    -15       C  
ATOM    943  OG  SER A 113     -16.978 -10.556  -5.922  1.00 21.47           O  
ANISOU  943  OG  SER A 113     2925   2928   2304     86   -184    103       O  
ATOM    944  N   MET A 114     -18.712 -10.222  -3.396  1.00 21.17           N  
ANISOU  944  N   MET A 114     2681   2825   2535     66    236    -66       N  
ATOM    945  CA  MET A 114     -18.764  -9.297  -2.261  1.00 21.84           C  
ANISOU  945  CA  MET A 114     2825   2701   2771     10    185     86       C  
ATOM    946  C   MET A 114     -19.612  -9.863  -1.114  1.00 21.57           C  
ANISOU  946  C   MET A 114     2710   2819   2664     60    119     27       C  
ATOM    947  O   MET A 114     -19.196  -9.787   0.024  1.00 22.02           O  
ANISOU  947  O   MET A 114     2825   2944   2595    129     95     11       O  
ATOM    948  CB  MET A 114     -19.215  -7.899  -2.757  1.00 21.13           C  
ANISOU  948  CB  MET A 114     2669   2393   2966    -85    135    149       C  
ATOM    949  CG  MET A 114     -18.091  -7.318  -3.632  1.00 21.99           C  
ANISOU  949  CG  MET A 114     2853   2708   2792    -34    196    270       C  
ATOM    950  SD  MET A 114     -18.521  -5.629  -4.099  1.00 22.53           S  
ANISOU  950  SD  MET A 114     3036   2977   2546     76     22    -30       S  
ATOM    951  CE  MET A 114     -18.145  -4.764  -2.552  1.00 20.74           C  
ANISOU  951  CE  MET A 114     2973   2614   2293   -247     60   -210       C  
ATOM    952  N   LEU A 115     -20.777 -10.471  -1.397  1.00 22.14           N  
ANISOU  952  N   LEU A 115     2869   2838   2701   -103    236     16       N  
ATOM    953  CA  LEU A 115     -21.548 -11.075  -0.309  1.00 22.35           C  
ANISOU  953  CA  LEU A 115     2799   2770   2923     53    231     -7       C  
ATOM    954  C   LEU A 115     -20.741 -12.168   0.416  1.00 22.81           C  
ANISOU  954  C   LEU A 115     2987   2790   2889     56    227    -27       C  
ATOM    955  O   LEU A 115     -20.766 -12.268   1.670  1.00 23.39           O  
ANISOU  955  O   LEU A 115     2978   2785   3123    185    246    -45       O  
ATOM    956  CB  LEU A 115     -22.858 -11.631  -0.855  1.00 23.02           C  
ANISOU  956  CB  LEU A 115     2731   2928   3085     -9    247     84       C  
ATOM    957  CG  LEU A 115     -23.836 -12.074   0.263  1.00 22.84           C  
ANISOU  957  CG  LEU A 115     2731   2977   2968      0    317   -133       C  
ATOM    958  CD1 LEU A 115     -24.305 -10.786   1.066  1.00 22.71           C  
ANISOU  958  CD1 LEU A 115     3150   2719   2757    -41    670   -378       C  
ATOM    959  CD2 LEU A 115     -24.998 -12.877  -0.360  1.00 24.26           C  
ANISOU  959  CD2 LEU A 115     2998   2978   3240   -660    -25    606       C  
ATOM    960  N   ALA A 116     -20.001 -12.983  -0.337  1.00 21.65           N  
ANISOU  960  N   ALA A 116     2613   2621   2990     68    241    -21       N  
ATOM    961  CA  ALA A 116     -19.203 -14.055   0.324  1.00 21.34           C  
ANISOU  961  CA  ALA A 116     2810   2647   2649    179    110    -79       C  
ATOM    962  C   ALA A 116     -18.105 -13.471   1.230  1.00 20.79           C  
ANISOU  962  C   ALA A 116     2600   2653   2646    114    102    -62       C  
ATOM    963  O   ALA A 116     -17.724 -14.089   2.278  1.00 22.74           O  
ANISOU  963  O   ALA A 116     2882   2815   2943     19      7     38       O  
ATOM    964  CB  ALA A 116     -18.569 -15.026  -0.714  1.00 19.54           C  
ANISOU  964  CB  ALA A 116     2620   2419   2384    231    204   -311       C  
ATOM    965  N   GLY A 117     -17.575 -12.319   0.838  1.00 20.40           N  
ANISOU  965  N   GLY A 117     2524   2631   2595     45     39    -95       N  
ATOM    966  CA  GLY A 117     -16.543 -11.638   1.665  1.00 20.78           C  
ANISOU  966  CA  GLY A 117     2593   2816   2486    146    103    -12       C  
ATOM    967  C   GLY A 117     -17.137 -11.026   2.908  1.00 21.44           C  
ANISOU  967  C   GLY A 117     2783   2805   2555    152    118     -6       C  
ATOM    968  O   GLY A 117     -16.409 -10.761   3.876  1.00 21.93           O  
ANISOU  968  O   GLY A 117     2959   2806   2567    394    107     -5       O  
ATOM    969  N   LEU A 118     -18.462 -10.775   2.881  1.00 20.65           N  
ANISOU  969  N   LEU A 118     2706   2732   2406    134    326    -40       N  
ATOM    970  CA  LEU A 118     -19.148 -10.229   4.111  1.00 21.71           C  
ANISOU  970  CA  LEU A 118     2963   2700   2582    172    258     20       C  
ATOM    971  C   LEU A 118     -19.640 -11.386   4.992  1.00 22.72           C  
ANISOU  971  C   LEU A 118     3012   2963   2654     24    276     15       C  
ATOM    972  O   LEU A 118     -19.906 -11.165   6.183  1.00 24.18           O  
ANISOU  972  O   LEU A 118     3271   3156   2759     69    264    -66       O  
ATOM    973  CB  LEU A 118     -20.345  -9.338   3.711  1.00 22.89           C  
ANISOU  973  CB  LEU A 118     2995   2819   2882    222    127     36       C  
ATOM    974  CG  LEU A 118     -19.933  -8.085   2.927  1.00 21.79           C  
ANISOU  974  CG  LEU A 118     2769   2984   2524     69    -10    -51       C  
ATOM    975  CD1 LEU A 118     -21.203  -7.452   2.263  1.00 24.12           C  
ANISOU  975  CD1 LEU A 118     3453   3075   2634    602     12    720       C  
ATOM    976  CD2 LEU A 118     -19.456  -7.107   3.991  1.00 25.62           C  
ANISOU  976  CD2 LEU A 118     3508   3022   3205   -260   -418    -34       C  
ATOM    977  N   TYR A 119     -19.776 -12.590   4.420  1.00 22.12           N  
ANISOU  977  N   TYR A 119     2887   2995   2521     86    218      0       N  
ATOM    978  CA  TYR A 119     -20.241 -13.800   5.140  1.00 23.28           C  
ANISOU  978  CA  TYR A 119     3078   2970   2798    100    219     31       C  
ATOM    979  C   TYR A 119     -19.258 -14.999   4.961  1.00 24.00           C  
ANISOU  979  C   TYR A 119     3097   3098   2924     30    175      2       C  
ATOM    980  O   TYR A 119     -19.655 -16.074   4.497  1.00 24.66           O  
ANISOU  980  O   TYR A 119     3232   3186   2951    -21    160    -38       O  
ATOM    981  CB  TYR A 119     -21.657 -14.201   4.692  1.00 22.78           C  
ANISOU  981  CB  TYR A 119     3145   2886   2622    123    422      4       C  
ATOM    982  CG  TYR A 119     -22.718 -13.264   5.222  1.00 23.39           C  
ANISOU  982  CG  TYR A 119     3049   3039   2798    129    152    222       C  
ATOM    983  CD1 TYR A 119     -23.231 -13.462   6.488  1.00 24.34           C  
ANISOU  983  CD1 TYR A 119     3567   2632   3046     29    464     87       C  
ATOM    984  CD2 TYR A 119     -23.119 -12.136   4.488  1.00 23.29           C  
ANISOU  984  CD2 TYR A 119     2704   2747   3396     18     52    -47       C  
ATOM    985  CE1 TYR A 119     -24.238 -12.664   6.984  1.00 25.32           C  
ANISOU  985  CE1 TYR A 119     3388   3022   3208    280    -71    -25       C  
ATOM    986  CE2 TYR A 119     -24.102 -11.305   4.956  1.00 25.49           C  
ANISOU  986  CE2 TYR A 119     3312   3221   3151    208    256    -40       C  
ATOM    987  CZ  TYR A 119     -24.655 -11.561   6.212  1.00 26.56           C  
ANISOU  987  CZ  TYR A 119     3685   3384   3023    449     34     44       C  
ATOM    988  OH  TYR A 119     -25.634 -10.726   6.692  1.00 24.33           O  
ANISOU  988  OH  TYR A 119     3734   2947   2563     94    277   -395       O  
ATOM    989  N   PRO A 120     -17.974 -14.787   5.258  1.00 24.97           N  
ANISOU  989  N   PRO A 120     3329   3242   2916    -20    -40     69       N  
ATOM    990  CA  PRO A 120     -17.013 -15.819   4.871  1.00 24.94           C  
ANISOU  990  CA  PRO A 120     3087   3247   3140     26     67     21       C  
ATOM    991  C   PRO A 120     -17.069 -17.011   5.795  1.00 27.95           C  
ANISOU  991  C   PRO A 120     3607   3526   3485    105    -32      0       C  
ATOM    992  O   PRO A 120     -16.499 -18.069   5.453  1.00 29.60           O  
ANISOU  992  O   PRO A 120     3945   3530   3770   -121   -144   -136       O  
ATOM    993  CB  PRO A 120     -15.641 -15.089   4.971  1.00 26.11           C  
ANISOU  993  CB  PRO A 120     3459   3224   3235   -108     31    -28       C  
ATOM    994  CG  PRO A 120     -15.840 -14.028   6.004  1.00 26.20           C  
ANISOU  994  CG  PRO A 120     3424   3220   3308    202   -327    -63       C  
ATOM    995  CD  PRO A 120     -17.322 -13.572   5.786  1.00 23.65           C  
ANISOU  995  CD  PRO A 120     2903   2957   3125   -180   -161   -144       C  
ATOM    996  N   ASP A 121     -17.714 -16.796   6.970  1.00 30.87           N  
ANISOU  996  N   ASP A 121     4036   3844   3847    114    166    252       N  
ATOM    997  CA  ASP A 121     -17.959 -17.778   8.022  1.00 33.09           C  
ANISOU  997  CA  ASP A 121     4475   4122   3973    -30    270    112       C  
ATOM    998  C   ASP A 121     -19.169 -18.648   7.701  1.00 33.43           C  
ANISOU  998  C   ASP A 121     4529   4033   4139    -72    244    241       C  
ATOM    999  O   ASP A 121     -19.283 -19.675   8.365  1.00 36.46           O  
ANISOU  999  O   ASP A 121     5093   4198   4561    -64    210    162       O  
ATOM   1000  CB  ASP A 121     -18.194 -17.076   9.408  1.00 33.95           C  
ANISOU 1000  CB  ASP A 121     4479   4325   4094    135    524    204       C  
ATOM   1001  CG  ASP A 121     -19.342 -15.996   9.372  1.00 34.94           C  
ANISOU 1001  CG  ASP A 121     5254   4297   3724    591    488    244       C  
ATOM   1002  OD1 ASP A 121     -19.604 -15.378   8.315  1.00 34.90           O  
ANISOU 1002  OD1 ASP A 121     5657   3812   3791   1373   1150    782       O  
ATOM   1003  OD2 ASP A 121     -20.047 -15.817  10.417  1.00 33.33           O  
ANISOU 1003  OD2 ASP A 121     5016   4318   3329    225    138   -128       O  
ATOM   1004  N   LEU A 122     -20.060 -18.248   6.754  1.00 30.90           N  
ANISOU 1004  N   LEU A 122     4312   3814   3612   -197    224    248       N  
ATOM   1005  CA  LEU A 122     -21.329 -18.942   6.450  1.00 29.90           C  
ANISOU 1005  CA  LEU A 122     4230   3836   3293    -42    305    226       C  
ATOM   1006  C   LEU A 122     -21.315 -19.605   5.063  1.00 30.03           C  
ANISOU 1006  C   LEU A 122     4209   3604   3595   -148    436     96       C  
ATOM   1007  O   LEU A 122     -21.696 -20.752   4.883  1.00 30.57           O  
ANISOU 1007  O   LEU A 122     4262   3606   3747   -355    794    -44       O  
ATOM   1008  CB  LEU A 122     -22.492 -17.939   6.514  1.00 30.21           C  
ANISOU 1008  CB  LEU A 122     4162   3806   3509   -114    264    219       C  
ATOM   1009  CG  LEU A 122     -23.896 -18.466   6.201  1.00 29.07           C  
ANISOU 1009  CG  LEU A 122     3865   3715   3464    118    106    265       C  
ATOM   1010  CD1 LEU A 122     -24.257 -19.730   7.129  1.00 31.24           C  
ANISOU 1010  CD1 LEU A 122     3855   4100   3913   -118    252    425       C  
ATOM   1011  CD2 LEU A 122     -25.036 -17.370   6.218  1.00 30.31           C  
ANISOU 1011  CD2 LEU A 122     3925   3928   3662     45    328    110       C  
ATOM   1012  N   ILE A 123     -20.886 -18.859   4.065  1.00 26.98           N  
ANISOU 1012  N   ILE A 123     3646   3526   3080   -186    448    176       N  
ATOM   1013  CA  ILE A 123     -20.908 -19.383   2.701  1.00 24.77           C  
ANISOU 1013  CA  ILE A 123     3275   3152   2984    -35    291    -62       C  
ATOM   1014  C   ILE A 123     -19.829 -20.439   2.603  1.00 26.00           C  
ANISOU 1014  C   ILE A 123     3410   3238   3229   -169    165    122       C  
ATOM   1015  O   ILE A 123     -18.733 -20.280   3.176  1.00 26.16           O  
ANISOU 1015  O   ILE A 123     3278   3362   3298    -50     23    181       O  
ATOM   1016  CB  ILE A 123     -20.675 -18.240   1.715  1.00 24.04           C  
ANISOU 1016  CB  ILE A 123     3171   3180   2783     42    313    -93       C  
ATOM   1017  CG1 ILE A 123     -21.702 -17.084   1.929  1.00 23.66           C  
ANISOU 1017  CG1 ILE A 123     2993   3210   2787    -24    212     42       C  
ATOM   1018  CG2 ILE A 123     -20.560 -18.765   0.212  1.00 23.96           C  
ANISOU 1018  CG2 ILE A 123     3133   3383   2586     42    104   -218       C  
ATOM   1019  CD1 ILE A 123     -23.148 -17.521   1.749  1.00 22.95           C  
ANISOU 1019  CD1 ILE A 123     2658   3236   2822    -61    373   -361       C  
ATOM   1020  N   LYS A 124     -20.147 -21.534   1.900  1.00 26.25           N  
ANISOU 1020  N   LYS A 124     3506   3283   3181     -4    189   -100       N  
ATOM   1021  CA  LYS A 124     -19.233 -22.709   1.836  1.00 27.57           C  
ANISOU 1021  CA  LYS A 124     3668   3404   3404   -134    196     81       C  
ATOM   1022  C   LYS A 124     -18.429 -22.764   0.561  1.00 26.45           C  
ANISOU 1022  C   LYS A 124     3514   3144   3391   -169    120     -7       C  
ATOM   1023  O   LYS A 124     -17.294 -23.215   0.586  1.00 25.76           O  
ANISOU 1023  O   LYS A 124     3169   3107   3511   -277    -98     43       O  
ATOM   1024  CB  LYS A 124     -20.019 -24.031   2.048  1.00 27.39           C  
ANISOU 1024  CB  LYS A 124     3666   3487   3251   -349    150    -13       C  
ATOM   1025  CG  LYS A 124     -20.669 -24.023   3.459  1.00 33.71           C  
ANISOU 1025  CG  LYS A 124     4666   4491   3649   -139    269    347       C  
ATOM   1026  CD  LYS A 124     -19.616 -23.815   4.579  1.00 38.55           C  
ANISOU 1026  CD  LYS A 124     5676   5064   3906   -527     12    115       C  
ATOM   1027  CE  LYS A 124     -20.326 -23.940   5.965  1.00 43.34           C  
ANISOU 1027  CE  LYS A 124     6321   6203   3943    -83      5   -140       C  
ATOM   1028  NZ  LYS A 124     -19.653 -23.077   6.994  1.00 46.61           N  
ANISOU 1028  NZ  LYS A 124     6863   6320   4526    -11   -227   -288       N  
ATOM   1029  N   LYS A 125     -19.009 -22.306  -0.543  1.00 25.69           N  
ANISOU 1029  N   LYS A 125     3358   3093   3308   -151    -55    -73       N  
ATOM   1030  CA  LYS A 125     -18.305 -22.340  -1.862  1.00 25.04           C  
ANISOU 1030  CA  LYS A 125     3408   2834   3272     85    124   -148       C  
ATOM   1031  C   LYS A 125     -18.919 -21.279  -2.688  1.00 24.44           C  
ANISOU 1031  C   LYS A 125     3142   3110   3032     64     19   -113       C  
ATOM   1032  O   LYS A 125     -20.111 -20.974  -2.458  1.00 24.31           O  
ANISOU 1032  O   LYS A 125     2989   3078   3168    151     90     -2       O  
ATOM   1033  CB  LYS A 125     -18.548 -23.690  -2.656  1.00 26.50           C  
ANISOU 1033  CB  LYS A 125     3432   2994   3642     31    -13   -357       C  
ATOM   1034  CG  LYS A 125     -18.074 -24.931  -1.924  1.00 28.62           C  
ANISOU 1034  CG  LYS A 125     3837   3129   3909    342     88   -174       C  
ATOM   1035  CD  LYS A 125     -18.200 -26.193  -2.778  1.00 32.55           C  
ANISOU 1035  CD  LYS A 125     4819   3582   3965    326    -85   -603       C  
ATOM   1036  CE  LYS A 125     -17.313 -27.300  -2.187  1.00 36.59           C  
ANISOU 1036  CE  LYS A 125     5603   3798   4499    927    -37  -1088       C  
ATOM   1037  NZ  LYS A 125     -17.317 -28.561  -2.969  1.00 40.41           N  
ANISOU 1037  NZ  LYS A 125     6826   3216   5311    858  -1053   -485       N  
ATOM   1038  N   VAL A 126     -18.131 -20.735  -3.647  1.00 23.26           N  
ANISOU 1038  N   VAL A 126     3222   2767   2846    119     51    -82       N  
ATOM   1039  CA  VAL A 126     -18.588 -19.716  -4.604  1.00 22.26           C  
ANISOU 1039  CA  VAL A 126     3022   2835   2600    121    143    -80       C  
ATOM   1040  C   VAL A 126     -18.199 -20.137  -6.011  1.00 23.51           C  
ANISOU 1040  C   VAL A 126     3062   2914   2957     51     -4   -144       C  
ATOM   1041  O   VAL A 126     -17.053 -20.620  -6.255  1.00 25.20           O  
ANISOU 1041  O   VAL A 126     3083   3237   3251    247    174   -223       O  
ATOM   1042  CB  VAL A 126     -17.877 -18.372  -4.233  1.00 21.25           C  
ANISOU 1042  CB  VAL A 126     3073   2617   2383   -147     42     29       C  
ATOM   1043  CG1 VAL A 126     -18.058 -17.256  -5.250  1.00 23.98           C  
ANISOU 1043  CG1 VAL A 126     3477   2750   2881    224    249    271       C  
ATOM   1044  CG2 VAL A 126     -18.423 -17.854  -2.872  1.00 21.51           C  
ANISOU 1044  CG2 VAL A 126     2748   2753   2673   -148     66   -141       C  
ATOM   1045  N   VAL A 127     -19.106 -19.903  -6.943  1.00 21.92           N  
ANISOU 1045  N   VAL A 127     2687   2835   2804    178     37   -108       N  
ATOM   1046  CA  VAL A 127     -18.839 -20.054  -8.384  1.00 23.52           C  
ANISOU 1046  CA  VAL A 127     2975   3005   2956     94    -18     19       C  
ATOM   1047  C   VAL A 127     -19.096 -18.696  -9.026  1.00 22.97           C  
ANISOU 1047  C   VAL A 127     2857   2904   2966     15     17     35       C  
ATOM   1048  O   VAL A 127     -20.205 -18.160  -8.914  1.00 22.57           O  
ANISOU 1048  O   VAL A 127     2564   3051   2958     -4     21    -38       O  
ATOM   1049  CB  VAL A 127     -19.747 -21.157  -9.016  1.00 22.69           C  
ANISOU 1049  CB  VAL A 127     2946   2867   2805     35    -16    103       C  
ATOM   1050  CG1 VAL A 127     -19.500 -21.253 -10.557  1.00 22.46           C  
ANISOU 1050  CG1 VAL A 127     2956   2990   2586      9    140   -269       C  
ATOM   1051  CG2 VAL A 127     -19.484 -22.529  -8.320  1.00 25.33           C  
ANISOU 1051  CG2 VAL A 127     3287   2878   3456     77    -69    160       C  
ATOM   1052  N   LEU A 128     -18.102 -18.128  -9.696  1.00 22.23           N  
ANISOU 1052  N   LEU A 128     2783   2837   2826    -85    -44     35       N  
ATOM   1053  CA  LEU A 128     -18.286 -16.874 -10.410  1.00 22.44           C  
ANISOU 1053  CA  LEU A 128     2970   2927   2627   -138   -146    -18       C  
ATOM   1054  C   LEU A 128     -18.155 -17.206 -11.902  1.00 23.65           C  
ANISOU 1054  C   LEU A 128     3058   3011   2916    -41    -44    -91       C  
ATOM   1055  O   LEU A 128     -17.117 -17.784 -12.326  1.00 23.53           O  
ANISOU 1055  O   LEU A 128     2889   3139   2911     86     86   -196       O  
ATOM   1056  CB  LEU A 128     -17.138 -15.869 -10.019  1.00 21.85           C  
ANISOU 1056  CB  LEU A 128     2917   2867   2516   -148   -178     53       C  
ATOM   1057  CG  LEU A 128     -17.056 -15.596  -8.489  1.00 22.20           C  
ANISOU 1057  CG  LEU A 128     2892   3077   2463    -46   -156     36       C  
ATOM   1058  CD1 LEU A 128     -15.920 -14.541  -8.270  1.00 26.14           C  
ANISOU 1058  CD1 LEU A 128     3429   3703   2799   -335    -18   -246       C  
ATOM   1059  CD2 LEU A 128     -18.413 -15.070  -7.916  1.00 24.82           C  
ANISOU 1059  CD2 LEU A 128     3217   3174   3036   -345     10   -606       C  
ATOM   1060  N   LEU A 129     -19.145 -16.765 -12.678  1.00 22.98           N  
ANISOU 1060  N   LEU A 129     3062   3098   2571   -306   -198   -169       N  
ATOM   1061  CA  LEU A 129     -19.144 -16.934 -14.145  1.00 23.18           C  
ANISOU 1061  CA  LEU A 129     3049   3072   2685    -25     78   -108       C  
ATOM   1062  C   LEU A 129     -19.012 -15.550 -14.741  1.00 22.99           C  
ANISOU 1062  C   LEU A 129     3102   3108   2523    -49    -43   -135       C  
ATOM   1063  O   LEU A 129     -19.901 -14.713 -14.608  1.00 23.42           O  
ANISOU 1063  O   LEU A 129     3154   3192   2550     30    217      4       O  
ATOM   1064  CB  LEU A 129     -20.436 -17.654 -14.626  1.00 23.79           C  
ANISOU 1064  CB  LEU A 129     3308   2996   2732   -191      5   -302       C  
ATOM   1065  CG  LEU A 129     -20.566 -19.064 -14.012  1.00 23.63           C  
ANISOU 1065  CG  LEU A 129     3119   3234   2622   -453    255   -344       C  
ATOM   1066  CD1 LEU A 129     -21.677 -19.060 -12.967  1.00 26.11           C  
ANISOU 1066  CD1 LEU A 129     3619   3694   2607   -279    359   -692       C  
ATOM   1067  CD2 LEU A 129     -20.896 -20.115 -15.089  1.00 23.32           C  
ANISOU 1067  CD2 LEU A 129     3465   3213   2181    -16   -303   -691       C  
ATOM   1068  N   ALA A 130     -17.945 -15.353 -15.479  1.00 24.15           N  
ANISOU 1068  N   ALA A 130     3320   3203   2651   -102    -37   -133       N  
ATOM   1069  CA  ALA A 130     -17.621 -14.045 -16.059  1.00 24.60           C  
ANISOU 1069  CA  ALA A 130     3545   3010   2789     64     31   -147       C  
ATOM   1070  C   ALA A 130     -17.895 -12.867 -15.106  1.00 24.51           C  
ANISOU 1070  C   ALA A 130     3400   3058   2853    116    -13   -131       C  
ATOM   1071  O   ALA A 130     -18.544 -11.890 -15.524  1.00 24.38           O  
ANISOU 1071  O   ALA A 130     3253   2989   3019    151      7   -187       O  
ATOM   1072  CB  ALA A 130     -18.342 -13.856 -17.424  1.00 25.58           C  
ANISOU 1072  CB  ALA A 130     3480   3346   2890    156     -4   -220       C  
ATOM   1073  N   PRO A 131     -17.335 -12.920 -13.854  1.00 24.57           N  
ANISOU 1073  N   PRO A 131     3500   2930   2903     37    -19   -148       N  
ATOM   1074  CA  PRO A 131     -17.734 -11.900 -12.838  1.00 23.94           C  
ANISOU 1074  CA  PRO A 131     3444   2879   2770     24     30    -88       C  
ATOM   1075  C   PRO A 131     -17.302 -10.482 -13.333  1.00 25.27           C  
ANISOU 1075  C   PRO A 131     3503   3141   2955    -97     -7   -194       C  
ATOM   1076  O   PRO A 131     -16.114 -10.276 -13.657  1.00 25.54           O  
ANISOU 1076  O   PRO A 131     3603   3267   2831   -155    127   -122       O  
ATOM   1077  CB  PRO A 131     -16.955 -12.335 -11.582  1.00 23.39           C  
ANISOU 1077  CB  PRO A 131     3210   2931   2744     60    -48   -243       C  
ATOM   1078  CG  PRO A 131     -15.670 -13.155 -12.179  1.00 23.97           C  
ANISOU 1078  CG  PRO A 131     3373   2890   2845    159      6   -400       C  
ATOM   1079  CD  PRO A 131     -16.365 -13.903 -13.314  1.00 22.90           C  
ANISOU 1079  CD  PRO A 131     2996   3037   2665    259    -66   -257       C  
ATOM   1080  N   ALA A 132     -18.257  -9.551 -13.369  1.00 23.74           N  
ANISOU 1080  N   ALA A 132     3173   3046   2800    -70   -174     43       N  
ATOM   1081  CA  ALA A 132     -18.096  -8.219 -13.982  1.00 24.86           C  
ANISOU 1081  CA  ALA A 132     3316   3179   2949    -82   -136     81       C  
ATOM   1082  C   ALA A 132     -17.349  -7.193 -13.101  1.00 25.06           C  
ANISOU 1082  C   ALA A 132     3348   3119   3053     -9     80    138       C  
ATOM   1083  O   ALA A 132     -17.758  -6.045 -12.987  1.00 24.57           O  
ANISOU 1083  O   ALA A 132     3510   3101   2723     66    168    181       O  
ATOM   1084  CB  ALA A 132     -19.472  -7.703 -14.469  1.00 25.58           C  
ANISOU 1084  CB  ALA A 132     3191   3318   3208     82    107     78       C  
ATOM   1085  N   ALA A 133     -16.198  -7.607 -12.539  1.00 24.21           N  
ANISOU 1085  N   ALA A 133     3092   3145   2961   -186     66    207       N  
ATOM   1086  CA  ALA A 133     -15.405  -6.705 -11.688  1.00 25.31           C  
ANISOU 1086  CA  ALA A 133     3245   3248   3122    -11    110     30       C  
ATOM   1087  C   ALA A 133     -14.871  -5.542 -12.504  1.00 26.52           C  
ANISOU 1087  C   ALA A 133     3458   3402   3215   -165     50    -34       C  
ATOM   1088  O   ALA A 133     -14.561  -4.483 -11.924  1.00 26.47           O  
ANISOU 1088  O   ALA A 133     3831   3082   3141   -325    285    -94       O  
ATOM   1089  CB  ALA A 133     -14.280  -7.447 -11.001  1.00 25.84           C  
ANISOU 1089  CB  ALA A 133     3259   3368   3189     29     32    -54       C  
ATOM   1090  N   THR A 134     -14.825  -5.697 -13.843  1.00 26.33           N  
ANISOU 1090  N   THR A 134     3471   3403   3128   -169    196   -119       N  
ATOM   1091  CA  THR A 134     -14.482  -4.597 -14.722  1.00 27.76           C  
ANISOU 1091  CA  THR A 134     3868   3642   3038    -65     96   -154       C  
ATOM   1092  C   THR A 134     -15.517  -3.477 -14.762  1.00 27.56           C  
ANISOU 1092  C   THR A 134     3792   3579   3099   -152    122   -264       C  
ATOM   1093  O   THR A 134     -15.250  -2.430 -15.368  1.00 26.49           O  
ANISOU 1093  O   THR A 134     3885   3306   2871   -229    324   -268       O  
ATOM   1094  CB  THR A 134     -14.348  -5.117 -16.212  1.00 27.07           C  
ANISOU 1094  CB  THR A 134     3633   3766   2885   -129    103   -192       C  
ATOM   1095  OG1 THR A 134     -15.486  -5.906 -16.527  1.00 29.31           O  
ANISOU 1095  OG1 THR A 134     5048   3243   2843   -234    195   -439       O  
ATOM   1096  CG2 THR A 134     -13.127  -5.951 -16.398  1.00 31.22           C  
ANISOU 1096  CG2 THR A 134     4503   3947   3410     78    462   -130       C  
ATOM   1097  N   LEU A 135     -16.728  -3.674 -14.207  1.00 26.98           N  
ANISOU 1097  N   LEU A 135     3698   3624   2928    -27     16   -206       N  
ATOM   1098  CA  LEU A 135     -17.721  -2.536 -14.201  1.00 26.73           C  
ANISOU 1098  CA  LEU A 135     3661   3390   3105    -86    -92   -313       C  
ATOM   1099  C   LEU A 135     -17.130  -1.281 -13.435  1.00 26.45           C  
ANISOU 1099  C   LEU A 135     3796   3335   2917     51    -70   -282       C  
ATOM   1100  O   LEU A 135     -17.528  -0.132 -13.708  1.00 25.74           O  
ANISOU 1100  O   LEU A 135     3790   3457   2531     26   -201   -286       O  
ATOM   1101  CB  LEU A 135     -19.080  -2.958 -13.626  1.00 25.81           C  
ANISOU 1101  CB  LEU A 135     3641   3216   2948   -101    -80   -172       C  
ATOM   1102  CG  LEU A 135     -19.182  -3.375 -12.126  1.00 25.45           C  
ANISOU 1102  CG  LEU A 135     3455   3272   2939   -308    248   -447       C  
ATOM   1103  CD1 LEU A 135     -19.305  -2.162 -11.109  1.00 24.06           C  
ANISOU 1103  CD1 LEU A 135     3406   2503   3233    194    300   -327       C  
ATOM   1104  CD2 LEU A 135     -20.330  -4.322 -12.007  1.00 24.59           C  
ANISOU 1104  CD2 LEU A 135     4156   2464   2723   -589   -212    295       C  
ATOM   1105  N   LYS A 136     -16.187  -1.514 -12.504  1.00 24.73           N  
ANISOU 1105  N   LYS A 136     3188   3218   2988    -50   -116   -259       N  
ATOM   1106  CA  LYS A 136     -15.565  -0.425 -11.726  1.00 25.88           C  
ANISOU 1106  CA  LYS A 136     3561   3295   2976    -58   -117    -21       C  
ATOM   1107  C   LYS A 136     -14.611   0.344 -12.626  1.00 26.30           C  
ANISOU 1107  C   LYS A 136     3549   3218   3225    -40    -15    -62       C  
ATOM   1108  O   LYS A 136     -14.651   1.597 -12.729  1.00 25.85           O  
ANISOU 1108  O   LYS A 136     3510   3192   3118    314    -21    -12       O  
ATOM   1109  CB  LYS A 136     -14.752  -1.031 -10.543  1.00 24.97           C  
