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HEADER    TRANSFERASE/DNA                         04-JUL-11   3SQ4              
TITLE     RB69 DNA POLYMERASE TERNARY COMPLEX WITH DTTP OPPOSITE 2AP (GC RICH   
TITLE    2 SEQUENCE)                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA POLYMERASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GP43;                                                       
COMPND   5 EC: 2.7.7.7;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-D(P*CP*(2PR)P*TP*CP*GP*CP*CP*GP*CP*CP*GP*CP*GP*CP*GP*G)-
COMPND  10 3';                                                                  
COMPND  11 CHAIN: T;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 OTHER_DETAILS: TEMPLATE;                                             
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: 5'-D(*CP*GP*CP*GP*CP*GP*GP*CP*GP*GP*CP*GP*(2DA))-3';       
COMPND  16 CHAIN: P;                                                            
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 OTHER_DETAILS: PRIMER                                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE RB69;                      
SOURCE   3 ORGANISM_TAXID: 12353;                                               
SOURCE   4 GENE: 43;                                                            
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 SYNTHETIC: YES                                                       
KEYWDS    2-AMINOPURINE, GC RICH, TRANSFERASE-DNA COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XIA,W.H.KONIGSBERG,J.WANG                                           
REVDAT   3   30-NOV-11 3SQ4    1       JRNL                                     
REVDAT   2   16-NOV-11 3SQ4    1       JRNL                                     
REVDAT   1   09-NOV-11 3SQ4    0                                                
JRNL        AUTH   L.J.REHA-KRANTZ,C.HARIHARAN,U.SUBUDDHI,S.XIA,C.ZHAO,         
JRNL        AUTH 2 J.BECKMAN,T.CHRISTIAN,W.KONIGSBERG                           
JRNL        TITL   STRUCTURE OF THE 2-AMINOPURINE-CYTOSINE BASE PAIR FORMED IN  
JRNL        TITL 2 THE POLYMERASE ACTIVE SITE OF THE RB69 Y567A-DNA POLYMERASE. 
JRNL        REF    BIOCHEMISTRY                  V.  50 10136 2011              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   22023103                                                     
JRNL        DOI    10.1021/BI2014618                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.23 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) : 2.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 88.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 54679                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2911                            
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) : 2.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3681                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 175                          
REMARK   3   BIN FREE R VALUE                    : 0.4260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7363                                    
REMARK   3   NUCLEIC ACID ATOMS       : 591                                     
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 285                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.13000                                             
REMARK   3    B22 (A**2) : 1.79000                                              
REMARK   3    B33 (A**2) : -0.67000                                             
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): 0.284         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.211         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.152         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.281        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8247 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11277 ; 1.116 ; 2.057       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   905 ; 5.100 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   376 ;34.877 ;24.202       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1349 ;15.024 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;14.700 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1193 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6102 ; 0.004 ; 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):  4507 ; 1.425 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7309 ; 2.507 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3740 ; 2.849 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3966 ; 4.263 ; 9.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
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  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     3        T    18                          
REMARK   3    RESIDUE RANGE :   P   103        P   115                          
REMARK   3    RESIDUE RANGE :   A   903        A   903                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.0420  -2.6440 -35.1860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1854 T22:   0.2730                                     
REMARK   3      T33:   0.2339 T12:   0.0472                                     
REMARK   3      T13:   0.0029 T23:   0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1238 L22:   0.0492                                     
REMARK   3      L33:   0.0537 L12:   0.0976                                     
REMARK   3      L13:   0.1264 L23:  -0.0130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2081 S12:  -0.0695 S13:   0.2642                       
REMARK   3      S21:  -0.0264 S22:   0.1024 S23:   0.0191                       
REMARK   3      S31:  -0.0026 S32:  -0.0567 S33:   0.1056                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   105                          
REMARK   3    RESIDUE RANGE :   A   340        A   389                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.7650   2.4370 -33.5300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1410 T22:   0.0998                                     
REMARK   3      T33:   0.0949 T12:   0.0001                                     
REMARK   3      T13:  -0.0131 T23:   0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1785 L22:   1.3207                                     
REMARK   3      L33:   0.5090 L12:   0.2456                                     
REMARK   3      L13:  -0.1558 L23:  -0.5312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0080 S12:   0.0127 S13:   0.0294                       
REMARK   3      S21:   0.0435 S22:  -0.0300 S23:  -0.0737                       
REMARK   3      S31:  -0.0206 S32:   0.0755 S33:   0.0219                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   106        A   339                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3480 -22.0590 -14.8710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1404 T22:   0.1027                                     
REMARK   3      T33:   0.0457 T12:   0.0016                                     
REMARK   3      T13:  -0.0123 T23:  -0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3194 L22:   0.7764                                     
REMARK   3      L33:   1.1027 L12:   0.2124                                     
REMARK   3      L13:   0.0997 L23:  -0.0272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0420 S12:  -0.0108 S13:   0.0213                       
REMARK   3      S21:   0.0984 S22:  -0.0627 S23:  -0.0098                       
REMARK   3      S31:   0.0303 S32:  -0.0774 S33:   0.0208                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   390        A   468                          
REMARK   3    RESIDUE RANGE :   A   576        A   706                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6570  -6.6670 -60.4370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1732 T22:   0.2028                                     
REMARK   3      T33:   0.0119 T12:  -0.0402                                     
REMARK   3      T13:  -0.0123 T23:   0.0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0346 L22:   0.9850                                     
REMARK   3      L33:   0.2187 L12:   0.7387                                     
REMARK   3      L13:  -0.2839 L23:  -0.0527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1450 S12:   0.3442 S13:   0.0605                       
REMARK   3      S21:  -0.1459 S22:   0.1922 S23:   0.0128                       
REMARK   3      S31:   0.0046 S32:  -0.1098 S33:  -0.0473                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   469        A   575                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3360 -25.9130 -47.0360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1700 T22:   0.1390                                     
REMARK   3      T33:   0.0491 T12:  -0.0034                                     
REMARK   3      T13:   0.0246 T23:  -0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5310 L22:   3.4064                                     
REMARK   3      L33:   0.4220 L12:  -0.0770                                     
REMARK   3      L13:  -0.1809 L23:   0.5473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0882 S12:   0.1098 S13:  -0.1349                       
REMARK   3      S21:   0.1448 S22:  -0.0217 S23:   0.0620                       
REMARK   3      S31:   0.0840 S32:   0.0269 S33:   0.1099                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   707        A   737                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6290 -22.8610 -47.9940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2007 T22:   0.1800                                     
REMARK   3      T33:   0.1033 T12:  -0.0332                                     
REMARK   3      T13:   0.0186 T23:  -0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9623 L22:   0.9262                                     
REMARK   3      L33:   0.5397 L12:  -0.1687                                     
REMARK   3      L13:  -0.6705 L23:   0.2223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1194 S12:   0.0131 S13:  -0.0943                       
REMARK   3      S21:  -0.0782 S22:   0.1158 S23:   0.0953                       
REMARK   3      S31:   0.0063 S32:   0.0663 S33:   0.0035                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   738        A   901                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3370 -20.7420 -28.0800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1462 T22:   0.1884                                     
REMARK   3      T33:   0.0379 T12:   0.0430                                     
REMARK   3      T13:   0.0098 T23:   0.0643                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2664 L22:   0.3391                                     
REMARK   3      L33:   1.6806 L12:  -0.1604                                     
REMARK   3      L13:   0.3157 L23:   0.4494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1150 S12:  -0.3851 S13:  -0.1407                       
REMARK   3      S21:   0.0267 S22:   0.1266 S23:   0.0497                       
REMARK   3      S31:   0.0382 S32:  -0.1874 S33:  -0.0116                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : RESIDUAL ONLY                                       
REMARK   4                                                                      
REMARK   4 3SQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066513.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : APEX II CCD                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54679                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.230                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 88.670                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM CALCIUM CHLORIDE, 15% W/V         
REMARK 280  PEG350 MME, 100 MM SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION,      
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
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       37.33950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.49600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.23350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.49600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.33950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.23350            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T, P                               
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 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     DC T   3   O4' -  C4' -  C3' ANGL. DEV. =  -4.3 DEGREES          
REMARK 500     DT T   5   O4' -  C1' -  N1  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DC T   6   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DC T  16   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC P 103   O4' -  C1' -  N1  ANGL. DEV. =   4.7 DEGREES          
REMARK 500     DC P 105   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DG P 112   O4' -  C1' -  N9  ANGL. DEV. =   2.8 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    TYR A  97       70.30   -118.87                                   
REMARK 500    ASN A  98       45.08    -84.94                                   
REMARK 500    PHE A 221      -69.50   -124.27                                   
REMARK 500    MET A 256      -90.27   -167.39                                   
REMARK 500    ASN A 316       74.70   -150.90                                   
REMARK 500    LYS A 352       63.62     61.95                                   
REMARK 500    SER A 414       67.41     37.49                                   
REMARK 500    ASN A 424       54.26     70.91                                   
REMARK 500    PRO A 458       -0.78    -58.99                                   
REMARK 500    ASP A 579      112.11   -160.71                                   
REMARK 500    THR A 622      -66.37     69.12                                   
REMARK 500    GLU A 686      -70.37   -107.92                                   
REMARK 500    GLU A 716       50.45     33.43                                   
REMARK 500    ASP A 899       40.76    -66.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1121        DISTANCE =  5.21 ANGSTROMS                       
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                              CA A 904  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 623   OD1                                                    
REMARK 620 2 TTP A 903   O2B  86.9                                              
REMARK 620 3 TTP A 903   O1G 157.9  78.8                                        
REMARK 620 4 ASP A 411   OD2  76.0 162.5 116.3                                  
REMARK 620 5 LEU A 412   O    92.3  87.7 103.7  96.8                            
REMARK 620 6 ASP A 411   OD1 125.0 144.8  74.1  52.5  77.5                      
REMARK 620 7 TTP A 903   O2A  69.5  80.2  91.4  90.0 158.5 122.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 906  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 531   O                                                      
REMARK 620 2 ASN A 507   OD1  79.2                                              
REMARK 620 3 ASN A 505   O   150.5  89.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 905  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP A 903   O2A                                                    
REMARK 620 2 ASP A 623   OD2  76.2                                              
REMARK 620 3 ASP A 411   OD2  82.1  78.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 908  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 116   OE2                                                    
REMARK 620 2 GLU A 116   OE1  45.5                                              
REMARK 620 3 HOH A 961   O    71.5  84.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 905                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 906                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 907                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 908                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3SQ2   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE TERNARY COMPLEX WITH DTTP OPPOSITE 2AP           
REMARK 900 (AT RICH SEQUENCE)                                                   
REMARK 900 RELATED ID: 3SUN   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DTTP                
REMARK 900 OPPOSITE 2AP (AT RICH SEQUENCE)                                      
REMARK 900 RELATED ID: 3SUO   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DTTP                
REMARK 900 OPPOSITE 2AP (GC RICH SEQUENCE)                                      
REMARK 900 RELATED ID: 3SUP   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DCTP                
REMARK 900 OPPOSITE 2AP (GC RICH SEQUENCE)                                      
REMARK 900 RELATED ID: 3SUQ   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DCTP                
REMARK 900 OPPOSITE 2AP (AT RICH SEQUENCE)                                      
DBREF  3SQ4 A    1   902  UNP    Q38087   DPOL_BPR69       1    902             
DBREF  3SQ4 T    3    18  PDB    3SQ4     3SQ4             3     18             
DBREF  3SQ4 P  103   115  PDB    3SQ4     3SQ4           103    115             
SEQADV 3SQ4 ALA A  222  UNP  Q38087    ASP   222 ENGINEERED MUTATION            
SEQADV 3SQ4 ALA A  327  UNP  Q38087    ASP   327 ENGINEERED MUTATION            
SEQRES   1 A  902  MET LYS GLU PHE TYR LEU THR VAL GLU GLN ILE GLY ASP          
SEQRES   2 A  902  SER ILE PHE GLU ARG TYR ILE ASP SER ASN GLY ARG GLU          
SEQRES   3 A  902  ARG THR ARG GLU VAL GLU TYR LYS PRO SER LEU PHE ALA          
SEQRES   4 A  902  HIS CYS PRO GLU SER GLN ALA THR LYS TYR PHE ASP ILE          
SEQRES   5 A  902  TYR GLY LYS PRO CYS THR ARG LYS LEU PHE ALA ASN MET          
SEQRES   6 A  902  ARG ASP ALA SER GLN TRP ILE LYS ARG MET GLU ASP ILE          
SEQRES   7 A  902  GLY LEU GLU ALA LEU GLY MET ASP ASP PHE LYS LEU ALA          
SEQRES   8 A  902  TYR LEU SER ASP THR TYR ASN TYR GLU ILE LYS TYR ASP          
SEQRES   9 A  902  HIS THR LYS ILE ARG VAL ALA ASN PHE ASP ILE GLU VAL          
SEQRES  10 A  902  THR SER PRO ASP GLY PHE PRO GLU PRO SER GLN ALA LYS          
SEQRES  11 A  902  HIS PRO ILE ASP ALA ILE THR HIS TYR ASP SER ILE ASP          
SEQRES  12 A  902  ASP ARG PHE TYR VAL PHE ASP LEU LEU ASN SER PRO TYR          
SEQRES  13 A  902  GLY ASN VAL GLU GLU TRP SER ILE GLU ILE ALA ALA LYS          
SEQRES  14 A  902  LEU GLN GLU GLN GLY GLY ASP GLU VAL PRO SER GLU ILE          
SEQRES  15 A  902  ILE ASP LYS ILE ILE TYR MET PRO PHE ASP ASN GLU LYS          
SEQRES  16 A  902  GLU LEU LEU MET GLU TYR LEU ASN PHE TRP GLN GLN LYS          
SEQRES  17 A  902  THR PRO VAL ILE LEU THR GLY TRP ASN VAL GLU SER PHE          
SEQRES  18 A  902  ALA ILE PRO TYR VAL TYR ASN ARG ILE LYS ASN ILE PHE          
SEQRES  19 A  902  GLY GLU SER THR ALA LYS ARG LEU SER PRO HIS ARG LYS          
SEQRES  20 A  902  THR ARG VAL LYS VAL ILE GLU ASN MET TYR GLY SER ARG          
SEQRES  21 A  902  GLU ILE ILE THR LEU PHE GLY ILE SER VAL LEU ASP TYR          
SEQRES  22 A  902  ILE ASP LEU TYR LYS LYS PHE SER PHE THR ASN GLN PRO          
SEQRES  23 A  902  SER TYR SER LEU ASP TYR ILE SER GLU PHE GLU LEU ASN          
SEQRES  24 A  902  VAL GLY LYS LEU LYS TYR ASP GLY PRO ILE SER LYS LEU          
SEQRES  25 A  902  ARG GLU SER ASN HIS GLN ARG TYR ILE SER TYR ASN ILE          
SEQRES  26 A  902  ILE ALA VAL TYR ARG VAL LEU GLN ILE ASP ALA LYS ARG          
SEQRES  27 A  902  GLN PHE ILE ASN LEU SER LEU ASP MET GLY TYR TYR ALA          
SEQRES  28 A  902  LYS ILE GLN ILE GLN SER VAL PHE SER PRO ILE LYS THR          
SEQRES  29 A  902  TRP ASP ALA ILE ILE PHE ASN SER LEU LYS GLU GLN ASN          
SEQRES  30 A  902  LYS VAL ILE PRO GLN GLY ARG SER HIS PRO VAL GLN PRO          
SEQRES  31 A  902  TYR PRO GLY ALA PHE VAL LYS GLU PRO ILE PRO ASN ARG          
SEQRES  32 A  902  TYR LYS TYR VAL MET SER PHE ASP LEU THR SER LEU TYR          
SEQRES  33 A  902  PRO SER ILE ILE ARG GLN VAL ASN ILE SER PRO GLU THR          
SEQRES  34 A  902  ILE ALA GLY THR PHE LYS VAL ALA PRO LEU HIS ASP TYR          
SEQRES  35 A  902  ILE ASN ALA VAL ALA GLU ARG PRO SER ASP VAL TYR SER          
SEQRES  36 A  902  CYS SER PRO ASN GLY MET MET TYR TYR LYS ASP ARG ASP          
SEQRES  37 A  902  GLY VAL VAL PRO THR GLU ILE THR LYS VAL PHE ASN GLN          
SEQRES  38 A  902  ARG LYS GLU HIS LYS GLY TYR MET LEU ALA ALA GLN ARG          
SEQRES  39 A  902  ASN GLY GLU ILE ILE LYS GLU ALA LEU HIS ASN PRO ASN          
SEQRES  40 A  902  LEU SER VAL ASP GLU PRO LEU ASP VAL ASP TYR ARG PHE          
SEQRES  41 A  902  ASP PHE SER ASP GLU ILE LYS GLU LYS ILE LYS LYS LEU          
SEQRES  42 A  902  SER ALA LYS SER LEU ASN GLU MET LEU PHE ARG ALA GLN          
SEQRES  43 A  902  ARG THR GLU VAL ALA GLY MET THR ALA GLN ILE ASN ARG          
SEQRES  44 A  902  LYS LEU LEU ILE ASN SER LEU TYR GLY ALA LEU GLY ASN          
SEQRES  45 A  902  VAL TRP PHE ARG TYR TYR ASP LEU ARG ASN ALA THR ALA          
SEQRES  46 A  902  ILE THR THR PHE GLY GLN MET ALA LEU GLN TRP ILE GLU          
SEQRES  47 A  902  ARG LYS VAL ASN GLU TYR LEU ASN GLU VAL CYS GLY THR          
SEQRES  48 A  902  GLU GLY GLU ALA PHE VAL LEU TYR GLY ASP THR ASP SER          
SEQRES  49 A  902  ILE TYR VAL SER ALA ASP LYS ILE ILE ASP LYS VAL GLY          
SEQRES  50 A  902  GLU SER LYS PHE ARG ASP THR ASN HIS TRP VAL ASP PHE          
SEQRES  51 A  902  LEU ASP LYS PHE ALA ARG GLU ARG MET GLU PRO ALA ILE          
SEQRES  52 A  902  ASP ARG GLY PHE ARG GLU MET CYS GLU TYR MET ASN ASN          
SEQRES  53 A  902  LYS GLN HIS LEU MET PHE MET ASP ARG GLU ALA ILE ALA          
SEQRES  54 A  902  GLY PRO PRO LEU GLY SER LYS GLY ILE GLY GLY PHE TRP          
SEQRES  55 A  902  THR GLY LYS LYS ARG TYR ALA LEU ASN VAL TRP ASP MET          
SEQRES  56 A  902  GLU GLY THR ARG TYR ALA GLU PRO LYS LEU LYS ILE MET          
SEQRES  57 A  902  GLY LEU GLU THR GLN LYS SER SER THR PRO LYS ALA VAL          
SEQRES  58 A  902  GLN LYS ALA LEU LYS GLU CYS ILE ARG ARG MET LEU GLN          
SEQRES  59 A  902  GLU GLY GLU GLU SER LEU GLN GLU TYR PHE LYS GLU PHE          
SEQRES  60 A  902  GLU LYS GLU PHE ARG GLN LEU ASN TYR ILE SER ILE ALA          
SEQRES  61 A  902  SER VAL SER SER ALA ASN ASN ILE ALA LYS TYR ASP VAL          
SEQRES  62 A  902  GLY GLY PHE PRO GLY PRO LYS CYS PRO PHE HIS ILE ARG          
SEQRES  63 A  902  GLY ILE LEU THR TYR ASN ARG ALA ILE LYS GLY ASN ILE          
SEQRES  64 A  902  ASP ALA PRO GLN VAL VAL GLU GLY GLU LYS VAL TYR VAL          
SEQRES  65 A  902  LEU PRO LEU ARG GLU GLY ASN PRO PHE GLY ASP LYS CYS          
SEQRES  66 A  902  ILE ALA TRP PRO SER GLY THR GLU ILE THR ASP LEU ILE          
SEQRES  67 A  902  LYS ASP ASP VAL LEU HIS TRP MET ASP TYR THR VAL LEU          
SEQRES  68 A  902  LEU GLU LYS THR PHE ILE LYS PRO LEU GLU GLY PHE THR          
SEQRES  69 A  902  SER ALA ALA LYS LEU ASP TYR GLU LYS LYS ALA SER LEU          
SEQRES  70 A  902  PHE ASP MET PHE ASP                                          
SEQRES   1 T   16   DC 2PR  DT  DC  DG  DC  DC  DG  DC  DC  DG  DC  DG          
SEQRES   2 T   16   DC  DG  DG                                                  
SEQRES   1 P   13   DC  DG  DC  DG  DC  DG  DG  DC  DG  DG  DC  DG 2DA          
MODRES 3SQ4 2PR T    4   DG  2-AMINOPURINE-2'-DEOXYRIBO-5'-MONOPHOSPHA          
MODRES 3SQ4 2DA P  115   DA  2',3'-DIDEOXYADENOSINE-5'-MONOPHOSPHATE            
HET    2PR  T   4      21                                                       
HET    2DA  P 115      20                                                       
HET    TTP  A 903      29                                                       
HET     CA  A 904       1                                                       
HET     CA  A 905       1                                                       
HET     CA  A 906       1                                                       
HET     CA  A 907       1                                                       
HET     CA  A 908       1                                                       
HETNAM     2PR 2-AMINO-9-[2-DEOXYRIBOFURANOSYL]-9H-PURINE-5'-                   
HETNAM   2 2PR  MONOPHOSPHATE                                                   
HETNAM     2DA 2',3'-DIDEOXYADENOSINE-5'-MONOPHOSPHATE                          
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
HETNAM      CA CALCIUM ION                                                      
HETSYN     2PR 2-AMINOPURINE-2'-DEOXYRIBO-5'-MONOPHOSPHATE                      
FORMUL   2  2PR    C10 H14 N5 O6 P                                              
FORMUL   3  2DA    C10 H14 N5 O5 P                                              
FORMUL   4  TTP    C10 H17 N2 O14 P3                                            
FORMUL   5   CA    5(CA 2+)                                                     
FORMUL  10  HOH   *285(H2 O)                                                    
HELIX    1   1 ASN A   64  GLY A   79  1                                  16    
HELIX    2   2 ASP A   87  TYR A   97  1                                  11    
HELIX    3   3 ASP A  104  ILE A  108  5                                   5    
HELIX    4   4 SER A  163  LYS A  169  1                                   7    
HELIX    5   5 LEU A  170  GLY A  174  5                                   5    
HELIX    6   6 PRO A  179  ASP A  184  1                                   6    
HELIX    7   7 ASN A  193  LYS A  208  1                                  16    
HELIX    8   8 PHE A  221  GLY A  235  1                                  15    
HELIX    9   9 GLY A  235  LYS A  240  1                                   6    
HELIX   10  10 ARG A  241  SER A  243  5                                   3    
HELIX   11  11 ASP A  272  SER A  281  1                                  10    
HELIX   12  12 SER A  289  ASN A  299  1                                  11    
HELIX   13  13 PRO A  308  ASN A  316  1                                   9    
HELIX   14  14 ASN A  316  GLN A  339  1                                  24    
HELIX   15  15 GLN A  339  LYS A  352  1                                  14    
HELIX   16  16 GLN A  354  PHE A  359  5                                   6    
HELIX   17  17 SER A  360  GLU A  375  1                                  16    
HELIX   18  18 SER A  414  ASN A  424  1                                  11    
HELIX   19  19 SER A  426  GLU A  428  5                                   3    
HELIX   20  20 PRO A  438  ASN A  444  1                                   7    
HELIX   21  21 GLY A  469  LEU A  503  1                                  35    
HELIX   22  22 SER A  523  LYS A  531  1                                   9    
HELIX   23  23 SER A  534  LEU A  570  1                                  37    
HELIX   24  24 ASP A  579  GLY A  610  1                                  32    
HELIX   25  25 ALA A  629  GLY A  637  1                                   9    
HELIX   26  26 GLU A  638  PHE A  641  5                                   4    
HELIX   27  27 ASP A  643  ARG A  658  1                                  16    
HELIX   28  28 ARG A  658  ASN A  675  1                                  18    
HELIX   29  29 LEU A  730  LYS A  734  5                                   5    
HELIX   30  30 PRO A  738  GLU A  755  1                                  18    
HELIX   31  31 GLY A  756  PHE A  771  1                                  16    
HELIX   32  32 ARG A  772  LEU A  774  5                                   3    
HELIX   33  33 ASN A  775  ALA A  780  1                                   6    
HELIX   34  34 ILE A  788  LYS A  790  5                                   3    
HELIX   35  35 PRO A  802  LYS A  816  1                                  15    
HELIX   36  36 ILE A  858  MET A  866  1                                   9    
HELIX   37  37 ASP A  867  PHE A  876  1                                  10    
HELIX   38  38 PHE A  876  LYS A  888  1                                  13    
SHEET    1   A 3 PHE A   4  ILE A  11  0                                        
SHEET    2   A 3 SER A  14  ILE A  20 -1  O  ARG A  18   N  LEU A   6           
SHEET    3   A 3 GLU A  26  VAL A  31 -1  O  ARG A  27   N  TYR A  19           
SHEET    1   B 4 SER A  36  HIS A  40  0                                        
SHEET    2   B 4 PRO A  56  LEU A  61 -1  O  LYS A  60   N  LEU A  37           
SHEET    3   B 4 TYR A  49  ASP A  51 -1  N  TYR A  49   O  CYS A  57           
SHEET    4   B 4 LYS A 378  VAL A 379  1  O  VAL A 379   N  PHE A  50           
SHEET    1   C 6 ILE A 186  PHE A 191  0                                        
SHEET    2   C 6 ARG A 145  LEU A 151  1  N  PHE A 146   O  ILE A 187           
SHEET    3   C 6 ILE A 133  ASP A 140 -1  N  ILE A 136   O  PHE A 149           
SHEET    4   C 6 VAL A 110  VAL A 117 -1  N  ASN A 112   O  TYR A 139           
SHEET    5   C 6 ILE A 212  THR A 214  1  O  THR A 214   N  ALA A 111           
SHEET    6   C 6 SER A 269  VAL A 270  1  O  SER A 269   N  LEU A 213           
SHEET    1   D 2 ASN A 153  SER A 154  0                                        
SHEET    2   D 2 GLY A 157  ASN A 158 -1  O  GLY A 157   N  SER A 154           
SHEET    1   E 2 THR A 248  ILE A 253  0                                        
SHEET    2   E 2 ARG A 260  LEU A 265 -1  O  THR A 264   N  ARG A 249           
SHEET    1   F 7 ASN A 402  ARG A 403  0                                        
SHEET    2   F 7 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   F 7 ARG A 707  MET A 715 -1  O  ARG A 707   N  THR A 703           
SHEET    4   F 7 MET A 683  ALA A 689 -1  N  ILE A 688   O  TRP A 713           
SHEET    5   F 7 VAL A 407  LEU A 412 -1  N  VAL A 407   O  ALA A 689           
SHEET    6   F 7 SER A 624  SER A 628 -1  O  VAL A 627   N  MET A 408           
SHEET    7   F 7 VAL A 617  ASP A 621 -1  N  TYR A 619   O  TYR A 626           
SHEET    1   G 4 ASN A 402  ARG A 403  0                                        
SHEET    2   G 4 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   G 4 ARG A 707  MET A 715 -1  O  ARG A 707   N  THR A 703           
SHEET    4   G 4 THR A 718  MET A 728 -1  O  MET A 728   N  TYR A 708           
SHEET    1   H 3 ILE A 430  THR A 433  0                                        
SHEET    2   H 3 MET A 461  TYR A 463 -1  O  MET A 462   N  ALA A 431           
SHEET    3   H 3 SER A 455  SER A 457 -1  N  SER A 455   O  TYR A 463           
SHEET    1   I 3 SER A 781  SER A 784  0                                        
SHEET    2   I 3 LYS A 829  PRO A 834 -1  O  VAL A 830   N  SER A 783           
SHEET    3   I 3 CYS A 845  PRO A 849 -1  O  TRP A 848   N  TYR A 831           
SHEET    1   J 2 ASP A 792  VAL A 793  0                                        
SHEET    2   J 2 PHE A 796  PRO A 797 -1  O  PHE A 796   N  VAL A 793           
LINK         O3'  DC T   3                 P   2PR T   4     1555   1555  1.60  
LINK         O3'  DG P 114                 P   2DA P 115     1555   1555  1.60  
LINK         OD1 ASP A 623                CA    CA A 904     1555   1555  2.24  
LINK         O2B TTP A 903                CA    CA A 904     1555   1555  2.25  
LINK         O   LYS A 531                CA    CA A 906     1555   1555  2.27  
LINK         O1G TTP A 903                CA    CA A 904     1555   1555  2.28  
LINK         OD2 ASP A 411                CA    CA A 904     1555   1555  2.31  
LINK         O   LEU A 412                CA    CA A 904     1555   1555  2.32  
LINK         OD1 ASN A 507                CA    CA A 906     1555   1555  2.36  
LINK         O   ASN A 505                CA    CA A 906     1555   1555  2.40  
LINK         O2A TTP A 903                CA    CA A 905     1555   1555  2.53  
LINK         OD1 ASP A 411                CA    CA A 904     1555   1555  2.60  
LINK         O2A TTP A 903                CA    CA A 904     1555   1555  2.73  
LINK         OE2 GLU A 116                CA    CA A 908     1555   1555  2.77  
LINK         OD2 ASP A 623                CA    CA A 905     1555   1555  2.85  
LINK         OE1 GLU A 116                CA    CA A 908     1555   1555  2.88  
LINK         OD2 ASP A 411                CA    CA A 905     1555   1555  2.89  
LINK        CA    CA A 907                 O   HOH A1076     1555   1555  2.31  
LINK        CA    CA A 908                 O   HOH A 961     1555   1555  2.64  
LINK         O3' 2PR T   4                 P    DT T   5     1555   1555  1.59  
SITE     1 AC1 17 ASP A 411  LEU A 412  SER A 414  LEU A 415                    
SITE     2 AC1 17 TYR A 416  ARG A 482  LYS A 560  ASN A 564                    
SITE     3 AC1 17 ASP A 623   CA A 904   CA A 905  HOH A 987                    
SITE     4 AC1 17 HOH A1065  HOH A1097  2DA P 115  2PR T   4                    
SITE     5 AC1 17  DT T   5                                                     
SITE     1 AC2  4 ASP A 411  LEU A 412  ASP A 623  TTP A 903                    
SITE     1 AC3  3 ASP A 411  ASP A 623  TTP A 903                               
SITE     1 AC4  3 ASN A 505  ASN A 507  LYS A 531                               
SITE     1 AC5  3 ASP A 411  GLU A 716  HOH A1076                               
SITE     1 AC6  2 GLU A 116  HOH A 961                                          
CRYST1   74.679  120.467  130.992  90.00  90.00  90.00 P 21 21 21    4          
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      0.013391  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008301  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007634        0.00000                         
ATOM      1  N   MET A   1      37.986 -17.990 -35.463  1.00 55.95           N  
ANISOU    1  N   MET A   1     7096   6676   7486    674    610    713       N  
ATOM      2  CA  MET A   1      36.652 -17.590 -35.999  1.00 55.67           C  
ANISOU    2  CA  MET A   1     7171   6652   7328    627    590    627       C  
ATOM      3  C   MET A   1      36.412 -16.086 -35.864  1.00 52.56           C  
ANISOU    3  C   MET A   1     6742   6309   6920    573    509    612       C  
ATOM      4  O   MET A   1      37.105 -15.397 -35.108  1.00 49.84           O  
ANISOU    4  O   MET A   1     6297   5995   6644    560    445    659       O  
ATOM      5  CB  MET A   1      35.527 -18.386 -35.318  1.00 57.44           C  
ANISOU    5  CB  MET A   1     7467   6881   7477    607    534    578       C  
ATOM      6  CG  MET A   1      35.441 -18.222 -33.794  1.00 63.51           C  
ANISOU    6  CG  MET A   1     8172   7690   8267    580    416    594       C  
ATOM      7  SD  MET A   1      33.927 -18.898 -33.051  1.00 68.14           S  
ANISOU    7  SD  MET A   1     8850   8284   8756    547    352    529       S  
ATOM      8  CE  MET A   1      32.677 -17.848 -33.789  1.00 67.24           C  
ANISOU    8  CE  MET A   1     8805   8193   8550    491    329    459       C  
ATOM      9  N   LYS A   2      35.435 -15.585 -36.618  1.00 51.21           N  
ANISOU    9  N   LYS A   2     6654   6142   6660    539    511    551       N  
ATOM     10  CA  LYS A   2      35.037 -14.187 -36.528  1.00 48.55           C  
ANISOU   10  CA  LYS A   2     6299   5849   6301    487    439    531       C  
ATOM     11  C   LYS A   2      34.271 -13.932 -35.235  1.00 44.71           C  
ANISOU   11  C   LYS A   2     5801   5400   5785    446    324    509       C  
ATOM     12  O   LYS A   2      33.320 -14.646 -34.910  1.00 43.67           O  
ANISOU   12  O   LYS A   2     5733   5263   5596    438    303    471       O  
ATOM     13  CB  LYS A   2      34.209 -13.759 -37.749  1.00 50.69           C  
ANISOU   13  CB  LYS A   2     6662   6109   6489    464    474    479       C  
ATOM     14  CG  LYS A   2      35.023 -13.116 -38.878  1.00 56.01           C  
ANISOU   14  CG  LYS A   2     7322   6765   7193    480    554    504       C  
ATOM     15  CD  LYS A   2      35.772 -11.872 -38.392  1.00 60.32           C  
ANISOU   15  CD  LYS A   2     7760   7349   7809    462    502    544       C  
ATOM     16  CE  LYS A   2      36.656 -11.257 -39.476  1.00 61.91           C  
ANISOU   16  CE  LYS A   2     7940   7531   8051    480    586    575       C  
ATOM     17  NZ  LYS A   2      35.929 -10.246 -40.301  1.00 62.51           N  
ANISOU   17  NZ  LYS A   2     8077   7618   8056    440    576    531       N  
ATOM     18  N   GLU A   3      34.713 -12.917 -34.501  1.00 40.52           N  
ANISOU   18  N   GLU A   3     5197   4904   5297    419    252    536       N  
ATOM     19  CA  GLU A   3      34.074 -12.509 -33.260  1.00 38.32           C  
ANISOU   19  CA  GLU A   3     4915   4654   4989    376    149    518       C  
ATOM     20  C   GLU A   3      32.646 -12.001 -33.478  1.00 35.26           C  
ANISOU   20  C   GLU A   3     4604   4278   4513    339    124    452       C  
ATOM     21  O   GLU A   3      32.346 -11.386 -34.501  1.00 34.04           O  
ANISOU   21  O   GLU A   3     4478   4123   4332    330    157    431       O  
ATOM     22  CB  GLU A   3      34.918 -11.442 -32.555  1.00 38.33           C  
ANISOU   22  CB  GLU A   3     4834   4681   5048    349     83    563       C  
ATOM     23  CG  GLU A   3      36.365 -11.862 -32.352  1.00 41.87           C  
ANISOU   23  CG  GLU A   3     5191   5119   5600    382     98    641       C  
ATOM     24  CD  GLU A   3      37.081 -11.088 -31.259  1.00 45.07           C  
ANISOU   24  CD  GLU A   3     5521   5546   6055    344      0    690       C  
ATOM     25  OE1 GLU A   3      38.099 -11.606 -30.746  1.00 49.35           O  
ANISOU   25  OE1 GLU A   3     5991   6081   6680    363    -16    759       O  
ATOM     26  OE2 GLU A   3      36.642  -9.971 -30.913  1.00 45.18           O  
ANISOU   26  OE2 GLU A   3     5553   5583   6030    293    -63    664       O  
ATOM     27  N   PHE A   4      31.771 -12.298 -32.519  1.00 31.20           N  
ANISOU   27  N   PHE A   4     4123   3773   3960    318     69    425       N  
ATOM     28  CA  PHE A   4      30.427 -11.730 -32.479  1.00 27.95           C  
ANISOU   28  CA  PHE A   4     3766   3373   3482    281     37    375       C  
ATOM     29  C   PHE A   4      29.980 -11.415 -31.061  1.00 25.97           C  
ANISOU   29  C   PHE A   4     3513   3136   3217    251    -38    368       C  
ATOM     30  O   PHE A   4      30.347 -12.103 -30.112  1.00 24.24           O  
ANISOU   30  O   PHE A   4     3281   2913   3015    260    -64    389       O  
ATOM     31  CB  PHE A   4      29.403 -12.626 -33.188  1.00 26.36           C  
ANISOU   31  CB  PHE A   4     3640   3151   3225    289     76    337       C  
ATOM     32  CG  PHE A   4      29.253 -13.996 -32.587  1.00 26.76           C  
ANISOU   32  CG  PHE A   4     3714   3183   3269    309     82    337       C  
ATOM     33  CD1 PHE A   4      30.158 -15.007 -32.888  1.00 25.19           C  
ANISOU   33  CD1 PHE A   4     3506   2960   3106    352    136    365       C  
ATOM     34  CD2 PHE A   4      28.178 -14.288 -31.752  1.00 23.29           C  
ANISOU   34  CD2 PHE A   4     3310   2748   2792    288     39    309       C  
ATOM     35  CE1 PHE A   4      30.009 -16.287 -32.343  1.00 25.44           C  
ANISOU   35  CE1 PHE A   4     3563   2972   3132    373    143    366       C  
ATOM     36  CE2 PHE A   4      28.023 -15.566 -31.204  1.00 23.59           C  
ANISOU   36  CE2 PHE A   4     3373   2768   2823    306     45    309       C  
ATOM     37  CZ  PHE A   4      28.940 -16.565 -31.506  1.00 24.52           C  
ANISOU   37  CZ  PHE A   4     3482   2863   2973    347     94    336       C  
ATOM     38  N   TYR A   5      29.184 -10.362 -30.932  1.00 25.68           N  
ANISOU   38  N   TYR A   5     3495   3112   3148    216    -69    341       N  
ATOM     39  CA  TYR A   5      28.619  -9.976 -29.648  1.00 24.86           C  
ANISOU   39  CA  TYR A   5     3409   3014   3022    187   -126    330       C  
ATOM     40  C   TYR A   5      27.548 -10.940 -29.166  1.00 22.48           C  
ANISOU   40  C   TYR A   5     3160   2701   2682    190   -123    302       C  
ATOM     41  O   TYR A   5      26.964 -11.686 -29.946  1.00 22.28           O  
ANISOU   41  O   TYR A   5     3163   2665   2638    205    -84    284       O  
ATOM     42  CB  TYR A   5      28.057  -8.549 -29.709  1.00 24.23           C  
ANISOU   42  CB  TYR A   5     3338   2943   2923    153   -145    311       C  
ATOM     43  CG  TYR A   5      26.802  -8.381 -30.547  1.00 24.70           C  
ANISOU   43  CG  TYR A   5     3436   3001   2949    149   -116    276       C  
ATOM     44  CD1 TYR A   5      26.883  -8.064 -31.900  1.00 23.32           C  
ANISOU   44  CD1 TYR A   5     3255   2828   2776    156    -81    275       C  
ATOM     45  CD2 TYR A   5      25.530  -8.514 -29.976  1.00 24.10           C  
ANISOU   45  CD2 TYR A   5     3400   2916   2840    137   -126    251       C  
ATOM     46  CE1 TYR A   5      25.730  -7.888 -32.667  1.00 26.74           C  
ANISOU   46  CE1 TYR A   5     3724   3258   3180    146    -68    251       C  
ATOM     47  CE2 TYR A   5      24.373  -8.337 -30.734  1.00 26.35           C  
ANISOU   47  CE2 TYR A   5     3708   3198   3105    130   -108    230       C  
ATOM     48  CZ  TYR A   5      24.484  -8.028 -32.081  1.00 25.86           C  
ANISOU   48  CZ  TYR A   5     3640   3139   3044    132    -85    231       C  
ATOM     49  OH  TYR A   5      23.356  -7.853 -32.844  1.00 26.77           O  
ANISOU   49  OH  TYR A   5     3780   3250   3141    119    -79    218       O  
ATOM     50  N   LEU A   6      27.305 -10.914 -27.863  1.00 24.00           N  
ANISOU   50  N   LEU A   6     3369   2890   2860    171   -166    301       N  
ATOM     51  CA  LEU A   6      26.213 -11.663 -27.262  1.00 23.07           C  
ANISOU   51  CA  LEU A   6     3301   2759   2706    170   -164    276       C  
ATOM     52  C   LEU A   6      25.183 -10.673 -26.753  1.00 22.07           C  
ANISOU   52  C   LEU A   6     3205   2629   2550    139   -177    251       C  
ATOM     53  O   LEU A   6      24.014 -10.758 -27.109  1.00 21.39           O  
ANISOU   53  O   LEU A   6     3143   2538   2446    137   -153    228       O  
ATOM     54  CB  LEU A   6      26.724 -12.543 -26.126  1.00 22.50           C  
ANISOU   54  CB  LEU A   6     3235   2677   2638    176   -192    296       C  
ATOM     55  CG  LEU A   6      27.642 -13.716 -26.485  1.00 25.35           C  
ANISOU   55  CG  LEU A   6     3567   3032   3032    213   -172    325       C  
ATOM     56  CD1 LEU A   6      28.306 -14.222 -25.229  1.00 24.77           C  
ANISOU   56  CD1 LEU A   6     3489   2952   2971    211   -219    356       C  
ATOM     57  CD2 LEU A   6      26.878 -14.849 -27.169  1.00 23.81           C  
ANISOU   57  CD2 LEU A   6     3408   2823   2816    236   -122    301       C  
ATOM     58  N   THR A   7      25.626  -9.732 -25.921  1.00 23.12           N  
ANISOU   58  N   THR A   7     3339   2763   2683    114   -214    261       N  
ATOM     59  CA  THR A   7      24.755  -8.692 -25.385  1.00 22.73           C  
ANISOU   59  CA  THR A   7     3325   2704   2608     87   -218    241       C  
ATOM     60  C   THR A   7      25.525  -7.391 -25.293  1.00 24.37           C  
ANISOU   60  C   THR A   7     3517   2917   2826     62   -247    254       C  
ATOM     61  O   THR A   7      26.757  -7.399 -25.199  1.00 27.52           O  
ANISOU   61  O   THR A   7     3882   3325   3249     59   -280    284       O  
ATOM     62  CB  THR A   7      24.241  -9.031 -23.965  1.00 23.43           C  
ANISOU   62  CB  THR A   7     3470   2768   2662     73   -231    232       C  
ATOM     63  OG1 THR A   7      25.336  -8.993 -23.044  1.00 26.05           O  
ANISOU   63  OG1 THR A   7     3808   3097   2993     55   -284    257       O  
ATOM     64  CG2 THR A   7      23.562 -10.413 -23.918  1.00 17.73           C  
ANISOU   64  CG2 THR A   7     2766   2039   1933     95   -207    223       C  
ATOM     65  N   VAL A   8      24.802  -6.276 -25.307  1.00 22.12           N  
ANISOU   65  N   VAL A   8     3254   2623   2526     45   -234    236       N  
ATOM     66  CA  VAL A   8      25.417  -4.965 -25.182  1.00 24.33           C  
ANISOU   66  CA  VAL A   8     3531   2904   2811     17   -260    245       C  
ATOM     67  C   VAL A   8      24.491  -4.058 -24.387  1.00 26.55           C  
ANISOU   67  C   VAL A   8     3874   3155   3058     -6   -248    224       C  
ATOM     68  O   VAL A   8      23.277  -4.110 -24.557  1.00 28.90           O  
ANISOU   68  O   VAL A   8     4188   3442   3350      7   -205    205       O  
ATOM     69  CB  VAL A   8      25.756  -4.345 -26.574  1.00 25.30           C  
ANISOU   69  CB  VAL A   8     3600   3048   2964     26   -242    252       C  
ATOM     70  CG1 VAL A   8      24.485  -3.958 -27.340  1.00 26.72           C  
ANISOU   70  CG1 VAL A   8     3789   3224   3138     35   -199    229       C  
ATOM     71  CG2 VAL A   8      26.672  -3.148 -26.425  1.00 23.46           C  
ANISOU   71  CG2 VAL A   8     3355   2817   2742     -4   -275    269       C  
ATOM     72  N   GLU A   9      25.072  -3.248 -23.507  1.00 27.22           N  
ANISOU   72  N   GLU A   9     3995   3223   3123    -42   -285    231       N  
ATOM     73  CA  GLU A   9      24.319  -2.297 -22.706  1.00 28.76           C  
ANISOU   73  CA  GLU A   9     4264   3381   3282    -66   -267    211       C  
ATOM     74  C   GLU A   9      25.104  -1.003 -22.527  1.00 28.21           C  
ANISOU   74  C   GLU A   9     4210   3302   3206   -105   -303    221       C  
ATOM     75  O   GLU A   9      26.333  -1.019 -22.454  1.00 29.81           O  
ANISOU   75  O   GLU A   9     4385   3520   3421   -126   -361    248       O  
ATOM     76  CB  GLU A   9      24.020  -2.876 -21.316  1.00 28.49           C  
ANISOU   76  CB  GLU A   9     4308   3314   3203    -80   -275    204       C  
ATOM     77  CG  GLU A   9      23.318  -4.230 -21.308  1.00 32.07           C  
ANISOU   77  CG  GLU A   9     4753   3772   3661    -46   -245    197       C  
ATOM     78  CD  GLU A   9      21.813  -4.158 -21.555  1.00 31.60           C  
ANISOU   78  CD  GLU A   9     4704   3696   3606    -24   -174    177       C  
ATOM     79  OE1 GLU A   9      21.278  -3.060 -21.834  1.00 29.90           O  
ANISOU   79  OE1 GLU A   9     4496   3467   3398    -27   -142    169       O  
ATOM     80  OE2 GLU A   9      21.162  -5.222 -21.463  1.00 33.13           O  
ANISOU   80  OE2 GLU A   9     4897   3889   3802     -3   -151    172       O  
ATOM     81  N   GLN A  10      24.389   0.111 -22.447  1.00 27.67           N  
ANISOU   81  N   GLN A  10     4184   3206   3121   -115   -266    203       N  
ATOM     82  CA  GLN A  10      24.980   1.359 -21.990  1.00 28.74           C  
ANISOU   82  CA  GLN A  10     4366   3318   3236   -159   -297    207       C  
ATOM     83  C   GLN A  10      24.687   1.537 -20.509  1.00 31.09           C  
ANISOU   83  C   GLN A  10     4780   3562   3471   -193   -300    194       C  
ATOM     84  O   GLN A  10      23.527   1.505 -20.095  1.00 33.21           O  
ANISOU   84  O   GLN A  10     5101   3797   3719   -175   -236    172       O  
ATOM     85  CB  GLN A  10      24.422   2.553 -22.769  1.00 28.31           C  
ANISOU   85  CB  GLN A  10     4301   3258   3199   -152   -251    197       C  
ATOM     86  CG  GLN A  10      25.122   3.862 -22.417  1.00 30.46           C  
ANISOU   86  CG  GLN A  10     4618   3507   3451   -200   -284    202       C  
ATOM     87  CD  GLN A  10      24.472   5.100 -23.017  1.00 35.37           C  
ANISOU   87  CD  GLN A  10     5244   4110   4083   -193   -232    190       C  
ATOM     88  OE1 GLN A  10      23.707   5.025 -23.986  1.00 33.54           O  
ANISOU   88  OE1 GLN A  10     4958   3898   3889   -152   -185    187       O  
ATOM     89  NE2 GLN A  10      24.788   6.258 -22.441  1.00 37.01           N  
ANISOU   89  NE2 GLN A  10     5523   4279   4259   -236   -246    187       N  
ATOM     90  N   ILE A  11      25.737   1.712 -19.712  1.00 33.76           N  
ANISOU   90  N   ILE A  11     5159   3888   3780   -243   -375    212       N  
ATOM     91  CA  ILE A  11      25.584   2.120 -18.318  1.00 35.34           C  
ANISOU   91  CA  ILE A  11     5491   4028   3907   -289   -385    200       C  
ATOM     92  C   ILE A  11      26.456   3.350 -18.044  1.00 35.99           C  
ANISOU   92  C   ILE A  11     5618   4088   3966   -351   -442    212       C  
ATOM     93  O   ILE A  11      27.686   3.258 -17.912  1.00 34.36           O  
ANISOU   93  O   ILE A  11     5383   3901   3770   -390   -534    246       O  
ATOM     94  CB  ILE A  11      25.866   0.963 -17.322  1.00 37.12           C  
ANISOU   94  CB  ILE A  11     5758   4246   4100   -303   -430    211       C  
ATOM     95  CG1 ILE A  11      24.869  -0.188 -17.544  1.00 39.93           C  
ANISOU   95  CG1 ILE A  11     6082   4615   4474   -244   -365    195       C  
ATOM     96  CG2 ILE A  11      25.781   1.461 -15.879  1.00 38.06           C  
ANISOU   96  CG2 ILE A  11     6031   4296   4132   -359   -446    199       C  
ATOM     97  CD1 ILE A  11      25.325  -1.545 -17.006  1.00 42.33           C  
ANISOU   97  CD1 ILE A  11     6379   4934   4772   -243   -413    214       C  
ATOM     98  N   GLY A  12      25.796   4.505 -17.972  1.00 37.26           N  
ANISOU   98  N   GLY A  12     5847   4206   4102   -359   -386    187       N  
ATOM     99  CA  GLY A  12      26.480   5.789 -17.841  1.00 37.63           C  
ANISOU   99  CA  GLY A  12     5942   4229   4128   -415   -427    194       C  
ATOM    100  C   GLY A  12      27.378   6.033 -19.038  1.00 36.89           C  
ANISOU  100  C   GLY A  12     5719   4193   4103   -410   -468    222       C  
ATOM    101  O   GLY A  12      26.909   6.084 -20.178  1.00 37.96           O  
ANISOU  101  O   GLY A  12     5770   4362   4292   -358   -413    216       O  
ATOM    102  N   ASP A  13      28.675   6.157 -18.774  1.00 35.93           N  
ANISOU  102  N   ASP A  13     5586   4082   3985   -465   -568    257       N  
ATOM    103  CA  ASP A  13      29.663   6.420 -19.815  1.00 34.95           C  
ANISOU  103  CA  ASP A  13     5343   4008   3930   -466   -608    291       C  
ATOM    104  C   ASP A  13      30.404   5.160 -20.236  1.00 34.28           C  
ANISOU  104  C   ASP A  13     5143   3977   3903   -438   -647    327       C  
ATOM    105  O   ASP A  13      31.426   5.223 -20.914  1.00 33.26           O  
ANISOU  105  O   ASP A  13     4918   3883   3834   -444   -689    367       O  
ATOM    106  CB  ASP A  13      30.643   7.503 -19.358  1.00 36.49           C  
ANISOU  106  CB  ASP A  13     5585   4175   4104   -546   -688    315       C  
ATOM    107  CG  ASP A  13      30.023   8.879 -19.363  1.00 37.09           C  
ANISOU  107  CG  ASP A  13     5747   4204   4141   -563   -635    282       C  
ATOM    108  OD1 ASP A  13      30.403   9.719 -18.518  1.00 43.42           O  
ANISOU  108  OD1 ASP A  13     6655   4954   4886   -636   -685    284       O  
ATOM    109  OD2 ASP A  13      29.146   9.119 -20.215  1.00 39.59           O  
ANISOU  109  OD2 ASP A  13     6026   4531   4483   -506   -546    257       O  
ATOM    110  N   SER A  14      29.865   4.010 -19.851  1.00 35.05           N  
ANISOU  110  N   SER A  14     5253   4078   3988   -404   -626    316       N  
ATOM    111  CA  SER A  14      30.460   2.739 -20.216  1.00 34.15           C  
ANISOU  111  CA  SER A  14     5041   4008   3927   -372   -651    348       C  
ATOM    112  C   SER A  14      29.524   1.915 -21.086  1.00 33.18           C  
ANISOU  112  C   SER A  14     4866   3912   3830   -297   -565    322       C  
ATOM    113  O   SER A  14      28.305   1.905 -20.882  1.00 30.71           O  
ANISOU  113  O   SER A  14     4613   3577   3480   -275   -501    282       O  
ATOM    114  CB  SER A  14      30.857   1.957 -18.959  1.00 37.00           C  
ANISOU  114  CB  SER A  14     5458   4349   4252   -406   -721    369       C  
ATOM    115  OG  SER A  14      32.093   2.429 -18.428  1.00 39.79           O  
ANISOU  115  OG  SER A  14     5814   4694   4611   -475   -826    417       O  
ATOM    116  N   ILE A  15      30.107   1.258 -22.083  1.00 31.68           N  
ANISOU  116  N   ILE A  15     4566   3767   3704   -259   -561    347       N  
ATOM    117  CA  ILE A  15      29.452   0.160 -22.766  1.00 29.70           C  
ANISOU  117  CA  ILE A  15     4272   3539   3474   -197   -501    332       C  
ATOM    118  C   ILE A  15      29.868  -1.119 -22.052  1.00 30.30           C  
ANISOU  118  C   ILE A  15     4345   3618   3551   -192   -540    354       C  
ATOM    119  O   ILE A  15      31.054  -1.344 -21.810  1.00 31.45           O  
ANISOU  119  O   ILE A  15     4447   3772   3729   -214   -605    401       O  
ATOM    120  CB  ILE A  15      29.845   0.096 -24.270  1.00 29.59           C  
ANISOU  120  CB  ILE A  15     4158   3563   3521   -159   -467    346       C  
ATOM    121  CG1 ILE A  15      29.225   1.263 -25.061  1.00 28.17           C  
ANISOU  121  CG1 ILE A  15     3986   3381   3338   -158   -421    321       C  
ATOM    122  CG2 ILE A  15      29.447  -1.248 -24.890  1.00 29.30           C  
ANISOU  122  CG2 ILE A  15     4084   3547   3504   -104   -421    339       C  
ATOM    123  CD1 ILE A  15      27.695   1.398 -24.926  1.00 27.35           C  
ANISOU  123  CD1 ILE A  15     3944   3255   3194   -140   -364    277       C  
ATOM    124  N   PHE A  16      28.894  -1.944 -21.690  1.00 29.40           N  
ANISOU  124  N   PHE A  16     4273   3492   3405   -166   -501    326       N  
ATOM    125  CA  PHE A  16      29.194  -3.272 -21.173  1.00 27.47           C  
ANISOU  125  CA  PHE A  16     4020   3252   3165   -152   -526    345       C  
ATOM    126  C   PHE A  16      28.833  -4.273 -22.253  1.00 27.77           C  
ANISOU  126  C   PHE A  16     3993   3318   3241    -91   -466    337       C  
ATOM    127  O   PHE A  16      27.681  -4.334 -22.698  1.00 26.87           O  
ANISOU  127  O   PHE A  16     3899   3201   3110    -66   -404    300       O  
ATOM    128  CB  PHE A  16      28.422  -3.556 -19.881  1.00 28.00           C  
ANISOU  128  CB  PHE A  16     4192   3280   3165   -171   -529    322       C  
ATOM    129  CG  PHE A  16      28.984  -2.858 -18.669  1.00 32.56           C  
ANISOU  129  CG  PHE A  16     4848   3824   3697   -238   -603    337       C  
ATOM    130  CD1 PHE A  16      29.835  -3.531 -17.797  1.00 34.37           C  
ANISOU  130  CD1 PHE A  16     5089   4048   3922   -266   -683    377       C  
ATOM    131  CD2 PHE A  16      28.669  -1.528 -18.402  1.00 32.45           C  
ANISOU  131  CD2 PHE A  16     4905   3781   3645   -275   -596    316       C  
ATOM    132  CE1 PHE A  16      30.364  -2.889 -16.675  1.00 34.83           C  
ANISOU  132  CE1 PHE A  16     5232   4071   3932   -337   -763    395       C  
ATOM    133  CE2 PHE A  16      29.191  -0.878 -17.284  1.00 35.75           C  
ANISOU  133  CE2 PHE A  16     5412   4160   4011   -344   -666    329       C  
ATOM    134  CZ  PHE A  16      30.042  -1.562 -16.418  1.00 36.42           C  
ANISOU  134  CZ  PHE A  16     5513   4240   4086   -379   -754    369       C  
ATOM    135  N   GLU A  17      29.823  -5.050 -22.681  1.00 27.29           N  
ANISOU  135  N   GLU A  17     3859   3279   3233    -70   -484    376       N  
ATOM    136  CA  GLU A  17      29.621  -5.993 -23.762  1.00 26.67           C  
ANISOU  136  CA  GLU A  17     3729   3220   3186    -16   -426    371       C  
ATOM    137  C   GLU A  17      30.024  -7.406 -23.358  1.00 27.70           C  
ANISOU  137  C   GLU A  17     3844   3349   3332      8   -438    395       C  
ATOM    138  O   GLU A  17      31.117  -7.625 -22.839  1.00 30.13           O  
ANISOU  138  O   GLU A  17     4118   3657   3672     -5   -495    443       O  
ATOM    139  CB  GLU A  17      30.401  -5.566 -25.012  1.00 26.20           C  
ANISOU  139  CB  GLU A  17     3591   3182   3181      0   -405    393       C  
ATOM    140  CG  GLU A  17      30.017  -6.372 -26.254  1.00 26.57           C  
ANISOU  140  CG  GLU A  17     3611   3240   3244     51   -333    379       C  
ATOM    141  CD  GLU A  17      31.048  -6.341 -27.365  1.00 27.31           C  
ANISOU  141  CD  GLU A  17     3631   3348   3397     73   -307    412       C  
ATOM    142  OE1 GLU A  17      30.781  -6.959 -28.415  1.00 27.13           O  
ANISOU  142  OE1 GLU A  17     3600   3327   3379    110   -246    400       O  
ATOM    143  OE2 GLU A  17      32.120  -5.727 -27.197  1.00 26.94           O  
ANISOU  143  OE2 GLU A  17     3538   3307   3392     52   -346    453       O  
ATOM    144  N   ARG A  18      29.126  -8.357 -23.592  1.00 26.05           N  
ANISOU  144  N   ARG A  18     3657   3136   3104     42   -389    366       N  
ATOM    145  CA  ARG A  18      29.478  -9.768 -23.560  1.00 22.89           C  
ANISOU  145  CA  ARG A  18     3236   2736   2726     75   -382    387       C  
ATOM    146  C   ARG A  18      29.597 -10.198 -25.014  1.00 24.26           C  
ANISOU  146  C   ARG A  18     3359   2922   2936    119   -318    386       C  
ATOM    147  O   ARG A  18      28.793  -9.786 -25.854  1.00 22.34           O  
ANISOU  147  O   ARG A  18     3131   2684   2675    123   -275    352       O  
ATOM    148  CB  ARG A  18      28.419 -10.592 -22.820  1.00 22.29           C  
ANISOU  148  CB  ARG A  18     3226   2641   2601     79   -369    357       C  
ATOM    149  CG  ARG A  18      28.228 -10.174 -21.346  1.00 23.00           C  
ANISOU  149  CG  ARG A  18     3386   2710   2644     35   -422    354       C  
ATOM    150  CD  ARG A  18      26.976 -10.810 -20.736  1.00 24.76           C  
ANISOU  150  CD  ARG A  18     3679   2911   2817     40   -390    318       C  
ATOM    151  NE  ARG A  18      27.099 -12.267 -20.602  1.00 23.30           N  
ANISOU  151  NE  ARG A  18     3486   2723   2642     70   -385    331       N  
ATOM    152  CZ  ARG A  18      26.073 -13.103 -20.465  1.00 22.25           C  
ANISOU  152  CZ  ARG A  18     3393   2578   2484     87   -344    304       C  
ATOM    153  NH1 ARG A  18      24.828 -12.636 -20.443  1.00 20.80           N  
ANISOU  153  NH1 ARG A  18     3251   2383   2268     78   -305    266       N  
ATOM    154  NH2 ARG A  18      26.287 -14.413 -20.351  1.00 20.18           N  
ANISOU  154  NH2 ARG A  18     3124   2311   2232    113   -342    318       N  
ATOM    155  N   TYR A  19      30.616 -10.999 -25.317  1.00 25.20           N  
ANISOU  155  N   TYR A  19     3424   3043   3107    149   -311    428       N  
ATOM    156  CA  TYR A  19      30.899 -11.386 -26.695  1.00 24.94           C  
ANISOU  156  CA  TYR A  19     3353   3013   3108    189   -243    432       C  
ATOM    157  C   TYR A  19      31.652 -12.704 -26.745  1.00 27.10           C  
ANISOU  157  C   TYR A  19     3596   3276   3426    231   -221    469       C  
ATOM    158  O   TYR A  19      32.174 -13.181 -25.729  1.00 27.33           O  
ANISOU  158  O   TYR A  19     3612   3299   3473    227   -270    504       O  
ATOM    159  CB  TYR A  19      31.697 -10.290 -27.410  1.00 26.81           C  
ANISOU  159  CB  TYR A  19     3537   3264   3386    180   -241    455       C  
ATOM    160  CG  TYR A  19      33.113 -10.105 -26.902  1.00 27.78           C  
ANISOU  160  CG  TYR A  19     3590   3391   3575    172   -290    521       C  
ATOM    161  CD1 TYR A  19      33.367  -9.459 -25.690  1.00 29.21           C  
ANISOU  161  CD1 TYR A  19     3779   3573   3747    123   -377    539       C  
ATOM    162  CD2 TYR A  19      34.204 -10.583 -27.635  1.00 30.41           C  
ANISOU  162  CD2 TYR A  19     3850   3720   3983    210   -249    570       C  
ATOM    163  CE1 TYR A  19      34.680  -9.290 -25.221  1.00 30.66           C  
ANISOU  163  CE1 TYR A  19     3896   3759   3996    106   -436    608       C  
ATOM    164  CE2 TYR A  19      35.518 -10.417 -27.177  1.00 27.22           C  
ANISOU  164  CE2 TYR A  19     3368   3319   3655    202   -297    643       C  
ATOM    165  CZ  TYR A  19      35.745  -9.769 -25.976  1.00 28.41           C  
ANISOU  165  CZ  TYR A  19     3523   3474   3797    147   -397    663       C  
ATOM    166  OH  TYR A  19      37.034  -9.614 -25.528  1.00 31.58           O  
ANISOU  166  OH  TYR A  19     3846   3878   4277    131   -457    741       O  
ATOM    167  N   ILE A  20      31.681 -13.290 -27.935  1.00 26.58           N  
ANISOU  167  N   ILE A  20     3524   3201   3373    271   -145    463       N  
ATOM    168  CA  ILE A  20      32.455 -14.480 -28.203  1.00 27.98           C  
ANISOU  168  CA  ILE A  20     3672   3360   3598    318   -103    500       C  
ATOM    169  C   ILE A  20      33.706 -14.054 -28.965  1.00 30.53           C  
ANISOU  169  C   ILE A  20     3919   3684   3996    339    -70    550       C  
ATOM    170  O   ILE A  20      33.617 -13.446 -30.040  1.00 28.70           O  
ANISOU  170  O   ILE A  20     3692   3455   3759    341    -23    532       O  
ATOM    171  CB  ILE A  20      31.634 -15.520 -29.026  1.00 27.47           C  
ANISOU  171  CB  ILE A  20     3670   3274   3492    347    -30    459       C  
ATOM    172  CG1 ILE A  20      30.409 -16.000 -28.233  1.00 23.91           C  
ANISOU  172  CG1 ILE A  20     3286   2821   2978    327    -61    417       C  
ATOM    173  CG2 ILE A  20      32.522 -16.686 -29.472  1.00 26.06           C  
ANISOU  173  CG2 ILE A  20     3468   3068   3367    402     33    499       C  
ATOM    174  CD1 ILE A  20      30.723 -16.785 -26.952  1.00 27.03           C  
ANISOU  174  CD1 ILE A  20     3676   3209   3387    331   -106    445       C  
ATOM    175  N   ASP A  21      34.869 -14.367 -28.398  1.00 31.88           N  
ANISOU  175  N   ASP A  21     4019   3851   4242    353    -97    617       N  
ATOM    176  CA  ASP A  21      36.132 -13.945 -28.985  1.00 33.42           C  
ANISOU  176  CA  ASP A  21     4127   4046   4525    371    -71    678       C  
ATOM    177  C   ASP A  21      36.553 -14.845 -30.149  1.00 35.50           C  
ANISOU  177  C   ASP A  21     4383   4279   4827    434     45    692       C  
ATOM    178  O   ASP A  21      35.887 -15.843 -30.455  1.00 33.12           O  
ANISOU  178  O   ASP A  21     4149   3956   4481    461     97    655       O  
ATOM    179  CB  ASP A  21      37.231 -13.840 -27.915  1.00 33.30           C  
ANISOU  179  CB  ASP A  21     4030   4036   4586    355   -154    756       C  
ATOM    180  CG  ASP A  21      37.665 -15.197 -27.353  1.00 33.85           C  
ANISOU  180  CG  ASP A  21     4079   4084   4698    393   -152    800       C  
ATOM    181  OD1 ASP A  21      37.307 -16.264 -27.906  1.00 32.64           O  
ANISOU  181  OD1 ASP A  21     3966   3908   4530    441    -70    777       O  
ATOM    182  OD2 ASP A  21      38.387 -15.185 -26.336  1.00 33.16           O  
ANISOU  182  OD2 ASP A  21     3939   4001   4660    372   -237    862       O  
ATOM    183  N   SER A  22      37.670 -14.485 -30.778  1.00 37.72           N  
ANISOU  183  N   SER A  22     4586   4554   5192    457     88    748       N  
ATOM    184  CA  SER A  22      38.202 -15.204 -31.935  1.00 40.63           C  
ANISOU  184  CA  SER A  22     4949   4886   5604    519    213    768       C  
ATOM    185  C   SER A  22      38.489 -16.688 -31.669  1.00 42.42           C  
ANISOU  185  C   SER A  22     5175   5078   5863    571    256    798       C  
ATOM    186  O   SER A  22      38.665 -17.461 -32.607  1.00 43.49           O  
ANISOU  186  O   SER A  22     5341   5174   6011    623    370    799       O  
ATOM    187  CB  SER A  22      39.462 -14.506 -32.443  1.00 41.30           C  
ANISOU  187  CB  SER A  22     4933   4970   5789    532    246    838       C  
ATOM    188  OG  SER A  22      40.429 -14.405 -31.411  1.00 46.42           O  
ANISOU  188  OG  SER A  22     5478   5631   6530    521    165    918       O  
ATOM    189  N   ASN A  23      38.518 -17.082 -30.398  1.00 43.71           N  
ANISOU  189  N   ASN A  23     5316   5253   6039    556    168    822       N  
ATOM    190  CA  ASN A  23      38.765 -18.477 -30.026  1.00 45.08           C  
ANISOU  190  CA  ASN A  23     5489   5394   6245    603    198    853       C  
ATOM    191  C   ASN A  23      37.506 -19.248 -29.654  1.00 44.53           C  
ANISOU  191  C   ASN A  23     5527   5320   6073    592    184    782       C  
ATOM    192  O   ASN A  23      37.564 -20.448 -29.366  1.00 46.06           O  
ANISOU  192  O   ASN A  23     5736   5485   6279    629    211    798       O  
ATOM    193  CB  ASN A  23      39.788 -18.549 -28.892  1.00 46.56           C  
ANISOU  193  CB  ASN A  23     5572   5589   6527    599    112    944       C  
ATOM    194  CG  ASN A  23      41.163 -18.101 -29.332  1.00 48.28           C  
ANISOU  194  CG  ASN A  23     5670   5802   6873    623    144   1033       C  
ATOM    195  OD1 ASN A  23      41.716 -18.634 -30.290  1.00 48.52           O  
ANISOU  195  OD1 ASN A  23     5679   5795   6962    686    266   1061       O  
ATOM    196  ND2 ASN A  23      41.716 -17.109 -28.644  1.00 49.42           N  
ANISOU  196  ND2 ASN A  23     5739   5976   7060    572     38   1079       N  
ATOM    197  N   GLY A  24      36.369 -18.558 -29.666  1.00 42.00           N  
ANISOU  197  N   GLY A  24     5277   5024   5656    543    144    708       N  
ATOM    198  CA  GLY A  24      35.099 -19.178 -29.324  1.00 39.12           C  
ANISOU  198  CA  GLY A  24     5008   4656   5199    527    129    643       C  
ATOM    199  C   GLY A  24      34.800 -19.124 -27.839  1.00 37.79           C  
ANISOU  199  C   GLY A  24     4839   4509   5011    488     21    647       C  
ATOM    200  O   GLY A  24      33.897 -19.808 -27.354  1.00 36.29           O  
ANISOU  200  O   GLY A  24     4716   4311   4761    481      8    608       O  
ATOM    201  N   ARG A  25      35.565 -18.310 -27.119  1.00 36.43           N  
ANISOU  201  N   ARG A  25     4596   4359   4888    461    -56    696       N  
ATOM    202  CA  ARG A  25      35.356 -18.113 -25.690  1.00 35.94           C  
ANISOU  202  CA  ARG A  25     4544   4311   4800    415   -164    703       C  
ATOM    203  C   ARG A  25      34.446 -16.919 -25.432  1.00 32.45           C  
ANISOU  203  C   ARG A  25     4153   3894   4282    357   -213    646       C  
ATOM    204  O   ARG A  25      34.556 -15.895 -26.104  1.00 31.11           O  
ANISOU  204  O   ARG A  25     3962   3739   4118    342   -201    637       O  
ATOM    205  CB  ARG A  25      36.696 -17.879 -24.982  1.00 37.48           C  
ANISOU  205  CB  ARG A  25     4644   4511   5086    408   -234    793       C  
ATOM    206  CG  ARG A  25      37.422 -19.140 -24.519  1.00 40.94           C  
ANISOU  206  CG  ARG A  25     5042   4923   5590    450   -232    858       C  
ATOM    207  CD  ARG A  25      38.326 -19.728 -25.594  1.00 40.81           C  
ANISOU  207  CD  ARG A  25     4957   4881   5667    520   -127    907       C  
ATOM    208  NE  ARG A  25      39.253 -20.710 -25.031  1.00 40.02           N  
ANISOU  208  NE  ARG A  25     4792   4758   5656    558   -140    992       N  
ATOM    209  CZ  ARG A  25      40.496 -20.444 -24.630  1.00 36.67           C  
ANISOU  209  CZ  ARG A  25     4256   4337   5342    556   -194   1091       C  
ATOM    210  NH1 ARG A  25      40.996 -19.216 -24.728  1.00 34.80           N  
ANISOU  210  NH1 ARG A  25     3962   4125   5137    516   -241   1115       N  
ATOM    211  NH2 ARG A  25      41.242 -21.416 -24.124  1.00 34.46           N  
ANISOU  211  NH2 ARG A  25     3918   4032   5143    593   -205   1170       N  
ATOM    212  N   GLU A  26      33.556 -17.059 -24.454  1.00 31.31           N  
ANISOU  212  N   GLU A  26     4076   3750   4069    325   -263    610       N  
ATOM    213  CA  GLU A  26      32.764 -15.936 -23.959  1.00 31.00           C  
ANISOU  213  CA  GLU A  26     4085   3727   3966    270   -312    567       C  
ATOM    214  C   GLU A  26      33.613 -15.017 -23.075  1.00 31.67           C  
ANISOU  214  C   GLU A  26     4133   3822   4078    224   -405    614       C  
ATOM    215  O   GLU A  26      34.304 -15.488 -22.167  1.00 30.50           O  
ANISOU  215  O   GLU A  26     3964   3665   3959    217   -465    667       O  
ATOM    216  CB  GLU A  26      31.530 -16.426 -23.186  1.00 30.94           C  
ANISOU  216  CB  GLU A  26     4166   3710   3882    254   -322    517       C  
ATOM    217  CG  GLU A  26      30.651 -15.282 -22.642  1.00 30.06           C  
ANISOU  217  CG  GLU A  26     4109   3605   3706    202   -357    475       C  
ATOM    218  CD  GLU A  26      29.374 -15.751 -21.952  1.00 32.89           C  
ANISOU  218  CD  GLU A  26     4550   3949   3996    191   -350    429       C  
ATOM    219  OE1 GLU A  26      28.941 -16.907 -22.178  1.00 30.93           O  
ANISOU  219  OE1 GLU A  26     4321   3690   3742    222   -309    416       O  
ATOM    220  OE2 GLU A  26      28.796 -14.945 -21.185  1.00 31.39           O  
ANISOU  220  OE2 GLU A  26     4410   3756   3760    150   -382    406       O  
ATOM    221  N   ARG A  27      33.552 -13.713 -23.355  1.00 31.41           N  
ANISOU  221  N   ARG A  27     4097   3805   4034    191   -419    598       N  
ATOM    222  CA  ARG A  27      34.249 -12.700 -22.563  1.00 32.86           C  
ANISOU  222  CA  ARG A  27     4261   3994   4230    137   -509    636       C  
ATOM    223  C   ARG A  27      33.316 -11.545 -22.223  1.00 31.90           C  
ANISOU  223  C   ARG A  27     4214   3875   4031     88   -528    580       C  
ATOM    224  O   ARG A  27      32.229 -11.426 -22.784  1.00 32.26           O  
ANISOU  224  O   ARG A  27     4303   3922   4032    101   -468    520       O  
ATOM    225  CB  ARG A  27      35.456 -12.138 -23.327  1.00 37.12           C  
ANISOU  225  CB  ARG A  27     4701   4546   4857    145   -505    692       C  
ATOM    226  CG  ARG A  27      36.387 -13.159 -23.963  1.00 44.48           C  
ANISOU  226  CG  ARG A  27     5549   5470   5879    205   -455    749       C  
ATOM    227  CD  ARG A  27      37.468 -13.614 -23.015  1.00 53.78           C  
ANISOU  227  CD  ARG A  27     6670   6641   7123    194   -535    833       C  
ATOM    228  NE  ARG A  27      38.742 -13.737 -23.720  1.00 64.74           N  
ANISOU  228  NE  ARG A  27     7942   8028   8629    231   -504    911       N  
ATOM    229  CZ  ARG A  27      39.673 -12.786 -23.764  1.00 68.62           C  
ANISOU  229  CZ  ARG A  27     8359   8530   9184    199   -553    966       C  
ATOM    230  NH1 ARG A  27      39.490 -11.632 -23.126  1.00 66.42           N  
ANISOU  230  NH1 ARG A  27     8117   8262   8855    126   -639    950       N  
ATOM    231  NH2 ARG A  27      40.798 -12.994 -24.439  1.00 70.67           N  
ANISOU  231  NH2 ARG A  27     8507   8785   9560    239   -510   1041       N  
ATOM    232  N   THR A  28      33.761 -10.686 -21.313  1.00 31.96           N  
ANISOU  232  N   THR A  28     4236   3878   4028     30   -614    604       N  
ATOM    233  CA  THR A  28      33.050  -9.465 -20.981  1.00 34.75           C  
ANISOU  233  CA  THR A  28     4660   4226   4316    -17   -630    559       C  
ATOM    234  C   THR A  28      34.059  -8.331 -20.964  1.00 35.58           C  
ANISOU  234  C   THR A  28     4721   4338   4458    -62   -691    602       C  
ATOM    235  O   THR A  28      35.205  -8.518 -20.557  1.00 37.37           O  
ANISOU  235  O   THR A  28     4893   4566   4741    -79   -760    671       O  
ATOM    236  CB  THR A  28      32.365  -9.553 -19.597  1.00 36.76           C  
ANISOU  236  CB  THR A  28     5022   4455   4492    -57   -674    536       C  
ATOM    237  OG1 THR A  28      31.774 -10.847 -19.432  1.00 42.00           O  
ANISOU  237  OG1 THR A  28     5708   5110   5138    -18   -637    519       O  
ATOM    238  CG2 THR A  28      31.282  -8.478 -19.446  1.00 34.11           C  
ANISOU  238  CG2 THR A  28     4769   4106   4085    -86   -648    475       C  
ATOM    239  N   ARG A  29      33.637  -7.159 -21.421  1.00 33.92           N  
ANISOU  239  N   ARG A  29     4532   4133   4224    -81   -669    566       N  
ATOM    240  CA  ARG A  29      34.485  -5.980 -21.361  1.00 35.10           C  
ANISOU  240  CA  ARG A  29     4653   4284   4398   -130   -727    601       C  
ATOM    241  C   ARG A  29      33.669  -4.720 -21.107  1.00 36.40           C  
ANISOU  241  C   ARG A  29     4904   4434   4491   -173   -725    549       C  
ATOM    242  O   ARG A  29      32.480  -4.648 -21.432  1.00 36.02           O  
ANISOU  242  O   ARG A  29     4906   4382   4397   -149   -655    489       O  
ATOM    243  CB  ARG A  29      35.345  -5.838 -22.628  1.00 34.78           C  
ANISOU  243  CB  ARG A  29     4500   4268   4446    -97   -689    638       C  
ATOM    244  CG  ARG A  29      34.564  -5.737 -23.935  1.00 32.51           C  
ANISOU  244  CG  ARG A  29     4208   3993   4151    -50   -585    586       C  
ATOM    245  CD  ARG A  29      35.505  -5.761 -25.118  1.00 31.11           C  
ANISOU  245  CD  ARG A  29     3929   3832   4058    -15   -542    627       C  
ATOM    246  NE  ARG A  29      34.790  -5.949 -26.372  1.00 29.68           N  
ANISOU  246  NE  ARG A  29     3755   3658   3865     32   -443    582       N  
ATOM    247  CZ  ARG A  29      35.333  -6.457 -27.475  1.00 32.02           C  
ANISOU  247  CZ  ARG A  29     3990   3959   4218     80   -376    605       C  
ATOM    248  NH1 ARG A  29      36.605  -6.837 -27.486  1.00 34.13           N  
ANISOU  248  NH1 ARG A  29     4171   4225   4570     94   -387    677       N  
ATOM    249  NH2 ARG A  29      34.599  -6.599 -28.567  1.00 29.94           N  
ANISOU  249  NH2 ARG A  29     3753   3697   3928    113   -295    561       N  
ATOM    250  N   GLU A  30      34.324  -3.742 -20.501  1.00 38.54           N  
ANISOU  250  N   GLU A  30     5194   4693   4757   -237   -804    577       N  
ATOM    251  CA  GLU A  30      33.735  -2.448 -20.244  1.00 39.48           C  
ANISOU  251  CA  GLU A  30     5395   4791   4813   -281   -804    536       C  
ATOM    252  C   GLU A  30      34.545  -1.464 -21.064  1.00 39.95           C  
ANISOU  252  C   GLU A  30     5382   4869   4930   -297   -814    565       C  
ATOM    253  O   GLU A  30      35.758  -1.340 -20.877  1.00 41.50           O  
ANISOU  253  O   GLU A  30     5518   5069   5180   -330   -889    630       O  
ATOM    254  CB  GLU A  30      33.817  -2.118 -18.754  1.00 40.78           C  
ANISOU  254  CB  GLU A  30     5667   4917   4910   -353   -891    543       C  
ATOM    255  CG  GLU A  30      33.107  -0.836 -18.355  1.00 44.18           C  
ANISOU  255  CG  GLU A  30     6208   5312   5265   -398   -879    496       C  
ATOM    256  CD  GLU A  30      33.412  -0.385 -16.931  1.00 46.07           C  
ANISOU  256  CD  GLU A  30     6563   5506   5436   -481   -973    510       C  
ATOM    257  OE1 GLU A  30      33.878  -1.208 -16.108  1.00 47.90           O  
ANISOU  257  OE1 GLU A  30     6808   5729   5661   -502  -1042    547       O  
ATOM    258  OE2 GLU A  30      33.174   0.808 -16.637  1.00 46.19           O  
ANISOU  258  OE2 GLU A  30     6662   5488   5399   -529   -977    486       O  
ATOM    259  N   VAL A  31      33.881  -0.793 -21.998  1.00 38.22           N  
ANISOU  259  N   VAL A  31     5161   4657   4703   -272   -739    522       N  
ATOM    260  CA  VAL A  31      34.561   0.149 -22.876  1.00 37.72           C  
ANISOU  260  CA  VAL A  31     5031   4609   4690   -282   -736    544       C  
ATOM    261  C   VAL A  31      34.028   1.554 -22.645  1.00 35.98           C  
ANISOU  261  C   VAL A  31     4893   4365   4414   -327   -738    507       C  
ATOM    262  O   VAL A  31      32.817   1.764 -22.598  1.00 33.72           O  
ANISOU  262  O   VAL A  31     4680   4062   4069   -312   -682    451       O  
ATOM    263  CB  VAL A  31      34.408  -0.237 -24.361  1.00 38.34           C  
ANISOU  263  CB  VAL A  31     5032   4717   4818   -214   -645    535       C  
ATOM    264  CG1 VAL A  31      35.389   0.538 -25.210  1.00 41.37           C  
ANISOU  264  CG1 VAL A  31     5335   5117   5268   -223   -647    574       C  
ATOM    265  CG2 VAL A  31      34.633  -1.734 -24.557  1.00 41.16           C  
ANISOU  265  CG2 VAL A  31     5337   5088   5213   -161   -621    556       C  
ATOM    266  N   GLU A  32      34.941   2.508 -22.483  1.00 36.75           N  
ANISOU  266  N   GLU A  32     4976   4455   4531   -384   -803    545       N  
ATOM    267  CA  GLU A  32      34.570   3.914 -22.351  1.00 38.40           C  
ANISOU  267  CA  GLU A  32     5259   4637   4692   -429   -804    514       C  
ATOM    268  C   GLU A  32      34.380   4.511 -23.747  1.00 37.17           C  
ANISOU  268  C   GLU A  32     5044   4506   4575   -390   -728    499       C  
ATOM    269  O   GLU A  32      35.189   5.314 -24.216  1.00 37.02           O  
ANISOU  269  O   GLU A  32     4975   4494   4598   -417   -752    531       O  
ATOM    270  CB  GLU A  32      35.630   4.683 -21.561  1.00 40.95           C  
ANISOU  270  CB  GLU A  32     5602   4939   5016   -515   -913    562       C  
ATOM    271  CG  GLU A  32      35.763   4.248 -20.108  1.00 48.10           C  
ANISOU  271  CG  GLU A  32     6595   5813   5868   -567   -998    576       C  
ATOM    272  CD  GLU A  32      36.906   4.948 -19.393  1.00 54.25           C  
ANISOU  272  CD  GLU A  32     7387   6571   6653   -661  -1121    634       C  
ATOM    273  OE1 GLU A  32      36.960   6.198 -19.428  1.00 56.12           O  
ANISOU  273  OE1 GLU A  32     7672   6786   6865   -709  -1134    623       O  
ATOM    274  OE2 GLU A  32      37.750   4.244 -18.795  1.00 56.21           O  
ANISOU  274  OE2 GLU A  32     7599   6824   6934   -688  -1210    694       O  
ATOM    275  N   TYR A  33      33.294   4.100 -24.400  1.00 34.72           N  
ANISOU  275  N   TYR A  33     4739   4204   4249   -330   -641    453       N  
ATOM    276  CA  TYR A  33      33.047   4.413 -25.803  1.00 32.70           C  
ANISOU  276  CA  TYR A  33     4427   3972   4026   -287   -569    441       C  
ATOM    277  C   TYR A  33      32.964   5.918 -26.048  1.00 31.87           C  
ANISOU  277  C   TYR A  33     4353   3850   3906   -322   -566    429       C  
ATOM    278  O   TYR A  33      32.303   6.638 -25.305  1.00 32.72           O  
ANISOU  278  O   TYR A  33     4555   3923   3955   -352   -571    398       O  
ATOM    279  CB  TYR A  33      31.765   3.710 -26.263  1.00 29.76           C  
ANISOU  279  CB  TYR A  33     4076   3604   3628   -229   -492    395       C  
ATOM    280  CG  TYR A  33      31.418   3.873 -27.724  1.00 27.60           C  
ANISOU  280  CG  TYR A  33     3755   3352   3381   -187   -423    383       C  
ATOM    281  CD1 TYR A  33      32.304   3.476 -28.732  1.00 29.96           C  
ANISOU  281  CD1 TYR A  33     3968   3678   3738   -162   -406    417       C  
ATOM    282  CD2 TYR A  33      30.190   4.396 -28.104  1.00 25.69           C  
ANISOU  282  CD2 TYR A  33     3557   3099   3105   -171   -373    342       C  
ATOM    283  CE1 TYR A  33      31.971   3.618 -30.083  1.00 26.02           C  
ANISOU  283  CE1 TYR A  33     3443   3192   3252   -128   -343    405       C  
ATOM    284  CE2 TYR A  33      29.849   4.536 -29.452  1.00 26.36           C  
ANISOU  284  CE2 TYR A  33     3606   3200   3209   -139   -319    335       C  
ATOM    285  CZ  TYR A  33      30.738   4.146 -30.429  1.00 23.72           C  
ANISOU  285  CZ  TYR A  33     3200   2890   2921   -119   -306    364       C  
ATOM    286  OH  TYR A  33      30.384   4.297 -31.753  1.00 23.23           O  
ANISOU  286  OH  TYR A  33     3121   2840   2867    -92   -254    356       O  
ATOM    287  N   LYS A  34      33.656   6.378 -27.084  1.00 31.36           N  
ANISOU  287  N   LYS A  34     4214   3807   3896   -316   -552    455       N  
ATOM    288  CA  LYS A  34      33.642   7.795 -27.464  1.00 33.71           C  
ANISOU  288  CA  LYS A  34     4531   4091   4186   -346   -545    447       C  
ATOM    289  C   LYS A  34      32.763   7.937 -28.699  1.00 31.70           C  
ANISOU  289  C   LYS A  34     4262   3849   3932   -293   -460    415       C  
ATOM    290  O   LYS A  34      33.197   7.641 -29.816  1.00 32.68           O  
ANISOU  290  O   LYS A  34     4313   4001   4104   -261   -425    434       O  
ATOM    291  CB  LYS A  34      35.061   8.307 -27.746  1.00 34.06           C  
ANISOU  291  CB  LYS A  34     4501   4146   4292   -383   -593    504       C  
ATOM    292  CG  LYS A  34      36.094   7.930 -26.682  1.00 38.37           C  
ANISOU  292  CG  LYS A  34     5033   4686   4858   -432   -689    553       C  
ATOM    293  CD  LYS A  34      36.588   9.122 -25.886  1.00 43.44           C  
ANISOU  293  CD  LYS A  34     5731   5297   5477   -517   -767    569       C  
ATOM    294  CE  LYS A  34      37.647   9.899 -26.668  1.00 47.82           C  
ANISOU  294  CE  LYS A  34     6201   5866   6103   -541   -782    617       C  
ATOM    295  NZ  LYS A  34      38.789  10.328 -25.793  1.00 53.47           N  
ANISOU  295  NZ  LYS A  34     6910   6565   6841   -626   -896    677       N  
ATOM    296  N   PRO A  35      31.511   8.373 -28.502  1.00 29.82           N  
ANISOU  296  N   PRO A  35     4100   3588   3644   -285   -423    370       N  
ATOM    297  CA  PRO A  35      30.579   8.424 -29.612  1.00 27.07           C  
ANISOU  297  CA  PRO A  35     3739   3249   3296   -238   -353    346       C  
ATOM    298  C   PRO A  35      30.813   9.639 -30.494  1.00 27.85           C  
ANISOU  298  C   PRO A  35     3821   3348   3414   -250   -337    354       C  
ATOM    299  O   PRO A  35      31.389  10.644 -30.045  1.00 25.31           O  
ANISOU  299  O   PRO A  35     3521   3007   3088   -298   -374    365       O  
ATOM    300  CB  PRO A  35      29.217   8.540 -28.920  1.00 26.66           C  
ANISOU  300  CB  PRO A  35     3768   3167   3195   -231   -327    307       C  
ATOM    301  CG  PRO A  35      29.500   9.118 -27.580  1.00 26.85           C  
ANISOU  301  CG  PRO A  35     3866   3154   3184   -284   -373    306       C  
ATOM    302  CD  PRO A  35      30.972   9.026 -27.295  1.00 29.78           C  
ANISOU  302  CD  PRO A  35     4196   3539   3581   -324   -445    346       C  
ATOM    303  N   SER A  36      30.373   9.532 -31.743  1.00 27.51           N  
ANISOU  303  N   SER A  36     3745   3323   3386   -211   -285    348       N  
ATOM    304  CA  SER A  36      30.324  10.680 -32.630  1.00 30.59           C  
ANISOU  304  CA  SER A  36     4131   3709   3785   -217   -261    350       C  
ATOM    305  C   SER A  36      28.888  11.022 -32.992  1.00 30.56           C  
ANISOU  305  C   SER A  36     4167   3690   3756   -191   -218    321       C  
ATOM    306  O   SER A  36      28.046  10.135 -33.159  1.00 30.48           O  
ANISOU  306  O   SER A  36     4159   3687   3736   -157   -195    308       O  
ATOM    307  CB  SER A  36      31.127  10.425 -33.904  1.00 30.32           C  
ANISOU  307  CB  SER A  36     4026   3703   3791   -198   -238    376       C  
ATOM    308  OG  SER A  36      32.516  10.445 -33.643  1.00 31.54           O  
ANISOU  308  OG  SER A  36     4133   3866   3985   -226   -275    414       O  
ATOM    309  N   LEU A  37      28.617  12.322 -33.078  1.00 31.19           N  
ANISOU  309  N   LEU A  37     4278   3745   3828   -210   -209    317       N  
ATOM    310  CA  LEU A  37      27.390  12.832 -33.690  1.00 30.35           C  
ANISOU  310  CA  LEU A  37     4192   3625   3716   -185   -167    304       C  
ATOM    311  C   LEU A  37      27.784  13.895 -34.712  1.00 30.02           C  
ANISOU  311  C   LEU A  37     4130   3584   3691   -195   -156    320       C  
ATOM    312  O   LEU A  37      28.966  14.201 -34.850  1.00 31.56           O  
ANISOU  312  O   LEU A  37     4298   3790   3902   -222   -178    338       O  
ATOM    313  CB  LEU A  37      26.425  13.367 -32.635  1.00 28.85           C  
ANISOU  313  CB  LEU A  37     4070   3392   3501   -191   -153    284       C  
ATOM    314  CG  LEU A  37      25.868  12.294 -31.705  1.00 29.01           C  
ANISOU  314  CG  LEU A  37     4113   3407   3502   -176   -153    269       C  
ATOM    315  CD1 LEU A  37      25.167  12.927 -30.518  1.00 30.34           C  
ANISOU  315  CD1 LEU A  37     4362   3523   3643   -189   -134    251       C  
ATOM    316  CD2 LEU A  37      24.952  11.307 -32.442  1.00 27.89           C  
ANISOU  316  CD2 LEU A  37     3937   3288   3374   -132   -127    268       C  
ATOM    317  N   PHE A  38      26.818  14.435 -35.447  1.00 29.52           N  
ANISOU  317  N   PHE A  38     4076   3511   3629   -175   -124    318       N  
ATOM    318  CA  PHE A  38      27.142  15.293 -36.590  1.00 28.60           C  
ANISOU  318  CA  PHE A  38     3940   3399   3527   -181   -112    334       C  
ATOM    319  C   PHE A  38      26.305  16.554 -36.645  1.00 30.34           C  
ANISOU  319  C   PHE A  38     4198   3585   3747   -182    -91    333       C  
ATOM    320  O   PHE A  38      25.163  16.574 -36.193  1.00 31.01           O  
ANISOU  320  O   PHE A  38     4309   3645   3827   -164    -72    324       O  
ATOM    321  CB  PHE A  38      26.979  14.523 -37.903  1.00 26.82           C  
ANISOU  321  CB  PHE A  38     3680   3202   3307   -152    -95    344       C  
ATOM    322  CG  PHE A  38      27.859  13.309 -38.009  1.00 26.79           C  
ANISOU  322  CG  PHE A  38     3643   3228   3309   -145   -102    349       C  
ATOM    323  CD1 PHE A  38      27.505  12.113 -37.379  1.00 30.47           C  
ANISOU  323  CD1 PHE A  38     4111   3702   3765   -128   -110    336       C  
ATOM    324  CD2 PHE A  38      29.035  13.353 -38.748  1.00 24.22           C  
ANISOU  324  CD2 PHE A  38     3282   2919   3002   -153    -95    369       C  
ATOM    325  CE1 PHE A  38      28.321  10.983 -37.464  1.00 28.06           C  
ANISOU  325  CE1 PHE A  38     3773   3419   3468   -118   -112    343       C  
ATOM    326  CE2 PHE A  38      29.852  12.228 -38.848  1.00 25.94           C  
ANISOU  326  CE2 PHE A  38     3466   3157   3234   -141    -90    379       C  
ATOM    327  CZ  PHE A  38      29.492  11.043 -38.199  1.00 28.97           C  
ANISOU  327  CZ  PHE A  38     3852   3547   3607   -123   -100    366       C  
ATOM    328  N   ALA A  39      26.891  17.602 -37.214  1.00 30.22           N  
ANISOU  328  N   ALA A  39     4180   3563   3740   -203    -90    346       N  
ATOM    329  CA  ALA A  39      26.181  18.835 -37.496  1.00 31.29           C  
ANISOU  329  CA  ALA A  39     4344   3666   3880   -202    -67    351       C  
ATOM    330  C   ALA A  39      26.442  19.239 -38.942  1.00 31.78           C  
ANISOU  330  C   ALA A  39     4377   3745   3955   -198    -58    372       C  
ATOM    331  O   ALA A  39      27.537  19.020 -39.458  1.00 32.13           O  
ANISOU  331  O   ALA A  39     4390   3814   4004   -212    -67    382       O  
ATOM    332  CB  ALA A  39      26.639  19.940 -36.536  1.00 30.20           C  
ANISOU  332  CB  ALA A  39     4254   3489   3731   -240    -73    344       C  
ATOM    333  N   HIS A  40      25.436  19.811 -39.602  1.00 32.47           N  
ANISOU  333  N   HIS A  40     4474   3815   4049   -179    -38    383       N  
ATOM    334  CA  HIS A  40      25.633  20.414 -40.917  1.00 34.62           C  
ANISOU  334  CA  HIS A  40     4734   4094   4327   -182    -32    405       C  
ATOM    335  C   HIS A  40      26.754  21.456 -40.846  1.00 36.22           C  
ANISOU  335  C   HIS A  40     4943   4286   4533   -217    -33    409       C  
ATOM    336  O   HIS A  40      26.844  22.198 -39.875  1.00 35.67           O  
ANISOU  336  O   HIS A  40     4905   4185   4461   -238    -35    399       O  
ATOM    337  CB  HIS A  40      24.337  21.074 -41.407  1.00 34.30           C  
ANISOU  337  CB  HIS A  40     4706   4028   4299   -161    -17    422       C  
ATOM    338  CG  HIS A  40      23.282  20.100 -41.834  1.00 35.17           C  
ANISOU  338  CG  HIS A  40     4800   4151   4413   -133    -25    431       C  
ATOM    339  ND1 HIS A  40      22.006  20.108 -41.311  1.00 36.42           N  
ANISOU  339  ND1 HIS A  40     4962   4285   4593   -110    -15    438       N  
ATOM    340  CD2 HIS A  40      23.313  19.086 -42.731  1.00 35.49           C  
ANISOU  340  CD2 HIS A  40     4825   4222   4438   -127    -40    437       C  
ATOM    341  CE1 HIS A  40      21.296  19.144 -41.871  1.00 35.76           C  
ANISOU  341  CE1 HIS A  40     4857   4219   4510    -94    -32    451       C  
ATOM    342  NE2 HIS A  40      22.065  18.511 -42.738  1.00 36.12           N  
ANISOU  342  NE2 HIS A  40     4897   4297   4528   -106    -49    448       N  
ATOM    343  N   CYS A  41      27.619  21.483 -41.855  1.00 40.47           N  
ANISOU  343  N   CYS A  41     5457   4846   5075   -227    -31    425       N  
ATOM    344  CA  CYS A  41      28.681  22.492 -41.937  1.00 47.29           C  
ANISOU  344  CA  CYS A  41     6319   5700   5949   -263    -31    436       C  
ATOM    345  C   CYS A  41      28.587  23.301 -43.248  1.00 50.55           C  
ANISOU  345  C   CYS A  41     6737   6106   6363   -261    -10    457       C  
ATOM    346  O   CYS A  41      27.761  22.982 -44.104  1.00 50.56           O  
ANISOU  346  O   CYS A  41     6743   6113   6355   -235     -2    465       O  
ATOM    347  CB  CYS A  41      30.061  21.843 -41.762  1.00 46.96           C  
ANISOU  347  CB  CYS A  41     6236   5685   5920   -283    -44    442       C  
ATOM    348  SG  CYS A  41      30.456  20.540 -42.957  1.00 50.33           S  
ANISOU  348  SG  CYS A  41     6623   6150   6348   -254    -20    454       S  
ATOM    349  N   PRO A  42      29.407  24.369 -43.395  1.00 55.51           N  
ANISOU  349  N   PRO A  42     7368   6720   7003   -293     -7    469       N  
ATOM    350  CA  PRO A  42      29.373  25.159 -44.636  1.00 58.27           C  
ANISOU  350  CA  PRO A  42     7726   7061   7351   -293     14    491       C  
ATOM    351  C   PRO A  42      29.750  24.346 -45.871  1.00 61.54           C  
ANISOU  351  C   PRO A  42     8120   7505   7757   -279     33    504       C  
ATOM    352  O   PRO A  42      30.586  23.436 -45.794  1.00 61.26           O  
ANISOU  352  O   PRO A  42     8053   7495   7730   -280     38    504       O  
ATOM    353  CB  PRO A  42      30.417  26.254 -44.391  1.00 58.72           C  
ANISOU  353  CB  PRO A  42     7785   7102   7426   -336     13    500       C  
ATOM    354  CG  PRO A  42      30.505  26.372 -42.915  1.00 59.00           C  
ANISOU  354  CG  PRO A  42     7836   7119   7461   -358    -14    481       C  
ATOM    355  CD  PRO A  42      30.293  24.982 -42.385  1.00 56.30           C  
ANISOU  355  CD  PRO A  42     7473   6804   7113   -335    -27    466       C  
ATOM    356  N   GLU A  43      29.124  24.687 -46.995  1.00 66.15           N  
ANISOU  356  N   GLU A  43     8728   8080   8325   -267     45    520       N  
ATOM    357  CA  GLU A  43      29.321  23.987 -48.269  1.00 70.89           C  
ANISOU  357  CA  GLU A  43     9334   8697   8903   -257     66    532       C  
ATOM    358  C   GLU A  43      30.789  23.944 -48.709  1.00 72.27           C  
ANISOU  358  C   GLU A  43     9485   8882   9092   -274    100    544       C  
ATOM    359  O   GLU A  43      31.228  22.978 -49.336  1.00 71.66           O  
ANISOU  359  O   GLU A  43     9404   8820   9002   -261    127    548       O  
ATOM    360  CB  GLU A  43      28.468  24.635 -49.374  1.00 73.22           C  
ANISOU  360  CB  GLU A  43     9670   8973   9178   -253     65    553       C  
ATOM    361  CG  GLU A  43      26.961  24.745 -49.069  1.00 76.34           C  
ANISOU  361  CG  GLU A  43    10078   9353   9573   -235     33    555       C  
ATOM    362  CD  GLU A  43      26.235  23.398 -49.055  1.00 79.50           C  
ANISOU  362  CD  GLU A  43    10477   9772   9957   -214     14    546       C  
ATOM    363  OE1 GLU A  43      26.649  22.470 -49.790  1.00 79.80           O  
ANISOU  363  OE1 GLU A  43    10526   9827   9966   -214     24    545       O  
ATOM    364  OE2 GLU A  43      25.238  23.272 -48.309  1.00 80.79           O  
ANISOU  364  OE2 GLU A  43    10631   9929  10137   -198     -7    542       O  
ATOM    365  N   SER A  44      31.535  24.993 -48.359  1.00 74.52           N  
ANISOU  365  N   SER A  44     9755   9154   9404   -302    102    554       N  
ATOM    366  CA  SER A  44      32.920  25.175 -48.804  1.00 76.43           C  
ANISOU  366  CA  SER A  44     9966   9401   9672   -322    135    576       C  
ATOM    367  C   SER A  44      33.958  24.318 -48.070  1.00 76.16           C  
ANISOU  367  C   SER A  44     9875   9389   9675   -327    135    579       C  
ATOM    368  O   SER A  44      34.989  23.972 -48.657  1.00 77.78           O  
ANISOU  368  O   SER A  44    10048   9601   9904   -327    176    602       O  
ATOM    369  CB  SER A  44      33.318  26.656 -48.737  1.00 77.10           C  
ANISOU  369  CB  SER A  44    10056   9462   9776   -357    132    590       C  
ATOM    370  OG  SER A  44      33.146  27.173 -47.428  1.00 79.41           O  
ANISOU  370  OG  SER A  44    10348   9742  10081   -377     90    575       O  
ATOM    371  N   GLN A  45      33.700  23.986 -46.802  1.00 74.32           N  
ANISOU  371  N   GLN A  45     9629   9162   9448   -330     92    559       N  
ATOM    372  CA  GLN A  45      34.667  23.211 -46.010  1.00 72.73           C  
ANISOU  372  CA  GLN A  45     9371   8978   9283   -338     79    567       C  
ATOM    373  C   GLN A  45      34.686  21.729 -46.403  1.00 70.65           C  
ANISOU  373  C   GLN A  45     9092   8737   9013   -300    107    565       C  
ATOM    374  O   GLN A  45      33.643  21.142 -46.723  1.00 69.85           O  
ANISOU  374  O   GLN A  45     9030   8638   8870   -271    110    543       O  
ATOM    375  CB  GLN A  45      34.467  23.403 -44.496  1.00 72.70           C  
ANISOU  375  CB  GLN A  45     9372   8969   9283   -362     21    550       C  
ATOM    376  CG  GLN A  45      33.400  22.526 -43.854  1.00 74.02           C  
ANISOU  376  CG  GLN A  45     9562   9142   9419   -332      2    518       C  
ATOM    377  CD  GLN A  45      33.703  22.202 -42.395  1.00 75.87           C  
ANISOU  377  CD  GLN A  45     9786   9377   9664   -354    -46    510       C  
ATOM    378  OE1 GLN A  45      34.091  21.076 -42.066  1.00 74.68           O  
ANISOU  378  OE1 GLN A  45     9599   9248   9527   -341    -52    513       O  
ATOM    379  NE2 GLN A  45      33.530  23.190 -41.516  1.00 74.77           N  
ANISOU  379  NE2 GLN A  45     9683   9209   9516   -389    -77    500       N  
ATOM    380  N   ALA A  46      35.885  21.146 -46.381  1.00 68.01           N  
ANISOU  380  N   ALA A  46     8700   8415   8725   -301    129    591       N  
ATOM    381  CA  ALA A  46      36.106  19.781 -46.859  1.00 64.74           C  
ANISOU  381  CA  ALA A  46     8271   8015   8312   -263    172    595       C  
ATOM    382  C   ALA A  46      35.738  18.726 -45.819  1.00 61.93           C  
ANISOU  382  C   ALA A  46     7904   7674   7952   -249    134    575       C  
ATOM    383  O   ALA A  46      36.203  18.770 -44.671  1.00 61.61           O  
ANISOU  383  O   ALA A  46     7824   7640   7944   -271     87    582       O  
ATOM    384  CB  ALA A  46      37.552  19.604 -47.319  1.00 66.16           C  
ANISOU  384  CB  ALA A  46     8390   8196   8554   -265    225    640       C  
ATOM    385  N   THR A  47      34.895  17.782 -46.233  1.00 56.65           N  
ANISOU  385  N   THR A  47     7275   7010   7239   -214    150    551       N  
ATOM    386  CA  THR A  47      34.501  16.663 -45.384  1.00 51.69           C  
ANISOU  386  CA  THR A  47     6641   6396   6604   -196    123    532       C  
ATOM    387  C   THR A  47      34.219  15.405 -46.211  1.00 48.50           C  
ANISOU  387  C   THR A  47     6263   5993   6170   -158    170    524       C  
ATOM    388  O   THR A  47      34.038  15.478 -47.429  1.00 48.74           O  
ANISOU  388  O   THR A  47     6338   6011   6170   -149    214    526       O  
ATOM    389  CB  THR A  47      33.274  17.024 -44.493  1.00 52.27           C  
ANISOU  389  CB  THR A  47     6750   6465   6644   -205     66    499       C  
ATOM    390  OG1 THR A  47      33.056  15.991 -43.520  1.00 47.67           O  
ANISOU  390  OG1 THR A  47     6156   5895   6062   -192     39    484       O  
ATOM    391  CG2 THR A  47      32.010  17.221 -45.337  1.00 50.60           C  
ANISOU  391  CG2 THR A  47     6599   6244   6384   -191     74    482       C  
ATOM    392  N   LYS A  48      34.194  14.256 -45.543  1.00 43.48           N  
ANISOU  392  N   LYS A  48     5611   5369   5540   -139    159    515       N  
ATOM    393  CA  LYS A  48      33.790  13.008 -46.186  1.00 40.79           C  
ANISOU  393  CA  LYS A  48     5307   5025   5164   -106    196    502       C  
ATOM    394  C   LYS A  48      32.427  12.497 -45.686  1.00 37.83           C  
ANISOU  394  C   LYS A  48     4973   4656   4745   -100    149    467       C  
ATOM    395  O   LYS A  48      31.960  11.438 -46.118  1.00 34.86           O  
ANISOU  395  O   LYS A  48     4634   4277   4335    -79    168    455       O  
ATOM    396  CB  LYS A  48      34.877  11.935 -46.031  1.00 41.00           C  
ANISOU  396  CB  LYS A  48     5286   5057   5237    -83    237    525       C  
ATOM    397  CG  LYS A  48      35.095  11.437 -44.601  1.00 42.92           C  
ANISOU  397  CG  LYS A  48     5476   5316   5514    -85    185    525       C  
ATOM    398  CD  LYS A  48      36.026  10.224 -44.579  1.00 42.08           C  
ANISOU  398  CD  LYS A  48     5326   5210   5452    -54    230    551       C  
ATOM    399  CE  LYS A  48      36.274   9.752 -43.163  1.00 40.53           C  
ANISOU  399  CE  LYS A  48     5079   5029   5291    -60    170    558       C  
ATOM    400  NZ  LYS A  48      37.155   8.551 -43.133  1.00 41.56           N  
ANISOU  400  NZ  LYS A  48     5163   5158   5471    -26    214    588       N  
ATOM    401  N   TYR A  49      31.803  13.244 -44.774  1.00 35.01           N  
ANISOU  401  N   TYR A  49     4611   4302   4388   -119     94    454       N  
ATOM    402  CA  TYR A  49      30.493  12.871 -44.226  1.00 32.66           C  
ANISOU  402  CA  TYR A  49     4345   4006   4060   -112     56    427       C  
ATOM    403  C   TYR A  49      29.386  13.740 -44.808  1.00 32.15           C  
ANISOU  403  C   TYR A  49     4323   3928   3966   -121     42    423       C  
ATOM    404  O   TYR A  49      29.483  14.973 -44.819  1.00 29.73           O  
ANISOU  404  O   TYR A  49     4013   3612   3672   -140     35    432       O  
ATOM    405  CB  TYR A  49      30.474  12.974 -42.699  1.00 31.13           C  
ANISOU  405  CB  TYR A  49     4125   3817   3887   -123     12    418       C  
ATOM    406  CG  TYR A  49      31.610  12.254 -42.015  1.00 32.00           C  
ANISOU  406  CG  TYR A  49     4187   3939   4032   -121     11    431       C  
ATOM    407  CD1 TYR A  49      32.728  12.953 -41.551  1.00 29.90           C  
ANISOU  407  CD1 TYR A  49     3878   3673   3809   -148     -3    456       C  
ATOM    408  CD2 TYR A  49      31.568  10.876 -41.824  1.00 30.56           C  
ANISOU  408  CD2 TYR A  49     4000   3765   3845    -96     19    424       C  
ATOM    409  CE1 TYR A  49      33.773  12.292 -40.919  1.00 31.22           C  
ANISOU  409  CE1 TYR A  49     3993   3850   4018   -148    -13    478       C  
ATOM    410  CE2 TYR A  49      32.605  10.208 -41.202  1.00 29.78           C  
ANISOU  410  CE2 TYR A  49     3854   3676   3787    -92     17    444       C  
ATOM    411  CZ  TYR A  49      33.701  10.913 -40.748  1.00 33.32           C  
ANISOU  411  CZ  TYR A  49     4253   4125   4281   -118     -1    473       C  
ATOM    412  OH  TYR A  49      34.722  10.230 -40.120  1.00 34.96           O  
ANISOU  412  OH  TYR A  49     4404   4340   4537   -116    -12    502       O  
ATOM    413  N   PHE A  50      28.335  13.085 -45.293  1.00 31.80           N  
ANISOU  413  N   PHE A  50     4316   3881   3887   -109     35    414       N  
ATOM    414  CA  PHE A  50      27.195  13.771 -45.899  1.00 30.80           C  
ANISOU  414  CA  PHE A  50     4224   3740   3740   -117     15    419       C  
ATOM    415  C   PHE A  50      25.885  13.184 -45.396  1.00 31.06           C  
ANISOU  415  C   PHE A  50     4265   3771   3763   -108    -20    409       C  
ATOM    416  O   PHE A  50      25.780  11.968 -45.196  1.00 28.19           O  
ANISOU  416  O   PHE A  50     3906   3417   3388    -96    -20    397       O  
ATOM    417  CB  PHE A  50      27.262  13.671 -47.426  1.00 31.64           C  
ANISOU  417  CB  PHE A  50     4376   3836   3810   -122     39    433       C  
ATOM    418  CG  PHE A  50      28.454  14.367 -48.023  1.00 32.54           C  
ANISOU  418  CG  PHE A  50     4483   3946   3934   -130     81    447       C  
ATOM    419  CD1 PHE A  50      29.658  13.692 -48.194  1.00 32.03           C  
ANISOU  419  CD1 PHE A  50     4403   3886   3881   -119    129    451       C  
ATOM    420  CD2 PHE A  50      28.377  15.706 -48.393  1.00 33.25           C  
ANISOU  420  CD2 PHE A  50     4579   4025   4031   -147     75    462       C  
ATOM    421  CE1 PHE A  50      30.766  14.344 -48.733  1.00 34.15           C  
ANISOU  421  CE1 PHE A  50     4658   4148   4170   -127    173    471       C  
ATOM    422  CE2 PHE A  50      29.482  16.366 -48.935  1.00 33.15           C  
ANISOU  422  CE2 PHE A  50     4558   4006   4030   -157    115    478       C  
ATOM    423  CZ  PHE A  50      30.674  15.681 -49.105  1.00 31.93           C  
ANISOU  423  CZ  PHE A  50     4385   3857   3891   -147    165    483       C  
ATOM    424  N   ASP A  51      24.885  14.040 -45.191  1.00 29.76           N  
ANISOU  424  N   ASP A  51     4103   3594   3611   -112    -44    417       N  
ATOM    425  CA  ASP A  51      23.563  13.541 -44.822  1.00 29.05           C  
ANISOU  425  CA  ASP A  51     4016   3500   3524   -103    -72    417       C  
ATOM    426  C   ASP A  51      22.921  12.883 -46.039  1.00 30.09           C  
ANISOU  426  C   ASP A  51     4182   3629   3622   -110    -89    432       C  
ATOM    427  O   ASP A  51      23.482  12.937 -47.135  1.00 32.82           O  
ANISOU  427  O   ASP A  51     4560   3972   3939   -121    -75    439       O  
ATOM    428  CB  ASP A  51      22.690  14.629 -44.183  1.00 27.45           C  
ANISOU  428  CB  ASP A  51     3800   3277   3354   -101    -82    427       C  
ATOM    429  CG  ASP A  51      22.184  15.668 -45.173  1.00 29.15           C  
ANISOU  429  CG  ASP A  51     4028   3475   3573   -111    -92    457       C  
ATOM    430  OD1 ASP A  51      22.300  15.497 -46.407  1.00 27.33           O  
ANISOU  430  OD1 ASP A  51     3823   3248   3313   -123    -99    471       O  