ANISOU 1109  CB  LYS A 136     3307   3078   3102    108   -165   -198       C  
ATOM   1110  CG  LYS A 136     -13.980  -0.073  -9.799  1.00 23.65           C  
ANISOU 1110  CG  LYS A 136     3267   3353   2364    -75   -274     67       C  
ATOM   1111  CD  LYS A 136     -13.380  -0.737  -8.526  1.00 26.52           C  
ANISOU 1111  CD  LYS A 136     3746   3850   2478   -142    -11    305       C  
ATOM   1112  CE  LYS A 136     -12.588   0.286  -7.723  1.00 25.89           C  
ANISOU 1112  CE  LYS A 136     3304   3547   2984   -335   -282    429       C  
ATOM   1113  NZ  LYS A 136     -12.053  -0.270  -6.409  1.00 27.53           N  
ANISOU 1113  NZ  LYS A 136     3526   3387   3546    137   -302    601       N  
ATOM   1114  N   GLY A 137     -13.718  -0.392 -13.276  1.00 27.21           N  
ANISOU 1114  N   GLY A 137     3665   3415   3256    -54     83    152       N  
ATOM   1115  CA  GLY A 137     -12.796   0.219 -14.194  1.00 29.02           C  
ANISOU 1115  CA  GLY A 137     3962   3530   3533   -199    151    312       C  
ATOM   1116  C   GLY A 137     -13.506   0.900 -15.346  1.00 28.76           C  
ANISOU 1116  C   GLY A 137     3810   3593   3524   -139    167    233       C  
ATOM   1117  O   GLY A 137     -13.017   1.943 -15.793  1.00 30.54           O  
ANISOU 1117  O   GLY A 137     4239   3847   3516   -210    467    459       O  
ATOM   1118  N   ASP A 138     -14.635   0.350 -15.812  1.00 29.71           N  
ANISOU 1118  N   ASP A 138     4042   3727   3520    -36    278    199       N  
ATOM   1119  CA  ASP A 138     -15.413   0.957 -16.892  1.00 29.17           C  
ANISOU 1119  CA  ASP A 138     3867   3770   3445     -7    149    131       C  
ATOM   1120  C   ASP A 138     -15.950   2.310 -16.446  1.00 28.39           C  
ANISOU 1120  C   ASP A 138     3950   3605   3232   -100    244     16       C  
ATOM   1121  O   ASP A 138     -15.880   3.269 -17.199  1.00 27.96           O  
ANISOU 1121  O   ASP A 138     4042   3635   2947     17    239   -108       O  
ATOM   1122  CB  ASP A 138     -16.580   0.074 -17.388  1.00 29.18           C  
ANISOU 1122  CB  ASP A 138     4015   3683   3386     22     84    310       C  
ATOM   1123  CG  ASP A 138     -16.111  -1.206 -18.102  1.00 31.40           C  
ANISOU 1123  CG  ASP A 138     4387   4097   3446      0    -47    252       C  
ATOM   1124  OD1 ASP A 138     -14.888  -1.413 -18.374  1.00 30.92           O  
ANISOU 1124  OD1 ASP A 138     4557   4032   3157   -192    680     19       O  
ATOM   1125  OD2 ASP A 138     -16.975  -2.056 -18.322  1.00 36.14           O  
ANISOU 1125  OD2 ASP A 138     5542   4482   3705   -340   -656   -240       O  
ATOM   1126  N   ALA A 139     -16.520   2.365 -15.226  1.00 26.58           N  
ANISOU 1126  N   ALA A 139     3685   3538   2874   -175     96     11       N  
ATOM   1127  CA  ALA A 139     -17.086   3.591 -14.684  1.00 25.98           C  
ANISOU 1127  CA  ALA A 139     3504   3462   2903    -67    135    156       C  
ATOM   1128  C   ALA A 139     -15.969   4.649 -14.490  1.00 27.05           C  
ANISOU 1128  C   ALA A 139     3654   3532   3089    -86    192    176       C  
ATOM   1129  O   ALA A 139     -16.208   5.843 -14.648  1.00 27.35           O  
ANISOU 1129  O   ALA A 139     3772   3540   3078      2    222    274       O  
ATOM   1130  CB  ALA A 139     -17.815   3.317 -13.355  1.00 24.91           C  
ANISOU 1130  CB  ALA A 139     3266   3446   2752    -77    231    105       C  
ATOM   1131  N   LEU A 140     -14.752   4.204 -14.125  1.00 26.76           N  
ANISOU 1131  N   LEU A 140     3534   3639   2992   -149    357    156       N  
ATOM   1132  CA  LEU A 140     -13.625   5.139 -13.951  1.00 27.47           C  
ANISOU 1132  CA  LEU A 140     3839   3572   3024   -174    229    144       C  
ATOM   1133  C   LEU A 140     -13.127   5.702 -15.303  1.00 28.03           C  
ANISOU 1133  C   LEU A 140     3955   3509   3186   -176    203    253       C  
ATOM   1134  O   LEU A 140     -12.663   6.844 -15.399  1.00 28.03           O  
ANISOU 1134  O   LEU A 140     3721   3608   3320   -370    146    239       O  
ATOM   1135  CB  LEU A 140     -12.483   4.457 -13.242  1.00 27.35           C  
ANISOU 1135  CB  LEU A 140     3755   3532   3104    -39    295    146       C  
ATOM   1136  CG  LEU A 140     -12.696   4.289 -11.702  1.00 26.26           C  
ANISOU 1136  CG  LEU A 140     3680   3460   2835    148    192    214       C  
ATOM   1137  CD1 LEU A 140     -11.618   3.365 -11.115  1.00 30.04           C  
ANISOU 1137  CD1 LEU A 140     4213   3565   3633    217     53    219       C  
ATOM   1138  CD2 LEU A 140     -12.629   5.686 -11.071  1.00 27.89           C  
ANISOU 1138  CD2 LEU A 140     3691   3778   3127   -415    416     86       C  
ATOM   1139  N   GLU A 141     -13.204   4.863 -16.324  1.00 29.76           N  
ANISOU 1139  N   GLU A 141     4344   3721   3240   -124    214    216       N  
ATOM   1140  CA AGLU A 141     -12.865   5.228 -17.723  0.50 31.28           C  
ANISOU 1140  CA AGLU A 141     4603   3810   3471   -191    243    254       C  
ATOM   1141  CA BGLU A 141     -12.832   5.304 -17.677  0.50 30.86           C  
ANISOU 1141  CA BGLU A 141     4544   3762   3420   -217    243    269       C  
ATOM   1142  C   GLU A 141     -13.924   6.181 -18.291  1.00 31.51           C  
ANISOU 1142  C   GLU A 141     4601   3849   3522   -190    242    157       C  
ATOM   1143  O   GLU A 141     -13.597   7.092 -19.097  1.00 33.83           O  
ANISOU 1143  O   GLU A 141     5122   3705   4026   -165    339    383       O  
ATOM   1144  CB AGLU A 141     -12.708   3.934 -18.569  0.50 32.17           C  
ANISOU 1144  CB AGLU A 141     4699   4070   3451   -171    317    146       C  
ATOM   1145  CB BGLU A 141     -12.448   4.124 -18.579  0.50 31.15           C  
ANISOU 1145  CB BGLU A 141     4553   3996   3287   -240    322    188       C  
ATOM   1146  CG AGLU A 141     -12.592   4.048 -20.124  0.50 36.17           C  
ANISOU 1146  CG AGLU A 141     5338   4554   3848   -145    169    321       C  
ATOM   1147  CG BGLU A 141     -12.429   4.435 -20.095  0.50 34.01           C  
ANISOU 1147  CG BGLU A 141     5045   4338   3540   -214     57    470       C  
ATOM   1148  CD AGLU A 141     -12.542   2.667 -20.820  0.50 40.86           C  
ANISOU 1148  CD AGLU A 141     6054   4911   4558     60    279    101       C  
ATOM   1149  CD BGLU A 141     -11.201   5.200 -20.537  0.50 36.17           C  
ANISOU 1149  CD BGLU A 141     5186   4707   3849   -394    -27    419       C  
ATOM   1150  OE1AGLU A 141     -12.367   1.637 -20.120  0.50 42.92           O  
ANISOU 1150  OE1AGLU A 141     6557   5064   4687   -138    513    211       O  
ATOM   1151  OE1BGLU A 141     -10.168   5.122 -19.844  0.50 37.78           O  
ANISOU 1151  OE1BGLU A 141     5664   5061   3627   -315   -109    834       O  
ATOM   1152  OE2AGLU A 141     -12.690   2.600 -22.067  0.50 41.76           O  
ANISOU 1152  OE2AGLU A 141     6104   5042   4721   -131    573    236       O  
ATOM   1153  OE2BGLU A 141     -11.255   5.860 -21.608  0.50 39.49           O  
ANISOU 1153  OE2BGLU A 141     6037   4935   4031   -447    129    432       O  
ATOM   1154  N   GLY A 142     -15.188   5.955 -17.921  1.00 30.86           N  
ANISOU 1154  N   GLY A 142     4641   3740   3342   -187    219     60       N  
ATOM   1155  CA  GLY A 142     -16.361   6.684 -18.444  1.00 32.38           C  
ANISOU 1155  CA  GLY A 142     4749   4037   3514   -243    133    -11       C  
ATOM   1156  C   GLY A 142     -17.024   6.045 -19.663  1.00 33.80           C  
ANISOU 1156  C   GLY A 142     4879   4105   3855   -232    -72    -51       C  
ATOM   1157  O   GLY A 142     -17.392   6.726 -20.601  1.00 32.49           O  
ANISOU 1157  O   GLY A 142     4900   3892   3549   -285    -65    -70       O  
ATOM   1158  N   ASN A 143     -17.140   4.722 -19.665  1.00 34.80           N  
ANISOU 1158  N   ASN A 143     5108   4270   3842   -302    -67   -195       N  
ATOM   1159  CA  ASN A 143     -17.604   3.979 -20.849  1.00 37.00           C  
ANISOU 1159  CA  ASN A 143     5227   4623   4207   -295   -111   -165       C  
ATOM   1160  C   ASN A 143     -18.206   2.710 -20.318  1.00 36.38           C  
ANISOU 1160  C   ASN A 143     5228   4564   4029   -286   -168   -225       C  
ATOM   1161  O   ASN A 143     -17.472   1.786 -19.957  1.00 37.80           O  
ANISOU 1161  O   ASN A 143     5517   4487   4356   -171   -113   -275       O  
ATOM   1162  CB  ASN A 143     -16.446   3.665 -21.838  1.00 37.86           C  
ANISOU 1162  CB  ASN A 143     5491   4824   4068   -280    -26   -284       C  
ATOM   1163  CG  ASN A 143     -16.879   2.749 -22.975  1.00 42.64           C  
ANISOU 1163  CG  ASN A 143     5777   5717   4707   -610     71   -576       C  
ATOM   1164  OD1 ASN A 143     -17.990   2.241 -22.972  1.00 44.99           O  
ANISOU 1164  OD1 ASN A 143     6116   6531   4447   -894      5  -1202       O  
ATOM   1165  ND2 ASN A 143     -15.998   2.556 -23.976  1.00 50.41           N  
ANISOU 1165  ND2 ASN A 143     6872   6997   5285   -629    163  -1091       N  
ATOM   1166  N   THR A 144     -19.521   2.712 -20.222  1.00 36.55           N  
ANISOU 1166  N   THR A 144     5188   4740   3957   -303   -155   -141       N  
ATOM   1167  CA  THR A 144     -20.247   1.518 -19.774  1.00 38.40           C  
ANISOU 1167  CA  THR A 144     5237   4963   4388   -246   -156    -69       C  
ATOM   1168  C   THR A 144     -20.960   0.799 -20.938  1.00 41.43           C  
ANISOU 1168  C   THR A 144     5547   5453   4741   -155   -174   -133       C  
ATOM   1169  O   THR A 144     -22.069   1.180 -21.356  1.00 41.05           O  
ANISOU 1169  O   THR A 144     5317   5753   4527   -138   -129    -10       O  
ATOM   1170  CB  THR A 144     -21.161   1.886 -18.609  1.00 37.90           C  
ANISOU 1170  CB  THR A 144     5195   4848   4356   -265   -161      9       C  
ATOM   1171  OG1 THR A 144     -20.320   2.380 -17.569  1.00 33.33           O  
ANISOU 1171  OG1 THR A 144     4866   3873   3924    -48   -103    220       O  
ATOM   1172  CG2 THR A 144     -22.009   0.663 -18.121  1.00 38.47           C  
ANISOU 1172  CG2 THR A 144     5277   5002   4338   -332    -28    267       C  
ATOM   1173  N   GLN A 145     -20.281  -0.261 -21.403  1.00 44.39           N  
ANISOU 1173  N   GLN A 145     5986   5678   5202   -176   -202   -175       N  
ATOM   1174  CA  GLN A 145     -20.698  -1.079 -22.579  1.00 47.03           C  
ANISOU 1174  CA  GLN A 145     6327   5943   5598   -191   -174   -131       C  
ATOM   1175  C   GLN A 145     -21.003  -0.183 -23.786  1.00 47.61           C  
ANISOU 1175  C   GLN A 145     6370   6091   5628   -206   -220    -94       C  
ATOM   1176  O   GLN A 145     -22.045  -0.333 -24.427  1.00 49.73           O  
ANISOU 1176  O   GLN A 145     6478   6443   5973   -233   -220     27       O  
ATOM   1177  CB  GLN A 145     -21.891  -1.997 -22.228  1.00 47.28           C  
ANISOU 1177  CB  GLN A 145     6323   5890   5751   -223   -182   -222       C  
ATOM   1178  CG  GLN A 145     -21.588  -3.098 -21.159  1.00 51.07           C  
ANISOU 1178  CG  GLN A 145     6970   6382   6053   -317   -164     54       C  
ATOM   1179  CD  GLN A 145     -22.864  -3.792 -20.669  1.00 56.34           C  
ANISOU 1179  CD  GLN A 145     7683   6881   6841   -535   -264    123       C  
ATOM   1180  OE1 GLN A 145     -23.975  -3.540 -21.197  1.00 60.35           O  
ANISOU 1180  OE1 GLN A 145     8111   7578   7241   -636   -544    341       O  
ATOM   1181  NE2 GLN A 145     -22.724  -4.661 -19.643  1.00 56.00           N  
ANISOU 1181  NE2 GLN A 145     8145   6899   6233   -462   -673   -105       N  
ATOM   1182  N   GLY A 146     -20.103   0.763 -24.073  1.00 47.45           N  
ANISOU 1182  N   GLY A 146     6502   6012   5515   -185   -166    -56       N  
ATOM   1183  CA  GLY A 146     -20.282   1.676 -25.222  1.00 46.58           C  
ANISOU 1183  CA  GLY A 146     6356   5940   5401   -117   -250   -109       C  
ATOM   1184  C   GLY A 146     -21.066   2.977 -25.088  1.00 45.24           C  
ANISOU 1184  C   GLY A 146     6087   5860   5241    -83   -231    -87       C  
ATOM   1185  O   GLY A 146     -21.164   3.737 -26.063  1.00 43.91           O  
ANISOU 1185  O   GLY A 146     6057   5673   4952   -194   -231   -158       O  
ATOM   1186  N   VAL A 147     -21.638   3.253 -23.905  1.00 43.32           N  
ANISOU 1186  N   VAL A 147     5731   5715   5013   -105   -358    -69       N  
ATOM   1187  CA  VAL A 147     -22.164   4.570 -23.659  1.00 41.74           C  
ANISOU 1187  CA  VAL A 147     5415   5619   4826   -133   -398    -59       C  
ATOM   1188  C   VAL A 147     -21.116   5.348 -22.865  1.00 41.32           C  
ANISOU 1188  C   VAL A 147     5410   5351   4937   -147   -385   -103       C  
ATOM   1189  O   VAL A 147     -20.592   4.833 -21.880  1.00 39.47           O  
ANISOU 1189  O   VAL A 147     5230   4961   4807   -128   -546   -149       O  
ATOM   1190  CB  VAL A 147     -23.512   4.535 -22.942  1.00 42.35           C  
ANISOU 1190  CB  VAL A 147     5489   5784   4816   -151   -402    -87       C  
ATOM   1191  CG1 VAL A 147     -24.039   5.953 -22.771  1.00 40.84           C  
ANISOU 1191  CG1 VAL A 147     5600   5691   4222    100   -289     45       C  
ATOM   1192  CG2 VAL A 147     -24.525   3.612 -23.736  1.00 43.67           C  
ANISOU 1192  CG2 VAL A 147     5477   6201   4911   -256   -305   -134       C  
ATOM   1193  N   THR A 148     -20.788   6.555 -23.318  1.00 40.61           N  
ANISOU 1193  N   THR A 148     5257   5194   4976   -137   -475   -155       N  
ATOM   1194  CA  THR A 148     -19.709   7.282 -22.680  1.00 40.66           C  
ANISOU 1194  CA  THR A 148     5454   5060   4933   -136   -442   -199       C  
ATOM   1195  C   THR A 148     -20.217   8.516 -21.941  1.00 38.22           C  
ANISOU 1195  C   THR A 148     5137   4762   4622    -27   -481   -153       C  
ATOM   1196  O   THR A 148     -21.344   9.001 -22.154  1.00 38.47           O  
ANISOU 1196  O   THR A 148     5419   4945   4253     62   -732   -430       O  
ATOM   1197  CB  THR A 148     -18.519   7.575 -23.642  1.00 41.77           C  
ANISOU 1197  CB  THR A 148     5482   5176   5211   -147   -499    -89       C  
ATOM   1198  OG1 THR A 148     -19.020   8.195 -24.799  1.00 44.82           O  
ANISOU 1198  OG1 THR A 148     6537   5282   5210   -581   -787    169       O  
ATOM   1199  CG2 THR A 148     -17.864   6.316 -24.136  1.00 43.96           C  
ANISOU 1199  CG2 THR A 148     5591   5517   5593   -286   -432   -505       C  
ATOM   1200  N   TYR A 149     -19.409   8.964 -20.989  1.00 34.92           N  
ANISOU 1200  N   TYR A 149     4994   4184   4091      1   -352     80       N  
ATOM   1201  CA  TYR A 149     -19.825  10.043 -20.084  1.00 31.66           C  
ANISOU 1201  CA  TYR A 149     4440   3898   3691    -40   -215    192       C  
ATOM   1202  C   TYR A 149     -18.550  10.522 -19.384  1.00 30.48           C  
ANISOU 1202  C   TYR A 149     4301   3790   3490    -52   -174    219       C  
ATOM   1203  O   TYR A 149     -17.461   9.895 -19.493  1.00 29.28           O  
ANISOU 1203  O   TYR A 149     4165   3783   3174   -148   -133     58       O  
ATOM   1204  CB  TYR A 149     -20.898   9.568 -19.078  1.00 31.25           C  
ANISOU 1204  CB  TYR A 149     4474   3638   3758    -66   -150    336       C  
ATOM   1205  CG  TYR A 149     -20.488   8.247 -18.380  1.00 31.48           C  
ANISOU 1205  CG  TYR A 149     4629   3677   3652   -206   -227    425       C  
ATOM   1206  CD1 TYR A 149     -19.786   8.252 -17.156  1.00 29.98           C  
ANISOU 1206  CD1 TYR A 149     4327   3595   3466    -66     78    434       C  
ATOM   1207  CD2 TYR A 149     -20.780   7.012 -18.974  1.00 30.36           C  
ANISOU 1207  CD2 TYR A 149     4876   3384   3272     36    167    446       C  
ATOM   1208  CE1 TYR A 149     -19.366   7.089 -16.585  1.00 30.71           C  
ANISOU 1208  CE1 TYR A 149     4585   3886   3197   -161   -530    671       C  
ATOM   1209  CE2 TYR A 149     -20.395   5.827 -18.379  1.00 29.84           C  
ANISOU 1209  CE2 TYR A 149     4458   3257   3620   -202   -379    489       C  
ATOM   1210  CZ  TYR A 149     -19.687   5.864 -17.184  1.00 31.67           C  
ANISOU 1210  CZ  TYR A 149     4640   3899   3494    -41   -252    441       C  
ATOM   1211  OH  TYR A 149     -19.308   4.670 -16.640  1.00 34.29           O  
ANISOU 1211  OH  TYR A 149     4908   3896   4222   -174   -588    910       O  
ATOM   1212  N   ASN A 150     -18.659  11.615 -18.643  1.00 28.33           N  
ANISOU 1212  N   ASN A 150     4055   3377   3332    -90   -172    337       N  
ATOM   1213  CA  ASN A 150     -17.449  12.156 -18.010  1.00 27.46           C  
ANISOU 1213  CA  ASN A 150     3848   3442   3140    -33   -109    282       C  
ATOM   1214  C   ASN A 150     -17.324  11.442 -16.630  1.00 26.82           C  
ANISOU 1214  C   ASN A 150     3628   3382   3179   -104    -50    382       C  
ATOM   1215  O   ASN A 150     -18.168  11.674 -15.782  1.00 26.13           O  
ANISOU 1215  O   ASN A 150     3680   3210   3037    -56   -107    207       O  
ATOM   1216  CB  ASN A 150     -17.643  13.662 -17.792  1.00 27.11           C  
ANISOU 1216  CB  ASN A 150     3885   3196   3217   -221     10    390       C  
ATOM   1217  CG  ASN A 150     -16.497  14.305 -16.988  1.00 26.86           C  
ANISOU 1217  CG  ASN A 150     3836   3558   2811    -94     21    255       C  
ATOM   1218  OD1 ASN A 150     -15.570  13.620 -16.518  1.00 29.62           O  
ANISOU 1218  OD1 ASN A 150     3832   3611   3809   -140    735     69       O  
ATOM   1219  ND2 ASN A 150     -16.501  15.645 -16.926  1.00 27.43           N  
ANISOU 1219  ND2 ASN A 150     4166   3355   2899    359     -6    -43       N  
ATOM   1220  N   PRO A 151     -16.278  10.617 -16.413  1.00 27.73           N  
ANISOU 1220  N   PRO A 151     3809   3463   3263    -82     -5    333       N  
ATOM   1221  CA  PRO A 151     -16.231   9.912 -15.117  1.00 28.04           C  
ANISOU 1221  CA  PRO A 151     3829   3442   3380    -98    -56    290       C  
ATOM   1222  C   PRO A 151     -15.998  10.891 -13.958  1.00 28.58           C  
ANISOU 1222  C   PRO A 151     3907   3556   3394   -205    -16    263       C  
ATOM   1223  O   PRO A 151     -16.270  10.543 -12.789  1.00 27.29           O  
ANISOU 1223  O   PRO A 151     4116   3205   3047   -467    178    168       O  
ATOM   1224  CB  PRO A 151     -15.062   8.951 -15.309  1.00 28.05           C  
ANISOU 1224  CB  PRO A 151     3537   3464   3654   -253   -119    334       C  
ATOM   1225  CG  PRO A 151     -14.148   9.669 -16.259  1.00 29.67           C  
ANISOU 1225  CG  PRO A 151     3788   3916   3570    138     30    357       C  
ATOM   1226  CD  PRO A 151     -15.051  10.398 -17.200  1.00 28.45           C  
ANISOU 1226  CD  PRO A 151     3720   3628   3459     38    -50    323       C  
ATOM   1227  N   ASP A 152     -15.436  12.082 -14.248  1.00 28.39           N  
ANISOU 1227  N   ASP A 152     4182   3264   3339   -179   -104    257       N  
ATOM   1228  CA  ASP A 152     -15.218  13.112 -13.195  1.00 28.77           C  
ANISOU 1228  CA  ASP A 152     4007   3406   3516   -222   -148    344       C  
ATOM   1229  C   ASP A 152     -16.460  13.891 -12.852  1.00 27.95           C  
ANISOU 1229  C   ASP A 152     4011   3196   3412   -315    -97    363       C  
ATOM   1230  O   ASP A 152     -16.487  14.643 -11.853  1.00 28.68           O  
ANISOU 1230  O   ASP A 152     4125   3337   3433   -261   -131    435       O  
ATOM   1231  CB  ASP A 152     -14.181  14.121 -13.669  1.00 31.10           C  
ANISOU 1231  CB  ASP A 152     4138   3781   3895   -263   -141    276       C  
ATOM   1232  CG  ASP A 152     -12.833  13.490 -13.977  1.00 31.86           C  
ANISOU 1232  CG  ASP A 152     4139   3876   4089   -221   -190    387       C  
ATOM   1233  OD1 ASP A 152     -12.473  12.431 -13.438  1.00 38.03           O  
ANISOU 1233  OD1 ASP A 152     5010   4262   5174   -320   -316    879       O  
ATOM   1234  OD2 ASP A 152     -12.105  14.066 -14.762  1.00 34.58           O  
ANISOU 1234  OD2 ASP A 152     4648   4338   4149   -284     18    643       O  
ATOM   1235  N   HIS A 153     -17.504  13.743 -13.652  1.00 26.64           N  
ANISOU 1235  N   HIS A 153     3891   2991   3239   -206   -202    461       N  
ATOM   1236  CA  HIS A 153     -18.745  14.489 -13.410  1.00 27.36           C  
ANISOU 1236  CA  HIS A 153     3817   3103   3475   -235   -221    341       C  
ATOM   1237  C   HIS A 153     -19.886  13.672 -13.973  1.00 27.27           C  
ANISOU 1237  C   HIS A 153     3783   3182   3394   -129   -192    317       C  
ATOM   1238  O   HIS A 153     -20.431  13.994 -15.025  1.00 28.12           O  
ANISOU 1238  O   HIS A 153     4121   3193   3367   -397   -179    443       O  
ATOM   1239  CB  HIS A 153     -18.637  15.916 -14.048  1.00 27.37           C  
ANISOU 1239  CB  HIS A 153     3902   3036   3461    -52   -238    414       C  
ATOM   1240  CG  HIS A 153     -19.841  16.787 -13.836  1.00 30.03           C  
ANISOU 1240  CG  HIS A 153     3720   3703   3986    -27   -240    170       C  
ATOM   1241  ND1 HIS A 153     -20.374  17.017 -12.595  1.00 34.44           N  
ANISOU 1241  ND1 HIS A 153     4546   4047   4492    349    282    762       N  
ATOM   1242  CD2 HIS A 153     -20.562  17.559 -14.708  1.00 34.38           C  
ANISOU 1242  CD2 HIS A 153     3885   4087   5089    183    -90     54       C  
ATOM   1243  CE1 HIS A 153     -21.425  17.820 -12.710  1.00 37.66           C  
ANISOU 1243  CE1 HIS A 153     4524   4806   4976    444    135    380       C  
ATOM   1244  NE2 HIS A 153     -21.537  18.193 -13.974  1.00 36.20           N  
ANISOU 1244  NE2 HIS A 153     4261   4567   4923    568   -274    -51       N  
ATOM   1245  N   ILE A 154     -20.241  12.594 -13.282  1.00 25.59           N  
ANISOU 1245  N   ILE A 154     3505   3032   3184   -175   -179    167       N  
ATOM   1246  CA  ILE A 154     -21.174  11.672 -13.833  1.00 25.91           C  
ANISOU 1246  CA  ILE A 154     3505   3260   3077   -142   -255    182       C  
ATOM   1247  C   ILE A 154     -22.561  12.367 -13.899  1.00 26.50           C  
ANISOU 1247  C   ILE A 154     3608   3232   3228     13   -361    107       C  
ATOM   1248  O   ILE A 154     -22.994  13.054 -12.928  1.00 26.90           O  
ANISOU 1248  O   ILE A 154     3838   3465   2918    -80   -646    182       O  
ATOM   1249  CB  ILE A 154     -21.180  10.328 -13.017  1.00 25.12           C  
ANISOU 1249  CB  ILE A 154     3425   3125   2992   -150   -297     85       C  
ATOM   1250  CG1 ILE A 154     -19.923   9.479 -13.392  1.00 23.16           C  
ANISOU 1250  CG1 ILE A 154     2970   2901   2926     90    -39    497       C  
ATOM   1251  CG2 ILE A 154     -22.519   9.579 -13.165  1.00 25.67           C  
ANISOU 1251  CG2 ILE A 154     2899   3696   3157      6   -330    451       C  
ATOM   1252  CD1 ILE A 154     -19.560   8.393 -12.359  1.00 25.17           C  
ANISOU 1252  CD1 ILE A 154     2800   3426   3337   -247   -464    715       C  
ATOM   1253  N   PRO A 155     -23.304  12.174 -15.018  1.00 28.76           N  
ANISOU 1253  N   PRO A 155     4011   3556   3359     75   -365    -72       N  
ATOM   1254  CA  PRO A 155     -24.616  12.826 -15.179  1.00 28.64           C  
ANISOU 1254  CA  PRO A 155     3828   3663   3390     64   -495   -110       C  
ATOM   1255  C   PRO A 155     -25.640  12.311 -14.191  1.00 29.06           C  
ANISOU 1255  C   PRO A 155     3941   3769   3329     44   -571   -256       C  
ATOM   1256  O   PRO A 155     -25.418  11.237 -13.596  1.00 28.92           O  
ANISOU 1256  O   PRO A 155     3664   3614   3707    -49   -539   -119       O  
ATOM   1257  CB  PRO A 155     -25.013  12.417 -16.640  1.00 28.75           C  
ANISOU 1257  CB  PRO A 155     4126   3469   3327    199   -518   -409       C  
ATOM   1258  CG  PRO A 155     -24.242  11.242 -16.921  1.00 32.03           C  
ANISOU 1258  CG  PRO A 155     4107   4247   3813    246   -432   -232       C  
ATOM   1259  CD  PRO A 155     -22.939  11.442 -16.241  1.00 29.93           C  
ANISOU 1259  CD  PRO A 155     4058   3772   3540     74   -369   -118       C  
ATOM   1260  N   ASP A 156     -26.748  13.024 -13.974  1.00 29.29           N  
ANISOU 1260  N   ASP A 156     3846   3792   3489      6   -558   -188       N  
ATOM   1261  CA  ASP A 156     -27.739  12.515 -13.015  1.00 30.40           C  
ANISOU 1261  CA  ASP A 156     3964   3907   3678    -98   -505    -74       C  
ATOM   1262  C   ASP A 156     -28.309  11.157 -13.474  1.00 31.19           C  
ANISOU 1262  C   ASP A 156     4096   3836   3917    -42   -307    -28       C  
ATOM   1263  O   ASP A 156     -28.626  10.292 -12.641  1.00 30.63           O  
ANISOU 1263  O   ASP A 156     3962   3701   3973   -210   -313     83       O  
ATOM   1264  CB  ASP A 156     -28.929  13.454 -12.856  1.00 31.76           C  
ANISOU 1264  CB  ASP A 156     4130   4112   3822     54   -568   -264       C  
ATOM   1265  CG  ASP A 156     -28.589  14.781 -12.198  1.00 35.66           C  
ANISOU 1265  CG  ASP A 156     4634   4415   4498     36   -427     92       C  
ATOM   1266  OD1 ASP A 156     -27.430  15.030 -11.768  1.00 37.83           O  
ANISOU 1266  OD1 ASP A 156     4837   4994   4543    118   -745   -221       O  
ATOM   1267  OD2 ASP A 156     -29.539  15.590 -12.081  1.00 39.96           O  
ANISOU 1267  OD2 ASP A 156     4891   5800   4491    657   -507     10       O  
ATOM   1268  N   ARG A 157     -28.456  10.999 -14.787  1.00 31.04           N  
ANISOU 1268  N   ARG A 157     4127   3808   3856   -136   -529    -20       N  
ATOM   1269  CA  ARG A 157     -28.982   9.754 -15.358  1.00 33.03           C  
ANISOU 1269  CA  ARG A 157     4313   4057   4178   -163   -367    -34       C  
ATOM   1270  C   ARG A 157     -28.366   9.574 -16.719  1.00 33.33           C  
ANISOU 1270  C   ARG A 157     4559   4158   3946   -267   -498      7       C  
ATOM   1271  O   ARG A 157     -27.843  10.568 -17.341  1.00 31.98           O  
ANISOU 1271  O   ARG A 157     4529   3939   3680   -485   -872    111       O  
ATOM   1272  CB  ARG A 157     -30.528   9.724 -15.395  1.00 33.70           C  
ANISOU 1272  CB  ARG A 157     4260   4075   4467   -145   -369    -70       C  
ATOM   1273  CG  ARG A 157     -31.158  10.784 -16.312  1.00 38.16           C  
ANISOU 1273  CG  ARG A 157     4727   4610   5163    -44   -435    -97       C  
ATOM   1274  CD  ARG A 157     -32.676  11.056 -16.040  1.00 42.05           C  
ANISOU 1274  CD  ARG A 157     4917   5391   5669    116    -95   -658       C  
ATOM   1275  NE  ARG A 157     -33.040  11.094 -14.633  1.00 47.57           N  
ANISOU 1275  NE  ARG A 157     6249   5750   6072    123    157   -233       N  
ATOM   1276  CZ  ARG A 157     -32.770  12.101 -13.780  1.00 50.29           C  
ANISOU 1276  CZ  ARG A 157     6670   6094   6342    107    302   -348       C  
ATOM   1277  NH1 ARG A 157     -32.087  13.198 -14.179  1.00 50.42           N  
ANISOU 1277  NH1 ARG A 157     6791   5529   6836    252    200   -416       N  
ATOM   1278  NH2 ARG A 157     -33.165  12.008 -12.502  1.00 49.18           N  
ANISOU 1278  NH2 ARG A 157     6514   6320   5850    566    354   -646       N  
ATOM   1279  N   LEU A 158     -28.327   8.313 -17.172  1.00 32.28           N  
ANISOU 1279  N   LEU A 158     4514   3964   3784   -336   -506     91       N  
ATOM   1280  CA  LEU A 158     -27.604   8.014 -18.409  1.00 34.48           C  
ANISOU 1280  CA  LEU A 158     4667   4381   4053   -269   -405   -122       C  
ATOM   1281  C   LEU A 158     -28.526   7.138 -19.264  1.00 35.51           C  
ANISOU 1281  C   LEU A 158     5037   4497   3956   -279   -412   -104       C  
ATOM   1282  O   LEU A 158     -28.653   5.959 -18.987  1.00 33.98           O  
ANISOU 1282  O   LEU A 158     4846   4638   3427   -627   -429    -54       O  
ATOM   1283  CB  LEU A 158     -26.264   7.306 -18.079  1.00 36.22           C  
ANISOU 1283  CB  LEU A 158     4942   4545   4274   -323   -282   -179       C  
ATOM   1284  CG  LEU A 158     -25.346   6.967 -19.267  1.00 37.22           C  
ANISOU 1284  CG  LEU A 158     4864   4889   4388   -307   -166     26       C  
ATOM   1285  CD1 LEU A 158     -24.554   8.212 -19.718  1.00 37.67           C  
ANISOU 1285  CD1 LEU A 158     4838   4956   4515   -991   -684   -440       C  
ATOM   1286  CD2 LEU A 158     -24.389   5.761 -19.058  1.00 40.12           C  
ANISOU 1286  CD2 LEU A 158     5557   5125   4559    -59   -253     42       C  
ATOM   1287  N   PRO A 159     -29.175   7.722 -20.304  1.00 37.28           N  
ANISOU 1287  N   PRO A 159     5127   4726   4310   -205   -462    -76       N  
ATOM   1288  CA  PRO A 159     -29.832   6.818 -21.294  1.00 37.82           C  
ANISOU 1288  CA  PRO A 159     5229   4872   4266   -110   -449    -87       C  
ATOM   1289  C   PRO A 159     -28.916   5.699 -21.806  1.00 37.65           C  
ANISOU 1289  C   PRO A 159     5208   4975   4120   -131   -480    -66       C  
ATOM   1290  O   PRO A 159     -27.780   5.933 -22.196  1.00 35.74           O  
ANISOU 1290  O   PRO A 159     4986   4788   3806   -151   -561   -321       O  
ATOM   1291  CB  PRO A 159     -30.244   7.751 -22.443  1.00 38.96           C  
ANISOU 1291  CB  PRO A 159     5390   4958   4454   -116   -446    -61       C  
ATOM   1292  CG  PRO A 159     -29.473   9.058 -22.223  1.00 39.58           C  
ANISOU 1292  CG  PRO A 159     5459   5021   4557   -169   -405     -6       C  
ATOM   1293  CD  PRO A 159     -29.179   9.142 -20.733  1.00 38.31           C  
ANISOU 1293  CD  PRO A 159     5433   4816   4306    -98   -535    -93       C  
ATOM   1294  N   PHE A 160     -29.461   4.494 -21.831  1.00 38.02           N  
ANISOU 1294  N   PHE A 160     5317   4927   4201   -152   -426     13       N  
ATOM   1295  CA  PHE A 160     -28.713   3.271 -21.990  1.00 41.10           C  
ANISOU 1295  CA  PHE A 160     5564   5300   4752   -111   -300    -43       C  
ATOM   1296  C   PHE A 160     -29.675   2.362 -22.795  1.00 40.60           C  
ANISOU 1296  C   PHE A 160     5514   5140   4772   -107   -164   -220       C  
ATOM   1297  O   PHE A 160     -30.624   1.806 -22.202  1.00 40.93           O  
ANISOU 1297  O   PHE A 160     5891   4952   4708    -32     -4   -356       O  
ATOM   1298  CB  PHE A 160     -28.409   2.635 -20.554  1.00 41.96           C  
ANISOU 1298  CB  PHE A 160     5633   5459   4849   -112   -304      5       C  
ATOM   1299  CG  PHE A 160     -27.376   1.567 -20.597  1.00 45.87           C  
ANISOU 1299  CG  PHE A 160     6115   5892   5419      3   -417    480       C  
ATOM   1300  CD1 PHE A 160     -26.009   1.903 -20.532  1.00 47.32           C  
ANISOU 1300  CD1 PHE A 160     6463   6643   4871    -52  -1271    646       C  
ATOM   1301  CD2 PHE A 160     -27.726   0.240 -20.839  1.00 51.79           C  
ANISOU 1301  CD2 PHE A 160     6970   6253   6454     42   -586    308       C  
ATOM   1302  CE1 PHE A 160     -24.975   0.894 -20.668  1.00 49.47           C  
ANISOU 1302  CE1 PHE A 160     6804   6743   5249   -156  -1087    618       C  
ATOM   1303  CE2 PHE A 160     -26.704  -0.766 -20.948  1.00 54.44           C  
ANISOU 1303  CE2 PHE A 160     7131   6721   6831      2   -781    486       C  
ATOM   1304  CZ  PHE A 160     -25.327  -0.432 -20.853  1.00 51.71           C  
ANISOU 1304  CZ  PHE A 160     7081   6546   6020    -66   -889    602       C  
ATOM   1305  N   LYS A 161     -29.482   2.230 -24.119  1.00 40.04           N  
ANISOU 1305  N   LYS A 161     5371   5097   4743    -80   -228    -85       N  
ATOM   1306  CA  LYS A 161     -30.424   1.428 -24.959  1.00 38.10           C  
ANISOU 1306  CA  LYS A 161     4864   4966   4646     85   -221    -99       C  
ATOM   1307  C   LYS A 161     -31.907   1.810 -24.712  1.00 36.71           C  
ANISOU 1307  C   LYS A 161     4731   4736   4481    -26   -341    -40       C  
ATOM   1308  O   LYS A 161     -32.286   2.955 -24.960  1.00 36.17           O  
ANISOU 1308  O   LYS A 161     4408   4757   4578     31   -339    101       O  
ATOM   1309  CB  LYS A 161     -30.180  -0.068 -24.774  1.00 40.15           C  
ANISOU 1309  CB  LYS A 161     5138   5255   4863    129   -246    -41       C  
ATOM   1310  CG  LYS A 161     -28.728  -0.520 -25.190  1.00 41.81           C  
ANISOU 1310  CG  LYS A 161     4895   5574   5414    287   -106    102       C  
ATOM   1311  CD  LYS A 161     -28.298  -1.802 -24.467  1.00 45.80           C  
ANISOU 1311  CD  LYS A 161     5123   5844   6432    239    -33    446       C  
ATOM   1312  CE  LYS A 161     -29.119  -3.041 -24.812  1.00 48.42           C  
ANISOU 1312  CE  LYS A 161     5395   6002   7001    128    359    667       C  
ATOM   1313  NZ  LYS A 161     -29.895  -3.475 -23.580  1.00 48.59           N  
ANISOU 1313  NZ  LYS A 161     5736   5748   6977    -73    442    696       N  
ATOM   1314  N   ASP A 162     -32.711   0.896 -24.186  1.00 34.39           N  
ANISOU 1314  N   ASP A 162     4478   4520   4069     66   -414    -14       N  
ATOM   1315  CA  ASP A 162     -34.093   1.166 -23.869  1.00 33.60           C  
ANISOU 1315  CA  ASP A 162     4424   4351   3992    -29   -392     23       C  
ATOM   1316  C   ASP A 162     -34.298   1.674 -22.454  1.00 33.28           C  
ANISOU 1316  C   ASP A 162     4367   4320   3956     -5   -408    -23       C  
ATOM   1317  O   ASP A 162     -35.470   1.949 -22.030  1.00 34.19           O  
ANISOU 1317  O   ASP A 162     4618   4626   3747     91   -508   -118       O  
ATOM   1318  CB  ASP A 162     -34.998  -0.091 -24.144  1.00 33.40           C  
ANISOU 1318  CB  ASP A 162     4495   4222   3973     26   -529    -80       C  
ATOM   1319  CG  ASP A 162     -35.152  -0.394 -25.653  1.00 33.72           C  
ANISOU 1319  CG  ASP A 162     4552   4139   4121    -90   -481     58       C  
ATOM   1320  OD1 ASP A 162     -35.178   0.575 -26.461  1.00 32.78           O  
ANISOU 1320  OD1 ASP A 162     4180   4037   4238    122  -1015    497       O  
ATOM   1321  OD2 ASP A 162     -35.261  -1.626 -26.011  1.00 32.11           O  
ANISOU 1321  OD2 ASP A 162     3765   4018   4418   -140   -330    103       O  
ATOM   1322  N   LEU A 163     -33.196   1.772 -21.699  1.00 32.67           N  
ANISOU 1322  N   LEU A 163     4348   4239   3824     73   -442     47       N  
ATOM   1323  CA  LEU A 163     -33.312   2.005 -20.262  1.00 31.33           C  
ANISOU 1323  CA  LEU A 163     4153   4012   3738     90   -256    -64       C  
ATOM   1324  C   LEU A 163     -32.635   3.315 -19.869  1.00 31.27           C  
ANISOU 1324  C   LEU A 163     4033   4132   3713    126   -285     70       C  
ATOM   1325  O   LEU A 163     -32.052   4.026 -20.696  1.00 31.44           O  
ANISOU 1325  O   LEU A 163     3931   4390   3625    -48   -230     79       O  
ATOM   1326  CB  LEU A 163     -32.692   0.811 -19.461  1.00 31.65           C  
ANISOU 1326  CB  LEU A 163     4332   3881   3810     93   -228    -48       C  
ATOM   1327  CG  LEU A 163     -33.330  -0.594 -19.661  1.00 31.68           C  
ANISOU 1327  CG  LEU A 163     4238   3849   3950    119   -185   -212       C  
ATOM   1328  CD1 LEU A 163     -32.353  -1.779 -19.196  1.00 31.23           C  
ANISOU 1328  CD1 LEU A 163     4668   3674   3522    126   -785   -371       C  
ATOM   1329  CD2 LEU A 163     -34.717  -0.713 -19.044  1.00 32.13           C  
ANISOU 1329  CD2 LEU A 163     4168   3834   4203   -297   -525   -355       C  
ATOM   1330  N   THR A 164     -32.750   3.644 -18.585  1.00 29.05           N  
ANISOU 1330  N   THR A 164     3834   3911   3291    130   -337    -83       N  
ATOM   1331  CA  THR A 164     -32.081   4.813 -18.046  1.00 29.20           C  
ANISOU 1331  CA  THR A 164     4072   3704   3316     79   -508    118       C  
ATOM   1332  C   THR A 164     -31.260   4.310 -16.847  1.00 28.06           C  
ANISOU 1332  C   THR A 164     3865   3574   3218     98   -406    166       C  
ATOM   1333  O   THR A 164     -31.845   3.860 -15.879  1.00 28.22           O  
ANISOU 1333  O   THR A 164     4084   3499   3137     69   -388     41       O  
ATOM   1334  CB  THR A 164     -33.080   5.857 -17.612  1.00 28.30           C  
ANISOU 1334  CB  THR A 164     4016   3641   3093      3   -639    103       C  
ATOM   1335  OG1 THR A 164     -33.778   6.309 -18.780  1.00 30.26           O  
ANISOU 1335  OG1 THR A 164     4483   3618   3397    383   -865    281       O  
ATOM   1336  CG2 THR A 164     -32.333   7.105 -17.054  1.00 28.46           C  
ANISOU 1336  CG2 THR A 164     4043   3409   3360   -225   -709   -329       C  
ATOM   1337  N   LEU A 165     -29.941   4.389 -16.952  1.00 27.22           N  
ANISOU 1337  N   LEU A 165     3821   3332   3189     25   -556    117       N  
ATOM   1338  CA  LEU A 165     -29.028   3.999 -15.874  1.00 26.73           C  
ANISOU 1338  CA  LEU A 165     3686   3482   2986     26   -460     49       C  
ATOM   1339  C   LEU A 165     -28.942   5.163 -14.882  1.00 26.85           C  
ANISOU 1339  C   LEU A 165     3812   3257   3133   -127   -401     34       C  
ATOM   1340  O   LEU A 165     -28.882   6.321 -15.313  1.00 27.47           O  
ANISOU 1340  O   LEU A 165     4011   3427   2999   -202   -539    156       O  
ATOM   1341  CB  LEU A 165     -27.621   3.682 -16.444  1.00 27.21           C  
ANISOU 1341  CB  LEU A 165     3738   3445   3155    132   -381    -44       C  
ATOM   1342  CG  LEU A 165     -26.647   2.991 -15.457  1.00 26.81           C  
ANISOU 1342  CG  LEU A 165     3523   3422   3242    -98   -708    -30       C  
ATOM   1343  CD1 LEU A 165     -27.139   1.672 -14.922  1.00 29.29           C  
ANISOU 1343  CD1 LEU A 165     4031   3408   3688   -267   -784    -39       C  
ATOM   1344  CD2 LEU A 165     -25.246   2.808 -16.124  1.00 32.17           C  
ANISOU 1344  CD2 LEU A 165     3863   4380   3979    206   -579    259       C  
ATOM   1345  N   GLY A 166     -29.037   4.893 -13.561  1.00 26.39           N  
ANISOU 1345  N   GLY A 166     3684   3434   2906   -125   -439   -305       N  
ATOM   1346  CA  GLY A 166     -28.776   5.991 -12.560  1.00 25.95           C  
ANISOU 1346  CA  GLY A 166     3558   3056   3242     18   -240   -245       C  
ATOM   1347  C   GLY A 166     -27.333   6.467 -12.515  1.00 26.01           C  
ANISOU 1347  C   GLY A 166     3691   3064   3128    -32   -183   -190       C  
ATOM   1348  O   GLY A 166     -26.400   5.668 -12.544  1.00 25.50           O  
ANISOU 1348  O   GLY A 166     3562   3074   3051     -3   -439   -436       O  
ATOM   1349  N   GLY A 167     -27.149   7.785 -12.399  1.00 25.38           N  
ANISOU 1349  N   GLY A 167     3704   2887   3053   -175   -215     12       N  
ATOM   1350  CA  GLY A 167     -25.860   8.356 -12.111  1.00 25.38           C  
ANISOU 1350  CA  GLY A 167     3528   2969   3143    -32   -339    172       C  
ATOM   1351  C   GLY A 167     -25.306   7.779 -10.816  1.00 25.47           C  
ANISOU 1351  C   GLY A 167     3575   3137   2964   -107   -371    -32       C  
ATOM   1352  O   GLY A 167     -24.123   7.536 -10.738  1.00 26.15           O  
ANISOU 1352  O   GLY A 167     3862   3148   2925    -21   -424    138       O  
ATOM   1353  N   PHE A 168     -26.164   7.443  -9.860  1.00 25.57           N  
ANISOU 1353  N   PHE A 168     3675   3071   2966     25   -460    -92       N  
ATOM   1354  CA  PHE A 168     -25.636   6.942  -8.581  1.00 25.81           C  
ANISOU 1354  CA  PHE A 168     3713   2964   3129    233   -386    -63       C  
ATOM   1355  C   PHE A 168     -25.063   5.502  -8.746  1.00 25.34           C  
ANISOU 1355  C   PHE A 168     3571   2881   3175    121   -366   -142       C  
ATOM   1356  O   PHE A 168     -24.038   5.179  -8.133  1.00 23.83           O  
ANISOU 1356  O   PHE A 168     3479   2662   2913     -1   -426     18       O  
ATOM   1357  CB  PHE A 168     -26.673   6.977  -7.503  1.00 25.31           C  
ANISOU 1357  CB  PHE A 168     3467   3119   3027    308   -431    -82       C  
ATOM   1358  CG  PHE A 168     -26.108   6.817  -6.082  1.00 25.83           C  
ANISOU 1358  CG  PHE A 168     3833   2965   3013    381   -226   -144       C  
ATOM   1359  CD1 PHE A 168     -25.004   7.572  -5.637  1.00 26.02           C  
ANISOU 1359  CD1 PHE A 168     3664   3256   2965    572   -355   -416       C  
ATOM   1360  CD2 PHE A 168     -26.733   5.913  -5.205  1.00 27.74           C  
ANISOU 1360  CD2 PHE A 168     4146   3506   2885     15   -113    -30       C  
ATOM   1361  CE1 PHE A 168     -24.501   7.421  -4.307  1.00 26.74           C  
ANISOU 1361  CE1 PHE A 168     3582   3364   3214    643    -24   -116       C  
ATOM   1362  CE2 PHE A 168     -26.266   5.766  -3.844  1.00 27.86           C  
ANISOU 1362  CE2 PHE A 168     4089   3426   3070    116   -246   -225       C  
ATOM   1363  CZ  PHE A 168     -25.132   6.506  -3.412  1.00 27.64           C  
ANISOU 1363  CZ  PHE A 168     3935   3417   3151     52    -54   -423       C  
ATOM   1364  N   TYR A 169     -25.669   4.689  -9.630  1.00 23.54           N  
ANISOU 1364  N   TYR A 169     3287   2805   2852    -58   -326    -61       N  
ATOM   1365  CA  TYR A 169     -25.021   3.421 -10.016  1.00 24.05           C  
ANISOU 1365  CA  TYR A 169     3268   3011   2855    -29   -282   -164       C  
ATOM   1366  C   TYR A 169     -23.535   3.647 -10.402  1.00 24.22           C  
ANISOU 1366  C   TYR A 169     3408   2961   2831   -102   -258    -64       C  
ATOM   1367  O   TYR A 169     -22.662   2.873 -10.008  1.00 22.66           O  
ANISOU 1367  O   TYR A 169     3180   2884   2543    -35   -162   -224       O  
ATOM   1368  CB  TYR A 169     -25.767   2.774 -11.239  1.00 23.92           C  
ANISOU 1368  CB  TYR A 169     3547   2832   2710     13   -358     48       C  
ATOM   1369  CG  TYR A 169     -25.104   1.544 -11.795  1.00 23.76           C  
ANISOU 1369  CG  TYR A 169     3234   3027   2767      4   -283     23       C  
ATOM   1370  CD1 TYR A 169     -25.620   0.296 -11.490  1.00 23.97           C  
ANISOU 1370  CD1 TYR A 169     3100   2921   3083     73   -269    -36       C  
ATOM   1371  CD2 TYR A 169     -23.983   1.625 -12.637  1.00 24.89           C  
ANISOU 1371  CD2 TYR A 169     3032   3122   3299    -71   -300   -129       C  
ATOM   1372  CE1 TYR A 169     -25.071  -0.861 -12.009  1.00 25.18           C  
ANISOU 1372  CE1 TYR A 169     3102   3253   3210    342   -267   -309       C  
ATOM   1373  CE2 TYR A 169     -23.345   0.460 -13.145  1.00 25.68           C  
ANISOU 1373  CE2 TYR A 169     3546   3169   3041   -147      7   -230       C  
ATOM   1374  CZ  TYR A 169     -23.892  -0.783 -12.802  1.00 25.33           C  
ANISOU 1374  CZ  TYR A 169     3687   3249   2686    107   -145   -253       C  
ATOM   1375  OH  TYR A 169     -23.309  -1.923 -13.265  1.00 27.51           O  
ANISOU 1375  OH  TYR A 169     4263   3155   3034    125   -200   -425       O  
ATOM   1376  N   LEU A 170     -23.266   4.667 -11.247  1.00 24.74           N  
ANISOU 1376  N   LEU A 170     3417   3072   2908    -80   -186    -24       N  
ATOM   1377  CA  LEU A 170     -21.941   4.841 -11.777  1.00 24.06           C  
ANISOU 1377  CA  LEU A 170     3426   3023   2690      2   -176     95       C  
ATOM   1378  C   LEU A 170     -20.993   5.375 -10.710  1.00 22.87           C  
ANISOU 1378  C   LEU A 170     3095   2920   2674     50   -175     71       C  
ATOM   1379  O   LEU A 170     -19.818   4.976 -10.620  1.00 23.31           O  
ANISOU 1379  O   LEU A 170     3291   3072   2493    178    -45    188       O  
ATOM   1380  CB  LEU A 170     -22.028   5.735 -13.007  1.00 24.89           C  
ANISOU 1380  CB  LEU A 170     3657   3055   2745    -30   -153    174       C  
ATOM   1381  CG  LEU A 170     -22.748   5.032 -14.177  1.00 22.34           C  
ANISOU 1381  CG  LEU A 170     3036   2620   2829     85   -258    332       C  
ATOM   1382  CD1 LEU A 170     -23.035   6.113 -15.229  1.00 28.10           C  
ANISOU 1382  CD1 LEU A 170     4624   3276   2775   -341  -1001    396       C  
ATOM   1383  CD2 LEU A 170     -21.893   3.909 -14.762  1.00 25.21           C  
ANISOU 1383  CD2 LEU A 170     3874   3209   2494    187   -355      4       C  
ATOM   1384  N   ARG A 171     -21.513   6.242  -9.854  1.00 22.58           N  
ANISOU 1384  N   ARG A 171     3123   2904   2550     30   -246     -8       N  
ATOM   1385  CA  ARG A 171     -20.650   6.884  -8.804  1.00 22.61           C  
ANISOU 1385  CA  ARG A 171     3178   2781   2631      6   -308     95       C  
ATOM   1386  C   ARG A 171     -20.232   5.782  -7.790  1.00 23.45           C  
ANISOU 1386  C   ARG A 171     3117   2879   2912     76   -291    158       C  
ATOM   1387  O   ARG A 171     -19.085   5.714  -7.402  1.00 25.39           O  
ANISOU 1387  O   ARG A 171     3429   3308   2911    -26   -580    128       O  
ATOM   1388  CB  ARG A 171     -21.423   8.040  -8.123  1.00 21.91           C  
ANISOU 1388  CB  ARG A 171     2964   2661   2697     27    -85    135       C  
ATOM   1389  CG  ARG A 171     -21.525   9.224  -9.095  1.00 22.96           C  
ANISOU 1389  CG  ARG A 171     3404   2737   2582    199   -428     45       C  
ATOM   1390  CD  ARG A 171     -22.333  10.366  -8.530  1.00 23.20           C  
ANISOU 1390  CD  ARG A 171     3676   2417   2720     37     60    179       C  
ATOM   1391  NE  ARG A 171     -22.390  11.490  -9.461  1.00 23.84           N  
ANISOU 1391  NE  ARG A 171     3926   3028   2101     41   -207     81       N  
ATOM   1392  CZ  ARG A 171     -21.535  12.525  -9.470  1.00 23.75           C  
ANISOU 1392  CZ  ARG A 171     3209   3107   2705    -44    -71    559       C  
ATOM   1393  NH1 ARG A 171     -20.526  12.614  -8.571  1.00 24.63           N  
ANISOU 1393  NH1 ARG A 171     3434   3126   2798   -356    -49     53       N  
ATOM   1394  NH2 ARG A 171     -21.716  13.502 -10.383  1.00 26.46           N  
ANISOU 1394  NH2 ARG A 171     3975   3109   2966    420   -373    553       N  
ATOM   1395  N   ILE A 172     -21.162   4.878  -7.476  1.00 22.50           N  
ANISOU 1395  N   ILE A 172     3010   2819   2718    101    -95    118       N  
ATOM   1396  CA AILE A 172     -20.918   3.733  -6.582  0.50 22.01           C  
ANISOU 1396  CA AILE A 172     2993   2806   2565     57   -142    160       C  
ATOM   1397  CA BILE A 172     -20.867   3.734  -6.586  0.50 22.45           C  
ANISOU 1397  CA BILE A 172     3006   2847   2677    106   -124    185       C  
ATOM   1398  C   ILE A 172     -19.914   2.791  -7.257  1.00 22.01           C  
ANISOU 1398  C   ILE A 172     3014   2789   2558     63   -121     84       C  
ATOM   1399  O   ILE A 172     -18.903   2.370  -6.634  1.00 23.66           O  
ANISOU 1399  O   ILE A 172     3173   3004   2811     -5    -18    -31       O  
ATOM   1400  CB AILE A 172     -22.294   3.034  -6.229  0.50 21.95           C  
ANISOU 1400  CB AILE A 172     3070   2746   2525    196      8    242       C  
ATOM   1401  CB BILE A 172     -22.123   2.936  -6.241  0.50 22.79           C  
ANISOU 1401  CB BILE A 172     3120   2808   2731    256     13    289       C  
ATOM   1402  CG1AILE A 172     -23.098   3.948  -5.263  0.50 22.20           C  
ANISOU 1402  CG1AILE A 172     3159   3046   2229    185    -18    224       C  
ATOM   1403  CG1BILE A 172     -22.978   3.767  -5.302  0.50 25.31           C  
ANISOU 1403  CG1BILE A 172     3152   3480   2984    300    148    238       C  
ATOM   1404  CG2AILE A 172     -22.115   1.545  -5.795  0.50 22.96           C  
ANISOU 1404  CG2AILE A 172     3238   2839   2646      7    -37    350       C  
ATOM   1405  CG2BILE A 172     -21.757   1.522  -5.684  0.50 23.14           C  
ANISOU 1405  CG2BILE A 172     3208   2758   2824    225     -7    491       C  
ATOM   1406  CD1AILE A 172     -22.556   4.002  -3.803  0.50 17.21           C  
ANISOU 1406  CD1AILE A 172     2469   2107   1963    318   -320    480       C  
ATOM   1407  CD1BILE A 172     -24.347   3.359  -5.393  0.50 26.69           C  
ANISOU 1407  CD1BILE A 172     2488   3768   3885    999    143     93       C  
ATOM   1408  N   ALA A 173     -20.160   2.472  -8.546  1.00 23.26           N  
ANISOU 1408  N   ALA A 173     3289   2953   2593     58    -57     54       N  
ATOM   1409  CA  ALA A 173     -19.279   1.527  -9.274  1.00 23.24           C  
ANISOU 1409  CA  ALA A 173     3269   3047   2513     -4    -29    -31       C  
ATOM   1410  C   ALA A 173     -17.810   1.927  -9.182  1.00 23.93           C  
ANISOU 1410  C   ALA A 173     3368   3084   2637     39    -45    -18       C  
ATOM   1411  O   ALA A 173     -16.940   1.081  -9.024  1.00 23.21           O  
ANISOU 1411  O   ALA A 173     3160   3006   2651    108     83    -73       O  
ATOM   1412  CB  ALA A 173     -19.705   1.434 -10.798  1.00 21.81           C  
ANISOU 1412  CB  ALA A 173     3231   2683   2372    -92   -162   -404       C  
ATOM   1413  N   GLN A 174     -17.529   3.218  -9.408  1.00 23.07           N  
ANISOU 1413  N   GLN A 174     3326   2737   2700     -3     33   -115       N  
ATOM   1414  CA  GLN A 174     -16.153   3.728  -9.441  1.00 23.64           C  
ANISOU 1414  CA  GLN A 174     3239   2893   2849   -146    -90    158       C  
ATOM   1415  C   GLN A 174     -15.355   3.424  -8.172  1.00 24.93           C  
ANISOU 1415  C   GLN A 174     3341   3069   3062   -108    -96    112       C  
ATOM   1416  O   GLN A 174     -14.113   3.335  -8.206  1.00 25.27           O  
ANISOU 1416  O   GLN A 174     3396   2990   3215     41   -129    116       O  
ATOM   1417  CB  GLN A 174     -16.177   5.252  -9.601  1.00 23.01           C  
ANISOU 1417  CB  GLN A 174     3118   2692   2932   -181     49     41       C  
ATOM   1418  CG  GLN A 174     -16.587   5.691 -11.000  1.00 25.41           C  
ANISOU 1418  CG  GLN A 174     3712   2929   3012   -284   -211    361       C  
ATOM   1419  CD  GLN A 174     -16.372   7.156 -11.184  1.00 28.24           C  
ANISOU 1419  CD  GLN A 174     4321   3181   3225     12    341    197       C  
ATOM   1420  OE1 GLN A 174     -16.445   7.889 -10.201  1.00 27.45           O  
ANISOU 1420  OE1 GLN A 174     4329   3115   2984   -365    -79    660       O  
ATOM   1421  NE2 GLN A 174     -16.084   7.614 -12.424  1.00 28.77           N  
ANISOU 1421  NE2 GLN A 174     4130   3089   3710    -16     64    993       N  
ATOM   1422  N   GLN A 175     -16.071   3.279  -7.054  1.00 25.44           N  
ANISOU 1422  N   GLN A 175     3607   2928   3132    -30    -97     65       N  
ATOM   1423  CA  GLN A 175     -15.410   3.205  -5.750  1.00 24.65           C  
ANISOU 1423  CA  GLN A 175     3652   2818   2893     34   -256     72       C  
ATOM   1424  C   GLN A 175     -15.712   1.912  -4.980  1.00 24.78           C  
ANISOU 1424  C   GLN A 175     3541   2897   2976    -70   -272     36       C  
ATOM   1425  O   GLN A 175     -15.449   1.803  -3.771  1.00 23.45           O  
ANISOU 1425  O   GLN A 175     3386   2746   2778     17     -4    178       O  
ATOM   1426  CB  GLN A 175     -15.678   4.490  -4.912  1.00 25.56           C  
ANISOU 1426  CB  GLN A 175     3766   3107   2837     87   -127     25       C  
ATOM   1427  CG  GLN A 175     -15.104   5.761  -5.632  1.00 27.81           C  
ANISOU 1427  CG  GLN A 175     4308   2799   3459    209    -20   -132       C  
ATOM   1428  CD  GLN A 175     -15.118   7.002  -4.776  1.00 29.73           C  
ANISOU 1428  CD  GLN A 175     4388   3683   3223    332   -270   -244       C  
ATOM   1429  OE1 GLN A 175     -15.794   8.038  -5.097  1.00 30.54           O  
ANISOU 1429  OE1 GLN A 175     3935   4288   3380    436     35    287       O  
ATOM   1430  NE2 GLN A 175     -14.377   6.931  -3.669  1.00 22.95           N  
ANISOU 1430  NE2 GLN A 175     3238   2570   2909    171   -133     11       N  
ATOM   1431  N   LEU A 176     -16.302   0.939  -5.667  1.00 25.40           N  
ANISOU 1431  N   LEU A 176     3710   2762   3179     96   -219     16       N  
ATOM   1432  CA  LEU A 176     -16.714  -0.296  -5.015  1.00 24.93           C  
ANISOU 1432  CA  LEU A 176     3515   2994   2962    -96   -305     72       C  
ATOM   1433  C   LEU A 176     -15.427  -1.040  -4.612  1.00 23.84           C  
ANISOU 1433  C   LEU A 176     3211   3018   2826     50   -185     33       C  
ATOM   1434  O   LEU A 176     -14.574  -1.282  -5.475  1.00 24.66           O  
ANISOU 1434  O   LEU A 176     3524   3367   2477   -233   -114    158       O  
ATOM   1435  CB  LEU A 176     -17.420  -1.192  -6.037  1.00 25.02           C  
ANISOU 1435  CB  LEU A 176     3404   3065   3034     51   -391   -283       C  
ATOM   1436  CG  LEU A 176     -18.939  -1.093  -6.235  1.00 28.28           C  
ANISOU 1436  CG  LEU A 176     3784   3818   3143   -289   -332   -258       C  
ATOM   1437  CD1 LEU A 176     -19.305  -2.007  -7.412  1.00 28.08           C  
ANISOU 1437  CD1 LEU A 176     4057   3965   2643   -730   -350   -785       C  
ATOM   1438  CD2 LEU A 176     -19.714  -1.571  -5.034  1.00 27.35           C  
ANISOU 1438  CD2 LEU A 176     3989   3757   2642   -224    464   -516       C  
ATOM   1439  N   PRO A 177     -15.311  -1.490  -3.340  1.00 23.64           N  
ANISOU 1439  N   PRO A 177     3318   3002   2661    -23    -48    -64       N  
ATOM   1440  CA  PRO A 177     -14.098  -2.214  -2.931  0.50 20.41           C  
ANISOU 1440  CA  PRO A 177     2725   2718   2309     14    -57     15       C  
ATOM   1441  C   PRO A 177     -14.237  -3.696  -3.269  1.00 22.30           C  
ANISOU 1441  C   PRO A 177     2924   3182   2364     60    -44     61       C  
ATOM   1442  O   PRO A 177     -14.362  -4.566  -2.375  1.00 21.59           O  
ANISOU 1442  O   PRO A 177     2975   2536   2690    -59    -10    -50       O  