ATOM    431  OD2 ASP A  51      21.644  16.681 -44.689  1.00 34.96           O  
ANISOU  431  OD2 ASP A  51     4753   4190   4340   -107    -89    468       O  
ATOM    432  N   ILE A  52      21.765  12.252 -45.856  1.00 30.20           N  
ANISOU  432  N   ILE A  52     4197   3640   3639   -106   -119    438       N  
ATOM    433  CA  ILE A  52      21.173  11.447 -46.935  1.00 30.15           C  
ANISOU  433  CA  ILE A  52     4232   3629   3596   -121   -146    452       C  
ATOM    434  C   ILE A  52      20.813  12.269 -48.179  1.00 31.75           C  
ANISOU  434  C   ILE A  52     4466   3816   3783   -143   -168    485       C  
ATOM    435  O   ILE A  52      20.698  11.721 -49.277  1.00 31.02           O  
ANISOU  435  O   ILE A  52     4429   3715   3643   -163   -185    495       O  
ATOM    436  CB  ILE A  52      19.952  10.608 -46.454  1.00 29.24           C  
ANISOU  436  CB  ILE A  52     4104   3512   3495   -118   -182    459       C  
ATOM    437  CG1 ILE A  52      18.810  11.511 -45.973  1.00 26.23           C  
ANISOU  437  CG1 ILE A  52     3683   3117   3168   -113   -204    488       C  
ATOM    438  CG2 ILE A  52      20.384   9.620 -45.385  1.00 30.11           C  
ANISOU  438  CG2 ILE A  52     4197   3636   3608    -99   -160    426       C  
ATOM    439  CD1 ILE A  52      17.504  10.770 -45.656  1.00 27.32           C  
ANISOU  439  CD1 ILE A  52     3801   3249   3331   -113   -239    508       C  
ATOM    440  N   TYR A  53      20.657  13.581 -47.994  1.00 32.82           N  
ANISOU  440  N   TYR A  53     4574   3942   3953   -140   -167    501       N  
ATOM    441  CA  TYR A  53      20.307  14.503 -49.076  1.00 33.28           C  
ANISOU  441  CA  TYR A  53     4658   3984   4004   -159   -189    536       C  
ATOM    442  C   TYR A  53      21.537  15.113 -49.766  1.00 35.43           C  
ANISOU  442  C   TYR A  53     4959   4255   4248   -168   -151    528       C  
ATOM    443  O   TYR A  53      21.397  15.982 -50.630  1.00 35.78           O  
ANISOU  443  O   TYR A  53     5028   4285   4284   -183   -162    554       O  
ATOM    444  CB  TYR A  53      19.393  15.618 -48.544  1.00 33.72           C  
ANISOU  444  CB  TYR A  53     4670   4024   4120   -149   -205    564       C  
ATOM    445  CG  TYR A  53      18.227  15.106 -47.720  1.00 34.70           C  
ANISOU  445  CG  TYR A  53     4754   4144   4286   -135   -227    575       C  
ATOM    446  CD1 TYR A  53      18.212  15.242 -46.328  1.00 34.70           C  
ANISOU  446  CD1 TYR A  53     4716   4143   4325   -110   -194    554       C  
ATOM    447  CD2 TYR A  53      17.144  14.476 -48.330  1.00 33.52           C  
ANISOU  447  CD2 TYR A  53     4612   3989   4137   -152   -282    610       C  
ATOM    448  CE1 TYR A  53      17.137  14.761 -45.563  1.00 34.46           C  
ANISOU  448  CE1 TYR A  53     4653   4105   4336    -95   -204    566       C  
ATOM    449  CE2 TYR A  53      16.074  13.999 -47.586  1.00 35.78           C  
ANISOU  449  CE2 TYR A  53     4855   4271   4470   -139   -299    627       C  
ATOM    450  CZ  TYR A  53      16.078  14.141 -46.205  1.00 34.86           C  
ANISOU  450  CZ  TYR A  53     4698   4152   4394   -108   -255    604       C  
ATOM    451  OH  TYR A  53      15.016  13.663 -45.482  1.00 36.86           O  
ANISOU  451  OH  TYR A  53     4913   4397   4696    -95   -263    622       O  
ATOM    452  N   GLY A  54      22.733  14.664 -49.378  1.00 35.21           N  
ANISOU  452  N   GLY A  54     4926   4242   4211   -157   -105    496       N  
ATOM    453  CA  GLY A  54      23.981  15.162 -49.955  1.00 34.80           C  
ANISOU  453  CA  GLY A  54     4891   4189   4144   -163    -60    492       C  
ATOM    454  C   GLY A  54      24.503  16.459 -49.351  1.00 36.95           C  
ANISOU  454  C   GLY A  54     5123   4460   4458   -161    -43    493       C  
ATOM    455  O   GLY A  54      25.346  17.137 -49.948  1.00 35.80           O  
ANISOU  455  O   GLY A  54     4989   4308   4305   -171    -13    501       O  
ATOM    456  N   LYS A  55      24.008  16.813 -48.168  1.00 37.66           N  
ANISOU  456  N   LYS A  55     5172   4550   4587   -150    -58    487       N  
ATOM    457  CA  LYS A  55      24.506  17.992 -47.462  1.00 39.24           C  
ANISOU  457  CA  LYS A  55     5345   4742   4820   -153    -43    484       C  
ATOM    458  C   LYS A  55      25.724  17.639 -46.599  1.00 37.52           C  
ANISOU  458  C   LYS A  55     5101   4541   4615   -152    -19    461       C  
ATOM    459  O   LYS A  55      25.701  16.642 -45.872  1.00 37.21           O  
ANISOU  459  O   LYS A  55     5047   4514   4576   -140    -24    443       O  
ATOM    460  CB  LYS A  55      23.402  18.662 -46.632  1.00 41.16           C  
ANISOU  460  CB  LYS A  55     5572   4967   5098   -143    -62    491       C  
ATOM    461  CG  LYS A  55      22.241  19.210 -47.473  1.00 47.68           C  
ANISOU  461  CG  LYS A  55     6412   5774   5930   -144    -88    528       C  
ATOM    462  CD  LYS A  55      21.468  20.322 -46.748  1.00 54.96           C  
ANISOU  462  CD  LYS A  55     7316   6668   6898   -133    -84    542       C  
ATOM    463  CE  LYS A  55      22.081  21.710 -46.969  1.00 58.63           C  
ANISOU  463  CE  LYS A  55     7793   7115   7370   -145    -63    549       C  
ATOM    464  NZ  LYS A  55      21.961  22.175 -48.385  1.00 60.32           N  
ANISOU  464  NZ  LYS A  55     8030   7322   7566   -158    -79    582       N  
ATOM    465  N   PRO A  56      26.795  18.454 -46.692  1.00 36.59           N  
ANISOU  465  N   PRO A  56     4974   4421   4509   -167      3    465       N  
ATOM    466  CA  PRO A  56      28.050  18.208 -45.978  1.00 35.67           C  
ANISOU  466  CA  PRO A  56     4824   4318   4412   -173     18    456       C  
ATOM    467  C   PRO A  56      27.904  18.328 -44.461  1.00 35.10           C  
ANISOU  467  C   PRO A  56     4733   4242   4360   -176     -6    439       C  
ATOM    468  O   PRO A  56      27.243  19.249 -43.975  1.00 34.08           O  
ANISOU  468  O   PRO A  56     4618   4091   4238   -181    -17    438       O  
ATOM    469  CB  PRO A  56      28.981  19.299 -46.520  1.00 35.94           C  
ANISOU  469  CB  PRO A  56     4854   4343   4460   -194     40    473       C  
ATOM    470  CG  PRO A  56      28.077  20.386 -46.955  1.00 35.73           C  
ANISOU  470  CG  PRO A  56     4856   4294   4425   -199     28    484       C  
ATOM    471  CD  PRO A  56      26.855  19.696 -47.487  1.00 36.17           C  
ANISOU  471  CD  PRO A  56     4938   4350   4455   -182     11    486       C  
ATOM    472  N   CYS A  57      28.515  17.389 -43.742  1.00 33.11           N  
ANISOU  472  N   CYS A  57     4458   4007   4116   -172     -9    428       N  
ATOM    473  CA  CYS A  57      28.440  17.318 -42.290  1.00 34.14           C  
ANISOU  473  CA  CYS A  57     4582   4133   4257   -178    -34    412       C  
ATOM    474  C   CYS A  57      29.832  17.260 -41.665  1.00 34.57           C  
ANISOU  474  C   CYS A  57     4603   4197   4335   -201    -42    419       C  
ATOM    475  O   CYS A  57      30.762  16.728 -42.257  1.00 36.78           O  
ANISOU  475  O   CYS A  57     4852   4495   4630   -197    -23    435       O  
ATOM    476  CB  CYS A  57      27.651  16.081 -41.858  1.00 34.35           C  
ANISOU  476  CB  CYS A  57     4612   4170   4270   -154    -43    396       C  
ATOM    477  SG  CYS A  57      25.876  16.155 -42.183  1.00 37.54           S  
ANISOU  477  SG  CYS A  57     5045   4558   4662   -134    -47    395       S  
ATOM    478  N   THR A  58      29.965  17.812 -40.468  1.00 33.31           N  
ANISOU  478  N   THR A  58     4453   4023   4181   -225    -70    412       N  
ATOM    479  CA  THR A  58      31.202  17.704 -39.713  1.00 33.14           C  
ANISOU  479  CA  THR A  58     4400   4007   4182   -254    -96    424       C  
ATOM    480  C   THR A  58      30.979  16.756 -38.546  1.00 31.13           C  
ANISOU  480  C   THR A  58     4153   3757   3919   -249   -123    408       C  
ATOM    481  O   THR A  58      29.918  16.778 -37.924  1.00 31.08           O  
ANISOU  481  O   THR A  58     4189   3733   3886   -240   -126    384       O  
ATOM    482  CB  THR A  58      31.721  19.088 -39.210  1.00 34.54           C  
ANISOU  482  CB  THR A  58     4595   4159   4369   -301   -119    432       C  
ATOM    483  OG1 THR A  58      32.811  18.889 -38.304  1.00 38.01           O  
ANISOU  483  OG1 THR A  58     5008   4603   4830   -336   -161    448       O  
ATOM    484  CG2 THR A  58      30.633  19.876 -38.490  1.00 33.45           C  
ANISOU  484  CG2 THR A  58     4523   3986   4202   -306   -123    408       C  
ATOM    485  N   ARG A  59      31.977  15.920 -38.268  1.00 30.83           N  
ANISOU  485  N   ARG A  59     4070   3739   3905   -253   -139    425       N  
ATOM    486  CA  ARG A  59      31.906  14.970 -37.168  1.00 31.49           C  
ANISOU  486  CA  ARG A  59     4158   3827   3981   -251   -169    415       C  
ATOM    487  C   ARG A  59      32.275  15.652 -35.849  1.00 32.73           C  
ANISOU  487  C   ARG A  59     4343   3960   4131   -300   -221    415       C  
ATOM    488  O   ARG A  59      33.228  16.425 -35.788  1.00 32.76           O  
ANISOU  488  O   ARG A  59     4330   3959   4159   -340   -246    440       O  
ATOM    489  CB  ARG A  59      32.816  13.758 -37.430  1.00 30.01           C  
ANISOU  489  CB  ARG A  59     3909   3666   3826   -232   -163    438       C  
ATOM    490  CG  ARG A  59      32.852  12.772 -36.270  1.00 33.82           C  
ANISOU  490  CG  ARG A  59     4393   4154   4305   -232   -199    433       C  
ATOM    491  CD  ARG A  59      33.249  11.376 -36.683  1.00 33.92           C  
ANISOU  491  CD  ARG A  59     4360   4188   4340   -195   -175    447       C  
ATOM    492  NE  ARG A  59      34.684  11.250 -36.882  1.00 37.11           N  
ANISOU  492  NE  ARG A  59     4694   4603   4804   -205   -177    493       N  
ATOM    493  CZ  ARG A  59      35.508  10.553 -36.105  1.00 34.58           C  
ANISOU  493  CZ  ARG A  59     4331   4290   4519   -213   -213    523       C  
ATOM    494  NH1 ARG A  59      35.058   9.892 -35.046  1.00 31.09           N  
ANISOU  494  NH1 ARG A  59     3917   3844   4050   -214   -251    505       N  
ATOM    495  NH2 ARG A  59      36.798  10.519 -36.402  1.00 34.84           N  
ANISOU  495  NH2 ARG A  59     4289   4329   4619   -220   -210    575       N  
ATOM    496  N   LYS A  60      31.500  15.369 -34.809  1.00 33.48           N  
ANISOU  496  N   LYS A  60     4490   4038   4192   -300   -236    389       N  
ATOM    497  CA  LYS A  60      31.792  15.843 -33.468  1.00 34.70           C  
ANISOU  497  CA  LYS A  60     4693   4164   4327   -348   -286    386       C  
ATOM    498  C   LYS A  60      32.031  14.660 -32.547  1.00 34.79           C  
ANISOU  498  C   LYS A  60     4699   4186   4334   -348   -321    388       C  
ATOM    499  O   LYS A  60      31.109  13.908 -32.227  1.00 34.69           O  
ANISOU  499  O   LYS A  60     4712   4171   4295   -316   -301    363       O  
ATOM    500  CB  LYS A  60      30.672  16.746 -32.960  1.00 37.59           C  
ANISOU  500  CB  LYS A  60     5144   4486   4651   -353   -265    355       C  
ATOM    501  CG  LYS A  60      30.595  18.068 -33.726  1.00 42.65           C  
ANISOU  501  CG  LYS A  60     5796   5111   5300   -363   -240    359       C  
ATOM    502  CD  LYS A  60      29.685  19.066 -33.050  1.00 46.57           C  
ANISOU  502  CD  LYS A  60     6381   5554   5760   -374   -220    335       C  
ATOM    503  CE  LYS A  60      29.564  20.346 -33.872  1.00 53.02           C  
ANISOU  503  CE  LYS A  60     7204   6353   6587   -378   -191    342       C  
ATOM    504  NZ  LYS A  60      30.692  21.302 -33.646  1.00 53.14           N  
ANISOU  504  NZ  LYS A  60     7232   6352   6606   -439   -231    359       N  
ATOM    505  N   LEU A  61      33.295  14.492 -32.162  1.00 35.23           N  
ANISOU  505  N   LEU A  61     4714   4252   4420   -385   -375    424       N  
ATOM    506  CA  LEU A  61      33.750  13.390 -31.325  1.00 36.64           C  
ANISOU  506  CA  LEU A  61     4876   4442   4605   -390   -418    438       C  
ATOM    507  C   LEU A  61      33.664  13.838 -29.867  1.00 37.00           C  
ANISOU  507  C   LEU A  61     5008   4447   4602   -445   -476    427       C  
ATOM    508  O   LEU A  61      34.230  14.873 -29.502  1.00 37.04           O  
ANISOU  508  O   LEU A  61     5042   4428   4603   -504   -518    441       O  
ATOM    509  CB  LEU A  61      35.206  13.043 -31.672  1.00 37.36           C  
ANISOU  509  CB  LEU A  61     4871   4558   4765   -404   -449    494       C  
ATOM    510  CG  LEU A  61      35.745  11.604 -31.574  1.00 41.14           C  
ANISOU  510  CG  LEU A  61     5286   5065   5282   -374   -458    521       C  
ATOM    511  CD1 LEU A  61      37.217  11.630 -31.165  1.00 42.37           C  
ANISOU  511  CD1 LEU A  61     5373   5225   5500   -420   -526    586       C  
ATOM    512  CD2 LEU A  61      34.958  10.701 -30.627  1.00 33.56           C  
ANISOU  512  CD2 LEU A  61     4380   4097   4275   -360   -471    491       C  
ATOM    513  N   PHE A  62      32.971  13.055 -29.042  1.00 32.87           N  
ANISOU  513  N   PHE A  62     4534   3914   4041   -431   -477    402       N  
ATOM    514  CA  PHE A  62      32.751  13.413 -27.643  1.00 33.45           C  
ANISOU  514  CA  PHE A  62     4711   3942   4056   -480   -519    386       C  
ATOM    515  C   PHE A  62      33.593  12.598 -26.666  1.00 34.46           C  
ANISOU  515  C   PHE A  62     4832   4074   4186   -516   -599    416       C  
ATOM    516  O   PHE A  62      33.872  11.413 -26.899  1.00 33.88           O  
ANISOU  516  O   PHE A  62     4688   4036   4148   -480   -600    435       O  
ATOM    517  CB  PHE A  62      31.259  13.322 -27.291  1.00 32.09           C  
ANISOU  517  CB  PHE A  62     4619   3743   3832   -444   -457    337       C  
ATOM    518  CG  PHE A  62      30.400  14.262 -28.086  1.00 30.80           C  
ANISOU  518  CG  PHE A  62     4470   3565   3668   -417   -389    315       C  
ATOM    519  CD1 PHE A  62      29.751  13.826 -29.231  1.00 27.76           C  
ANISOU  519  CD1 PHE A  62     4024   3212   3312   -355   -332    309       C  
ATOM    520  CD2 PHE A  62      30.255  15.592 -27.694  1.00 29.00           C  
ANISOU  520  CD2 PHE A  62     4323   3288   3408   -457   -386    304       C  
ATOM    521  CE1 PHE A  62      28.955  14.693 -29.978  1.00 29.70           C  
ANISOU  521  CE1 PHE A  62     4279   3443   3561   -333   -277    296       C  
ATOM    522  CE2 PHE A  62      29.473  16.471 -28.443  1.00 31.65           C  
ANISOU  522  CE2 PHE A  62     4667   3609   3750   -429   -323    289       C  
ATOM    523  CZ  PHE A  62      28.819  16.023 -29.586  1.00 25.33           C  
ANISOU  523  CZ  PHE A  62     3797   2844   2984   -367   -271    288       C  
ATOM    524  N   ALA A  63      33.994  13.247 -25.574  1.00 33.88           N  
ANISOU  524  N   ALA A  63     4841   3960   4072   -589   -667    423       N  
ATOM    525  CA  ALA A  63      34.840  12.631 -24.558  1.00 35.57           C  
ANISOU  525  CA  ALA A  63     5060   4170   4284   -638   -760    459       C  
ATOM    526  C   ALA A  63      34.164  11.432 -23.899  1.00 36.21           C  
ANISOU  526  C   ALA A  63     5175   4251   4331   -603   -746    437       C  
ATOM    527  O   ALA A  63      34.837  10.514 -23.434  1.00 38.46           O  
ANISOU  527  O   ALA A  63     5422   4554   4639   -614   -806    473       O  
ATOM    528  CB  ALA A  63      35.249  13.667 -23.506  1.00 36.72           C  
ANISOU  528  CB  ALA A  63     5315   4262   4376   -732   -836    466       C  
ATOM    529  N   ASN A  64      32.833  11.453 -23.866  1.00 36.11           N  
ANISOU  529  N   ASN A  64     5231   4219   4272   -561   -666    383       N  
ATOM    530  CA  ASN A  64      32.023  10.378 -23.288  1.00 35.34           C  
ANISOU  530  CA  ASN A  64     5169   4117   4141   -524   -639    358       C  
ATOM    531  C   ASN A  64      30.572  10.466 -23.765  1.00 33.81           C  
ANISOU  531  C   ASN A  64     5002   3914   3930   -463   -534    311       C  
ATOM    532  O   ASN A  64      30.167  11.472 -24.357  1.00 33.34           O  
ANISOU  532  O   ASN A  64     4952   3842   3873   -456   -490    296       O  
ATOM    533  CB  ASN A  64      32.084  10.415 -21.753  1.00 35.30           C  
ANISOU  533  CB  ASN A  64     5288   4060   4063   -587   -698    354       C  
ATOM    534  CG  ASN A  64      31.771  11.794 -21.186  1.00 39.13           C  
ANISOU  534  CG  ASN A  64     5900   4482   4485   -640   -692    329       C  
ATOM    535  OD1 ASN A  64      30.725  12.376 -21.481  1.00 41.16           O  
ANISOU  535  OD1 ASN A  64     6200   4715   4723   -605   -604    290       O  
ATOM    536  ND2 ASN A  64      32.682  12.324 -20.368  1.00 37.67           N  
ANISOU  536  ND2 ASN A  64     5777   4265   4269   -726   -787    356       N  
ATOM    537  N   MET A  65      29.790   9.429 -23.478  1.00 32.35           N  
ANISOU  537  N   MET A  65     4828   3733   3731   -421   -500    291       N  
ATOM    538  CA  MET A  65      28.400   9.358 -23.939  1.00 33.32           C  
ANISOU  538  CA  MET A  65     4960   3850   3850   -363   -407    256       C  
ATOM    539  C   MET A  65      27.467  10.396 -23.304  1.00 34.18           C  
ANISOU  539  C   MET A  65     5182   3896   3909   -376   -357    226       C  
ATOM    540  O   MET A  65      26.515  10.848 -23.946  1.00 34.90           O  
ANISOU  540  O   MET A  65     5264   3980   4017   -337   -285    210       O  
ATOM    541  CB  MET A  65      27.840   7.943 -23.772  1.00 30.19           C  
ANISOU  541  CB  MET A  65     4544   3472   3456   -319   -387    248       C  
ATOM    542  CG  MET A  65      28.413   6.961 -24.779  1.00 30.89           C  
ANISOU  542  CG  MET A  65     4516   3620   3601   -283   -398    272       C  
ATOM    543  SD  MET A  65      27.784   5.289 -24.583  1.00 31.65           S  
ANISOU  543  SD  MET A  65     4596   3734   3697   -236   -376    263       S  
ATOM    544  CE  MET A  65      28.621   4.773 -23.086  1.00 28.57           C  
ANISOU  544  CE  MET A  65     4261   3323   3271   -285   -456    281       C  
ATOM    545  N   ARG A  66      27.732  10.769 -22.056  1.00 35.36           N  
ANISOU  545  N   ARG A  66     5442   3994   3998   -433   -394    220       N  
ATOM    546  CA  ARG A  66      26.961  11.837 -21.419  1.00 39.95           C  
ANISOU  546  CA  ARG A  66     6146   4504   4528   -450   -340    193       C  
ATOM    547  C   ARG A  66      27.145  13.184 -22.119  1.00 37.50           C  
ANISOU  547  C   ARG A  66     5829   4184   4237   -464   -326    195       C  
ATOM    548  O   ARG A  66      26.180  13.923 -22.282  1.00 38.03           O  
ANISOU  548  O   ARG A  66     5936   4213   4300   -437   -245    176       O  
ATOM    549  CB  ARG A  66      27.260  11.943 -19.920  1.00 43.50           C  
ANISOU  549  CB  ARG A  66     6737   4894   4897   -515   -383    186       C  
ATOM    550  CG  ARG A  66      26.403  10.986 -19.098  1.00 53.87           C  
ANISOU  550  CG  ARG A  66     8108   6184   6176   -488   -341    166       C  
ATOM    551  CD  ARG A  66      26.851  10.893 -17.648  1.00 62.04           C  
ANISOU  551  CD  ARG A  66     9279   7165   7127   -557   -399    165       C  
ATOM    552  NE  ARG A  66      26.249   9.738 -16.979  1.00 63.71           N  
ANISOU  552  NE  ARG A  66     9521   7371   7315   -529   -374    154       N  
ATOM    553  CZ  ARG A  66      26.578   9.312 -15.763  1.00 67.80           C  
ANISOU  553  CZ  ARG A  66    10145   7851   7764   -580   -426    156       C  
ATOM    554  NH1 ARG A  66      27.515   9.940 -15.057  1.00 69.12           N  
ANISOU  554  NH1 ARG A  66    10402   7983   7876   -666   -515    170       N  
ATOM    555  NH2 ARG A  66      25.969   8.248 -15.250  1.00 69.78           N  
ANISOU  555  NH2 ARG A  66    10415   8099   7999   -548   -394    146       N  
ATOM    556  N   ASP A  67      28.370  13.491 -22.542  1.00 36.12           N  
ANISOU  556  N   ASP A  67     5597   4040   4087   -504   -402    224       N  
ATOM    557  CA  ASP A  67      28.616  14.728 -23.293  1.00 38.32           C  
ANISOU  557  CA  ASP A  67     5859   4314   4387   -518   -391    230       C  
ATOM    558  C   ASP A  67      27.773  14.745 -24.563  1.00 35.97           C  
ANISOU  558  C   ASP A  67     5477   4048   4143   -445   -313    224       C  
ATOM    559  O   ASP A  67      27.097  15.731 -24.846  1.00 36.77           O  
ANISOU  559  O   ASP A  67     5614   4115   4243   -432   -254    210       O  
ATOM    560  CB  ASP A  67      30.102  14.900 -23.636  1.00 39.19           C  
ANISOU  560  CB  ASP A  67     5901   4459   4531   -568   -483    270       C  
ATOM    561  CG  ASP A  67      30.915  15.462 -22.476  1.00 41.94           C  
ANISOU  561  CG  ASP A  67     6351   4760   4824   -660   -566    282       C  
ATOM    562  OD1 ASP A  67      30.318  15.979 -21.510  1.00 44.71           O  
ANISOU  562  OD1 ASP A  67     6843   5041   5102   -687   -542    252       O  
ATOM    563  OD2 ASP A  67      32.160  15.388 -22.535  1.00 45.84           O  
ANISOU  563  OD2 ASP A  67     6787   5282   5350   -707   -656    324       O  
ATOM    564  N   ALA A  68      27.791  13.632 -25.295  1.00 32.80           N  
ANISOU  564  N   ALA A  68     4971   3706   3786   -399   -314    235       N  
ATOM    565  CA  ALA A  68      27.037  13.499 -26.543  1.00 32.31           C  
ANISOU  565  CA  ALA A  68     4831   3675   3770   -337   -254    234       C  
ATOM    566  C   ALA A  68      25.545  13.783 -26.343  1.00 32.59           C  
ANISOU  566  C   ALA A  68     4920   3669   3793   -299   -172    210       C  
ATOM    567  O   ALA A  68      24.943  14.536 -27.122  1.00 31.30           O  
ANISOU  567  O   ALA A  68     4739   3499   3656   -274   -125    211       O  
ATOM    568  CB  ALA A  68      27.252  12.121 -27.146  1.00 30.30           C  
ANISOU  568  CB  ALA A  68     4484   3480   3550   -301   -268    246       C  
ATOM    569  N   SER A  69      24.973  13.201 -25.285  1.00 31.78           N  
ANISOU  569  N   SER A  69     4883   3536   3655   -295   -154    193       N  
ATOM    570  CA  SER A  69      23.567  13.411 -24.922  1.00 33.97           C  
ANISOU  570  CA  SER A  69     5215   3766   3927   -260    -69    177       C  
ATOM    571  C   SER A  69      23.257  14.865 -24.581  1.00 35.06           C  
ANISOU  571  C   SER A  69     5441   3837   4043   -278    -24    168       C  
ATOM    572  O   SER A  69      22.253  15.414 -25.032  1.00 33.46           O  
ANISOU  572  O   SER A  69     5230   3612   3872   -239     48    170       O  
ATOM    573  CB  SER A  69      23.171  12.508 -23.750  1.00 34.67           C  
ANISOU  573  CB  SER A  69     5367   3829   3976   -259    -59    162       C  
ATOM    574  OG  SER A  69      23.111  11.152 -24.160  1.00 38.14           O  
ANISOU  574  OG  SER A  69     5724   4324   4444   -227    -77    170       O  
ATOM    575  N   GLN A  70      24.122  15.481 -23.783  1.00 36.68           N  
ANISOU  575  N   GLN A  70     5732   4007   4196   -341    -68    162       N  
ATOM    576  CA  GLN A  70      23.951  16.878 -23.409  1.00 38.23           C  
ANISOU  576  CA  GLN A  70     6030   4134   4364   -368    -30    152       C  
ATOM    577  C   GLN A  70      24.066  17.812 -24.613  1.00 36.26           C  
ANISOU  577  C   GLN A  70     5712   3904   4161   -356    -20    167       C  
ATOM    578  O   GLN A  70      23.448  18.876 -24.632  1.00 35.24           O  
ANISOU  578  O   GLN A  70     5637   3721   4032   -346     45    162       O  
ATOM    579  CB  GLN A  70      24.948  17.282 -22.316  1.00 39.08           C  
ANISOU  579  CB  GLN A  70     6250   4200   4398   -450    -96    145       C  
ATOM    580  CG  GLN A  70      24.675  16.650 -20.947  1.00 48.85           C  
ANISOU  580  CG  GLN A  70     7599   5392   5571   -469    -90    127       C  
ATOM    581  CD  GLN A  70      23.188  16.607 -20.581  1.00 55.31           C  
ANISOU  581  CD  GLN A  70     8471   6157   6389   -411     31    108       C  
ATOM    582  OE1 GLN A  70      22.583  15.531 -20.528  1.00 58.89           O  
ANISOU  582  OE1 GLN A  70     8879   6636   6863   -367     56    108       O  
ATOM    583  NE2 GLN A  70      22.595  17.775 -20.338  1.00 57.85           N  
ANISOU  583  NE2 GLN A  70     8885   6402   6692   -409    111     97       N  
ATOM    584  N   TRP A  71      24.858  17.407 -25.607  1.00 34.61           N  
ANISOU  584  N   TRP A  71     5389   3768   3992   -356    -80    187       N  
ATOM    585  CA  TRP A  71      25.026  18.188 -26.829  1.00 33.34           C  
ANISOU  585  CA  TRP A  71     5161   3631   3876   -345    -74    203       C  
ATOM    586  C   TRP A  71      23.735  18.182 -27.625  1.00 32.35           C  
ANISOU  586  C   TRP A  71     4987   3508   3796   -277      1    208       C  
ATOM    587  O   TRP A  71      23.330  19.207 -28.167  1.00 31.60           O  
ANISOU  587  O   TRP A  71     4895   3389   3722   -265     41    215       O  
ATOM    588  CB  TRP A  71      26.183  17.647 -27.682  1.00 32.15           C  
ANISOU  588  CB  TRP A  71     4906   3553   3757   -358   -146    225       C  
ATOM    589  CG  TRP A  71      26.385  18.401 -28.980  1.00 30.14           C  
ANISOU  589  CG  TRP A  71     4586   3321   3543   -347   -137    243       C  
ATOM    590  CD1 TRP A  71      26.960  19.635 -29.133  1.00 30.29           C  
ANISOU  590  CD1 TRP A  71     4635   3317   3559   -387   -149    249       C  
ATOM    591  CD2 TRP A  71      26.013  17.968 -30.296  1.00 26.06           C  
ANISOU  591  CD2 TRP A  71     3974   2854   3074   -298   -115    256       C  
ATOM    592  NE1 TRP A  71      26.970  19.992 -30.462  1.00 30.48           N  
ANISOU  592  NE1 TRP A  71     4583   3372   3625   -362   -133    266       N  
ATOM    593  CE2 TRP A  71      26.393  18.989 -31.196  1.00 27.22           C  
ANISOU  593  CE2 TRP A  71     4098   3003   3242   -309   -114    271       C  
ATOM    594  CE3 TRP A  71      25.397  16.817 -30.803  1.00 27.54           C  
ANISOU  594  CE3 TRP A  71     4102   3078   3283   -250   -100    258       C  
ATOM    595  CZ2 TRP A  71      26.170  18.897 -32.573  1.00 27.61           C  
ANISOU  595  CZ2 TRP A  71     4072   3090   3329   -273    -96    287       C  
ATOM    596  CZ3 TRP A  71      25.179  16.724 -32.176  1.00 26.31           C  
ANISOU  596  CZ3 TRP A  71     3874   2959   3163   -218    -87    274       C  
ATOM    597  CH2 TRP A  71      25.566  17.758 -33.042  1.00 28.16           C  
ANISOU  597  CH2 TRP A  71     4091   3193   3413   -230    -85    288       C  
ATOM    598  N   ILE A  72      23.090  17.021 -27.678  1.00 33.32           N  
ANISOU  598  N   ILE A  72     5065   3660   3937   -236     15    208       N  
ATOM    599  CA  ILE A  72      21.802  16.875 -28.345  1.00 35.82           C  
ANISOU  599  CA  ILE A  72     5332   3977   4300   -177     76    219       C  
ATOM    600  C   ILE A  72      20.782  17.853 -27.749  1.00 38.20           C  
ANISOU  600  C   ILE A  72     5712   4200   4602   -161    159    216       C  
ATOM    601  O   ILE A  72      20.044  18.520 -28.481  1.00 37.72           O  
ANISOU  601  O   ILE A  72     5619   4127   4586   -129    203    235       O  
ATOM    602  CB  ILE A  72      21.292  15.423 -28.259  1.00 35.29           C  
ANISOU  602  CB  ILE A  72     5222   3943   4244   -146     74    218       C  
ATOM    603  CG1 ILE A  72      22.137  14.511 -29.162  1.00 35.90           C  
ANISOU  603  CG1 ILE A  72     5212   4095   4335   -149     10    228       C  
ATOM    604  CG2 ILE A  72      19.804  15.338 -28.622  1.00 37.14           C  
ANISOU  604  CG2 ILE A  72     5424   4160   4526    -93    140    234       C  
ATOM    605  CD1 ILE A  72      21.870  13.000 -28.970  1.00 38.66           C  
ANISOU  605  CD1 ILE A  72     5529   4475   4685   -128     -2    224       C  
ATOM    606  N   LYS A  73      20.767  17.944 -26.421  1.00 40.52           N  
ANISOU  606  N   LYS A  73     6114   4438   4844   -184    182    194       N  
ATOM    607  CA  LYS A  73      19.880  18.864 -25.713  1.00 43.78           C  
ANISOU  607  CA  LYS A  73     6621   4763   5249   -170    273    188       C  
ATOM    608  C   LYS A  73      20.187  20.329 -26.021  1.00 42.87           C  
ANISOU  608  C   LYS A  73     6547   4611   5132   -191    287    192       C  
ATOM    609  O   LYS A  73      19.270  21.132 -26.180  1.00 42.81           O  
ANISOU  609  O   LYS A  73     6554   4553   5159   -155    368    205       O  
ATOM    610  CB  LYS A  73      19.902  18.599 -24.206  1.00 45.35           C  
ANISOU  610  CB  LYS A  73     6945   4905   5380   -198    293    162       C  
ATOM    611  CG  LYS A  73      19.023  17.424 -23.790  1.00 54.76           C  
ANISOU  611  CG  LYS A  73     8116   6102   6587   -157    331    162       C  
ATOM    612  CD  LYS A  73      19.156  17.118 -22.301  1.00 61.67           C  
ANISOU  612  CD  LYS A  73     9125   6922   7386   -190    344    135       C  
ATOM    613  CE  LYS A  73      18.170  16.038 -21.859  1.00 65.21           C  
ANISOU  613  CE  LYS A  73     9559   7366   7854   -146    397    138       C  
ATOM    614  NZ  LYS A  73      16.763  16.543 -21.790  1.00 66.54           N  
ANISOU  614  NZ  LYS A  73     9739   7471   8073    -89    523    153       N  
ATOM    615  N   ARG A  74      21.468  20.673 -26.124  1.00 43.02           N  
ANISOU  615  N   ARG A  74     6577   4652   5116   -249    209    185       N  
ATOM    616  CA  ARG A  74      21.846  22.043 -26.482  1.00 44.84           C  
ANISOU  616  CA  ARG A  74     6841   4851   5344   -274    214    189       C  
ATOM    617  C   ARG A  74      21.445  22.396 -27.908  1.00 43.59           C  
ANISOU  617  C   ARG A  74     6576   4731   5257   -231    229    218       C  
ATOM    618  O   ARG A  74      21.071  23.536 -28.170  1.00 46.36           O  
ANISOU  618  O   ARG A  74     6955   5035   5624   -222    279    227       O  
ATOM    619  CB  ARG A  74      23.336  22.304 -26.257  1.00 45.42           C  
ANISOU  619  CB  ARG A  74     6945   4940   5371   -351    121    182       C  
ATOM    620  CG  ARG A  74      23.730  22.340 -24.791  1.00 48.81           C  
ANISOU  620  CG  ARG A  74     7514   5311   5721   -409    104    158       C  
ATOM    621  CD  ARG A  74      25.175  22.770 -24.610  1.00 52.98           C  
ANISOU  621  CD  ARG A  74     8070   5847   6212   -492      6    161       C  
ATOM    622  NE  ARG A  74      25.815  21.992 -23.551  1.00 57.57           N  
ANISOU  622  NE  ARG A  74     8707   6427   6738   -543    -63    153       N  
ATOM    623  CZ  ARG A  74      26.706  21.024 -23.754  1.00 56.65           C  
ANISOU  623  CZ  ARG A  74     8502   6383   6640   -560   -151    171       C  
ATOM    624  NH1 ARG A  74      27.103  20.709 -24.988  1.00 52.09           N  
ANISOU  624  NH1 ARG A  74     7780   5881   6129   -532   -177    194       N  
ATOM    625  NH2 ARG A  74      27.213  20.379 -22.713  1.00 58.12           N  
ANISOU  625  NH2 ARG A  74     8747   6559   6776   -607   -212    168       N  
ATOM    626  N   MET A  75      21.496  21.418 -28.816  1.00 41.95           N  
ANISOU  626  N   MET A  75     6251   4601   5087   -207    187    233       N  
ATOM    627  CA  MET A  75      21.133  21.646 -30.222  1.00 40.76           C  
ANISOU  627  CA  MET A  75     6004   4487   4995   -172    191    262       C  
ATOM    628  C   MET A  75      19.636  21.882 -30.377  1.00 43.21           C  
ANISOU  628  C   MET A  75     6302   4759   5357   -113    272    283       C  
ATOM    629  O   MET A  75      19.201  22.592 -31.293  1.00 43.72           O  
ANISOU  629  O   MET A  75     6325   4820   5466    -91    292    310       O  
ATOM    630  CB  MET A  75      21.593  20.492 -31.126  1.00 37.08           C  
ANISOU  630  CB  MET A  75     5436   4106   4546   -165    129    271       C  
ATOM    631  CG  MET A  75      23.107  20.409 -31.325  1.00 34.00           C  
ANISOU  631  CG  MET A  75     5030   3757   4131   -215     55    266       C  
ATOM    632  SD  MET A  75      23.861  21.839 -32.159  1.00 33.55           S  
ANISOU  632  SD  MET A  75     4972   3693   4083   -245     43    280       S  
ATOM    633  CE  MET A  75      23.648  21.393 -33.878  1.00 25.13           C  
ANISOU  633  CE  MET A  75     3795   2690   3064   -207     34    308       C  
ATOM    634  N   GLU A  76      18.857  21.272 -29.485  1.00 44.74           N  
ANISOU  634  N   GLU A  76     6527   4923   5548    -90    318    275       N  
ATOM    635  CA  GLU A  76      17.416  21.496 -29.428  1.00 46.92           C  
ANISOU  635  CA  GLU A  76     6794   5151   5881    -35    405    301       C  
ATOM    636  C   GLU A  76      17.144  22.921 -28.939  1.00 46.32           C  
ANISOU  636  C   GLU A  76     6809   4988   5801    -34    481    302       C  
ATOM    637  O   GLU A  76      16.386  23.657 -29.572  1.00 46.25           O  
ANISOU  637  O   GLU A  76     6764   4954   5853      3    528    336       O  
ATOM    638  CB  GLU A  76      16.737  20.455 -28.525  1.00 48.22           C  
ANISOU  638  CB  GLU A  76     6975   5303   6043    -13    439    293       C  
ATOM    639  CG  GLU A  76      15.205  20.527 -28.505  1.00 54.18           C  
ANISOU  639  CG  GLU A  76     7700   6014   6873     48    529    330       C  
ATOM    640  CD  GLU A  76      14.557  19.524 -27.542  1.00 59.52           C  
ANISOU  640  CD  GLU A  76     8398   6672   7547     67    571    323       C  
ATOM    641  OE1 GLU A  76      13.401  19.769 -27.122  1.00 60.50           O  
ANISOU  641  OE1 GLU A  76     8532   6733   7722    111    668    348       O  
ATOM    642  OE2 GLU A  76      15.191  18.495 -27.205  1.00 60.13           O  
ANISOU  642  OE2 GLU A  76     8479   6792   7574     40    512    295       O  
ATOM    643  N   ASP A  77      17.790  23.307 -27.835  1.00 46.02           N  
ANISOU  643  N   ASP A  77     6894   4901   5691    -77    489    265       N  
ATOM    644  CA  ASP A  77      17.658  24.655 -27.267  1.00 47.22           C  
ANISOU  644  CA  ASP A  77     7158   4960   5822    -86    561    258       C  
ATOM    645  C   ASP A  77      18.108  25.755 -28.229  1.00 46.75           C  
ANISOU  645  C   ASP A  77     7073   4909   5782    -99    538    274       C  
ATOM    646  O   ASP A  77      17.628  26.883 -28.138  1.00 47.48           O  
ANISOU  646  O   ASP A  77     7221   4928   5890    -83    614    285       O  
ATOM    647  CB  ASP A  77      18.445  24.796 -25.956  1.00 47.77           C  
ANISOU  647  CB  ASP A  77     7375   4981   5795   -148    551    215       C  
ATOM    648  CG  ASP A  77      17.975  23.843 -24.870  1.00 50.43           C  
ANISOU  648  CG  ASP A  77     7764   5294   6103   -138    585    198       C  
ATOM    649  OD1 ASP A  77      16.830  23.339 -24.945  1.00 51.42           O  
ANISOU  649  OD1 ASP A  77     7835   5414   6288    -76    652    220       O  
ATOM    650  OD2 ASP A  77      18.764  23.605 -23.929  1.00 50.87           O  
ANISOU  650  OD2 ASP A  77     7917   5335   6076   -195    542    166       O  
ATOM    651  N   ILE A  78      19.047  25.433 -29.120  1.00 44.84           N  
ANISOU  651  N   ILE A  78     6752   4748   5537   -129    441    276       N  
ATOM    652  CA  ILE A  78      19.498  26.384 -30.143  1.00 44.04           C  
ANISOU  652  CA  ILE A  78     6616   4661   5456   -141    416    293       C  
ATOM    653  C   ILE A  78      18.534  26.396 -31.331  1.00 43.18           C  
ANISOU  653  C   ILE A  78     6399   4577   5430    -82    438    338       C  
ATOM    654  O   ILE A  78      18.243  27.452 -31.880  1.00 44.22           O  
ANISOU  654  O   ILE A  78     6530   4677   5594    -67    472    362       O  
ATOM    655  CB  ILE A  78      20.953  26.115 -30.613  1.00 43.33           C  
ANISOU  655  CB  ILE A  78     6492   4641   5332   -198    312    281       C  
ATOM    656  CG1 ILE A  78      21.943  26.394 -29.475  1.00 43.81           C  
ANISOU  656  CG1 ILE A  78     6663   4665   5316   -267    281    248       C  
ATOM    657  CG2 ILE A  78      21.303  26.987 -31.821  1.00 43.79           C  
ANISOU  657  CG2 ILE A  78     6499   4718   5420   -202    293    305       C  
ATOM    658  CD1 ILE A  78      23.362  25.931 -29.737  1.00 40.82           C  
ANISOU  658  CD1 ILE A  78     6242   4353   4915   -322    177    244       C  
ATOM    659  N   GLY A  79      18.037  25.220 -31.707  1.00 42.45           N  
ANISOU  659  N   GLY A  79     6221   4540   5370    -52    416    352       N  
ATOM    660  CA  GLY A  79      17.103  25.087 -32.822  1.00 42.24           C  
ANISOU  660  CA  GLY A  79     6092   4538   5418     -5    421    400       C  
ATOM    661  C   GLY A  79      17.716  24.483 -34.071  1.00 41.66           C  
ANISOU  661  C   GLY A  79     5932   4551   5346    -20    334    409       C  
ATOM    662  O   GLY A  79      17.272  24.765 -35.182  1.00 43.33           O  
ANISOU  662  O   GLY A  79     6081   4779   5603      0    323    448       O  
ATOM    663  N   LEU A  80      18.727  23.639 -33.888  1.00 40.71           N  
ANISOU  663  N   LEU A  80     5812   4481   5176    -56    274    378       N  
ATOM    664  CA  LEU A  80      19.446  23.033 -35.007  1.00 39.61           C  
ANISOU  664  CA  LEU A  80     5603   4416   5031    -72    203    383       C  
ATOM    665  C   LEU A  80      19.450  21.515 -34.929  1.00 38.58           C  
ANISOU  665  C   LEU A  80     5431   4336   4891    -66    168    373       C  
ATOM    666  O   LEU A  80      19.461  20.945 -33.832  1.00 38.75           O  
ANISOU  666  O   LEU A  80     5492   4345   4889    -70    179    349       O  
ATOM    667  CB  LEU A  80      20.892  23.527 -35.035  1.00 38.67           C  
ANISOU  667  CB  LEU A  80     5513   4310   4868   -122    163    362       C  
ATOM    668  CG  LEU A  80      21.131  24.973 -35.462  1.00 37.82           C  
ANISOU  668  CG  LEU A  80     5434   4170   4768   -137    180    374       C  
ATOM    669  CD1 LEU A  80      22.492  25.424 -34.970  1.00 33.14           C  
ANISOU  669  CD1 LEU A  80     4891   3573   4129   -194    146    349       C  
ATOM    670  CD2 LEU A  80      21.016  25.098 -36.975  1.00 34.57           C  
ANISOU  670  CD2 LEU A  80     4951   3794   4388   -122    158    407       C  
ATOM    671  N   GLU A  81      19.474  20.870 -36.094  1.00 35.98           N  
ANISOU  671  N   GLU A  81     5035   4061   4576    -59    127    392       N  
ATOM    672  CA  GLU A  81      19.486  19.414 -36.166  1.00 35.57           C  
ANISOU  672  CA  GLU A  81     4947   4055   4515    -54     94    384       C  
ATOM    673  C   GLU A  81      20.790  18.798 -35.639  1.00 34.94           C  
ANISOU  673  C   GLU A  81     4883   4004   4387    -86     59    351       C  
ATOM    674  O   GLU A  81      21.890  19.223 -36.014  1.00 34.33           O  
ANISOU  674  O   GLU A  81     4807   3944   4294   -115     34    346       O  
ATOM    675  CB  GLU A  81      19.226  18.952 -37.598  1.00 35.92           C  
ANISOU  675  CB  GLU A  81     4931   4140   4576    -45     60    412       C  
ATOM    676  CG  GLU A  81      19.027  17.445 -37.738  1.00 38.28           C  
ANISOU  676  CG  GLU A  81     5199   4478   4868    -37     32    407       C  
ATOM    677  CD  GLU A  81      18.732  17.020 -39.163  1.00 38.64           C  
ANISOU  677  CD  GLU A  81     5205   4554   4921    -35     -3    435       C  
ATOM    678  OE1 GLU A  81      18.744  17.890 -40.058  1.00 39.84           O  
ANISOU  678  OE1 GLU A  81     5353   4701   5084    -41     -9    458       O  
ATOM    679  OE2 GLU A  81      18.486  15.813 -39.387  1.00 38.70           O  
ANISOU  679  OE2 GLU A  81     5194   4588   4921    -32    -26    435       O  
ATOM    680  N   ALA A  82      20.645  17.807 -34.758  1.00 33.00           N  
ANISOU  680  N   ALA A  82     4649   3763   4128    -81     59    333       N  
ATOM    681  CA  ALA A  82      21.758  17.006 -34.269  1.00 30.79           C  
ANISOU  681  CA  ALA A  82     4374   3512   3812   -106     21    310       C  
ATOM    682  C   ALA A  82      21.670  15.632 -34.924  1.00 30.47           C  
ANISOU  682  C   ALA A  82     4279   3520   3776    -89     -4    314       C  
ATOM    683  O   ALA A  82      20.808  14.823 -34.571  1.00 31.44           O  
ANISOU  683  O   ALA A  82     4398   3641   3908    -66      8    314       O  
ATOM    684  CB  ALA A  82      21.696  16.887 -32.753  1.00 30.21           C  
ANISOU  684  CB  ALA A  82     4364   3402   3712   -117     36    287       C  
ATOM    685  N   LEU A  83      22.555  15.377 -35.884  1.00 27.88           N  
ANISOU  685  N   LEU A  83     3916   3232   3444   -100    -33    321       N  
ATOM    686  CA  LEU A  83      22.463  14.180 -36.715  1.00 26.92           C  
ANISOU  686  CA  LEU A  83     3757   3149   3324    -84    -49    327       C  
ATOM    687  C   LEU A  83      23.268  13.011 -36.155  1.00 27.42           C  
ANISOU  687  C   LEU A  83     3813   3237   3368    -89    -69    311       C  
ATOM    688  O   LEU A  83      24.179  13.204 -35.341  1.00 27.40           O  
ANISOU  688  O   LEU A  83     3826   3231   3355   -112    -83    301       O  
ATOM    689  CB  LEU A  83      22.916  14.477 -38.146  1.00 24.92           C  
ANISOU  689  CB  LEU A  83     3478   2916   3072    -89    -58    344       C  
ATOM    690  CG  LEU A  83      22.146  15.520 -38.954  1.00 26.72           C  
ANISOU  690  CG  LEU A  83     3707   3125   3319    -84    -47    368       C  
ATOM    691  CD1 LEU A  83      22.757  16.905 -38.760  1.00 23.36           C  
ANISOU  691  CD1 LEU A  83     3302   2677   2897   -104    -36    368       C  
ATOM    692  CD2 LEU A  83      22.133  15.153 -40.429  1.00 23.96           C  
ANISOU  692  CD2 LEU A  83     3341   2799   2963    -83    -61    386       C  
ATOM    693  N   GLY A  84      22.918  11.800 -36.591  1.00 25.09           N  
ANISOU  693  N   GLY A  84     3498   2965   3071    -71    -75    311       N  
ATOM    694  CA  GLY A  84      23.694  10.609 -36.269  1.00 22.90           C  
ANISOU  694  CA  GLY A  84     3210   2712   2781    -71    -90    301       C  
ATOM    695  C   GLY A  84      22.966   9.687 -35.320  1.00 23.63           C  
ANISOU  695  C   GLY A  84     3315   2796   2866    -57    -89    288       C  
ATOM    696  O   GLY A  84      21.889  10.019 -34.817  1.00 23.50           O  
ANISOU  696  O   GLY A  84     3318   2754   2859    -49    -71    287       O  
ATOM    697  N   MET A  85      23.562   8.532 -35.061  1.00 23.54           N  
ANISOU  697  N   MET A  85     3294   2805   2844    -54   -102    281       N  
ATOM    698  CA  MET A  85      22.941   7.529 -34.203  1.00 24.07           C  
ANISOU  698  CA  MET A  85     3375   2867   2903    -41   -101    269       C  
ATOM    699  C   MET A  85      23.036   7.887 -32.721  1.00 25.14           C  
ANISOU  699  C   MET A  85     3548   2976   3027    -56   -103    256       C  
ATOM    700  O   MET A  85      24.090   7.772 -32.097  1.00 27.19           O  
ANISOU  700  O   MET A  85     3814   3242   3276    -74   -128    254       O  
ATOM    701  CB  MET A  85      23.521   6.140 -34.491  1.00 22.33           C  
ANISOU  701  CB  MET A  85     3135   2673   2675    -31   -112    267       C  
ATOM    702  CG  MET A  85      22.974   5.025 -33.602  1.00 23.70           C  
ANISOU  702  CG  MET A  85     3323   2842   2839    -19   -113    255       C  
ATOM    703  SD  MET A  85      21.178   4.933 -33.561  1.00 28.53           S  
ANISOU  703  SD  MET A  85     3946   3433   3460     -5    -92    256       S  
ATOM    704  CE  MET A  85      20.842   4.145 -35.137  1.00 23.35           C  
ANISOU  704  CE  MET A  85     3269   2799   2805      3   -100    269       C  
ATOM    705  N   ASP A  86      21.901   8.299 -32.173  1.00 28.39           N  
ANISOU  705  N   ASP A  86     3988   3356   3441    -48    -76    252       N  
ATOM    706  CA  ASP A  86      21.771   8.716 -30.781  1.00 29.94           C  
ANISOU  706  CA  ASP A  86     4242   3515   3620    -61    -64    239       C  
ATOM    707  C   ASP A  86      21.637   7.526 -29.813  1.00 30.64           C  
ANISOU  707  C   ASP A  86     4351   3602   3689    -55    -68    226       C  
ATOM    708  O   ASP A  86      21.792   7.688 -28.601  1.00 30.31           O  
ANISOU  708  O   ASP A  86     4366   3530   3619    -73    -68    214       O  
ATOM    709  CB  ASP A  86      20.569   9.655 -30.642  1.00 32.28           C  
ANISOU  709  CB  ASP A  86     4561   3769   3933    -48    -16    244       C  
ATOM    710  CG  ASP A  86      19.292   9.074 -31.257  1.00 37.99           C  
ANISOU  710  CG  ASP A  86     5246   4497   4691    -16      6    260       C  
ATOM    711  OD1 ASP A  86      18.280   8.977 -30.537  1.00 41.96           O  
ANISOU  711  OD1 ASP A  86     5769   4966   5206     -1     46    261       O  
ATOM    712  OD2 ASP A  86      19.291   8.715 -32.457  1.00 39.62           O  
ANISOU  712  OD2 ASP A  86     5405   4737   4912    -10    -15    274       O  
ATOM    713  N   ASP A  87      21.337   6.339 -30.341  1.00 29.68           N  
ANISOU  713  N   ASP A  87     4193   3508   3578    -34    -73    230       N  
ATOM    714  CA  ASP A  87      21.398   5.117 -29.532  1.00 28.61           C  
ANISOU  714  CA  ASP A  87     4071   3376   3424    -30    -83    220       C  
ATOM    715  C   ASP A  87      22.838   4.580 -29.602  1.00 28.28           C  
ANISOU  715  C   ASP A  87     4008   3363   3372    -43   -126    223       C  
ATOM    716  O   ASP A  87      23.212   3.833 -30.517  1.00 26.84           O  
ANISOU  716  O   ASP A  87     3783   3212   3202    -30   -135    231       O  
ATOM    717  CB  ASP A  87      20.354   4.084 -29.987  1.00 30.53           C  
ANISOU  717  CB  ASP A  87     4289   3628   3683     -4    -67    224       C  
ATOM    718  CG  ASP A  87      20.243   2.883 -29.031  1.00 33.26           C  
ANISOU  718  CG  ASP A  87     4658   3970   4010      1    -69    213       C  
ATOM    719  OD1 ASP A  87      21.163   2.651 -28.219  1.00 31.55           O  
ANISOU  719  OD1 ASP A  87     4465   3753   3768    -14    -93    205       O  
ATOM    720  OD2 ASP A  87      19.224   2.165 -29.095  1.00 35.83           O  
ANISOU  720  OD2 ASP A  87     4974   4291   4348     18    -50    216       O  
ATOM    721  N   PHE A  88      23.636   4.988 -28.620  1.00 26.49           N  
ANISOU  721  N   PHE A  88     3816   3122   3125    -72   -152    221       N  
ATOM    722  CA  PHE A  88      25.081   4.852 -28.674  1.00 27.19           C  
ANISOU  722  CA  PHE A  88     3878   3235   3220    -91   -198    236       C  
ATOM    723  C   PHE A  88      25.563   3.409 -28.715  1.00 28.70           C  
ANISOU  723  C   PHE A  88     4035   3450   3417    -74   -214    244       C  
ATOM    724  O   PHE A  88      26.622   3.133 -29.275  1.00 29.70           O  
ANISOU  724  O   PHE A  88     4115   3603   3568    -73   -233    264       O  
ATOM    725  CB  PHE A  88      25.741   5.622 -27.525  1.00 27.45           C  
ANISOU  725  CB  PHE A  88     3963   3240   3228   -135   -233    237       C  
ATOM    726  CG  PHE A  88      25.446   7.104 -27.542  1.00 26.48           C  
ANISOU  726  CG  PHE A  88     3876   3087   3097   -154   -215    231       C  
ATOM    727  CD1 PHE A  88      25.637   7.851 -28.698  1.00 25.09           C  
ANISOU  727  CD1 PHE A  88     3656   2927   2949   -150   -204    241       C  
ATOM    728  CD2 PHE A  88      24.978   7.744 -26.396  1.00 27.29           C  
ANISOU  728  CD2 PHE A  88     4067   3140   3162   -177   -204    215       C  
ATOM    729  CE1 PHE A  88      25.359   9.217 -28.724  1.00 25.42           C  
ANISOU  729  CE1 PHE A  88     3733   2940   2986   -166   -186    237       C  
ATOM    730  CE2 PHE A  88      24.701   9.104 -26.402  1.00 28.87           C  
ANISOU  730  CE2 PHE A  88     4307   3306   3355   -193   -179    210       C  
ATOM    731  CZ  PHE A  88      24.886   9.844 -27.574  1.00 29.50           C  
ANISOU  731  CZ  PHE A  88     4336   3406   3468   -187   -172    221       C  
ATOM    732  N   LYS A  89      24.787   2.492 -28.146  1.00 25.67           N  
ANISOU  732  N   LYS A  89     3678   3059   3018    -58   -201    231       N  
ATOM    733  CA  LYS A  89      25.153   1.086 -28.215  1.00 28.68           C  
ANISOU  733  CA  LYS A  89     4033   3461   3406    -38   -211    237       C  
ATOM    734  C   LYS A  89      24.996   0.453 -29.612  1.00 27.04           C  
ANISOU  734  C   LYS A  89     3779   3277   3219     -8   -185    241       C  
ATOM    735  O   LYS A  89      25.716  -0.487 -29.943  1.00 29.69           O  
ANISOU  735  O   LYS A  89     4085   3629   3566      6   -190    253       O  
ATOM    736  CB  LYS A  89      24.474   0.267 -27.112  1.00 29.17           C  
ANISOU  736  CB  LYS A  89     4140   3503   3442    -34   -208    224       C  
ATOM    737  CG  LYS A  89      22.982   0.123 -27.209  1.00 28.35           C  
ANISOU  737  CG  LYS A  89     4055   3383   3333    -15   -163    207       C  
ATOM    738  CD  LYS A  89      22.464  -0.266 -25.820  1.00 30.56           C  
ANISOU  738  CD  LYS A  89     4396   3632   3583    -22   -157    195       C  
ATOM    739  CE  LYS A  89      20.958  -0.386 -25.789  1.00 29.80           C  
ANISOU  739  CE  LYS A  89     4314   3515   3493     -3   -106    186       C  
ATOM    740  NZ  LYS A  89      20.316   0.934 -25.837  1.00 24.45           N  
ANISOU  740  NZ  LYS A  89     3654   2811   2824     -8    -73    184       N  
ATOM    741  N   LEU A  90      24.086   0.983 -30.426  1.00 25.13           N  
ANISOU  741  N   LEU A  90     3536   3032   2980     -1   -158    234       N  
ATOM    742  CA  LEU A  90      23.988   0.587 -31.835  1.00 26.51           C  
ANISOU  742  CA  LEU A  90     3682   3224   3165     16   -140    239       C  
ATOM    743  C   LEU A  90      25.184   1.099 -32.634  1.00 26.64           C  
ANISOU  743  C   LEU A  90     3667   3257   3199     11   -143    256       C  
ATOM    744  O   LEU A  90      25.676   0.415 -33.532  1.00 27.36           O  
ANISOU  744  O   LEU A  90     3739   3360   3297     27   -128    264       O  
ATOM    745  CB  LEU A  90      22.688   1.095 -32.479  1.00 25.47           C  
ANISOU  745  CB  LEU A  90     3558   3083   3035     18   -121    236       C  
ATOM    746  CG  LEU A  90      21.346   0.585 -31.946  1.00 27.93           C  
ANISOU  746  CG  LEU A  90     3890   3379   3345     26   -110    228       C  
ATOM    747  CD1 LEU A  90      20.202   1.131 -32.802  1.00 26.64           C  
ANISOU  747  CD1 LEU A  90     3717   3208   3198     26    -99    239       C  
ATOM    748  CD2 LEU A  90      21.290  -0.948 -31.869  1.00 26.53           C  
ANISOU  748  CD2 LEU A  90     3715   3207   3156     39   -112    223       C  
ATOM    749  N   ALA A  91      25.645   2.305 -32.309  1.00 26.43           N  
ANISOU  749  N   ALA A  91     3638   3224   3179    -11   -157    262       N  
ATOM    750  CA  ALA A  91      26.840   2.863 -32.939  1.00 23.83           C  
ANISOU  750  CA  ALA A  91     3274   2907   2872    -20   -161    282       C  
ATOM    751  C   ALA A  91      28.088   2.091 -32.510  1.00 23.47           C  
ANISOU  751  C   ALA A  91     3197   2873   2848    -17   -180    303       C  
ATOM    752  O   ALA A  91      28.982   1.841 -33.326  1.00 21.30           O  
ANISOU  752  O   ALA A  91     2882   2610   2600     -5   -164    325       O  
ATOM    753  CB  ALA A  91      26.973   4.349 -32.620  1.00 22.88           C  
ANISOU  753  CB  ALA A  91     3165   2774   2753    -49   -176    284       C  
ATOM    754  N   TYR A  92      28.141   1.700 -31.234  1.00 24.93           N  
ANISOU  754  N   TYR A  92     3400   3049   3022    -28   -213    302       N  
ATOM    755  CA  TYR A  92      29.232   0.852 -30.734  1.00 25.55           C  
ANISOU  755  CA  TYR A  92     3447   3135   3125    -26   -238    328       C  
ATOM    756  C   TYR A  92      29.291  -0.472 -31.498  1.00 26.32           C  
ANISOU  756  C   TYR A  92     3523   3243   3235     15   -201    332       C  
ATOM    757  O   TYR A  92      30.361  -0.890 -31.955  1.00 27.42           O  
ANISOU  757  O   TYR A  92     3615   3392   3414     30   -190    362       O  
ATOM    758  CB  TYR A  92      29.088   0.575 -29.229  1.00 27.00           C  
ANISOU  758  CB  TYR A  92     3670   3304   3285    -46   -281    323       C  
ATOM    759  CG  TYR A  92      30.063  -0.476 -28.715  1.00 29.68           C  
ANISOU  759  CG  TYR A  92     3976   3650   3649    -40   -310    354       C  
ATOM    760  CD1 TYR A  92      29.660  -1.800 -28.502  1.00 31.36           C  
ANISOU  760  CD1 TYR A  92     4200   3863   3852    -11   -295    346       C  
ATOM    761  CD2 TYR A  92      31.393  -0.148 -28.463  1.00 32.41           C  
ANISOU  761  CD2 TYR A  92     4277   4001   4036    -63   -354    398       C  
ATOM    762  CE1 TYR A  92      30.571  -2.768 -28.038  1.00 33.61           C  
ANISOU  762  CE1 TYR A  92     4452   4151   4166     -1   -321    379       C  
ATOM    763  CE2 TYR A  92      32.302  -1.101 -28.003  1.00 33.80           C  
ANISOU  763  CE2 TYR A  92     4414   4182   4248    -56   -384    436       C  
ATOM    764  CZ  TYR A  92      31.890  -2.401 -27.792  1.00 34.90           C  
ANISOU  764  CZ  TYR A  92     4566   4320   4376    -23   -366    427       C  
ATOM    765  OH  TYR A  92      32.812  -3.316 -27.334  1.00 36.12           O  
ANISOU  765  OH  TYR A  92     4678   4476   4569    -14   -394    470       O  
ATOM    766  N   LEU A  93      28.138  -1.127 -31.626  1.00 26.33           N  
ANISOU  766  N   LEU A  93     3561   3240   3205     32   -178    303       N  
ATOM    767  CA  LEU A  93      28.044  -2.407 -32.338  1.00 25.87           C  
ANISOU  767  CA  LEU A  93     3500   3184   3147     65   -143    302       C  
ATOM    768  C   LEU A  93      28.474  -2.278 -33.790  1.00 26.12           C  
ANISOU  768  C   LEU A  93     3513   3220   3192     80   -101    312       C  
ATOM    769  O   LEU A  93      29.155  -3.159 -34.327  1.00 26.24           O  
ANISOU  769  O   LEU A  93     3512   3233   3224    105    -68    327       O  
ATOM    770  CB  LEU A  93      26.626  -2.976 -32.262  1.00 24.39           C  
ANISOU  770  CB  LEU A  93     3357   2986   2923     71   -133    272       C  
ATOM    771  CG  LEU A  93      26.245  -3.754 -30.998  1.00 23.45           C  
ANISOU  771  CG  LEU A  93     3261   2859   2789     71   -154    264       C  
ATOM    772  CD1 LEU A  93      24.846  -4.326 -31.165  1.00 19.78           C  
ANISOU  772  CD1 LEU A  93     2831   2385   2299     78   -136    241       C  
ATOM    773  CD2 LEU A  93      27.239  -4.882 -30.701  1.00 21.55           C  
ANISOU  773  CD2 LEU A  93     2999   2621   2569     90   -157    285       C  
ATOM    774  N   SER A  94      28.086  -1.167 -34.409  1.00 26.75           N  
ANISOU  774  N   SER A  94     3600   3300   3263     64    -97    304       N  
ATOM    775  CA  SER A  94      28.429  -0.894 -35.795  1.00 27.56           C  
ANISOU  775  CA  SER A  94     3697   3404   3371     72    -58    313       C  
ATOM    776  C   SER A  94      29.940  -0.703 -35.969  1.00 27.92           C  
ANISOU  776  C   SER A  94     3690   3454   3463     77    -44    348       C  
ATOM    777  O   SER A  94      30.521  -1.218 -36.919  1.00 27.31           O  
ANISOU  777  O   SER A  94     3606   3371   3399    101      6    362       O  
ATOM    778  CB  SER A  94      27.679   0.338 -36.299  1.00 26.04           C  
ANISOU  778  CB  SER A  94     3523   3211   3162     51    -64    301       C  
ATOM    779  OG  SER A  94      27.910   0.511 -37.688  1.00 27.18           O  
ANISOU  779  OG  SER A  94     3675   3352   3301     56    -27    308       O  
ATOM    780  N   ASP A  95      30.559   0.039 -35.049  1.00 27.41           N  
ANISOU  780  N   ASP A  95     3593   3396   3426     54    -86    365       N  
ATOM    781  CA  ASP A  95      32.011   0.231 -35.033  1.00 26.87           C  
ANISOU  781  CA  ASP A  95     3463   3332   3415     53    -87    409       C  
ATOM    782  C   ASP A  95      32.793  -1.059 -34.743  1.00 29.08           C  
ANISOU  782  C   ASP A  95     3709   3610   3731     82    -74    437       C  
ATOM    783  O   ASP A  95      33.812  -1.339 -35.383  1.00 31.39           O  
ANISOU  783  O   ASP A  95     3955   3899   4073    105    -32    473       O  
ATOM    784  CB  ASP A  95      32.388   1.307 -34.011  1.00 25.03           C  
ANISOU  784  CB  ASP A  95     3213   3101   3195     11   -150    422       C  
ATOM    785  CG  ASP A  95      32.104   2.718 -34.515  1.00 27.04           C  
ANISOU  785  CG  ASP A  95     3482   3355   3436    -15   -149    411       C  
ATOM    786  OD1 ASP A  95      31.726   3.587 -33.696  1.00 23.14           O  
ANISOU  786  OD1 ASP A  95     3016   2855   2922    -49   -192    398       O  
ATOM    787  OD2 ASP A  95      32.257   2.953 -35.732  1.00 23.91           O  
ANISOU  787  OD2 ASP A  95     3077   2960   3048     -1   -101    416       O  
ATOM    788  N   THR A  96      32.314  -1.837 -33.779  1.00 27.60           N  
ANISOU  788  N   THR A  96     3543   3420   3522     84   -106    424       N  
ATOM    789  CA  THR A  96      33.032  -3.029 -33.331  1.00 27.63           C  
ANISOU  789  CA  THR A  96     3515   3421   3563    110   -103    454       C  
ATOM    790  C   THR A  96      32.889  -4.195 -34.324  1.00 27.43           C  
ANISOU  790  C   THR A  96     3509   3383   3531    155    -28    446       C  
ATOM    791  O   THR A  96      33.825  -4.959 -34.517  1.00 30.48           O  
ANISOU  791  O   THR A  96     3854   3761   3966    187      7    483       O  
ATOM    792  CB  THR A  96      32.606  -3.420 -31.893  1.00 26.75           C  
ANISOU  792  CB  THR A  96     3428   3309   3428     92   -166    444       C  
ATOM    793  OG1 THR A  96      32.574  -2.244 -31.078  1.00 25.28           O  
ANISOU  793  OG1 THR A  96     3251   3125   3230     45   -227    442       O  
ATOM    794  CG2 THR A  96      33.577  -4.409 -31.271  1.00 26.22           C  
ANISOU  794  CG2 THR A  96     3314   3238   3409    109   -182    489       C  
ATOM    795  N   TYR A  97      31.735  -4.298 -34.976  1.00 27.65           N  
ANISOU  795  N   TYR A  97     3600   3406   3500    157     -4    402       N  
ATOM    796  CA  TYR A  97      31.472  -5.373 -35.944  1.00 28.81           C  
ANISOU  796  CA  TYR A  97     3787   3534   3625    190     61    389       C  
ATOM    797  C   TYR A  97      31.204  -4.766 -37.321  1.00 30.28           C  
ANISOU  797  C   TYR A  97     4007   3713   3785    186    105    376       C  
ATOM    798  O   TYR A  97      30.083  -4.770 -37.824  1.00 31.22           O  
ANISOU  798  O   TYR A  97     4186   3828   3849    173    103    342       O  
ATOM    799  CB  TYR A  97      30.344  -6.300 -35.446  1.00 25.37           C  
ANISOU  799  CB  TYR A  97     3405   3093   3142    191     43    355       C  
ATOM    800  CG  TYR A  97      30.670  -6.828 -34.068  1.00 24.58           C  
ANISOU  800  CG  TYR A  97     3276   2998   3065    193     -1    371       C  
ATOM    801  CD1 TYR A  97      30.245  -6.152 -32.920  1.00 23.66           C  
ANISOU  801  CD1 TYR A  97     3160   2893   2937    160    -66    362       C  
ATOM    802  CD2 TYR A  97      31.483  -7.953 -33.910  1.00 26.28           C  
ANISOU  802  CD2 TYR A  97     3467   3201   3317    227     25    400       C  
ATOM    803  CE1 TYR A  97      30.604  -6.604 -31.641  1.00 22.48           C  
ANISOU  803  CE1 TYR A  97     2995   2744   2802    156   -111    379       C  
ATOM    804  CE2 TYR A  97      31.840  -8.415 -32.650  1.00 27.08           C  
ANISOU  804  CE2 TYR A  97     3542   3306   3442    226    -22    421       C  
ATOM    805  CZ  TYR A  97      31.401  -7.736 -31.520  1.00 25.21           C  
ANISOU  805  CZ  TYR A  97     3313   3082   3185    188    -93    410       C  
ATOM    806  OH  TYR A  97      31.755  -8.204 -30.281  1.00 23.13           O  
ANISOU  806  OH  TYR A  97     3035   2817   2935    182   -143    431       O  
ATOM    807  N   ASN A  98      32.267  -4.227 -37.909  1.00 31.94           N  
ANISOU  807  N   ASN A  98     4175   3921   4038    193    141    408       N  
ATOM    808  CA  ASN A  98      32.198  -3.532 -39.184  1.00 35.71           C  
ANISOU  808  CA  ASN A  98     4682   4390   4495    187    183    402       C  
ATOM    809  C   ASN A  98      32.293  -4.523 -40.341  1.00 36.60           C  
ANISOU  809  C   ASN A  98     4852   4471   4584    218    266    398       C  
ATOM    810  O   ASN A  98      33.028  -4.310 -41.305  1.00 39.00           O  
ANISOU  810  O   ASN A  98     5157   4758   4905    232    332    418       O  
ATOM    811  CB  ASN A  98      33.298  -2.465 -39.258  1.00 37.58           C  
ANISOU  811  CB  ASN A  98     4852   4637   4791    179    187    440       C  
ATOM    812  CG  ASN A  98      33.044  -1.427 -40.336  1.00 42.45           C  
ANISOU  812  CG  ASN A  98     5500   5251   5380    161    208    429       C  
ATOM    813  OD1 ASN A  98      31.977  -1.397 -40.961  1.00 46.87           O  
ANISOU  813  OD1 ASN A  98     6129   5804   5877    150    208    395       O  
ATOM    814  ND2 ASN A  98      34.032  -0.564 -40.563  1.00 42.91           N  
ANISOU  814  ND2 ASN A  98     5503   5312   5489    155    224    463       N  
ATOM    815  N   TYR A  99      31.543  -5.613 -40.214  1.00 35.82           N  
ANISOU  815  N   TYR A  99     4807   4360   4444    226    265    373       N  
ATOM    816  CA  TYR A  99      31.474  -6.679 -41.207  1.00 35.73           C  
ANISOU  816  CA  TYR A  99     4870   4312   4396    249    337    363       C  
ATOM    817  C   TYR A  99      30.141  -7.409 -41.038  1.00 35.92           C  
ANISOU  817  C   TYR A  99     4962   4331   4355    231    298    325       C  
ATOM    818  O   TYR A  99      29.419  -7.167 -40.059  1.00 34.02           O  
ANISOU  818  O   TYR A  99     4698   4116   4113    211    226    312       O  
ATOM    819  CB  TYR A  99      32.649  -7.663 -41.047  1.00 35.86           C  
ANISOU  819  CB  TYR A  99     4851   4307   4469    297    403    398       C  
ATOM    820  CG  TYR A  99      32.919  -8.146 -39.623  1.00 37.55           C  
ANISOU  820  CG  TYR A  99     4996   4539   4731    307    352    416       C  
ATOM    821  CD1 TYR A  99      33.852  -7.499 -38.813  1.00 36.79           C  
ANISOU  821  CD1 TYR A  99     4802   4467   4710    306    317    457       C  
ATOM    822  CD2 TYR A  99      32.253  -9.261 -39.095  1.00 38.50           C  
ANISOU  822  CD2 TYR A  99     5156   4652   4820    314    335    394       C  
ATOM    823  CE1 TYR A  99      34.114  -7.939 -37.515  1.00 35.73           C  
ANISOU  823  CE1 TYR A  99     4616   4347   4615    310    263    477       C  
ATOM    824  CE2 TYR A  99      32.509  -9.711 -37.798  1.00 34.65           C  
ANISOU  824  CE2 TYR A  99     4614   4179   4372    323    289    412       C  
ATOM    825  CZ  TYR A  99      33.441  -9.042 -37.016  1.00 37.53           C  
ANISOU  825  CZ  TYR A  99     4887   4566   4808    319    251    454       C  
ATOM    826  OH  TYR A  99      33.703  -9.466 -35.734  1.00 35.45           O  
ANISOU  826  OH  TYR A  99     4577   4314   4577    321    197    475       O  
ATOM    827  N   GLU A 100      29.814  -8.287 -41.985  1.00 35.20           N  
ANISOU  827  N   GLU A 100     4960   4203   4212    237    347    309       N  
ATOM    828  CA  GLU A 100      28.644  -9.153 -41.854  1.00 37.50           C  
ANISOU  828  CA  GLU A 100     5317   4484   4448    219    313    279       C  
ATOM    829  C   GLU A 100      28.899 -10.203 -40.772  1.00 35.90           C  
ANISOU  829  C   GLU A 100     5081   4283   4276    248    311    285       C  
ATOM    830  O   GLU A 100      29.852 -10.977 -40.866  1.00 37.86           O  
ANISOU  830  O   GLU A 100     5324   4507   4554    287    377    305       O  
ATOM    831  CB  GLU A 100      28.324  -9.846 -43.180  1.00 38.68           C  
ANISOU  831  CB  GLU A 100     5582   4587   4527    211    365    264       C  
ATOM    832  CG  GLU A 100      27.028 -10.653 -43.139  1.00 47.79           C  
ANISOU  832  CG  GLU A 100     6805   5729   5622    181    318    236       C  
ATOM    833  CD  GLU A 100      26.838 -11.553 -44.350  1.00 55.80           C  
ANISOU  833  CD  GLU A 100     7948   6688   6564    171    370    223       C  
ATOM    834  OE1 GLU A 100      25.807 -11.396 -45.046  1.00 59.40           O  
ANISOU  834  OE1 GLU A 100     8476   7133   6958    123    324    209       O  
ATOM    835  OE2 GLU A 100      27.713 -12.413 -44.605  1.00 58.85           O  
ANISOU  835  OE2 GLU A 100     8367   7038   6957    210    455    230       O  
ATOM    836  N   ILE A 101      28.043 -10.232 -39.757  1.00 33.90           N  
ANISOU  836  N   ILE A 101     4808   4053   4019    228    239    270       N  
ATOM    837  CA  ILE A 101      28.221 -11.144 -38.630  1.00 32.16           C  
ANISOU  837  CA  ILE A 101     4557   3835   3825    250    228    276       C  
ATOM    838  C   ILE A 101      27.916 -12.589 -38.996  1.00 33.44           C  
ANISOU  838  C   ILE A 101     4796   3961   3950    264    266    262       C  
ATOM    839  O   ILE A 101      26.820 -12.911 -39.461  1.00 32.93           O  
ANISOU  839  O   ILE A 101     4801   3883   3827    234    247    236       O  
ATOM    840  CB  ILE A 101      27.369 -10.727 -37.412  1.00 30.76           C  
ANISOU  840  CB  ILE A 101     4347   3689   3650    225    148    264       C  
ATOM    841  CG1 ILE A 101      27.891  -9.404 -36.844  1.00 31.86           C  
ANISOU  841  CG1 ILE A 101     4415   3859   3831    215    114    281       C  
ATOM    842  CG2 ILE A 101      27.370 -11.833 -36.340  1.00 29.99           C  
ANISOU  842  CG2 ILE A 101     4243   3588   3565    243    136    266       C  
ATOM    843  CD1 ILE A 101      26.970  -8.738 -35.878  1.00 30.13           C  
ANISOU  843  CD1 ILE A 101     4183   3661   3604    186     49    267       C  
ATOM    844  N   LYS A 102      28.914 -13.441 -38.796  1.00 35.06           N  
ANISOU  844  N   LYS A 102     4983   4146   4192    307    320    285       N  
ATOM    845  CA  LYS A 102      28.725 -14.876 -38.772  1.00 38.03           C  
ANISOU  845  CA  LYS A 102     5417   4487   4544    326    353    275       C  
ATOM    846  C   LYS A 102      28.739 -15.311 -37.319  1.00 36.60           C  
ANISOU  846  C   LYS A 102     5179   4328   4400    337    305    285       C  
ATOM    847  O   LYS A 102      29.748 -15.164 -36.629  1.00 38.21           O  
ANISOU  847  O   LYS A 102     5305   4545   4669    363    306    321       O  
ATOM    848  CB  LYS A 102      29.830 -15.588 -39.563  1.00 42.69           C  
ANISOU  848  CB  LYS A 102     6035   5033   5155    372    458    298       C  
ATOM    849  CG  LYS A 102      29.385 -16.132 -40.923  1.00 51.80           C  
ANISOU  849  CG  LYS A 102     7315   6135   6231    360    517    272       C  
ATOM    850  CD  LYS A 102      28.722 -15.066 -41.802  1.00 56.87           C  
ANISOU  850  CD  LYS A 102     7997   6789   6824    313    485    252       C  
ATOM    851  CE  LYS A 102      27.644 -15.686 -42.683  1.00 60.78           C  
ANISOU  851  CE  LYS A 102     8622   7246   7225    272    479    219       C  
ATOM    852  NZ  LYS A 102      26.717 -14.661 -43.242  1.00 63.47           N  
ANISOU  852  NZ  LYS A 102     8985   7607   7524    217    414    205       N  
ATOM    853  N   TYR A 103      27.605 -15.815 -36.847  1.00 34.13           N  
ANISOU  853  N   TYR A 103     4904   4016   4045    312    260    258       N  
ATOM    854  CA  TYR A 103      27.493 -16.249 -35.463  1.00 32.17           C  
ANISOU  854  CA  TYR A 103     4617   3785   3821    318    215    264       C  
ATOM    855  C   TYR A 103      27.423 -17.767 -35.399  1.00 31.81           C  
ANISOU  855  C   TYR A 103     4625   3704   3760    341    251    260       C  
ATOM    856  O   TYR A 103      27.063 -18.423 -36.381  1.00 31.43           O  
ANISOU  856  O   TYR A 103     4658   3619   3666    337    294    241       O  
ATOM    857  CB  TYR A 103      26.296 -15.583 -34.765  1.00 28.93           C  
ANISOU  857  CB  TYR A 103     4200   3403   3388    275    140    242       C  
ATOM    858  CG  TYR A 103      24.930 -16.101 -35.178  1.00 30.72           C  
ANISOU  858  CG  TYR A 103     4498   3615   3558    244    126    212       C  
ATOM    859  CD1 TYR A 103      24.264 -15.583 -36.299  1.00 28.23           C  
ANISOU  859  CD1 TYR A 103     4225   3294   3206    213    123    198       C  
ATOM    860  CD2 TYR A 103      24.295 -17.099 -34.438  1.00 28.42           C  
ANISOU  860  CD2 TYR A 103     4231   3314   3254    242    109    202       C  
ATOM    861  CE1 TYR A 103      22.997 -16.055 -36.672  1.00 27.56           C  
ANISOU  861  CE1 TYR A 103     4201   3195   3077    177     98    179       C  
ATOM    862  CE2 TYR A 103      23.038 -17.582 -34.806  1.00 28.80           C  
ANISOU  862  CE2 TYR A 103     4338   3347   3258    209     92    181       C  
ATOM    863  CZ  TYR A 103      22.396 -17.055 -35.915  1.00 29.19           C  
ANISOU  863  CZ  TYR A 103     4424   3391   3276    175     83    172       C  
ATOM    864  OH  TYR A 103      21.157 -17.538 -36.256  1.00 28.16           O  
ANISOU  864  OH  TYR A 103     4346   3245   3109    136     54    160       O  
ATOM    865  N   ASP A 104      27.796 -18.315 -34.248  1.00 30.49           N  
ANISOU  865  N   ASP A 104     4416   3542   3627    362    232    278       N  
ATOM    866  CA  ASP A 104      27.784 -19.756 -34.030  1.00 31.23           C  
ANISOU  866  CA  ASP A 104     4552   3602   3713    387    263    278       C  
ATOM    867  C   ASP A 104      26.889 -20.030 -32.831  1.00 30.03           C  
ANISOU  867  C   ASP A 104     4399   3466   3543    363    197    263       C  
ATOM    868  O   ASP A 104      27.317 -19.861 -31.690  1.00 31.85           O  
ANISOU  868  O   ASP A 104     4573   3717   3811    371    159    286       O  
ATOM    869  CB  ASP A 104      29.211 -20.254 -33.791  1.00 31.11           C  
ANISOU  869  CB  ASP A 104     4485   3570   3765    441    310    325       C  
ATOM    870  CG  ASP A 104      29.287 -21.753 -33.479  1.00 36.04           C  
ANISOU  870  CG  ASP A 104     5148   4157   4389    473    346    331       C  
ATOM    871  OD1 ASP A 104      28.242 -22.444 -33.389  1.00 37.68           O  
ANISOU  871  OD1 ASP A 104     5425   4352   4541    450    330    297       O  
ATOM    872  OD2 ASP A 104      30.425 -22.241 -33.320  1.00 35.19           O  
ANISOU  872  OD2 ASP A 104     4997   4030   4344    522    390    375       O  
ATOM    873  N   HIS A 105      25.652 -20.448 -33.100  1.00 29.70           N  
ANISOU  873  N   HIS A 105     4424   3412   3446    332    185    230       N  
ATOM    874  CA  HIS A 105      24.631 -20.642 -32.061  1.00 31.52           C  
ANISOU  874  CA  HIS A 105     4658   3656   3661    306    130    215       C  
ATOM    875  C   HIS A 105      25.054 -21.561 -30.914  1.00 30.81           C  
ANISOU  875  C   HIS A 105     4554   3558   3594    333    126    232       C  
ATOM    876  O   HIS A 105      24.558 -21.418 -29.803  1.00 30.49           O  
ANISOU  876  O   HIS A 105     4498   3535   3553    317     79    230       O  
ATOM    877  CB  HIS A 105      23.298 -21.118 -32.659  1.00 31.35           C  
ANISOU  877  CB  HIS A 105     4709   3616   3587    269    123    185       C  
ATOM    878  CG  HIS A 105      23.305 -22.541 -33.126  1.00 33.58           C  
ANISOU  878  CG  HIS A 105     5065   3853   3841    282    167    179       C  
ATOM    879  ND1 HIS A 105      22.837 -23.581 -32.350  1.00 35.17           N  
ANISOU  879  ND1 HIS A 105     5289   4039   4033    282    158    174       N  
ATOM    880  CD2 HIS A 105      23.698 -23.096 -34.298  1.00 36.83           C  
ANISOU  880  CD2 HIS A 105     5541   4226   4228    293    226    175       C  
ATOM    881  CE1 HIS A 105      22.955 -24.717 -33.019  1.00 39.12           C  
ANISOU  881  CE1 HIS A 105     5863   4494   4506    294    206    168       C  
ATOM    882  NE2 HIS A 105      23.473 -24.449 -34.205  1.00 37.30           N  
ANISOU  882  NE2 HIS A 105     5663   4246   4263    300    250    167       N  
ATOM    883  N   THR A 106      25.977 -22.483 -31.184  1.00 31.41           N  
ANISOU  883  N   THR A 106     4007   4305   3622    264    243    103       N  
ATOM    884  CA  THR A 106      26.447 -23.431 -30.166  1.00 32.33           C  
ANISOU  884  CA  THR A 106     4089   4415   3778    312    219     96       C  
ATOM    885  C   THR A 106      27.303 -22.753 -29.089  1.00 30.60           C  
ANISOU  885  C   THR A 106     3802   4222   3603    288    185    123       C  
ATOM    886  O   THR A 106      27.549 -23.335 -28.035  1.00 29.89           O  
ANISOU  886  O   THR A 106     3692   4121   3545    316    147    124       O  
ATOM    887  CB  THR A 106      27.220 -24.624 -30.787  1.00 32.40           C  
ANISOU  887  CB  THR A 106     4076   4440   3795    378    268     74       C  
ATOM    888  OG1 THR A 106      28.459 -24.161 -31.341  1.00 35.94           O  
ANISOU  888  OG1 THR A 106     4448   4948   4258    372    316     85       O  
ATOM    889  CG2 THR A 106      26.389 -25.293 -31.886  1.00 35.41           C  
ANISOU  889  CG2 THR A 106     4535   4793   4126    394    301     46       C  
ATOM    890  N   LYS A 107      27.740 -21.523 -29.359  1.00 30.24           N  
ANISOU  890  N   LYS A 107     3728   4207   3556    231    195    146       N  
ATOM    891  CA  LYS A 107      28.492 -20.722 -28.385  1.00 30.86           C  
ANISOU  891  CA  LYS A 107     3751   4308   3668    192    159    173       C  
ATOM    892  C   LYS A 107      27.593 -19.804 -27.557  1.00 29.80           C  
ANISOU  892  C   LYS A 107     3668   4132   3521    144    105    184       C  
ATOM    893  O   LYS A 107      28.037 -19.207 -26.569  1.00 30.91           O  
ANISOU  893  O   LYS A 107     3781   4278   3685    111     65    203       O  
ATOM    894  CB  LYS A 107      29.567 -19.884 -29.085  1.00 33.11           C  
ANISOU  894  CB  LYS A 107     3974   4650   3956    149    200    192       C  
ATOM    895  CG  LYS A 107      30.528 -20.677 -29.973  1.00 38.09           C  
ANISOU  895  CG  LYS A 107     4545   5332   4597    195    266    180       C  
ATOM    896  CD  LYS A 107      31.364 -21.654 -29.174  1.00 40.11           C  
ANISOU  896  CD  LYS A 107     4729   5608   4903    256    248    176       C  
ATOM    897  CE  LYS A 107      32.477 -22.250 -30.027  1.00 46.37           C  
ANISOU  897  CE  LYS A 107     5445   6460   5711    302    318    166       C  
ATOM    898  NZ  LYS A 107      33.438 -23.003 -29.174  1.00 49.38           N  
ANISOU  898  NZ  LYS A 107     5742   6870   6149    359    293    169       N  
ATOM    899  N   ILE A 108      26.335 -19.678 -27.969  1.00 28.12           N  
ANISOU  899  N   ILE A 108     3531   3881   3272    141    104    172       N  
ATOM    900  CA  ILE A 108      25.388 -18.791 -27.292  1.00 26.01           C  
ANISOU  900  CA  ILE A 108     3315   3576   2993    105     60    178       C  
ATOM    901  C   ILE A 108      24.600 -19.581 -26.254  1.00 25.52           C  
ANISOU  901  C   ILE A 108     3281   3478   2937    135     22    162       C  
ATOM    902  O   ILE A 108      23.952 -20.577 -26.576  1.00 26.34           O  
ANISOU  902  O   ILE A 108     3415   3567   3028    173     32    141       O  
ATOM    903  CB  ILE A 108      24.418 -18.110 -28.287  1.00 25.65           C  
ANISOU  903  CB  ILE A 108     3330   3510   2905     85     76    177       C  
ATOM    904  CG1 ILE A 108      25.206 -17.385 -29.377  1.00 24.24           C  
ANISOU  904  CG1 ILE A 108     3132   3364   2712     51    117    195       C  
ATOM    905  CG2 ILE A 108      23.481 -17.155 -27.546  1.00 27.17           C  
ANISOU  905  CG2 ILE A 108     3570   3664   3089     58     32    183       C  
ATOM    906  CD1 ILE A 108      24.373 -16.732 -30.450  1.00 24.98           C  
ANISOU  906  CD1 ILE A 108     3289   3440   2762     32    131    198       C  
ATOM    907  N   ARG A 109      24.661 -19.129 -25.006  1.00 25.46           N  
ANISOU  907  N   ARG A 109     3271   3458   2946    112    -23    172       N  
ATOM    908  CA  ARG A 109      23.981 -19.811 -23.919  1.00 21.81           C  
ANISOU  908  CA  ARG A 109     2837   2964   2486    132    -59    160       C  
ATOM    909  C   ARG A 109      22.515 -19.420 -23.878  1.00 21.19           C  
ANISOU  909  C   ARG A 109     2822   2851   2377    122    -68    147       C  
ATOM    910  O   ARG A 109      22.175 -18.303 -23.470  1.00 20.84           O  
ANISOU  910  O   ARG A 109     2799   2792   2326     88    -86    155       O  
ATOM    911  CB  ARG A 109      24.665 -19.508 -22.582  1.00 21.50           C  
ANISOU  911  CB  ARG A 109     2772   2925   2470    109   -103    175       C  
ATOM    912  CG  ARG A 109      24.174 -20.375 -21.415  1.00 21.12           C  
ANISOU  912  CG  ARG A 109     2752   2849   2423    130   -139    165       C  
ATOM    913  CD  ARG A 109      24.949 -20.083 -20.124  1.00 18.21           C  
ANISOU  913  CD  ARG A 109     2361   2484   2074    104   -186    182       C  
ATOM    914  NE  ARG A 109      26.384 -20.294 -20.305  1.00 23.84           N  
ANISOU  914  NE  ARG A 109     2999   3240   2821    114   -186    200       N  
ATOM    915  CZ  ARG A 109      27.003 -21.456 -20.097  1.00 28.71           C  
ANISOU  915  CZ  ARG A 109     3582   3867   3461    163   -195    201       C  
ATOM    916  NH1 ARG A 109      26.320 -22.521 -19.685  1.00 25.02           N  
ANISOU  916  NH1 ARG A 109     3160   3364   2982    199   -207    186       N  
ATOM    917  NH2 ARG A 109      28.310 -21.555 -20.303  1.00 27.29           N  
ANISOU  917  NH2 ARG A 109     3323   3733   3314    175   -192    217       N  
ATOM    918  N   VAL A 110      21.654 -20.345 -24.300  1.00 21.53           N  
ANISOU  918  N   VAL A 110     2894   2881   2403    153    -56    127       N  
ATOM    919  CA  VAL A 110      20.207 -20.144 -24.251  1.00 21.99           C  
ANISOU  919  CA  VAL A 110     3001   2916   2436    147    -65    113       C  
ATOM    920  C   VAL A 110      19.651 -20.902 -23.051  1.00 25.25           C  
ANISOU  920  C   VAL A 110     3434   3309   2851    154    -92    101       C  
ATOM    921  O   VAL A 110      19.858 -22.117 -22.911  1.00 25.12           O  
ANISOU  921  O   VAL A 110     3417   3288   2839    179    -92     93       O  
ATOM    922  CB  VAL A 110      19.483 -20.588 -25.563  1.00 21.24           C  
ANISOU  922  CB  VAL A 110     2930   2825   2315    164    -37    100       C  
ATOM    923  CG1 VAL A 110      17.994 -20.276 -25.490  1.00 18.74           C  
ANISOU  923  CG1 VAL A 110     2651   2492   1977    157    -52     89       C  
ATOM    924  CG2 VAL A 110      20.083 -19.893 -26.780  1.00 21.84           C  
ANISOU  924  CG2 VAL A 110     2995   2921   2383    154     -7    113       C  
ATOM    925  N   ALA A 111      18.962 -20.165 -22.184  1.00 24.06           N  
ANISOU  925  N   ALA A 111     3306   3143   2695    132   -114    100       N  
ATOM    926  CA  ALA A 111      18.385 -20.716 -20.974  1.00 23.53           C  
ANISOU  926  CA  ALA A 111     3260   3057   2622    129   -136     89       C  
ATOM    927  C   ALA A 111      16.861 -20.724 -21.037  1.00 23.61           C  
ANISOU  927  C   ALA A 111     3302   3061   2609    128   -131     71       C  
ATOM    928  O   ALA A 111      16.235 -19.714 -21.366  1.00 22.57           O  
ANISOU  928  O   ALA A 111     3177   2929   2469    122   -127     70       O  
ATOM    929  CB  ALA A 111      18.865 -19.939 -19.748  1.00 22.70           C  
ANISOU  929  CB  ALA A 111     3156   2942   2526    103   -164    100       C  
ATOM    930  N   ASN A 112      16.308 -21.899 -20.739  1.00 24.58           N  
ANISOU  930  N   ASN A 112     3442   3177   2721    134   -133     57       N  
ATOM    931  CA AASN A 112      14.871 -22.119 -20.637  0.50 24.82           C  
ANISOU  931  CA AASN A 112     3493   3208   2728    126   -129     39       C  
ATOM    932  CA BASN A 112      14.871 -22.122 -20.651  0.50 24.84           C  
ANISOU  932  CA BASN A 112     3495   3210   2731    126   -129     39       C  
ATOM    933  C   ASN A 112      14.571 -22.522 -19.214  1.00 24.64           C  
ANISOU  933  C   ASN A 112     3491   3172   2699    108   -145     33       C  
ATOM    934  O   ASN A 112      15.063 -23.546 -18.741  1.00 25.69           O  
ANISOU  934  O   ASN A 112     3637   3292   2832    109   -156     35       O  
ATOM    935  CB AASN A 112      14.421 -23.259 -21.556  0.50 25.56           C  
ANISOU  935  CB AASN A 112     3598   3306   2808    136   -116     28       C  
ATOM    936  CB BASN A 112      14.473 -23.252 -21.614  0.50 25.36           C  
ANISOU  936  CB BASN A 112     3572   3282   2784    137   -116     29       C  
ATOM    937  CG AASN A 112      14.283 -22.835 -22.992  0.50 25.79           C  
ANISOU  937  CG AASN A 112     3618   3351   2831    147   -100     30       C  
ATOM    938  CG BASN A 112      12.987 -23.269 -21.942  0.50 26.21           C  
ANISOU  938  CG BASN A 112     3688   3402   2869    125   -111     13       C  
ATOM    939  OD1AASN A 112      13.194 -22.886 -23.559  0.50 30.40           O  
ANISOU  939  OD1AASN A 112     4209   3946   3396    142    -97     19       O  
ATOM    940  OD1BASN A 112      12.129 -23.221 -21.059  0.50 23.68           O  
ANISOU  940  OD1BASN A 112     3373   3083   2539    108   -117      4       O  
ATOM    941  ND2AASN A 112      15.385 -22.426 -23.598  0.50 26.93           N  
ANISOU  941  ND2AASN A 112     3744   3499   2989    159    -90     44       N  
ATOM    942  ND2BASN A 112      12.678 -23.371 -23.230  0.50 29.38           N  
ANISOU  942  ND2BASN A 112     4089   3816   3259    133   -101     11       N  
ATOM    943  N   PHE A 113      13.781 -21.717 -18.516  1.00 24.47           N  
ANISOU  943  N   PHE A 113     3478   3151   2669     94   -146     24       N  
ATOM    944  CA  PHE A 113      13.457 -22.060 -17.139  1.00 26.20           C  
ANISOU  944  CA  PHE A 113     3722   3360   2874     71   -156     17       C  
ATOM    945  C   PHE A 113      11.999 -21.826 -16.772  1.00 26.65           C  
ANISOU  945  C   PHE A 113     3785   3430   2911     59   -140     -4       C  
ATOM    946  O   PHE A 113      11.297 -21.042 -17.417  1.00 26.74           O  
ANISOU  946  O   PHE A 113     3779   3457   2924     73   -128    -10       O  
ATOM    947  CB  PHE A 113      14.435 -21.395 -16.136  1.00 26.00           C  
ANISOU  947  CB  PHE A 113     3704   3318   2858     60   -177     30       C  
ATOM    948  CG  PHE A 113      14.035 -20.008 -15.682  1.00 24.90           C  
ANISOU  948  CG  PHE A 113     3572   3175   2714     52   -173     23       C  
ATOM    949  CD1 PHE A 113      13.872 -18.970 -16.594  1.00 29.45           C  
ANISOU  949  CD1 PHE A 113     4133   3756   3299     68   -162     25       C  
ATOM    950  CD2 PHE A 113      13.858 -19.739 -14.336  1.00 24.62           C  
ANISOU  950  CD2 PHE A 113     3567   3125   2661     29   -182     15       C  
ATOM    951  CE1 PHE A 113      13.518 -17.685 -16.159  1.00 31.07           C  
ANISOU  951  CE1 PHE A 113     4356   3949   3500     66   -160     18       C  
ATOM    952  CE2 PHE A 113      13.505 -18.464 -13.892  1.00 27.84           C  
ANISOU  952  CE2 PHE A 113     3992   3524   3062     25   -175      5       C  
ATOM    953  CZ  PHE A 113      13.339 -17.433 -14.810  1.00 25.39           C  
ANISOU  953  CZ  PHE A 113     3668   3216   2765     47   -165      6       C  
ATOM    954  N   ASP A 114      11.548 -22.539 -15.747  1.00 26.97           N  
ANISOU  954  N   ASP A 114     3850   3466   2930     34   -141    -12       N  
ATOM    955  CA  ASP A 114      10.279 -22.228 -15.102  1.00 28.55           C  
ANISOU  955  CA  ASP A 114     4054   3684   3111     18   -122    -33       C  
ATOM    956  C   ASP A 114      10.368 -22.498 -13.612  1.00 27.71           C  
ANISOU  956  C   ASP A 114     3984   3561   2982    -14   -128    -36       C  
ATOM    957  O   ASP A 114      11.182 -23.305 -13.162  1.00 29.46           O  
ANISOU  957  O   ASP A 114     4232   3760   3200    -27   -150    -22       O  
ATOM    958  CB  ASP A 114       9.105 -22.999 -15.717  1.00 28.14           C  
ANISOU  958  CB  ASP A 114     3986   3659   3045      8   -106    -46       C  
ATOM    959  CG  ASP A 114       7.767 -22.280 -15.512  1.00 38.81           C  
ANISOU  959  CG  ASP A 114     5313   5044   4389      9    -82    -66       C  
ATOM    960  OD1 ASP A 114       7.740 -21.157 -14.918  1.00 41.43           O  
ANISOU  960  OD1 ASP A 114     5646   5370   4725     23    -75    -73       O  
ATOM    961  OD2 ASP A 114       6.737 -22.836 -15.946  1.00 44.82           O  
ANISOU  961  OD2 ASP A 114     6054   5837   5140     -4    -71    -77       O  
ATOM    962  N   ILE A 115       9.528 -21.809 -12.852  1.00 28.20           N  
ANISOU  962  N   ILE A 115     4052   3635   3029    -24   -107    -54       N  
ATOM    963  CA  ILE A 115       9.519 -21.951 -11.410  1.00 27.65           C  
ANISOU  963  CA  ILE A 115     4024   3552   2930    -57   -107    -60       C  
ATOM    964  C   ILE A 115       8.152 -22.435 -10.930  1.00 27.34           C  
ANISOU  964  C   ILE A 115     3984   3542   2861    -85    -74    -82       C  
ATOM    965  O   ILE A 115       7.166 -22.355 -11.668  1.00 27.03           O  
ANISOU  965  O   ILE A 115     3904   3537   2829    -73    -52    -95       O  
ATOM    966  CB  ILE A 115       9.944 -20.636 -10.698  1.00 28.92           C  
ANISOU  966  CB  ILE A 115     4203   3694   3091    -51   -111    -64       C  
ATOM    967  CG1 ILE A 115       8.850 -19.562 -10.788  1.00 26.84           C  
ANISOU  967  CG1 ILE A 115     3920   3451   2827    -27    -76    -90       C  
ATOM    968  CG2 ILE A 115      11.291 -20.144 -11.241  1.00 26.71           C  
ANISOU  968  CG2 ILE A 115     3916   3392   2841    -32   -143    -40       C  
ATOM    969  CD1 ILE A 115       9.081 -18.359  -9.862  1.00 20.47           C  
ANISOU  969  CD1 ILE A 115     3150   2618   2008    -27    -73   -100       C  
ATOM    970  N   GLU A 116       8.123 -22.978  -9.718  1.00 24.34           N  
ANISOU  970  N   GLU A 116     3650   3151   2447   -127    -73    -85       N  
ATOM    971  CA  GLU A 116       6.888 -23.328  -9.044  1.00 25.05           C  
ANISOU  971  CA  GLU A 116     3745   3271   2503   -163    -36   -106       C  
ATOM    972  C   GLU A 116       6.803 -22.574  -7.727  1.00 27.01           C  
ANISOU  972  C   GLU A 116     4029   3510   2722   -178    -19   -121       C  
ATOM    973  O   GLU A 116       7.805 -22.420  -7.025  1.00 28.76           O  
ANISOU  973  O   GLU A 116     4298   3694   2935   -188    -49   -108       O  
ATOM    974  CB  GLU A 116       6.819 -24.830  -8.781  1.00 26.74           C  
ANISOU  974  CB  GLU A 116     3994   3477   2689   -212    -46    -95       C  
ATOM    975  CG  GLU A 116       6.867 -25.700 -10.033  1.00 31.54           C  
ANISOU  975  CG  GLU A 116     4579   4087   3317   -202    -62    -84       C  
ATOM    976  CD  GLU A 116       5.681 -25.481 -10.952  1.00 38.13           C  
ANISOU  976  CD  GLU A 116     5353   4972   4162   -193    -33   -101       C  
ATOM    977  OE1 GLU A 116       4.591 -25.117 -10.461  1.00 42.53           O  
ANISOU  977  OE1 GLU A 116     5887   5569   4703   -210      4   -123       O  
ATOM    978  OE2 GLU A 116       5.834 -25.670 -12.177  1.00 42.33           O  
ANISOU  978  OE2 GLU A 116     5858   5506   4719   -167    -46    -94       O  
ATOM    979  N   VAL A 117       5.605 -22.088  -7.413  1.00 27.86           N  
ANISOU  979  N   VAL A 117     4114   3656   2815   -179     29   -151       N  
ATOM    980  CA  VAL A 117       5.333 -21.369  -6.175  1.00 28.37           C  
ANISOU  980  CA  VAL A 117     4215   3718   2847   -192     58   -173       C  
ATOM    981  C   VAL A 117       3.991 -21.845  -5.615  1.00 28.30           C  
ANISOU  981  C   VAL A 117     4192   3758   2804   -229    112   -198       C  
ATOM    982  O   VAL A 117       2.947 -21.569  -6.201  1.00 29.09           O  
ANISOU  982  O   VAL A 117     4227   3906   2920   -205    146   -216       O  
ATOM    983  CB  VAL A 117       5.267 -19.830  -6.400  1.00 27.76           C  
ANISOU  983  CB  VAL A 117     4118   3636   2794   -135     71   -190       C  
ATOM    984  CG1 VAL A 117       5.107 -19.091  -5.069  1.00 24.74           C  
ANISOU  984  CG1 VAL A 117     3788   3240   2372   -148    100   -215       C  
ATOM    985  CG2 VAL A 117       6.499 -19.316  -7.157  1.00 27.21           C  
ANISOU  985  CG2 VAL A 117     4050   3526   2761   -102     23   -165       C  
ATOM    986  N   THR A 118       4.023 -22.559  -4.492  1.00 29.45           N  
ANISOU  986  N   THR A 118     4398   3893   2900   -290    118   -196       N  
ATOM    987  CA  THR A 118       2.798 -22.993  -3.805  1.00 32.13           C  
ANISOU  987  CA  THR A 118     4731   4280   3197   -338    174   -220       C  
ATOM    988  C   THR A 118       2.156 -21.791  -3.100  1.00 35.51           C  
ANISOU  988  C   THR A 118     5152   4730   3611   -312    229   -257       C  
ATOM    989  O   THR A 118       2.824 -21.075  -2.343  1.00 34.59           O  
ANISOU  989  O   THR A 118     5094   4572   3477   -305    220   -262       O  
ATOM    990  CB  THR A 118       3.091 -24.144  -2.801  1.00 32.65           C  
ANISOU  990  CB  THR A 118     4877   4322   3207   -417    162   -203       C  
ATOM    991  OG1 THR A 118       3.486 -25.319  -3.523  1.00 32.24           O  
ANISOU  991  OG1 THR A 118     4828   4252   3168   -435    119   -173       O  
ATOM    992  CG2 THR A 118       1.867 -24.472  -1.922  1.00 30.20           C  
ANISOU  992  CG2 THR A 118     4570   4061   2844   -476    228   -229       C  
ATOM    993  N   SER A 119       0.872 -21.562  -3.375  1.00 39.27           N  
ANISOU  993  N   SER A 119     5555   5270   4094   -296    284   -285       N  
ATOM    994  CA  SER A 119       0.134 -20.430  -2.800  1.00 44.34           C  
ANISOU  994  CA  SER A 119     6181   5938   4727   -259    343   -325       C  
ATOM    995  C   SER A 119      -1.312 -20.797  -2.435  1.00 47.48           C  
ANISOU  995  C   SER A 119     6523   6416   5100   -290    414   -354       C  
ATOM    996  O   SER A 119      -2.130 -21.057  -3.321  1.00 46.70           O  
ANISOU  996  O   SER A 119     6337   6374   5034   -276    424   -355       O  
ATOM    997  CB  SER A 119       0.150 -19.232  -3.754  1.00 44.41           C  
ANISOU  997  CB  SER A 119     6139   5942   4793   -167    332   -332       C  
ATOM    998  OG  SER A 119      -0.633 -18.165  -3.241  1.00 47.95           O  
ANISOU  998  OG  SER A 119     6572   6413   5235   -122    390   -373       O  
ATOM    999  N   PRO A 120      -1.627 -20.817  -1.123  1.00 51.07           N  
ANISOU  999  N   PRO A 120     7030   6879   5497   -335    465   -377       N  
ATOM   1000  CA  PRO A 120      -2.974 -21.143  -0.635  1.00 53.70           C  
ANISOU 1000  CA  PRO A 120     7312   7294   5799   -373    543   -406       C  
ATOM   1001  C   PRO A 120      -3.961 -19.971  -0.673  1.00 55.85           C  
ANISOU 1001  C   PRO A 120     7509   7618   6094   -295    607   -451       C  
ATOM   1002  O   PRO A 120      -5.164 -20.182  -0.495  1.00 58.23           O  
ANISOU 1002  O   PRO A 120     7739   8001   6384   -313    672   -475       O  
ATOM   1003  CB  PRO A 120      -2.721 -21.557   0.817  1.00 54.19           C  
ANISOU 1003  CB  PRO A 120     7476   7332   5783   -451    567   -411       C  
ATOM   1004  CG  PRO A 120      -1.537 -20.744   1.227  1.00 53.38           C  
ANISOU 1004  CG  PRO A 120     7459   7145   5676   -416    525   -406       C  
ATOM   1005  CD  PRO A 120      -0.671 -20.636  -0.011  1.00 52.22           C  
ANISOU 1005  CD  PRO A 120     7288   6959   5595   -365    448   -373       C  
ATOM   1006  N   ASP A 121      -3.459 -18.757  -0.896  1.00 56.12           N  
ANISOU 1006  N   ASP A 121     7559   7604   6159   -211    589   -460       N  
ATOM   1007  CA  ASP A 121      -4.291 -17.555  -0.855  1.00 57.68           C  
ANISOU 1007  CA  ASP A 121     7705   7835   6377   -126    647   -503       C  
ATOM   1008  C   ASP A 121      -4.326 -16.798  -2.180  1.00 57.33           C  
ANISOU 1008  C   ASP A 121     7591   7786   6404    -32    608   -495       C  
ATOM   1009  O   ASP A 121      -4.226 -15.569  -2.208  1.00 57.97           O  
ANISOU 1009  O   ASP A 121     7689   7834   6505     49    614   -515       O  
ATOM   1010  CB  ASP A 121      -3.852 -16.626   0.285  1.00 60.61           C  
ANISOU 1010  CB  ASP A 121     8174   8151   6705   -109    675   -533       C  
ATOM   1011  CG  ASP A 121      -2.367 -16.308   0.248  1.00 63.81           C  
ANISOU 1011  CG  ASP A 121     8676   8457   7113   -110    598   -503       C  
ATOM   1012  OD1 ASP A 121      -1.550 -17.251   0.329  1.00 66.41           O  
ANISOU 1012  OD1 ASP A 121     9052   8756   7424   -180    546   -466       O  
ATOM   1013  OD2 ASP A 121      -2.017 -15.112   0.152  1.00 66.47           O  
ANISOU 1013  OD2 ASP A 121     9042   8746   7468    -40    589   -517       O  
ATOM   1014  N   GLY A 122      -4.478 -17.540  -3.274  1.00 56.28           N  
ANISOU 1014  N   GLY A 122     7391   7686   6307    -45    568   -465       N  
ATOM   1015  CA  GLY A 122      -4.657 -16.944  -4.595  1.00 54.34           C  
ANISOU 1015  CA  GLY A 122     7073   7448   6125     36    533   -455       C  
ATOM   1016  C   GLY A 122      -3.392 -16.929  -5.426  1.00 52.48           C  
ANISOU 1016  C   GLY A 122     6886   7138   5915     45    452   -415       C  
ATOM   1017  O   GLY A 122      -2.395 -17.561  -5.068  1.00 51.99           O  
ANISOU 1017  O   GLY A 122     6900   7027   5829    -16    418   -391       O  
ATOM   1018  N   PHE A 123      -3.441 -16.204  -6.540  1.00 50.93           N  
ANISOU 1018  N   PHE A 123     6645   6936   5770    121    421   -407       N  
ATOM   1019  CA  PHE A 123      -2.303 -16.092  -7.449  1.00 49.32           C  
ANISOU 1019  CA  PHE A 123     6477   6669   5593    133    350   -370       C  
ATOM   1020  C   PHE A 123      -1.121 -15.401  -6.763  1.00 46.51           C  
ANISOU 1020  C   PHE A 123     6224   6228   5219    135    332   -368       C  
ATOM   1021  O   PHE A 123      -1.293 -14.334  -6.159  1.00 46.89           O  
ANISOU 1021  O   PHE A 123     6302   6255   5259    181    363   -397       O  
ATOM   1022  CB  PHE A 123      -2.698 -15.333  -8.718  1.00 50.36           C  
ANISOU 1022  CB  PHE A 123     6546   6813   5776    215    326   -363       C  
ATOM   1023  CG  PHE A 123      -1.595 -15.228  -9.728  1.00 51.08           C  
ANISOU 1023  CG  PHE A 123     6669   6847   5891    224    259   -326       C  
ATOM   1024  CD1 PHE A 123      -1.364 -16.261 -10.631  1.00 50.87           C  
ANISOU 1024  CD1 PHE A 123     6618   6838   5875    183    221   -296       C  
ATOM   1025  CD2 PHE A 123      -0.785 -14.094  -9.776  1.00 52.32           C  
ANISOU 1025  CD2 PHE A 123     6886   6933   6058    270    237   -322       C  
ATOM   1026  CE1 PHE A 123      -0.335 -16.171 -11.571  1.00 53.19           C  
ANISOU 1026  CE1 PHE A 123     6939   7082   6188    192    167   -263       C  
ATOM   1027  CE2 PHE A 123       0.243 -13.991 -10.707  1.00 52.52           C  
ANISOU 1027  CE2 PHE A 123     6939   6913   6104    272    182   -287       C  
ATOM   1028  CZ  PHE A 123       0.467 -15.032 -11.612  1.00 52.95           C  
ANISOU 1028  CZ  PHE A 123     6961   6989   6169    235    149   -258       C  
ATOM   1029  N   PRO A 124       0.074 -16.017  -6.844  1.00 42.45           N  
ANISOU 1029  N   PRO A 124     5764   5668   4698     85    283   -335       N  
ATOM   1030  CA  PRO A 124       1.284 -15.476  -6.228  1.00 41.91           C  
ANISOU 1030  CA  PRO A 124     5787   5524   4612     75    256   -327       C  
ATOM   1031  C   PRO A 124       1.814 -14.278  -7.008  1.00 41.32           C  
ANISOU 1031  C   PRO A 124     5722   5403   4573    139    224   -318       C  
ATOM   1032  O   PRO A 124       2.482 -14.450  -8.025  1.00 42.82           O  
ANISOU 1032  O   PRO A 124     5899   5578   4793    143    177   -286       O  
ATOM   1033  CB  PRO A 124       2.269 -16.647  -6.299  1.00 39.39           C  
ANISOU 1033  CB  PRO A 124     5496   5186   4284      9    210   -291       C  
ATOM   1034  CG  PRO A 124       1.822 -17.445  -7.470  1.00 39.33           C  
ANISOU 1034  CG  PRO A 124     5417   5222   4306     10    196   -273       C  
ATOM   1035  CD  PRO A 124       0.326 -17.306  -7.517  1.00 41.97           C  
ANISOU 1035  CD  PRO A 124     5680   5624   4643     35    248   -303       C  
ATOM   1036  N   GLU A 125       1.504 -13.077  -6.534  1.00 42.00           N  
ANISOU 1036  N   GLU A 125     5838   5467   4654    189    253   -348       N  
ATOM   1037  CA  GLU A 125       1.915 -11.847  -7.208  1.00 43.24           C  
ANISOU 1037  CA  GLU A 125     6015   5573   4839    250    225   -342       C  
ATOM   1038  C   GLU A 125       3.432 -11.647  -7.171  1.00 40.45           C  
ANISOU 1038  C   GLU A 125     5735   5153   4481    212    172   -312       C  
ATOM   1039  O   GLU A 125       4.020 -11.595  -6.094  1.00 41.05           O  
ANISOU 1039  O   GLU A 125     5881   5195   4521    169    172   -320       O  
ATOM   1040  CB  GLU A 125       1.185 -10.635  -6.611  1.00 46.46           C  
ANISOU 1040  CB  GLU A 125     6448   5966   5237    313    272   -384       C  
ATOM   1041  CG  GLU A 125      -0.169 -10.342  -7.260  1.00 52.31           C  
ANISOU 1041  CG  GLU A 125     7101   6763   6010    390    303   -403       C  
ATOM   1042  CD  GLU A 125      -0.042  -9.864  -8.704  1.00 59.31           C  
ANISOU 1042  CD  GLU A 125     7955   7636   6943    442    256   -374       C  
ATOM   1043  OE1 GLU A 125       0.934  -9.141  -9.020  1.00 62.85           O  
ANISOU 1043  OE1 GLU A 125     8469   8014   7397    448    215   -355       O  
ATOM   1044  OE2 GLU A 125      -0.921 -10.212  -9.525  1.00 60.22           O  
ANISOU 1044  OE2 GLU A 125     7982   7813   7087    473    257   -370       O  
ATOM   1045  N   PRO A 126       4.070 -11.552  -8.354  1.00 39.64           N  
ANISOU 1045  N   PRO A 126     5614   5034   4414    224    126   -278       N  
ATOM   1046  CA  PRO A 126       5.521 -11.346  -8.447  1.00 38.51           C  
ANISOU 1046  CA  PRO A 126     5524   4837   4272    188     76   -248       C  
ATOM   1047  C   PRO A 126       6.031 -10.130  -7.671  1.00 38.73           C  
ANISOU 1047  C   PRO A 126     5638   4801   4278    191     73   -263       C  
ATOM   1048  O   PRO A 126       7.077 -10.221  -7.028  1.00 39.53           O  
ANISOU 1048  O   PRO A 126     5792   4868   4358    136     45   -250       O  
ATOM   1049  CB  PRO A 126       5.751 -11.162  -9.946  1.00 37.99           C  
ANISOU 1049  CB  PRO A 126     5416   4771   4246    220     44   -219       C  
ATOM   1050  CG  PRO A 126       4.657 -11.948 -10.580  1.00 39.40           C  
ANISOU 1050  CG  PRO A 126     5515   5015   4440    241     64   -224       C  
ATOM   1051  CD  PRO A 126       3.464 -11.751  -9.687  1.00 39.04           C  
ANISOU 1051  CD  PRO A 126     5460   4997   4375    264    117   -265       C  
ATOM   1052  N   SER A 127       5.294  -9.021  -7.704  1.00 37.55           N  
ANISOU 1052  N   SER A 127     5504   4632   4132    254    100   -290       N  
ATOM   1053  CA  SER A 127       5.724  -7.791  -7.028  1.00 39.54           C  
ANISOU 1053  CA  SER A 127     5849   4814   4360    260     98   -307       C  
ATOM   1054  C   SER A 127       5.759  -7.911  -5.500  1.00 40.34           C  
ANISOU 1054  C   SER A 127     6013   4903   4410    217    124   -336       C  
ATOM   1055  O   SER A 127       6.469  -7.158  -4.836  1.00 42.22           O  
ANISOU 1055  O   SER A 127     6340   5082   4621    191    108   -342       O  
ATOM   1056  CB  SER A 127       4.862  -6.598  -7.451  1.00 39.79           C  
ANISOU 1056  CB  SER A 127     5889   4824   4408    348    121   -331       C  
ATOM   1057  OG  SER A 127       3.577  -6.673  -6.864  1.00 40.45           O  
ANISOU 1057  OG  SER A 127     5941   4947   4479    392    181   -373       O  
ATOM   1058  N   GLN A 128       4.995  -8.857  -4.952  1.00 40.42           N  
ANISOU 1058  N   GLN A 128     5982   4971   4403    203    164   -354       N  
ATOM   1059  CA  GLN A 128       4.995  -9.117  -3.512  1.00 40.58           C  
ANISOU 1059  CA  GLN A 128     6063   4986   4369    154    191   -379       C  
ATOM   1060  C   GLN A 128       5.938 -10.269  -3.139  1.00 37.57           C  
ANISOU 1060  C   GLN A 128     5691   4614   3971     69    150   -345       C  
ATOM   1061  O   GLN A 128       6.671 -10.178  -2.158  1.00 37.04           O  
ANISOU 1061  O   GLN A 128     5701   4510   3863     17    131   -346       O  
ATOM   1062  CB  GLN A 128       3.575  -9.406  -2.995  1.00 43.36           C  
ANISOU 1062  CB  GLN A 128     6375   5396   4704    183    266   -420       C  
ATOM   1063  CG  GLN A 128       2.519  -8.340  -3.330  1.00 49.62           C  
ANISOU 1063  CG  GLN A 128     7146   6190   5517    279    310   -456       C  
ATOM   1064  CD  GLN A 128       2.747  -6.999  -2.627  1.00 56.87           C  
ANISOU 1064  CD  GLN A 128     8170   7032   6406    307    322   -487       C  
ATOM   1065  OE1 GLN A 128       2.648  -5.936  -3.250  1.00 58.26           O  
ANISOU 1065  OE1 GLN A 128     8361   7168   6609    375    313   -492       O  
ATOM   1066  NE2 GLN A 128       3.041  -7.044  -1.324  1.00 57.22           N  
ANISOU 1066  NE2 GLN A 128     8295   7053   6391    252    341   -509       N  
ATOM   1067  N   ALA A 129       5.905 -11.345  -3.928  1.00 34.45           N  
ANISOU 1067  N   ALA A 129     5218   4264   3605     59    134   -317       N  
ATOM   1068  CA  ALA A 129       6.727 -12.546  -3.710  1.00 31.71           C  
ANISOU 1068  CA  ALA A 129     4873   3926   3249     -8     95   -284       C  
ATOM   1069  C   ALA A 129       6.794 -12.997  -2.245  1.00 33.22           C  
ANISOU 1069  C   ALA A 129     5130   4112   3380    -68    108   -298       C  
ATOM   1070  O   ALA A 129       7.879 -13.135  -1.671  1.00 34.32           O  