ATOM   1443  CB  PRO A 177     -14.078  -1.957  -1.402  1.00 23.71           C  
ANISOU 1443  CB  PRO A 177     2924   3094   2988   -239    -58    -67       C  
ATOM   1444  CG  PRO A 177     -15.532  -1.848  -1.061  1.00 23.80           C  
ANISOU 1444  CG  PRO A 177     3148   3265   2627    385     31     57       C  
ATOM   1445  CD  PRO A 177     -16.078  -1.026  -2.166  1.00 23.34           C  
ANISOU 1445  CD  PRO A 177     3170   3031   2665    206   -177    149       C  
ATOM   1446  N   ILE A 178     -14.309  -4.019  -4.573  1.00 21.93           N  
ANISOU 1446  N   ILE A 178     2920   2906   2506    121     48   -255       N  
ATOM   1447  CA  ILE A 178     -14.696  -5.359  -5.016  1.00 21.29           C  
ANISOU 1447  CA  ILE A 178     2924   2776   2386     53    -14     46       C  
ATOM   1448  C   ILE A 178     -13.684  -6.413  -4.528  1.00 21.79           C  
ANISOU 1448  C   ILE A 178     2826   2796   2654    132     45     11       C  
ATOM   1449  O   ILE A 178     -14.056  -7.435  -3.857  1.00 22.27           O  
ANISOU 1449  O   ILE A 178     3008   3024   2429    161    109    117       O  
ATOM   1450  CB  ILE A 178     -14.788  -5.437  -6.568  1.00 21.00           C  
ANISOU 1450  CB  ILE A 178     2983   2785   2209    211    -92     33       C  
ATOM   1451  CG1 ILE A 178     -15.935  -4.485  -7.061  1.00 22.54           C  
ANISOU 1451  CG1 ILE A 178     3168   3236   2159    301    -63    163       C  
ATOM   1452  CG2 ILE A 178     -15.063  -6.896  -6.963  1.00 21.63           C  
ANISOU 1452  CG2 ILE A 178     2917   2912   2390     -4    -77   -138       C  
ATOM   1453  CD1 ILE A 178     -16.070  -4.431  -8.588  1.00 24.01           C  
ANISOU 1453  CD1 ILE A 178     4197   2965   1958     95   -537    116       C  
ATOM   1454  N   TYR A 179     -12.407  -6.201  -4.859  1.00 21.84           N  
ANISOU 1454  N   TYR A 179     2697   2957   2644    179    -26     30       N  
ATOM   1455  CA  TYR A 179     -11.393  -7.234  -4.519  1.00 22.95           C  
ANISOU 1455  CA  TYR A 179     2830   3049   2840    209     20     29       C  
ATOM   1456  C   TYR A 179     -11.095  -7.233  -3.031  1.00 22.80           C  
ANISOU 1456  C   TYR A 179     2673   3102   2886     93    -86    172       C  
ATOM   1457  O   TYR A 179     -10.901  -8.281  -2.464  1.00 23.93           O  
ANISOU 1457  O   TYR A 179     2678   3171   3241     15   -180    216       O  
ATOM   1458  CB  TYR A 179     -10.110  -7.012  -5.300  1.00 22.58           C  
ANISOU 1458  CB  TYR A 179     2587   3106   2886    194    -57    177       C  
ATOM   1459  CG  TYR A 179     -10.324  -7.192  -6.784  1.00 26.08           C  
ANISOU 1459  CG  TYR A 179     3110   3643   3156    268    226    114       C  
ATOM   1460  CD1 TYR A 179     -10.975  -8.332  -7.287  1.00 28.31           C  
ANISOU 1460  CD1 TYR A 179     3613   3995   3147    159    257   -159       C  
ATOM   1461  CD2 TYR A 179      -9.958  -6.187  -7.694  1.00 32.01           C  
ANISOU 1461  CD2 TYR A 179     3823   4435   3902     51    322    310       C  
ATOM   1462  CE1 TYR A 179     -11.183  -8.487  -8.658  1.00 32.72           C  
ANISOU 1462  CE1 TYR A 179     3796   4815   3821    -24    -73   -103       C  
ATOM   1463  CE2 TYR A 179     -10.175  -6.356  -9.068  1.00 33.16           C  
ANISOU 1463  CE2 TYR A 179     4329   4559   3710      3    144    255       C  
ATOM   1464  CZ  TYR A 179     -10.800  -7.498  -9.526  1.00 33.65           C  
ANISOU 1464  CZ  TYR A 179     3815   5000   3971     82   -164    131       C  
ATOM   1465  OH  TYR A 179     -10.956  -7.690 -10.882  1.00 39.20           O  
ANISOU 1465  OH  TYR A 179     4391   6123   4380      6   -253   -136       O  
ATOM   1466  N   GLU A 180     -11.140  -6.062  -2.397  1.00 22.87           N  
ANISOU 1466  N   GLU A 180     2766   3093   2827    -18     48    118       N  
ATOM   1467  CA  GLU A 180     -10.878  -5.967  -0.924  1.00 25.41           C  
ANISOU 1467  CA  GLU A 180     3101   3359   3193    -80    129    -51       C  
ATOM   1468  C   GLU A 180     -11.855  -6.793  -0.161  1.00 24.29           C  
ANISOU 1468  C   GLU A 180     3124   3121   2981    -10    -38    -30       C  
ATOM   1469  O   GLU A 180     -11.473  -7.617   0.707  1.00 25.75           O  
ANISOU 1469  O   GLU A 180     3080   3365   3339     29   -136    301       O  
ATOM   1470  CB  GLU A 180     -10.994  -4.505  -0.435  1.00 25.82           C  
ANISOU 1470  CB  GLU A 180     2968   3310   3530   -126    404    -60       C  
ATOM   1471  CG  GLU A 180      -9.834  -3.594  -0.918  1.00 32.46           C  
ANISOU 1471  CG  GLU A 180     3590   4103   4639   -389    123    174       C  
ATOM   1472  CD  GLU A 180      -9.977  -3.033  -2.394  1.00 36.49           C  
ANISOU 1472  CD  GLU A 180     4138   4769   4957   -518      3    377       C  
ATOM   1473  OE1 GLU A 180     -10.932  -3.359  -3.221  1.00 32.35           O  
ANISOU 1473  OE1 GLU A 180     2972   4013   5305   -371   -199    714       O  
ATOM   1474  OE2 GLU A 180      -9.070  -2.246  -2.730  1.00 38.25           O  
ANISOU 1474  OE2 GLU A 180     4370   4170   5990   -246    200    183       O  
ATOM   1475  N   VAL A 181     -13.146  -6.564  -0.432  1.00 22.86           N  
ANISOU 1475  N   VAL A 181     2941   3094   2651    -26     67    -62       N  
ATOM   1476  CA  VAL A 181     -14.177  -7.319   0.285  1.00 21.96           C  
ANISOU 1476  CA  VAL A 181     2767   2854   2720    -42    -31    -30       C  
ATOM   1477  C   VAL A 181     -14.155  -8.790  -0.136  1.00 21.69           C  
ANISOU 1477  C   VAL A 181     2676   2944   2619    163     30     26       C  
ATOM   1478  O   VAL A 181     -14.193  -9.661   0.732  1.00 21.84           O  
ANISOU 1478  O   VAL A 181     2634   2994   2670    448    -95     85       O  
ATOM   1479  CB  VAL A 181     -15.559  -6.704   0.127  1.00 22.12           C  
ANISOU 1479  CB  VAL A 181     2910   2688   2804    -16    245      5       C  
ATOM   1480  CG1 VAL A 181     -16.596  -7.608   0.740  1.00 20.43           C  
ANISOU 1480  CG1 VAL A 181     2419   2659   2684   -410    157   -159       C  
ATOM   1481  CG2 VAL A 181     -15.571  -5.272   0.741  1.00 22.57           C  
ANISOU 1481  CG2 VAL A 181     3486   2941   2149    -88    234   -104       C  
ATOM   1482  N   SER A 182     -14.060  -9.068  -1.450  1.00 20.60           N  
ANISOU 1482  N   SER A 182     2538   2895   2393    301    191   -101       N  
ATOM   1483  CA  SER A 182     -14.194 -10.449  -1.921  1.00 19.66           C  
ANISOU 1483  CA  SER A 182     2572   2755   2142    241     -7    -59       C  
ATOM   1484  C   SER A 182     -13.067 -11.366  -1.355  1.00 21.66           C  
ANISOU 1484  C   SER A 182     2875   2911   2441    157     78      6       C  
ATOM   1485  O   SER A 182     -13.330 -12.555  -1.082  1.00 22.90           O  
ANISOU 1485  O   SER A 182     3105   2956   2637    130     91      4       O  
ATOM   1486  CB  SER A 182     -14.116 -10.490  -3.489  1.00 19.27           C  
ANISOU 1486  CB  SER A 182     2473   2621   2225    251     16    263       C  
ATOM   1487  OG  SER A 182     -15.201  -9.678  -3.983  1.00 22.33           O  
ANISOU 1487  OG  SER A 182     2915   2998   2570    231   -259    248       O  
ATOM   1488  N   ALA A 183     -11.843 -10.815  -1.256  1.00 21.87           N  
ANISOU 1488  N   ALA A 183     2899   3105   2303    156     11   -267       N  
ATOM   1489  CA  ALA A 183     -10.657 -11.585  -0.837  1.00 22.60           C  
ANISOU 1489  CA  ALA A 183     2900   3206   2480    112     40    -62       C  
ATOM   1490  C   ALA A 183     -10.775 -12.123   0.580  1.00 23.40           C  
ANISOU 1490  C   ALA A 183     2969   3248   2671     72    -78     -4       C  
ATOM   1491  O   ALA A 183      -9.964 -12.986   0.972  1.00 23.73           O  
ANISOU 1491  O   ALA A 183     3304   3148   2564      4   -152    -92       O  
ATOM   1492  CB  ALA A 183      -9.312 -10.774  -0.992  1.00 23.02           C  
ANISOU 1492  CB  ALA A 183     2859   3107   2779    156   -232   -119       C  
ATOM   1493  N   GLN A 184     -11.784 -11.684   1.328  1.00 22.97           N  
ANISOU 1493  N   GLN A 184     3092   2989   2645     63   -113   -292       N  
ATOM   1494  CA  GLN A 184     -11.925 -12.218   2.687  1.00 24.88           C  
ANISOU 1494  CA  GLN A 184     3290   3114   3049     17    161   -109       C  
ATOM   1495  C   GLN A 184     -12.498 -13.634   2.731  1.00 25.44           C  
ANISOU 1495  C   GLN A 184     3418   3146   3101     -2     22   -181       C  
ATOM   1496  O   GLN A 184     -12.525 -14.269   3.791  1.00 24.88           O  
ANISOU 1496  O   GLN A 184     3336   3083   3032     32    -20    104       O  
ATOM   1497  CB  GLN A 184     -12.722 -11.266   3.604  1.00 24.87           C  
ANISOU 1497  CB  GLN A 184     3313   3057   3079     70    195   -255       C  
ATOM   1498  CG  GLN A 184     -12.219  -9.821   3.528  1.00 24.91           C  
ANISOU 1498  CG  GLN A 184     3460   2835   3171     81    -31    -90       C  
ATOM   1499  CD  GLN A 184     -10.688  -9.735   3.653  1.00 26.18           C  
ANISOU 1499  CD  GLN A 184     3585   3099   3264   -221   -379     -6       C  
ATOM   1500  OE1 GLN A 184     -10.065 -10.413   4.511  1.00 28.12           O  
ANISOU 1500  OE1 GLN A 184     3976   3618   3090    -70   -570    -83       O  
ATOM   1501  NE2 GLN A 184     -10.062  -8.978   2.751  1.00 24.97           N  
ANISOU 1501  NE2 GLN A 184     2963   3315   3208   -108   -287   -129       N  
ATOM   1502  N   PHE A 185     -13.065 -14.058   1.611  1.00 24.67           N  
ANISOU 1502  N   PHE A 185     3102   3096   3175    -48    -45   -292       N  
ATOM   1503  CA  PHE A 185     -13.583 -15.419   1.484  1.00 24.00           C  
ANISOU 1503  CA  PHE A 185     3081   3006   3030    -75   -219   -149       C  
ATOM   1504  C   PHE A 185     -12.435 -16.358   1.097  1.00 24.13           C  
ANISOU 1504  C   PHE A 185     3203   2970   2993    -75   -104    -95       C  
ATOM   1505  O   PHE A 185     -11.861 -16.288   0.003  1.00 24.88           O  
ANISOU 1505  O   PHE A 185     3422   2995   3036     -8    -19   -176       O  
ATOM   1506  CB  PHE A 185     -14.667 -15.437   0.389  1.00 23.27           C  
ANISOU 1506  CB  PHE A 185     2845   2946   3050   -291   -334   -291       C  
ATOM   1507  CG  PHE A 185     -15.324 -16.794   0.255  1.00 23.50           C  
ANISOU 1507  CG  PHE A 185     2772   3059   3096   -340    -23   -222       C  
ATOM   1508  CD1 PHE A 185     -16.246 -17.250   1.278  1.00 21.56           C  
ANISOU 1508  CD1 PHE A 185     2500   2997   2694   -556   -276    244       C  
ATOM   1509  CD2 PHE A 185     -15.019 -17.649  -0.842  1.00 22.76           C  
ANISOU 1509  CD2 PHE A 185     2734   2793   3120   -179   -450   -327       C  
ATOM   1510  CE1 PHE A 185     -16.875 -18.535   1.160  1.00 24.11           C  
ANISOU 1510  CE1 PHE A 185     2947   2890   3324    -59    -55   -177       C  
ATOM   1511  CE2 PHE A 185     -15.634 -18.904  -0.910  1.00 23.85           C  
ANISOU 1511  CE2 PHE A 185     2732   2880   3450     83     50   -356       C  
ATOM   1512  CZ  PHE A 185     -16.560 -19.339   0.055  1.00 24.74           C  
ANISOU 1512  CZ  PHE A 185     3147   3220   3032     18   -237   -196       C  
ATOM   1513  N   THR A 186     -12.076 -17.246   1.998  1.00 24.84           N  
ANISOU 1513  N   THR A 186     3259   3054   3125     44    -72     72       N  
ATOM   1514  CA  THR A 186     -10.871 -18.097   1.831  1.00 25.25           C  
ANISOU 1514  CA  THR A 186     3240   3145   3206     82   -127    -49       C  
ATOM   1515  C   THR A 186     -11.244 -19.576   1.586  1.00 25.19           C  
ANISOU 1515  C   THR A 186     3226   3151   3194     47   -166    -17       C  
ATOM   1516  O   THR A 186     -10.326 -20.434   1.418  1.00 25.96           O  
ANISOU 1516  O   THR A 186     3328   3108   3428    118   -451      9       O  
ATOM   1517  CB  THR A 186      -9.932 -17.993   3.054  1.00 25.96           C  
ANISOU 1517  CB  THR A 186     3308   3161   3393     -1   -278    125       C  
ATOM   1518  OG1 THR A 186     -10.624 -18.466   4.219  1.00 27.93           O  
ANISOU 1518  OG1 THR A 186     3404   4177   3030    228    -92    231       O  
ATOM   1519  CG2 THR A 186      -9.372 -16.549   3.299  1.00 25.48           C  
ANISOU 1519  CG2 THR A 186     3218   3239   3222    144   -488   -274       C  
ATOM   1520  N   LYS A 187     -12.564 -19.847   1.467  1.00 24.82           N  
ANISOU 1520  N   LYS A 187     3337   3051   3040    -99      5     -4       N  
ATOM   1521  CA  LYS A 187     -13.061 -21.174   1.100  1.00 24.81           C  
ANISOU 1521  CA  LYS A 187     3338   3093   2994    -57   -126    -11       C  
ATOM   1522  C   LYS A 187     -13.028 -21.359  -0.432  1.00 24.93           C  
ANISOU 1522  C   LYS A 187     3345   3033   3093    -20    -70      6       C  
ATOM   1523  O   LYS A 187     -12.599 -20.437  -1.167  1.00 24.37           O  
ANISOU 1523  O   LYS A 187     2947   3354   2958   -104   -174   -208       O  
ATOM   1524  CB  LYS A 187     -14.434 -21.428   1.761  1.00 23.07           C  
ANISOU 1524  CB  LYS A 187     3220   2659   2885      6   -186    221       C  
ATOM   1525  CG  LYS A 187     -14.357 -21.665   3.321  1.00 29.21           C  
ANISOU 1525  CG  LYS A 187     4026   3990   3082    -70   -131    337       C  
ATOM   1526  CD  LYS A 187     -15.797 -21.621   3.949  1.00 34.36           C  
ANISOU 1526  CD  LYS A 187     4493   5066   3493   -496    373    437       C  
ATOM   1527  CE  LYS A 187     -15.847 -21.214   5.447  1.00 39.07           C  
ANISOU 1527  CE  LYS A 187     4820   5851   4172   -161   1430    557       C  
ATOM   1528  NZ  LYS A 187     -17.229 -20.664   5.711  1.00 40.52           N  
ANISOU 1528  NZ  LYS A 187     5487   5674   4233    190   1646     94       N  
ATOM   1529  N   PRO A 188     -13.462 -22.545  -0.932  1.00 25.04           N  
ANISOU 1529  N   PRO A 188     3397   3140   2975   -147    -68    -75       N  
ATOM   1530  CA  PRO A 188     -13.196 -22.787  -2.373  1.00 25.49           C  
ANISOU 1530  CA  PRO A 188     3545   3111   3029    -80   -162    -94       C  
ATOM   1531  C   PRO A 188     -14.033 -21.909  -3.335  1.00 25.84           C  
ANISOU 1531  C   PRO A 188     3508   3122   3187   -104   -145   -188       C  
ATOM   1532  O   PRO A 188     -15.232 -21.713  -3.108  1.00 26.06           O  
ANISOU 1532  O   PRO A 188     3512   3107   3279     59   -212   -299       O  
ATOM   1533  CB  PRO A 188     -13.534 -24.258  -2.530  1.00 25.51           C  
ANISOU 1533  CB  PRO A 188     3526   2989   3174   -147   -235     49       C  
ATOM   1534  CG  PRO A 188     -13.220 -24.880  -1.121  1.00 27.24           C  
ANISOU 1534  CG  PRO A 188     3985   3394   2968   -183     73    -22       C  
ATOM   1535  CD  PRO A 188     -13.773 -23.807  -0.203  1.00 26.35           C  
ANISOU 1535  CD  PRO A 188     3550   3184   3275    -81    -43    -50       C  
ATOM   1536  N   VAL A 189     -13.364 -21.392  -4.375  1.00 26.21           N  
ANISOU 1536  N   VAL A 189     3576   3230   3152     -6   -205    -13       N  
ATOM   1537  CA  VAL A 189     -13.987 -20.559  -5.387  1.00 24.26           C  
ANISOU 1537  CA  VAL A 189     3286   3051   2879    -59     23   -103       C  
ATOM   1538  C   VAL A 189     -13.663 -21.189  -6.720  1.00 25.03           C  
ANISOU 1538  C   VAL A 189     3145   3305   3058     12    -25   -160       C  
ATOM   1539  O   VAL A 189     -12.494 -21.633  -6.942  1.00 25.79           O  
ANISOU 1539  O   VAL A 189     3072   3416   3311     38     83   -327       O  
ATOM   1540  CB  VAL A 189     -13.446 -19.089  -5.363  1.00 22.95           C  
ANISOU 1540  CB  VAL A 189     3515   2572   2630     35     10     16       C  
ATOM   1541  CG1 VAL A 189     -14.119 -18.271  -6.548  1.00 25.08           C  
ANISOU 1541  CG1 VAL A 189     3660   2865   3004    164   -429    157       C  
ATOM   1542  CG2 VAL A 189     -13.640 -18.431  -3.986  1.00 23.09           C  
ANISOU 1542  CG2 VAL A 189     3315   2850   2607   -176    503     77       C  
ATOM   1543  N   CYS A 190     -14.670 -21.244  -7.599  1.00 23.41           N  
ANISOU 1543  N   CYS A 190     2838   3066   2987   -142     80   -175       N  
ATOM   1544  CA  CYS A 190     -14.503 -21.693  -8.955  1.00 22.69           C  
ANISOU 1544  CA  CYS A 190     2788   3064   2767   -100    -62   -242       C  
ATOM   1545  C   CYS A 190     -14.749 -20.488  -9.853  1.00 23.49           C  
ANISOU 1545  C   CYS A 190     2919   3062   2944   -143      3   -226       C  
ATOM   1546  O   CYS A 190     -15.839 -19.835  -9.730  1.00 25.30           O  
ANISOU 1546  O   CYS A 190     3267   3245   3100    210     51     44       O  
ATOM   1547  CB  CYS A 190     -15.561 -22.785  -9.209  1.00 23.19           C  
ANISOU 1547  CB  CYS A 190     3085   2910   2813   -153    -33   -137       C  
ATOM   1548  SG  CYS A 190     -15.538 -23.459 -10.943  1.00 27.70           S  
ANISOU 1548  SG  CYS A 190     3723   3621   3180   -136     19   -283       S  
ATOM   1549  N   LEU A 191     -13.829 -20.191 -10.783  1.00 23.51           N  
ANISOU 1549  N   LEU A 191     3076   3123   2734    -37     -1   -364       N  
ATOM   1550  CA  LEU A 191     -13.902 -19.019 -11.665  1.00 23.75           C  
ANISOU 1550  CA  LEU A 191     3179   3234   2608    -97    -14   -442       C  
ATOM   1551  C   LEU A 191     -14.035 -19.564 -13.091  1.00 24.17           C  
ANISOU 1551  C   LEU A 191     3337   3193   2653    -92    -34   -339       C  
ATOM   1552  O   LEU A 191     -13.183 -20.381 -13.505  1.00 25.34           O  
ANISOU 1552  O   LEU A 191     3462   3482   2683   -205     56   -224       O  
ATOM   1553  CB  LEU A 191     -12.582 -18.188 -11.541  1.00 23.33           C  
ANISOU 1553  CB  LEU A 191     3077   3167   2620    -97    -22   -380       C  
ATOM   1554  CG  LEU A 191     -12.298 -17.683 -10.087  1.00 22.74           C  
ANISOU 1554  CG  LEU A 191     2788   3033   2817     16    134   -967       C  
ATOM   1555  CD1 LEU A 191     -10.960 -17.056 -10.056  1.00 27.63           C  
ANISOU 1555  CD1 LEU A 191     3402   3638   3454   -404   -254   -183       C  
ATOM   1556  CD2 LEU A 191     -13.315 -16.587  -9.706  1.00 23.09           C  
ANISOU 1556  CD2 LEU A 191     2869   2902   3000     67    258   -281       C  
ATOM   1557  N   ILE A 192     -15.065 -19.137 -13.814  1.00 23.51           N  
ANISOU 1557  N   ILE A 192     3298   3026   2608   -218    -33   -284       N  
ATOM   1558  CA  ILE A 192     -15.325 -19.684 -15.171  1.00 24.58           C  
ANISOU 1558  CA  ILE A 192     3346   3185   2808   -161   -124   -269       C  
ATOM   1559  C   ILE A 192     -15.487 -18.510 -16.103  1.00 25.32           C  
ANISOU 1559  C   ILE A 192     3356   3233   3029    -85    -45   -205       C  
ATOM   1560  O   ILE A 192     -16.367 -17.657 -15.858  1.00 25.15           O  
ANISOU 1560  O   ILE A 192     2952   3420   3182   -127   -247   -277       O  
ATOM   1561  CB  ILE A 192     -16.626 -20.554 -15.211  1.00 24.50           C  
ANISOU 1561  CB  ILE A 192     3578   2987   2741   -164   -213   -301       C  
ATOM   1562  CG1 ILE A 192     -16.542 -21.743 -14.236  1.00 23.94           C  
ANISOU 1562  CG1 ILE A 192     3068   3100   2927   -192   -236    -25       C  
ATOM   1563  CG2 ILE A 192     -16.898 -21.009 -16.664  1.00 26.18           C  
ANISOU 1563  CG2 ILE A 192     3747   3253   2946   -331   -254   -701       C  
ATOM   1564  CD1 ILE A 192     -17.993 -22.338 -13.945  1.00 24.07           C  
ANISOU 1564  CD1 ILE A 192     3111   3112   2921   -261    260   -396       C  
ATOM   1565  N   HIS A 193     -14.683 -18.434 -17.176  1.00 24.78           N  
ANISOU 1565  N   HIS A 193     3210   3203   3001    -47    125   -238       N  
ATOM   1566  CA  HIS A 193     -14.725 -17.240 -18.023  1.00 24.67           C  
ANISOU 1566  CA  HIS A 193     3236   3174   2963   -138     26   -184       C  
ATOM   1567  C   HIS A 193     -14.454 -17.662 -19.459  1.00 25.24           C  
ANISOU 1567  C   HIS A 193     3308   3223   3057   -111    106   -208       C  
ATOM   1568  O   HIS A 193     -13.529 -18.492 -19.702  1.00 25.40           O  
ANISOU 1568  O   HIS A 193     3337   3125   3187   -254    289   -235       O  
ATOM   1569  CB  HIS A 193     -13.629 -16.217 -17.595  1.00 24.37           C  
ANISOU 1569  CB  HIS A 193     3192   3259   2806    -24   -202   -337       C  
ATOM   1570  CG  HIS A 193     -14.015 -14.785 -17.741  1.00 25.64           C  
ANISOU 1570  CG  HIS A 193     3376   3254   3112   -230   -275   -239       C  
ATOM   1571  ND1 HIS A 193     -14.385 -14.183 -18.953  1.00 29.85           N  
ANISOU 1571  ND1 HIS A 193     4296   3384   3658    -69    335   -216       N  
ATOM   1572  CD2 HIS A 193     -14.074 -13.804 -16.801  1.00 19.37           C  
ANISOU 1572  CD2 HIS A 193     2720   2579   2057    -80    204   -205       C  
ATOM   1573  CE1 HIS A 193     -14.683 -12.908 -18.725  1.00 23.00           C  
ANISOU 1573  CE1 HIS A 193     3075   2887   2776   -169    126   -264       C  
ATOM   1574  NE2 HIS A 193     -14.492 -12.660 -17.436  1.00 28.53           N  
ANISOU 1574  NE2 HIS A 193     3964   3344   3531    -36    111     68       N  
ATOM   1575  N   GLY A 194     -15.206 -17.117 -20.415  1.00 25.58           N  
ANISOU 1575  N   GLY A 194     3532   3315   2869   -202    187   -181       N  
ATOM   1576  CA  GLY A 194     -14.952 -17.521 -21.817  1.00 26.61           C  
ANISOU 1576  CA  GLY A 194     3669   3388   3052   -159    283   -420       C  
ATOM   1577  C   GLY A 194     -13.851 -16.621 -22.429  1.00 28.64           C  
ANISOU 1577  C   GLY A 194     3922   3666   3292    -80    422   -336       C  
ATOM   1578  O   GLY A 194     -13.750 -15.392 -22.136  1.00 27.67           O  
ANISOU 1578  O   GLY A 194     4165   3539   2808   -102    162   -421       O  
ATOM   1579  N   THR A 195     -12.977 -17.229 -23.232  1.00 29.91           N  
ANISOU 1579  N   THR A 195     3994   3816   3551     48    407   -511       N  
ATOM   1580  CA  THR A 195     -11.800 -16.480 -23.741  1.00 30.90           C  
ANISOU 1580  CA  THR A 195     4172   3844   3724     57    454   -434       C  
ATOM   1581  C   THR A 195     -12.212 -15.400 -24.723  1.00 31.34           C  
ANISOU 1581  C   THR A 195     4315   3985   3605     13    472   -474       C  
ATOM   1582  O   THR A 195     -11.516 -14.391 -24.901  1.00 30.84           O  
ANISOU 1582  O   THR A 195     4190   3836   3689   -240    827   -419       O  
ATOM   1583  CB  THR A 195     -10.771 -17.391 -24.439  1.00 31.57           C  
ANISOU 1583  CB  THR A 195     4130   4048   3814     45    366   -475       C  
ATOM   1584  OG1 THR A 195     -11.403 -18.035 -25.568  1.00 32.82           O  
ANISOU 1584  OG1 THR A 195     4778   4046   3644   -144    649   -450       O  
ATOM   1585  CG2 THR A 195     -10.224 -18.408 -23.418  1.00 31.87           C  
ANISOU 1585  CG2 THR A 195     4176   4099   3831    199    323   -435       C  
ATOM   1586  N   ASP A 196     -13.346 -15.603 -25.350  1.00 31.81           N  
ANISOU 1586  N   ASP A 196     4349   4197   3541     58    313   -407       N  
ATOM   1587  CA  ASP A 196     -13.867 -14.626 -26.295  1.00 33.09           C  
ANISOU 1587  CA  ASP A 196     4747   4223   3603    135     39   -359       C  
ATOM   1588  C   ASP A 196     -15.003 -13.788 -25.724  1.00 32.31           C  
ANISOU 1588  C   ASP A 196     4607   4095   3574     86      5   -350       C  
ATOM   1589  O   ASP A 196     -15.898 -13.292 -26.460  1.00 33.25           O  
ANISOU 1589  O   ASP A 196     5030   3791   3810    289   -143   -436       O  
ATOM   1590  CB  ASP A 196     -14.280 -15.354 -27.621  1.00 33.87           C  
ANISOU 1590  CB  ASP A 196     4982   4437   3448    124    -86   -576       C  
ATOM   1591  CG  ASP A 196     -13.073 -15.979 -28.377  1.00 39.80           C  
ANISOU 1591  CG  ASP A 196     5415   5614   4091     97   -103   -592       C  
ATOM   1592  OD1 ASP A 196     -11.926 -16.083 -27.856  1.00 46.34           O  
ANISOU 1592  OD1 ASP A 196     6283   7030   4291   -186   -355   -901       O  
ATOM   1593  OD2 ASP A 196     -13.268 -16.381 -29.544  1.00 44.09           O  
ANISOU 1593  OD2 ASP A 196     6173   6355   4222    -79     86  -1367       O  
ATOM   1594  N   ASP A 197     -14.994 -13.588 -24.396  1.00 29.96           N  
ANISOU 1594  N   ASP A 197     4245   3809   3328    -13    243   -198       N  
ATOM   1595  CA  ASP A 197     -15.979 -12.688 -23.794  1.00 30.89           C  
ANISOU 1595  CA  ASP A 197     4360   3850   3527     62    230   -208       C  
ATOM   1596  C   ASP A 197     -15.646 -11.246 -24.144  1.00 30.33           C  
ANISOU 1596  C   ASP A 197     4238   3800   3483    105    267   -275       C  
ATOM   1597  O   ASP A 197     -14.538 -10.757 -23.792  1.00 30.98           O  
ANISOU 1597  O   ASP A 197     4287   3928   3555    185    428   -310       O  
ATOM   1598  CB  ASP A 197     -15.951 -12.882 -22.263  1.00 29.50           C  
ANISOU 1598  CB  ASP A 197     4183   3879   3145    104    252   -316       C  
ATOM   1599  CG  ASP A 197     -17.062 -12.162 -21.551  1.00 29.49           C  
ANISOU 1599  CG  ASP A 197     3910   3732   3562    -77    218   -219       C  
ATOM   1600  OD1 ASP A 197     -17.619 -11.144 -22.056  1.00 30.63           O  
ANISOU 1600  OD1 ASP A 197     4508   3961   3166   -218    586   -140       O  
ATOM   1601  OD2 ASP A 197     -17.398 -12.655 -20.453  1.00 29.49           O  
ANISOU 1601  OD2 ASP A 197     4218   3799   3186    101    -76   -408       O  
ATOM   1602  N   THR A 198     -16.599 -10.564 -24.793  1.00 30.84           N  
ANISOU 1602  N   THR A 198     4414   3819   3483     92    222   -415       N  
ATOM   1603  CA  THR A 198     -16.366  -9.214 -25.309  0.60 31.56           C  
ANISOU 1603  CA  THR A 198     4515   3797   3677    187    248   -263       C  
ATOM   1604  C   THR A 198     -16.955  -8.192 -24.334  1.00 32.43           C  
ANISOU 1604  C   THR A 198     4667   3793   3862     74    278   -190       C  
ATOM   1605  O   THR A 198     -16.740  -6.974 -24.503  1.00 33.11           O  
ANISOU 1605  O   THR A 198     4933   3687   3957    184    270   -323       O  
ATOM   1606  CB  THR A 198     -16.960  -8.991 -26.755  1.00 31.87           C  
ANISOU 1606  CB  THR A 198     4410   3829   3868    244    293   -312       C  
ATOM   1607  OG1 THR A 198     -18.401  -9.087 -26.735  1.00 35.27           O  
ANISOU 1607  OG1 THR A 198     4786   4695   3920    100   -416   -309       O  
ATOM   1608  CG2 THR A 198     -16.410 -10.005 -27.788  1.00 34.20           C  
ANISOU 1608  CG2 THR A 198     5303   3868   3821    434    346   -315       C  
ATOM   1609  N   VAL A 199     -17.676  -8.689 -23.317  1.00 32.00           N  
ANISOU 1609  N   VAL A 199     4533   3816   3808     89    290   -102       N  