ANISOU 1070  O   ALA A 129     5326   4217   3499   -118     61   -277       O  
ATOM   1071  CB  ALA A 129       8.132 -12.360  -4.299  1.00 27.96           C  
ANISOU 1071  CB  ALA A 129     4410   3414   2800    -25     28   -244       C  
ATOM   1072  N   LYS A 130       5.628 -13.225  -1.647  1.00 34.10           N  
ANISOU 1072  N   LYS A 130     5234   4261   3463    -64    171   -332       N  
ATOM   1073  CA  LYS A 130       5.556 -13.551  -0.224  1.00 36.40           C  
ANISOU 1073  CA  LYS A 130     5595   4547   3688   -120    194   -350       C  
ATOM   1074  C   LYS A 130       5.574 -15.052   0.036  1.00 36.06           C  
ANISOU 1074  C   LYS A 130     5539   4537   3627   -181    183   -327       C  
ATOM   1075  O   LYS A 130       5.654 -15.485   1.183  1.00 36.66           O  
ANISOU 1075  O   LYS A 130     5679   4606   3645   -238    190   -332       O  
ATOM   1076  CB  LYS A 130       4.340 -12.888   0.442  1.00 37.87           C  
ANISOU 1076  CB  LYS A 130     5794   4753   3844    -88    275   -405       C  
ATOM   1077  CG  LYS A 130       2.992 -13.210  -0.189  1.00 44.22           C  
ANISOU 1077  CG  LYS A 130     6499   5628   4675    -44    332   -423       C  
ATOM   1078  CD  LYS A 130       1.863 -12.444   0.495  1.00 50.04           C  
ANISOU 1078  CD  LYS A 130     7244   6385   5385     -3    415   -479       C  
ATOM   1079  CE  LYS A 130       0.495 -12.881  -0.024  1.00 53.40           C  
ANISOU 1079  CE  LYS A 130     7559   6894   5835     31    471   -496       C  
ATOM   1080  NZ  LYS A 130      -0.628 -12.085   0.565  1.00 55.41           N  
ANISOU 1080  NZ  LYS A 130     7807   7176   6072     85    555   -552       N  
ATOM   1081  N   HIS A 131       5.515 -15.840  -1.033  1.00 34.81           N  
ANISOU 1081  N   HIS A 131     5305   4409   3512   -170    164   -301       N  
ATOM   1082  CA  HIS A 131       5.541 -17.292  -0.909  1.00 34.01           C  
ANISOU 1082  CA  HIS A 131     5196   4332   3397   -224    150   -277       C  
ATOM   1083  C   HIS A 131       6.865 -17.894  -1.382  1.00 32.49           C  
ANISOU 1083  C   HIS A 131     5010   4107   3229   -241     73   -230       C  
ATOM   1084  O   HIS A 131       7.492 -17.380  -2.311  1.00 32.09           O  
ANISOU 1084  O   HIS A 131     4927   4039   3225   -202     39   -214       O  
ATOM   1085  CB  HIS A 131       4.359 -17.914  -1.648  1.00 34.10           C  
ANISOU 1085  CB  HIS A 131     5123   4405   3429   -208    192   -286       C  
ATOM   1086  CG  HIS A 131       3.033 -17.381  -1.206  1.00 37.62           C  
ANISOU 1086  CG  HIS A 131     5545   4894   3854   -187    271   -332       C  
ATOM   1087  ND1 HIS A 131       2.308 -16.475  -1.951  1.00 38.13           N  
ANISOU 1087  ND1 HIS A 131     5546   4982   3958   -114    300   -354       N  
ATOM   1088  CD2 HIS A 131       2.314 -17.603  -0.082  1.00 38.67           C  
ANISOU 1088  CD2 HIS A 131     5710   5051   3931   -228    327   -360       C  
ATOM   1089  CE1 HIS A 131       1.192 -16.177  -1.313  1.00 36.30           C  
ANISOU 1089  CE1 HIS A 131     5301   4791   3700   -104    372   -395       C  
ATOM   1090  NE2 HIS A 131       1.173 -16.845  -0.174  1.00 39.82           N  
ANISOU 1090  NE2 HIS A 131     5803   5240   4087   -175    393   -401       N  
ATOM   1091  N   PRO A 132       7.309 -18.968  -0.713  1.00 31.35           N  
ANISOU 1091  N   PRO A 132     4909   3953   3051   -298     44   -208       N  
ATOM   1092  CA  PRO A 132       8.538 -19.660  -1.087  1.00 28.80           C  
ANISOU 1092  CA  PRO A 132     4590   3602   2751   -309    -28   -165       C  
ATOM   1093  C   PRO A 132       8.531 -20.193  -2.521  1.00 28.93           C  
ANISOU 1093  C   PRO A 132     4529   3640   2825   -273    -39   -147       C  
ATOM   1094  O   PRO A 132       7.505 -20.675  -3.006  1.00 28.87           O  
ANISOU 1094  O   PRO A 132     4477   3671   2822   -267      1   -159       O  
ATOM   1095  CB  PRO A 132       8.599 -20.822  -0.091  1.00 28.06           C  
ANISOU 1095  CB  PRO A 132     4556   3501   2605   -373    -41   -151       C  
ATOM   1096  CG  PRO A 132       7.872 -20.316   1.116  1.00 29.19           C  
ANISOU 1096  CG  PRO A 132     4755   3649   2686   -405     10   -185       C  
ATOM   1097  CD  PRO A 132       6.790 -19.420   0.598  1.00 31.95           C  
ANISOU 1097  CD  PRO A 132     5048   4035   3058   -356     77   -224       C  
ATOM   1098  N   ILE A 133       9.672 -20.077  -3.195  1.00 27.32           N  
ANISOU 1098  N   ILE A 133     4308   3413   2661   -250    -91   -118       N  
ATOM   1099  CA  ILE A 133       9.885 -20.769  -4.453  1.00 27.40           C  
ANISOU 1099  CA  ILE A 133     4259   3435   2715   -223   -108    -97       C  
ATOM   1100  C   ILE A 133      10.262 -22.209  -4.106  1.00 27.01           C  
ANISOU 1100  C   ILE A 133     4240   3374   2647   -259   -139    -73       C  
ATOM   1101  O   ILE A 133      11.266 -22.444  -3.429  1.00 26.82           O  
ANISOU 1101  O   ILE A 133     4261   3320   2610   -279   -187    -50       O  
ATOM   1102  CB  ILE A 133      11.017 -20.121  -5.269  1.00 26.55           C  
ANISOU 1102  CB  ILE A 133     4124   3310   2654   -189   -148    -76       C  
ATOM   1103  CG1 ILE A 133      10.633 -18.692  -5.665  1.00 26.13           C  
ANISOU 1103  CG1 ILE A 133     4052   3259   2617   -154   -121    -98       C  
ATOM   1104  CG2 ILE A 133      11.348 -20.984  -6.497  1.00 26.70           C  
ANISOU 1104  CG2 ILE A 133     4093   3340   2712   -164   -165    -55       C  
ATOM   1105  CD1 ILE A 133      11.768 -17.880  -6.219  1.00 22.83           C  
ANISOU 1105  CD1 ILE A 133     3624   2818   2232   -137   -158    -78       C  
ATOM   1106  N   ASP A 134       9.466 -23.170  -4.556  1.00 25.83           N  
ANISOU 1106  N   ASP A 134     4071   3248   2494   -267   -116    -76       N  
ATOM   1107  CA  ASP A 134       9.719 -24.562  -4.170  1.00 27.05           C  
ANISOU 1107  CA  ASP A 134     4269   3385   2625   -304   -143    -55       C  
ATOM   1108  C   ASP A 134      10.232 -25.470  -5.291  1.00 26.13           C  
ANISOU 1108  C   ASP A 134     4124   3260   2546   -276   -172    -33       C  
ATOM   1109  O   ASP A 134      10.399 -26.670  -5.093  1.00 28.96           O  
ANISOU 1109  O   ASP A 134     4521   3597   2886   -300   -194    -16       O  
ATOM   1110  CB  ASP A 134       8.504 -25.174  -3.448  1.00 28.49           C  
ANISOU 1110  CB  ASP A 134     4482   3589   2755   -357    -99    -73       C  
ATOM   1111  CG  ASP A 134       7.190 -24.928  -4.176  1.00 28.42           C  
ANISOU 1111  CG  ASP A 134     4409   3632   2759   -346    -41   -102       C  
ATOM   1112  OD1 ASP A 134       7.159 -25.017  -5.417  1.00 35.39           O  
ANISOU 1112  OD1 ASP A 134     5236   4528   3684   -309    -46    -98       O  
ATOM   1113  OD2 ASP A 134       6.177 -24.662  -3.498  1.00 28.71           O  
ANISOU 1113  OD2 ASP A 134     4450   3699   2761   -374     10   -128       O  
ATOM   1114  N   ALA A 135      10.479 -24.900  -6.464  1.00 24.56           N  
ANISOU 1114  N   ALA A 135     3864   3074   2395   -227   -171    -33       N  
ATOM   1115  CA  ALA A 135      11.045 -25.658  -7.582  1.00 23.90           C  
ANISOU 1115  CA  ALA A 135     3753   2982   2346   -196   -193    -15       C  
ATOM   1116  C   ALA A 135      11.510 -24.734  -8.685  1.00 24.07           C  
ANISOU 1116  C   ALA A 135     3716   3016   2415   -147   -193    -14       C  
ATOM   1117  O   ALA A 135      10.807 -23.795  -9.073  1.00 22.20           O  
ANISOU 1117  O   ALA A 135     3445   2803   2185   -133   -161    -33       O  
ATOM   1118  CB  ALA A 135      10.045 -26.671  -8.142  1.00 19.33           C  
ANISOU 1118  CB  ALA A 135     3171   2420   1754   -214   -168    -24       C  
ATOM   1119  N   ILE A 136      12.712 -25.000  -9.179  1.00 23.95           N  
ANISOU 1119  N   ILE A 136     3689   2982   2429   -119   -229      9       N  
ATOM   1120  CA  ILE A 136      13.187 -24.352 -10.390  1.00 22.53           C  
ANISOU 1120  CA  ILE A 136     3454   2815   2291    -77   -226     13       C  
ATOM   1121  C   ILE A 136      13.749 -25.430 -11.282  1.00 22.83           C  
ANISOU 1121  C   ILE A 136     3481   2844   2348    -52   -239     27       C  
ATOM   1122  O   ILE A 136      14.564 -26.237 -10.838  1.00 22.32           O  
ANISOU 1122  O   ILE A 136     3443   2755   2284    -50   -273     45       O  
ATOM   1123  CB  ILE A 136      14.276 -23.288 -10.100  1.00 22.19           C  
ANISOU 1123  CB  ILE A 136     3401   2763   2267    -69   -251     26       C  
ATOM   1124  CG1 ILE A 136      13.740 -22.224  -9.132  1.00 21.57           C  
ANISOU 1124  CG1 ILE A 136     3349   2684   2163    -94   -238     10       C  
ATOM   1125  CG2 ILE A 136      14.793 -22.658 -11.406  1.00 19.20           C  
ANISOU 1125  CG2 ILE A 136     2968   2398   1928    -33   -245     33       C  
ATOM   1126  CD1 ILE A 136      14.802 -21.290  -8.549  1.00 23.09           C  
ANISOU 1126  CD1 ILE A 136     3552   2860   2363   -104   -271     23       C  
ATOM   1127  N   THR A 137      13.282 -25.462 -12.527  1.00 22.13           N  
ANISOU 1127  N   THR A 137     3359   2775   2275    -30   -214     17       N  
ATOM   1128  CA  THR A 137      13.952 -26.223 -13.563  1.00 22.15           C  
ANISOU 1128  CA  THR A 137     3348   2770   2299      2   -221     27       C  
ATOM   1129  C   THR A 137      14.516 -25.242 -14.570  1.00 21.88           C  
ANISOU 1129  C   THR A 137     3263   2754   2296     34   -212     32       C  
ATOM   1130  O   THR A 137      13.791 -24.405 -15.107  1.00 19.81           O  
ANISOU 1130  O   THR A 137     2979   2514   2035     34   -189     20       O  
ATOM   1131  CB  THR A 137      13.025 -27.245 -14.238  1.00 21.89           C  
ANISOU 1131  CB  THR A 137     3331   2740   2248     -6   -202     14       C  
ATOM   1132  OG1 THR A 137      12.614 -28.203 -13.259  1.00 22.27           O  
ANISOU 1132  OG1 THR A 137     3433   2766   2263    -43   -213     14       O  
ATOM   1133  CG2 THR A 137      13.763 -27.974 -15.368  1.00 22.10           C  
ANISOU 1133  CG2 THR A 137     3349   2754   2293     32   -206     21       C  
ATOM   1134  N   HIS A 138      15.821 -25.358 -14.800  1.00 22.38           N  
ANISOU 1134  N   HIS A 138     3308   2810   2386     60   -232     50       N  
ATOM   1135  CA  HIS A 138      16.575 -24.442 -15.641  1.00 22.74           C  
ANISOU 1135  CA  HIS A 138     3307   2873   2460     81   -225     59       C  
ATOM   1136  C   HIS A 138      17.373 -25.285 -16.630  1.00 23.49           C  
ANISOU 1136  C   HIS A 138     3383   2969   2575    119   -221     66       C  
ATOM   1137  O   HIS A 138      18.319 -25.974 -16.238  1.00 24.95           O  
ANISOU 1137  O   HIS A 138     3567   3140   2772    136   -245     79       O  
ATOM   1138  CB  HIS A 138      17.492 -23.594 -14.745  1.00 21.48           C  
ANISOU 1138  CB  HIS A 138     3138   2711   2313     67   -254     75       C  
ATOM   1139  CG  HIS A 138      18.359 -22.614 -15.479  1.00 22.08           C  
ANISOU 1139  CG  HIS A 138     3169   2805   2416     77   -250     88       C  
ATOM   1140  ND1 HIS A 138      18.267 -21.250 -15.283  1.00 20.72           N  
ANISOU 1140  ND1 HIS A 138     2995   2635   2242     55   -249     88       N  
ATOM   1141  CD2 HIS A 138      19.357 -22.798 -16.378  1.00 20.90           C  
ANISOU 1141  CD2 HIS A 138     2977   2671   2293    104   -245    100       C  
ATOM   1142  CE1 HIS A 138      19.158 -20.637 -16.043  1.00 20.61           C  
ANISOU 1142  CE1 HIS A 138     2943   2637   2251     61   -245    102       C  
ATOM   1143  NE2 HIS A 138      19.839 -21.553 -16.711  1.00 22.44           N  
ANISOU 1143  NE2 HIS A 138     3145   2881   2501     89   -241    110       N  
ATOM   1144  N   TYR A 139      16.964 -25.260 -17.901  1.00 23.43           N  
ANISOU 1144  N   TYR A 139     3361   2974   2566    133   -191     56       N  
ATOM   1145  CA  TYR A 139      17.691 -25.960 -18.961  1.00 21.88           C  
ANISOU 1145  CA  TYR A 139     3150   2780   2384    170   -177     57       C  
ATOM   1146  C   TYR A 139      18.740 -25.028 -19.569  1.00 24.03           C  
ANISOU 1146  C   TYR A 139     3371   3077   2684    183   -168     72       C  
ATOM   1147  O   TYR A 139      18.462 -23.852 -19.849  1.00 23.23           O  
ANISOU 1147  O   TYR A 139     3254   2990   2581    165   -159     73       O  
ATOM   1148  CB  TYR A 139      16.740 -26.490 -20.046  1.00 19.85           C  
ANISOU 1148  CB  TYR A 139     2912   2524   2104    172   -151     39       C  
ATOM   1149  CG  TYR A 139      17.443 -27.047 -21.268  1.00 20.41           C  
ANISOU 1149  CG  TYR A 139     2973   2598   2183    209   -129     37       C  
ATOM   1150  CD1 TYR A 139      17.724 -26.238 -22.362  1.00 22.91           C  
ANISOU 1150  CD1 TYR A 139     3258   2941   2507    217   -104     39       C  
ATOM   1151  CD2 TYR A 139      17.836 -28.388 -21.325  1.00 23.40           C  
ANISOU 1151  CD2 TYR A 139     3381   2951   2561    237   -131     31       C  
ATOM   1152  CE1 TYR A 139      18.376 -26.740 -23.489  1.00 20.76           C  
ANISOU 1152  CE1 TYR A 139     2978   2673   2236    249    -77     35       C  
ATOM   1153  CE2 TYR A 139      18.484 -28.901 -22.443  1.00 23.23           C  
ANISOU 1153  CE2 TYR A 139     3353   2929   2543    276   -105     25       C  
ATOM   1154  CZ  TYR A 139      18.758 -28.068 -23.521  1.00 24.76           C  
ANISOU 1154  CZ  TYR A 139     3510   3154   2742    281    -76     26       C  
ATOM   1155  OH  TYR A 139      19.405 -28.565 -24.639  1.00 24.69           O  
ANISOU 1155  OH  TYR A 139     3498   3150   2733    317    -44     17       O  
ATOM   1156  N   ASP A 140      19.936 -25.574 -19.769  1.00 23.08           N  
ANISOU 1156  N   ASP A 140     3223   2959   2586    216   -171     82       N  
ATOM   1157  CA  ASP A 140      21.062 -24.866 -20.359  1.00 24.33           C  
ANISOU 1157  CA  ASP A 140     3325   3147   2770    226   -159     96       C  
ATOM   1158  C   ASP A 140      21.405 -25.512 -21.703  1.00 26.40           C  
ANISOU 1158  C   ASP A 140     3575   3420   3034    264   -121     87       C  
ATOM   1159  O   ASP A 140      21.636 -26.716 -21.765  1.00 25.51           O  
ANISOU 1159  O   ASP A 140     3479   3290   2923    301   -120     79       O  
ATOM   1160  CB  ASP A 140      22.261 -24.953 -19.418  1.00 24.05           C  
ANISOU 1160  CB  ASP A 140     3257   3117   2764    234   -194    116       C  
ATOM   1161  CG  ASP A 140      23.438 -24.146 -19.900  1.00 28.24           C  
ANISOU 1161  CG  ASP A 140     3721   3686   3322    233   -184    133       C  
ATOM   1162  OD1 ASP A 140      24.192 -24.647 -20.770  1.00 31.57           O  
ANISOU 1162  OD1 ASP A 140     4106   4128   3761    271   -156    133       O  
ATOM   1163  OD2 ASP A 140      23.625 -23.021 -19.386  1.00 30.97           O  
ANISOU 1163  OD2 ASP A 140     4053   4042   3672    192   -201    147       O  
ATOM   1164  N   SER A 141      21.447 -24.704 -22.762  1.00 26.20           N  
ANISOU 1164  N   SER A 141     3530   3420   3006    255    -89     87       N  
ATOM   1165  CA  SER A 141      21.638 -25.204 -24.126  1.00 28.58           C  
ANISOU 1165  CA  SER A 141     3830   3732   3299    284    -47     76       C  
ATOM   1166  C   SER A 141      23.071 -25.652 -24.405  1.00 29.33           C  
ANISOU 1166  C   SER A 141     3874   3848   3423    324    -30     82       C  
ATOM   1167  O   SER A 141      23.301 -26.522 -25.239  1.00 29.28           O  
ANISOU 1167  O   SER A 141     3876   3840   3411    363      2     67       O  
ATOM   1168  CB  SER A 141      21.236 -24.137 -25.145  1.00 28.38           C  
ANISOU 1168  CB  SER A 141     3803   3725   3255    257    -21     78       C  
ATOM   1169  OG  SER A 141      22.140 -23.042 -25.101  1.00 30.32           O  
ANISOU 1169  OG  SER A 141     4002   3998   3521    236    -19     99       O  
ATOM   1170  N   ILE A 142      24.029 -25.043 -23.714  1.00 28.92           N  
ANISOU 1170  N   ILE A 142     3768   3819   3402    314    -50    104       N  
ATOM   1171  CA  ILE A 142      25.432 -25.406 -23.867  1.00 29.66           C  
ANISOU 1171  CA  ILE A 142     3796   3943   3530    353    -38    113       C  
ATOM   1172  C   ILE A 142      25.751 -26.736 -23.159  1.00 31.37           C  
ANISOU 1172  C   ILE A 142     4024   4134   3763    406    -64    109       C  
ATOM   1173  O   ILE A 142      26.432 -27.596 -23.720  1.00 31.13           O  
ANISOU 1173  O   ILE A 142     3973   4109   3746    463    -38     99       O  
ATOM   1174  CB  ILE A 142      26.357 -24.260 -23.397  1.00 29.94           C  
ANISOU 1174  CB  ILE A 142     3766   4017   3592    315    -55    140       C  
ATOM   1175  CG1 ILE A 142      26.226 -23.072 -24.360  1.00 26.61           C  
ANISOU 1175  CG1 ILE A 142     3338   3620   3153    271    -20    145       C  
ATOM   1176  CG2 ILE A 142      27.822 -24.744 -23.261  1.00 28.83           C  
ANISOU 1176  CG2 ILE A 142     3546   3914   3494    356    -56    152       C  
ATOM   1177  CD1 ILE A 142      27.167 -21.920 -24.075  1.00 30.97           C  
ANISOU 1177  CD1 ILE A 142     3831   4209   3726    225    -31    171       C  
ATOM   1178  N   ASP A 143      25.246 -26.907 -21.940  1.00 30.22           N  
ANISOU 1178  N   ASP A 143     3914   3955   3612    388   -115    115       N  
ATOM   1179  CA  ASP A 143      25.419 -28.172 -21.226  1.00 32.55           C  
ANISOU 1179  CA  ASP A 143     4238   4216   3916    432   -146    113       C  
ATOM   1180  C   ASP A 143      24.463 -29.239 -21.742  1.00 31.60           C  
ANISOU 1180  C   ASP A 143     4194   4051   3762    452   -126     87       C  
ATOM   1181  O   ASP A 143      24.744 -30.432 -21.607  1.00 29.23           O  
ANISOU 1181  O   ASP A 143     3921   3719   3466    503   -135     81       O  
ATOM   1182  CB  ASP A 143      25.210 -27.988 -19.718  1.00 34.07           C  
ANISOU 1182  CB  ASP A 143     4451   4388   4107    399   -206    130       C  
ATOM   1183  CG  ASP A 143      26.253 -27.085 -19.088  1.00 37.53           C  
ANISOU 1183  CG  ASP A 143     4818   4864   4576    378   -236    157       C  
ATOM   1184  OD1 ASP A 143      27.319 -26.866 -19.710  1.00 39.40           O  
ANISOU 1184  OD1 ASP A 143     4981   5145   4844    402   -215    165       O  
ATOM   1185  OD2 ASP A 143      26.007 -26.598 -17.965  1.00 37.52           O  
ANISOU 1185  OD2 ASP A 143     4838   4853   4567    335   -280    169       O  
ATOM   1186  N   ASP A 144      23.344 -28.798 -22.335  1.00 30.34           N  
ANISOU 1186  N   ASP A 144     4071   3888   3568    412   -103     73       N  
ATOM   1187  CA  ASP A 144      22.254 -29.691 -22.760  1.00 28.39           C  
ANISOU 1187  CA  ASP A 144     3899   3602   3283    411    -91     49       C  
ATOM   1188  C   ASP A 144      21.740 -30.469 -21.545  1.00 27.04           C  
ANISOU 1188  C   ASP A 144     3784   3388   3101    401   -136     52       C  
ATOM   1189  O   ASP A 144      21.588 -31.691 -21.586  1.00 29.11           O  
ANISOU 1189  O   ASP A 144     4102   3610   3351    428   -139     40       O  
ATOM   1190  CB  ASP A 144      22.728 -30.630 -23.896  1.00 31.24           C  
ANISOU 1190  CB  ASP A 144     4272   3956   3643    467    -51     30       C  
ATOM   1191  CG  ASP A 144      21.592 -31.429 -24.535  1.00 31.87           C  
ANISOU 1191  CG  ASP A 144     4433   3999   3677    455    -37      5       C  
ATOM   1192  OD1 ASP A 144      20.432 -30.972 -24.512  1.00 33.77           O  
ANISOU 1192  OD1 ASP A 144     4700   4241   3891    401    -44      1       O  
ATOM   1193  OD2 ASP A 144      21.869 -32.521 -25.075  1.00 37.02           O  
ANISOU 1193  OD2 ASP A 144     5122   4622   4321    502    -18    -13       O  
ATOM   1194  N   ARG A 145      21.492 -29.750 -20.452  1.00 25.83           N  
ANISOU 1194  N   ARG A 145     3624   3241   2951    359   -169     67       N  
ATOM   1195  CA  ARG A 145      21.062 -30.371 -19.197  1.00 24.85           C  
ANISOU 1195  CA  ARG A 145     3552   3080   2812    341   -211     72       C  
ATOM   1196  C   ARG A 145      19.913 -29.598 -18.565  1.00 24.78           C  
ANISOU 1196  C   ARG A 145     3563   3075   2777    277   -219     70       C  
ATOM   1197  O   ARG A 145      19.854 -28.370 -18.675  1.00 23.01           O  
ANISOU 1197  O   ARG A 145     3299   2882   2560    253   -209     74       O  
ATOM   1198  CB  ARG A 145      22.223 -30.453 -18.201  1.00 25.69           C  
ANISOU 1198  CB  ARG A 145     3628   3184   2948    366   -254     97       C  
ATOM   1199  CG  ARG A 145      23.407 -31.340 -18.628  1.00 28.39           C  
ANISOU 1199  CG  ARG A 145     3946   3521   3321    441   -253    100       C  
ATOM   1200  CD  ARG A 145      23.048 -32.825 -18.618  1.00 27.45           C  
ANISOU 1200  CD  ARG A 145     3907   3343   3180    473   -260     88       C  
ATOM   1201  NE  ARG A 145      24.183 -33.687 -18.959  1.00 31.32           N  
ANISOU 1201  NE  ARG A 145     4378   3821   3700    555   -260     90       N  
ATOM   1202  CZ  ARG A 145      24.487 -34.081 -20.196  1.00 34.77           C  
ANISOU 1202  CZ  ARG A 145     4805   4264   4143    604   -212     69       C  
ATOM   1203  NH1 ARG A 145      23.751 -33.689 -21.233  1.00 30.72           N  
ANISOU 1203  NH1 ARG A 145     4301   3766   3605    573   -164     48       N  
ATOM   1204  NH2 ARG A 145      25.534 -34.871 -20.401  1.00 36.30           N  
ANISOU 1204  NH2 ARG A 145     4980   4447   4366    687   -211     70       N  
ATOM   1205  N   PHE A 146      19.000 -30.328 -17.925  1.00 22.37           N  
ANISOU 1205  N   PHE A 146     3322   2738   2441    250   -233     63       N  
ATOM   1206  CA  PHE A 146      17.961 -29.737 -17.082  1.00 23.85           C  
ANISOU 1206  CA  PHE A 146     3529   2930   2603    193   -241     60       C  
ATOM   1207  C   PHE A 146      18.453 -29.730 -15.633  1.00 24.57           C  
ANISOU 1207  C   PHE A 146     3635   3006   2697    180   -284     79       C  
ATOM   1208  O   PHE A 146      18.649 -30.791 -15.019  1.00 24.15           O  
ANISOU 1208  O   PHE A 146     3628   2915   2632    189   -311     87       O  
ATOM   1209  CB  PHE A 146      16.645 -30.533 -17.173  1.00 24.24           C  
ANISOU 1209  CB  PHE A 146     3636   2960   2613    160   -229     42       C  
ATOM   1210  CG  PHE A 146      16.052 -30.594 -18.563  1.00 25.93           C  
ANISOU 1210  CG  PHE A 146     3844   3189   2819    164   -194     24       C  
ATOM   1211  CD1 PHE A 146      16.543 -31.487 -19.507  1.00 23.25           C  
ANISOU 1211  CD1 PHE A 146     3522   2831   2482    204   -182     17       C  
ATOM   1212  CD2 PHE A 146      14.991 -29.766 -18.917  1.00 26.76           C  
ANISOU 1212  CD2 PHE A 146     3930   3327   2911    131   -175     13       C  
ATOM   1213  CE1 PHE A 146      16.006 -31.545 -20.789  1.00 25.69           C  
ANISOU 1213  CE1 PHE A 146     3833   3152   2776    203   -153     -1       C  
ATOM   1214  CE2 PHE A 146      14.440 -29.814 -20.199  1.00 26.32           C  
ANISOU 1214  CE2 PHE A 146     3871   3286   2845    133   -150     -1       C  
ATOM   1215  CZ  PHE A 146      14.947 -30.706 -21.135  1.00 26.54           C  
ANISOU 1215  CZ  PHE A 146     3921   3293   2870    165   -139     -8       C  
ATOM   1216  N   TYR A 147      18.665 -28.541 -15.087  1.00 23.12           N  
ANISOU 1216  N   TYR A 147     3418   2846   2523    158   -293     88       N  
ATOM   1217  CA  TYR A 147      19.052 -28.427 -13.692  1.00 24.29           C  
ANISOU 1217  CA  TYR A 147     3584   2980   2664    137   -335    105       C  
ATOM   1218  C   TYR A 147      17.811 -28.186 -12.847  1.00 24.98           C  
ANISOU 1218  C   TYR A 147     3719   3062   2711     82   -329     92       C  
ATOM   1219  O   TYR A 147      17.130 -27.161 -12.994  1.00 24.45           O  
ANISOU 1219  O   TYR A 147     3634   3019   2639     59   -303     79       O  
ATOM   1220  CB  TYR A 147      20.077 -27.312 -13.497  1.00 25.51           C  
ANISOU 1220  CB  TYR A 147     3684   3162   2849    139   -352    122       C  
ATOM   1221  CG  TYR A 147      21.382 -27.548 -14.233  1.00 27.87           C  
ANISOU 1221  CG  TYR A 147     3925   3476   3189    190   -357    135       C  
ATOM   1222  CD1 TYR A 147      21.589 -27.037 -15.522  1.00 28.35           C  
ANISOU 1222  CD1 TYR A 147     3936   3567   3270    209   -317    128       C  
ATOM   1223  CD2 TYR A 147      22.409 -28.278 -13.640  1.00 24.69           C  
ANISOU 1223  CD2 TYR A 147     3517   3060   2804    221   -401    156       C  
ATOM   1224  CE1 TYR A 147      22.795 -27.243 -16.198  1.00 28.53           C  
ANISOU 1224  CE1 TYR A 147     3901   3610   3330    255   -313    139       C  
ATOM   1225  CE2 TYR A 147      23.613 -28.488 -14.296  1.00 30.10           C  
ANISOU 1225  CE2 TYR A 147     4140   3766   3530    273   -402    168       C  
ATOM   1226  CZ  TYR A 147      23.801 -27.975 -15.573  1.00 32.78           C  
ANISOU 1226  CZ  TYR A 147     4427   4140   3889    289   -354    157       C  
ATOM   1227  OH  TYR A 147      24.995 -28.200 -16.206  1.00 31.57           O  
ANISOU 1227  OH  TYR A 147     4207   4013   3774    340   -347    167       O  
ATOM   1228  N   VAL A 148      17.523 -29.143 -11.968  1.00 24.28           N  
ANISOU 1228  N   VAL A 148     3691   2940   2593     63   -351     96       N  
ATOM   1229  CA  VAL A 148      16.320 -29.110 -11.143  1.00 22.09           C  
ANISOU 1229  CA  VAL A 148     3463   2660   2273      7   -339     84       C  
ATOM   1230  C   VAL A 148      16.695 -28.716  -9.709  1.00 23.36           C  
ANISOU 1230  C   VAL A 148     3651   2810   2416    -23   -375     98       C  
ATOM   1231  O   VAL A 148      17.565 -29.323  -9.088  1.00 21.44           O  
ANISOU 1231  O   VAL A 148     3432   2539   2173    -11   -421    121       O  
ATOM   1232  CB  VAL A 148      15.552 -30.467 -11.185  1.00 21.68           C  
ANISOU 1232  CB  VAL A 148     3470   2579   2187    -10   -333     77       C  
ATOM   1233  CG1 VAL A 148      14.203 -30.363 -10.465  1.00 20.56           C  
ANISOU 1233  CG1 VAL A 148     3364   2447   2001    -74   -310     61       C  
ATOM   1234  CG2 VAL A 148      15.331 -30.923 -12.631  1.00 20.04           C  
ANISOU 1234  CG2 VAL A 148     3242   2377   1995     20   -305     63       C  
ATOM   1235  N   PHE A 149      16.048 -27.674  -9.204  1.00 24.03           N  
ANISOU 1235  N   PHE A 149     3733   2914   2482    -59   -355     84       N  
ATOM   1236  CA  PHE A 149      16.264 -27.215  -7.839  1.00 24.71           C  
ANISOU 1236  CA  PHE A 149     3856   2990   2543    -95   -383     93       C  
ATOM   1237  C   PHE A 149      14.958 -27.467  -7.110  1.00 26.35           C  
ANISOU 1237  C   PHE A 149     4117   3196   2699   -145   -354     74       C  
ATOM   1238  O   PHE A 149      13.933 -26.884  -7.447  1.00 29.54           O  
ANISOU 1238  O   PHE A 149     4500   3626   3096   -157   -307     49       O  
ATOM   1239  CB  PHE A 149      16.632 -25.725  -7.816  1.00 25.07           C  
ANISOU 1239  CB  PHE A 149     3862   3057   2606    -96   -380     89       C  
ATOM   1240  CG  PHE A 149      17.935 -25.393  -8.530  1.00 24.01           C  
ANISOU 1240  CG  PHE A 149     3669   2932   2521    -56   -405    109       C  
ATOM   1241  CD1 PHE A 149      18.019 -25.421  -9.926  1.00 24.50           C  
ANISOU 1241  CD1 PHE A 149     3678   3013   2618    -17   -377    105       C  
ATOM   1242  CD2 PHE A 149      19.065 -25.026  -7.803  1.00 25.65           C  
ANISOU 1242  CD2 PHE A 149     3873   3135   2737    -64   -456    132       C  
ATOM   1243  CE1 PHE A 149      19.212 -25.099 -10.586  1.00 24.37           C  
ANISOU 1243  CE1 PHE A 149     3605   3012   2644     15   -393    122       C  
ATOM   1244  CE2 PHE A 149      20.271 -24.705  -8.453  1.00 25.01           C  
ANISOU 1244  CE2 PHE A 149     3727   3072   2702    -33   -476    151       C  
ATOM   1245  CZ  PHE A 149      20.339 -24.747  -9.846  1.00 27.78           C  
ANISOU 1245  CZ  PHE A 149     4025   3443   3087      6   -441    145       C  
ATOM   1246  N   ASP A 150      14.997 -28.345  -6.119  1.00 26.63           N  
ANISOU 1246  N   ASP A 150     4220   3201   2698   -176   -382     87       N  
ATOM   1247  CA  ASP A 150      13.788 -28.829  -5.467  1.00 27.81           C  
ANISOU 1247  CA  ASP A 150     4425   3349   2795   -230   -353     72       C  
ATOM   1248  C   ASP A 150      13.818 -28.546  -3.965  1.00 26.60           C  
ANISOU 1248  C   ASP A 150     4333   3182   2594   -279   -371     77       C  
ATOM   1249  O   ASP A 150      14.724 -28.994  -3.270  1.00 27.18           O  
ANISOU 1249  O   ASP A 150     4447   3222   2657   -280   -428    104       O  
ATOM   1250  CB  ASP A 150      13.645 -30.335  -5.729  1.00 26.45           C  
ANISOU 1250  CB  ASP A 150     4295   3146   2609   -233   -365     82       C  
ATOM   1251  CG  ASP A 150      12.376 -30.922  -5.143  1.00 33.41           C  
ANISOU 1251  CG  ASP A 150     5231   4028   3433   -299   -332     69       C  
ATOM   1252  OD1 ASP A 150      11.483 -30.155  -4.693  1.00 30.59           O  
ANISOU 1252  OD1 ASP A 150     4864   3706   3053   -335   -290     46       O  
ATOM   1253  OD2 ASP A 150      12.276 -32.172  -5.146  1.00 34.82           O  
ANISOU 1253  OD2 ASP A 150     5465   4173   3591   -315   -348     80       O  
ATOM   1254  N   LEU A 151      12.820 -27.808  -3.479  1.00 25.08           N  
ANISOU 1254  N   LEU A 151     4145   3015   2370   -315   -324     50       N  
ATOM   1255  CA  LEU A 151      12.706 -27.499  -2.058  1.00 25.84           C  
ANISOU 1255  CA  LEU A 151     4307   3101   2412   -366   -330     48       C  
ATOM   1256  C   LEU A 151      11.970 -28.605  -1.299  1.00 27.12           C  
ANISOU 1256  C   LEU A 151     4543   3248   2515   -424   -320     50       C  
ATOM   1257  O   LEU A 151      10.810 -28.904  -1.586  1.00 26.93           O  
ANISOU 1257  O   LEU A 151     4509   3250   2474   -448   -266     29       O  
ATOM   1258  CB  LEU A 151      11.999 -26.155  -1.856  1.00 24.91           C  
ANISOU 1258  CB  LEU A 151     4165   3015   2286   -373   -279     14       C  
ATOM   1259  CG  LEU A 151      11.842 -25.656  -0.419  1.00 23.28           C  
ANISOU 1259  CG  LEU A 151     4028   2799   2021   -423   -275      5       C  
ATOM   1260  CD1 LEU A 151      13.193 -25.643   0.275  1.00 23.19           C  
ANISOU 1260  CD1 LEU A 151     4057   2750   2003   -428   -351     37       C  
ATOM   1261  CD2 LEU A 151      11.208 -24.270  -0.386  1.00 25.11           C  
ANISOU 1261  CD2 LEU A 151     4232   3057   2252   -414   -222    -31       C  
ATOM   1262  N   LEU A 152      12.650 -29.199  -0.324  1.00 30.29           N  
ANISOU 1262  N   LEU A 152     5020   3609   2881   -450   -374     78       N  
ATOM   1263  CA  LEU A 152      12.074 -30.314   0.449  1.00 32.12           C  
ANISOU 1263  CA  LEU A 152     5338   3818   3050   -511   -373     87       C  
ATOM   1264  C   LEU A 152      11.289 -29.847   1.663  1.00 31.18           C  
ANISOU 1264  C   LEU A 152     5272   3712   2862   -579   -334     67       C  
ATOM   1265  O   LEU A 152      10.358 -30.523   2.103  1.00 28.08           O  
ANISOU 1265  O   LEU A 152     4928   3324   2417   -638   -299     60       O  
ATOM   1266  CB  LEU A 152      13.150 -31.317   0.885  1.00 31.39           C  
ANISOU 1266  CB  LEU A 152     5310   3668   2950   -504   -455    130       C  
ATOM   1267  CG  LEU A 152      13.888 -32.107  -0.198  1.00 32.17           C  
ANISOU 1267  CG  LEU A 152     5375   3744   3105   -438   -492    150       C  
ATOM   1268  CD1 LEU A 152      14.437 -33.382   0.424  1.00 36.34           C  
ANISOU 1268  CD1 LEU A 152     5995   4210   3601   -448   -556    187       C  
ATOM   1269  CD2 LEU A 152      12.993 -32.448  -1.383  1.00 33.36           C  
ANISOU 1269  CD2 LEU A 152     5479   3917   3278   -428   -435    127       C  
ATOM   1270  N   ASN A 153      11.679 -28.695   2.196  1.00 31.14           N  
ANISOU 1270  N   ASN A 153     5262   3715   2854   -574   -339     58       N  
ATOM   1271  CA  ASN A 153      11.086 -28.174   3.415  1.00 34.36           C  
ANISOU 1271  CA  ASN A 153     5730   4131   3193   -633   -305     38       C  
ATOM   1272  C   ASN A 153      10.584 -26.755   3.217  1.00 35.02           C  
ANISOU 1272  C   ASN A 153     5757   4253   3294   -611   -247     -3       C  
ATOM   1273  O   ASN A 153      11.328 -25.869   2.789  1.00 34.77           O  
ANISOU 1273  O   ASN A 153     5682   4219   3309   -564   -273     -2       O  
ATOM   1274  CB  ASN A 153      12.079 -28.248   4.580  1.00 35.93           C  
ANISOU 1274  CB  ASN A 153     6016   4286   3350   -662   -377     67       C  
ATOM   1275  CG  ASN A 153      12.585 -29.667   4.838  1.00 40.96           C  
ANISOU 1275  CG  ASN A 153     6719   4878   3967   -678   -441    110       C  
ATOM   1276  OD1 ASN A 153      11.832 -30.639   4.767  1.00 45.14           O  
ANISOU 1276  OD1 ASN A 153     7279   5404   4470   -711   -413    111       O  
ATOM   1277  ND2 ASN A 153      13.869 -29.785   5.137  1.00 44.71           N  
ANISOU 1277  ND2 ASN A 153     7216   5317   4455   -656   -529    147       N  
ATOM   1278  N   SER A 154       9.312 -26.555   3.543  1.00 35.61           N  
ANISOU 1278  N   SER A 154     5835   4365   3331   -645   -168    -38       N  
ATOM   1279  CA  SER A 154       8.622 -25.298   3.306  1.00 35.19           C  
ANISOU 1279  CA  SER A 154     5727   4350   3294   -617   -104    -81       C  
ATOM   1280  C   SER A 154       7.607 -25.096   4.419  1.00 35.39           C  
ANISOU 1280  C   SER A 154     5804   4397   3245   -674    -37   -113       C  
ATOM   1281  O   SER A 154       7.202 -26.065   5.053  1.00 36.37           O  
ANISOU 1281  O   SER A 154     5985   4520   3314   -737    -27   -104       O  
ATOM   1282  CB  SER A 154       7.913 -25.365   1.948  1.00 35.18           C  
ANISOU 1282  CB  SER A 154     5626   4389   3351   -572    -65    -94       C  
ATOM   1283  OG  SER A 154       6.843 -24.444   1.862  1.00 35.25           O  
ANISOU 1283  OG  SER A 154     5589   4445   3361   -557     10   -137       O  
ATOM   1284  N   PRO A 155       7.192 -23.840   4.669  1.00 37.69           N  
ANISOU 1284  N   PRO A 155     6081   4707   3531   -653     13   -152       N  
ATOM   1285  CA  PRO A 155       6.056 -23.627   5.575  1.00 38.80           C  
ANISOU 1285  CA  PRO A 155     6254   4882   3608   -697     95   -191       C  
ATOM   1286  C   PRO A 155       4.750 -24.247   5.062  1.00 39.84           C  
ANISOU 1286  C   PRO A 155     6320   5073   3745   -710    164   -208       C  
ATOM   1287  O   PRO A 155       3.813 -24.407   5.842  1.00 42.54           O  
ANISOU 1287  O   PRO A 155     6689   5448   4027   -761    231   -233       O  
ATOM   1288  CB  PRO A 155       5.936 -22.094   5.651  1.00 38.29           C  
ANISOU 1288  CB  PRO A 155     6173   4821   3555   -649    131   -230       C  
ATOM   1289  CG  PRO A 155       6.709 -21.579   4.468  1.00 37.71           C  
ANISOU 1289  CG  PRO A 155     6033   4732   3565   -578     81   -213       C  
ATOM   1290  CD  PRO A 155       7.822 -22.564   4.278  1.00 37.40           C  
ANISOU 1290  CD  PRO A 155     6015   4656   3540   -595     -6   -161       C  
ATOM   1291  N   TYR A 156       4.694 -24.607   3.779  1.00 39.44           N  
ANISOU 1291  N   TYR A 156     6187   5039   3761   -668    148   -195       N  
ATOM   1292  CA  TYR A 156       3.500 -25.246   3.207  1.00 40.62           C  
ANISOU 1292  CA  TYR A 156     6271   5245   3917   -686    203   -208       C  
ATOM   1293  C   TYR A 156       3.605 -26.766   3.060  1.00 41.30           C  
ANISOU 1293  C   TYR A 156     6390   5315   3986   -741    167   -172       C  
ATOM   1294  O   TYR A 156       2.715 -27.403   2.483  1.00 41.59           O  
ANISOU 1294  O   TYR A 156     6377   5395   4031   -763    200   -177       O  
ATOM   1295  CB  TYR A 156       3.087 -24.581   1.882  1.00 38.79           C  
ANISOU 1295  CB  TYR A 156     5925   5051   3762   -608    221   -224       C  
ATOM   1296  CG  TYR A 156       2.895 -23.085   2.015  1.00 40.54           C  
ANISOU 1296  CG  TYR A 156     6121   5284   3998   -551    258   -260       C  
ATOM   1297  CD1 TYR A 156       2.204 -22.544   3.106  1.00 42.90           C  
ANISOU 1297  CD1 TYR A 156     6454   5605   4242   -575    325   -297       C  
ATOM   1298  CD2 TYR A 156       3.413 -22.206   1.066  1.00 38.71           C  
ANISOU 1298  CD2 TYR A 156     5840   5037   3831   -473    228   -258       C  
ATOM   1299  CE1 TYR A 156       2.037 -21.166   3.247  1.00 44.13           C  
ANISOU 1299  CE1 TYR A 156     6598   5762   4408   -517    359   -333       C  
ATOM   1300  CE2 TYR A 156       3.242 -20.822   1.195  1.00 40.91           C  
ANISOU 1300  CE2 TYR A 156     6108   5316   4120   -420    259   -290       C  
ATOM   1301  CZ  TYR A 156       2.554 -20.315   2.288  1.00 43.25           C  
ANISOU 1301  CZ  TYR A 156     6442   5629   4363   -440    324   -328       C  
ATOM   1302  OH  TYR A 156       2.385 -18.961   2.431  1.00 46.80           O  
ANISOU 1302  OH  TYR A 156     6890   6071   4820   -384    355   -363       O  
ATOM   1303  N   GLY A 157       4.681 -27.342   3.596  1.00 41.03           N  
ANISOU 1303  N   GLY A 157     6444   5218   3928   -765     97   -135       N  
ATOM   1304  CA  GLY A 157       4.837 -28.797   3.630  1.00 40.90           C  
ANISOU 1304  CA  GLY A 157     6482   5172   3886   -818     59   -100       C  
ATOM   1305  C   GLY A 157       6.265 -29.298   3.499  1.00 40.19           C  
ANISOU 1305  C   GLY A 157     6440   5013   3818   -791    -38    -56       C  
ATOM   1306  O   GLY A 157       7.072 -28.737   2.749  1.00 40.43           O  
ANISOU 1306  O   GLY A 157     6420   5030   3912   -719    -77    -49       O  
ATOM   1307  N   ASN A 158       6.573 -30.348   4.253  1.00 39.09           N  
ANISOU 1307  N   ASN A 158     6400   4830   3624   -849    -77    -25       N  
ATOM   1308  CA  ASN A 158       7.827 -31.076   4.118  1.00 37.95           C  
ANISOU 1308  CA  ASN A 158     6301   4620   3498   -824   -170     20       C  
ATOM   1309  C   ASN A 158       7.600 -32.321   3.262  1.00 37.79           C  
ANISOU 1309  C   ASN A 158     6277   4586   3496   -828   -182     37       C  
ATOM   1310  O   ASN A 158       6.644 -33.075   3.490  1.00 37.39           O  
ANISOU 1310  O   ASN A 158     6260   4549   3397   -899   -142     32       O  
ATOM   1311  CB  ASN A 158       8.393 -31.459   5.493  1.00 38.30           C  
ANISOU 1311  CB  ASN A 158     6467   4615   3470   -878   -217     47       C  
ATOM   1312  CG  ASN A 158       8.715 -30.244   6.359  1.00 40.94           C  
ANISOU 1312  CG  ASN A 158     6818   4956   3781   -878   -213     31       C  
ATOM   1313  OD1 ASN A 158       9.121 -29.194   5.859  1.00 40.16           O  
ANISOU 1313  OD1 ASN A 158     6650   4872   3737   -816   -216     16       O  
ATOM   1314  ND2 ASN A 158       8.536 -30.387   7.669  1.00 41.86           N  
ANISOU 1314  ND2 ASN A 158     7036   5057   3811   -951   -208     34       N  
ATOM   1315  N   VAL A 159       8.479 -32.530   2.284  1.00 36.22           N  
ANISOU 1315  N   VAL A 159     6039   4360   3363   -757   -234     56       N  
ATOM   1316  CA  VAL A 159       8.293 -33.575   1.278  1.00 37.20           C  
ANISOU 1316  CA  VAL A 159     6152   4471   3512   -747   -242     66       C  
ATOM   1317  C   VAL A 159       9.514 -34.490   1.118  1.00 37.12           C  
ANISOU 1317  C   VAL A 159     6195   4388   3520   -708   -327    107       C  
ATOM   1318  O   VAL A 159      10.600 -34.180   1.603  1.00 36.49           O  
ANISOU 1318  O   VAL A 159     6135   4279   3449   -674   -384    128       O  
ATOM   1319  CB  VAL A 159       7.895 -32.969  -0.105  1.00 36.48           C  
ANISOU 1319  CB  VAL A 159     5942   4430   3490   -691   -203     39       C  
ATOM   1320  CG1 VAL A 159       6.554 -32.259  -0.015  1.00 38.69           C  
ANISOU 1320  CG1 VAL A 159     6166   4781   3751   -727   -121      0       C  
ATOM   1321  CG2 VAL A 159       8.956 -32.015  -0.621  1.00 37.68           C  
ANISOU 1321  CG2 VAL A 159     6032   4578   3705   -606   -236     42       C  
ATOM   1322  N   GLU A 160       9.315 -35.618   0.439  1.00 37.77           N  
ANISOU 1322  N   GLU A 160     6301   4444   3606   -713   -336    117       N  
ATOM   1323  CA  GLU A 160      10.404 -36.526   0.080  1.00 37.87           C  
ANISOU 1323  CA  GLU A 160     6357   4389   3645   -660   -408    150       C  
ATOM   1324  C   GLU A 160      11.071 -36.107  -1.239  1.00 35.47           C  
ANISOU 1324  C   GLU A 160     5954   4098   3424   -564   -417    143       C  
ATOM   1325  O   GLU A 160      10.505 -35.329  -2.013  1.00 33.59           O  
ANISOU 1325  O   GLU A 160     5627   3917   3219   -549   -365    113       O  
ATOM   1326  CB  GLU A 160       9.889 -37.969  -0.011  1.00 39.91           C  
ANISOU 1326  CB  GLU A 160     6703   4602   3861   -712   -414    163       C  
ATOM   1327  CG  GLU A 160       9.409 -38.543   1.330  1.00 49.92           C  
ANISOU 1327  CG  GLU A 160     8086   5843   5040   -809   -416    179       C  
ATOM   1328  CD  GLU A 160      10.527 -38.640   2.362  1.00 55.72           C  
ANISOU 1328  CD  GLU A 160     8897   6521   5753   -791   -492    216       C  
ATOM   1329  OE1 GLU A 160      11.450 -39.461   2.166  1.00 59.95           O  
ANISOU 1329  OE1 GLU A 160     9482   6990   6307   -740   -562    247       O  
ATOM   1330  OE2 GLU A 160      10.485 -37.896   3.369  1.00 57.83           O  
ANISOU 1330  OE2 GLU A 160     9177   6812   5984   -826   -484    213       O  
ATOM   1331  N   GLU A 161      12.273 -36.623  -1.488  1.00 34.49           N  
ANISOU 1331  N   GLU A 161     5848   3923   3334   -498   -482    171       N  
ATOM   1332  CA  GLU A 161      12.990 -36.330  -2.723  1.00 33.69           C  
ANISOU 1332  CA  GLU A 161     5660   3833   3307   -409   -489    166       C  
ATOM   1333  C   GLU A 161      12.216 -36.849  -3.921  1.00 32.97           C  
ANISOU 1333  C   GLU A 161     5546   3752   3228   -410   -446    144       C  
ATOM   1334  O   GLU A 161      11.493 -37.843  -3.835  1.00 30.68           O  
ANISOU 1334  O   GLU A 161     5328   3435   2895   -465   -437    145       O  
ATOM   1335  CB  GLU A 161      14.389 -36.952  -2.715  1.00 35.61           C  
ANISOU 1335  CB  GLU A 161     5931   4020   3580   -338   -564    200       C  
ATOM   1336  CG  GLU A 161      15.434 -36.172  -1.915  1.00 36.01           C  
ANISOU 1336  CG  GLU A 161     5961   4076   3644   -313   -613    220       C  
ATOM   1337  CD  GLU A 161      16.819 -36.807  -1.953  1.00 40.83           C  
ANISOU 1337  CD  GLU A 161     6584   4640   4290   -237   -690    255       C  
ATOM   1338  OE1 GLU A 161      17.177 -37.452  -2.966  1.00 41.10           O  
ANISOU 1338  OE1 GLU A 161     6597   4653   4364   -174   -692    254       O  
ATOM   1339  OE2 GLU A 161      17.565 -36.650  -0.961  1.00 47.35           O  
ANISOU 1339  OE2 GLU A 161     7438   5450   5103   -239   -749    283       O  
ATOM   1340  N   TRP A 162      12.362 -36.146  -5.036  1.00 32.17           N  
ANISOU 1340  N   TRP A 162     5348   3690   3183   -354   -421    126       N  
ATOM   1341  CA  TRP A 162      11.826 -36.590  -6.305  1.00 31.00           C  
ANISOU 1341  CA  TRP A 162     5175   3551   3053   -343   -390    107       C  
ATOM   1342  C   TRP A 162      12.600 -37.823  -6.728  1.00 31.20           C  
ANISOU 1342  C   TRP A 162     5260   3507   3087   -298   -433    126       C  
ATOM   1343  O   TRP A 162      13.802 -37.915  -6.496  1.00 30.86           O  
ANISOU 1343  O   TRP A 162     5224   3432   3071   -237   -481    148       O  
ATOM   1344  CB  TRP A 162      11.992 -35.472  -7.317  1.00 29.40           C  
ANISOU 1344  CB  TRP A 162     4862   3402   2907   -289   -362     88       C  
ATOM   1345  CG  TRP A 162      11.687 -35.788  -8.744  1.00 27.81           C  
ANISOU 1345  CG  TRP A 162     4627   3211   2730   -263   -337     71       C  
ATOM   1346  CD1 TRP A 162      10.455 -35.847  -9.330  1.00 27.06           C  
ANISOU 1346  CD1 TRP A 162     4515   3150   2618   -309   -294     48       C  
ATOM   1347  CD2 TRP A 162      12.640 -36.018  -9.785  1.00 26.96           C  
ANISOU 1347  CD2 TRP A 162     4493   3083   2668   -185   -353     75       C  
ATOM   1348  NE1 TRP A 162      10.584 -36.107 -10.676  1.00 25.60           N  
ANISOU 1348  NE1 TRP A 162     4303   2964   2461   -267   -286     38       N  
ATOM   1349  CE2 TRP A 162      11.915 -36.223 -10.979  1.00 25.57           C  
ANISOU 1349  CE2 TRP A 162     4295   2926   2494   -191   -318     53       C  
ATOM   1350  CE3 TRP A 162      14.040 -36.084  -9.823  1.00 26.30           C  
ANISOU 1350  CE3 TRP A 162     4401   2971   2622   -112   -392     95       C  
ATOM   1351  CZ2 TRP A 162      12.543 -36.499 -12.197  1.00 26.69           C  
ANISOU 1351  CZ2 TRP A 162     4416   3054   2669   -127   -318     48       C  
ATOM   1352  CZ3 TRP A 162      14.663 -36.336 -11.034  1.00 26.85           C  
ANISOU 1352  CZ3 TRP A 162     4439   3033   2729    -45   -388     89       C  
ATOM   1353  CH2 TRP A 162      13.914 -36.538 -12.208  1.00 27.12           C  
ANISOU 1353  CH2 TRP A 162     4462   3083   2761    -53   -349     65       C  
ATOM   1354  N   SER A 163      11.896 -38.774  -7.329  1.00 31.85           N  
ANISOU 1354  N   SER A 163     5388   3566   3145   -329   -416    116       N  
ATOM   1355  CA  SER A 163      12.507 -40.003  -7.811  1.00 32.36           C  
ANISOU 1355  CA  SER A 163     5524   3559   3214   -286   -451    128       C  
ATOM   1356  C   SER A 163      12.552 -40.016  -9.334  1.00 32.67           C  
ANISOU 1356  C   SER A 163     5508   3612   3292   -234   -425    105       C  
ATOM   1357  O   SER A 163      11.508 -40.054  -9.990  1.00 33.70           O  
ANISOU 1357  O   SER A 163     5626   3773   3407   -283   -385     83       O  
ATOM   1358  CB  SER A 163      11.733 -41.222  -7.299  1.00 31.66           C  
ANISOU 1358  CB  SER A 163     5555   3417   3058   -367   -459    135       C  
ATOM   1359  OG  SER A 163      12.091 -42.373  -8.040  1.00 34.37           O  
ANISOU 1359  OG  SER A 163     5964   3691   3403   -328   -480    138       O  
ATOM   1360  N   ILE A 164      13.762 -39.987  -9.884  1.00 32.36           N  
ANISOU 1360  N   ILE A 164     5437   3555   3303   -138   -447    112       N  
ATOM   1361  CA  ILE A 164      13.965 -40.085 -11.329  1.00 34.43           C  
ANISOU 1361  CA  ILE A 164     5659   3823   3599    -83   -423     92       C  
ATOM   1362  C   ILE A 164      13.471 -41.430 -11.880  1.00 34.35           C  
ANISOU 1362  C   ILE A 164     5746   3752   3552   -105   -422     83       C  
ATOM   1363  O   ILE A 164      13.056 -41.511 -13.033  1.00 36.20           O  
ANISOU 1363  O   ILE A 164     5961   4001   3791   -103   -390     59       O  
ATOM   1364  CB  ILE A 164      15.456 -39.797 -11.745  1.00 34.43           C  
ANISOU 1364  CB  ILE A 164     5602   3820   3660     26   -443    102       C  
ATOM   1365  CG1 ILE A 164      15.589 -39.647 -13.271  1.00 35.05           C  
ANISOU 1365  CG1 ILE A 164     5626   3922   3770     76   -405     78       C  
ATOM   1366  CG2 ILE A 164      16.414 -40.868 -11.193  1.00 36.18           C  
ANISOU 1366  CG2 ILE A 164     5902   3964   3880     78   -499    127       C  
ATOM   1367  CD1 ILE A 164      16.823 -38.869 -13.732  1.00 33.63           C  
ANISOU 1367  CD1 ILE A 164     5351   3775   3650    161   -405     83       C  
ATOM   1368  N   GLU A 165      13.496 -42.471 -11.051  1.00 33.92           N  
ANISOU 1368  N   GLU A 165     5803   3627   3459   -131   -459    102       N  
ATOM   1369  CA  GLU A 165      13.029 -43.797 -11.472  1.00 34.78           C  
ANISOU 1369  CA  GLU A 165     6023   3667   3527   -160   -463     95       C  
ATOM   1370  C   GLU A 165      11.529 -43.787 -11.727  1.00 32.19           C  
ANISOU 1370  C   GLU A 165     5699   3379   3155   -270   -423     75       C  
ATOM   1371  O   GLU A 165      11.061 -44.309 -12.738  1.00 33.40           O  
ANISOU 1371  O   GLU A 165     5876   3519   3295   -284   -405     54       O  
ATOM   1372  CB  GLU A 165      13.371 -44.879 -10.431  1.00 38.08           C  
ANISOU 1372  CB  GLU A 165     6568   3995   3907   -170   -517    125       C  
ATOM   1373  CG  GLU A 165      14.864 -45.087 -10.168  1.00 45.99           C  
ANISOU 1373  CG  GLU A 165     7575   4950   4950    -57   -567    148       C  
ATOM   1374  CD  GLU A 165      15.465 -44.060  -9.205  1.00 52.43           C  
ANISOU 1374  CD  GLU A 165     8315   5814   5792    -41   -589    170       C  
ATOM   1375  OE1 GLU A 165      14.720 -43.190  -8.692  1.00 54.08           O  
ANISOU 1375  OE1 GLU A 165     8478   6087   5984   -116   -563    166       O  
ATOM   1376  OE2 GLU A 165      16.692 -44.122  -8.964  1.00 54.18           O  
ANISOU 1376  OE2 GLU A 165     8524   6012   6052     48   -633    191       O  
ATOM   1377  N   ILE A 166      10.768 -43.196 -10.809  1.00 32.54           N  
ANISOU 1377  N   ILE A 166     5718   3472   3173   -349   -410     80       N  
ATOM   1378  CA  ILE A 166       9.313 -43.130 -10.982  1.00 33.09           C  
ANISOU 1378  CA  ILE A 166     5775   3592   3204   -453   -370     61       C  
ATOM   1379  C   ILE A 166       8.939 -42.142 -12.093  1.00 30.01           C  
ANISOU 1379  C   ILE A 166     5267   3283   2854   -430   -330     35       C  
ATOM   1380  O   ILE A 166       7.993 -42.374 -12.845  1.00 30.54           O  
ANISOU 1380  O   ILE A 166     5328   3374   2901   -483   -306     15       O  
ATOM   1381  CB  ILE A 166       8.580 -42.803  -9.661  1.00 33.55           C  
ANISOU 1381  CB  ILE A 166     5841   3684   3222   -542   -360     72       C  
ATOM   1382  CG1 ILE A 166       8.847 -43.899  -8.625  1.00 32.44           C  
ANISOU 1382  CG1 ILE A 166     5837   3458   3032   -577   -402    100       C  
ATOM   1383  CG2 ILE A 166       7.077 -42.651  -9.898  1.00 33.80           C  
ANISOU 1383  CG2 ILE A 166     5837   3783   3222   -642   -314     50       C  
ATOM   1384  CD1 ILE A 166       8.333 -43.568  -7.229  1.00 32.59           C  
ANISOU 1384  CD1 ILE A 166     5873   3504   3008   -657   -395    113       C  
ATOM   1385  N   ALA A 167       9.704 -41.061 -12.209  1.00 26.87           N  
ANISOU 1385  N   ALA A 167     4777   2923   2509   -354   -326     35       N  
ATOM   1386  CA  ALA A 167       9.484 -40.078 -13.264  1.00 27.25           C  
ANISOU 1386  CA  ALA A 167     4719   3039   2595   -324   -293     14       C  
ATOM   1387  C   ALA A 167       9.579 -40.709 -14.657  1.00 27.37           C  
ANISOU 1387  C   ALA A 167     4755   3029   2615   -293   -288     -2       C  
ATOM   1388  O   ALA A 167       8.821 -40.347 -15.557  1.00 27.16           O  
ANISOU 1388  O   ALA A 167     4679   3052   2589   -317   -262    -21       O  
ATOM   1389  CB  ALA A 167      10.463 -38.919 -13.127  1.00 24.96           C  
ANISOU 1389  CB  ALA A 167     4346   2780   2358   -247   -296     22       C  