ATOM   1610  CA  VAL A 199     -18.470  -7.860 -22.394  1.00 30.96           C  
ANISOU 1610  CA  VAL A 199     4307   3748   3709     37    200   -111       C  
ATOM   1611  C   VAL A 199     -17.649  -7.611 -21.106  1.00 31.41           C  
ANISOU 1611  C   VAL A 199     4436   3734   3763    -25    184    -41       C  
ATOM   1612  O   VAL A 199     -17.492  -6.456 -20.662  1.00 30.78           O  
ANISOU 1612  O   VAL A 199     4645   3544   3503     -3    403    -62       O  
ATOM   1613  CB  VAL A 199     -19.895  -8.488 -22.084  1.00 29.84           C  
ANISOU 1613  CB  VAL A 199     4161   3579   3594    -20    150   -218       C  
ATOM   1614  CG1 VAL A 199     -20.674  -7.629 -21.052  1.00 29.12           C  
ANISOU 1614  CG1 VAL A 199     3521   3657   3885    201    287   -336       C  
ATOM   1615  CG2 VAL A 199     -20.735  -8.638 -23.348  1.00 33.36           C  
ANISOU 1615  CG2 VAL A 199     4725   3850   4099      7     36   -418       C  
ATOM   1616  N   VAL A 200     -17.090  -8.694 -20.549  1.00 30.38           N  
ANISOU 1616  N   VAL A 200     4112   3821   3606     23    103     75       N  
ATOM   1617  CA  VAL A 200     -16.212  -8.645 -19.389  1.00 30.16           C  
ANISOU 1617  CA  VAL A 200     4039   3787   3632     59    129     55       C  
ATOM   1618  C   VAL A 200     -14.869  -9.295 -19.800  1.00 31.24           C  
ANISOU 1618  C   VAL A 200     4154   3975   3739    -52     66     23       C  
ATOM   1619  O   VAL A 200     -14.841 -10.495 -20.155  1.00 30.85           O  
ANISOU 1619  O   VAL A 200     4173   3777   3771   -160    133   -117       O  
ATOM   1620  CB  VAL A 200     -16.856  -9.367 -18.162  1.00 29.58           C  
ANISOU 1620  CB  VAL A 200     3766   3989   3482    254    191     16       C  
ATOM   1621  CG1 VAL A 200     -15.843  -9.442 -17.063  1.00 26.10           C  
ANISOU 1621  CG1 VAL A 200     4020   3294   2601    287    -60   -234       C  
ATOM   1622  CG2 VAL A 200     -18.217  -8.655 -17.716  1.00 29.60           C  
ANISOU 1622  CG2 VAL A 200     4030   3460   3757    398     75     13       C  
ATOM   1623  N   SER A 201     -13.769  -8.510 -19.790  1.00 30.89           N  
ANISOU 1623  N   SER A 201     4028   4000   3707   -151    113     21       N  
ATOM   1624  CA  SER A 201     -12.485  -9.096 -20.108  1.00 31.21           C  
ANISOU 1624  CA  SER A 201     4147   3966   3742   -184    147   -130       C  
ATOM   1625  C   SER A 201     -12.197 -10.322 -19.208  1.00 30.81           C  
ANISOU 1625  C   SER A 201     4120   3863   3722   -262    196   -221       C  
ATOM   1626  O   SER A 201     -12.437 -10.264 -17.980  1.00 30.24           O  
ANISOU 1626  O   SER A 201     4230   3803   3454   -502    223   -331       O  
ATOM   1627  CB  SER A 201     -11.374  -8.074 -19.970  1.00 31.23           C  
ANISOU 1627  CB  SER A 201     4087   3961   3817   -130     74    -97       C  
ATOM   1628  OG  SER A 201     -10.156  -8.717 -20.063  1.00 32.13           O  
ANISOU 1628  OG  SER A 201     4335   4559   3311   -163    403     21       O  
ATOM   1629  N   PRO A 202     -11.683 -11.440 -19.801  1.00 30.66           N  
ANISOU 1629  N   PRO A 202     4126   3846   3677   -162    237   -303       N  
ATOM   1630  CA  PRO A 202     -11.182 -12.525 -18.978  1.00 30.92           C  
ANISOU 1630  CA  PRO A 202     4114   3858   3775    -35    273   -408       C  
ATOM   1631  C   PRO A 202     -10.176 -12.055 -17.903  1.00 30.95           C  
ANISOU 1631  C   PRO A 202     4099   3978   3681    -25    390   -395       C  
ATOM   1632  O   PRO A 202      -9.941 -12.795 -16.945  1.00 31.08           O  
ANISOU 1632  O   PRO A 202     3897   4230   3679     10    601   -411       O  
ATOM   1633  CB  PRO A 202     -10.443 -13.418 -20.000  1.00 30.99           C  
ANISOU 1633  CB  PRO A 202     4083   3958   3730     99    366   -428       C  
ATOM   1634  CG  PRO A 202     -11.176 -13.198 -21.251  1.00 30.35           C  
ANISOU 1634  CG  PRO A 202     4454   3479   3595   -106    123   -378       C  
ATOM   1635  CD  PRO A 202     -11.472 -11.719 -21.236  1.00 31.80           C  
ANISOU 1635  CD  PRO A 202     4492   3812   3777    -68    218   -401       C  
ATOM   1636  N   ASN A 203      -9.527 -10.885 -18.093  1.00 30.89           N  
ANISOU 1636  N   ASN A 203     3977   4196   3563   -128    448   -383       N  
ATOM   1637  CA  ASN A 203      -8.634 -10.369 -17.061  1.00 32.11           C  
ANISOU 1637  CA  ASN A 203     4221   4250   3726   -291    405   -185       C  
ATOM   1638  C   ASN A 203      -9.316 -10.268 -15.689  1.00 30.10           C  
ANISOU 1638  C   ASN A 203     3842   4032   3561   -311    445   -104       C  
ATOM   1639  O   ASN A 203      -8.634 -10.404 -14.674  1.00 30.49           O  
ANISOU 1639  O   ASN A 203     3890   4199   3494   -536    463   -201       O  
ATOM   1640  CB  ASN A 203      -8.064  -8.995 -17.451  1.00 32.70           C  
ANISOU 1640  CB  ASN A 203     4167   4439   3816   -399    530   -253       C  
ATOM   1641  CG  ASN A 203      -7.137  -9.078 -18.619  1.00 36.53           C  
ANISOU 1641  CG  ASN A 203     4656   5001   4220   -428    588    164       C  
ATOM   1642  OD1 ASN A 203      -6.528 -10.137 -18.873  1.00 39.69           O  
ANISOU 1642  OD1 ASN A 203     4977   5647   4455   -229    847   -164       O  
ATOM   1643  ND2 ASN A 203      -6.984  -7.953 -19.331  1.00 40.81           N  
ANISOU 1643  ND2 ASN A 203     5167   5890   4449   -817    836    750       N  
ATOM   1644  N   ALA A 204     -10.614  -9.980 -15.661  1.00 29.62           N  
ANISOU 1644  N   ALA A 204     3835   3832   3584   -276    328   -109       N  
ATOM   1645  CA  ALA A 204     -11.399  -9.997 -14.371  1.00 28.78           C  
ANISOU 1645  CA  ALA A 204     3663   3807   3465   -186    229   -113       C  
ATOM   1646  C   ALA A 204     -11.219 -11.307 -13.612  1.00 28.57           C  
ANISOU 1646  C   ALA A 204     3496   3829   3527   -220    212   -230       C  
ATOM   1647  O   ALA A 204     -10.909 -11.270 -12.420  1.00 27.78           O  
ANISOU 1647  O   ALA A 204     3619   3865   3070   -211    332   -354       O  
ATOM   1648  CB  ALA A 204     -12.912  -9.712 -14.591  1.00 28.83           C  
ANISOU 1648  CB  ALA A 204     3697   3647   3608   -208    395    -41       C  
ATOM   1649  N   SER A 205     -11.416 -12.467 -14.270  1.00 26.98           N  
ANISOU 1649  N   SER A 205     3280   3569   3402   -124    428   -343       N  
ATOM   1650  CA  SER A 205     -11.253 -13.734 -13.539  1.00 26.94           C  
ANISOU 1650  CA  SER A 205     3136   3707   3392   -137    177   -319       C  
ATOM   1651  C   SER A 205      -9.824 -14.033 -13.249  1.00 28.36           C  
ANISOU 1651  C   SER A 205     3434   3817   3524   -176    154   -286       C  
ATOM   1652  O   SER A 205      -9.553 -14.662 -12.229  1.00 27.58           O  
ANISOU 1652  O   SER A 205     2945   3920   3612    -35    222   -137       O  
ATOM   1653  CB  SER A 205     -11.867 -14.941 -14.247  1.00 26.14           C  
ANISOU 1653  CB  SER A 205     3347   3264   3318   -140    177   -269       C  
ATOM   1654  OG  SER A 205     -13.287 -14.772 -14.392  1.00 25.40           O  
ANISOU 1654  OG  SER A 205     3103   3692   2855   -270    537   -512       O  
ATOM   1655  N   LYS A 206      -8.920 -13.569 -14.133  1.00 29.76           N  
ANISOU 1655  N   LYS A 206     3445   4310   3549   -246    257   -418       N  
ATOM   1656  CA  LYS A 206      -7.459 -13.742 -13.871  1.00 31.66           C  
ANISOU 1656  CA  LYS A 206     3828   4468   3733   -222    112   -296       C  
ATOM   1657  C   LYS A 206      -7.088 -12.976 -12.594  1.00 31.19           C  
ANISOU 1657  C   LYS A 206     3799   4246   3803   -217     96   -278       C  
ATOM   1658  O   LYS A 206      -6.333 -13.472 -11.758  1.00 33.77           O  
ANISOU 1658  O   LYS A 206     3823   4750   4258   -235    215   -224       O  
ATOM   1659  CB  LYS A 206      -6.605 -13.359 -15.070  1.00 31.74           C  
ANISOU 1659  CB  LYS A 206     3914   4330   3814   -437    234   -234       C  
ATOM   1660  CG  LYS A 206      -6.836 -14.339 -16.248  1.00 32.05           C  
ANISOU 1660  CG  LYS A 206     4266   4831   3077   -547    130   -130       C  
ATOM   1661  CD  LYS A 206      -6.018 -13.979 -17.523  1.00 34.47           C  
ANISOU 1661  CD  LYS A 206     4260   5017   3820   -189    401   -232       C  
ATOM   1662  CE  LYS A 206      -6.456 -14.835 -18.724  1.00 36.69           C  
ANISOU 1662  CE  LYS A 206     5272   4924   3742   -342    437     27       C  
ATOM   1663  NZ  LYS A 206      -6.041 -14.193 -20.039  1.00 37.38           N  
ANISOU 1663  NZ  LYS A 206     5011   5185   4005    105    874    -64       N  
ATOM   1664  N   LYS A 207      -7.678 -11.800 -12.421  1.00 30.48           N  
ANISOU 1664  N   LYS A 207     3593   4146   3841   -319    291   -345       N  
ATOM   1665  CA  LYS A 207      -7.425 -10.997 -11.219  1.00 29.84           C  
ANISOU 1665  CA  LYS A 207     3725   4001   3610   -269     82   -304       C  
ATOM   1666  C   LYS A 207      -8.064 -11.633  -9.999  1.00 28.44           C  
ANISOU 1666  C   LYS A 207     3281   3852   3672   -368    168   -321       C  
ATOM   1667  O   LYS A 207      -7.410 -11.772  -8.955  1.00 27.92           O  
ANISOU 1667  O   LYS A 207     2962   3885   3758   -559    320   -324       O  
ATOM   1668  CB  LYS A 207      -7.914  -9.560 -11.397  1.00 30.80           C  
ANISOU 1668  CB  LYS A 207     3949   3930   3823   -368    251   -410       C  
ATOM   1669  CG  LYS A 207      -7.629  -8.703 -10.118  1.00 34.95           C  
ANISOU 1669  CG  LYS A 207     4752   4592   3935   -189    117   -531       C  
ATOM   1670  CD  LYS A 207      -6.961  -7.372 -10.388  1.00 38.71           C  
ANISOU 1670  CD  LYS A 207     4873   5115   4719   -497    404   -839       C  
ATOM   1671  CE  LYS A 207      -6.761  -6.571  -9.062  1.00 42.55           C  
ANISOU 1671  CE  LYS A 207     5051   6545   4572   -450     -4  -1050       C  
ATOM   1672  NZ  LYS A 207      -5.343  -6.565  -8.516  1.00 41.41           N  
ANISOU 1672  NZ  LYS A 207     5378   6448   3906   -386     49   -955       N  
ATOM   1673  N   TYR A 208      -9.332 -12.079 -10.086  1.00 28.65           N  
ANISOU 1673  N   TYR A 208     3351   3975   3557   -434    165   -273       N  
ATOM   1674  CA  TYR A 208      -9.876 -12.823  -8.937  1.00 27.35           C  
ANISOU 1674  CA  TYR A 208     3123   3849   3419   -276    167   -293       C  
ATOM   1675  C   TYR A 208      -9.021 -14.038  -8.579  1.00 28.47           C  
ANISOU 1675  C   TYR A 208     3339   3999   3479   -225    160   -377       C  
ATOM   1676  O   TYR A 208      -8.848 -14.381  -7.394  1.00 28.40           O  
ANISOU 1676  O   TYR A 208     2998   4234   3559   -363    271   -285       O  
ATOM   1677  CB  TYR A 208     -11.271 -13.321  -9.250  1.00 26.40           C  
ANISOU 1677  CB  TYR A 208     2948   3688   3395   -294    375   -329       C  
ATOM   1678  CG  TYR A 208     -12.427 -12.368  -9.000  1.00 26.05           C  
ANISOU 1678  CG  TYR A 208     3479   3287   3132    -64    -15   -262       C  
ATOM   1679  CD1 TYR A 208     -12.892 -12.111  -7.683  1.00 24.40           C  
ANISOU 1679  CD1 TYR A 208     2977   3137   3153      7    656   -355       C  
ATOM   1680  CD2 TYR A 208     -13.116 -11.816 -10.070  1.00 24.14           C  
ANISOU 1680  CD2 TYR A 208     3330   3036   2806   -132   -114   -312       C  
ATOM   1681  CE1 TYR A 208     -14.004 -11.279  -7.466  1.00 22.85           C  
ANISOU 1681  CE1 TYR A 208     3146   2898   2637   -109    287   -155       C  
ATOM   1682  CE2 TYR A 208     -14.240 -11.010  -9.883  1.00 21.39           C  
ANISOU 1682  CE2 TYR A 208     2904   2568   2654   -272    132   -215       C  
ATOM   1683  CZ  TYR A 208     -14.677 -10.734  -8.544  1.00 21.02           C  
ANISOU 1683  CZ  TYR A 208     2693   2730   2561    -92    310     18       C  
ATOM   1684  OH  TYR A 208     -15.783  -9.990  -8.343  1.00 23.12           O  
ANISOU 1684  OH  TYR A 208     2964   3048   2769     81     91   -220       O  
ATOM   1685  N   ASP A 209      -8.473 -14.723  -9.580  1.00 27.96           N  
ANISOU 1685  N   ASP A 209     3244   4024   3354     -3    188   -566       N  
ATOM   1686  CA  ASP A 209      -7.689 -15.926  -9.273  1.00 29.10           C  
ANISOU 1686  CA  ASP A 209     3562   4106   3386     56    -37   -463       C  
ATOM   1687  C   ASP A 209      -6.405 -15.582  -8.498  1.00 30.76           C  
ANISOU 1687  C   ASP A 209     3815   4258   3614     85    -32   -325       C  
ATOM   1688  O   ASP A 209      -5.899 -16.437  -7.756  1.00 29.19           O  
ANISOU 1688  O   ASP A 209     3695   4047   3346    147    -48   -321       O  
ATOM   1689  CB  ASP A 209      -7.275 -16.616 -10.573  1.00 28.93           C  
ANISOU 1689  CB  ASP A 209     3282   4029   3681    205    161   -671       C  
ATOM   1690  CG  ASP A 209      -6.749 -18.007 -10.335  1.00 31.17           C  
ANISOU 1690  CG  ASP A 209     3670   4339   3833    107     98   -429       C  
ATOM   1691  OD1 ASP A 209      -7.346 -18.844  -9.606  1.00 33.30           O  
ANISOU 1691  OD1 ASP A 209     3723   5203   3727   -366    -90   -109       O  
ATOM   1692  OD2 ASP A 209      -5.697 -18.255 -10.906  1.00 33.02           O  
ANISOU 1692  OD2 ASP A 209     3473   4678   4395    753    202   -829       O  
ATOM   1693  N   GLN A 210      -5.883 -14.358  -8.682  1.00 32.34           N  
ANISOU 1693  N   GLN A 210     3929   4508   3847    -59    -43   -191       N  
ATOM   1694  CA AGLN A 210      -4.730 -13.977  -7.890  0.50 34.30           C  
ANISOU 1694  CA AGLN A 210     4233   4783   4016    -86   -101   -156       C  
ATOM   1695  CA BGLN A 210      -4.730 -13.823  -7.918  0.50 33.49           C  
ANISOU 1695  CA BGLN A 210     4080   4665   3978    -35    -48   -150       C  
ATOM   1696  C   GLN A 210      -5.164 -13.611  -6.475  1.00 34.67           C  
ANISOU 1696  C   GLN A 210     4251   4847   4072    -67   -107    -60       C  
ATOM   1697  O   GLN A 210      -4.468 -14.041  -5.532  1.00 37.47           O  
ANISOU 1697  O   GLN A 210     4504   5419   4311    -83      4    -35       O  
ATOM   1698  CB AGLN A 210      -3.860 -12.907  -8.581  0.50 34.87           C  
ANISOU 1698  CB AGLN A 210     4244   4833   4171   -112   -146    -97       C  
ATOM   1699  CB BGLN A 210      -4.184 -12.472  -8.502  0.50 33.00           C  
ANISOU 1699  CB BGLN A 210     4001   4542   3993     63    -67    -85       C  
ATOM   1700  CG AGLN A 210      -3.092 -13.463  -9.814  0.50 37.05           C  
ANISOU 1700  CG AGLN A 210     4772   5065   4240    -31   -282   -103       C  
ATOM   1701  CG BGLN A 210      -3.781 -12.488 -10.005  0.50 32.08           C  
ANISOU 1701  CG BGLN A 210     3631   4451   4107    217     72      9       C  
ATOM   1702  CD AGLN A 210      -2.575 -14.880  -9.605  0.50 39.87           C  
ANISOU 1702  CD AGLN A 210     5188   5334   4626    146   -544   -113       C  
ATOM   1703  CD BGLN A 210      -3.063 -11.215 -10.519  0.50 32.95           C  
ANISOU 1703  CD BGLN A 210     3680   4565   4273    422    242    234       C  
ATOM   1704  OE1AGLN A 210      -2.378 -15.324  -8.467  0.50 41.54           O  
ANISOU 1704  OE1AGLN A 210     5231   5738   4811     98  -1220   -125       O  
ATOM   1705  OE1BGLN A 210      -3.402 -10.080 -10.158  0.50 34.24           O  
ANISOU 1705  OE1BGLN A 210     4182   4323   4503    113    582    443       O  
ATOM   1706  NE2AGLN A 210      -2.368 -15.604 -10.699  0.50 41.70           N  
ANISOU 1706  NE2AGLN A 210     5475   5629   4738    367   -729   -127       N  
ATOM   1707  NE2BGLN A 210      -2.065 -11.415 -11.382  0.50 32.82           N  
ANISOU 1707  NE2BGLN A 210     3951   4800   3716    404    177    267       N  
ATOM   1708  N   ILE A 211      -6.312 -12.933  -6.305  1.00 33.24           N  
ANISOU 1708  N   ILE A 211     4067   4647   3915   -235    -22   -316       N  
ATOM   1709  CA  ILE A 211      -6.748 -12.480  -4.968  1.00 33.07           C  
ANISOU 1709  CA  ILE A 211     4122   4456   3986   -335   -145   -335       C  
ATOM   1710  C   ILE A 211      -7.270 -13.546  -4.014  1.00 31.87           C  
ANISOU 1710  C   ILE A 211     3911   4377   3821   -309   -117   -351       C  
ATOM   1711  O   ILE A 211      -7.119 -13.401  -2.802  1.00 32.28           O  
ANISOU 1711  O   ILE A 211     4134   4499   3631   -669   -292   -546       O  
ATOM   1712  CB  ILE A 211      -7.744 -11.296  -4.991  1.00 33.15           C  
ANISOU 1712  CB  ILE A 211     4203   4341   4050   -354   -217   -408       C  
ATOM   1713  CG1 ILE A 211      -9.187 -11.823  -5.152  1.00 32.79           C  
ANISOU 1713  CG1 ILE A 211     4060   4430   3966    -20   -570   -790       C  
ATOM   1714  CG2 ILE A 211      -7.276 -10.189  -5.999  1.00 35.35           C  
ANISOU 1714  CG2 ILE A 211     4758   4648   4024   -346    -16   -455       C  
ATOM   1715  CD1 ILE A 211     -10.247 -11.030  -4.588  1.00 36.93           C  
ANISOU 1715  CD1 ILE A 211     4785   5039   4208      0   -305   -800       C  
ATOM   1716  N   TYR A 212      -7.853 -14.630  -4.515  1.00 28.11           N  
ANISOU 1716  N   TYR A 212     3375   3856   3446   -160   -106   -369       N  
ATOM   1717  CA  TYR A 212      -8.378 -15.614  -3.616  1.00 27.10           C  
ANISOU 1717  CA  TYR A 212     3142   3721   3431    -66   -123   -245       C  
ATOM   1718  C   TYR A 212      -7.313 -16.561  -3.062  1.00 28.16           C  
ANISOU 1718  C   TYR A 212     3144   3988   3565    -41    -78   -214       C  
ATOM   1719  O   TYR A 212      -6.419 -16.977  -3.796  1.00 29.81           O  
ANISOU 1719  O   TYR A 212     3169   4424   3734     -6     96    -43       O  
ATOM   1720  CB  TYR A 212      -9.367 -16.462  -4.390  1.00 26.93           C  
ANISOU 1720  CB  TYR A 212     3095   3780   3355      4   -177   -295       C  
ATOM   1721  CG  TYR A 212     -10.709 -15.782  -4.509  1.00 25.94           C  
ANISOU 1721  CG  TYR A 212     3217   3333   3306     96    131    -82       C  
ATOM   1722  CD1 TYR A 212     -11.398 -15.370  -3.332  1.00 24.56           C  
ANISOU 1722  CD1 TYR A 212     3148   2861   3324    -51    518   -150       C  
ATOM   1723  CD2 TYR A 212     -11.328 -15.611  -5.752  1.00 22.90           C  
ANISOU 1723  CD2 TYR A 212     3048   2784   2869     21    139   -310       C  
ATOM   1724  CE1 TYR A 212     -12.676 -14.814  -3.423  1.00 23.42           C  
ANISOU 1724  CE1 TYR A 212     3155   2741   3000    240    415    154       C  
ATOM   1725  CE2 TYR A 212     -12.599 -15.011  -5.857  1.00 21.55           C  
ANISOU 1725  CE2 TYR A 212     3163   2315   2710   -151    492   -586       C  
ATOM   1726  CZ  TYR A 212     -13.272 -14.636  -4.670  1.00 24.42           C  
ANISOU 1726  CZ  TYR A 212     3349   2992   2936    100    334   -294       C  
ATOM   1727  OH  TYR A 212     -14.544 -14.116  -4.741  1.00 23.73           O  
ANISOU 1727  OH  TYR A 212     3430   3043   2541    -31    -85    -42       O  
ATOM   1728  N   GLN A 213      -7.432 -16.955  -1.804  1.00 27.59           N  
ANISOU 1728  N   GLN A 213     2886   3990   3605   -125    171    -24       N  
ATOM   1729  CA  GLN A 213      -6.582 -18.012  -1.224  1.00 29.20           C  
ANISOU 1729  CA  GLN A 213     3303   3872   3919   -190      4   -107       C  
ATOM   1730  C   GLN A 213      -6.790 -19.410  -1.790  1.00 30.86           C  
ANISOU 1730  C   GLN A 213     3586   4040   4099    -27    -78   -225       C  
ATOM   1731  O   GLN A 213      -5.860 -20.222  -1.751  1.00 32.97           O  
ANISOU 1731  O   GLN A 213     3811   4237   4476    -20   -184   -147       O  
ATOM   1732  CB  GLN A 213      -6.781 -18.103   0.293  1.00 31.01           C  
ANISOU 1732  CB  GLN A 213     3700   4086   3996   -300    -77   -170       C  
ATOM   1733  CG  GLN A 213      -6.435 -16.820   0.984  1.00 32.91           C  
ANISOU 1733  CG  GLN A 213     4042   4101   4361   -207   -301   -474       C  
ATOM   1734  CD  GLN A 213      -5.017 -16.378   0.588  1.00 36.65           C  
ANISOU 1734  CD  GLN A 213     4659   4681   4585   -376   -139   -172       C  
ATOM   1735  OE1 GLN A 213      -4.844 -15.479  -0.243  1.00 38.94           O  
ANISOU 1735  OE1 GLN A 213     4998   4550   5246   -594   -505   -129       O  
ATOM   1736  NE2 GLN A 213      -4.007 -17.058   1.132  1.00 37.01           N  
ANISOU 1736  NE2 GLN A 213     4289   5061   4712   -180   -517   -427       N  
ATOM   1737  N   ASN A 214      -8.013 -19.704  -2.266  1.00 31.55           N  
ANISOU 1737  N   ASN A 214     3561   4046   4377     -8   -169   -200       N  
ATOM   1738  CA  ASN A 214      -8.368 -21.049  -2.764  1.00 32.55           C  
ANISOU 1738  CA  ASN A 214     3765   4266   4335    -38   -133   -250       C  
ATOM   1739  C   ASN A 214      -9.307 -20.954  -3.980  1.00 32.63           C  
ANISOU 1739  C   ASN A 214     3848   4316   4233    -53    -19   -249       C  
ATOM   1740  O   ASN A 214     -10.484 -21.152  -3.840  1.00 33.02           O  
ANISOU 1740  O   ASN A 214     3786   4521   4237   -290    -17   -158       O  
ATOM   1741  CB  ASN A 214      -8.950 -21.936  -1.626  1.00 33.50           C  
ANISOU 1741  CB  ASN A 214     3835   4319   4574    -73   -140   -245       C  
ATOM   1742  CG  ASN A 214      -9.220 -23.408  -2.083  1.00 38.68           C  
ANISOU 1742  CG  ASN A 214     4582   4926   5186    -44     31     86       C  
ATOM   1743  OD1 ASN A 214      -8.966 -23.788  -3.233  1.00 44.40           O  
ANISOU 1743  OD1 ASN A 214     5304   5846   5719    206    -46   -113       O  
ATOM   1744  ND2 ASN A 214      -9.743 -24.218  -1.175  1.00 43.59           N  
ANISOU 1744  ND2 ASN A 214     4776   5638   6147   -266     -6    715       N  
ATOM   1745  N   SER A 215      -8.781 -20.623  -5.156  1.00 32.44           N  
ANISOU 1745  N   SER A 215     3905   4488   3930    -15     52   -344       N  
ATOM   1746  CA  SER A 215      -9.595 -20.505  -6.371  1.00 31.02           C  
ANISOU 1746  CA  SER A 215     3627   4367   3791    114    -19   -551       C  
ATOM   1747  C   SER A 215      -9.067 -21.440  -7.479  1.00 32.12           C  
ANISOU 1747  C   SER A 215     3777   4521   3905    136      0   -489       C  
ATOM   1748  O   SER A 215      -7.860 -21.805  -7.510  1.00 32.67           O  
ANISOU 1748  O   SER A 215     3631   4689   4089    175    -85   -716       O  
ATOM   1749  CB  SER A 215      -9.654 -19.064  -6.886  1.00 30.88           C  
ANISOU 1749  CB  SER A 215     3575   4356   3799    -57    202   -487       C  
ATOM   1750  OG  SER A 215      -8.355 -18.511  -7.113  1.00 33.40           O  
ANISOU 1750  OG  SER A 215     4096   4830   3763    -50   -292   -703       O  
ATOM   1751  N   THR A 216      -9.979 -21.870  -8.355  1.00 30.29           N  
ANISOU 1751  N   THR A 216     3690   4100   3717    135     65   -554       N  
ATOM   1752  CA  THR A 216      -9.593 -22.607  -9.541  1.00 30.49           C  
ANISOU 1752  CA  THR A 216     3993   4079   3512    142     82   -375       C  
ATOM   1753  C   THR A 216     -10.193 -21.860 -10.700  1.00 30.29           C  
ANISOU 1753  C   THR A 216     3975   3877   3656    116    176   -328       C  
ATOM   1754  O   THR A 216     -11.415 -21.594 -10.704  1.00 31.32           O  
ANISOU 1754  O   THR A 216     4221   4226   3452    102    328   -311       O  
ATOM   1755  CB  THR A 216     -10.136 -24.062  -9.474  1.00 30.92           C  
ANISOU 1755  CB  THR A 216     4238   3967   3541    266     27   -290       C  
ATOM   1756  OG1 THR A 216      -9.783 -24.697  -8.191  1.00 33.80           O  
ANISOU 1756  OG1 THR A 216     4648   4303   3893    335   -173   -266       O  
ATOM   1757  CG2 THR A 216      -9.579 -24.894 -10.602  1.00 31.69           C  
ANISOU 1757  CG2 THR A 216     4513   4028   3499    577    170   -456       C  
ATOM   1758  N   LEU A 217      -9.349 -21.602 -11.714  1.00 30.12           N  
ANISOU 1758  N   LEU A 217     3975   3779   3690   -119    113   -316       N  
ATOM   1759  CA  LEU A 217      -9.698 -20.792 -12.866  1.00 29.60           C  
ANISOU 1759  CA  LEU A 217     3784   3865   3596   -166    147   -402       C  
ATOM   1760  C   LEU A 217      -9.884 -21.735 -14.052  1.00 30.02           C  
ANISOU 1760  C   LEU A 217     3834   3919   3654    -40    108   -350       C  
ATOM   1761  O   LEU A 217      -9.037 -22.638 -14.254  1.00 31.27           O  
ANISOU 1761  O   LEU A 217     4022   4136   3720    -73    242   -740       O  
ATOM   1762  CB  LEU A 217      -8.571 -19.790 -13.175  1.00 30.18           C  
ANISOU 1762  CB  LEU A 217     3908   3823   3733   -288    130   -421       C  
ATOM   1763  CG  LEU A 217      -8.763 -18.945 -14.436  1.00 29.99           C  
ANISOU 1763  CG  LEU A 217     3421   4016   3956   -375    589   -135       C  
ATOM   1764  CD1 LEU A 217     -10.032 -18.053 -14.324  1.00 31.40           C  
ANISOU 1764  CD1 LEU A 217     3867   3797   4267   -211    968   -150       C  
ATOM   1765  CD2 LEU A 217      -7.500 -18.068 -14.768  1.00 34.98           C  
ANISOU 1765  CD2 LEU A 217     4221   4536   4533  -1154    650   -220       C  
ATOM   1766  N   HIS A 218     -11.017 -21.557 -14.755  1.00 29.39           N  
ANISOU 1766  N   HIS A 218     3665   3931   3570     -4    111   -395       N  
ATOM   1767  CA  HIS A 218     -11.351 -22.259 -15.981  1.00 29.03           C  
ANISOU 1767  CA  HIS A 218     3559   3841   3628    -24    111   -229       C  
ATOM   1768  C   HIS A 218     -11.611 -21.268 -17.091  1.00 29.04           C  
ANISOU 1768  C   HIS A 218     3580   3837   3614    -36    175   -167       C  
ATOM   1769  O   HIS A 218     -12.635 -20.603 -17.078  1.00 29.27           O  
ANISOU 1769  O   HIS A 218     3761   3945   3416     28    648    -88       O  
ATOM   1770  CB  HIS A 218     -12.615 -23.104 -15.749  1.00 29.55           C  
ANISOU 1770  CB  HIS A 218     3686   3920   3619    -49    178    -92       C  
ATOM   1771  CG  HIS A 218     -12.458 -24.104 -14.661  1.00 30.24           C  
ANISOU 1771  CG  HIS A 218     3699   3905   3884    210     70     28       C  
ATOM   1772  ND1 HIS A 218     -11.867 -25.339 -14.870  1.00 30.00           N  
ANISOU 1772  ND1 HIS A 218     3422   3900   4073    193    -76     69       N  
ATOM   1773  CD2 HIS A 218     -12.769 -24.040 -13.337  1.00 27.69           C  
ANISOU 1773  CD2 HIS A 218     2817   3819   3884    404     39    283       C  
ATOM   1774  CE1 HIS A 218     -11.856 -26.004 -13.726  1.00 32.26           C  
ANISOU 1774  CE1 HIS A 218     3761   4434   4059    503   -266    247       C  
ATOM   1775  NE2 HIS A 218     -12.409 -25.244 -12.784  1.00 31.25           N  
ANISOU 1775  NE2 HIS A 218     3613   4123   4135    679   -354    294       N  
ATOM   1776  N   LEU A 219     -10.684 -21.179 -18.052  1.00 29.61           N  
ANISOU 1776  N   LEU A 219     3709   3872   3667     -2     82   -202       N  
ATOM   1777  CA  LEU A 219     -10.815 -20.322 -19.221  1.00 30.72           C  
ANISOU 1777  CA  LEU A 219     3746   4007   3918    -28    -31   -209       C  
ATOM   1778  C   LEU A 219     -11.390 -21.201 -20.309  1.00 30.71           C  
ANISOU 1778  C   LEU A 219     3907   3941   3817     96    -55   -282       C  
ATOM   1779  O   LEU A 219     -10.752 -22.221 -20.666  1.00 31.99           O  
ANISOU 1779  O   LEU A 219     3952   4134   4069    311   -327   -359       O  
ATOM   1780  CB  LEU A 219      -9.452 -19.691 -19.632  1.00 29.58           C  
ANISOU 1780  CB  LEU A 219     3614   3860   3762   -183     50   -192       C  
ATOM   1781  CG  LEU A 219      -8.838 -18.717 -18.615  1.00 32.77           C  
ANISOU 1781  CG  LEU A 219     3791   4412   4247   -135    -11   -148       C  
ATOM   1782  CD1 LEU A 219      -7.381 -18.300 -19.105  1.00 33.58           C  
ANISOU 1782  CD1 LEU A 219     4103   4515   4140   -518    562   -474       C  
ATOM   1783  CD2 LEU A 219      -9.725 -17.481 -18.326  1.00 30.25           C  
ANISOU 1783  CD2 LEU A 219     3076   4616   3801   -313    179   -436       C  
ATOM   1784  N   ILE A 220     -12.619 -20.894 -20.769  1.00 28.93           N  
ANISOU 1784  N   ILE A 220     3779   3752   3462    -60   -130   -200       N  
ATOM   1785  CA  ILE A 220     -13.340 -21.749 -21.753  1.00 29.40           C  
ANISOU 1785  CA  ILE A 220     3918   3833   3421   -131    -10   -179       C  
ATOM   1786  C   ILE A 220     -13.033 -21.224 -23.145  1.00 30.14           C  
ANISOU 1786  C   ILE A 220     3964   3925   3561     -7     61   -206       C  
ATOM   1787  O   ILE A 220     -13.424 -20.132 -23.498  1.00 28.53           O  
ANISOU 1787  O   ILE A 220     3581   3786   3471     83     48   -176       O  
ATOM   1788  CB  ILE A 220     -14.870 -21.786 -21.501  1.00 28.08           C  
ANISOU 1788  CB  ILE A 220     3677   3737   3253   -317    -99   -240       C  
ATOM   1789  CG1 ILE A 220     -15.198 -22.175 -20.023  1.00 30.73           C  
ANISOU 1789  CG1 ILE A 220     4506   3812   3357   -134   -132     -2       C  
ATOM   1790  CG2 ILE A 220     -15.564 -22.849 -22.414  1.00 25.81           C  
ANISOU 1790  CG2 ILE A 220     3594   3614   2599   -417   -453   -487       C  
ATOM   1791  CD1 ILE A 220     -14.520 -23.519 -19.484  1.00 31.59           C  
ANISOU 1791  CD1 ILE A 220     3816   4247   3939    -68   -186    118       C  
ATOM   1792  N   GLU A 221     -12.236 -21.996 -23.887  1.00 31.51           N  
ANISOU 1792  N   GLU A 221     4099   4214   3657    127    298   -224       N  
ATOM   1793  CA  GLU A 221     -11.716 -21.547 -25.168  1.00 32.97           C  
ANISOU 1793  CA  GLU A 221     4273   4431   3822    199    293   -158       C  
ATOM   1794  C   GLU A 221     -12.883 -21.292 -26.142  1.00 31.76           C  
ANISOU 1794  C   GLU A 221     4065   4276   3727    240    369   -256       C  
ATOM   1795  O   GLU A 221     -13.736 -22.171 -26.351  1.00 32.99           O  
ANISOU 1795  O   GLU A 221     4158   4532   3845    249    143   -417       O  
ATOM   1796  CB  GLU A 221     -10.702 -22.588 -25.692  1.00 33.60           C  
ANISOU 1796  CB  GLU A 221     4432   4597   3736    286    432   -264       C  
ATOM   1797  CG  GLU A 221     -10.213 -22.364 -27.115  1.00 41.73           C  
ANISOU 1797  CG  GLU A 221     5269   5840   4747      7    714    131       C  
ATOM   1798  CD  GLU A 221      -9.499 -21.036 -27.261  1.00 46.86           C  
ANISOU 1798  CD  GLU A 221     5744   6409   5649     -9    807    -37       C  
ATOM   1799  OE1 GLU A 221      -8.715 -20.665 -26.360  1.00 47.66           O  
ANISOU 1799  OE1 GLU A 221     5453   7396   5258    330   1142   -573       O  
ATOM   1800  OE2 GLU A 221      -9.733 -20.360 -28.287  1.00 52.50           O  
ANISOU 1800  OE2 GLU A 221     6417   7317   6212    -14    967    411       O  
ATOM   1801  N   GLY A 222     -12.932 -20.086 -26.689  1.00 30.43           N  
ANISOU 1801  N   GLY A 222     3891   4008   3661    506    342   -360       N  
ATOM   1802  CA  GLY A 222     -13.940 -19.741 -27.667  1.00 30.85           C  
ANISOU 1802  CA  GLY A 222     4087   4080   3552    213    163   -228       C  
ATOM   1803  C   GLY A 222     -15.268 -19.196 -27.113  1.00 30.18           C  
ANISOU 1803  C   GLY A 222     4085   3845   3536    226     39   -213       C  
ATOM   1804  O   GLY A 222     -16.045 -18.633 -27.882  1.00 30.28           O  
ANISOU 1804  O   GLY A 222     4443   3790   3272     59   -148   -182       O  
ATOM   1805  N   ALA A 223     -15.547 -19.377 -25.809  1.00 28.69           N  
ANISOU 1805  N   ALA A 223     4092   3555   3251     89    -19   -464       N  
ATOM   1806  CA  ALA A 223     -16.854 -19.031 -25.205  1.00 28.40           C  
ANISOU 1806  CA  ALA A 223     4131   3427   3229     12    -38   -357       C  
ATOM   1807  C   ALA A 223     -17.032 -17.508 -25.108  1.00 28.91           C  
ANISOU 1807  C   ALA A 223     4107   3629   3247     50     20   -366       C  
ATOM   1808  O   ALA A 223     -16.076 -16.785 -24.959  1.00 29.88           O  
ANISOU 1808  O   ALA A 223     4382   3771   3199    170    -67   -369       O  
ATOM   1809  CB  ALA A 223     -16.974 -19.642 -23.827  1.00 28.05           C  
ANISOU 1809  CB  ALA A 223     4047   3350   3257    -34    253   -463       C  
ATOM   1810  N   ASP A 224     -18.275 -17.075 -25.206  1.00 29.21           N  
ANISOU 1810  N   ASP A 224     4078   3660   3359    129      7   -374       N  
ATOM   1811  CA  ASP A 224     -18.713 -15.697 -25.117  1.00 29.03           C  
ANISOU 1811  CA  ASP A 224     4006   3637   3386    234    -12   -396       C  
ATOM   1812  C   ASP A 224     -19.217 -15.384 -23.693  1.00 28.68           C  
ANISOU 1812  C   ASP A 224     3977   3518   3402    273     87   -325       C  
ATOM   1813  O   ASP A 224     -19.193 -16.249 -22.800  1.00 28.86           O  
ANISOU 1813  O   ASP A 224     4114   3610   3241    262    169   -530       O  
ATOM   1814  CB  ASP A 224     -19.803 -15.464 -26.150  1.00 30.31           C  
ANISOU 1814  CB  ASP A 224     4256   3885   3374    181    -34   -413       C  
ATOM   1815  CG  ASP A 224     -21.021 -16.339 -25.947  1.00 32.32           C  
ANISOU 1815  CG  ASP A 224     4401   4057   3821    216   -187   -370       C  
ATOM   1816  OD1 ASP A 224     -20.975 -17.392 -25.284  1.00 36.08           O  
ANISOU 1816  OD1 ASP A 224     5150   4459   4096    357   -227   -480       O  
ATOM   1817  OD2 ASP A 224     -22.075 -15.973 -26.502  1.00 38.77           O  
ANISOU 1817  OD2 ASP A 224     5439   4371   4921    471   -426   -451       O  
ATOM   1818  N   HIS A 225     -19.721 -14.167 -23.498  1.00 27.80           N  
ANISOU 1818  N   HIS A 225     3975   3338   3249    243    134   -577       N  
ATOM   1819  CA  HIS A 225     -20.108 -13.703 -22.156  1.00 27.63           C  
ANISOU 1819  CA  HIS A 225     4007   3209   3282    343    213   -370       C  
ATOM   1820  C   HIS A 225     -21.169 -14.557 -21.493  1.00 28.59           C  
ANISOU 1820  C   HIS A 225     4003   3337   3521    354     69   -364       C  
ATOM   1821  O   HIS A 225     -21.099 -14.800 -20.274  1.00 28.58           O  
ANISOU 1821  O   HIS A 225     4038   3275   3543    282    151   -182       O  
ATOM   1822  CB  HIS A 225     -20.630 -12.266 -22.245  1.00 26.63           C  
ANISOU 1822  CB  HIS A 225     4022   3064   3031    413    257   -371       C  
ATOM   1823  CG  HIS A 225     -20.904 -11.658 -20.892  1.00 26.14           C  
ANISOU 1823  CG  HIS A 225     4181   2859   2890    257    149   -495       C  
ATOM   1824  ND1 HIS A 225     -19.951 -11.624 -19.891  1.00 27.28           N  
ANISOU 1824  ND1 HIS A 225     3860   3376   3126     66    281   -264       N  
ATOM   1825  CD2 HIS A 225     -22.021 -11.102 -20.374  1.00 27.58           C  
ANISOU 1825  CD2 HIS A 225     3624   3635   3220     15     26   -196       C  
ATOM   1826  CE1 HIS A 225     -20.458 -11.005 -18.825  1.00 26.91           C  
ANISOU 1826  CE1 HIS A 225     3653   3445   3124    225   -168   -854       C  
ATOM   1827  NE2 HIS A 225     -21.716 -10.682 -19.091  1.00 25.90           N  
ANISOU 1827  NE2 HIS A 225     3731   3075   3033    -58    -99     65       N  
ATOM   1828  N   CYS A 226     -22.164 -15.022 -22.269  1.00 28.67           N  
ANISOU 1828  N   CYS A 226     3933   3369   3589    226     23   -512       N  
ATOM   1829  CA  CYS A 226     -23.236 -15.792 -21.667  1.00 30.72           C  
ANISOU 1829  CA  CYS A 226     4125   3722   3825    153   -129   -451       C  
ATOM   1830  C   CYS A 226     -23.069 -17.305 -21.764  1.00 28.80           C  
ANISOU 1830  C   CYS A 226     3886   3627   3427    149   -230   -348       C  
ATOM   1831  O   CYS A 226     -23.994 -18.039 -21.410  1.00 29.34           O  
ANISOU 1831  O   CYS A 226     3940   4004   3203    180   -117   -482       O  
ATOM   1832  CB  CYS A 226     -24.601 -15.365 -22.246  1.00 31.61           C  
ANISOU 1832  CB  CYS A 226     4059   3701   4250    360    -97   -339       C  
ATOM   1833  SG  CYS A 226     -24.954 -13.617 -21.815  1.00 39.85           S  
ANISOU 1833  SG  CYS A 226     5341   4343   5456    -69   -397   -617       S  
ATOM   1834  N   PHE A 227     -21.903 -17.778 -22.205  1.00 28.28           N  
ANISOU 1834  N   PHE A 227     3727   3774   3241    -13   -327   -355       N  
ATOM   1835  CA  PHE A 227     -21.737 -19.220 -22.461  1.00 27.64           C  
ANISOU 1835  CA  PHE A 227     3718   3509   3274     10   -394   -111       C  
ATOM   1836  C   PHE A 227     -22.915 -19.763 -23.316  1.00 28.26           C  
ANISOU 1836  C   PHE A 227     3733   3558   3444    -40   -229   -119       C  
ATOM   1837  O   PHE A 227     -23.520 -20.759 -22.984  1.00 28.58           O  
ANISOU 1837  O   PHE A 227     3839   3718   3301   -222   -418   -268       O  
ATOM   1838  CB  PHE A 227     -21.551 -20.018 -21.141  1.00 28.00           C  
ANISOU 1838  CB  PHE A 227     3733   3642   3261    -61   -267   -157       C  
ATOM   1839  CG  PHE A 227     -20.460 -19.457 -20.285  1.00 26.99           C  
ANISOU 1839  CG  PHE A 227     3254   3469   3531   -158   -349      0       C  
ATOM   1840  CD1 PHE A 227     -19.111 -19.880 -20.481  1.00 28.38           C  
ANISOU 1840  CD1 PHE A 227     3299   3998   3484     31      2    -91       C  
ATOM   1841  CD2 PHE A 227     -20.739 -18.445 -19.346  1.00 28.48           C  
ANISOU 1841  CD2 PHE A 227     3642   3597   3582   -160   -297    188       C  
ATOM   1842  CE1 PHE A 227     -18.044 -19.302 -19.745  1.00 27.09           C  
ANISOU 1842  CE1 PHE A 227     3243   3916   3133     78     98      0       C  
ATOM   1843  CE2 PHE A 227     -19.639 -17.818 -18.598  1.00 29.12           C  
ANISOU 1843  CE2 PHE A 227     3653   3940   3471    144   -478    323       C  
ATOM   1844  CZ  PHE A 227     -18.287 -18.288 -18.790  1.00 26.99           C  
ANISOU 1844  CZ  PHE A 227     3574   3354   3328   -135    200     83       C  
ATOM   1845  N   SER A 228     -23.202 -19.091 -24.421  1.00 28.38           N  
ANISOU 1845  N   SER A 228     3847   3515   3421    243   -188   -254       N  
ATOM   1846  CA  SER A 228     -24.331 -19.391 -25.251  1.00 30.06           C  
ANISOU 1846  CA  SER A 228     4032   3640   3748    272   -233   -191       C  
ATOM   1847  C   SER A 228     -24.120 -20.689 -26.060  1.00 29.91           C  
ANISOU 1847  C   SER A 228     3996   3728   3638    289   -257   -246       C  
ATOM   1848  O   SER A 228     -22.998 -21.082 -26.348  1.00 28.48           O  
ANISOU 1848  O   SER A 228     3932   3516   3371    249   -291   -446       O  
ATOM   1849  CB  SER A 228     -24.623 -18.196 -26.214  1.00 32.82           C  
ANISOU 1849  CB  SER A 228     4276   4136   4056    228   -102     89       C  
ATOM   1850  OG  SER A 228     -23.571 -17.986 -27.141  1.00 33.49           O  
ANISOU 1850  OG  SER A 228     4420   4220   4082    478   -256    171       O  
ATOM   1851  N   ASP A 229     -25.234 -21.335 -26.377  1.00 30.69           N  
ANISOU 1851  N   ASP A 229     4182   3549   3930    263   -312   -279       N  
ATOM   1852  CA  ASP A 229     -25.304 -22.416 -27.390  1.00 31.62           C  
ANISOU 1852  CA  ASP A 229     4286   3815   3912    299   -449   -356       C  
ATOM   1853  C   ASP A 229     -24.335 -23.558 -27.052  1.00 31.42           C  
ANISOU 1853  C   ASP A 229     4140   3783   4013    255   -403   -322       C  
ATOM   1854  O   ASP A 229     -24.501 -24.191 -25.979  1.00 31.54           O  
ANISOU 1854  O   ASP A 229     4029   3911   4042    369   -353   -434       O  
ATOM   1855  CB  ASP A 229     -25.083 -21.821 -28.798  1.00 33.54           C  
ANISOU 1855  CB  ASP A 229     4435   3959   4350    230   -350   -259       C  
ATOM   1856  CG  ASP A 229     -26.148 -20.757 -29.143  1.00 38.44           C  
ANISOU 1856  CG  ASP A 229     4973   4782   4851    365   -441     46       C  
ATOM   1857  OD1 ASP A 229     -27.332 -20.894 -28.667  1.00 41.67           O  
ANISOU 1857  OD1 ASP A 229     5269   5362   5201    184   -642   -422       O  
ATOM   1858  OD2 ASP A 229     -25.779 -19.746 -29.816  1.00 45.44           O  
ANISOU 1858  OD2 ASP A 229     6388   5926   4951    178     72     67       O  
ATOM   1859  N   SER A 230     -23.309 -23.765 -27.890  1.00 31.43           N  
ANISOU 1859  N   SER A 230     4321   3946   3673    407   -543   -371       N  
ATOM   1860  CA  SER A 230     -22.338 -24.898 -27.722  1.00 31.69           C  
ANISOU 1860  CA  SER A 230     4408   3961   3670    362   -483   -282       C  
ATOM   1861  C   SER A 230     -21.454 -24.785 -26.508  1.00 30.69           C  
ANISOU 1861  C   SER A 230     4166   3828   3663    249   -440   -279       C  
ATOM   1862  O   SER A 230     -20.821 -25.759 -26.170  1.00 31.07           O  
ANISOU 1862  O   SER A 230     4366   3836   3601    108   -427   -392       O  
ATOM   1863  CB  SER A 230     -21.367 -24.979 -28.892  1.00 31.98           C  
ANISOU 1863  CB  SER A 230     4424   4124   3604    390   -566   -382       C  
ATOM   1864  OG  SER A 230     -22.166 -25.193 -30.039  1.00 38.33           O  
ANISOU 1864  OG  SER A 230     5566   5118   3879    459   -658   -109       O  
ATOM   1865  N   TYR A 231     -21.362 -23.600 -25.895  1.00 29.17           N  
ANISOU 1865  N   TYR A 231     3820   3593   3668     82   -295   -333       N  
ATOM   1866  CA  TYR A 231     -20.512 -23.426 -24.719  1.00 29.43           C  
ANISOU 1866  CA  TYR A 231     3926   3623   3631      0    -93   -203       C  
ATOM   1867  C   TYR A 231     -21.259 -23.586 -23.417  1.00 29.28           C  
ANISOU 1867  C   TYR A 231     3760   3604   3759      3    -70   -155       C  
ATOM   1868  O   TYR A 231     -20.610 -23.717 -22.360  1.00 27.99           O  
ANISOU 1868  O   TYR A 231     3904   3468   3262    -89   -206   -296       O  
ATOM   1869  CB  TYR A 231     -19.828 -22.032 -24.741  1.00 30.44           C  
ANISOU 1869  CB  TYR A 231     3917   3741   3905   -181     19   -276       C  
ATOM   1870  CG  TYR A 231     -19.082 -21.804 -26.049  1.00 31.89           C  
ANISOU 1870  CG  TYR A 231     4169   4109   3838   -290     99   -364       C  
ATOM   1871  CD1 TYR A 231     -17.842 -22.425 -26.304  1.00 33.20           C  
ANISOU 1871  CD1 TYR A 231     4097   4578   3937   -725    136   -568       C  
ATOM   1872  CD2 TYR A 231     -19.651 -21.005 -27.045  1.00 36.19           C  
ANISOU 1872  CD2 TYR A 231     4510   5077   4163   -469    -26   -201       C  
ATOM   1873  CE1 TYR A 231     -17.169 -22.205 -27.576  1.00 33.70           C  
ANISOU 1873  CE1 TYR A 231     4047   4808   3947   -562    359   -291       C  
ATOM   1874  CE2 TYR A 231     -19.016 -20.778 -28.285  1.00 37.40           C  
ANISOU 1874  CE2 TYR A 231     4292   5480   4438   -501    164   -489       C  
ATOM   1875  CZ  TYR A 231     -17.797 -21.379 -28.545  1.00 37.94           C  
ANISOU 1875  CZ  TYR A 231     4576   5267   4572   -735    471   -218       C  
ATOM   1876  OH  TYR A 231     -17.230 -21.124 -29.799  1.00 42.62           O  
ANISOU 1876  OH  TYR A 231     5119   6309   4766   -722    806   -323       O  
ATOM   1877  N   GLN A 232     -22.600 -23.616 -23.474  1.00 28.57           N  
ANISOU 1877  N   GLN A 232     3560   3610   3683     26      8   -287       N  
ATOM   1878  CA  GLN A 232     -23.365 -23.623 -22.197  1.00 28.05           C  
ANISOU 1878  CA  GLN A 232     3401   3688   3567     68     47   -196       C  
ATOM   1879  C   GLN A 232     -22.989 -24.748 -21.238  1.00 28.11           C  
ANISOU 1879  C   GLN A 232     3486   3605   3586    213      1   -350       C  
ATOM   1880  O   GLN A 232     -22.877 -24.553 -20.007  1.00 28.92           O  
ANISOU 1880  O   GLN A 232     3416   3738   3833    480    -17   -438       O  
ATOM   1881  CB  GLN A 232     -24.897 -23.536 -22.420  1.00 29.18           C  
ANISOU 1881  CB  GLN A 232     3416   4067   3602    116     88   -277       C  
ATOM   1882  CG  GLN A 232     -25.638 -23.090 -21.154  1.00 28.25           C  
ANISOU 1882  CG  GLN A 232     3054   3992   3686    365    198   -324       C  
ATOM   1883  CD  GLN A 232     -27.126 -23.035 -21.388  1.00 32.36           C  
ANISOU 1883  CD  GLN A 232     3522   4377   4394    244    171   -627       C  
ATOM   1884  OE1 GLN A 232     -27.845 -24.076 -21.378  1.00 34.60           O  
ANISOU 1884  OE1 GLN A 232     4039   4527   4579     80    148   -648       O  
ATOM   1885  NE2 GLN A 232     -27.603 -21.826 -21.673  1.00 32.76           N  
ANISOU 1885  NE2 GLN A 232     3454   4389   4602    543   -383   -884       N  
ATOM   1886  N   LYS A 233     -22.837 -25.939 -21.772  1.00 26.47           N  
ANISOU 1886  N   LYS A 233     3432   3354   3268    209     32   -431       N  
ATOM   1887  CA  LYS A 233     -22.559 -27.093 -20.922  1.00 27.30           C  
ANISOU 1887  CA  LYS A 233     3581   3421   3370     64     31   -527       C  
ATOM   1888  C   LYS A 233     -21.198 -26.982 -20.210  1.00 27.43           C  
ANISOU 1888  C   LYS A 233     3585   3470   3367    -26    -33   -481       C  
ATOM   1889  O   LYS A 233     -21.018 -27.569 -19.157  1.00 28.69           O  
ANISOU 1889  O   LYS A 233     3746   3325   3828    -75   -118   -463       O  
ATOM   1890  CB  LYS A 233     -22.650 -28.376 -21.757  1.00 26.42           C  
ANISOU 1890  CB  LYS A 233     3399   3317   3321    -62    -14   -580       C  
ATOM   1891  CG  LYS A 233     -24.088 -28.847 -21.883  1.00 28.69           C  
ANISOU 1891  CG  LYS A 233     3874   3401   3623   -182    -62   -873       C  
ATOM   1892  CD  LYS A 233     -24.087 -30.203 -22.578  1.00 32.70           C  
ANISOU 1892  CD  LYS A 233     4347   3694   4380     65     86   -797       C  
ATOM   1893  CE  LYS A 233     -25.448 -30.768 -22.441  1.00 38.82           C  
ANISOU 1893  CE  LYS A 233     4579   4857   5314    126   -563   -609       C  
ATOM   1894  NZ  LYS A 233     -25.614 -31.902 -23.393  1.00 41.95           N  
ANISOU 1894  NZ  LYS A 233     4648   5842   5449     79   -724   -977       N  
ATOM   1895  N   ASN A 234     -20.244 -26.230 -20.781  1.00 27.29           N  
ANISOU 1895  N   ASN A 234     3571   3618   3179     92      0   -526       N  
ATOM   1896  CA  ASN A 234     -18.941 -26.039 -20.116  1.00 28.37           C  
ANISOU 1896  CA  ASN A 234     3641   3791   3348     98    -71   -349       C  
ATOM   1897  C   ASN A 234     -19.233 -25.346 -18.764  1.00 26.34           C  
ANISOU 1897  C   ASN A 234     3430   3561   3017    151     37   -369       C  
ATOM   1898  O   ASN A 234     -18.754 -25.772 -17.700  1.00 27.21           O  
ANISOU 1898  O   ASN A 234     3650   3622   3066    188   -220   -335       O  
ATOM   1899  CB  ASN A 234     -18.055 -25.071 -20.898  1.00 28.44           C  
ANISOU 1899  CB  ASN A 234     3534   3852   3419    135      4   -240       C  
ATOM   1900  CG  ASN A 234     -17.205 -25.768 -21.932  1.00 32.15           C  
ANISOU 1900  CG  ASN A 234     4288   4018   3908    333    -74   -109       C  
ATOM   1901  OD1 ASN A 234     -16.230 -26.464 -21.598  1.00 36.17           O  
ANISOU 1901  OD1 ASN A 234     4574   4611   4558    708   -335    226       O  
ATOM   1902  ND2 ASN A 234     -17.548 -25.574 -23.191  1.00 29.80           N  
ANISOU 1902  ND2 ASN A 234     4633   3217   3470     87   -718   -494       N  
ATOM   1903  N   ALA A 235     -20.015 -24.271 -18.833  1.00 25.58           N  
ANISOU 1903  N   ALA A 235     3239   3406   3070      2    152   -361       N  
ATOM   1904  CA  ALA A 235     -20.424 -23.523 -17.602  1.00 26.04           C  
ANISOU 1904  CA  ALA A 235     3316   3387   3189     80    167   -322       C  
ATOM   1905  C   ALA A 235     -21.239 -24.355 -16.604  1.00 26.61           C  
ANISOU 1905  C   ALA A 235     3530   3252   3327     51     48   -235       C  
ATOM   1906  O   ALA A 235     -20.942 -24.386 -15.395  1.00 26.87           O  
ANISOU 1906  O   ALA A 235     3634   3371   3202   -154    243   -384       O  
ATOM   1907  CB  ALA A 235     -21.187 -22.212 -18.006  1.00 25.83           C  
ANISOU 1907  CB  ALA A 235     3489   2998   3327    143    315   -308       C  
ATOM   1908  N   VAL A 236     -22.262 -25.045 -17.107  1.00 27.49           N  
ANISOU 1908  N   VAL A 236     3620   3335   3487     56    127   -153       N  
ATOM   1909  CA  VAL A 236     -23.168 -25.840 -16.296  1.00 27.69           C  
ANISOU 1909  CA  VAL A 236     3403   3380   3737    -32     54    -73       C  
ATOM   1910  C   VAL A 236     -22.416 -27.017 -15.618  1.00 28.11           C  
ANISOU 1910  C   VAL A 236     3567   3362   3750   -110     21   -115       C  
ATOM   1911  O   VAL A 236     -22.566 -27.246 -14.389  1.00 28.33           O  
ANISOU 1911  O   VAL A 236     3516   3374   3875     58   -176   -330       O  
ATOM   1912  CB  VAL A 236     -24.361 -26.312 -17.155  1.00 28.05           C  
ANISOU 1912  CB  VAL A 236     3624   3523   3508   -147    106     72       C  
ATOM   1913  CG1 VAL A 236     -25.276 -27.210 -16.309  1.00 28.75           C  
ANISOU 1913  CG1 VAL A 236     3798   3417   3708   -467     74    263       C  
ATOM   1914  CG2 VAL A 236     -25.142 -25.077 -17.652  1.00 28.22           C  
ANISOU 1914  CG2 VAL A 236     3025   3644   4053    305    170   -137       C  
ATOM   1915  N   ASN A 237     -21.586 -27.714 -16.402  1.00 27.09           N  
ANISOU 1915  N   ASN A 237     3390   3157   3746    -79     -5   -305       N  
ATOM   1916  CA  ASN A 237     -20.880 -28.900 -15.875  1.00 26.04           C  
ANISOU 1916  CA  ASN A 237     3251   3284   3359     87     -7   -354       C  
ATOM   1917  C   ASN A 237     -19.920 -28.477 -14.775  1.00 26.13           C  
ANISOU 1917  C   ASN A 237     3297   3375   3254    170     92   -349       C  
ATOM   1918  O   ASN A 237     -19.889 -29.084 -13.729  1.00 25.70           O  
ANISOU 1918  O   ASN A 237     3157   3296   3312     89    -29   -444       O  
ATOM   1919  CB  ASN A 237     -20.059 -29.631 -16.977  1.00 27.85           C  
ANISOU 1919  CB  ASN A 237     3755   3541   3284     91     95   -497       C  
ATOM   1920  CG  ASN A 237     -20.931 -30.408 -17.985  1.00 28.47           C  
ANISOU 1920  CG  ASN A 237     3541   3506   3770   -127    -20   -235       C  
ATOM   1921  OD1 ASN A 237     -22.108 -30.675 -17.757  1.00 34.03           O  
ANISOU 1921  OD1 ASN A 237     3934   4306   4688   -281   -791      0       O  
ATOM   1922  ND2 ASN A 237     -20.323 -30.755 -19.131  1.00 34.07           N  
ANISOU 1922  ND2 ASN A 237     5114   4055   3773     84   -432   -906       N  
ATOM   1923  N   LEU A 238     -19.146 -27.436 -15.026  1.00 26.34           N  
ANISOU 1923  N   LEU A 238     3242   3480   3285     88     69   -306       N  
ATOM   1924  CA  LEU A 238     -18.108 -27.012 -14.053  1.00 27.15           C  
ANISOU 1924  CA  LEU A 238     3405   3591   3317     -7    237   -317       C  
ATOM   1925  C   LEU A 238     -18.781 -26.518 -12.766  1.00 26.06           C  
ANISOU 1925  C   LEU A 238     3132   3488   3279    -27    273   -159       C  
ATOM   1926  O   LEU A 238     -18.350 -26.849 -11.646  1.00 24.49           O  
ANISOU 1926  O   LEU A 238     2821   3427   3056    110    100   -419       O  
ATOM   1927  CB  LEU A 238     -17.184 -25.921 -14.617  1.00 27.10           C  
ANISOU 1927  CB  LEU A 238     3297   3672   3325     66    381   -128       C  
ATOM   1928  CG  LEU A 238     -16.172 -26.325 -15.715  1.00 27.26           C  
ANISOU 1928  CG  LEU A 238     3390   3603   3363    137    340     17       C  
ATOM   1929  CD1 LEU A 238     -15.509 -25.034 -16.354  1.00 28.95           C  
ANISOU 1929  CD1 LEU A 238     3482   3515   4001    205    607    111       C  
ATOM   1930  CD2 LEU A 238     -15.105 -27.237 -15.142  1.00 28.38           C  
ANISOU 1930  CD2 LEU A 238     3329   3636   3817    355    264    197       C  
ATOM   1931  N   THR A 239     -19.870 -25.777 -12.927  1.00 24.22           N  
ANISOU 1931  N   THR A 239     2997   2990   3212    -43    245   -178       N  
ATOM   1932  CA  THR A 239     -20.554 -25.276 -11.739  1.00 24.87           C  
ANISOU 1932  CA  THR A 239     3104   3185   3161    115    182   -246       C  
ATOM   1933  C   THR A 239     -21.117 -26.446 -10.925  1.00 25.13           C  
ANISOU 1933  C   THR A 239     3127   3249   3171     32     89   -130       C  
ATOM   1934  O   THR A 239     -20.982 -26.484  -9.658  1.00 26.31           O  
ANISOU 1934  O   THR A 239     3350   3523   3122    -21    120    -84       O  
ATOM   1935  CB  THR A 239     -21.737 -24.338 -12.148  1.00 24.27           C  
ANISOU 1935  CB  THR A 239     3034   3058   3127     69    197   -284       C  
ATOM   1936  OG1 THR A 239     -21.217 -23.192 -12.849  1.00 24.35           O  
ANISOU 1936  OG1 THR A 239     2747   3361   3141    195    255    102       O  
ATOM   1937  CG2 THR A 239     -22.607 -23.980 -10.889  1.00 24.49           C  
ANISOU 1937  CG2 THR A 239     2863   3274   3165    460    243   -715       C  
ATOM   1938  N   THR A 240     -21.729 -27.423 -11.614  1.00 26.70           N  
ANISOU 1938  N   THR A 240     3491   3183   3467    -60     96   -143       N  
ATOM   1939  CA  THR A 240     -22.378 -28.556 -10.895  1.00 28.01           C  
ANISOU 1939  CA  THR A 240     3523   3435   3683    -90    -35    -46       C  
ATOM   1940  C   THR A 240     -21.288 -29.425 -10.225  1.00 28.13           C  
ANISOU 1940  C   THR A 240     3469   3577   3640   -210   -113   -103       C  
ATOM   1941  O   THR A 240     -21.395 -29.771  -9.031  1.00 28.46           O  
ANISOU 1941  O   THR A 240     3509   3639   3664   -190   -101   -227       O  
ATOM   1942  CB  THR A 240     -23.197 -29.449 -11.891  1.00 28.19           C  
ANISOU 1942  CB  THR A 240     3461   3349   3898   -337   -111    123       C  
ATOM   1943  OG1 THR A 240     -24.179 -28.601 -12.551  1.00 31.57           O  