ATOM   1390  N   ALA A 168      10.493 -41.662 -14.820  1.00 28.60           N  
ANISOU 1390  N   ALA A 168     4987   3107   2773   -240   -315      6       N  
ATOM   1391  CA  ALA A 168      10.705 -42.314 -16.115  1.00 31.86           C  
ANISOU 1391  CA  ALA A 168     5432   3486   3187   -202   -309    -12       C  
ATOM   1392  C   ALA A 168       9.621 -43.331 -16.465  1.00 32.47           C  
ANISOU 1392  C   ALA A 168     5596   3534   3208   -289   -306    -25       C  
ATOM   1393  O   ALA A 168       9.382 -43.595 -17.643  1.00 34.65           O  
ANISOU 1393  O   ALA A 168     5880   3809   3477   -286   -292    -46       O  
ATOM   1394  CB  ALA A 168      12.091 -42.971 -16.172  1.00 34.66           C  
ANISOU 1394  CB  ALA A 168     5837   3767   3566   -104   -335     -2       C  
ATOM   1395  N   LYS A 169       8.971 -43.895 -15.448  1.00 32.03           N  
ANISOU 1395  N   LYS A 169     5607   3456   3107   -373   -320    -12       N  
ATOM   1396  CA  LYS A 169       7.950 -44.931 -15.646  1.00 32.78           C  
ANISOU 1396  CA  LYS A 169     5792   3519   3142   -471   -321    -21       C  
ATOM   1397  C   LYS A 169       6.696 -44.389 -16.318  1.00 31.73           C  
ANISOU 1397  C   LYS A 169     5585   3473   2998   -544   -290    -41       C  
ATOM   1398  O   LYS A 169       6.382 -43.196 -16.204  1.00 29.41           O  
ANISOU 1398  O   LYS A 169     5176   3265   2734   -541   -268    -43       O  
ATOM   1399  CB  LYS A 169       7.565 -45.588 -14.314  1.00 34.18           C  
ANISOU 1399  CB  LYS A 169     6057   3658   3271   -551   -342      1       C  
ATOM   1400  CG  LYS A 169       8.644 -46.450 -13.688  1.00 38.69           C  
ANISOU 1400  CG  LYS A 169     6735   4126   3838   -493   -384     23       C  
ATOM   1401  CD  LYS A 169       8.074 -47.300 -12.562  1.00 45.70           C  
ANISOU 1401  CD  LYS A 169     7736   4965   4662   -593   -405     44       C  
ATOM   1402  CE  LYS A 169       9.168 -47.868 -11.671  1.00 52.37           C  
ANISOU 1402  CE  LYS A 169     8669   5722   5507   -531   -453     74       C  
ATOM   1403  NZ  LYS A 169      10.120 -48.749 -12.411  1.00 54.78           N  
ANISOU 1403  NZ  LYS A 169     9052   5934   5828   -435   -480     70       N  
ATOM   1404  N   LEU A 170       5.977 -45.282 -17.001  1.00 32.62           N  
ANISOU 1404  N   LEU A 170     5766   3560   3067   -612   -292    -55       N  
ATOM   1405  CA  LEU A 170       4.710 -44.952 -17.661  1.00 33.72           C  
ANISOU 1405  CA  LEU A 170     5844   3777   3189   -693   -272    -72       C  
ATOM   1406  C   LEU A 170       3.643 -44.537 -16.655  1.00 34.22           C  
ANISOU 1406  C   LEU A 170     5855   3912   3233   -788   -256    -63       C  
ATOM   1407  O   LEU A 170       3.680 -44.961 -15.498  1.00 35.43           O  
ANISOU 1407  O   LEU A 170     6070   4032   3362   -826   -265    -46       O  
ATOM   1408  CB  LEU A 170       4.196 -46.163 -18.444  1.00 34.86           C  
ANISOU 1408  CB  LEU A 170     6094   3868   3282   -759   -285    -85       C  
ATOM   1409  CG  LEU A 170       5.157 -46.948 -19.344  1.00 37.39           C  
ANISOU 1409  CG  LEU A 170     6509   4095   3602   -681   -300    -97       C  
ATOM   1410  CD1 LEU A 170       4.530 -48.291 -19.718  1.00 40.19           C  
ANISOU 1410  CD1 LEU A 170     6998   4381   3889   -772   -318   -107       C  
ATOM   1411  CD2 LEU A 170       5.545 -46.149 -20.585  1.00 34.87           C  
ANISOU 1411  CD2 LEU A 170     6104   3820   3323   -601   -282   -115       C  
ATOM   1412  N   GLN A 171       2.685 -43.727 -17.097  1.00 33.59           N  
ANISOU 1412  N   GLN A 171     5668   3931   3165   -824   -233    -76       N  
ATOM   1413  CA  GLN A 171       1.549 -43.366 -16.251  1.00 37.06           C  
ANISOU 1413  CA  GLN A 171     6050   4447   3584   -916   -211    -73       C  
ATOM   1414  C   GLN A 171       0.772 -44.583 -15.749  1.00 36.77           C  
ANISOU 1414  C   GLN A 171     6113   4377   3480  -1043   -219    -68       C  
ATOM   1415  O   GLN A 171       0.187 -44.543 -14.673  1.00 37.18           O  
ANISOU 1415  O   GLN A 171     6158   4462   3507  -1114   -203    -58       O  
ATOM   1416  CB  GLN A 171       0.617 -42.377 -16.956  1.00 37.67           C  
ANISOU 1416  CB  GLN A 171     5993   4634   3685   -928   -190    -89       C  
ATOM   1417  CG  GLN A 171       1.176 -40.955 -16.984  1.00 47.27           C  
ANISOU 1417  CG  GLN A 171     7102   5896   4961   -824   -175    -90       C  
ATOM   1418  CD  GLN A 171       0.102 -39.891 -16.842  1.00 54.25           C  
ANISOU 1418  CD  GLN A 171     7859   6892   5862   -850   -146    -98       C  
ATOM   1419  OE1 GLN A 171      -0.729 -39.943 -15.928  1.00 57.49           O  
ANISOU 1419  OE1 GLN A 171     8253   7344   6247   -926   -126    -97       O  
ATOM   1420  NE2 GLN A 171       0.123 -38.906 -17.740  1.00 55.40           N  
ANISOU 1420  NE2 GLN A 171     7916   7085   6048   -785   -143   -107       N  
ATOM   1421  N   GLU A 172       0.799 -45.663 -16.527  1.00 35.20           N  
ANISOU 1421  N   GLU A 172     6014   4111   3248  -1071   -244    -73       N  
ATOM   1422  CA  GLU A 172       0.120 -46.906 -16.181  1.00 35.87           C  
ANISOU 1422  CA  GLU A 172     6213   4151   3264  -1196   -256    -68       C  
ATOM   1423  C   GLU A 172       0.873 -47.706 -15.114  1.00 36.62           C  
ANISOU 1423  C   GLU A 172     6438   4143   3333  -1191   -276    -45       C  
ATOM   1424  O   GLU A 172       0.341 -48.671 -14.559  1.00 34.62           O  
ANISOU 1424  O   GLU A 172     6286   3850   3019  -1299   -285    -35       O  
ATOM   1425  CB  GLU A 172      -0.094 -47.755 -17.442  1.00 38.36           C  
ANISOU 1425  CB  GLU A 172     6601   4424   3552  -1227   -278    -84       C  
ATOM   1426  CG  GLU A 172      -1.084 -47.158 -18.427  1.00 39.25           C  
ANISOU 1426  CG  GLU A 172     6600   4641   3673  -1267   -267   -102       C  
ATOM   1427  CD  GLU A 172      -0.461 -46.162 -19.406  1.00 46.68           C  
ANISOU 1427  CD  GLU A 172     7450   5613   4674  -1143   -262   -114       C  
ATOM   1428  OE1 GLU A 172      -1.229 -45.494 -20.137  1.00 49.13           O  
ANISOU 1428  OE1 GLU A 172     7656   6014   4998  -1162   -255   -125       O  
ATOM   1429  OE2 GLU A 172       0.783 -46.047 -19.457  1.00 46.54           O  
ANISOU 1429  OE2 GLU A 172     7464   5532   4688  -1029   -266   -112       O  
ATOM   1430  N   GLN A 173       2.111 -47.302 -14.833  1.00 36.63           N  
ANISOU 1430  N   GLN A 173     6438   4103   3378  -1068   -286    -36       N  
ATOM   1431  CA  GLN A 173       2.894 -47.896 -13.747  1.00 37.03           C  
ANISOU 1431  CA  GLN A 173     6596   4065   3411  -1049   -310    -11       C  
ATOM   1432  C   GLN A 173       2.897 -46.986 -12.531  1.00 35.94           C  
ANISOU 1432  C   GLN A 173     6384   3985   3287  -1047   -292      3       C  
ATOM   1433  O   GLN A 173       3.551 -47.281 -11.526  1.00 36.63           O  
ANISOU 1433  O   GLN A 173     6544   4012   3362  -1029   -314     26       O  
ATOM   1434  CB  GLN A 173       4.336 -48.144 -14.184  1.00 37.41           C  
ANISOU 1434  CB  GLN A 173     6695   4024   3495   -913   -339     -9       C  
ATOM   1435  CG  GLN A 173       4.520 -49.199 -15.256  1.00 39.29           C  
ANISOU 1435  CG  GLN A 173     7038   4180   3711   -903   -358    -23       C  
ATOM   1436  CD  GLN A 173       5.966 -49.298 -15.692  1.00 42.95           C  
ANISOU 1436  CD  GLN A 173     7528   4572   4219   -755   -376    -24       C  
ATOM   1437  OE1 GLN A 173       6.458 -48.453 -16.447  1.00 44.93           O  
ANISOU 1437  OE1 GLN A 173     7678   4871   4524   -667   -359    -38       O  
ATOM   1438  NE2 GLN A 173       6.662 -50.325 -15.209  1.00 42.50           N  
ANISOU 1438  NE2 GLN A 173     7608   4401   4140   -726   -412     -8       N  
ATOM   1439  N   GLY A 174       2.166 -45.880 -12.627  1.00 34.62           N  
ANISOU 1439  N   GLY A 174     6076   3932   3144  -1063   -254    -11       N  
ATOM   1440  CA  GLY A 174       2.098 -44.903 -11.545  1.00 34.50           C  
ANISOU 1440  CA  GLY A 174     5986   3978   3143  -1058   -230     -3       C  
ATOM   1441  C   GLY A 174       3.182 -43.850 -11.669  1.00 35.01           C  
ANISOU 1441  C   GLY A 174     5975   4052   3275   -925   -234     -4       C  
ATOM   1442  O   GLY A 174       3.379 -43.039 -10.757  1.00 32.32           O  
ANISOU 1442  O   GLY A 174     5588   3744   2948   -905   -222      4       O  
ATOM   1443  N   GLY A 175       3.885 -43.872 -12.802  1.00 34.20           N  
ANISOU 1443  N   GLY A 175     5865   3920   3210   -840   -250    -12       N  
ATOM   1444  CA  GLY A 175       4.952 -42.923 -13.078  1.00 32.89           C  
ANISOU 1444  CA  GLY A 175     5627   3764   3107   -718   -253    -12       C  
ATOM   1445  C   GLY A 175       4.451 -41.669 -13.765  1.00 33.24           C  
ANISOU 1445  C   GLY A 175     5533   3905   3190   -696   -221    -31       C  
ATOM   1446  O   GLY A 175       3.247 -41.496 -13.956  1.00 32.57           O  
ANISOU 1446  O   GLY A 175     5400   3888   3088   -770   -197    -44       O  
ATOM   1447  N   ASP A 176       5.386 -40.800 -14.146  1.00 32.33           N  
ANISOU 1447  N   ASP A 176     5355   3799   3130   -593   -223    -32       N  
ATOM   1448  CA  ASP A 176       5.061 -39.479 -14.675  1.00 32.89           C  
ANISOU 1448  CA  ASP A 176     5303   3954   3240   -561   -197    -45       C  
ATOM   1449  C   ASP A 176       5.325 -39.378 -16.169  1.00 33.68           C  
ANISOU 1449  C   ASP A 176     5375   4057   3367   -508   -198    -58       C  
ATOM   1450  O   ASP A 176       5.026 -38.356 -16.786  1.00 33.14           O  
ANISOU 1450  O   ASP A 176     5213   4053   3327   -482   -180    -68       O  
ATOM   1451  CB  ASP A 176       5.864 -38.400 -13.938  1.00 31.95           C  
ANISOU 1451  CB  ASP A 176     5132   3849   3159   -496   -195    -35       C  
ATOM   1452  CG  ASP A 176       5.754 -38.518 -12.423  1.00 34.92           C  
ANISOU 1452  CG  ASP A 176     5550   4214   3505   -545   -197    -21       C  
ATOM   1453  OD1 ASP A 176       4.621 -38.670 -11.913  1.00 34.16           O  
ANISOU 1453  OD1 ASP A 176     5454   4155   3370   -631   -175    -28       O  
ATOM   1454  OD2 ASP A 176       6.803 -38.462 -11.744  1.00 35.37           O  
ANISOU 1454  OD2 ASP A 176     5638   4228   3574   -498   -222     -4       O  
ATOM   1455  N   GLU A 177       5.909 -40.431 -16.736  1.00 35.75           N  
ANISOU 1455  N   GLU A 177     5723   4245   3616   -488   -218    -58       N  
ATOM   1456  CA  GLU A 177       6.171 -40.508 -18.172  1.00 39.05           C  
ANISOU 1456  CA  GLU A 177     6134   4657   4047   -444   -217    -72       C  
ATOM   1457  C   GLU A 177       6.986 -39.301 -18.657  1.00 37.11           C  
ANISOU 1457  C   GLU A 177     5798   4446   3856   -351   -206    -72       C  
ATOM   1458  O   GLU A 177       6.649 -38.681 -19.668  1.00 38.00           O  
ANISOU 1458  O   GLU A 177     5851   4606   3982   -339   -192    -84       O  
ATOM   1459  CB  GLU A 177       4.844 -40.599 -18.930  1.00 40.40           C  
ANISOU 1459  CB  GLU A 177     6281   4879   4189   -522   -207    -88       C  
ATOM   1460  CG  GLU A 177       4.738 -41.726 -19.923  1.00 47.88           C  
ANISOU 1460  CG  GLU A 177     7316   5774   5101   -546   -220   -101       C  
ATOM   1461  CD  GLU A 177       3.304 -41.906 -20.406  1.00 54.14           C  
ANISOU 1461  CD  GLU A 177     8091   6623   5859   -648   -218   -113       C  
ATOM   1462  OE1 GLU A 177       2.818 -41.043 -21.177  1.00 56.79           O  
ANISOU 1462  OE1 GLU A 177     8336   7030   6213   -639   -209   -121       O  
ATOM   1463  OE2 GLU A 177       2.661 -42.900 -20.003  1.00 53.56           O  
ANISOU 1463  OE2 GLU A 177     8092   6521   5736   -738   -229   -112       O  
ATOM   1464  N   VAL A 178       8.035 -38.949 -17.914  1.00 35.83           N  
ANISOU 1464  N   VAL A 178     5628   4262   3724   -291   -214    -57       N  
ATOM   1465  CA  VAL A 178       9.013 -37.963 -18.389  1.00 33.84           C  
ANISOU 1465  CA  VAL A 178     5304   4030   3522   -204   -206    -54       C  
ATOM   1466  C   VAL A 178       9.745 -38.618 -19.569  1.00 33.57           C  
ANISOU 1466  C   VAL A 178     5311   3953   3493   -149   -206    -64       C  
ATOM   1467  O   VAL A 178      10.275 -39.720 -19.416  1.00 32.82           O  
ANISOU 1467  O   VAL A 178     5300   3788   3383   -133   -223    -61       O  
ATOM   1468  CB  VAL A 178       9.995 -37.530 -17.263  1.00 33.93           C  
ANISOU 1468  CB  VAL A 178     5303   4027   3561   -162   -221    -34       C  
ATOM   1469  CG1 VAL A 178      11.089 -36.614 -17.798  1.00 31.09           C  
ANISOU 1469  CG1 VAL A 178     4875   3686   3251    -79   -215    -30       C  
ATOM   1470  CG2 VAL A 178       9.245 -36.845 -16.135  1.00 30.10           C  
ANISOU 1470  CG2 VAL A 178     4786   3585   3066   -217   -216    -29       C  
ATOM   1471  N   PRO A 179       9.728 -37.969 -20.758  1.00 33.79           N  
ANISOU 1471  N   PRO A 179     5283   4019   3536   -122   -187    -76       N  
ATOM   1472  CA  PRO A 179      10.255 -38.554 -22.001  1.00 32.91           C  
ANISOU 1472  CA  PRO A 179     5210   3875   3420    -79   -178    -90       C  
ATOM   1473  C   PRO A 179      11.649 -39.151 -21.814  1.00 33.69           C  
ANISOU 1473  C   PRO A 179     5349   3911   3539     -1   -185    -84       C  
ATOM   1474  O   PRO A 179      12.525 -38.493 -21.248  1.00 34.92           O  
ANISOU 1474  O   PRO A 179     5452   4081   3735     49   -189    -68       O  
ATOM   1475  CB  PRO A 179      10.323 -37.349 -22.937  1.00 33.12           C  
ANISOU 1475  CB  PRO A 179     5150   3962   3472    -49   -157    -94       C  
ATOM   1476  CG  PRO A 179       9.215 -36.478 -22.488  1.00 33.91           C  
ANISOU 1476  CG  PRO A 179     5190   4125   3571   -105   -158    -90       C  
ATOM   1477  CD  PRO A 179       9.235 -36.596 -20.982  1.00 34.19           C  
ANISOU 1477  CD  PRO A 179     5236   4145   3608   -127   -171    -76       C  
ATOM   1478  N   SER A 180      11.846 -40.383 -22.275  1.00 34.35           N  
ANISOU 1478  N   SER A 180     5526   3929   3596     11   -190    -96       N  
ATOM   1479  CA  SER A 180      13.116 -41.099 -22.070  1.00 36.32           C  
ANISOU 1479  CA  SER A 180     5822   4114   3864     92   -199    -92       C  
ATOM   1480  C   SER A 180      14.351 -40.385 -22.637  1.00 35.90           C  
ANISOU 1480  C   SER A 180     5692   4087   3860    185   -177    -91       C  
ATOM   1481  O   SER A 180      15.457 -40.561 -22.126  1.00 35.24           O  
ANISOU 1481  O   SER A 180     5602   3978   3809    253   -188    -78       O  
ATOM   1482  CB  SER A 180      13.035 -42.546 -22.597  1.00 39.39           C  
ANISOU 1482  CB  SER A 180     6333   4421   4211     91   -203   -110       C  
ATOM   1483  OG  SER A 180      12.873 -42.594 -24.008  1.00 41.67           O  
ANISOU 1483  OG  SER A 180     6630   4719   4483     98   -175   -136       O  
ATOM   1484  N   GLU A 181      14.162 -39.569 -23.672  1.00 36.24           N  
ANISOU 1484  N   GLU A 181     5675   4185   3909    184   -147   -102       N  
ATOM   1485  CA  GLU A 181      15.282 -38.853 -24.287  1.00 36.14           C  
ANISOU 1485  CA  GLU A 181     5590   4203   3937    260   -120   -101       C  
ATOM   1486  C   GLU A 181      15.844 -37.694 -23.442  1.00 34.66           C  
ANISOU 1486  C   GLU A 181     5309   4065   3797    276   -130    -76       C  
ATOM   1487  O   GLU A 181      16.844 -37.082 -23.824  1.00 36.20           O  
ANISOU 1487  O   GLU A 181     5440   4287   4028    333   -111    -71       O  
ATOM   1488  CB  GLU A 181      14.928 -38.381 -25.711  1.00 38.60           C  
ANISOU 1488  CB  GLU A 181     5882   4553   4232    251    -86   -120       C  
ATOM   1489  CG  GLU A 181      13.966 -37.188 -25.802  1.00 40.93           C  
ANISOU 1489  CG  GLU A 181     6111   4916   4525    191    -87   -113       C  
ATOM   1490  CD  GLU A 181      12.497 -37.595 -25.842  1.00 44.94           C  
ANISOU 1490  CD  GLU A 181     6664   5424   4987    106   -103   -122       C  
ATOM   1491  OE1 GLU A 181      12.184 -38.784 -25.607  1.00 45.08           O  
ANISOU 1491  OE1 GLU A 181     6768   5386   4973     81   -118   -131       O  
ATOM   1492  OE2 GLU A 181      11.649 -36.715 -26.115  1.00 44.17           O  
ANISOU 1492  OE2 GLU A 181     6515   5382   4885     64   -103   -120       O  
ATOM   1493  N   ILE A 182      15.209 -37.378 -22.314  1.00 29.82           N  
ANISOU 1493  N   ILE A 182     4688   3462   3180    223   -156    -61       N  
ATOM   1494  CA  ILE A 182      15.746 -36.334 -21.433  1.00 29.07           C  
ANISOU 1494  CA  ILE A 182     4518   3404   3122    234   -168    -38       C  
ATOM   1495  C   ILE A 182      16.122 -36.841 -20.040  1.00 29.21           C  
ANISOU 1495  C   ILE A 182     4569   3384   3145    236   -207    -19       C  
ATOM   1496  O   ILE A 182      16.780 -36.132 -19.275  1.00 30.27           O  
ANISOU 1496  O   ILE A 182     4651   3540   3310    253   -224      1       O  
ATOM   1497  CB  ILE A 182      14.835 -35.058 -21.335  1.00 27.86           C  
ANISOU 1497  CB  ILE A 182     4305   3312   2968    179   -161    -36       C  
ATOM   1498  CG1 ILE A 182      13.608 -35.310 -20.452  1.00 27.03           C  
ANISOU 1498  CG1 ILE A 182     4237   3204   2830    105   -177    -36       C  
ATOM   1499  CG2 ILE A 182      14.449 -34.532 -22.742  1.00 27.25           C  
ANISOU 1499  CG2 ILE A 182     4199   3271   2884    177   -129    -51       C  
ATOM   1500  CD1 ILE A 182      12.956 -34.026 -19.939  1.00 28.41           C  
ANISOU 1500  CD1 ILE A 182     4349   3434   3013     68   -174    -30       C  
ATOM   1501  N   ILE A 183      15.728 -38.072 -19.730  1.00 28.53           N  
ANISOU 1501  N   ILE A 183     4576   3239   3025    217   -225    -23       N  
ATOM   1502  CA  ILE A 183      16.005 -38.667 -18.424  1.00 31.96           C  
ANISOU 1502  CA  ILE A 183     5059   3628   3454    213   -266     -2       C  
ATOM   1503  C   ILE A 183      17.486 -38.591 -18.036  1.00 32.87           C  
ANISOU 1503  C   ILE A 183     5138   3735   3616    296   -287     17       C  
ATOM   1504  O   ILE A 183      17.817 -38.239 -16.901  1.00 33.86           O  
ANISOU 1504  O   ILE A 183     5247   3865   3752    289   -320     40       O  
ATOM   1505  CB  ILE A 183      15.487 -40.133 -18.344  1.00 33.76           C  
ANISOU 1505  CB  ILE A 183     5409   3783   3637    187   -281    -10       C  
ATOM   1506  CG1 ILE A 183      13.959 -40.149 -18.184  1.00 35.09           C  
ANISOU 1506  CG1 ILE A 183     5606   3968   3758     83   -273    -19       C  
ATOM   1507  CG2 ILE A 183      16.192 -40.923 -17.224  1.00 30.40           C  
ANISOU 1507  CG2 ILE A 183     5045   3295   3213    216   -327     14       C  
ATOM   1508  CD1 ILE A 183      13.425 -39.465 -16.926  1.00 38.04           C  
ANISOU 1508  CD1 ILE A 183     5952   4376   4125     23   -286     -2       C  
ATOM   1509  N   ASP A 184      18.366 -38.904 -18.985  1.00 33.18           N  
ANISOU 1509  N   ASP A 184     5163   3765   3680    373   -268      6       N  
ATOM   1510  CA  ASP A 184      19.807 -38.888 -18.746  1.00 33.56           C  
ANISOU 1510  CA  ASP A 184     5164   3812   3775    457   -285     23       C  
ATOM   1511  C   ASP A 184      20.370 -37.465 -18.704  1.00 31.12           C  
ANISOU 1511  C   ASP A 184     4739   3579   3507    461   -276     35       C  
ATOM   1512  O   ASP A 184      21.543 -37.274 -18.401  1.00 31.28           O  
ANISOU 1512  O   ASP A 184     4704   3613   3569    518   -294     53       O  
ATOM   1513  CB  ASP A 184      20.537 -39.722 -19.815  1.00 36.51           C  
ANISOU 1513  CB  ASP A 184     5558   4153   4159    541   -259      4       C  
ATOM   1514  CG  ASP A 184      20.186 -41.214 -19.751  1.00 44.00           C  
ANISOU 1514  CG  ASP A 184     6635   5012   5070    548   -276     -7       C  
ATOM   1515  OD1 ASP A 184      19.762 -41.697 -18.676  1.00 49.48           O  
ANISOU 1515  OD1 ASP A 184     7395   5664   5739    507   -320     11       O  
ATOM   1516  OD2 ASP A 184      20.335 -41.911 -20.777  1.00 47.04           O  
ANISOU 1516  OD2 ASP A 184     7062   5365   5445    592   -246    -32       O  
ATOM   1517  N   LYS A 185      19.534 -36.476 -19.010  1.00 28.24           N  
ANISOU 1517  N   LYS A 185     4339   3262   3130    400   -251     28       N  
ATOM   1518  CA  LYS A 185      19.962 -35.073 -19.061  1.00 26.90           C  
ANISOU 1518  CA  LYS A 185     4071   3158   2993    396   -240     38       C  
ATOM   1519  C   LYS A 185      19.548 -34.266 -17.832  1.00 25.09           C  
ANISOU 1519  C   LYS A 185     3828   2946   2758    339   -269     55       C  
ATOM   1520  O   LYS A 185      19.712 -33.039 -17.804  1.00 24.19           O  
ANISOU 1520  O   LYS A 185     3647   2880   2662    323   -262     62       O  
ATOM   1521  CB  LYS A 185      19.426 -34.403 -20.331  1.00 24.20           C  
ANISOU 1521  CB  LYS A 185     3698   2855   2642    379   -191     18       C  
ATOM   1522  CG  LYS A 185      19.890 -35.090 -21.606  1.00 28.65           C  
ANISOU 1522  CG  LYS A 185     4275   3405   3206    434   -156     -2       C  
ATOM   1523  CD  LYS A 185      19.451 -34.357 -22.855  1.00 27.31           C  
ANISOU 1523  CD  LYS A 185     4075   3276   3025    415   -112    -17       C  
ATOM   1524  CE  LYS A 185      19.971 -35.083 -24.095  1.00 30.88           C  
ANISOU 1524  CE  LYS A 185     4549   3713   3472    469    -74    -39       C  
ATOM   1525  NZ  LYS A 185      19.780 -34.278 -25.339  1.00 30.43           N  
ANISOU 1525  NZ  LYS A 185     4457   3699   3405    455    -32    -50       N  
ATOM   1526  N   ILE A 186      18.998 -34.951 -16.831  1.00 24.95           N  
ANISOU 1526  N   ILE A 186     3881   2888   2710    305   -301     61       N  
ATOM   1527  CA  ILE A 186      18.512 -34.281 -15.621  1.00 26.91           C  
ANISOU 1527  CA  ILE A 186     4130   3149   2944    246   -324     74       C  
ATOM   1528  C   ILE A 186      19.557 -34.313 -14.512  1.00 27.73           C  
ANISOU 1528  C   ILE A 186     4228   3241   3068    270   -374    102       C  
ATOM   1529  O   ILE A 186      20.120 -35.367 -14.199  1.00 26.19           O  
ANISOU 1529  O   ILE A 186     4079   2999   2874    309   -406    113       O  
ATOM   1530  CB  ILE A 186      17.151 -34.851 -15.124  1.00 26.28           C  
ANISOU 1530  CB  ILE A 186     4128   3045   2813    177   -323     64       C  
ATOM   1531  CG1 ILE A 186      16.069 -34.658 -16.194  1.00 29.42           C  
ANISOU 1531  CG1 ILE A 186     4517   3469   3193    147   -279     39       C  
ATOM   1532  CG2 ILE A 186      16.712 -34.163 -13.835  1.00 23.85           C  
ANISOU 1532  CG2 ILE A 186     3821   2753   2487    121   -341     75       C  
ATOM   1533  CD1 ILE A 186      14.768 -35.412 -15.917  1.00 31.63           C  
ANISOU 1533  CD1 ILE A 186     4868   3728   3424     80   -276     28       C  
ATOM   1534  N   ILE A 187      19.826 -33.138 -13.951  1.00 27.29           N  
ANISOU 1534  N   ILE A 187     4117   3223   3027    248   -384    114       N  
ATOM   1535  CA  ILE A 187      20.732 -32.997 -12.826  1.00 26.89           C  
ANISOU 1535  CA  ILE A 187     4059   3168   2990    256   -437    141       C  
ATOM   1536  C   ILE A 187      19.889 -32.453 -11.691  1.00 27.32           C  
ANISOU 1536  C   ILE A 187     4150   3224   3007    182   -448    143       C  
ATOM   1537  O   ILE A 187      19.489 -31.278 -11.689  1.00 26.08           O  
ANISOU 1537  O   ILE A 187     3956   3105   2849    147   -426    134       O  
ATOM   1538  CB  ILE A 187      21.956 -32.098 -13.160  1.00 28.89           C  
ANISOU 1538  CB  ILE A 187     4215   3467   3293    293   -441    154       C  
ATOM   1539  CG1 ILE A 187      22.786 -32.753 -14.273  1.00 30.46           C  
ANISOU 1539  CG1 ILE A 187     4380   3667   3528    370   -423    150       C  
ATOM   1540  CG2 ILE A 187      22.830 -31.881 -11.916  1.00 28.05           C  
ANISOU 1540  CG2 ILE A 187     4100   3361   3198    290   -504    184       C  
ATOM   1541  CD1 ILE A 187      23.853 -31.882 -14.875  1.00 32.99           C  
ANISOU 1541  CD1 ILE A 187     4599   4042   3894    400   -409    157       C  
ATOM   1542  N   TYR A 188      19.609 -33.342 -10.741  1.00 25.32           N  
ANISOU 1542  N   TYR A 188     3977   2925   2718    160   -481    153       N  
ATOM   1543  CA  TYR A 188      18.651 -33.103  -9.690  1.00 24.94           C  
ANISOU 1543  CA  TYR A 188     3981   2872   2622     86   -484    151       C  
ATOM   1544  C   TYR A 188      19.357 -32.700  -8.393  1.00 27.87           C  
ANISOU 1544  C   TYR A 188     4362   3240   2989     71   -537    177       C  
ATOM   1545  O   TYR A 188      20.262 -33.401  -7.930  1.00 26.80           O  
ANISOU 1545  O   TYR A 188     4248   3074   2863    105   -591    202       O  
ATOM   1546  CB  TYR A 188      17.798 -34.364  -9.482  1.00 27.76           C  
ANISOU 1546  CB  TYR A 188     4431   3182   2934     56   -482    146       C  
ATOM   1547  CG  TYR A 188      16.846 -34.271  -8.304  1.00 29.49           C  
ANISOU 1547  CG  TYR A 188     4710   3396   3098    -24   -483    145       C  
ATOM   1548  CD1 TYR A 188      15.726 -33.442  -8.360  1.00 27.00           C  
ANISOU 1548  CD1 TYR A 188     4371   3123   2764    -76   -434    121       C  
ATOM   1549  CD2 TYR A 188      17.073 -35.002  -7.131  1.00 29.86           C  
ANISOU 1549  CD2 TYR A 188     4839   3397   3111    -46   -531    169       C  
ATOM   1550  CE1 TYR A 188      14.851 -33.338  -7.286  1.00 27.77           C  
ANISOU 1550  CE1 TYR A 188     4518   3222   2811   -147   -426    117       C  
ATOM   1551  CE2 TYR A 188      16.194 -34.911  -6.042  1.00 31.41           C  
ANISOU 1551  CE2 TYR A 188     5093   3591   3249   -125   -525    167       C  
ATOM   1552  CZ  TYR A 188      15.084 -34.068  -6.130  1.00 28.30           C  
ANISOU 1552  CZ  TYR A 188     4668   3245   2839   -175   -469    140       C  
ATOM   1553  OH  TYR A 188      14.202 -33.957  -5.076  1.00 22.87           O  
ANISOU 1553  OH  TYR A 188     4031   2562   2096   -250   -454    134       O  
ATOM   1554  N   MET A 189      18.943 -31.571  -7.819  1.00 27.26           N  
ANISOU 1554  N   MET A 189     4269   3192   2895     21   -525    170       N  
ATOM   1555  CA  MET A 189      19.532 -31.061  -6.569  1.00 30.05           C  
ANISOU 1555  CA  MET A 189     4636   3543   3236     -5   -575    191       C  
ATOM   1556  C   MET A 189      18.427 -30.686  -5.585  1.00 30.30           C  
ANISOU 1556  C   MET A 189     4728   3575   3211    -80   -556    177       C  
ATOM   1557  O   MET A 189      17.767 -29.662  -5.773  1.00 28.96           O  
ANISOU 1557  O   MET A 189     4527   3437   3037   -104   -511    154       O  
ATOM   1558  CB  MET A 189      20.417 -29.830  -6.827  1.00 30.35           C  
ANISOU 1558  CB  MET A 189     4592   3623   3317     13   -582    196       C  
ATOM   1559  CG  MET A 189      21.599 -30.068  -7.765  1.00 34.68           C  
ANISOU 1559  CG  MET A 189     5067   4185   3924     84   -596    210       C  
ATOM   1560  SD  MET A 189      22.178 -28.583  -8.625  1.00 38.86           S  
ANISOU 1560  SD  MET A 189     5494   4772   4499     92   -569    204       S  
ATOM   1561  CE  MET A 189      20.889 -28.379  -9.863  1.00 31.59           C  
ANISOU 1561  CE  MET A 189     4568   3864   3571     88   -488    168       C  
ATOM   1562  N   PRO A 190      18.209 -31.520  -4.545  1.00 30.85           N  
ANISOU 1562  N   PRO A 190     4884   3604   3232   -114   -587    191       N  
ATOM   1563  CA  PRO A 190      17.250 -31.207  -3.485  1.00 31.63           C  
ANISOU 1563  CA  PRO A 190     5045   3704   3271   -189   -568    179       C  
ATOM   1564  C   PRO A 190      17.845 -30.294  -2.411  1.00 33.07           C  
ANISOU 1564  C   PRO A 190     5235   3893   3438   -215   -606    192       C  
ATOM   1565  O   PRO A 190      19.046 -30.327  -2.166  1.00 35.35           O  
ANISOU 1565  O   PRO A 190     5510   4172   3751   -186   -669    220       O  
ATOM   1566  CB  PRO A 190      16.924 -32.578  -2.898  1.00 33.26           C  
ANISOU 1566  CB  PRO A 190     5346   3861   3430   -215   -591    194       C  
ATOM   1567  CG  PRO A 190      18.169 -33.374  -3.104  1.00 34.97           C  
ANISOU 1567  CG  PRO A 190     5562   4043   3682   -151   -655    226       C  
ATOM   1568  CD  PRO A 190      18.770 -32.878  -4.399  1.00 32.83           C  
ANISOU 1568  CD  PRO A 190     5188   3806   3481    -84   -635    217       C  
ATOM   1569  N   PHE A 191      17.007 -29.489  -1.770  1.00 32.76           N  
ANISOU 1569  N   PHE A 191     5218   3870   3357   -270   -569    169       N  
ATOM   1570  CA  PHE A 191      17.485 -28.537  -0.764  1.00 32.78           C  
ANISOU 1570  CA  PHE A 191     5239   3876   3339   -301   -600    175       C  
ATOM   1571  C   PHE A 191      16.656 -28.611   0.501  1.00 34.21           C  
ANISOU 1571  C   PHE A 191     5512   4044   3444   -373   -586    166       C  
ATOM   1572  O   PHE A 191      15.433 -28.760   0.445  1.00 31.60           O  
ANISOU 1572  O   PHE A 191     5199   3724   3082   -402   -523    139       O  
ATOM   1573  CB  PHE A 191      17.477 -27.105  -1.326  1.00 31.12           C  
ANISOU 1573  CB  PHE A 191     4959   3704   3163   -289   -565    152       C  
ATOM   1574  CG  PHE A 191      18.492 -26.880  -2.415  1.00 29.66           C  
ANISOU 1574  CG  PHE A 191     4686   3534   3048   -229   -585    166       C  
ATOM   1575  CD1 PHE A 191      18.179 -27.153  -3.749  1.00 28.50           C  
ANISOU 1575  CD1 PHE A 191     4484   3404   2941   -185   -543    154       C  
ATOM   1576  CD2 PHE A 191      19.769 -26.425  -2.107  1.00 28.93           C  
ANISOU 1576  CD2 PHE A 191     4569   3445   2979   -221   -646    192       C  
ATOM   1577  CE1 PHE A 191      19.116 -26.965  -4.757  1.00 26.97           C  
ANISOU 1577  CE1 PHE A 191     4213   3227   2806   -133   -555    165       C  
ATOM   1578  CE2 PHE A 191      20.719 -26.232  -3.112  1.00 29.57           C  
ANISOU 1578  CE2 PHE A 191     4564   3547   3123   -170   -659    205       C  
ATOM   1579  CZ  PHE A 191      20.391 -26.501  -4.438  1.00 28.09           C  
ANISOU 1579  CZ  PHE A 191     4324   3375   2972   -125   -610    191       C  
ATOM   1580  N   ASP A 192      17.334 -28.507   1.642  1.00 38.73           N  
ANISOU 1580  N   ASP A 192     6141   4594   3982   -403   -646    188       N  
ATOM   1581  CA  ASP A 192      16.683 -28.532   2.950  1.00 41.13           C  
ANISOU 1581  CA  ASP A 192     6542   4882   4204   -476   -637    181       C  
ATOM   1582  C   ASP A 192      15.935 -27.239   3.272  1.00 39.26           C  
ANISOU 1582  C   ASP A 192     6301   4674   3941   -509   -575    142       C  
ATOM   1583  O   ASP A 192      15.018 -27.246   4.091  1.00 40.84           O  
ANISOU 1583  O   ASP A 192     6567   4874   4076   -564   -534    122       O  
ATOM   1584  CB  ASP A 192      17.710 -28.816   4.056  1.00 46.53           C  
ANISOU 1584  CB  ASP A 192     7292   5533   4856   -497   -729    221       C  
ATOM   1585  CG  ASP A 192      18.312 -30.206   3.951  1.00 54.00           C  
ANISOU 1585  CG  ASP A 192     8263   6441   5814   -466   -791    260       C  
ATOM   1586  OD1 ASP A 192      17.547 -31.183   3.757  1.00 57.09           O  
ANISOU 1586  OD1 ASP A 192     8694   6814   6184   -476   -759    256       O  
ATOM   1587  OD2 ASP A 192      19.553 -30.320   4.069  1.00 58.61           O  
ANISOU 1587  OD2 ASP A 192     8828   7012   6427   -432   -872    295       O  
ATOM   1588  N   ASN A 193      16.342 -26.131   2.655  1.00 35.50           N  
ANISOU 1588  N   ASN A 193     5754   4221   3514   -475   -569    130       N  
ATOM   1589  CA  ASN A 193      15.680 -24.845   2.884  1.00 33.48           C  
ANISOU 1589  CA  ASN A 193     5497   3985   3239   -495   -512     91       C  
ATOM   1590  C   ASN A 193      15.764 -23.889   1.685  1.00 31.69           C  
ANISOU 1590  C   ASN A 193     5177   3784   3078   -443   -483     75       C  
ATOM   1591  O   ASN A 193      16.632 -24.033   0.819  1.00 28.68           O  
ANISOU 1591  O   ASN A 193     4734   3408   2757   -399   -518     97       O  
ATOM   1592  CB  ASN A 193      16.191 -24.176   4.170  1.00 34.39           C  
ANISOU 1592  CB  ASN A 193     5686   4080   3302   -544   -553     96       C  
ATOM   1593  CG  ASN A 193      17.646 -23.756   4.072  1.00 39.16           C  
ANISOU 1593  CG  ASN A 193     6257   4676   3945   -526   -635    128       C  
ATOM   1594  OD1 ASN A 193      17.951 -22.632   3.672  1.00 41.85           O  
ANISOU 1594  OD1 ASN A 193     6555   5030   4317   -513   -627    115       O  
ATOM   1595  ND2 ASN A 193      18.552 -24.665   4.412  1.00 41.64           N  
ANISOU 1595  ND2 ASN A 193     6590   4972   4261   -525   -713    170       N  
ATOM   1596  N   GLU A 194      14.852 -22.918   1.648  1.00 31.14           N  
ANISOU 1596  N   GLU A 194     5103   3733   2997   -448   -417     35       N  
ATOM   1597  CA  GLU A 194      14.712 -22.013   0.508  1.00 29.85           C  
ANISOU 1597  CA  GLU A 194     4862   3591   2888   -400   -382     18       C  
ATOM   1598  C   GLU A 194      15.941 -21.143   0.316  1.00 30.16           C  
ANISOU 1598  C   GLU A 194     4877   3621   2961   -389   -434     36       C  
ATOM   1599  O   GLU A 194      16.357 -20.900  -0.818  1.00 29.22           O  
ANISOU 1599  O   GLU A 194     4685   3516   2901   -347   -436     44       O  
ATOM   1600  CB  GLU A 194      13.465 -21.126   0.655  1.00 30.19           C  
ANISOU 1600  CB  GLU A 194     4914   3651   2906   -404   -305    -28       C  
ATOM   1601  CG  GLU A 194      13.051 -20.456  -0.650  1.00 28.13           C  
ANISOU 1601  CG  GLU A 194     4574   3413   2700   -350   -265    -45       C  
ATOM   1602  CD  GLU A 194      12.085 -19.298  -0.476  1.00 31.27           C  
ANISOU 1602  CD  GLU A 194     4980   3820   3081   -341   -203    -87       C  
ATOM   1603  OE1 GLU A 194      11.745 -18.669  -1.502  1.00 29.42           O  
ANISOU 1603  OE1 GLU A 194     4689   3601   2889   -294   -176    -99       O  
ATOM   1604  OE2 GLU A 194      11.656 -19.010   0.663  1.00 34.35           O  
ANISOU 1604  OE2 GLU A 194     5437   4200   3414   -377   -181   -109       O  
ATOM   1605  N   LYS A 195      16.511 -20.667   1.422  1.00 31.29           N  
ANISOU 1605  N   LYS A 195     5082   3742   3064   -432   -476     42       N  
ATOM   1606  CA  LYS A 195      17.693 -19.811   1.372  1.00 32.87           C  
ANISOU 1606  CA  LYS A 195     5265   3935   3290   -437   -530     61       C  
ATOM   1607  C   LYS A 195      18.841 -20.477   0.625  1.00 31.57           C  
ANISOU 1607  C   LYS A 195     5030   3782   3184   -405   -587    102       C  
ATOM   1608  O   LYS A 195      19.434 -19.864  -0.269  1.00 29.32           O  
ANISOU 1608  O   LYS A 195     4679   3512   2949   -379   -592    109       O  
ATOM   1609  CB  LYS A 195      18.139 -19.389   2.774  1.00 34.26           C  
ANISOU 1609  CB  LYS A 195     5527   4084   3405   -498   -576     64       C  
ATOM   1610  CG  LYS A 195      17.184 -18.424   3.461  1.00 40.71           C  
ANISOU 1610  CG  LYS A 195     6413   4887   4166   -525   -518     19       C  
ATOM   1611  CD  LYS A 195      17.880 -17.675   4.592  1.00 43.75           C  
ANISOU 1611  CD  LYS A 195     6878   5244   4502   -583   -569     23       C  
ATOM   1612  CE  LYS A 195      16.878 -17.012   5.519  1.00 46.92           C  
ANISOU 1612  CE  LYS A 195     7370   5627   4833   -613   -510    -24       C  
ATOM   1613  NZ  LYS A 195      16.367 -17.989   6.534  1.00 49.95           N  
ANISOU 1613  NZ  LYS A 195     7822   6006   5150   -651   -503    -23       N  
ATOM   1614  N   GLU A 196      19.138 -21.730   0.979  1.00 32.14           N  
ANISOU 1614  N   GLU A 196     5119   3847   3247   -405   -626    128       N  
ATOM   1615  CA  GLU A 196      20.221 -22.461   0.324  1.00 33.86           C  
ANISOU 1615  CA  GLU A 196     5271   4074   3519   -365   -679    165       C  
ATOM   1616  C   GLU A 196      19.906 -22.757  -1.147  1.00 30.92           C  
ANISOU 1616  C   GLU A 196     4821   3723   3202   -307   -629    156       C  
ATOM   1617  O   GLU A 196      20.794 -22.688  -1.994  1.00 33.17           O  
ANISOU 1617  O   GLU A 196     5033   4027   3543   -271   -650    175       O  
ATOM   1618  CB  GLU A 196      20.675 -23.704   1.128  1.00 36.46           C  
ANISOU 1618  CB  GLU A 196     5647   4381   3823   -374   -741    197       C  
ATOM   1619  CG  GLU A 196      19.756 -24.932   1.099  1.00 42.99           C  
ANISOU 1619  CG  GLU A 196     6513   5194   4627   -365   -708    191       C  
ATOM   1620  CD  GLU A 196      20.315 -26.135   1.898  1.00 49.83           C  
ANISOU 1620  CD  GLU A 196     7435   6029   5467   -373   -779    228       C  
ATOM   1621  OE1 GLU A 196      20.149 -27.301   1.442  1.00 45.64           O  
ANISOU 1621  OE1 GLU A 196     6905   5486   4950   -340   -776    238       O  
ATOM   1622  OE2 GLU A 196      20.917 -25.913   2.980  1.00 50.57           O  
ANISOU 1622  OE2 GLU A 196     7579   6109   5525   -412   -841    248       O  
ATOM   1623  N   LEU A 197      18.644 -23.045  -1.454  1.00 29.81           N  
ANISOU 1623  N   LEU A 197     4696   3586   3046   -301   -563    128       N  
ATOM   1624  CA  LEU A 197      18.217 -23.242  -2.848  1.00 28.43           C  
ANISOU 1624  CA  LEU A 197     4455   3432   2916   -252   -516    117       C  
ATOM   1625  C   LEU A 197      18.515 -21.976  -3.679  1.00 27.82           C  
ANISOU 1625  C   LEU A 197     4319   3374   2878   -235   -498    108       C  
ATOM   1626  O   LEU A 197      19.119 -22.042  -4.756  1.00 26.07           O  
ANISOU 1626  O   LEU A 197     4030   3169   2705   -196   -501    121       O  
ATOM   1627  CB  LEU A 197      16.723 -23.612  -2.910  1.00 26.22           C  
ANISOU 1627  CB  LEU A 197     4201   3156   2605   -261   -451     86       C  
ATOM   1628  CG  LEU A 197      16.082 -24.023  -4.246  1.00 27.35           C  
ANISOU 1628  CG  LEU A 197     4290   3319   2782   -221   -405     74       C  
ATOM   1629  CD1 LEU A 197      14.763 -24.744  -4.008  1.00 25.05           C  
ANISOU 1629  CD1 LEU A 197     4035   3031   2452   -245   -361     53       C  
ATOM   1630  CD2 LEU A 197      15.858 -22.832  -5.186  1.00 26.01           C  
ANISOU 1630  CD2 LEU A 197     4065   3173   2645   -195   -368     56       C  
ATOM   1631  N   LEU A 198      18.108 -20.825  -3.154  1.00 26.68           N  
ANISOU 1631  N   LEU A 198     4208   3224   2706   -265   -479     87       N  
ATOM   1632  CA  LEU A 198      18.269 -19.570  -3.862  1.00 27.24           C  
ANISOU 1632  CA  LEU A 198     4241   3304   2805   -253   -461     78       C  
ATOM   1633  C   LEU A 198      19.725 -19.140  -3.983  1.00 28.52           C  
ANISOU 1633  C   LEU A 198     4368   3470   2998   -261   -518    108       C  
ATOM   1634  O   LEU A 198      20.127 -18.621  -5.025  1.00 28.52           O  
ANISOU 1634  O   LEU A 198     4310   3486   3039   -239   -507    114       O  
ATOM   1635  CB  LEU A 198      17.413 -18.476  -3.226  1.00 27.56           C  
ANISOU 1635  CB  LEU A 198     4337   3330   2806   -278   -425     44       C  
ATOM   1636  CG  LEU A 198      15.910 -18.593  -3.505  1.00 27.85           C  
ANISOU 1636  CG  LEU A 198     4376   3377   2827   -257   -354     10       C  
ATOM   1637  CD1 LEU A 198      15.165 -17.487  -2.802  1.00 26.47           C  
ANISOU 1637  CD1 LEU A 198     4255   3187   2615   -274   -319    -24       C  
ATOM   1638  CD2 LEU A 198      15.609 -18.548  -5.007  1.00 27.60           C  
ANISOU 1638  CD2 LEU A 198     4273   3368   2845   -208   -323      8       C  
ATOM   1639  N   MET A 199      20.511 -19.364  -2.932  1.00 30.17           N  
ANISOU 1639  N   MET A 199     4611   3668   3186   -297   -579    130       N  
ATOM   1640  CA  MET A 199      21.932 -19.025  -2.951  1.00 31.43           C  
ANISOU 1640  CA  MET A 199     4729   3839   3375   -310   -640    162       C  
ATOM   1641  C   MET A 199      22.676 -19.879  -3.971  1.00 30.84           C  
ANISOU 1641  C   MET A 199     4569   3792   3357   -260   -651    187       C  
ATOM   1642  O   MET A 199      23.496 -19.366  -4.737  1.00 30.29           O  
ANISOU 1642  O   MET A 199     4432   3746   3329   -251   -659    201       O  
ATOM   1643  CB  MET A 199      22.568 -19.175  -1.558  1.00 32.90           C  
ANISOU 1643  CB  MET A 199     4971   4009   3522   -359   -710    181       C  
ATOM   1644  CG  MET A 199      22.235 -18.033  -0.608  1.00 34.53           C  
ANISOU 1644  CG  MET A 199     5256   4189   3675   -416   -709    160       C  
ATOM   1645  SD  MET A 199      23.093 -18.109   0.977  1.00 40.48           S  
ANISOU 1645  SD  MET A 199     6078   4924   4379   -482   -800    185       S  
ATOM   1646  CE  MET A 199      22.377 -19.574   1.732  1.00 34.70           C  
ANISOU 1646  CE  MET A 199     5405   4175   3604   -473   -799    186       C  
ATOM   1647  N   GLU A 200      22.373 -21.176  -3.981  1.00 29.11           N  
ANISOU 1647  N   GLU A 200     4356   3567   3136   -228   -649    191       N  
ATOM   1648  CA  GLU A 200      22.938 -22.086  -4.969  1.00 30.85           C  
ANISOU 1648  CA  GLU A 200     4508   3808   3407   -171   -651    208       C  
ATOM   1649  C   GLU A 200      22.514 -21.708  -6.395  1.00 28.79           C  
ANISOU 1649  C   GLU A 200     4194   3566   3178   -138   -587    190       C  
ATOM   1650  O   GLU A 200      23.344 -21.707  -7.307  1.00 28.55           O  
ANISOU 1650  O   GLU A 200     4091   3563   3193   -108   -589    204       O  
ATOM   1651  CB  GLU A 200      22.573 -23.539  -4.647  1.00 32.99           C  
ANISOU 1651  CB  GLU A 200     4817   4057   3661   -148   -660    212       C  
ATOM   1652  CG  GLU A 200      23.163 -24.571  -5.607  1.00 40.12           C  
ANISOU 1652  CG  GLU A 200     5662   4972   4612    -84   -663    227       C  
ATOM   1653  CD  GLU A 200      24.686 -24.558  -5.653  1.00 50.14           C  
ANISOU 1653  CD  GLU A 200     6863   6265   5924    -63   -721    260       C  
ATOM   1654  OE1 GLU A 200      25.325 -24.516  -4.571  1.00 52.18           O  
ANISOU 1654  OE1 GLU A 200     7143   6517   6167    -92   -787    283       O  
ATOM   1655  OE2 GLU A 200      25.241 -24.594  -6.779  1.00 54.13           O  
ANISOU 1655  OE2 GLU A 200     7290   6799   6477    -19   -699    264       O  
ATOM   1656  N   TYR A 201      21.241 -21.368  -6.583  1.00 26.62           N  
ANISOU 1656  N   TYR A 201     3954   3282   2878   -144   -532    159       N  
ATOM   1657  CA  TYR A 201      20.768 -20.943  -7.905  1.00 26.08           C  
ANISOU 1657  CA  TYR A 201     3843   3231   2835   -115   -478    143       C  
ATOM   1658  C   TYR A 201      21.558 -19.738  -8.422  1.00 26.69           C  
ANISOU 1658  C   TYR A 201     3878   3325   2940   -127   -483    153       C  
ATOM   1659  O   TYR A 201      22.016 -19.733  -9.566  1.00 27.45           O  
ANISOU 1659  O   TYR A 201     3914   3445   3072    -99   -466    161       O  
ATOM   1660  CB  TYR A 201      19.266 -20.650  -7.907  1.00 24.48           C  
ANISOU 1660  CB  TYR A 201     3681   3019   2602   -121   -425    109       C  
ATOM   1661  CG  TYR A 201      18.711 -20.423  -9.299  1.00 26.19           C  
ANISOU 1661  CG  TYR A 201     3856   3252   2842    -87   -376     96       C  
ATOM   1662  CD1 TYR A 201      18.810 -21.419 -10.279  1.00 24.09           C  
ANISOU 1662  CD1 TYR A 201     3553   3000   2600    -49   -364    102       C  
ATOM   1663  CD2 TYR A 201      18.093 -19.213  -9.644  1.00 24.14           C  
ANISOU 1663  CD2 TYR A 201     3601   2994   2579    -91   -345     78       C  
ATOM   1664  CE1 TYR A 201      18.319 -21.218 -11.563  1.00 22.26           C  
ANISOU 1664  CE1 TYR A 201     3289   2784   2384    -22   -324     91       C  
ATOM   1665  CE2 TYR A 201      17.591 -19.008 -10.936  1.00 22.87           C  
ANISOU 1665  CE2 TYR A 201     3404   2848   2437    -59   -307     70       C  
ATOM   1666  CZ  TYR A 201      17.705 -20.018 -11.884  1.00 24.72           C  
ANISOU 1666  CZ  TYR A 201     3603   3099   2692    -28   -297     77       C  
ATOM   1667  OH  TYR A 201      17.209 -19.841 -13.157  1.00 25.13           O  
ANISOU 1667  OH  TYR A 201     3627   3165   2757     -2   -264     69       O  
ATOM   1668  N   LEU A 202      21.741 -18.734  -7.572  1.00 24.32           N  
ANISOU 1668  N   LEU A 202     3613   3010   2616   -173   -506    152       N  
ATOM   1669  CA  LEU A 202      22.516 -17.561  -7.954  1.00 27.71           C  
ANISOU 1669  CA  LEU A 202     4013   3450   3064   -198   -517    163       C  
ATOM   1670  C   LEU A 202      23.964 -17.902  -8.321  1.00 28.21           C  
ANISOU 1670  C   LEU A 202     4002   3547   3170   -193   -556    197       C  
ATOM   1671  O   LEU A 202      24.487 -17.380  -9.307  1.00 28.99           O  
ANISOU 1671  O   LEU A 202     4046   3669   3298   -189   -539    206       O  
ATOM   1672  CB  LEU A 202      22.472 -16.494  -6.863  1.00 27.18           C  
ANISOU 1672  CB  LEU A 202     4012   3356   2959   -254   -540    156       C  
ATOM   1673  CG  LEU A 202      21.156 -15.726  -6.749  1.00 29.85           C  
ANISOU 1673  CG  LEU A 202     4412   3665   3264   -254   -491    120       C  
ATOM   1674  CD1 LEU A 202      21.195 -14.834  -5.513  1.00 29.61           C  
ANISOU 1674  CD1 LEU A 202     4458   3603   3191   -308   -517    110       C  
ATOM   1675  CD2 LEU A 202      20.867 -14.906  -8.013  1.00 25.87           C  
ANISOU 1675  CD2 LEU A 202     3879   3166   2784   -231   -450    112       C  
ATOM   1676  N   ASN A 203      24.600 -18.774  -7.537  1.00 28.10           N  
ANISOU 1676  N   ASN A 203     3985   3537   3157   -192   -607    216       N  
ATOM   1677  CA  ASN A 203      25.950 -19.238  -7.863  1.00 29.47           C  
ANISOU 1677  CA  ASN A 203     4076   3746   3373   -174   -644    248       C  
ATOM   1678  C   ASN A 203      25.994 -19.971  -9.202  1.00 28.88           C  
ANISOU 1678  C   ASN A 203     3940   3696   3338   -111   -600    246       C  
ATOM   1679  O   ASN A 203      26.918 -19.782 -10.000  1.00 29.77           O  
ANISOU 1679  O   ASN A 203     3976   3847   3489   -100   -596    262       O  
ATOM   1680  CB  ASN A 203      26.515 -20.123  -6.752  1.00 30.07           C  
ANISOU 1680  CB  ASN A 203     4166   3816   3441   -175   -711    270       C  
ATOM   1681  CG  ASN A 203      26.994 -19.323  -5.554  1.00 33.58           C  
ANISOU 1681  CG  ASN A 203     4649   4253   3857   -244   -771    282       C  
ATOM   1682  OD1 ASN A 203      27.002 -19.822  -4.433  1.00 36.73           O  
ANISOU 1682  OD1 ASN A 203     5100   4631   4226   -259   -819    291       O  
ATOM   1683  ND2 ASN A 203      27.413 -18.085  -5.788  1.00 33.27           N  
ANISOU 1683  ND2 ASN A 203     4590   4227   3823   -289   -771    284       N  
ATOM   1684  N   PHE A 204      24.977 -20.793  -9.435  1.00 26.00           N  
ANISOU 1684  N   PHE A 204     3612   3310   2958    -75   -564    226       N  
ATOM   1685  CA  PHE A 204      24.801 -21.504 -10.697  1.00 26.72           C  
ANISOU 1685  CA  PHE A 204     3664   3414   3074    -19   -518    218       C  
ATOM   1686  C   PHE A 204      24.617 -20.501 -11.848  1.00 24.94           C  
ANISOU 1686  C   PHE A 204     3409   3207   2860    -25   -469    208       C  
ATOM   1687  O   PHE A 204      25.300 -20.591 -12.867  1.00 24.66           O  
ANISOU 1687  O   PHE A 204     3310   3202   2857      0   -449    216       O  
ATOM   1688  CB  PHE A 204      23.631 -22.490 -10.555  1.00 23.74           C  
ANISOU 1688  CB  PHE A 204     3346   3006   2669      3   -496    197       C  
ATOM   1689  CG  PHE A 204      23.040 -22.946 -11.847  1.00 27.85           C  
ANISOU 1689  CG  PHE A 204     3850   3531   3199     44   -441    180       C  
ATOM   1690  CD1 PHE A 204      23.521 -24.087 -12.481  1.00 29.27           C  
ANISOU 1690  CD1 PHE A 204     4001   3717   3403     97   -437    185       C  
ATOM   1691  CD2 PHE A 204      21.966 -22.260 -12.416  1.00 24.35           C  
ANISOU 1691  CD2 PHE A 204     3426   3086   2739     31   -395    157       C  
ATOM   1692  CE1 PHE A 204      22.959 -24.523 -13.670  1.00 27.08           C  
ANISOU 1692  CE1 PHE A 204     3719   3441   3128    129   -388    167       C  
ATOM   1693  CE2 PHE A 204      21.408 -22.690 -13.604  1.00 24.87           C  
ANISOU 1693  CE2 PHE A 204     3481   3158   2810     64   -351    143       C  
ATOM   1694  CZ  PHE A 204      21.908 -23.823 -14.234  1.00 24.65           C  
ANISOU 1694  CZ  PHE A 204     3429   3135   2802    109   -347    147       C  
ATOM   1695  N   TRP A 205      23.721 -19.537 -11.657  1.00 24.76           N  
ANISOU 1695  N   TRP A 205     3436   3164   2808    -59   -450    190       N  
ATOM   1696  CA  TRP A 205      23.468 -18.468 -12.630  1.00 26.30           C  
ANISOU 1696  CA  TRP A 205     3620   3366   3007    -69   -411    183       C  
ATOM   1697  C   TRP A 205      24.772 -17.756 -12.973  1.00 28.38           C  
ANISOU 1697  C   TRP A 205     3825   3659   3297    -95   -428    208       C  
ATOM   1698  O   TRP A 205      25.040 -17.474 -14.137  1.00 27.91           O  
ANISOU 1698  O   TRP A 205     3724   3623   3256    -84   -395    212       O  
ATOM   1699  CB  TRP A 205      22.455 -17.472 -12.055  1.00 24.35           C  
ANISOU 1699  CB  TRP A 205     3441   3087   2725   -100   -402    163       C  
ATOM   1700  CG  TRP A 205      21.899 -16.426 -13.011  1.00 21.88           C  
ANISOU 1700  CG  TRP A 205     3135   2770   2410   -100   -363    152       C  
ATOM   1701  CD1 TRP A 205      22.499 -15.254 -13.395  1.00 23.09           C  
ANISOU 1701  CD1 TRP A 205     3279   2925   2570   -132   -366    165       C  
ATOM   1702  CD2 TRP A 205      20.611 -16.438 -13.645  1.00 20.14           C  
ANISOU 1702  CD2 TRP A 205     2935   2539   2177    -70   -320    129       C  
ATOM   1703  NE1 TRP A 205      21.667 -14.546 -14.238  1.00 21.20           N  
ANISOU 1703  NE1 TRP A 205     3060   2672   2322   -119   -329    152       N  
ATOM   1704  CE2 TRP A 205      20.505 -15.251 -14.406  1.00 21.84           C  
ANISOU 1704  CE2 TRP A 205     3156   2750   2394    -79   -302    130       C  
ATOM   1705  CE3 TRP A 205      19.538 -17.344 -13.652  1.00 23.30           C  
ANISOU 1705  CE3 TRP A 205     3351   2937   2565    -40   -299    109       C  
ATOM   1706  CZ2 TRP A 205      19.365 -14.943 -15.164  1.00 24.35           C  
ANISOU 1706  CZ2 TRP A 205     3491   3059   2702    -51   -267    113       C  
ATOM   1707  CZ3 TRP A 205      18.404 -17.038 -14.414  1.00 23.51           C  
ANISOU 1707  CZ3 TRP A 205     3387   2962   2583    -18   -262     91       C  
ATOM   1708  CH2 TRP A 205      18.327 -15.842 -15.148  1.00 22.37           C  
ANISOU 1708  CH2 TRP A 205     3246   2813   2442    -20   -248     93       C  
ATOM   1709  N   GLN A 206      25.587 -17.507 -11.951  1.00 30.29           N  
ANISOU 1709  N   GLN A 206     4065   3904   3539   -133   -482    226       N  