ANISOU 1943  OG1 THR A 240     4055   3484   4454   -151   -373    -89       O  
ATOM   1944  CG2 THR A 240     -23.918 -30.675 -11.137  1.00 28.66           C  
ANISOU 1944  CG2 THR A 240     3742   3375   3772   -175    276    176       C  
ATOM   1945  N   ASP A 241     -20.249 -29.773 -10.989  1.00 28.19           N  
ANISOU 1945  N   ASP A 241     3559   3384   3766     65   -165   -352       N  
ATOM   1946  CA  ASP A 241     -19.148 -30.564 -10.428  1.00 29.58           C  
ANISOU 1946  CA  ASP A 241     3494   3879   3867     20    -70   -349       C  
ATOM   1947  C   ASP A 241     -18.537 -29.872  -9.191  1.00 28.74           C  
ANISOU 1947  C   ASP A 241     3539   3708   3671     88    105   -245       C  
ATOM   1948  O   ASP A 241     -18.205 -30.559  -8.196  1.00 28.86           O  
ANISOU 1948  O   ASP A 241     3380   3700   3883     51   -172   -278       O  
ATOM   1949  CB  ASP A 241     -18.079 -30.829 -11.509  1.00 30.24           C  
ANISOU 1949  CB  ASP A 241     3615   3863   4011    202    -10   -433       C  
ATOM   1950  CG  ASP A 241     -18.565 -31.778 -12.621  1.00 37.34           C  
ANISOU 1950  CG  ASP A 241     4899   4738   4548    222      4   -363       C  
ATOM   1951  OD1 ASP A 241     -19.573 -32.525 -12.459  1.00 41.76           O  
ANISOU 1951  OD1 ASP A 241     5393   5045   5428   -202   -352   -682       O  
ATOM   1952  OD2 ASP A 241     -17.921 -31.779 -13.673  1.00 44.46           O  
ANISOU 1952  OD2 ASP A 241     6538   5670   4684   1007    604   -630       O  
ATOM   1953  N   PHE A 242     -18.372 -28.536  -9.281  1.00 26.67           N  
ANISOU 1953  N   PHE A 242     3209   3422   3499     -5    130   -241       N  
ATOM   1954  CA  PHE A 242     -17.783 -27.793  -8.202  1.00 26.83           C  
ANISOU 1954  CA  PHE A 242     3432   3288   3471    -21     10     45       C  
ATOM   1955  C   PHE A 242     -18.581 -27.920  -6.894  1.00 27.37           C  
ANISOU 1955  C   PHE A 242     3543   3399   3457    -65      7     38       C  
ATOM   1956  O   PHE A 242     -17.970 -28.101  -5.791  1.00 28.37           O  
ANISOU 1956  O   PHE A 242     3703   3511   3563    228    -59    439       O  
ATOM   1957  CB  PHE A 242     -17.501 -26.314  -8.566  1.00 27.33           C  
ANISOU 1957  CB  PHE A 242     3526   3202   3655    -86   -141    -19       C  
ATOM   1958  CG  PHE A 242     -16.591 -25.633  -7.593  1.00 26.74           C  
ANISOU 1958  CG  PHE A 242     3716   2866   3576   -115      0    104       C  
ATOM   1959  CD1 PHE A 242     -15.213 -25.960  -7.555  1.00 29.51           C  
ANISOU 1959  CD1 PHE A 242     3779   3623   3807     55   -301   -288       C  
ATOM   1960  CD2 PHE A 242     -17.075 -24.706  -6.686  1.00 28.45           C  
ANISOU 1960  CD2 PHE A 242     3915   3510   3384    -45     61      0       C  
ATOM   1961  CE1 PHE A 242     -14.340 -25.342  -6.672  1.00 33.54           C  
ANISOU 1961  CE1 PHE A 242     4193   4170   4379    435   -292   -221       C  
ATOM   1962  CE2 PHE A 242     -16.175 -24.103  -5.764  1.00 29.20           C  
ANISOU 1962  CE2 PHE A 242     3697   3610   3785     15   -262   -161       C  
ATOM   1963  CZ  PHE A 242     -14.802 -24.413  -5.793  1.00 30.60           C  
ANISOU 1963  CZ  PHE A 242     4261   3992   3372     81    207   -162       C  
ATOM   1964  N   LEU A 243     -19.905 -27.827  -7.007  1.00 26.71           N  
ANISOU 1964  N   LEU A 243     3683   3130   3333     41    205     57       N  
ATOM   1965  CA  LEU A 243     -20.781 -27.792  -5.817  1.00 28.10           C  
ANISOU 1965  CA  LEU A 243     3743   3305   3629     40    305     22       C  
ATOM   1966  C   LEU A 243     -21.127 -29.161  -5.282  1.00 31.26           C  
ANISOU 1966  C   LEU A 243     4081   3738   4057     24    195    195       C  
ATOM   1967  O   LEU A 243     -21.475 -29.298  -4.110  1.00 30.95           O  
ANISOU 1967  O   LEU A 243     4243   3480   4035    171     -8    163       O  
ATOM   1968  CB  LEU A 243     -22.015 -26.974  -6.148  1.00 26.28           C  
ANISOU 1968  CB  LEU A 243     3438   3204   3342     22    488    -11       C  
ATOM   1969  CG  LEU A 243     -21.701 -25.522  -6.501  1.00 25.07           C  
ANISOU 1969  CG  LEU A 243     3063   3194   3267    -65    257   -105       C  
ATOM   1970  CD1 LEU A 243     -23.035 -24.727  -6.828  1.00 23.13           C  
ANISOU 1970  CD1 LEU A 243     3369   2611   2806   -138    221    366       C  
ATOM   1971  CD2 LEU A 243     -20.901 -24.848  -5.317  1.00 23.84           C  
ANISOU 1971  CD2 LEU A 243     3100   3030   2925     92   -209    259       C  
ATOM   1972  N   GLN A 244     -21.016 -30.185  -6.124  1.00 36.79           N  
ANISOU 1972  N   GLN A 244     4872   4405   4700     16     92    153       N  
ATOM   1973  CA  GLN A 244     -21.270 -31.589  -5.671  1.00 43.46           C  
ANISOU 1973  CA  GLN A 244     5672   5139   5702    -42     65    286       C  
ATOM   1974  C   GLN A 244     -20.245 -32.123  -4.709  1.00 47.64           C  
ANISOU 1974  C   GLN A 244     6099   5737   6262     82    -15    397       C  
ATOM   1975  O   GLN A 244     -20.560 -33.028  -3.928  1.00 49.50           O  
ANISOU 1975  O   GLN A 244     6171   5888   6747    142     -1    471       O  
ATOM   1976  CB  GLN A 244     -21.237 -32.522  -6.835  1.00 44.98           C  
ANISOU 1976  CB  GLN A 244     6008   5185   5897    -85     -5    306       C  
ATOM   1977  CG  GLN A 244     -22.510 -32.741  -7.444  1.00 48.18           C  
ANISOU 1977  CG  GLN A 244     5997   5826   6482   -146     20    276       C  
ATOM   1978  CD  GLN A 244     -22.352 -33.813  -8.480  1.00 53.35           C  
ANISOU 1978  CD  GLN A 244     6800   6219   7251    162    230    154       C  
ATOM   1979  OE1 GLN A 244     -21.924 -33.560  -9.633  1.00 55.69           O  
ANISOU 1979  OE1 GLN A 244     7043   6597   7517    158    491    542       O  
ATOM   1980  NE2 GLN A 244     -22.641 -35.034  -8.073  1.00 54.45           N  
ANISOU 1980  NE2 GLN A 244     6531   6495   7663   -314    231    588       N  
ATOM   1981  N   ASN A 245     -19.027 -31.582  -4.820  1.00 52.10           N  
ANISOU 1981  N   ASN A 245     6570   6397   6826      2    -27    451       N  
ATOM   1982  CA  ASN A 245     -17.817 -31.813  -3.970  1.00 56.04           C  
ANISOU 1982  CA  ASN A 245     7095   7095   7099    -23    -82    328       C  
ATOM   1983  C   ASN A 245     -16.554 -31.292  -4.688  1.00 57.03           C  
ANISOU 1983  C   ASN A 245     7269   7246   7152    -78     -6    317       C  
ATOM   1984  O   ASN A 245     -16.486 -31.235  -5.943  1.00 57.92           O  
ANISOU 1984  O   ASN A 245     7359   7570   7076    -15    -80    236       O  
ATOM   1985  CB  ASN A 245     -17.606 -33.294  -3.500  1.00 57.80           C  
ANISOU 1985  CB  ASN A 245     7364   7248   7348    -18    -90    373       C  
ATOM   1986  CG  ASN A 245     -17.861 -33.499  -1.966  1.00 61.12           C  
ANISOU 1986  CG  ASN A 245     7740   7972   7511    -35   -149    326       C  
ATOM   1987  OD1 ASN A 245     -16.903 -33.591  -1.182  1.00 65.43           O  
ANISOU 1987  OD1 ASN A 245     8041   8648   8171   -181   -458    309       O  
ATOM   1988  ND2 ASN A 245     -19.147 -33.606  -1.554  1.00 63.60           N  
ANISOU 1988  ND2 ASN A 245     7830   8402   7929    -16     29    221       N  
TER    1989      ASN A 245                                                      
HETATM 1990 NA    NA A 250     -39.616  -5.851 -15.102  1.00 29.09          NA  
ANISOU 1990 NA    NA A 250     3122   3959   3969      3   -611   -561      NA  
HETATM 1991 NA    NA A 251     -11.590   0.937  -1.145  1.00 37.52          NA  
ANISOU 1991 NA    NA A 251     4749   4328   5177   -525   -301   -123      NA  
HETATM 1992 NA    NA A 252      -5.673 -20.608  -5.383  1.00 55.89          NA  
ANISOU 1992 NA    NA A 252     5057   8654   7521   -573    202    865      NA  
HETATM 1993 NA    NA A 253      -6.054 -18.427  -5.808  1.00 44.90          NA  
ANISOU 1993 NA    NA A 253     5067   6379   5613    322   -372   -409      NA  
HETATM 1994  O   HOH A 254     -10.406   8.184 -16.605  1.00 40.45           O  
ANISOU 1994  O   HOH A 254     4512   5355   5500  -1604   -381    254       O  
HETATM 1995  O   HOH A 255     -32.661  -3.529   4.850  1.00 34.47           O  
ANISOU 1995  O   HOH A 255     5458   3828   3809    518    561   -162       O  
HETATM 1996  O   HOH A 256     -30.942  -5.789 -26.626  1.00 44.73           O  
ANISOU 1996  O   HOH A 256     5654   5736   5605  -1303    -21  -1304       O  
HETATM 1997  O   HOH A 257     -36.444 -14.333   5.389  1.00 50.52           O  
ANISOU 1997  O   HOH A 257     5265   5390   8538    792   3027   -209       O  
HETATM 1998  O   HOH A 258     -19.387 -11.877 -25.657  1.00 26.19           O  
ANISOU 1998  O   HOH A 258     4649   3043   2255   -460    261     79       O  
HETATM 1999  O   HOH A 259     -43.894 -30.513  -8.073  1.00 44.48           O  
ANISOU 1999  O   HOH A 259     5087   6691   5122   -412   1092   -699       O  
HETATM 2000  O   HOH A 260     -15.568 -13.620  -2.276  1.00 21.28           O  
ANISOU 2000  O   HOH A 260     2608   2884   2594    206     29    330       O  
HETATM 2001  O   HOH A 261     -38.713 -17.827   5.833  1.00 53.65           O  
ANISOU 2001  O   HOH A 261     6565   6693   7126   1374   1955    773       O  
HETATM 2002  O   HOH A 262     -38.557 -21.009 -15.224  1.00 50.28           O  
ANISOU 2002  O   HOH A 262     4919   5331   8850  -1234   -593  -2836       O  
HETATM 2003  O   HOH A 263     -28.910   4.349  -9.495  1.00 31.64           O  
ANISOU 2003  O   HOH A 263     3738   4683   3599    608   -754    148       O  
HETATM 2004  O   HOH A 264     -34.857  -3.163 -21.904  1.00 45.70           O  
ANISOU 2004  O   HOH A 264     5731   5999   5633   -545   -843  -1048       O  
HETATM 2005  O   HOH A 265     -17.415 -29.540 -19.411  1.00 31.74           O  
ANISOU 2005  O   HOH A 265     3864   4658   3536    945    239  -1100       O  
HETATM 2006  O   HOH A 266     -39.152 -33.091   4.761  1.00 29.42           O  
ANISOU 2006  O   HOH A 266     3723   4418   3035  -1320    496   -133       O  
HETATM 2007  O   HOH A 267     -34.458 -17.926 -21.663  1.00 49.90           O  
ANISOU 2007  O   HOH A 267     5095   8496   5367   -453  -1480    647       O  
HETATM 2008  O   HOH A 268     -28.203 -17.249 -21.113  1.00 29.14           O  
ANISOU 2008  O   HOH A 268     3514   3458   4099    245   -841   -670       O  
HETATM 2009  O   HOH A 269     -15.071 -29.824 -21.665  1.00 30.97           O  
ANISOU 2009  O   HOH A 269     4392   3801   3572    -46    446   -250       O  
HETATM 2010  O   HOH A 270     -29.394   2.205 -12.474  1.00 28.01           O  
ANISOU 2010  O   HOH A 270     4480   3454   2707    165   -292    136       O  
HETATM 2011  O   HOH A 271     -30.745 -11.963  -7.318  1.00 29.58           O  
ANISOU 2011  O   HOH A 271     3533   3392   4311   -215    224   -383       O  
HETATM 2012  O   HOH A 272     -26.938 -27.003 -23.643  1.00 43.22           O  
ANISOU 2012  O   HOH A 272     5103   6881   4435   -954   -402   -401       O  
HETATM 2013  O   HOH A 273     -14.989  14.218  -9.584  1.00 39.69           O  
ANISOU 2013  O   HOH A 273     6800   4228   4051   -268    313   -299       O  
HETATM 2014  O   HOH A 274      -9.461   2.787  -8.718  1.00 59.42           O  
ANISOU 2014  O   HOH A 274     3816  10731   8027  -1809  -2057   2514       O  
HETATM 2015  O   HOH A 275     -30.709 -14.359 -10.240  1.00 24.72           O  
ANISOU 2015  O   HOH A 275     3171   2925   3294     -8   -308   -122       O  
HETATM 2016  O   HOH A 276      -9.566  -6.478 -15.129  1.00 45.33           O  
ANISOU 2016  O   HOH A 276     5914   6216   5092   -760    957  -1089       O  
HETATM 2017  O   HOH A 277     -10.651 -18.424  -1.568  1.00 26.38           O  
ANISOU 2017  O   HOH A 277     3515   3385   3123   -156      4   -171       O  
HETATM 2018  O   HOH A 278     -38.944 -27.640   2.002  1.00 32.36           O  
ANISOU 2018  O   HOH A 278     4140   4419   3735   -961    333    -65       O  
HETATM 2019  O   HOH A 279     -36.650 -41.023   4.980  1.00 53.57           O  
ANISOU 2019  O   HOH A 279     6895   6387   7070   -157   1413   1456       O  
HETATM 2020  O   HOH A 280     -23.290   0.264  -9.217  1.00 24.60           O  
ANISOU 2020  O   HOH A 280     3090   2961   3294    286   -170    315       O  
HETATM 2021  O   HOH A 281     -28.712 -37.393  -4.460  1.00 62.39           O  
ANISOU 2021  O   HOH A 281     6343   5063  12298    691  -2551   -704       O  
HETATM 2022  O   HOH A 282     -26.488  -8.226 -11.307  1.00 24.29           O  
ANISOU 2022  O   HOH A 282     2848   2970   3409   -144    128   -250       O  
HETATM 2023  O   HOH A 283     -23.964  16.555 -15.998  1.00 58.03           O  
ANISOU 2023  O   HOH A 283     6848   6483   8717   1636    220    715       O  
HETATM 2024  O   HOH A 284     -17.399 -15.437 -20.441  1.00 25.61           O  
ANISOU 2024  O   HOH A 284     3348   3336   3045    166   -104    -72       O  
HETATM 2025  O   HOH A 285     -14.802 -10.784   6.339  1.00 29.61           O  
ANISOU 2025  O   HOH A 285     4170   3541   3538    197    222    733       O  
HETATM 2026  O   HOH A 286     -35.982   3.011 -14.678  1.00 31.61           O  
ANISOU 2026  O   HOH A 286     4219   4059   3732    172   -988   -201       O  
HETATM 2027  O   HOH A 287     -19.626  -1.947 -17.067  1.00 39.84           O  
ANISOU 2027  O   HOH A 287     4865   5398   4873      3   -186   -131       O  
HETATM 2028  O   HOH A 288     -10.354 -26.119 -17.388  1.00 53.76           O  
ANISOU 2028  O   HOH A 288     9887   5440   5098    970   1936    -66       O  
HETATM 2029  O   HOH A 289     -23.487  -7.908 -15.807  1.00 24.69           O  
ANISOU 2029  O   HOH A 289     3442   3363   2576     55   -242   -262       O  
HETATM 2030  O   HOH A 290     -11.503   2.303  -5.005  1.00 39.29           O  
ANISOU 2030  O   HOH A 290     4325   6733   3868   -291   -432   -370       O  
HETATM 2031  O   HOH A 291     -34.637  -7.500 -16.172  1.00 30.17           O  
ANISOU 2031  O   HOH A 291     4117   3648   3696   -198   -675   -506       O  
HETATM 2032  O   HOH A 292     -11.789   4.260  -7.283  1.00 29.35           O  
ANISOU 2032  O   HOH A 292     3321   4094   3735    -39   -309    -16       O  
HETATM 2033  O   HOH A 293     -38.690  -4.957 -13.058  1.00 37.77           O  
ANISOU 2033  O   HOH A 293     5366   3527   5455    732   -437   -996       O  
HETATM 2034  O   HOH A 294     -29.002 -28.223 -17.181  1.00 32.41           O  
ANISOU 2034  O   HOH A 294     4103   3669   4542    212   -283     62       O  
HETATM 2035  O   HOH A 295     -32.955  -3.475 -25.862  1.00 38.08           O  
ANISOU 2035  O   HOH A 295     5233   4386   4847     96   -641  -1117       O  
HETATM 2036  O   HOH A 296     -21.944 -26.109 -32.415  1.00 35.73           O  
ANISOU 2036  O   HOH A 296     4722   4453   4400    399  -1142    -20       O  
HETATM 2037  O   HOH A 297      -5.616 -20.412  -8.637  1.00 45.77           O  
ANISOU 2037  O   HOH A 297     3114   6971   7306    553    858    630       O  
HETATM 2038  O   HOH A 298     -32.727   4.870 -23.092  1.00 42.26           O  
ANISOU 2038  O   HOH A 298     6765   4439   4850    846  -1581     68       O  
HETATM 2039  O   HOH A 299     -35.201   5.881 -23.419  1.00 44.18           O  
ANISOU 2039  O   HOH A 299     6097   5924   4765    708    416    206       O  
HETATM 2040  O   HOH A 300     -26.620 -32.820 -13.156  1.00 35.17           O  
ANISOU 2040  O   HOH A 300     4323   3913   5126     75   -127   -579       O  
HETATM 2041  O   HOH A 301      -8.768 -14.159 -24.030  1.00 40.74           O  
ANISOU 2041  O   HOH A 301     5365   6166   3947  -1387   1009  -1760       O  
HETATM 2042  O   HOH A 302     -33.295 -32.171 -15.024  1.00 54.45           O  
ANISOU 2042  O   HOH A 302     7954   7853   4880   -662   -953   -688       O  
HETATM 2043  O   HOH A 303     -31.002   2.069  -2.657  1.00 29.94           O  
ANISOU 2043  O   HOH A 303     4288   3442   3643    311   -109   -611       O  
HETATM 2044  O   HOH A 304     -36.600 -37.795  -0.365  1.00 53.77           O  
ANISOU 2044  O   HOH A 304     5369   6437   8623  -1727   2321  -1460       O  
HETATM 2045  O   HOH A 305     -10.534  10.737 -14.721  1.00 41.47           O  
ANISOU 2045  O   HOH A 305     5214   5300   5243  -1190    130    927       O  
HETATM 2046  O   HOH A 306      -4.010 -14.753 -12.746  1.00 45.23           O  
ANISOU 2046  O   HOH A 306     3829   6597   6758    132    609  -1296       O  
HETATM 2047  O   HOH A 307     -27.252  12.017 -19.489  1.00 50.40           O  
ANISOU 2047  O   HOH A 307     7797   6893   4459  -2348  -1014   1146       O  
HETATM 2048  O   HOH A 308     -35.708  -4.770   4.886  1.00 57.85           O  
ANISOU 2048  O   HOH A 308    11252   7267   3460   2373  -1049     47       O  
HETATM 2049  O   HOH A 309     -42.692  -7.542  -7.474  1.00 47.48           O  
ANISOU 2049  O   HOH A 309     4412   4570   9059   -965   -495   -894       O  
HETATM 2050  O   HOH A 310     -35.546 -12.249   3.846  1.00 31.88           O  
ANISOU 2050  O   HOH A 310     3228   4348   4536   -546    744   -761       O  
HETATM 2051  O   HOH A 311     -35.410   9.248 -15.557  1.00 45.98           O  
ANISOU 2051  O   HOH A 311     4856   5517   7097    696  -2004   -321       O  
HETATM 2052  O   HOH A 312     -29.111  18.312 -11.221  1.00 52.41           O  
ANISOU 2052  O   HOH A 312     7675   7654   4583  -2682  -2625   1213       O  
HETATM 2053  O   HOH A 313     -28.802 -37.187  -7.190  1.00 55.48           O  
ANISOU 2053  O   HOH A 313     8285   5656   7139   -210    673    395       O  
HETATM 2054  O   HOH A 314     -31.075 -34.316  -0.614  1.00 54.06           O  
ANISOU 2054  O   HOH A 314     2534   6653  11353   -393   -729   -532       O  
HETATM 2055  O   HOH A 315     -15.346  -5.636 -26.317  1.00 55.14           O  
ANISOU 2055  O   HOH A 315     8447   7606   4897  -2535    572   -954       O  
HETATM 2056  O   HOH A 316     -11.208  -0.119  -3.714  1.00 44.63           O  
ANISOU 2056  O   HOH A 316     5985   6169   4802  -1154   1738    -19       O  
HETATM 2057  O   HOH A 317     -25.265 -32.507  -2.363  1.00 46.12           O  
ANISOU 2057  O   HOH A 317     6467   5483   5570    535    586   1988       O  
HETATM 2058  O   HOH A 318     -44.868  -4.665  -4.217  1.00 55.36           O  
ANISOU 2058  O   HOH A 318     2498   7171  11365    905   -258    423       O  
HETATM 2059  O   HOH A 319     -41.487 -14.288 -15.143  1.00 44.51           O  
ANISOU 2059  O   HOH A 319     5320   5345   6245   -273   1487  -1944       O  
HETATM 2060  O   HOH A 320     -31.281  -2.032 -27.594  1.00 41.25           O  
ANISOU 2060  O   HOH A 320     3686   5259   6727   -254   -276    662       O  
HETATM 2061  O   HOH A 321     -29.785 -22.039 -24.487  1.00 46.04           O  
ANISOU 2061  O   HOH A 321     5531   5369   6592   -294  -1151    105       O  
HETATM 2062  O   HOH A 322     -31.382  14.226 -16.386  1.00 47.46           O  
ANISOU 2062  O   HOH A 322     3464   6510   8059    799    631    908       O  
HETATM 2063  O   HOH A 323     -35.930  -1.272   5.851  1.00 30.50           O  
ANISOU 2063  O   HOH A 323     3645   3252   4690   -240    184   -613       O  
HETATM 2064  O   HOH A 324     -25.923 -31.446 -15.918  1.00 50.62           O  
ANISOU 2064  O   HOH A 324     7008   6560   5663    297    647  -2475       O  
HETATM 2065  O   HOH A 325     -27.416   3.397 -26.229  1.00 52.01           O  
ANISOU 2065  O   HOH A 325     6829   7370   5561  -2330  -1227    409       O  
HETATM 2066  O   HOH A 326     -13.373   2.656  -2.214  1.00 32.02           O  
ANISOU 2066  O   HOH A 326     4603   3158   4402   -622   -114    145       O  
HETATM 2067  O   HOH A 327     -29.351  12.223 -21.660  1.00 67.52           O  
ANISOU 2067  O   HOH A 327     8137   4646  12869    111  -1654   -187       O  
HETATM 2068  O   HOH A 328     -38.594 -19.100 -17.366  1.00 43.28           O  
ANISOU 2068  O   HOH A 328     5320   4130   6994    716    691   -706       O  
HETATM 2069  O   HOH A 329     -25.151 -30.246 -18.505  1.00 49.87           O  
ANISOU 2069  O   HOH A 329     7665   5251   6032   1537   -210  -1040       O  
HETATM 2070  O   HOH A 330     -26.641   8.318 -23.225  1.00 45.02           O  
ANISOU 2070  O   HOH A 330     7141   5602   4361   -459  -1035   1571       O  
HETATM 2071  O   HOH A 331     -26.372 -29.527 -24.634  1.00 51.72           O  
ANISOU 2071  O   HOH A 331     5341   5013   9297  -1460   2014  -1392       O  
HETATM 2072  O   HOH A 332     -27.896 -12.935   5.650  1.00 33.44           O  
ANISOU 2072  O   HOH A 332     4345   3918   4441   -648    -17   -550       O  
HETATM 2073  O   HOH A 333     -32.310   0.575 -27.712  1.00 51.35           O  
ANISOU 2073  O   HOH A 333     7135   6593   5781   1002    130   1547       O  
HETATM 2074  O   HOH A 334     -30.735   4.960 -25.378  1.00 51.72           O  
ANISOU 2074  O   HOH A 334     7219   5753   6678   -951    770   1468       O  
HETATM 2075  O   HOH A 335     -17.449   7.867  -7.637  1.00 26.67           O  
ANISOU 2075  O   HOH A 335     3844   3200   3088    -27   -511   -347       O  
HETATM 2076  O   HOH A 336     -43.182  -8.222 -14.314  1.00 50.85           O  
ANISOU 2076  O   HOH A 336     6886   4353   8081   -223  -2651  -1162       O  
HETATM 2077  O   HOH A 337     -26.905  14.606 -19.005  1.00 57.76           O  
ANISOU 2077  O   HOH A 337     6789   6519   8635   -756  -1094    379       O  
HETATM 2078  O   HOH A 338     -27.607  -4.534 -21.831  1.00 55.46           O  
ANISOU 2078  O   HOH A 338     9342   5781   5950   1414   -599    988       O  
HETATM 2079  O   HOH A 339     -35.394   9.188 -18.127  1.00 57.42           O  
ANISOU 2079  O   HOH A 339     8053   5867   7897   -705  -3436   1763       O  
HETATM 2080  O   HOH A 340     -13.222  -7.297 -25.896  1.00 57.15           O  
ANISOU 2080  O   HOH A 340     9237   5582   6895    614    545   1602       O  
HETATM 2081  O   HOH A 341     -28.618 -34.084  -0.410  1.00 48.29           O  
ANISOU 2081  O   HOH A 341     6560   3949   7836   -928    585    945       O  
HETATM 2082  O   HOH A 342     -27.468 -33.701 -15.389  1.00 48.06           O  
ANISOU 2082  O   HOH A 342     5624   5418   7217  -1745   -720    443       O  
HETATM 2083  O   HOH A 343     -34.854 -38.368   6.034  1.00 48.94           O  
ANISOU 2083  O   HOH A 343     5370   6459   6766     77    334    676       O  
HETATM 2084  O   HOH A 344     -37.545 -21.662   4.017  1.00 42.75           O  
ANISOU 2084  O   HOH A 344     5770   4875   5598   -611   1024   1038       O  
HETATM 2085  O   HOH A 345      -9.524  -5.474 -17.794  1.00 49.41           O  
ANISOU 2085  O   HOH A 345     7163   3839   7771  -2010     66  -1128       O  
HETATM 2086  O   HOH A 346     -26.040 -10.115 -17.810  1.00 46.19           O  
ANISOU 2086  O   HOH A 346     7006   6095   4448  -1118   -390    264       O  
HETATM 2087  O   HOH A 347     -27.246 -12.200 -19.034  1.00 47.13           O  
ANISOU 2087  O   HOH A 347     6824   6599   4483   1575   -714   -387       O  
HETATM 2088  O   HOH A 348     -13.919 -18.062   4.136  1.00 27.73           O  
ANISOU 2088  O   HOH A 348     3908   3407   3221    280    548    516       O  
HETATM 2089  O   HOH A 349     -41.145 -18.614 -10.246  1.00 45.28           O  
ANISOU 2089  O   HOH A 349     5325   5853   6025  -1800  -1014   -656       O  
HETATM 2090  O   HOH A 350     -14.513 -29.640  -8.664  1.00 51.37           O  
ANISOU 2090  O   HOH A 350     5682   6176   7660    487   3132   -402       O  
HETATM 2091  O   HOH A 351     -23.432 -16.207   9.565  1.00 47.99           O  
ANISOU 2091  O   HOH A 351     8586   5615   4032  -2661    540   -136       O  
HETATM 2092  O   HOH A 352     -31.415 -26.353  -8.142  1.00 29.11           O  
ANISOU 2092  O   HOH A 352     3033   3774   4252   -184    324   -440       O  
HETATM 2093  O   HOH A 353     -27.116   2.218  -3.814  1.00 28.91           O  
ANISOU 2093  O   HOH A 353     4233   3361   3388   -427    382   -533       O  
HETATM 2094  O   HOH A 354     -13.262 -26.141 -10.469  1.00 32.18           O  
ANISOU 2094  O   HOH A 354     3760   4116   4350    598    462    534       O  
HETATM 2095  O   HOH A 355     -14.181 -27.789  -3.973  1.00 50.29           O  
ANISOU 2095  O   HOH A 355     7354   5210   6544   1789   1043   1077       O  
HETATM 2096  O   HOH A 356     -30.889 -22.921   9.263  1.00 52.56           O  
ANISOU 2096  O   HOH A 356     5959   6711   7299    267   -687   1435       O  
HETATM 2097  O   HOH A 357     -23.312  11.309 -21.398  1.00 53.65           O  
ANISOU 2097  O   HOH A 357     6388   6538   7458  -1254   -419   3249       O  
HETATM 2098  O   HOH A 358     -24.141  15.182 -12.687  1.00 51.25           O  
ANISOU 2098  O   HOH A 358     6721   6236   6515   2351  -3626  -3249       O  
HETATM 2099  O   HOH A 359     -31.966 -35.860   7.529  1.00 49.96           O  
ANISOU 2099  O   HOH A 359     6062   5838   7080  -1459  -1246   1134       O  
HETATM 2100  O   HOH A 360     -31.651 -35.919   4.288  1.00 41.43           O  
ANISOU 2100  O   HOH A 360     3817   5307   6617   -224    -22    315       O  
HETATM 2101  O   HOH A 361     -10.230 -26.710  -2.268  1.00 47.55           O  
ANISOU 2101  O   HOH A 361     6358   4952   6756   1496  -1372   -658       O  
HETATM 2102  O   HOH A 362     -11.125 -11.297   6.859  1.00 45.95           O  
ANISOU 2102  O   HOH A 362     7260   6116   4080    -47   -807    723       O  
HETATM 2103  O   HOH A 363     -29.673 -24.675  10.713  1.00 62.54           O  
ANISOU 2103  O   HOH A 363     8681   7697   7383   2137   -728  -2136       O  
HETATM 2104  O   HOH A 364     -17.465   1.272 -26.497  1.00 55.09           O  
ANISOU 2104  O   HOH A 364     7896   7492   5544  -1423   -967     12       O  
HETATM 2105  O   HOH A 365      -8.374 -22.679 -22.266  1.00 55.02           O  
ANISOU 2105  O   HOH A 365     5804   8190   6908   1979    767   -881       O  
HETATM 2106  O   HOH A 366      -5.629 -22.660  -7.399  1.00 51.07           O  
ANISOU 2106  O   HOH A 366     3394   7525   8483   3298    -97  -2219       O  
HETATM 2107  O   HOH A 367     -30.880 -14.683  -6.385  1.00 25.05           O  
ANISOU 2107  O   HOH A 367     3265   3073   3176     35   -383   -420       O  
HETATM 2108  O   HOH A 368     -41.716  -0.695  -8.140  1.00 46.52           O  
ANISOU 2108  O   HOH A 368     4480   4567   8627   1548   -223     58       O  
HETATM 2109  O   HOH A 369     -29.142  -9.485   7.620  1.00 37.34           O  
ANISOU 2109  O   HOH A 369     5428   4936   3824  -1280    588   -231       O  
HETATM 2110  O   HOH A 370     -34.815  -0.239  -7.924  1.00 30.30           O  
ANISOU 2110  O   HOH A 370     3915   3650   3948    203   -912   -239       O  
HETATM 2111  O   HOH A 371      -6.003  -9.555 -14.578  1.00 39.36           O  
ANISOU 2111  O   HOH A 371     5391   5218   4345  -1483    833    273       O  
HETATM 2112  O   HOH A 372     -24.925  11.699 -10.820  1.00 30.08           O  
ANISOU 2112  O   HOH A 372     3532   4229   3668    -17   -505    212       O  
HETATM 2113  O   HOH A 373     -26.696  10.859  -9.308  1.00 32.91           O  
ANISOU 2113  O   HOH A 373     4112   4480   3911  -1095   -425    269       O  
HETATM 2114  O   HOH A 374     -30.259  -6.525   3.208  1.00 25.94           O  
ANISOU 2114  O   HOH A 374     3310   3130   3416     46    530   -352       O  
HETATM 2115  O   HOH A 375     -29.058   7.891  -9.716  1.00 32.39           O  
ANISOU 2115  O   HOH A 375     4376   4538   3390    795   -104    204       O  
HETATM 2116  O   HOH A 376      -8.328 -22.749 -17.683  1.00 43.70           O  
ANISOU 2116  O   HOH A 376     4544   5723   6337   1155   1173     61       O  
HETATM 2117  O   HOH A 377     -13.839  -5.642 -19.953  1.00 32.84           O  
ANISOU 2117  O   HOH A 377     5812   3332   3333    304    435    -23       O  
HETATM 2118  O   HOH A 378     -21.998  -5.568 -15.502  1.00 33.49           O  
ANISOU 2118  O   HOH A 378     4520   3786   4417   -645    222    992       O  
HETATM 2119  O   HOH A 379     -23.762  -9.068 -18.169  1.00 27.76           O  
ANISOU 2119  O   HOH A 379     3940   3790   2815    293   -457   -137       O  
HETATM 2120  O   HOH A 380     -18.451  11.760 -11.127  1.00 27.21           O  
ANISOU 2120  O   HOH A 380     3518   3954   2866   -217   -538    527       O  
HETATM 2121  O   HOH A 381     -11.810 -14.169   6.300  1.00 31.59           O  
ANISOU 2121  O   HOH A 381     4548   4543   2909    535    129    -51       O  
HETATM 2122  O   HOH A 382      -7.978 -15.734 -21.854  1.00 42.27           O  
ANISOU 2122  O   HOH A 382     5738   6211   4108   -724    622  -1092       O  
HETATM 2123  O   HOH A 383     -37.297   2.674  -7.609  1.00 33.87           O  
ANISOU 2123  O   HOH A 383     3807   3729   5332    173   -252   -804       O  
HETATM 2124  O   HOH A 384     -35.024  -7.739   4.200  1.00 36.75           O  
ANISOU 2124  O   HOH A 384     4390   5062   4508    765    389   -460       O  
HETATM 2125  O   HOH A 385     -33.517  -5.018 -17.047  1.00 38.96           O  
ANISOU 2125  O   HOH A 385     4882   4556   5364   1357  -1624  -1015       O  
HETATM 2126  O   HOH A 386     -23.362 -31.658 -15.220  1.00 55.56           O  
ANISOU 2126  O   HOH A 386     7081   6372   7655  -2259    504   -569       O  
HETATM 2127  O   HOH A 387     -12.149 -11.679 -24.795  1.00 36.90           O  
ANISOU 2127  O   HOH A 387     5595   3630   4794   -778    363    250       O  
HETATM 2128  O   HOH A 388     -33.732 -34.099  -7.490  1.00 52.23           O  
ANISOU 2128  O   HOH A 388     5436   6079   8328  -1595   -128   1199       O  
HETATM 2129  O   HOH A 389     -27.782 -31.566  -1.431  1.00 30.36           O  
ANISOU 2129  O   HOH A 389     4118   3424   3990   -566    522   -286       O  
HETATM 2130  O   HOH A 390     -28.324  -6.484 -12.262  1.00 30.47           O  
ANISOU 2130  O   HOH A 390     4433   3490   3652    538   -761    -48       O  
HETATM 2131  O   HOH A 391     -11.608  -3.618  -6.050  1.00 32.76           O  
ANISOU 2131  O   HOH A 391     4418   2716   5314   -811    184     49       O  
HETATM 2132  O   HOH A 392     -25.512 -14.342  10.028  1.00 45.24           O  
ANISOU 2132  O   HOH A 392     6700   5163   5325   -519    171   1075       O  
HETATM 2133  O   HOH A 393     -11.788 -24.711 -22.969  1.00 40.87           O  
ANISOU 2133  O   HOH A 393     7915   4095   3518   2094   2279   -879       O  
HETATM 2134  O   HOH A 394     -43.843 -33.147  -5.273  1.00 30.66           O  
ANISOU 2134  O   HOH A 394     2992   4250   4407   -186    508    300       O  
HETATM 2135  O   HOH A 395      -9.230 -15.292  -0.202  1.00 29.38           O  
ANISOU 2135  O   HOH A 395     3879   4000   3281    152    272    274       O  
HETATM 2136  O   HOH A 396     -11.558  -4.255 -19.025  1.00 43.25           O  
ANISOU 2136  O   HOH A 396     6314   5303   4815   -348   1648    111       O  
HETATM 2137  O   HOH A 397     -31.403  -6.787   7.071  1.00 36.58           O  
ANISOU 2137  O   HOH A 397     5132   4207   4557    251    739    978       O  
HETATM 2138  O   HOH A 398     -37.901 -12.481 -14.595  1.00 36.75           O  
ANISOU 2138  O   HOH A 398     3927   5032   5005    133   -969  -1152       O  
HETATM 2139  O   HOH A 399     -33.463 -21.692  -8.692  1.00 29.29           O  
ANISOU 2139  O   HOH A 399     3289   3586   4252   -364    173   -363       O  
HETATM 2140  O   HOH A 400     -13.315  -8.387 -23.454  1.00 41.69           O  
ANISOU 2140  O   HOH A 400     6591   4797   4450   -944    605   -492       O  
HETATM 2141  O   HOH A 401     -10.188  -2.345  -7.768  1.00 34.94           O  
ANISOU 2141  O   HOH A 401     4802   4956   3518   1343    896    821       O  
HETATM 2142  O   HOH A 402     -29.749   4.780  -6.682  1.00 33.82           O  
ANISOU 2142  O   HOH A 402     4409   4361   4077    884   -694   -963       O  
HETATM 2143  O   HOH A 403      -3.796  -8.691  -7.595  1.00 45.27           O  
ANISOU 2143  O   HOH A 403     3898   6761   6542   -588   -218    532       O  
HETATM 2144  O   HOH A 404     -19.770   0.419 -15.534  1.00 33.40           O  
ANISOU 2144  O   HOH A 404     4684   4574   3431    -85    -94    208       O  
HETATM 2145  O   HOH A 405     -26.883 -12.861 -16.189  1.00 29.55           O  
ANISOU 2145  O   HOH A 405     4133   3470   3622    -15     52   -290       O  
HETATM 2146  O   HOH A 406     -26.768 -24.889 -25.330  1.00 36.01           O  
ANISOU 2146  O   HOH A 406     4234   4543   4904    385     85   -185       O  
HETATM 2147  O   HOH A 407     -23.429 -22.762   4.832  1.00 29.93           O  
ANISOU 2147  O   HOH A 407     4797   3286   3288   -338    -27   -121       O  
HETATM 2148  O   HOH A 408     -32.514  -2.164 -23.254  1.00 35.94           O  
ANISOU 2148  O   HOH A 408     5449   3933   4272   1142   -216   -327       O  
HETATM 2149  O   HOH A 409     -41.460   1.597  -9.208  1.00 46.13           O  
ANISOU 2149  O   HOH A 409     5783   6242   5501   -214  -1023    134       O  
HETATM 2150  O   HOH A 410     -23.430 -30.384  -2.430  1.00 39.06           O  
ANISOU 2150  O   HOH A 410     4765   5453   4622   -870    674    752       O  
HETATM 2151  O   HOH A 411     -21.901 -21.879 -29.987  1.00 39.14           O  
ANISOU 2151  O   HOH A 411     5790   5247   3834    920   -415  -1037       O  
HETATM 2152  O   HOH A 412     -12.445  -2.085 -17.276  1.00 39.84           O  
ANISOU 2152  O   HOH A 412     5131   4927   5078  -1460    884  -1288       O  
HETATM 2153  O   HOH A 413     -14.624 -27.934 -23.856  1.00 32.42           O  
ANISOU 2153  O   HOH A 413     3811   4171   4333    603   -422   -790       O  
HETATM 2154  O   HOH A 414     -38.081  -2.585 -12.625  1.00 37.74           O  
ANISOU 2154  O   HOH A 414     4948   5077   4312   -444   -910   -760       O  
HETATM 2155  O   HOH A 415     -36.855  -3.561 -25.185  1.00 38.35           O  
ANISOU 2155  O   HOH A 415     4779   4737   5054    -14  -1537    752       O  
HETATM 2156  O   HOH A 416     -11.127 -23.938  -5.915  1.00 32.50           O  
ANISOU 2156  O   HOH A 416     3940   4006   4400    626    445    233       O  
HETATM 2157  O   HOH A 417     -26.444 -19.226 -22.132  1.00 33.90           O  
ANISOU 2157  O   HOH A 417     3854   5254   3772    898   -558   -756       O  
HETATM 2158  O   HOH A 418     -33.619  -5.258 -19.782  1.00 51.35           O  
ANISOU 2158  O   HOH A 418     6466   6000   7043    949  -2203  -1560       O  
HETATM 2159  O   HOH A 419     -23.710 -26.474 -24.655  1.00 32.11           O  
ANISOU 2159  O   HOH A 419     4465   4562   3172   -210   -257  -1256       O  
HETATM 2160  O   HOH A 420     -37.459   7.337  -8.377  1.00 41.57           O  
ANISOU 2160  O   HOH A 420     4854   3976   6965    915   -572    103       O  
HETATM 2161  O   HOH A 421     -29.457   3.995  -4.005  1.00 28.73           O  
ANISOU 2161  O   HOH A 421     4369   2688   3856    135   -622   -311       O  
HETATM 2162  O   HOH A 422     -11.562   8.395 -13.399  1.00 39.12           O  
ANISOU 2162  O   HOH A 422     5202   3695   5966   -544   -177    227       O  
HETATM 2163  O   HOH A 423     -12.318  -2.914 -12.522  1.00 30.14           O  
ANISOU 2163  O   HOH A 423     3639   3397   4416   -226   -151   -156       O  
HETATM 2164  O   HOH A 424      -8.038 -25.308 -14.165  1.00 49.73           O  
ANISOU 2164  O   HOH A 424     6647   6208   6037    216   1944    814       O  
HETATM 2165  O   HOH A 425     -15.639 -27.720 -11.282  1.00 30.79           O  
ANISOU 2165  O   HOH A 425     3805   4183   3710    667    -71   -551       O  
HETATM 2166  O   HOH A 426     -37.792   2.336 -23.641  1.00 36.55           O  
ANISOU 2166  O   HOH A 426     5959   4263   3665   -415  -1515    976       O  
HETATM 2167  O   HOH A 427     -27.390 -15.408 -17.460  1.00 47.05           O  
ANISOU 2167  O   HOH A 427     4532   4762   8580   -258   -543  -1089       O  
HETATM 2168  O   HOH A 428     -19.913 -28.955  -0.365  1.00 50.33           O  
ANISOU 2168  O   HOH A 428     3881   5300   9939    837   -926   1488       O  
HETATM 2169  O   HOH A 429     -42.792  -1.586  -3.634  1.00 41.98           O  
ANISOU 2169  O   HOH A 429     3664   5612   6675    991   -432   -157       O  
HETATM 2170  O   HOH A 430     -32.890  -6.460   4.397  1.00 34.39           O  
ANISOU 2170  O   HOH A 430     4565   4663   3838     58   1174    354       O  
HETATM 2171  O   HOH A 431     -12.869  10.231 -11.977  1.00 35.19           O  
ANISOU 2171  O   HOH A 431     4896   4510   3964    151   -512   -295       O  
HETATM 2172  O   HOH A 432     -32.979   0.634   4.679  1.00 27.51           O  
ANISOU 2172  O   HOH A 432     3433   3019   3999   -287    -47    -59       O  
HETATM 2173  O   HOH A 433     -43.236 -16.721  -0.955  1.00 39.44           O  
ANISOU 2173  O   HOH A 433     4498   3509   6978   -929    786   -367       O  
HETATM 2174  O   HOH A 434     -38.996 -14.691 -15.559  1.00 37.73           O  
ANISOU 2174  O   HOH A 434     4245   4310   5780   -719   -726  -1063       O  
HETATM 2175  O   HOH A 435      -3.961 -16.756  -5.339  1.00 46.97           O  
ANISOU 2175  O   HOH A 435     4404   7440   6000  -1576    168   -805       O  
HETATM 2176  O   HOH A 436     -27.680 -20.268 -24.885  1.00 44.45           O  
ANISOU 2176  O   HOH A 436     4703   5774   6410    926   -542  -1647       O  
HETATM 2177  O   HOH A 437      -6.571 -22.274 -11.180  1.00 45.68           O  
ANISOU 2177  O   HOH A 437     3902   9168   4286    395   -686    817       O  
HETATM 2178  O   HOH A 438     -24.276  -6.856 -19.668  1.00 39.75           O  
ANISOU 2178  O   HOH A 438     5432   4435   5236   -487   -882   -783       O  
HETATM 2179  O   HOH A 439      -9.366   7.040 -12.739  1.00 42.45           O  
ANISOU 2179  O   HOH A 439     3996   5199   6933   -113   -468   1740       O  
HETATM 2180  O   HOH A 440     -17.915  -4.241 -22.117  1.00 44.58           O  
ANISOU 2180  O   HOH A 440     7186   4178   5572    -93   -880   -860       O  
HETATM 2181  O   HOH A 441     -16.967  -4.818 -18.252  1.00 39.95           O  
ANISOU 2181  O   HOH A 441     5610   4289   5279    308   -966   -166       O  
HETATM 2182  O   HOH A 442     -18.112 -10.477   8.261  1.00 36.81           O  
ANISOU 2182  O   HOH A 442     5291   4158   4533    497     85   -581       O  
HETATM 2183  O   HOH A 443     -22.979 -13.761 -24.840  1.00 45.20           O  
ANISOU 2183  O   HOH A 443     4507   8547   4117   1549   -428    488       O  
HETATM 2184  O   HOH A 444     -14.615   9.867  -9.997  1.00 29.19           O  
ANISOU 2184  O   HOH A 444     4065   4010   3013   -546    343   -172       O  
HETATM 2185  O   HOH A 445     -44.947 -20.928  -8.865  1.00 45.00           O  
ANISOU 2185  O   HOH A 445     4812   5294   6989   -947  -1247  -1324       O  
HETATM 2186  O   HOH A 446     -15.136 -29.867 -12.778  1.00 46.99           O  
ANISOU 2186  O   HOH A 446     5934   6483   5434   -203  -1521   -552       O  
HETATM 2187  O   HOH A 447     -21.830 -14.719 -28.932  1.00 57.42           O  
ANISOU 2187  O   HOH A 447     8845   7309   5662   2364   -620   1001       O  
HETATM 2188  O   HOH A 448     -43.256 -33.208  -7.863  1.00 49.30           O  
ANISOU 2188  O   HOH A 448     6414   7180   5137  -1045   -967    234       O  
HETATM 2189  O   HOH A 449     -10.622  -2.191 -10.462  1.00 43.10           O  
ANISOU 2189  O   HOH A 449     4754   6123   5496   -751    566   -865       O  
HETATM 2190  O   HOH A 450     -36.609 -19.420   5.385  1.00 36.47           O  
ANISOU 2190  O   HOH A 450     4412   4595   4848    653   1315    -78       O  
HETATM 2191  O   HOH A 451     -30.334  -7.953 -21.104  1.00 52.57           O  
ANISOU 2191  O   HOH A 451     7852   6816   5306   -224   -150  -1744       O  
HETATM 2192  O   HOH A 452     -41.605 -37.705  -3.110  1.00 55.25           O  
ANISOU 2192  O   HOH A 452     5484   5794   9715   -945    633   1004       O  
HETATM 2193  O   HOH A 453     -35.699 -24.566 -17.675  1.00 57.98           O  
ANISOU 2193  O   HOH A 453     5941   8704   7383   1667  -1622    692       O  
HETATM 2194  O   HOH A 454     -20.096  -5.048 -17.377  1.00 54.59           O  
ANISOU 2194  O   HOH A 454     5126   9668   5944   -448   -842    702       O  
HETATM 2195  O   HOH A 455     -10.390  -5.826 -12.710  1.00 74.24           O  
ANISOU 2195  O   HOH A 455    10512  10296   7397   3681    742   1648       O  
HETATM 2196  O   HOH A 456     -29.469 -11.822   9.706  1.00 35.94           O  
ANISOU 2196  O   HOH A 456     4204   4295   5157    562    289   -305       O  
HETATM 2197  O   HOH A 457      -4.062 -21.724  -3.443  1.00 56.89           O  
ANISOU 2197  O   HOH A 457     4484   7967   9164    298   1122  -1433       O  
HETATM 2198  O   HOH A 458     -11.099  -2.819 -14.949  1.00 40.94           O  
ANISOU 2198  O   HOH A 458     5188   5419   4945     -9     -2  -1314       O  
HETATM 2199  O   HOH A 459     -14.923 -22.310 -30.703  1.00 43.66           O  
ANISOU 2199  O   HOH A 459     6854   4464   5269   -932    477    -78       O  
HETATM 2200  O   HOH A 460     -15.989 -27.121 -19.028  1.00 40.70           O  
ANISOU 2200  O   HOH A 460     4013   6400   5051    495   1573   -816       O  
HETATM 2201  O   HOH A 461     -17.451 -13.475 -28.499  1.00 51.41           O  
ANISOU 2201  O   HOH A 461     6595   8454   4485   -181     71    355       O  
HETATM 2202  O   HOH A 462     -33.901 -37.402   3.662  1.00 43.91           O  
ANISOU 2202  O   HOH A 462     5401   3590   7692   -773    387    675       O  
HETATM 2203  O   HOH A 463     -29.858 -30.579 -16.684  1.00 48.74           O  
ANISOU 2203  O   HOH A 463     8190   4662   5664  -2028   -928    -54       O  
HETATM 2204  O   HOH A 464     -21.944   7.491 -26.044  1.00 46.98           O  
ANISOU 2204  O   HOH A 464     6290   7500   4058   -672  -1404    544       O  
HETATM 2205  O   HOH A 465     -44.223  -9.013 -10.130  1.00 58.11           O  
ANISOU 2205  O   HOH A 465     5591   8556   7932   1710  -2260   -736       O  
HETATM 2206  O   HOH A 466     -31.554 -16.733 -22.101  1.00 38.60           O  
ANISOU 2206  O   HOH A 466     6629   3295   4740    294   -349   -295       O  
HETATM 2207  O   HOH A 467     -17.693 -16.884 -28.892  1.00 48.54           O  
ANISOU 2207  O   HOH A 467     6480   7521   4440    333   1141  -1431       O  
HETATM 2208  O   HOH A 468     -30.910   8.625 -11.683  1.00 43.93           O  
ANISOU 2208  O   HOH A 468     5187   6726   4777    852  -1038    281       O  
HETATM 2209  O   HOH A 469      -6.788 -17.787 -22.706  1.00 40.48           O  
ANISOU 2209  O   HOH A 469     3933   6055   5392      7    883    -81       O  
HETATM 2210  O   HOH A 470     -38.086 -10.917   3.199  1.00 37.82           O  
ANISOU 2210  O   HOH A 470     4650   5076   4644    791    967   -615       O  
HETATM 2211  O   HOH A 471     -10.384   2.487 -15.643  1.00 37.71           O  
ANISOU 2211  O   HOH A 471     5508   4670   4148     -9   1118     44       O  
HETATM 2212  O   HOH A 472     -35.951   4.572 -19.361  1.00 44.49           O  
ANISOU 2212  O   HOH A 472     5225   5871   5808    -14  -1321   2012       O  
HETATM 2213  O   HOH A 473     -33.765 -22.787  11.205  1.00 64.88           O  
ANISOU 2213  O   HOH A 473     8780  10120   5750  -1695   -631   2066       O  
HETATM 2214  O   HOH A 474     -16.274  12.138  -8.887  1.00 39.05           O  
ANISOU 2214  O   HOH A 474     6771   4433   3632  -1555   1668  -1160       O  
HETATM 2215  O   HOH A 475      -6.684 -22.575 -20.037  1.00 48.87           O  
ANISOU 2215  O   HOH A 475     4537   6697   7332   1651   4026  -1939       O  
HETATM 2216  O   HOH A 476     -13.296   9.055  -7.384  1.00 44.57           O  
ANISOU 2216  O   HOH A 476     6048   7114   3770    309   2017    284       O  
HETATM 2217  O   HOH A 477      -3.546 -18.711  -9.135  1.00 52.14           O  
ANISOU 2217  O   HOH A 477     4712   6439   8658    103    268   -137       O  
HETATM 2218  O   HOH A 478     -13.614  -6.143 -22.394  1.00 45.02           O  
ANISOU 2218  O   HOH A 478     5829   5121   6154   -632    -15     22       O  
HETATM 2219  O   HOH A 479      -6.549 -21.841 -15.900  1.00 54.89           O  
ANISOU 2219  O   HOH A 479     5653   7983   7220   -336   1111   -209       O  
HETATM 2220  O   HOH A 480     -33.211 -38.580  -5.866  1.00 45.61           O  
ANISOU 2220  O   HOH A 480     3425   5468   8435    149    608  -1781       O  
HETATM 2221  O   HOH A 481     -40.038   3.308  -7.609  1.00 46.28           O  
ANISOU 2221  O   HOH A 481     5017   7423   5142    160     40     29       O  
HETATM 2222  O   HOH A 482     -32.417 -23.610 -21.702  1.00 52.95           O  
ANISOU 2222  O   HOH A 482     6004   5851   8261    866    983   -259       O  
HETATM 2223  O   HOH A 483     -10.187   0.343 -11.232  1.00 50.21           O  
ANISOU 2223  O   HOH A 483     6255   5551   7272    -48    761   2314       O  
HETATM 2224  O   HOH A 484     -42.848 -14.787 -11.682  1.00 39.93           O  
ANISOU 2224  O   HOH A 484     3874   4320   6975   -213   -918   -848       O  
HETATM 2225  O   HOH A 485     -18.803 -27.390   1.776  1.00 49.43           O  
ANISOU 2225  O   HOH A 485     6811   4397   7572   -376   -693   1235       O  
HETATM 2226  O   HOH A 486     -42.115 -28.212 -10.767  1.00 54.51           O  
ANISOU 2226  O   HOH A 486     8151   4356   8204  -1461   -553  -2850       O  
HETATM 2227  O   HOH A 487     -42.052 -16.885 -13.738  1.00 47.92           O  
ANISOU 2227  O   HOH A 487     7914   6059   4235   -622  -1184   -947       O  
HETATM 2228  O   HOH A 488     -14.052  -1.520 -22.555  1.00 57.28           O  
ANISOU 2228  O   HOH A 488     8798   7959   5006   -334    386   -789       O  
HETATM 2229  O   HOH A 489     -27.038 -28.439 -19.245  1.00 37.76           O  
ANISOU 2229  O   HOH A 489     5501   4818   4026    189    550   -909       O  
HETATM 2230  O   HOH A 490     -42.024 -22.950 -10.076  1.00 67.78           O  
ANISOU 2230  O   HOH A 490     6811  11537   7404   1589   -553  -1577       O  
HETATM 2231  O   HOH A 491     -26.499 -26.429 -20.974  1.00 37.68           O  
ANISOU 2231  O   HOH A 491     4751   4583   4981    -43    113   -483       O  
HETATM 2232  O   HOH A 492     -34.571  -9.962   5.389  1.00 36.30           O  
ANISOU 2232  O   HOH A 492     3172   5478   5141    735    625   -397       O  
HETATM 2233  O   HOH A 493     -20.384  11.914 -23.642  1.00 51.97           O  
ANISOU 2233  O   HOH A 493     6631   8264   4850   -813   -370   -412       O  
HETATM 2234  O   HOH A 494     -25.420 -34.383  -4.758  1.00 50.57           O  
ANISOU 2234  O   HOH A 494     4742   7590   6880    786   -783    472       O  
HETATM 2235  O   HOH A 495     -18.608  -2.033 -20.099  1.00 49.20           O  
ANISOU 2235  O   HOH A 495     6840   4368   7484    -22  -1372   -205       O  
HETATM 2236  O   HOH A 496     -36.732 -30.031   8.504  1.00 59.06           O  
ANISOU 2236  O   HOH A 496     8574  10378   3486   -217  -1152    101       O  
HETATM 2237  O   HOH A 497     -22.214 -11.182 -25.492  1.00 42.39           O  
ANISOU 2237  O   HOH A 497     5239   4990   5875   1171    -81    382       O  
HETATM 2238  O   HOH A 498     -32.913 -36.655  -9.072  1.00 78.95           O  
ANISOU 2238  O   HOH A 498    13152   6774  10071    984   -243   -686       O  
HETATM 2239  O   HOH A 499     -11.498   6.862  -7.210  1.00 40.94           O  
ANISOU 2239  O   HOH A 499     4160   6527   4865   -273    272    903       O  
HETATM 2240  O   HOH A 500     -10.511 -20.930   4.943  1.00 44.77           O  
ANISOU 2240  O   HOH A 500     6959   5049   5000    703    -83    439       O  
HETATM 2241  O   HOH A 501     -24.083 -10.262 -23.310  1.00 49.74           O  
ANISOU 2241  O   HOH A 501     5524   7028   6345   -567  -1406   1214       O  
HETATM 2242  O   HOH A 502     -35.463 -24.226 -14.073  1.00 58.08           O  
ANISOU 2242  O   HOH A 502     8621   8180   5265   -679   -488   -454       O  
HETATM 2243  O   HOH A 503     -21.484 -30.877   5.176  1.00 56.95           O  
ANISOU 2243  O   HOH A 503     9283   5999   6355   1004   -532   3070       O  
HETATM 2244  O   HOH A 504      -6.700  -2.300  -1.163  1.00 45.21           O  
ANISOU 2244  O   HOH A 504     4149   5461   7566    -70   -453   -803       O  
HETATM 2245  O   HOH A 505     -16.665 -20.786   9.321  1.00 46.13           O  
ANISOU 2245  O   HOH A 505     6296   5900   5328    520     42   1666       O  
HETATM 2246  O   HOH A 506     -33.471  -9.328 -19.371  1.00 45.40           O  
ANISOU 2246  O   HOH A 506     5844   4709   6698    346  -2888  -1361       O  
HETATM 2247  O   HOH A 507     -19.437  -6.593 -26.424  1.00 44.75           O  
ANISOU 2247  O   HOH A 507     6091   7129   3781   -315     96    377       O  
HETATM 2248  O   HOH A 508      -5.382 -20.968 -20.927  1.00 60.21           O  
ANISOU 2248  O   HOH A 508     7845   7227   7804  -1571   2377  -1280       O  
HETATM 2249  O   HOH A 509      -4.224 -22.488  -0.775  1.00 49.32           O  
ANISOU 2249  O   HOH A 509     4938   5859   7941   -421   1374    441       O  
HETATM 2250  O   HOH A 510     -38.665  -5.546   4.513  1.00 72.82           O  
ANISOU 2250  O   HOH A 510     7194  12046   8428  -1860    536  -2352       O  
HETATM 2251  O   HOH A 511     -22.141  -2.389 -15.834  1.00 43.65           O  
ANISOU 2251  O   HOH A 511     6015   6765   3804   1130   -476    978       O  
HETATM 2252  O   HOH A 512     -36.589   5.634 -14.803  1.00 37.05           O  
ANISOU 2252  O   HOH A 512     4872   4253   4950   1316  -1005   -316       O  
HETATM 2253  O   HOH A 513     -39.416 -19.298 -12.929  1.00 46.24           O  
ANISOU 2253  O   HOH A 513     5916   6374   5279    200   1006    891       O  
HETATM 2254  O   HOH A 514     -25.671 -22.958   6.503  1.00 37.26           O  
ANISOU 2254  O   HOH A 514     4313   4514   5330     55    402    890       O  
HETATM 2255  O   HOH A 515     -16.325 -25.283   1.930  1.00 47.40           O  
ANISOU 2255  O   HOH A 515     5905   5143   6962    853    418   2716       O  
HETATM 2256  O   HOH A 516      -4.457 -16.825 -20.883  1.00 58.80           O  
ANISOU 2256  O   HOH A 516     5035   9450   7854    819     86    235       O  
HETATM 2257  O   HOH A 517      -9.326  -7.982 -22.763  1.00 55.13           O  
ANISOU 2257  O   HOH A 517     6814   8261   5870   1970   2588   -394       O  
HETATM 2258  O   HOH A 518     -15.455   0.328 -20.828  1.00 45.01           O  
ANISOU 2258  O   HOH A 518     6275   6612   4214   -741    442   1505       O  
HETATM 2259  O   HOH A 519      -7.044 -11.836 -20.458  1.00 49.41           O  
ANISOU 2259  O   HOH A 519     7577   5807   5386    258   1618   -873       O  
HETATM 2260  O   HOH A 520     -21.860 -19.180 -29.154  1.00 57.72           O  
ANISOU 2260  O   HOH A 520     8455   5894   7580   1370   1990   -379       O  
HETATM 2261  O   HOH A 521      -6.687  -6.973 -14.255  1.00 50.73           O  
ANISOU 2261  O   HOH A 521     7446   5402   6423    -23    250   -607       O  
HETATM 2262  O   HOH A 522      -9.270 -17.976   6.530  1.00 45.72           O  
ANISOU 2262  O   HOH A 522     7153   5221   4997  -1411    554    713       O  
HETATM 2263  O   HOH A 523     -26.618  15.555 -15.317  1.00 46.23           O  
ANISOU 2263  O   HOH A 523     7131   4533   5898   1954  -1272    848       O  
HETATM 2264  O   HOH A 524     -41.742  -5.589 -11.817  1.00 52.37           O  
ANISOU 2264  O   HOH A 524     4959   5338   9600    666  -1359    597       O  
HETATM 2265  O   HOH A 525     -40.515  -2.846 -10.675  1.00 54.58           O  
ANISOU 2265  O   HOH A 525     7092   6873   6772  -2103  -1869    294       O  
HETATM 2266  O   HOH A 526     -16.394 -33.979 -13.330  1.00 50.95           O  
ANISOU 2266  O   HOH A 526     8701   6097   4559   1673    493    709       O  
HETATM 2267  O   HOH A 527     -38.478 -24.934   3.150  1.00 38.88           O  
ANISOU 2267  O   HOH A 527     5516   4337   4917   -762    575   -232       O  
HETATM 2268  O   HOH A 528      -3.074 -18.886  -1.022  1.00 42.20           O  
ANISOU 2268  O   HOH A 528     4770   6058   5205   1253   -986   -709       O  
CONECT  584 1990                                                                
CONECT 1688 1993                                                                
CONECT 1719 1993                                                                
CONECT 1750 1993                                                                
CONECT 1990  584 2033                                                           
CONECT 1991 2056 2066                                                           
CONECT 1992 2106 2197                                                           
CONECT 1993 1688 1719 1750 2175                                                 
CONECT 2033 1990                                                                
CONECT 2056 1991                                                                
CONECT 2066 1991                                                                
CONECT 2106 1992                                                                
CONECT 2175 1993                                                                
CONECT 2197 1992                                                                
MASTER      423    0    4   10   12    0    6    6 2241    1   14   21          
END                                                                             



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