ATOM   1710  CA  GLN A 206      26.894 -16.876 -12.116  1.00 33.45           C  
ANISOU 1710  CA  GLN A 206     4404   4339   3964   -169   -507    252       C  
ATOM   1711  C   GLN A 206      27.844 -17.675 -13.012  1.00 32.48           C  
ANISOU 1711  C   GLN A 206     4188   4266   3885   -126   -494    269       C  
ATOM   1712  O   GLN A 206      28.534 -17.094 -13.848  1.00 31.10           O  
ANISOU 1712  O   GLN A 206     3959   4126   3732   -143   -474    281       O  
ATOM   1713  CB  GLN A 206      27.548 -16.654 -10.751  1.00 36.56           C  
ANISOU 1713  CB  GLN A 206     4814   4729   4348   -218   -575    269       C  
ATOM   1714  CG  GLN A 206      28.095 -15.255 -10.539  1.00 45.47           C  
ANISOU 1714  CG  GLN A 206     5951   5859   5468   -293   -597    281       C  
ATOM   1715  CD  GLN A 206      27.005 -14.258 -10.146  1.00 50.89           C  
ANISOU 1715  CD  GLN A 206     6737   6491   6109   -323   -580    255       C  
ATOM   1716  OE1 GLN A 206      26.080 -13.975 -10.922  1.00 51.33           O  
ANISOU 1716  OE1 GLN A 206     6817   6527   6157   -296   -527    235       O  
ATOM   1717  NE2 GLN A 206      27.115 -13.719  -8.934  1.00 48.12           N  
ANISOU 1717  NE2 GLN A 206     6444   6113   5727   -377   -626    256       N  
ATOM   1718  N   GLN A 207      27.893 -18.993 -12.828  1.00 32.30           N  
ANISOU 1718  N   GLN A 207     4153   4246   3876    -72   -505    268       N  
ATOM   1719  CA  GLN A 207      28.739 -19.854 -13.668  1.00 35.56           C  
ANISOU 1719  CA  GLN A 207     4483   4700   4329    -17   -488    278       C  
ATOM   1720  C   GLN A 207      28.170 -20.036 -15.068  1.00 33.76           C  
ANISOU 1720  C   GLN A 207     4251   4475   4103     20   -417    259       C  
ATOM   1721  O   GLN A 207      28.916 -20.190 -16.030  1.00 35.98           O  
ANISOU 1721  O   GLN A 207     4462   4796   4411     44   -387    266       O  
ATOM   1722  CB  GLN A 207      28.969 -21.227 -13.029  1.00 38.07           C  
ANISOU 1722  CB  GLN A 207     4799   5008   4657     35   -524    284       C  
ATOM   1723  CG  GLN A 207      30.283 -21.356 -12.257  1.00 52.25           C  
ANISOU 1723  CG  GLN A 207     6534   6837   6482     28   -591    316       C  
ATOM   1724  CD  GLN A 207      31.511 -21.433 -13.172  1.00 61.96           C  
ANISOU 1724  CD  GLN A 207     7648   8131   7761     56   -573    331       C  
ATOM   1725  OE1 GLN A 207      31.673 -22.388 -13.940  1.00 64.89           O  
ANISOU 1725  OE1 GLN A 207     7986   8515   8156    129   -539    324       O  
ATOM   1726  NE2 GLN A 207      32.384 -20.426 -13.085  1.00 63.62           N  
ANISOU 1726  NE2 GLN A 207     7801   8385   7985     -3   -593    352       N  
ATOM   1727  N   LYS A 208      26.847 -20.029 -15.174  1.00 30.58           N  
ANISOU 1727  N   LYS A 208     3920   4032   3667     24   -391    235       N  
ATOM   1728  CA  LYS A 208      26.179 -20.328 -16.434  1.00 28.95           C  
ANISOU 1728  CA  LYS A 208     3720   3825   3456     59   -332    216       C  
ATOM   1729  C   LYS A 208      25.159 -19.241 -16.713  1.00 27.82           C  
ANISOU 1729  C   LYS A 208     3627   3659   3283     24   -308    203       C  
ATOM   1730  O   LYS A 208      23.956 -19.493 -16.716  1.00 29.40           O  
ANISOU 1730  O   LYS A 208     3881   3831   3460     37   -293    182       O  
ATOM   1731  CB  LYS A 208      25.507 -21.702 -16.367  1.00 27.48           C  
ANISOU 1731  CB  LYS A 208     3567   3612   3261    110   -327    199       C  
ATOM   1732  CG  LYS A 208      26.471 -22.837 -16.072  1.00 27.78           C  
ANISOU 1732  CG  LYS A 208     3565   3662   3327    156   -353    212       C  
ATOM   1733  CD  LYS A 208      25.739 -24.130 -15.754  1.00 31.09           C  
ANISOU 1733  CD  LYS A 208     4041   4042   3729    194   -359    198       C  
ATOM   1734  CE  LYS A 208      26.704 -25.173 -15.176  1.00 30.95           C  
ANISOU 1734  CE  LYS A 208     3999   4025   3737    238   -401    215       C  
ATOM   1735  NZ  LYS A 208      27.723 -25.589 -16.184  1.00 31.58           N  
ANISOU 1735  NZ  LYS A 208     4003   4142   3855    292   -374    219       N  
ATOM   1736  N   THR A 209      25.661 -18.027 -16.928  1.00 27.59           N  
ANISOU 1736  N   THR A 209     3582   3644   3258    -21   -308    216       N  
ATOM   1737  CA  THR A 209      24.833 -16.849 -17.129  1.00 26.99           C  
ANISOU 1737  CA  THR A 209     3557   3541   3155    -53   -293    207       C  
ATOM   1738  C   THR A 209      24.139 -16.895 -18.483  1.00 25.88           C  
ANISOU 1738  C   THR A 209     3424   3403   3007    -25   -243    195       C  
ATOM   1739  O   THR A 209      24.796 -17.008 -19.513  1.00 26.41           O  
ANISOU 1739  O   THR A 209     3444   3502   3088    -15   -215    204       O  
ATOM   1740  CB  THR A 209      25.662 -15.564 -17.025  1.00 27.26           C  
ANISOU 1740  CB  THR A 209     3580   3586   3193   -115   -310    228       C  
ATOM   1741  OG1 THR A 209      26.495 -15.634 -15.862  1.00 29.88           O  
ANISOU 1741  OG1 THR A 209     3894   3925   3535   -143   -362    243       O  
ATOM   1742  CG2 THR A 209      24.750 -14.329 -16.934  1.00 24.60           C  
ANISOU 1742  CG2 THR A 209     3316   3206   2825   -145   -306    217       C  
ATOM   1743  N   PRO A 210      22.802 -16.816 -18.477  1.00 24.73           N  
ANISOU 1743  N   PRO A 210     3333   3226   2836    -11   -231    174       N  
ATOM   1744  CA  PRO A 210      22.042 -16.796 -19.729  1.00 23.62           C  
ANISOU 1744  CA  PRO A 210     3203   3087   2684     13   -192    164       C  
ATOM   1745  C   PRO A 210      22.435 -15.621 -20.618  1.00 23.50           C  
ANISOU 1745  C   PRO A 210     3185   3079   2667    -16   -176    179       C  
ATOM   1746  O   PRO A 210      22.728 -14.533 -20.121  1.00 23.39           O  
ANISOU 1746  O   PRO A 210     3189   3050   2648    -58   -196    190       O  
ATOM   1747  CB  PRO A 210      20.602 -16.636 -19.259  1.00 21.38           C  
ANISOU 1747  CB  PRO A 210     2975   2772   2377     21   -194    142       C  
ATOM   1748  CG  PRO A 210      20.598 -17.258 -17.861  1.00 24.86           C  
ANISOU 1748  CG  PRO A 210     3429   3201   2817     17   -224    136       C  
ATOM   1749  CD  PRO A 210      21.929 -16.884 -17.285  1.00 25.34           C  
ANISOU 1749  CD  PRO A 210     3462   3272   2894    -15   -254    158       C  
ATOM   1750  N   VAL A 211      22.473 -15.868 -21.920  1.00 21.88           N  
ANISOU 1750  N   VAL A 211     2962   2893   2459      2   -140    180       N  
ATOM   1751  CA  VAL A 211      22.565 -14.811 -22.907  1.00 22.56           C  
ANISOU 1751  CA  VAL A 211     3060   2980   2532    -23   -121    194       C  
ATOM   1752  C   VAL A 211      21.152 -14.551 -23.401  1.00 24.59           C  
ANISOU 1752  C   VAL A 211     3370   3209   2763     -1   -113    179       C  
ATOM   1753  O   VAL A 211      20.654 -13.423 -23.334  1.00 24.67           O  
ANISOU 1753  O   VAL A 211     3425   3191   2760    -18   -125    183       O  
ATOM   1754  CB  VAL A 211      23.462 -15.226 -24.083  1.00 23.21           C  
ANISOU 1754  CB  VAL A 211     3094   3103   2620    -19    -84    204       C  
ATOM   1755  CG1 VAL A 211      23.334 -14.229 -25.244  1.00 18.10           C  
ANISOU 1755  CG1 VAL A 211     2474   2453   1949    -45    -60    217       C  
ATOM   1756  CG2 VAL A 211      24.910 -15.352 -23.605  1.00 19.47           C  
ANISOU 1756  CG2 VAL A 211     2556   2665   2176    -41    -92    221       C  
ATOM   1757  N   ILE A 212      20.523 -15.610 -23.908  1.00 24.23           N  
ANISOU 1757  N   ILE A 212     3321   3173   2712     39    -97    162       N  
ATOM   1758  CA  ILE A 212      19.117 -15.582 -24.260  1.00 23.27           C  
ANISOU 1758  CA  ILE A 212     3238   3035   2570     62    -96    147       C  
ATOM   1759  C   ILE A 212      18.400 -16.272 -23.118  1.00 23.87           C  
ANISOU 1759  C   ILE A 212     3321   3099   2649     78   -114    127       C  
ATOM   1760  O   ILE A 212      18.725 -17.413 -22.770  1.00 23.94           O  
ANISOU 1760  O   ILE A 212     3309   3119   2668     91   -113    120       O  
ATOM   1761  CB  ILE A 212      18.815 -16.313 -25.592  1.00 22.44           C  
ANISOU 1761  CB  ILE A 212     3130   2948   2449     85    -68    141       C  
ATOM   1762  CG1 ILE A 212      19.705 -15.795 -26.739  1.00 22.42           C  
ANISOU 1762  CG1 ILE A 212     3117   2962   2439     66    -42    161       C  
ATOM   1763  CG2 ILE A 212      17.319 -16.215 -25.933  1.00 20.55           C  
ANISOU 1763  CG2 ILE A 212     2925   2695   2189    105    -75    128       C  
ATOM   1764  CD1 ILE A 212      19.445 -14.338 -27.194  1.00 19.81           C  
ANISOU 1764  CD1 ILE A 212     2826   2612   2091     40    -50    179       C  
ATOM   1765  N   LEU A 213      17.448 -15.565 -22.520  1.00 22.08           N  
ANISOU 1765  N   LEU A 213     3128   2849   2413     78   -128    118       N  
ATOM   1766  CA  LEU A 213      16.645 -16.131 -21.454  1.00 22.98           C  
ANISOU 1766  CA  LEU A 213     3252   2955   2525     88   -139     98       C  
ATOM   1767  C   LEU A 213      15.200 -16.279 -21.905  1.00 23.23           C  
ANISOU 1767  C   LEU A 213     3296   2989   2540    113   -131     81       C  
ATOM   1768  O   LEU A 213      14.545 -15.308 -22.256  1.00 24.80           O  
ANISOU 1768  O   LEU A 213     3513   3177   2732    121   -133     81       O  
ATOM   1769  CB  LEU A 213      16.738 -15.275 -20.189  1.00 20.98           C  
ANISOU 1769  CB  LEU A 213     3023   2677   2272     67   -159     97       C  
ATOM   1770  CG  LEU A 213      16.038 -15.806 -18.933  1.00 19.73           C  
ANISOU 1770  CG  LEU A 213     2879   2512   2106     69   -167     76       C  
ATOM   1771  CD1 LEU A 213      16.596 -17.163 -18.534  1.00 18.16           C  
ANISOU 1771  CD1 LEU A 213     2659   2326   1914     67   -173     78       C  
ATOM   1772  CD2 LEU A 213      16.196 -14.785 -17.792  1.00 17.73           C  
ANISOU 1772  CD2 LEU A 213     2660   2230   1847     45   -184     75       C  
ATOM   1773  N   THR A 214      14.703 -17.505 -21.893  1.00 23.83           N  
ANISOU 1773  N   THR A 214     3363   3080   2612    123   -125     67       N  
ATOM   1774  CA  THR A 214      13.365 -17.742 -22.391  1.00 22.90           C  
ANISOU 1774  CA  THR A 214     3248   2973   2479    139   -120     52       C  
ATOM   1775  C   THR A 214      12.602 -18.728 -21.512  1.00 24.07           C  
ANISOU 1775  C   THR A 214     3396   3128   2620    135   -121     33       C  
ATOM   1776  O   THR A 214      13.100 -19.144 -20.466  1.00 23.50           O  
ANISOU 1776  O   THR A 214     3330   3046   2553    121   -127     31       O  
ATOM   1777  CB  THR A 214      13.368 -18.116 -23.907  1.00 23.56           C  
ANISOU 1777  CB  THR A 214     3327   3073   2553    149   -109     59       C  
ATOM   1778  OG1 THR A 214      12.028 -18.126 -24.394  1.00 22.47           O  
ANISOU 1778  OG1 THR A 214     3190   2948   2400    161   -113     48       O  
ATOM   1779  CG2 THR A 214      14.024 -19.476 -24.177  1.00 22.54           C  
ANISOU 1779  CG2 THR A 214     3189   2952   2424    148    -98     56       C  
ATOM   1780  N   GLY A 215      11.385 -19.065 -21.935  1.00 24.94           N  
ANISOU 1780  N   GLY A 215     3502   3257   2718    142   -117     20       N  
ATOM   1781  CA  GLY A 215      10.455 -19.877 -21.155  1.00 25.39           C  
ANISOU 1781  CA  GLY A 215     3558   3325   2764    130   -115      1       C  
ATOM   1782  C   GLY A 215       9.037 -19.423 -21.441  1.00 26.74           C  
ANISOU 1782  C   GLY A 215     3712   3519   2927    142   -113    -11       C  
ATOM   1783  O   GLY A 215       8.803 -18.647 -22.370  1.00 28.87           O  
ANISOU 1783  O   GLY A 215     3976   3794   3199    164   -118     -3       O  
ATOM   1784  N   TRP A 216       8.082 -19.900 -20.653  1.00 26.14           N  
ANISOU 1784  N   TRP A 216     3628   3461   2841    129   -106    -29       N  
ATOM   1785  CA  TRP A 216       6.692 -19.509 -20.849  1.00 26.09           C  
ANISOU 1785  CA  TRP A 216     3593   3487   2831    142   -103    -42       C  
ATOM   1786  C   TRP A 216       6.249 -18.518 -19.764  1.00 24.65           C  
ANISOU 1786  C   TRP A 216     3409   3302   2655    158    -92    -54       C  
ATOM   1787  O   TRP A 216       6.221 -18.859 -18.591  1.00 25.04           O  
ANISOU 1787  O   TRP A 216     3469   3348   2696    136    -80    -66       O  
ATOM   1788  CB  TRP A 216       5.787 -20.747 -20.899  1.00 25.97           C  
ANISOU 1788  CB  TRP A 216     3563   3506   2800    112   -100    -54       C  
ATOM   1789  CG  TRP A 216       4.469 -20.479 -21.589  1.00 30.54           C  
ANISOU 1789  CG  TRP A 216     4101   4127   3375    125   -105    -61       C  
ATOM   1790  CD1 TRP A 216       3.272 -20.208 -20.989  1.00 30.48           C  
ANISOU 1790  CD1 TRP A 216     4056   4157   3369    128    -94    -78       C  
ATOM   1791  CD2 TRP A 216       4.227 -20.438 -23.005  1.00 29.12           C  
ANISOU 1791  CD2 TRP A 216     3910   3961   3192    137   -124    -50       C  
ATOM   1792  NE1 TRP A 216       2.300 -20.008 -21.942  1.00 34.07           N  
ANISOU 1792  NE1 TRP A 216     4470   4650   3824    144   -109    -77       N  
ATOM   1793  CE2 TRP A 216       2.858 -20.141 -23.186  1.00 31.41           C  
ANISOU 1793  CE2 TRP A 216     4154   4298   3483    148   -131    -59       C  
ATOM   1794  CE3 TRP A 216       5.033 -20.624 -24.136  1.00 31.00           C  
ANISOU 1794  CE3 TRP A 216     4175   4181   3425    139   -136    -34       C  
ATOM   1795  CZ2 TRP A 216       2.273 -20.025 -24.454  1.00 32.15           C  
ANISOU 1795  CZ2 TRP A 216     4228   4418   3571    159   -156    -49       C  
ATOM   1796  CZ3 TRP A 216       4.447 -20.507 -25.404  1.00 33.83           C  
ANISOU 1796  CZ3 TRP A 216     4521   4561   3772    147   -155    -27       C  
ATOM   1797  CH2 TRP A 216       3.081 -20.213 -25.547  1.00 32.13           C  
ANISOU 1797  CH2 TRP A 216     4262   4390   3558    156   -169    -33       C  
ATOM   1798  N   ASN A 217       5.931 -17.283 -20.161  1.00 25.97           N  
ANISOU 1798  N   ASN A 217     3570   3464   2832    197    -97    -52       N  
ATOM   1799  CA  ASN A 217       5.599 -16.208 -19.205  1.00 25.55           C  
ANISOU 1799  CA  ASN A 217     3526   3398   2784    221    -86    -66       C  
ATOM   1800  C   ASN A 217       6.719 -15.845 -18.234  1.00 24.70           C  
ANISOU 1800  C   ASN A 217     3463   3247   2676    203    -84    -63       C  
ATOM   1801  O   ASN A 217       6.455 -15.373 -17.131  1.00 26.32           O  
ANISOU 1801  O   ASN A 217     3684   3443   2875    206    -70    -80       O  
ATOM   1802  CB  ASN A 217       4.358 -16.564 -18.386  1.00 29.40           C  
ANISOU 1802  CB  ASN A 217     3982   3925   3263    218    -63    -92       C  
ATOM   1803  CG  ASN A 217       3.089 -16.213 -19.084  1.00 34.41           C  
ANISOU 1803  CG  ASN A 217     4567   4600   3905    255    -65    -99       C  
ATOM   1804  OD1 ASN A 217       2.890 -15.069 -19.495  1.00 38.23           O  
ANISOU 1804  OD1 ASN A 217     5053   5071   4403    304    -74    -95       O  
ATOM   1805  ND2 ASN A 217       2.207 -17.197 -19.229  1.00 38.99           N  
ANISOU 1805  ND2 ASN A 217     5106   5232   4478    230    -59   -108       N  
ATOM   1806  N   VAL A 218       7.964 -16.077 -18.623  1.00 23.50           N  
ANISOU 1806  N   VAL A 218     3330   3073   2528    184    -99    -41       N  
ATOM   1807  CA  VAL A 218       9.073 -15.761 -17.736  1.00 26.22           C  
ANISOU 1807  CA  VAL A 218     3709   3382   2873    163   -105    -35       C  
ATOM   1808  C   VAL A 218       9.215 -14.262 -17.492  1.00 27.49           C  
ANISOU 1808  C   VAL A 218     3901   3509   3037    182   -108    -35       C  
ATOM   1809  O   VAL A 218       9.689 -13.857 -16.433  1.00 29.45           O  
ANISOU 1809  O   VAL A 218     4182   3731   3278    164   -109    -41       O  
ATOM   1810  CB  VAL A 218      10.410 -16.374 -18.211  1.00 25.59           C  
ANISOU 1810  CB  VAL A 218     3631   3293   2800    140   -119    -12       C  
ATOM   1811  CG1 VAL A 218      10.367 -17.897 -18.064  1.00 23.83           C  
ANISOU 1811  CG1 VAL A 218     3395   3089   2569    120   -116    -16       C  
ATOM   1812  CG2 VAL A 218      10.733 -15.953 -19.657  1.00 25.42           C  
ANISOU 1812  CG2 VAL A 218     3599   3272   2787    157   -125      7       C  
ATOM   1813  N   GLU A 219       8.786 -13.443 -18.451  1.00 28.11           N  
ANISOU 1813  N   GLU A 219     3975   3583   3121    217   -113    -29       N  
ATOM   1814  CA  GLU A 219       8.890 -11.989 -18.299  1.00 33.69           C  
ANISOU 1814  CA  GLU A 219     4723   4249   3830    238   -119    -28       C  
ATOM   1815  C   GLU A 219       7.831 -11.437 -17.347  1.00 34.64           C  
ANISOU 1815  C   GLU A 219     4852   4365   3943    269   -100    -58       C  
ATOM   1816  O   GLU A 219       8.106 -10.529 -16.567  1.00 34.87           O  
ANISOU 1816  O   GLU A 219     4930   4355   3966    270    -99    -67       O  
ATOM   1817  CB  GLU A 219       8.818 -11.267 -19.649  1.00 34.73           C  
ANISOU 1817  CB  GLU A 219     4858   4371   3968    265   -133     -8       C  
ATOM   1818  CG  GLU A 219       9.223  -9.793 -19.555  1.00 42.31           C  
ANISOU 1818  CG  GLU A 219     5875   5276   4925    276   -144      0       C  
ATOM   1819  CD  GLU A 219       9.012  -9.021 -20.845  1.00 48.20           C  
ANISOU 1819  CD  GLU A 219     6634   6007   5672    305   -161     21       C  
ATOM   1820  OE1 GLU A 219      10.016  -8.516 -21.390  1.00 47.92           O  
ANISOU 1820  OE1 GLU A 219     6630   5943   5632    277   -174     47       O  
ATOM   1821  OE2 GLU A 219       7.851  -8.913 -21.310  1.00 51.98           O  
ANISOU 1821  OE2 GLU A 219     7091   6504   6154    354   -163     13       O  
ATOM   1822  N   SER A 220       6.623 -11.989 -17.415  1.00 35.77           N  
ANISOU 1822  N   SER A 220     4950   4553   4087    292    -84    -76       N  
ATOM   1823  CA  SER A 220       5.523 -11.510 -16.582  1.00 35.93           C  
ANISOU 1823  CA  SER A 220     4966   4582   4103    327    -59   -107       C  
ATOM   1824  C   SER A 220       5.492 -12.181 -15.201  1.00 34.21           C  
ANISOU 1824  C   SER A 220     4755   4375   3866    290    -34   -130       C  
ATOM   1825  O   SER A 220       4.992 -11.595 -14.239  1.00 34.65           O  
ANISOU 1825  O   SER A 220     4833   4421   3912    308    -10   -156       O  
ATOM   1826  CB  SER A 220       4.178 -11.662 -17.315  1.00 35.75           C  
ANISOU 1826  CB  SER A 220     4884   4610   4092    371    -54   -115       C  
ATOM   1827  OG  SER A 220       3.965 -12.995 -17.758  1.00 38.78           O  
ANISOU 1827  OG  SER A 220     5220   5042   4473    337    -56   -109       O  
ATOM   1828  N   PHE A 221       6.038 -13.393 -15.102  1.00 30.64           N  
ANISOU 1828  N   PHE A 221     4292   3940   3408    239    -40   -119       N  
ATOM   1829  CA  PHE A 221       5.996 -14.133 -13.846  1.00 29.90           C  
ANISOU 1829  CA  PHE A 221     4211   3856   3292    199    -21   -135       C  
ATOM   1830  C   PHE A 221       7.348 -14.592 -13.285  1.00 29.53           C  
ANISOU 1830  C   PHE A 221     4204   3779   3236    150    -43   -117       C  
ATOM   1831  O   PHE A 221       7.784 -14.081 -12.250  1.00 32.14           O  
ANISOU 1831  O   PHE A 221     4583   4079   3551    133    -42   -126       O  
ATOM   1832  CB  PHE A 221       5.013 -15.312 -13.910  1.00 29.34           C  
ANISOU 1832  CB  PHE A 221     4090   3843   3216    184     -3   -145       C  
ATOM   1833  CG  PHE A 221       4.939 -16.097 -12.629  1.00 31.81           C  
ANISOU 1833  CG  PHE A 221     4423   4163   3500    137     17   -160       C  
ATOM   1834  CD1 PHE A 221       5.496 -17.372 -12.545  1.00 28.52           C  
ANISOU 1834  CD1 PHE A 221     4014   3749   3073     88      3   -144       C  
ATOM   1835  CD2 PHE A 221       4.338 -15.547 -11.490  1.00 31.60           C  
ANISOU 1835  CD2 PHE A 221     4416   4138   3454    143     51   -189       C  
ATOM   1836  CE1 PHE A 221       5.446 -18.096 -11.356  1.00 28.83           C  
ANISOU 1836  CE1 PHE A 221     4082   3791   3082     42     16   -154       C  
ATOM   1837  CE2 PHE A 221       4.284 -16.263 -10.291  1.00 29.47           C  
ANISOU 1837  CE2 PHE A 221     4172   3874   3150     93     70   -201       C  
ATOM   1838  CZ  PHE A 221       4.837 -17.537 -10.225  1.00 33.52           C  
ANISOU 1838  CZ  PHE A 221     4695   4388   3652     41     50   -181       C  
ATOM   1839  N   ALA A 222       7.997 -15.552 -13.942  1.00 25.33           N  
ANISOU 1839  N   ALA A 222     3654   3256   2713    127    -63    -94       N  
ATOM   1840  CA  ALA A 222       9.191 -16.196 -13.368  1.00 26.13           C  
ANISOU 1840  CA  ALA A 222     3782   3337   2808     86    -84    -78       C  
ATOM   1841  C   ALA A 222      10.306 -15.220 -12.981  1.00 25.86           C  
ANISOU 1841  C   ALA A 222     3787   3262   2776     76   -106    -66       C  
ATOM   1842  O   ALA A 222      10.774 -15.239 -11.850  1.00 25.23           O  
ANISOU 1842  O   ALA A 222     3745   3163   2679     46   -114    -69       O  
ATOM   1843  CB  ALA A 222       9.734 -17.294 -14.293  1.00 21.96           C  
ANISOU 1843  CB  ALA A 222     3227   2823   2293     77   -100    -57       C  
ATOM   1844  N   ILE A 223      10.728 -14.379 -13.922  1.00 24.26           N  
ANISOU 1844  N   ILE A 223     3581   3045   2593     96   -117    -51       N  
ATOM   1845  CA  ILE A 223      11.827 -13.446 -13.670  1.00 25.67           C  
ANISOU 1845  CA  ILE A 223     3794   3185   2773     77   -140    -37       C  
ATOM   1846  C   ILE A 223      11.517 -12.482 -12.515  1.00 24.81           C  
ANISOU 1846  C   ILE A 223     3740   3044   2642     74   -132    -59       C  
ATOM   1847  O   ILE A 223      12.288 -12.421 -11.560  1.00 25.34           O  
ANISOU 1847  O   ILE A 223     3844   3091   2695     35   -151    -56       O  
ATOM   1848  CB  ILE A 223      12.279 -12.694 -14.961  1.00 24.71           C  
ANISOU 1848  CB  ILE A 223     3663   3054   2671     93   -150    -16       C  
ATOM   1849  CG1 ILE A 223      12.932 -13.677 -15.940  1.00 24.06           C  
ANISOU 1849  CG1 ILE A 223     3537   3000   2606     86   -157      7       C  
ATOM   1850  CG2 ILE A 223      13.233 -11.558 -14.623  1.00 24.35           C  
ANISOU 1850  CG2 ILE A 223     3662   2967   2622     68   -170     -4       C  
ATOM   1851  CD1 ILE A 223      12.913 -13.210 -17.402  1.00 24.74           C  
ANISOU 1851  CD1 ILE A 223     3607   3089   2703    109   -155     22       C  
ATOM   1852  N   PRO A 224      10.380 -11.753 -12.581  1.00 25.29           N  
ANISOU 1852  N   PRO A 224     3809   3102   2699    116   -107    -83       N  
ATOM   1853  CA  PRO A 224      10.073 -10.843 -11.470  1.00 24.66           C  
ANISOU 1853  CA  PRO A 224     3787   2988   2595    118    -94   -109       C  
ATOM   1854  C   PRO A 224       9.812 -11.529 -10.126  1.00 26.23           C  
ANISOU 1854  C   PRO A 224     4005   3199   2764     88    -78   -130       C  
ATOM   1855  O   PRO A 224      10.133 -10.954  -9.079  1.00 26.14           O  
ANISOU 1855  O   PRO A 224     4054   3153   2726     65    -81   -143       O  
ATOM   1856  CB  PRO A 224       8.821 -10.087 -11.945  1.00 25.47           C  
ANISOU 1856  CB  PRO A 224     3880   3093   2704    183    -66   -131       C  
ATOM   1857  CG  PRO A 224       8.295 -10.851 -13.111  1.00 26.58           C  
ANISOU 1857  CG  PRO A 224     3951   3281   2867    206    -64   -119       C  
ATOM   1858  CD  PRO A 224       9.445 -11.581 -13.714  1.00 25.03           C  
ANISOU 1858  CD  PRO A 224     3737   3091   2683    166    -93    -85       C  
ATOM   1859  N   TYR A 225       9.240 -12.735 -10.145  1.00 26.83           N  
ANISOU 1859  N   TYR A 225     4035   3319   2839     84    -62   -134       N  
ATOM   1860  CA  TYR A 225       9.026 -13.470  -8.904  1.00 27.18           C  
ANISOU 1860  CA  TYR A 225     4103   3375   2851     47    -48   -149       C  
ATOM   1861  C   TYR A 225      10.359 -13.834  -8.245  1.00 27.84           C  
ANISOU 1861  C   TYR A 225     4223   3432   2922     -6    -90   -126       C  
ATOM   1862  O   TYR A 225      10.548 -13.613  -7.045  1.00 28.03           O  
ANISOU 1862  O   TYR A 225     4303   3434   2912    -37    -91   -138       O  
ATOM   1863  CB  TYR A 225       8.160 -14.736  -9.082  1.00 27.28           C  
ANISOU 1863  CB  TYR A 225     4065   3438   2862     44    -26   -154       C  
ATOM   1864  CG  TYR A 225       7.584 -15.134  -7.744  1.00 26.49           C  
ANISOU 1864  CG  TYR A 225     3996   3347   2720     13      3   -179       C  
ATOM   1865  CD1 TYR A 225       8.359 -15.825  -6.805  1.00 26.34           C  
ANISOU 1865  CD1 TYR A 225     4022   3311   2674    -42    -20   -166       C  
ATOM   1866  CD2 TYR A 225       6.301 -14.734  -7.375  1.00 27.33           C  
ANISOU 1866  CD2 TYR A 225     4092   3479   2813     39     54   -214       C  
ATOM   1867  CE1 TYR A 225       7.854 -16.137  -5.545  1.00 28.57           C  
ANISOU 1867  CE1 TYR A 225     4345   3600   2911    -76      7   -188       C  
ATOM   1868  CE2 TYR A 225       5.784 -15.048  -6.129  1.00 29.15           C  
ANISOU 1868  CE2 TYR A 225     4355   3720   3000      7     88   -239       C  
ATOM   1869  CZ  TYR A 225       6.564 -15.747  -5.217  1.00 30.63           C  
ANISOU 1869  CZ  TYR A 225     4594   3887   3155    -54     65   -225       C  
ATOM   1870  OH  TYR A 225       6.054 -16.051  -3.978  1.00 30.56           O  
ANISOU 1870  OH  TYR A 225     4626   3889   3098    -91     98   -248       O  
ATOM   1871  N   VAL A 226      11.268 -14.392  -9.038  1.00 25.48           N  
ANISOU 1871  N   VAL A 226     3892   3140   2651    -15   -123    -94       N  
ATOM   1872  CA  VAL A 226      12.591 -14.758  -8.561  1.00 26.00           C  
ANISOU 1872  CA  VAL A 226     3976   3189   2713    -57   -167    -68       C  
ATOM   1873  C   VAL A 226      13.377 -13.526  -8.093  1.00 24.54           C  
ANISOU 1873  C   VAL A 226     3840   2964   2520    -77   -190    -65       C  
ATOM   1874  O   VAL A 226      14.005 -13.555  -7.040  1.00 22.37           O  
ANISOU 1874  O   VAL A 226     3608   2671   2221   -119   -217    -61       O  
ATOM   1875  CB  VAL A 226      13.377 -15.534  -9.641  1.00 24.91           C  
ANISOU 1875  CB  VAL A 226     3785   3070   2610    -50   -190    -37       C  
ATOM   1876  CG1 VAL A 226      14.846 -15.589  -9.294  1.00 28.07           C  
ANISOU 1876  CG1 VAL A 226     4193   3455   3017    -84   -237     -9       C  
ATOM   1877  CG2 VAL A 226      12.813 -16.938  -9.786  1.00 25.87           C  
ANISOU 1877  CG2 VAL A 226     3881   3220   2730    -47   -177    -39       C  
ATOM   1878  N   TYR A 227      13.330 -12.449  -8.872  1.00 24.73           N  
ANISOU 1878  N   TYR A 227     3862   2972   2562    -52   -184    -65       N  
ATOM   1879  CA  TYR A 227      14.034 -11.219  -8.509  1.00 25.74           C  
ANISOU 1879  CA  TYR A 227     4044   3056   2679    -76   -207    -62       C  
ATOM   1880  C   TYR A 227      13.534 -10.652  -7.175  1.00 26.37           C  
ANISOU 1880  C   TYR A 227     4199   3106   2716    -89   -192    -94       C  
ATOM   1881  O   TYR A 227      14.334 -10.300  -6.308  1.00 27.56           O  
ANISOU 1881  O   TYR A 227     4402   3229   2843   -138   -224    -89       O  
ATOM   1882  CB  TYR A 227      13.896 -10.176  -9.614  1.00 25.58           C  
ANISOU 1882  CB  TYR A 227     4019   3019   2680    -43   -199    -58       C  
ATOM   1883  CG  TYR A 227      14.596  -8.873  -9.313  1.00 27.68           C  
ANISOU 1883  CG  TYR A 227     4350   3235   2934    -73   -223    -54       C  
ATOM   1884  CD1 TYR A 227      15.944  -8.704  -9.613  1.00 28.95           C  
ANISOU 1884  CD1 TYR A 227     4501   3391   3107   -120   -263    -20       C  
ATOM   1885  CD2 TYR A 227      13.908  -7.807  -8.737  1.00 29.44           C  
ANISOU 1885  CD2 TYR A 227     4642   3412   3130    -55   -203    -85       C  
ATOM   1886  CE1 TYR A 227      16.591  -7.512  -9.340  1.00 32.49           C  
ANISOU 1886  CE1 TYR A 227     5010   3793   3541   -159   -287    -15       C  
ATOM   1887  CE2 TYR A 227      14.547  -6.604  -8.462  1.00 31.93           C  
ANISOU 1887  CE2 TYR A 227     5030   3674   3430    -87   -226    -83       C  
ATOM   1888  CZ  TYR A 227      15.889  -6.467  -8.770  1.00 32.37           C  
ANISOU 1888  CZ  TYR A 227     5077   3727   3497   -144   -270    -46       C  
ATOM   1889  OH  TYR A 227      16.534  -5.286  -8.510  1.00 35.32           O  
ANISOU 1889  OH  TYR A 227     5522   4046   3851   -187   -296    -42       O  
ATOM   1890  N   ASN A 228      12.214 -10.584  -7.015  1.00 26.11           N  
ANISOU 1890  N   ASN A 228     4168   3082   2670    -48   -144   -128       N  
ATOM   1891  CA  ASN A 228      11.605 -10.025  -5.808  1.00 25.81           C  
ANISOU 1891  CA  ASN A 228     4199   3018   2588    -52   -117   -165       C  
ATOM   1892  C   ASN A 228      11.711 -10.908  -4.571  1.00 28.19           C  
ANISOU 1892  C   ASN A 228     4529   3331   2851   -100   -121   -170       C  
ATOM   1893  O   ASN A 228      11.869 -10.397  -3.460  1.00 28.37           O  
ANISOU 1893  O   ASN A 228     4628   3321   2832   -132   -123   -188       O  
ATOM   1894  CB  ASN A 228      10.151  -9.634  -6.069  1.00 26.66           C  
ANISOU 1894  CB  ASN A 228     4292   3139   2699     13    -61   -200       C  
ATOM   1895  CG  ASN A 228      10.029  -8.307  -6.801  1.00 26.69           C  
ANISOU 1895  CG  ASN A 228     4317   3105   2721     59    -60   -205       C  
ATOM   1896  OD1 ASN A 228      10.446  -7.276  -6.294  1.00 32.05           O  
ANISOU 1896  OD1 ASN A 228     5071   3728   3378     45    -71   -214       O  
ATOM   1897  ND2 ASN A 228       9.463  -8.335  -7.997  1.00 25.23           N  
ANISOU 1897  ND2 ASN A 228     4070   2944   2572    110    -50   -197       N  
ATOM   1898  N   ARG A 229      11.625 -12.226  -4.762  1.00 27.84           N  
ANISOU 1898  N   ARG A 229     4431   3329   2817   -108   -122   -155       N  
ATOM   1899  CA  ARG A 229      11.764 -13.181  -3.658  1.00 27.96           C  
ANISOU 1899  CA  ARG A 229     4476   3353   2795   -156   -132   -153       C  
ATOM   1900  C   ARG A 229      13.167 -13.111  -3.064  1.00 27.85           C  
ANISOU 1900  C   ARG A 229     4503   3310   2769   -210   -195   -126       C  
ATOM   1901  O   ARG A 229      13.333 -13.065  -1.845  1.00 29.23           O  
ANISOU 1901  O   ARG A 229     4746   3464   2897   -252   -206   -135       O  
ATOM   1902  CB  ARG A 229      11.453 -14.610  -4.132  1.00 26.80           C  
ANISOU 1902  CB  ARG A 229     4269   3249   2665   -153   -127   -138       C  
ATOM   1903  CG  ARG A 229      11.483 -15.673  -3.043  1.00 26.88           C  
ANISOU 1903  CG  ARG A 229     4315   3265   2634   -201   -135   -135       C  
ATOM   1904  CD  ARG A 229      10.319 -15.500  -2.068  1.00 26.20           C  
ANISOU 1904  CD  ARG A 229     4271   3186   2498   -209    -78   -175       C  
ATOM   1905  NE  ARG A 229      10.414 -16.387  -0.910  1.00 25.28           N  
ANISOU 1905  NE  ARG A 229     4207   3068   2331   -266    -88   -171       N  
ATOM   1906  CZ  ARG A 229       9.730 -16.221   0.223  1.00 27.98           C  
ANISOU 1906  CZ  ARG A 229     4607   3408   2615   -292    -48   -202       C  
ATOM   1907  NH1 ARG A 229       8.900 -15.194   0.371  1.00 25.46           N  
ANISOU 1907  NH1 ARG A 229     4299   3089   2285   -261      8   -243       N  
ATOM   1908  NH2 ARG A 229       9.888 -17.076   1.220  1.00 28.75           N  
ANISOU 1908  NH2 ARG A 229     4757   3501   2664   -348    -62   -192       N  
ATOM   1909  N   ILE A 230      14.171 -13.099  -3.938  1.00 28.20           N  
ANISOU 1909  N   ILE A 230     4504   3356   2856   -209   -237    -91       N  
ATOM   1910  CA  ILE A 230      15.567 -12.934  -3.528  1.00 26.94           C  
ANISOU 1910  CA  ILE A 230     4365   3176   2693   -257   -301    -62       C  
ATOM   1911  C   ILE A 230      15.778 -11.560  -2.882  1.00 26.33           C  
ANISOU 1911  C   ILE A 230     4365   3054   2586   -284   -309    -79       C  
ATOM   1912  O   ILE A 230      16.455 -11.454  -1.858  1.00 26.00           O  
ANISOU 1912  O   ILE A 230     4379   2992   2510   -338   -349    -72       O  
ATOM   1913  CB  ILE A 230      16.543 -13.187  -4.704  1.00 26.24           C  
ANISOU 1913  CB  ILE A 230     4202   3108   2659   -246   -333    -24       C  
ATOM   1914  CG1 ILE A 230      16.559 -14.681  -5.050  1.00 25.52           C  
ANISOU 1914  CG1 ILE A 230     4056   3052   2587   -230   -337     -7       C  
ATOM   1915  CG2 ILE A 230      17.958 -12.689  -4.373  1.00 25.08           C  
ANISOU 1915  CG2 ILE A 230     4069   2946   2514   -297   -395      4       C  
ATOM   1916  CD1 ILE A 230      17.288 -15.031  -6.343  1.00 27.27           C  
ANISOU 1916  CD1 ILE A 230     4201   3299   2862   -206   -351     22       C  
ATOM   1917  N   LYS A 231      15.173 -10.525  -3.465  1.00 28.16           N  
ANISOU 1917  N   LYS A 231     4606   3267   2827   -247   -273   -100       N  
ATOM   1918  CA  LYS A 231      15.203  -9.185  -2.880  1.00 30.60           C  
ANISOU 1918  CA  LYS A 231     5000   3522   3103   -264   -273   -123       C  
ATOM   1919  C   LYS A 231      14.610  -9.161  -1.460  1.00 32.06           C  
ANISOU 1919  C   LYS A 231     5266   3689   3227   -286   -250   -158       C  
ATOM   1920  O   LYS A 231      15.196  -8.575  -0.546  1.00 31.40           O  
ANISOU 1920  O   LYS A 231     5261   3566   3102   -337   -281   -162       O  
ATOM   1921  CB  LYS A 231      14.489  -8.180  -3.786  1.00 31.48           C  
ANISOU 1921  CB  LYS A 231     5110   3615   3237   -207   -234   -141       C  
ATOM   1922  CG  LYS A 231      14.673  -6.725  -3.354  1.00 37.11           C  
ANISOU 1922  CG  LYS A 231     5917   4262   3920   -224   -241   -160       C  
ATOM   1923  CD  LYS A 231      13.910  -5.742  -4.239  1.00 41.30           C  
ANISOU 1923  CD  LYS A 231     6454   4767   4471   -158   -205   -177       C  
ATOM   1924  CE  LYS A 231      12.413  -5.749  -3.937  1.00 47.10           C  
ANISOU 1924  CE  LYS A 231     7194   5510   5192    -91   -138   -223       C  
ATOM   1925  NZ  LYS A 231      11.751  -4.473  -4.327  1.00 50.62           N  
ANISOU 1925  NZ  LYS A 231     7686   5908   5640    -31   -111   -248       N  
ATOM   1926  N   ASN A 232      13.467  -9.819  -1.275  1.00 32.71           N  
ANISOU 1926  N   ASN A 232     5330   3801   3298   -251   -196   -183       N  
ATOM   1927  CA  ASN A 232      12.800  -9.857   0.033  1.00 35.57           C  
ANISOU 1927  CA  ASN A 232     5764   4153   3598   -271   -162   -219       C  
ATOM   1928  C   ASN A 232      13.574 -10.621   1.112  1.00 35.58           C  
ANISOU 1928  C   ASN A 232     5808   4154   3559   -342   -210   -199       C  
ATOM   1929  O   ASN A 232      13.478 -10.294   2.296  1.00 35.95           O  
ANISOU 1929  O   ASN A 232     5943   4173   3544   -380   -204   -223       O  
ATOM   1930  CB  ASN A 232      11.382 -10.427  -0.091  1.00 36.52           C  
ANISOU 1930  CB  ASN A 232     5842   4315   3719   -222    -90   -248       C  
ATOM   1931  CG  ASN A 232      10.425  -9.476  -0.802  1.00 36.16           C  
ANISOU 1931  CG  ASN A 232     5778   4264   3698   -148    -38   -279       C  
ATOM   1932  OD1 ASN A 232      10.734  -8.304  -1.014  1.00 40.37           O  
ANISOU 1932  OD1 ASN A 232     6353   4750   4235   -134    -50   -285       O  
ATOM   1933  ND2 ASN A 232       9.253  -9.984  -1.167  1.00 34.90           N  
ANISOU 1933  ND2 ASN A 232     5555   4151   3552   -103     16   -297       N  
ATOM   1934  N   ILE A 233      14.339 -11.628   0.692  1.00 35.81           N  
ANISOU 1934  N   ILE A 233     5775   4211   3619   -359   -258   -156       N  
ATOM   1935  CA  ILE A 233      15.070 -12.501   1.613  1.00 33.65           C  
ANISOU 1935  CA  ILE A 233     5531   3940   3314   -417   -311   -131       C  
ATOM   1936  C   ILE A 233      16.488 -12.006   1.897  1.00 33.82           C  
ANISOU 1936  C   ILE A 233     5580   3936   3334   -469   -390   -100       C  
ATOM   1937  O   ILE A 233      16.944 -12.038   3.043  1.00 35.38           O  
ANISOU 1937  O   ILE A 233     5850   4113   3480   -526   -429    -97       O  
ATOM   1938  CB  ILE A 233      15.121 -13.959   1.092  1.00 33.25           C  
ANISOU 1938  CB  ILE A 233     5406   3932   3296   -403   -322   -101       C  
ATOM   1939  CG1 ILE A 233      13.716 -14.581   1.099  1.00 33.61           C  
ANISOU 1939  CG1 ILE A 233     5439   4004   3327   -375   -249   -130       C  
ATOM   1940  CG2 ILE A 233      16.100 -14.804   1.927  1.00 31.50           C  
ANISOU 1940  CG2 ILE A 233     5213   3706   3050   -456   -393    -66       C  
ATOM   1941  CD1 ILE A 233      13.616 -15.916   0.353  1.00 33.38           C  
ANISOU 1941  CD1 ILE A 233     5337   4012   3335   -355   -253   -105       C  
ATOM   1942  N   PHE A 234      17.175 -11.543   0.856  1.00 32.69           N  
ANISOU 1942  N   PHE A 234     5379   3796   3246   -453   -415    -78       N  
ATOM   1943  CA  PHE A 234      18.596 -11.214   0.958  1.00 32.31           C  
ANISOU 1943  CA  PHE A 234     5330   3738   3207   -504   -492    -42       C  
ATOM   1944  C   PHE A 234      18.911  -9.732   0.782  1.00 32.01           C  
ANISOU 1944  C   PHE A 234     5336   3661   3165   -524   -498    -53       C  
ATOM   1945  O   PHE A 234      19.966  -9.279   1.203  1.00 32.47           O  
ANISOU 1945  O   PHE A 234     5422   3704   3211   -585   -561    -32       O  
ATOM   1946  CB  PHE A 234      19.395 -12.017  -0.075  1.00 30.68           C  
ANISOU 1946  CB  PHE A 234     5016   3574   3066   -484   -525      1       C  
ATOM   1947  CG  PHE A 234      19.364 -13.500   0.148  1.00 30.49           C  
ANISOU 1947  CG  PHE A 234     4959   3579   3044   -472   -538     19       C  
ATOM   1948  CD1 PHE A 234      18.684 -14.333  -0.735  1.00 29.39           C  
ANISOU 1948  CD1 PHE A 234     4757   3470   2940   -416   -493     17       C  
ATOM   1949  CD2 PHE A 234      20.020 -14.071   1.239  1.00 30.29           C  
ANISOU 1949  CD2 PHE A 234     4974   3550   2985   -521   -598     40       C  
ATOM   1950  CE1 PHE A 234      18.658 -15.718  -0.539  1.00 28.50           C  
ANISOU 1950  CE1 PHE A 234     4626   3377   2828   -408   -506     33       C  
ATOM   1951  CE2 PHE A 234      19.999 -15.453   1.438  1.00 30.55           C  
ANISOU 1951  CE2 PHE A 234     4987   3603   3018   -508   -613     59       C  
ATOM   1952  CZ  PHE A 234      19.317 -16.273   0.550  1.00 29.26           C  
ANISOU 1952  CZ  PHE A 234     4765   3463   2889   -453   -566     55       C  
ATOM   1953  N   GLY A 235      18.011  -8.987   0.147  1.00 32.08           N  
ANISOU 1953  N   GLY A 235     5351   3653   3185   -474   -437    -83       N  
ATOM   1954  CA  GLY A 235      18.262  -7.577  -0.167  1.00 34.14           C  
ANISOU 1954  CA  GLY A 235     5657   3868   3445   -485   -441    -92       C  
ATOM   1955  C   GLY A 235      18.476  -7.369  -1.655  1.00 34.71           C  
ANISOU 1955  C   GLY A 235     5648   3959   3581   -448   -435    -69       C  
ATOM   1956  O   GLY A 235      18.704  -8.333  -2.394  1.00 34.75           O  
ANISOU 1956  O   GLY A 235     5559   4013   3630   -425   -440    -42       O  
ATOM   1957  N   GLU A 236      18.406  -6.113  -2.089  1.00 36.26           N  
ANISOU 1957  N   GLU A 236     5888   4112   3777   -443   -424    -80       N  
ATOM   1958  CA  GLU A 236      18.510  -5.749  -3.506  1.00 39.97           C  
ANISOU 1958  CA  GLU A 236     6299   4590   4298   -410   -414    -61       C  
ATOM   1959  C   GLU A 236      19.800  -6.205  -4.191  1.00 40.55           C  
ANISOU 1959  C   GLU A 236     6289   4705   4413   -449   -463    -11       C  
ATOM   1960  O   GLU A 236      19.758  -6.718  -5.316  1.00 41.80           O  
ANISOU 1960  O   GLU A 236     6362   4902   4616   -409   -445      6       O  
ATOM   1961  CB  GLU A 236      18.318  -4.240  -3.707  1.00 43.36           C  
ANISOU 1961  CB  GLU A 236     6812   4953   4711   -410   -403    -80       C  
ATOM   1962  CG  GLU A 236      16.978  -3.874  -4.353  1.00 52.06           C  
ANISOU 1962  CG  GLU A 236     7916   6040   5824   -320   -339   -110       C  
ATOM   1963  CD  GLU A 236      16.866  -2.400  -4.739  1.00 59.02           C  
ANISOU 1963  CD  GLU A 236     8878   6852   6696   -311   -335   -121       C  
ATOM   1964  OE1 GLU A 236      17.898  -1.774  -5.078  1.00 61.47           O  
ANISOU 1964  OE1 GLU A 236     9206   7139   7009   -371   -378    -92       O  
ATOM   1965  OE2 GLU A 236      15.732  -1.867  -4.712  1.00 61.73           O  
ANISOU 1965  OE2 GLU A 236     9265   7162   7028   -243   -288   -159       O  
ATOM   1966  N   SER A 237      20.937  -6.008  -3.522  1.00 38.73           N  
ANISOU 1966  N   SER A 237     6080   4469   4165   -527   -524     10       N  
ATOM   1967  CA  SER A 237      22.244  -6.298  -4.120  1.00 36.41           C  
ANISOU 1967  CA  SER A 237     5705   4219   3911   -568   -571     57       C  
ATOM   1968  C   SER A 237      22.381  -7.765  -4.528  1.00 34.41           C  
ANISOU 1968  C   SER A 237     5347   4031   3698   -529   -569     78       C  
ATOM   1969  O   SER A 237      22.969  -8.072  -5.565  1.00 33.78           O  
ANISOU 1969  O   SER A 237     5181   3991   3665   -518   -572    106       O  
ATOM   1970  CB  SER A 237      23.387  -5.894  -3.179  1.00 37.18           C  
ANISOU 1970  CB  SER A 237     5842   4305   3980   -662   -642     76       C  
ATOM   1971  OG  SER A 237      23.635  -6.889  -2.191  1.00 37.63           O  
ANISOU 1971  OG  SER A 237     5889   4387   4020   -677   -677     83       O  
ATOM   1972  N   THR A 238      21.855  -8.666  -3.701  1.00 30.93           N  
ANISOU 1972  N   THR A 238     4919   3597   3235   -510   -565     63       N  
ATOM   1973  CA  THR A 238      21.866 -10.083  -4.037  1.00 30.27           C  
ANISOU 1973  CA  THR A 238     4753   3563   3183   -470   -561     79       C  
ATOM   1974  C   THR A 238      20.954 -10.352  -5.247  1.00 29.66           C  
ANISOU 1974  C   THR A 238     4629   3503   3139   -397   -499     67       C  
ATOM   1975  O   THR A 238      21.330 -11.107  -6.138  1.00 30.63           O  
ANISOU 1975  O   THR A 238     4668   3665   3303   -370   -497     89       O  
ATOM   1976  CB  THR A 238      21.484 -10.954  -2.823  1.00 29.28           C  
ANISOU 1976  CB  THR A 238     4669   3436   3019   -475   -572     68       C  
ATOM   1977  OG1 THR A 238      22.364 -10.652  -1.736  1.00 31.42           O  
ANISOU 1977  OG1 THR A 238     4988   3692   3257   -546   -637     82       O  
ATOM   1978  CG2 THR A 238      21.609 -12.429  -3.134  1.00 26.50           C  
ANISOU 1978  CG2 THR A 238     4242   3127   2698   -439   -577     88       C  
ATOM   1979  N   ALA A 239      19.789  -9.704  -5.295  1.00 27.96           N  
ANISOU 1979  N   ALA A 239     4465   3256   2903   -365   -449     32       N  
ATOM   1980  CA  ALA A 239      18.842  -9.890  -6.405  1.00 29.43           C  
ANISOU 1980  CA  ALA A 239     4610   3457   3117   -298   -395     20       C  
ATOM   1981  C   ALA A 239      19.414  -9.407  -7.728  1.00 29.57           C  
ANISOU 1981  C   ALA A 239     4578   3484   3172   -292   -397     44       C  
ATOM   1982  O   ALA A 239      19.142  -9.992  -8.781  1.00 26.05           O  
ANISOU 1982  O   ALA A 239     4069   3070   2759   -248   -372     52       O  
ATOM   1983  CB  ALA A 239      17.506  -9.203  -6.120  1.00 28.09           C  
ANISOU 1983  CB  ALA A 239     4502   3254   2918   -262   -347    -22       C  
ATOM   1984  N   LYS A 240      20.212  -8.341  -7.657  1.00 30.68           N  
ANISOU 1984  N   LYS A 240     4753   3597   3306   -342   -427     57       N  
ATOM   1985  CA  LYS A 240      20.883  -7.775  -8.827  1.00 30.70           C  
ANISOU 1985  CA  LYS A 240     4719   3607   3338   -354   -431     83       C  
ATOM   1986  C   LYS A 240      21.944  -8.697  -9.439  1.00 29.31           C  
ANISOU 1986  C   LYS A 240     4445   3490   3201   -364   -451    119       C  
ATOM   1987  O   LYS A 240      22.451  -8.425 -10.531  1.00 31.57           O  
ANISOU 1987  O   LYS A 240     4688   3795   3514   -368   -444    140       O  
ATOM   1988  CB  LYS A 240      21.468  -6.403  -8.494  1.00 30.83           C  
ANISOU 1988  CB  LYS A 240     4807   3576   3331   -417   -459     88       C  
ATOM   1989  CG  LYS A 240      20.445  -5.282  -8.577  1.00 33.45           C  
ANISOU 1989  CG  LYS A 240     5225   3846   3638   -387   -427     57       C  
ATOM   1990  CD  LYS A 240      20.775  -4.147  -7.629  1.00 38.03           C  
ANISOU 1990  CD  LYS A 240     5909   4365   4175   -447   -456     47       C  
ATOM   1991  CE  LYS A 240      19.644  -3.135  -7.576  1.00 41.70           C  
ANISOU 1991  CE  LYS A 240     6466   4764   4615   -402   -420     10       C  
ATOM   1992  NZ  LYS A 240      19.959  -1.907  -8.352  1.00 45.36           N  
ANISOU 1992  NZ  LYS A 240     6977   5181   5078   -423   -427     24       N  
ATOM   1993  N   ARG A 241      22.255  -9.794  -8.757  1.00 28.67           N  
ANISOU 1993  N   ARG A 241     4332   3438   3123   -365   -474    125       N  
ATOM   1994  CA  ARG A 241      23.200 -10.786  -9.279  1.00 27.24           C  
ANISOU 1994  CA  ARG A 241     4058   3312   2981   -360   -491    155       C  
ATOM   1995  C   ARG A 241      22.674 -11.544 -10.502  1.00 27.44           C  
ANISOU 1995  C   ARG A 241     4025   3365   3035   -295   -445    153       C  
ATOM   1996  O   ARG A 241      23.439 -12.224 -11.188  1.00 29.66           O  
ANISOU 1996  O   ARG A 241     4231   3689   3350   -283   -448    175       O  
ATOM   1997  CB  ARG A 241      23.667 -11.747  -8.175  1.00 25.11           C  
ANISOU 1997  CB  ARG A 241     3779   3057   2704   -373   -535    164       C  
ATOM   1998  CG  ARG A 241      24.715 -11.116  -7.229  1.00 24.63           C  
ANISOU 1998  CG  ARG A 241     3743   2989   2626   -449   -597    182       C  
ATOM   1999  CD  ARG A 241      25.061 -12.038  -6.065  1.00 19.94           C  
ANISOU 1999  CD  ARG A 241     3154   2405   2019   -461   -646    190       C  
ATOM   2000  NE  ARG A 241      25.582 -13.319  -6.536  1.00 23.18           N  
ANISOU 2000  NE  ARG A 241     3476   2862   2470   -418   -654    212       N  
ATOM   2001  CZ  ARG A 241      25.549 -14.460  -5.854  1.00 25.50           C  
ANISOU 2001  CZ  ARG A 241     3770   3161   2758   -397   -678    217       C  
ATOM   2002  NH1 ARG A 241      25.017 -14.501  -4.638  1.00 26.42           N  
ANISOU 2002  NH1 ARG A 241     3969   3244   2826   -420   -696    202       N  
ATOM   2003  NH2 ARG A 241      26.061 -15.568  -6.395  1.00 22.42           N  
ANISOU 2003  NH2 ARG A 241     3302   2808   2407   -352   -684    236       N  
ATOM   2004  N   LEU A 242      21.374 -11.415 -10.772  1.00 26.72           N  
ANISOU 2004  N   LEU A 242     3970   3252   2930   -252   -403    125       N  
ATOM   2005  CA  LEU A 242      20.767 -11.963 -11.982  1.00 26.42           C  
ANISOU 2005  CA  LEU A 242     3889   3236   2913   -198   -362    121       C  
ATOM   2006  C   LEU A 242      21.207 -11.182 -13.221  1.00 26.55           C  
ANISOU 2006  C   LEU A 242     3883   3258   2946   -204   -349    138       C  
ATOM   2007  O   LEU A 242      21.109 -11.677 -14.341  1.00 24.57           O  
ANISOU 2007  O   LEU A 242     3586   3034   2715   -171   -322    144       O  
ATOM   2008  CB  LEU A 242      19.237 -11.984 -11.868  1.00 25.57           C  
ANISOU 2008  CB  LEU A 242     3821   3109   2785   -155   -325     88       C  
ATOM   2009  CG  LEU A 242      18.653 -12.924 -10.806  1.00 25.24           C  
ANISOU 2009  CG  LEU A 242     3796   3069   2723   -148   -326     70       C  
ATOM   2010  CD1 LEU A 242      17.204 -12.580 -10.531  1.00 24.81           C  
ANISOU 2010  CD1 LEU A 242     3786   2996   2645   -119   -290     36       C  
ATOM   2011  CD2 LEU A 242      18.795 -14.385 -11.239  1.00 21.50           C  
ANISOU 2011  CD2 LEU A 242     3267   2632   2271   -122   -324     80       C  
ATOM   2012  N   SER A 243      21.676  -9.957 -13.015  1.00 26.37           N  
ANISOU 2012  N   SER A 243     3900   3206   2911   -252   -367    146       N  
ATOM   2013  CA  SER A 243      22.345  -9.220 -14.076  1.00 27.26           C  
ANISOU 2013  CA  SER A 243     3994   3326   3037   -277   -362    170       C  
ATOM   2014  C   SER A 243      23.857  -9.403 -13.946  1.00 28.56           C  
ANISOU 2014  C   SER A 243     4101   3529   3220   -331   -395    200       C  
ATOM   2015  O   SER A 243      24.412  -9.176 -12.863  1.00 29.76           O  
ANISOU 2015  O   SER A 243     4274   3672   3362   -378   -436    205       O  
ATOM   2016  CB  SER A 243      22.006  -7.732 -14.007  1.00 26.63           C  
ANISOU 2016  CB  SER A 243     3998   3189   2931   -303   -364    163       C  
ATOM   2017  OG  SER A 243      22.955  -6.985 -14.751  1.00 27.87           O  
ANISOU 2017  OG  SER A 243     4144   3351   3095   -354   -371    192       O  
ATOM   2018  N   PRO A 244      24.531  -9.795 -15.048  1.00 27.34           N  
ANISOU 2018  N   PRO A 244     3873   3420   3094   -325   -376    221       N  
ATOM   2019  CA  PRO A 244      25.992  -9.971 -15.030  1.00 28.49           C  
ANISOU 2019  CA  PRO A 244     3947   3613   3263   -371   -402    251       C  
ATOM   2020  C   PRO A 244      26.776  -8.673 -14.833  1.00 30.08           C  
ANISOU 2020  C   PRO A 244     4177   3801   3452   -456   -429    270       C  
ATOM   2021  O   PRO A 244      27.973  -8.725 -14.577  1.00 33.88           O  
ANISOU 2021  O   PRO A 244     4600   4322   3949   -505   -460    294       O  
ATOM   2022  CB  PRO A 244      26.302 -10.577 -16.404  1.00 28.01           C  
ANISOU 2022  CB  PRO A 244     3813   3600   3228   -337   -361    262       C  
ATOM   2023  CG  PRO A 244      25.125 -10.228 -17.256  1.00 26.11           C  
ANISOU 2023  CG  PRO A 244     3624   3327   2970   -299   -321    245       C  
ATOM   2024  CD  PRO A 244      23.943 -10.200 -16.339  1.00 25.18           C  
ANISOU 2024  CD  PRO A 244     3576   3162   2830   -272   -330    217       C  
ATOM   2025  N   HIS A 245      26.112  -7.529 -14.962  1.00 30.02           N  
ANISOU 2025  N   HIS A 245     4255   3735   3414   -472   -420    260       N  
ATOM   2026  CA  HIS A 245      26.739  -6.237 -14.678  1.00 30.62           C  
ANISOU 2026  CA  HIS A 245     4381   3782   3470   -558   -449    275       C  
ATOM   2027  C   HIS A 245      26.142  -5.626 -13.414  1.00 32.46           C  
ANISOU 2027  C   HIS A 245     4714   3950   3668   -573   -478    252       C  
ATOM   2028  O   HIS A 245      26.382  -4.459 -13.105  1.00 33.69           O  
ANISOU 2028  O   HIS A 245     4942   4060   3797   -637   -501    256       O  
ATOM   2029  CB  HIS A 245      26.564  -5.274 -15.855  1.00 29.61           C  
ANISOU 2029  CB  HIS A 245     4289   3630   3332   -572   -419    286       C  
ATOM   2030  CG  HIS A 245      26.795  -5.904 -17.194  1.00 27.42           C  
ANISOU 2030  CG  HIS A 245     3933   3407   3079   -541   -377    300       C  
ATOM   2031  ND1 HIS A 245      27.976  -6.532 -17.530  1.00 29.34           N  
ANISOU 2031  ND1 HIS A 245     4072   3724   3352   -565   -375    323       N  
ATOM   2032  CD2 HIS A 245      25.997  -5.994 -18.283  1.00 25.14           C  
ANISOU 2032  CD2 HIS A 245     3655   3110   2788   -486   -335    293       C  
ATOM   2033  CE1 HIS A 245      27.890  -6.996 -18.766  1.00 28.03           C  
ANISOU 2033  CE1 HIS A 245     3861   3590   3197   -526   -329    327       C  
ATOM   2034  NE2 HIS A 245      26.702  -6.674 -19.248  1.00 28.21           N  
ANISOU 2034  NE2 HIS A 245     3955   3564   3200   -482   -306    310       N  
ATOM   2035  N   ARG A 246      25.367  -6.435 -12.690  1.00 33.19           N  
ANISOU 2035  N   ARG A 246     4817   4038   3758   -517   -476    226       N  
ATOM   2036  CA  ARG A 246      24.695  -6.031 -11.439  1.00 35.17           C  
ANISOU 2036  CA  ARG A 246     5159   4232   3971   -522   -494    198       C  
ATOM   2037  C   ARG A 246      23.873  -4.740 -11.558  1.00 35.00           C  
ANISOU 2037  C   ARG A 246     5242   4137   3918   -519   -476    179       C  
ATOM   2038  O   ARG A 246      23.809  -3.940 -10.617  1.00 35.67           O  
ANISOU 2038  O   ARG A 246     5415   4169   3968   -558   -500    164       O  
ATOM   2039  CB  ARG A 246      25.683  -5.938 -10.261  1.00 35.74           C  
ANISOU 2039  CB  ARG A 246     5239   4309   4030   -597   -553    211       C  
ATOM   2040  CG  ARG A 246      26.731  -7.048 -10.189  1.00 39.54           C  
ANISOU 2040  CG  ARG A 246     5613   4865   4547   -605   -582    238       C  
ATOM   2041  CD  ARG A 246      26.139  -8.408  -9.833  1.00 42.47           C  
ANISOU 2041  CD  ARG A 246     5952   5256   4927   -534   -570    223       C  
ATOM   2042  NE  ARG A 246      27.194  -9.403  -9.637  1.00 49.16           N  
ANISOU 2042  NE  ARG A 246     6709   6164   5805   -541   -606    250       N  
ATOM   2043  CZ  ARG A 246      27.518 -10.360 -10.504  1.00 51.31           C  
ANISOU 2043  CZ  ARG A 246     6889   6489   6119   -493   -585    263       C  
ATOM   2044  NH1 ARG A 246      26.862 -10.488 -11.653  1.00 51.86           N  
ANISOU 2044  NH1 ARG A 246     6945   6559   6200   -441   -527    253       N  
ATOM   2045  NH2 ARG A 246      28.503 -11.203 -10.214  1.00 51.28           N  
ANISOU 2045  NH2 ARG A 246     6807   6534   6142   -494   -622    286       N  
ATOM   2046  N   LYS A 247      23.252  -4.534 -12.713  1.00 34.11           N  
ANISOU 2046  N   LYS A 247     5127   4019   3817   -472   -437    178       N  
ATOM   2047  CA  LYS A 247      22.300  -3.435 -12.856  1.00 37.10           C  
ANISOU 2047  CA  LYS A 247     5602   4326   4168   -447   -419    157       C  
ATOM   2048  C   LYS A 247      20.948  -3.950 -13.333  1.00 35.10           C  
ANISOU 2048  C   LYS A 247     5337   4076   3924   -351   -377    133       C  
ATOM   2049  O   LYS A 247      20.868  -4.742 -14.266  1.00 34.23           O  
ANISOU 2049  O   LYS A 247     5152   4014   3840   -315   -355    144       O  
ATOM   2050  CB  LYS A 247      22.821  -2.325 -13.780  1.00 37.04           C  
ANISOU 2050  CB  LYS A 247     5627   4290   4155   -494   -423    183       C  
ATOM   2051  CG  LYS A 247      22.001  -1.028 -13.675  1.00 42.97           C  
ANISOU 2051  CG  LYS A 247     6502   4951   4873   -478   -419    163       C  
ATOM   2052  CD  LYS A 247      22.314  -0.031 -14.784  1.00 45.19           C  
ANISOU 2052  CD  LYS A 247     6820   5200   5147   -510   -418    190       C  
ATOM   2053  CE  LYS A 247      21.367   1.171 -14.750  1.00 47.94           C  
ANISOU 2053  CE  LYS A 247     7293   5454   5466   -473   -413    169       C  
ATOM   2054  NZ  LYS A 247      21.593   2.048 -13.561  1.00 49.65           N  
ANISOU 2054  NZ  LYS A 247     7614   5604   5647   -526   -443    152       N  
ATOM   2055  N   THR A 248      19.895  -3.512 -12.657  1.00 36.70           N  
ANISOU 2055  N   THR A 248     5611   4229   4102   -311   -365     98       N  
ATOM   2056  CA  THR A 248      18.535  -3.836 -13.048  1.00 38.77           C  
ANISOU 2056  CA  THR A 248     5865   4495   4372   -222   -326     73       C  
ATOM   2057  C   THR A 248      17.689  -2.569 -13.060  1.00 43.56           C  
ANISOU 2057  C   THR A 248     6567   5029   4956   -188   -316     53       C  
ATOM   2058  O   THR A 248      18.090  -1.535 -12.514  1.00 43.06           O  
ANISOU 2058  O   THR A 248     6588   4907   4866   -233   -337     50       O  
ATOM   2059  CB  THR A 248      17.880  -4.871 -12.102  1.00 37.85           C  
ANISOU 2059  CB  THR A 248     5722   4406   4251   -190   -312     45       C  
ATOM   2060  OG1 THR A 248      17.784  -4.324 -10.783  1.00 36.41           O  
ANISOU 2060  OG1 THR A 248     5620   4180   4035   -214   -324     21       O  
ATOM   2061  CG2 THR A 248      18.674  -6.179 -12.066  1.00 34.86           C  
ANISOU 2061  CG2 THR A 248     5259   4093   3895   -214   -326     66       C  
ATOM   2062  N   ARG A 249      16.520  -2.660 -13.689  1.00 48.46           N  
ANISOU 2062  N   ARG A 249     7174   5653   5587   -108   -286     38       N  
ATOM   2063  CA  ARG A 249      15.554  -1.574 -13.702  1.00 54.49           C  
ANISOU 2063  CA  ARG A 249     8017   6352   6334    -53   -274     15       C  
ATOM   2064  C   ARG A 249      14.156  -2.158 -13.519  1.00 57.52           C  
ANISOU 2064  C   ARG A 249     8366   6763   6726     32   -238    -19       C  
ATOM   2065  O   ARG A 249      13.793  -3.137 -14.178  1.00 56.57           O  
ANISOU 2065  O   ARG A 249     8161   6703   6629     62   -225    -11       O  
ATOM   2066  CB  ARG A 249      15.647  -0.790 -15.017  1.00 56.44           C  
ANISOU 2066  CB  ARG A 249     8286   6571   6587    -45   -282     44       C  
ATOM   2067  CG  ARG A 249      15.245   0.682 -14.919  1.00 63.16           C  
ANISOU 2067  CG  ARG A 249     9254   7331   7414    -24   -289     32       C  
ATOM   2068  CD  ARG A 249      16.330   1.533 -14.233  1.00 70.72           C  
ANISOU 2068  CD  ARG A 249    10295   8232   8342   -115   -320     41       C  
ATOM   2069  NE  ARG A 249      17.524   1.706 -15.066  1.00 74.36           N  
ANISOU 2069  NE  ARG A 249    10742   8705   8808   -196   -343     87       N  
ATOM   2070  CZ  ARG A 249      17.775   2.775 -15.822  1.00 77.57           C  
ANISOU 2070  CZ  ARG A 249    11220   9054   9200   -219   -358    111       C  
ATOM   2071  NH1 ARG A 249      16.920   3.792 -15.857  1.00 79.63           N  
ANISOU 2071  NH1 ARG A 249    11578   9234   9443   -161   -357     93       N  
ATOM   2072  NH2 ARG A 249      18.888   2.832 -16.543  1.00 77.17           N  
ANISOU 2072  NH2 ARG A 249    11144   9027   9152   -299   -374    153       N  
ATOM   2073  N   VAL A 250      13.388  -1.565 -12.608  1.00 62.55           N  
ANISOU 2073  N   VAL A 250     9067   7357   7341     69   -222    -57       N  
ATOM   2074  CA  VAL A 250      12.003  -1.968 -12.362  1.00 68.09           C  
ANISOU 2074  CA  VAL A 250     9738   8086   8049    150   -184    -92       C  
ATOM   2075  C   VAL A 250      11.087  -0.991 -13.102  1.00 73.61           C  
ANISOU 2075  C   VAL A 250    10471   8742   8754    229   -176    -99       C  
ATOM   2076  O   VAL A 250      10.871   0.136 -12.646  1.00 73.34           O  
ANISOU 2076  O   VAL A 250    10531   8637   8699    251   -175   -119       O  
ATOM   2077  CB  VAL A 250      11.672  -1.995 -10.840  1.00 68.31           C  
ANISOU 2077  CB  VAL A 250     9809   8100   8047    145   -163   -134       C  
ATOM   2078  CG1 VAL A 250      10.310  -2.626 -10.590  1.00 68.60           C  
ANISOU 2078  CG1 VAL A 250     9791   8182   8090    216   -118   -167       C  
ATOM   2079  CG2 VAL A 250      12.748  -2.741 -10.055  1.00 67.13           C  
ANISOU 2079  CG2 VAL A 250     9648   7975   7885     58   -185   -121       C  
ATOM   2080  N   LYS A 251      10.559  -1.425 -14.248  1.00 80.44           N  
ANISOU 2080  N   LYS A 251    11267   9650   9646    273   -173    -82       N  
ATOM   2081  CA  LYS A 251       9.854  -0.521 -15.167  1.00 87.58           C  
ANISOU 2081  CA  LYS A 251    12201  10517  10558    343   -179    -77       C  
ATOM   2082  C   LYS A 251       8.475  -1.018 -15.621  1.00 91.21           C  
ANISOU 2082  C   LYS A 251    12585  11030  11040    431   -156    -93       C  
ATOM   2083  O   LYS A 251       8.254  -2.222 -15.779  1.00 90.82           O  
ANISOU 2083  O   LYS A 251    12445  11056  11005    423   -144    -91       O  
ATOM   2084  CB  LYS A 251      10.729  -0.216 -16.394  1.00 88.56           C  
ANISOU 2084  CB  LYS A 251    12336  10627  10687    301   -212    -28       C  
ATOM   2085  CG  LYS A 251      10.463   1.149 -17.030  1.00 90.89           C  
ANISOU 2085  CG  LYS A 251    12718  10842  10972    342   -231    -18       C  
ATOM   2086  CD  LYS A 251      10.662   1.123 -18.538  1.00 91.63           C  
ANISOU 2086  CD  LYS A 251    12788  10951  11076    339   -252     26       C  
ATOM   2087  CE  LYS A 251      10.041   2.355 -19.186  1.00 93.36           C  
ANISOU 2087  CE  LYS A 251    13087  11098  11289    404   -272     34       C  
ATOM   2088  NZ  LYS A 251      10.041   2.280 -20.674  1.00 93.44           N  
ANISOU 2088  NZ  LYS A 251    13074  11126  11303    409   -293     75       N  
ATOM   2089  N   VAL A 252       7.569  -0.063 -15.844  1.00 96.63           N  
ANISOU 2089  N   VAL A 252    13312  11674  11729    514   -154   -107       N  
ATOM   2090  CA  VAL A 252       6.186  -0.321 -16.271  1.00100.93           C  
ANISOU 2090  CA  VAL A 252    13787  12265  12297    606   -138   -122       C  
ATOM   2091  C   VAL A 252       6.045  -0.609 -17.771  1.00103.51           C  
ANISOU 2091  C   VAL A 252    14062  12624  12642    621   -167    -83       C  
ATOM   2092  O   VAL A 252       6.775  -0.046 -18.593  1.00103.69           O  
ANISOU 2092  O   VAL A 252    14136  12603  12657    592   -199    -47       O  
ATOM   2093  CB  VAL A 252       5.228   0.864 -15.904  1.00102.02           C  
ANISOU 2093  CB  VAL A 252    13987  12345  12432    703   -126   -154       C  
ATOM   2094  CG1 VAL A 252       4.899   0.874 -14.413  1.00102.14           C  
ANISOU 2094  CG1 VAL A 252    14023  12354  12429    712    -82   -205       C  
ATOM   2095  CG2 VAL A 252       5.806   2.218 -16.351  1.00102.74           C  
ANISOU 2095  CG2 VAL A 252    14197  12333  12508    704   -162   -132       C  
ATOM   2096  N   ILE A 253       5.101  -1.488 -18.109  1.00106.94           N  
ANISOU 2096  N   ILE A 253    14399  13138  13097    659   -154    -91       N  
ATOM   2097  CA  ILE A 253       4.690  -1.726 -19.498  1.00110.38           C  
ANISOU 2097  CA  ILE A 253    14786  13607  13548    687   -181    -60       C  
ATOM   2098  C   ILE A 253       3.377  -0.980 -19.761  1.00113.52           C  
ANISOU 2098  C   ILE A 253    15177  13995  13959    797   -187    -74       C  
ATOM   2099  O   ILE A 253       2.376  -1.199 -19.069  1.00114.22           O  
ANISOU 2099  O   ILE A 253    15215  14124  14060    850   -156   -111       O  
ATOM   2100  CB  ILE A 253       4.532  -3.253 -19.817  1.00109.60           C  
ANISOU 2100  CB  ILE A 253    14582  13602  13459    651   -172    -56       C  
ATOM   2101  CG1 ILE A 253       5.886  -3.983 -19.762  1.00109.24           C  
ANISOU 2101  CG1 ILE A 253    14542  13563  13403    553   -172    -37       C  
ATOM   2102  CG2 ILE A 253       3.823  -3.484 -21.165  1.00109.55           C  
ANISOU 2102  CG2 ILE A 253    14524  13635  13465    690   -199    -33       C  
ATOM   2103  CD1 ILE A 253       6.880  -3.633 -20.880  1.00108.91           C  
ANISOU 2103  CD1 ILE A 253    14538  13489  13352    512   -204      7       C  
ATOM   2104  N   GLU A 254       3.397  -0.092 -20.754  1.00116.49           N  
ANISOU 2104  N   GLU A 254    15607  14320  14334    831   -227    -44       N  
ATOM   2105  CA  GLU A 254       2.234   0.729 -21.095  1.00119.59           C  
ANISOU 2105  CA  GLU A 254    16004  14694  14742    943   -242    -51       C  
ATOM   2106  C   GLU A 254       1.754   0.476 -22.523  1.00120.84           C  
ANISOU 2106  C   GLU A 254    16113  14890  14909    970   -284    -15       C  
ATOM   2107  O   GLU A 254       2.522   0.623 -23.480  1.00121.03           O  
ANISOU 2107  O   GLU A 254    16182  14886  14917    922   -317     27       O  
ATOM   2108  CB  GLU A 254       2.552   2.221 -20.926  1.00120.63           C  
ANISOU 2108  CB  GLU A 254    16266  14710  14858    977   -259    -49       C  
ATOM   2109  CG  GLU A 254       2.855   2.670 -19.500  1.00121.92           C  
ANISOU 2109  CG  GLU A 254    16493  14824  15007    966   -221    -89       C  
ATOM   2110  CD  GLU A 254       3.053   4.177 -19.386  1.00123.55           C  
ANISOU 2110  CD  GLU A 254    16837  14911  15195   1005   -241    -89       C  
ATOM   2111  OE1 GLU A 254       3.755   4.762 -20.242  1.00123.86           O  
ANISOU 2111  OE1 GLU A 254    16951  14892  15220    970   -282    -47       O  
ATOM   2112  OE2 GLU A 254       2.509   4.778 -18.434  1.00124.34           O  
ANISOU 2112  OE2 GLU A 254    16977  14973  15293   1069   -212   -132       O  
ATOM   2113  N   ASN A 255       0.487   0.087 -22.656  1.00122.37           N  
ANISOU 2113  N   ASN A 255    16215  15153  15128   1041   -282    -30       N  
ATOM   2114  CA  ASN A 255      -0.180   0.037 -23.959  1.00123.61           C  
ANISOU 2114  CA  ASN A 255    16331  15342  15294   1084   -330      2       C  
ATOM   2115  C   ASN A 255      -1.366   1.006 -23.990  1.00124.91           C  
ANISOU 2115  C   ASN A 255    16496  15486  15480   1213   -349    -10       C  
ATOM   2116  O   ASN A 255      -1.494   1.816 -24.913  1.00125.27           O  
ANISOU 2116  O   ASN A 255    16595  15481  15521   1261   -400     23       O  
ATOM   2117  CB  ASN A 255      -0.596  -1.398 -24.338  1.00123.17           C  
ANISOU 2117  CB  ASN A 255    16156  15396  15247   1044   -325      2       C  
ATOM   2118  CG  ASN A 255      -1.644  -1.989 -23.398  1.00123.50           C  
ANISOU 2118  CG  ASN A 255    16099  15514  15312   1080   -283    -42       C  
ATOM   2119  OD1 ASN A 255      -1.517  -1.917 -22.173  1.00123.44           O  
ANISOU 2119  OD1 ASN A 255    16106  15493  15304   1075   -236    -78       O  
ATOM   2120  ND2 ASN A 255      -2.683  -2.584 -23.976  1.00123.20           N  
ANISOU 2120  ND2 ASN A 255    15961  15559  15292   1112   -301    -39       N  
ATOM   2121  N   MET A 256      -2.212   0.914 -22.965  1.00125.51           N  
ANISOU 2121  N   MET A 256    16511  15599  15576   1270   -306    -57       N  
ATOM   2122  CA  MET A 256      -3.316   1.842 -22.733  1.00126.67           C  
ANISOU 2122  CA  MET A 256    16654  15728  15747   1401   -309    -79       C  
ATOM   2123  C   MET A 256      -3.861   1.614 -21.317  1.00126.59           C  
ANISOU 2123  C   MET A 256    16594  15756  15749   1427   -238   -138       C  
ATOM   2124  O   MET A 256      -3.364   2.211 -20.362  1.00126.86           O  
ANISOU 2124  O   MET A 256    16714  15720  15767   1423   -204   -165       O  
ATOM   2125  CB  MET A 256      -4.407   1.704 -23.810  1.00127.47           C  
ANISOU 2125  CB  MET A 256    16668  15893  15873   1473   -358    -56       C  
ATOM   2126  CG  MET A 256      -5.391   2.878 -23.877  1.00129.07           C  
ANISOU 2126  CG  MET A 256    16886  16055  16099   1620   -382    -64       C  
ATOM   2127  SD  MET A 256      -5.822   3.419 -25.554  1.00130.02           S  
ANISOU 2127  SD  MET A 256    17022  16157  16224   1683   -480     -4       S  
ATOM   2128  CE  MET A 256      -6.405   1.903 -26.317  1.00129.21           C  
ANISOU 2128  CE  MET A 256    16762  16202  16131   1625   -499     12       C  
ATOM   2129  N   TYR A 257      -4.844   0.725 -21.181  1.00125.99           N  
ANISOU 2129  N   TYR A 257    16383  15792  15696   1444   -216   -158       N  
ATOM   2130  CA  TYR A 257      -5.542   0.514 -19.907  1.00125.36           C  
ANISOU 2130  CA  TYR A 257    16243  15760  15626   1476   -146   -214       C  
ATOM   2131  C   TYR A 257      -4.741  -0.330 -18.910  1.00123.15           C  
ANISOU 2131  C   TYR A 257    15977  15494  15320   1363    -94   -235       C  
ATOM   2132  O   TYR A 257      -4.387  -1.478 -19.195  1.00122.44           O  
ANISOU 2132  O   TYR A 257    15835  15463  15223   1269    -98   -217       O  
ATOM   2133  CB  TYR A 257      -6.919  -0.115 -20.152  1.00126.47           C  
ANISOU 2133  CB  TYR A 257    16231  16023  15801   1530   -142   -225       C  
ATOM   2134  CG  TYR A 257      -7.611   0.376 -21.409  1.00128.42           C  
ANISOU 2134  CG  TYR A 257    16445  16277  16072   1615   -212   -190       C  
ATOM   2135  CD1 TYR A 257      -7.674  -0.427 -22.550  1.00128.42           C  
ANISOU 2135  CD1 TYR A 257    16384  16338  16073   1563   -265   -148       C  
ATOM   2136  CD2 TYR A 257      -8.196   1.645 -21.460  1.00130.08           C  
ANISOU 2136  CD2 TYR A 257    16694  16429  16301   1749   -230   -197       C  
ATOM   2137  CE1 TYR A 257      -8.306   0.017 -23.710  1.00129.66           C  
ANISOU 2137  CE1 TYR A 257    16516  16502  16247   1637   -336   -113       C  
ATOM   2138  CE2 TYR A 257      -8.834   2.098 -22.616  1.00131.21           C  
ANISOU 2138  CE2 TYR A 257    16810  16577  16466   1831   -302   -161       C  
ATOM   2139  CZ  TYR A 257      -8.885   1.279 -23.736  1.00130.95           C  
ANISOU 2139  CZ  TYR A 257    16715  16610  16431   1771   -357   -118       C  
ATOM   2140  OH  TYR A 257      -9.512   1.720 -24.880  1.00131.15           O  
ANISOU 2140  OH  TYR A 257    16718  16640  16473   1848   -434    -81       O  
ATOM   2141  N   GLY A 258      -4.465   0.252 -17.742  1.00121.38           N  
ANISOU 2141  N   GLY A 258    15827  15212  15080   1373    -47   -273       N  
ATOM   2142  CA  GLY A 258      -3.720  -0.426 -16.680  1.00117.97           C  
ANISOU 2142  CA  GLY A 258    15419  14785  14619   1273     -1   -294       C  
ATOM   2143  C   GLY A 258      -2.213  -0.421 -16.881  1.00115.11           C  
ANISOU 2143  C   GLY A 258    15155  14351  14229   1174    -31   -260       C  
ATOM   2144  O   GLY A 258      -1.711   0.102 -17.882  1.00114.96           O  
ANISOU 2144  O   GLY A 258    15189  14279  14211   1175    -85   -220       O  
ATOM   2145  N   SER A 259      -1.493  -1.004 -15.921  1.00112.11           N  
ANISOU 2145  N   SER A 259    14799  13974  13825   1086      2   -276       N  
ATOM   2146  CA  SER A 259      -0.030  -1.105 -15.981  1.00108.44           C  
ANISOU 2146  CA  SER A 259    14413  13454  13336    986    -23   -247       C  
ATOM   2147  C   SER A 259       0.512  -2.294 -15.183  1.00104.76           C  
ANISOU 2147  C   SER A 259    13917  13036  12852    888      6   -255       C  
ATOM   2148  O   SER A 259      -0.065  -2.692 -14.167  1.00104.64           O  
ANISOU 2148  O   SER A 259    13868  13061  12829    892     55   -294       O  
ATOM   2149  CB  SER A 259       0.630   0.196 -15.498  1.00109.33           C  
ANISOU 2149  CB  SER A 259    14661  13453  13426    998    -29   -255       C  
ATOM   2150  OG  SER A 259       0.307   0.471 -14.145  1.00109.98           O  
ANISOU 2150  OG  SER A 259    14776  13521  13491   1019     24   -305       O  
ATOM   2151  N   ARG A 260       1.620  -2.857 -15.662  1.00100.32           N  
ANISOU 2151  N   ARG A 260    13368  12469  12282    801    -25   -219       N  
ATOM   2152  CA  ARG A 260       2.342  -3.914 -14.949  1.00 96.02           C  
ANISOU 2152  CA  ARG A 260    12811  11954  11720    708     -9   -221       C  
ATOM   2153  C   ARG A 260       3.857  -3.682 -15.020  1.00 91.65           C  
ANISOU 2153  C   ARG A 260    12334  11338  11149    632    -40   -191       C  
ATOM   2154  O   ARG A 260       4.363  -3.151 -16.013  1.00 91.55           O  
ANISOU 2154  O   ARG A 260    12353  11290  11144    633    -78   -158       O  
ATOM   2155  CB  ARG A 260       1.961  -5.309 -15.474  1.00 96.35           C  
ANISOU 2155  CB  ARG A 260    12748  12086  11775    677     -8   -208       C  
ATOM   2156  CG  ARG A 260       2.282  -5.574 -16.945  1.00 96.87           C  
ANISOU 2156  CG  ARG A 260    12789  12163  11856    666    -53   -165       C  
ATOM   2157  CD  ARG A 260       1.922  -6.999 -17.335  1.00 97.45           C  
ANISOU 2157  CD  ARG A 260    12773  12320  11936    629    -50   -158       C  
ATOM   2158  NE  ARG A 260       2.434  -7.359 -18.657  1.00 98.14           N  
ANISOU 2158  NE  ARG A 260    12848  12412  12028    604    -89   -119       N  
ATOM   2159  CZ  ARG A 260       3.583  -7.995 -18.876  1.00 98.51           C  
ANISOU 2159  CZ  ARG A 260    12914  12451  12066    533   -101    -96       C  
ATOM   2160  NH1 ARG A 260       4.359  -8.352 -17.860  1.00 98.32           N  
ANISOU 2160  NH1 ARG A 260    12918  12412  12028    480    -83   -106       N  
ATOM   2161  NH2 ARG A 260       3.960  -8.278 -20.117  1.00 98.30           N  
ANISOU 2161  NH2 ARG A 260    12878  12432  12041    517   -130    -64       N  
ATOM   2162  N   GLU A 261       4.568  -4.073 -13.965  1.00 86.17           N  
ANISOU 2162  N   GLU A 261    11670  10637  10433    566    -25   -203       N  
ATOM   2163  CA  GLU A 261       6.011  -3.828 -13.871  1.00 79.94           C  
ANISOU 2163  CA  GLU A 261    10948   9795   9629    492    -55   -177       C  
ATOM   2164  C   GLU A 261       6.870  -5.060 -14.148  1.00 73.46           C  
ANISOU 2164  C   GLU A 261    10078   9021   8813    416    -71   -149       C  
ATOM   2165  O   GLU A 261       6.719  -6.106 -13.505  1.00 72.62           O  
ANISOU 2165  O   GLU A 261     9929   8963   8701    388    -51   -162       O  
ATOM   2166  CB  GLU A 261       6.376  -3.199 -12.522  1.00 81.47           C  
ANISOU 2166  CB  GLU A 261    11228   9935   9792    469    -40   -206       C  
ATOM   2167  CG  GLU A 261       6.191  -1.682 -12.492  1.00 83.18           C  
ANISOU 2167  CG  GLU A 261    11537  10068   9999    522    -45   -219       C  
ATOM   2168  CD  GLU A 261       6.295  -1.082 -11.099  1.00 83.86           C  
ANISOU 2168  CD  GLU A 261    11710  10102  10049    511    -21   -257       C  
ATOM   2169  OE1 GLU A 261       6.845  -1.745 -10.190  1.00 84.65           O  
ANISOU 2169  OE1 GLU A 261    11814  10222  10129    441    -15   -263       O  
ATOM   2170  OE2 GLU A 261       5.827   0.063 -10.917  1.00 82.84           O  
ANISOU 2170  OE2 GLU A 261    11653   9910   9911    573    -12   -281       O  
ATOM   2171  N   ILE A 262       7.764  -4.916 -15.122  1.00 65.74           N  
ANISOU 2171  N   ILE A 262     9109   8027   7844    386   -105   -110       N  
ATOM   2172  CA  ILE A 262       8.724  -5.960 -15.466  1.00 57.40           C  
ANISOU 2172  CA  ILE A 262     8012   7006   6792    320   -120    -83       C  
ATOM   2173  C   ILE A 262      10.133  -5.553 -15.016  1.00 51.83           C  
ANISOU 2173  C   ILE A 262     7364   6257   6073    252   -142    -65       C  
ATOM   2174  O   ILE A 262      10.403  -4.369 -14.765  1.00 49.16           O  
ANISOU 2174  O   ILE A 262     7101   5855   5721    251   -153    -67       O  
ATOM   2175  CB  ILE A 262       8.693  -6.318 -16.989  1.00 57.81           C  
ANISOU 2175  CB  ILE A 262     8014   7087   6862    333   -136    -52       C  
ATOM   2176  CG1 ILE A 262       9.332  -5.217 -17.843  1.00 59.52           C  
ANISOU 2176  CG1 ILE A 262     8286   7251   7076    329   -162    -23       C  
ATOM   2177  CG2 ILE A 262       7.265  -6.602 -17.455  1.00 56.31           C  
ANISOU 2177  CG2 ILE A 262     7770   6941   6685    399   -122    -67       C  
ATOM   2178  CD1 ILE A 262       9.848  -5.704 -19.200  1.00 60.21           C  
ANISOU 2178  CD1 ILE A 262     8338   7367   7173    307   -178     13       C  
ATOM   2179  N   ILE A 263      11.020  -6.537 -14.904  1.00 44.25           N  
ANISOU 2179  N   ILE A 263     6367   5329   5116    195   -151    -49       N  
ATOM   2180  CA  ILE A 263      12.385  -6.284 -14.465  1.00 39.94           C  
ANISOU 2180  CA  ILE A 263     5858   4756   4561    126   -176    -30       C  
ATOM   2181  C   ILE A 263      13.325  -6.384 -15.659  1.00 36.72           C  
ANISOU 2181  C   ILE A 263     5421   4361   4169     97   -196      9       C  
ATOM   2182  O   ILE A 263      13.380  -7.420 -16.324  1.00 35.24           O  
ANISOU 2182  O   ILE A 263     5169   4224   3998    100   -191     21       O  
ATOM   2183  CB  ILE A 263      12.833  -7.281 -13.349  1.00 38.80           C  
ANISOU 2183  CB  ILE A 263     5695   4639   4408     83   -177    -38       C  
ATOM   2184  CG1 ILE A 263      11.812  -7.345 -12.205  1.00 38.20           C  
ANISOU 2184  CG1 ILE A 263     5642   4561   4311    108   -150    -78       C  
ATOM   2185  CG2 ILE A 263      14.236  -6.948 -12.828  1.00 38.22           C  
ANISOU 2185  CG2 ILE A 263     5657   4540   4325     12   -210    -18       C  
ATOM   2186  CD1 ILE A 263      11.515  -6.025 -11.525  1.00 34.86           C  
ANISOU 2186  CD1 ILE A 263     5304   4077   3865    124   -144   -103       C  
ATOM   2187  N   THR A 264      14.051  -5.303 -15.931  1.00 32.97           N  
ANISOU 2187  N   THR A 264     5001   3840   3687     67   -215     28       N  
ATOM   2188  CA  THR A 264      15.075  -5.315 -16.966  1.00 31.64           C  
ANISOU 2188  CA  THR A 264     4809   3685   3529     27   -230     66       C  
ATOM   2189  C   THR A 264      16.393  -5.794 -16.358  1.00 31.57           C  
ANISOU 2189  C   THR A 264     4777   3695   3522    -43   -247     81       C  
ATOM   2190  O   THR A 264      16.886  -5.207 -15.391  1.00 31.08           O  
ANISOU 2190  O   THR A 264     4766   3600   3445    -85   -265     76       O  
ATOM   2191  CB  THR A 264      15.268  -3.927 -17.616  1.00 33.39           C  
ANISOU 2191  CB  THR A 264     5099   3848   3738     19   -243     84       C  
ATOM   2192  OG1 THR A 264      14.040  -3.499 -18.216  1.00 33.63           O  
ANISOU 2192  OG1 THR A 264     5149   3861   3769     92   -233     73       O  
ATOM   2193  CG2 THR A 264      16.364  -3.978 -18.692  1.00 30.74           C  
ANISOU 2193  CG2 THR A 264     4737   3534   3409    -32   -252    123       C  
ATOM   2194  N   LEU A 265      16.942  -6.865 -16.925  1.00 27.52           N  
ANISOU 2194  N   LEU A 265     4191   3237   3028    -54   -243     98       N  
ATOM   2195  CA  LEU A 265      18.216  -7.413 -16.490  1.00 26.32           C  
ANISOU 2195  CA  LEU A 265     4002   3112   2885   -110   -261    115       C  
ATOM   2196  C   LEU A 265      19.274  -7.032 -17.504  1.00 27.38           C  
ANISOU 2196  C   LEU A 265     4117   3258   3027   -151   -266    149       C  
ATOM   2197  O   LEU A 265      19.338  -7.614 -18.589  1.00 26.41           O  
ANISOU 2197  O   LEU A 265     3944   3171   2917   -132   -247    161       O  
ATOM   2198  CB  LEU A 265      18.147  -8.936 -16.360  1.00 24.04           C  
ANISOU 2198  CB  LEU A 265     3646   2876   2612    -88   -252    109       C  
ATOM   2199  CG  LEU A 265      17.066  -9.549 -15.468  1.00 25.87           C  
ANISOU 2199  CG  LEU A 265     3888   3109   2835    -53   -241     77       C  
ATOM   2200  CD1 LEU A 265      17.005 -11.045 -15.669  1.00 26.80           C  
ANISOU 2200  CD1 LEU A 265     3944   3273   2966    -34   -231     77       C  
ATOM   2201  CD2 LEU A 265      17.293  -9.210 -13.990  1.00 23.38           C  
ANISOU 2201  CD2 LEU A 265     3620   2765   2499    -87   -261     65       C  
ATOM   2202  N   PHE A 266      20.093  -6.048 -17.145  1.00 26.41           N  
ANISOU 2202  N   PHE A 266     4036   3105   2894   -211   -289    164       N  
ATOM   2203  CA  PHE A 266      21.176  -5.574 -18.003  1.00 29.52           C  
ANISOU 2203  CA  PHE A 266     4414   3511   3292   -266   -293    198       C  
ATOM   2204  C   PHE A 266      22.185  -6.689 -18.286  1.00 28.62           C  
ANISOU 2204  C   PHE A 266     4204   3468   3205   -283   -289    215       C  
ATOM   2205  O   PHE A 266      22.603  -7.408 -17.376  1.00 26.19           O  
ANISOU 2205  O   PHE A 266     3861   3184   2908   -291   -306    210       O  
ATOM   2206  CB  PHE A 266      21.858  -4.353 -17.377  1.00 30.06           C  
ANISOU 2206  CB  PHE A 266     4548   3532   3340   -338   -323    208       C  
ATOM   2207  CG  PHE A 266      21.082  -3.074 -17.551  1.00 34.33           C  
ANISOU 2207  CG  PHE A 266     5190   3998   3854   -324   -324    200       C  
ATOM   2208  CD1 PHE A 266      19.886  -2.863 -16.868  1.00 35.54           C  
ANISOU 2208  CD1 PHE A 266     5399   4109   3995   -265   -319    165       C  
ATOM   2209  CD2 PHE A 266      21.547  -2.078 -18.403  1.00 37.43           C  
ANISOU 2209  CD2 PHE A 266     5624   4363   4234   -368   -327    227       C  
ATOM   2210  CE1 PHE A 266      19.156  -1.682 -17.036  1.00 37.08           C  
ANISOU 2210  CE1 PHE A 266     5688   4233   4169   -240   -320    157       C  
ATOM   2211  CE2 PHE A 266      20.828  -0.887 -18.576  1.00 41.86           C  
ANISOU 2211  CE2 PHE A 266     6289   4847   4770   -350   -332    221       C  
ATOM   2212  CZ  PHE A 266      19.628  -0.693 -17.886  1.00 40.76           C  
ANISOU 2212  CZ  PHE A 266     6202   4663   4622   -280   -329    185       C  
ATOM   2213  N   GLY A 267      22.534  -6.845 -19.560  1.00 27.61           N  
ANISOU 2213  N   GLY A 267     4035   3370   3084   -282   -265    234       N  
ATOM   2214  CA  GLY A 267      23.464  -7.885 -19.980  1.00 27.80           C  
ANISOU 2214  CA  GLY A 267     3968   3462   3133   -288   -252    248       C  
ATOM   2215  C   GLY A 267      22.822  -9.239 -20.232  1.00 27.57           C  
ANISOU 2215  C   GLY A 267     3894   3462   3117   -218   -230    230       C  
ATOM   2216  O   GLY A 267      23.527 -10.229 -20.436  1.00 28.52           O  
ANISOU 2216  O   GLY A 267     3944   3632   3259   -210   -221    236       O  
ATOM   2217  N   ILE A 268      21.489  -9.286 -20.195  1.00 25.72           N  
ANISOU 2217  N   ILE A 268     3702   3199   2871   -167   -223    206       N  
ATOM   2218  CA  ILE A 268      20.728 -10.466 -20.611  1.00 23.90           C  
ANISOU 2218  CA  ILE A 268     3440   2993   2646   -108   -201    189       C  
ATOM   2219  C   ILE A 268      19.664 -10.077 -21.653  1.00 25.29           C  
ANISOU 2219  C   ILE A 268     3650   3152   2806    -73   -183    185       C  
ATOM   2220  O   ILE A 268      19.071  -8.995 -21.581  1.00 25.01           O  
ANISOU 2220  O   ILE A 268     3674   3074   2756    -72   -193    183       O  
ATOM   2221  CB  ILE A 268      20.113 -11.199 -19.398  1.00 25.20           C  
ANISOU 2221  CB  ILE A 268     3609   3152   2813    -84   -215    165       C  
ATOM   2222  CG1 ILE A 268      21.239 -11.817 -18.555  1.00 24.66           C  
ANISOU 2222  CG1 ILE A 268     3500   3108   2762   -112   -236    175       C  
ATOM   2223  CG2 ILE A 268      19.118 -12.296 -19.841  1.00 23.82           C  
ANISOU 2223  CG2 ILE A 268     3416   2995   2638    -30   -193    146       C  
ATOM   2224  CD1 ILE A 268      20.842 -12.221 -17.199  1.00 24.48           C  
ANISOU 2224  CD1 ILE A 268     3499   3070   2732   -108   -258    157       C  
ATOM   2225  N   SER A 269      19.450 -10.948 -22.635  1.00 21.59           N  
ANISOU 2225  N   SER A 269     3147   2716   2340    -43   -159    183       N  
ATOM   2226  CA  SER A 269      18.410 -10.725 -23.625  1.00 23.19           C  
ANISOU 2226  CA  SER A 269     3377   2909   2526     -9   -148    180       C  
ATOM   2227  C   SER A 269      17.264 -11.680 -23.345  1.00 23.55           C  
ANISOU 2227  C   SER A 269     3410   2964   2573     38   -146    153       C  
ATOM   2228  O   SER A 269      17.376 -12.891 -23.578  1.00 22.65           O  
ANISOU 2228  O   SER A 269     3257   2882   2465     51   -133    146       O  
ATOM   2229  CB  SER A 269      18.952 -10.917 -25.046  1.00 22.58           C  
ANISOU 2229  CB  SER A 269     3279   2858   2441    -18   -124    198       C  
ATOM   2230  OG  SER A 269      19.906  -9.913 -25.346  1.00 22.45           O  
ANISOU 2230  OG  SER A 269     3278   2832   2418    -69   -124    224       O  
ATOM   2231  N   VAL A 270      16.171 -11.121 -22.829  1.00 22.93           N  
ANISOU 2231  N   VAL A 270     3367   2858   2487     62   -157    138       N  
ATOM   2232  CA  VAL A 270      14.994 -11.892 -22.461  1.00 22.12           C  
ANISOU 2232  CA  VAL A 270     3252   2768   2384    100   -154    112       C  
ATOM   2233  C   VAL A 270      14.047 -12.002 -23.656  1.00 24.15           C  
ANISOU 2233  C   VAL A 270     3507   3038   2631    133   -148    112       C  
ATOM   2234  O   VAL A 270      13.555 -10.993 -24.160  1.00 23.30           O  
ANISOU 2234  O   VAL A 270     3432   2908   2513    148   -157    120       O  
ATOM   2235  CB  VAL A 270      14.255 -11.278 -21.241  1.00 22.28           C  
ANISOU 2235  CB  VAL A 270     3303   2760   2402    112   -164     92       C  
ATOM   2236  CG1 VAL A 270      12.981 -12.051 -20.961  1.00 21.72           C  
ANISOU 2236  CG1 VAL A 270     3212   2711   2329    147   -155     67       C  
ATOM   2237  CG2 VAL A 270      15.147 -11.295 -19.999  1.00 16.94           C  
ANISOU 2237  CG2 VAL A 270     2633   2072   1730     75   -174     91       C  
ATOM   2238  N   LEU A 271      13.823 -13.234 -24.116  1.00 23.46           N  
ANISOU 2238  N   LEU A 271     3386   2984   2542    142   -137    104       N  
ATOM   2239  CA  LEU A 271      12.859 -13.507 -25.176  1.00 24.37           C  
ANISOU 2239  CA  LEU A 271     3499   3117   2644    168   -137    102       C  
ATOM   2240  C   LEU A 271      11.834 -14.479 -24.631  1.00 24.52           C  
ANISOU 2240  C   LEU A 271     3494   3159   2665    184   -136     77       C  
ATOM   2241  O   LEU A 271      11.992 -15.696 -24.775  1.00 24.35           O  
ANISOU 2241  O   LEU A 271     3453   3158   2641    175   -126     70       O  
ATOM   2242  CB  LEU A 271      13.535 -14.114 -26.422  1.00 24.21           C  
ANISOU 2242  CB  LEU A 271     3468   3116   2612    155   -122    115       C  
ATOM   2243  CG  LEU A 271      14.698 -13.394 -27.128  1.00 27.29           C  
ANISOU 2243  CG  LEU A 271     3874   3498   2998    128   -113    141       C  
ATOM   2244  CD1 LEU A 271      15.336 -14.299 -28.175  1.00 24.78           C  
ANISOU 2244  CD1 LEU A 271     3538   3208   2669    120    -89    146       C  
ATOM   2245  CD2 LEU A 271      14.247 -12.096 -27.775  1.00 27.27           C  
ANISOU 2245  CD2 LEU A 271     3913   3469   2979    134   -129    159       C  
ATOM   2246  N   ASP A 272      10.790 -13.938 -24.002  1.00 25.35           N  
ANISOU 2246  N   ASP A 272     3603   3257   2771    207   -144     63       N  
ATOM   2247  CA  ASP A 272       9.703 -14.744 -23.429  1.00 24.68           C  
ANISOU 2247  CA  ASP A 272     3493   3199   2686    217   -140     39       C  
ATOM   2248  C   ASP A 272       9.048 -15.499 -24.584  1.00 22.19           C  
ANISOU 2248  C   ASP A 272     3158   2915   2358    222   -143     40       C  
ATOM   2249  O   ASP A 272       8.671 -14.886 -25.581  1.00 22.28           O  
ANISOU 2249  O   ASP A 272     3176   2927   2361    241   -156     52       O  
ATOM   2250  CB  ASP A 272       8.698 -13.815 -22.733  1.00 25.05           C  
ANISOU 2250  CB  ASP A 272     3545   3237   2737    247   -143     24       C  
ATOM   2251  CG  ASP A 272       7.696 -14.556 -21.839  1.00 28.56           C  
ANISOU 2251  CG  ASP A 272     3960   3712   3181    249   -131     -3       C  
ATOM   2252  OD1 ASP A 272       7.392 -15.752 -22.065  1.00 31.71           O  
ANISOU 2252  OD1 ASP A 272     4334   4142   3573    231   -127     -8       O  
ATOM   2253  OD2 ASP A 272       7.188 -13.908 -20.901  1.00 27.88           O  
ANISOU 2253  OD2 ASP A 272     3880   3615   3097    266   -123    -19       O  
ATOM   2254  N   TYR A 273       8.937 -16.821 -24.480  1.00 23.01           N  
ANISOU 2254  N   TYR A 273     3245   3041   2456    204   -135     28       N  
ATOM   2255  CA  TYR A 273       8.428 -17.596 -25.620  1.00 21.75           C  
ANISOU 2255  CA  TYR A 273     3076   2907   2279    200   -140     28       C  
ATOM   2256  C   TYR A 273       6.988 -17.245 -25.997  1.00 24.55           C  
ANISOU 2256  C   TYR A 273     3410   3289   2629    221   -157     23       C  
ATOM   2257  O   TYR A 273       6.631 -17.294 -27.176  1.00 26.22           O  
ANISOU 2257  O   TYR A 273     3623   3514   2824    226   -172     32       O  
ATOM   2258  CB  TYR A 273       8.619 -19.107 -25.461  1.00 22.61           C  
ANISOU 2258  CB  TYR A 273     3183   3026   2380    174   -130     17       C  
ATOM   2259  CG  TYR A 273       8.929 -19.736 -26.794  1.00 22.86           C  
ANISOU 2259  CG  TYR A 273     3228   3064   2392    167   -129     23       C  
ATOM   2260  CD1 TYR A 273       7.906 -20.176 -27.644  1.00 22.83           C  
ANISOU 2260  CD1 TYR A 273     3221   3087   2368    162   -142     18       C  
ATOM   2261  CD2 TYR A 273      10.246 -19.828 -27.244  1.00 21.75           C  
ANISOU 2261  CD2 TYR A 273     3104   2906   2253    165   -114     35       C  
ATOM   2262  CE1 TYR A 273       8.200 -20.717 -28.898  1.00 22.08           C  
ANISOU 2262  CE1 TYR A 273     3148   2993   2248    153   -141     23       C  
ATOM   2263  CE2 TYR A 273      10.546 -20.368 -28.491  1.00 22.73           C  
ANISOU 2263  CE2 TYR A 273     3246   3036   2356    161   -106     38       C  
ATOM   2264  CZ  TYR A 273       9.519 -20.810 -29.312  1.00 23.74           C  
ANISOU 2264  CZ  TYR A 273     3380   3183   2458    154   -120     31       C  
ATOM   2265  OH  TYR A 273       9.824 -21.346 -30.548  1.00 27.05           O  
ANISOU 2265  OH  TYR A 273     3825   3603   2848    148   -111     32       O  
ATOM   2266  N   ILE A 274       6.171 -16.864 -25.014  1.00 23.64           N  
ANISOU 2266  N   ILE A 274     3274   3182   2525    236   -155      8       N  
ATOM   2267  CA  ILE A 274       4.805 -16.422 -25.302  1.00 25.22           C  
ANISOU 2267  CA  ILE A 274     3443   3414   2726    265   -171      2       C  
ATOM   2268  C   ILE A 274       4.793 -15.224 -26.281  1.00 24.12           C  
ANISOU 2268  C   ILE A 274     3322   3256   2587    302   -194     23       C  
ATOM   2269  O   ILE A 274       4.013 -15.199 -27.237  1.00 24.53           O  
ANISOU 2269  O   ILE A 274     3358   3333   2629    316   -219     31       O  
ATOM   2270  CB  ILE A 274       4.005 -16.123 -23.995  1.00 26.41           C  
ANISOU 2270  CB  ILE A 274     3567   3578   2890    281   -156    -21       C  
ATOM   2271  CG1 ILE A 274       2.500 -16.189 -24.257  1.00 32.37           C  
ANISOU 2271  CG1 ILE A 274     4268   4385   3646    300   -167    -31       C  
ATOM   2272  CG2 ILE A 274       4.402 -14.773 -23.390  1.00 29.54           C  
ANISOU 2272  CG2 ILE A 274     3992   3932   3300    314   -152    -19       C  
ATOM   2273  CD1 ILE A 274       1.641 -16.247 -22.982  1.00 36.92           C  
ANISOU 2273  CD1 ILE A 274     4808   4990   4231    304   -142    -58       C  
ATOM   2274  N   ASP A 275       5.681 -14.261 -26.051  1.00 21.87           N  
ANISOU 2274  N   ASP A 275     3074   2926   2308    312   -190     35       N  
ATOM   2275  CA  ASP A 275       5.799 -13.077 -26.901  1.00 23.25           C  
ANISOU 2275  CA  ASP A 275     3282   3072   2479    339   -212     58       C  
ATOM   2276  C   ASP A 275       6.388 -13.427 -28.266  1.00 24.00           C  
ANISOU 2276  C   ASP A 275     3399   3169   2552    316   -220     81       C  
ATOM   2277  O   ASP A 275       5.956 -12.884 -29.278  1.00 24.48           O  
ANISOU 2277  O   ASP A 275     3474   3230   2600    336   -246     98       O  
ATOM   2278  CB  ASP A 275       6.641 -11.994 -26.217  1.00 25.20           C  
ANISOU 2278  CB  ASP A 275     3571   3268   2736    344   -204     64       C  
ATOM   2279  CG  ASP A 275       6.025 -11.499 -24.909  1.00 27.51           C  
ANISOU 2279  CG  ASP A 275     3855   3553   3045    372   -194     40       C  
ATOM   2280  OD1 ASP A 275       4.787 -11.522 -24.770  1.00 29.28           O  
ANISOU 2280  OD1 ASP A 275     4043   3808   3276    407   -198     25       O  
ATOM   2281  OD2 ASP A 275       6.788 -11.088 -24.011  1.00 37.37           O  
ANISOU 2281  OD2 ASP A 275     5133   4767   4298    356   -181     36       O  
ATOM   2282  N   LEU A 276       7.373 -14.325 -28.290  1.00 22.58           N  
ANISOU 2282  N   LEU A 276     3224   2990   2366    276   -198     80       N  
ATOM   2283  CA  LEU A 276       7.885 -14.864 -29.553  1.00 23.92           C  
ANISOU 2283  CA  LEU A 276     3411   3168   2511    253   -197     93       C  
ATOM   2284  C   LEU A 276       6.753 -15.525 -30.341  1.00 24.53           C  
ANISOU 2284  C   LEU A 276     3469   3282   2569    257   -219     88       C  
ATOM   2285  O   LEU A 276       6.598 -15.290 -31.543  1.00 23.83           O  
ANISOU 2285  O   LEU A 276     3403   3196   2456    258   -238    105       O  
ATOM   2286  CB  LEU A 276       9.010 -15.883 -29.307  1.00 22.32           C  
ANISOU 2286  CB  LEU A 276     3207   2964   2308    220   -167     86       C  
ATOM   2287  CG  LEU A 276      10.407 -15.425 -28.850  1.00 24.16           C  
ANISOU 2287  CG  LEU A 276     3454   3170   2555    206   -147     97       C  
ATOM   2288  CD1 LEU A 276      11.251 -16.622 -28.463  1.00 18.81           C  
ANISOU 2288  CD1 LEU A 276     2763   2500   1884    185   -123     86       C  
ATOM   2289  CD2 LEU A 276      11.129 -14.622 -29.919  1.00 23.69           C  
ANISOU 2289  CD2 LEU A 276     3427   3095   2479    197   -145    123       C  
ATOM   2290  N   TYR A 277       5.962 -16.342 -29.648  1.00 24.58           N  
ANISOU 2290  N   TYR A 277     3438   3317   2584    252   -217     65       N  
ATOM   2291  CA  TYR A 277       4.866 -17.079 -30.261  1.00 24.83           C  
ANISOU 2291  CA  TYR A 277     3446   3389   2598    244   -238     58       C  
ATOM   2292  C   TYR A 277       3.798 -16.129 -30.794  1.00 25.05           C  
ANISOU 2292  C   TYR A 277     3458   3433   2626    282   -277     71       C  
ATOM   2293  O   TYR A 277       3.355 -16.263 -31.935  1.00 26.55           O  
ANISOU 2293  O   TYR A 277     3656   3641   2791    277   -305     83       O  
ATOM   2294  CB  TYR A 277       4.266 -18.084 -29.267  1.00 23.82           C  
ANISOU 2294  CB  TYR A 277     3281   3289   2479    223   -226     32       C  
ATOM   2295  CG  TYR A 277       3.294 -19.068 -29.881  1.00 25.32           C  
ANISOU 2295  CG  TYR A 277     3451   3522   2648    196   -246     24       C  
ATOM   2296  CD1 TYR A 277       3.723 -20.325 -30.315  1.00 24.01           C  
ANISOU 2296  CD1 TYR A 277     3313   3353   2457    154   -236     17       C  
ATOM   2297  CD2 TYR A 277       1.939 -18.747 -30.016  1.00 23.71           C  
ANISOU 2297  CD2 TYR A 277     3200   3361   2448    212   -275     23       C  
ATOM   2298  CE1 TYR A 277       2.830 -21.231 -30.877  1.00 21.10           C  
ANISOU 2298  CE1 TYR A 277     2935   3019   2063    121   -256      9       C  
ATOM   2299  CE2 TYR A 277       1.039 -19.641 -30.574  1.00 20.89           C  
ANISOU 2299  CE2 TYR A 277     2821   3047   2068    179   -298     17       C  
ATOM   2300  CZ  TYR A 277       1.486 -20.875 -30.999  1.00 23.24           C  
ANISOU 2300  CZ  TYR A 277     3155   3337   2337    129   -289     10       C  
ATOM   2301  OH  TYR A 277       0.583 -21.748 -31.539  1.00 21.67           O  
ANISOU 2301  OH  TYR A 277     2942   3177   2113     89   -314      3       O  
ATOM   2302  N   LYS A 278       3.397 -15.160 -29.978  1.00 24.98           N  
ANISOU 2302  N   LYS A 278     3431   3415   2644    322   -279     68       N  
ATOM   2303  CA  LYS A 278       2.386 -14.179 -30.401  1.00 24.33           C  
ANISOU 2303  CA  LYS A 278     3333   3343   2567    371   -316     79       C  
ATOM   2304  C   LYS A 278       2.801 -13.349 -31.624  1.00 24.45           C  
ANISOU 2304  C   LYS A 278     3403   3327   2561    384   -344    111       C  
ATOM   2305  O   LYS A 278       1.958 -12.952 -32.417  1.00 24.28           O  
ANISOU 2305  O   LYS A 278     3373   3322   2530    412   -386    126       O  
ATOM   2306  CB  LYS A 278       1.999 -13.257 -29.244  1.00 22.52           C  
ANISOU 2306  CB  LYS A 278     3085   3101   2369    418   -306     66       C  
ATOM   2307  CG  LYS A 278       1.084 -13.933 -28.220  1.00 28.69           C  
ANISOU 2307  CG  LYS A 278     3803   3931   3168    415   -287     36       C  
ATOM   2308  CD  LYS A 278       0.863 -13.080 -26.977  1.00 25.47           C  
ANISOU 2308  CD  LYS A 278     3386   3506   2786    457   -266     18       C  
ATOM   2309  CE  LYS A 278      -0.267 -13.662 -26.127  1.00 28.97           C  
ANISOU 2309  CE  LYS A 278     3757   4008   3241    458   -248    -10       C  
ATOM   2310  NZ  LYS A 278      -0.527 -12.864 -24.898  1.00 30.72           N  
ANISOU 2310  NZ  LYS A 278     3973   4216   3483    500   -220    -32       N  
ATOM   2311  N   LYS A 279       4.090 -13.064 -31.768  1.00 24.66           N  
ANISOU 2311  N   LYS A 279     3482   3309   2578    363   -322    124       N  
ATOM   2312  CA  LYS A 279       4.520 -12.222 -32.875  1.00 26.64           C  
ANISOU 2312  CA  LYS A 279     3789   3528   2804    367   -343    156       C  
ATOM   2313  C   LYS A 279       4.840 -13.020 -34.134  1.00 25.74           C  
ANISOU 2313  C   LYS A 279     3699   3431   2650    326   -346    167       C  
ATOM   2314  O   LYS A 279       4.560 -12.553 -35.243  1.00 27.00           O  
ANISOU 2314  O   LYS A 279     3892   3587   2782    334   -381    191       O  
ATOM   2315  CB  LYS A 279       5.709 -11.348 -32.474  1.00 29.20           C  
ANISOU 2315  CB  LYS A 279     4160   3798   3135    360   -319    168       C  
ATOM   2316  CG  LYS A 279       5.925 -10.159 -33.403  1.00 31.46           C  
ANISOU 2316  CG  LYS A 279     4510   4043   3399    373   -346    202       C  
ATOM   2317  CD  LYS A 279       7.276  -9.512 -33.167  1.00 37.84           C  
ANISOU 2317  CD  LYS A 279     5366   4805   4206    342   -319    215       C  
ATOM   2318  CE  LYS A 279       7.588  -8.466 -34.234  1.00 40.70           C  
ANISOU 2318  CE  LYS A 279     5800   5128   4536    338   -342    253       C  
ATOM   2319  NZ  LYS A 279       6.535  -7.408 -34.347  1.00 43.04           N  
ANISOU 2319  NZ  LYS A 279     6119   5397   4836    399   -391    266       N  
ATOM   2320  N   PHE A 280       5.392 -14.224 -33.968  1.00 22.53           N  
ANISOU 2320  N   PHE A 280     3281   3040   2238    286   -312    148       N  
ATOM   2321  CA  PHE A 280       5.943 -14.973 -35.105  1.00 24.70           C  
ANISOU 2321  CA  PHE A 280     3590   3322   2473    247   -303    154       C  
ATOM   2322  C   PHE A 280       5.150 -16.199 -35.579  1.00 25.51           C  
ANISOU 2322  C   PHE A 280     3674   3466   2553    225   -318    138       C  
ATOM   2323  O   PHE A 280       5.444 -16.753 -36.649  1.00 27.56           O  
ANISOU 2323  O   PHE A 280     3972   3729   2772    196   -316    142       O  
ATOM   2324  CB  PHE A 280       7.408 -15.368 -34.835  1.00 22.18           C  
ANISOU 2324  CB  PHE A 280     3289   2983   2157    218   -251    148       C  
ATOM   2325  CG  PHE A 280       8.325 -14.194 -34.557  1.00 22.13           C  
ANISOU 2325  CG  PHE A 280     3307   2938   2163    224   -237    168       C  
ATOM   2326  CD1 PHE A 280       9.229 -14.243 -33.507  1.00 19.53           C  
ANISOU 2326  CD1 PHE A 280     2962   2594   1863    215   -204    158       C  
ATOM   2327  CD2 PHE A 280       8.293 -13.048 -35.361  1.00 24.63           C  
ANISOU 2327  CD2 PHE A 280     3669   3231   2459    232   -261    198       C  
ATOM   2328  CE1 PHE A 280      10.083 -13.175 -33.250  1.00 22.49           C  
ANISOU 2328  CE1 PHE A 280     3361   2936   2247    210   -195    176       C  
ATOM   2329  CE2 PHE A 280       9.140 -11.975 -35.117  1.00 24.56           C  
ANISOU 2329  CE2 PHE A 280     3690   3183   2457    227   -250    217       C  
ATOM   2330  CZ  PHE A 280      10.036 -12.036 -34.055  1.00 26.28           C  
ANISOU 2330  CZ  PHE A 280     3888   3391   2706    214   -217    205       C  
ATOM   2331  N   SER A 281       4.155 -16.625 -34.809  1.00 22.39           N  
ANISOU 2331  N   SER A 281     3224   3101   2181    234   -331    119       N  
ATOM   2332  CA  SER A 281       3.447 -17.873 -35.135  1.00 24.11           C  
ANISOU 2332  CA  SER A 281     3426   3358   2378    200   -343    102       C  
ATOM   2333  C   SER A 281       2.337 -17.718 -36.175  1.00 24.83           C  
ANISOU 2333  C   SER A 281     3512   3481   2441    203   -399    116       C  
ATOM   2334  O   SER A 281       1.992 -18.691 -36.851  1.00 23.30           O  
ANISOU 2334  O   SER A 281     3330   3311   2214    163   -413    109       O  
ATOM   2335  CB  SER A 281       2.861 -18.520 -33.882  1.00 22.09           C  
ANISOU 2335  CB  SER A 281     3114   3126   2151    195   -331     76       C  
ATOM   2336  OG  SER A 281       1.716 -17.808 -33.470  1.00 24.42           O  
ANISOU 2336  OG  SER A 281     3357   3450   2471    230   -361     78       O  
ATOM   2337  N   PHE A 282       1.778 -16.510 -36.270  1.00 24.88           N  
ANISOU 2337  N   PHE A 282     3505   3486   2462    249   -435    137       N  
ATOM   2338  CA  PHE A 282       0.634 -16.205 -37.146  1.00 28.03           C  
ANISOU 2338  CA  PHE A 282     3889   3919   2843    263   -498    155       C  
ATOM   2339  C   PHE A 282      -0.602 -17.047 -36.820  1.00 29.83           C  
ANISOU 2339  C   PHE A 282     4046   4209   3079    246   -522    135       C  
ATOM   2340  O   PHE A 282      -1.276 -17.594 -37.706  1.00 27.95           O  
ANISOU 2340  O   PHE A 282     3806   4005   2807    216   -563    140       O  
ATOM   2341  CB  PHE A 282       1.025 -16.278 -38.628  1.00 28.04           C  
ANISOU 2341  CB  PHE A 282     3961   3906   2786    235   -519    176       C  
ATOM   2342  CG  PHE A 282       1.858 -15.119 -39.072  1.00 31.12           C  
ANISOU 2342  CG  PHE A 282     4412   4246   3167    258   -514    205       C  
ATOM   2343  CD1 PHE A 282       1.288 -14.074 -39.788  1.00 33.05           C  
ANISOU 2343  CD1 PHE A 282     4677   4484   3399    293   -571    237       C  
ATOM   2344  CD2 PHE A 282       3.208 -15.049 -38.743  1.00 31.28           C  
ANISOU 2344  CD2 PHE A 282     4469   4226   3191    244   -456    201       C  
ATOM   2345  CE1 PHE A 282       2.056 -12.990 -40.185  1.00 35.46           C  
ANISOU 2345  CE1 PHE A 282     5047   4737   3691    308   -567    265       C  
ATOM   2346  CE2 PHE A 282       3.979 -13.967 -39.136  1.00 30.05           C  
ANISOU 2346  CE2 PHE A 282     4367   4025   3024    255   -450    228       C  
ATOM   2347  CZ  PHE A 282       3.403 -12.937 -39.853  1.00 33.53           C  
ANISOU 2347  CZ  PHE A 282     4837   4454   3448    284   -505    260       C  
ATOM   2348  N   THR A 283      -0.862 -17.152 -35.519  1.00 30.63           N  
ANISOU 2348  N   THR A 283     4091   4324   3223    259   -493    113       N  
ATOM   2349  CA  THR A 283      -2.088 -17.731 -34.984  1.00 30.95           C  
ANISOU 2349  CA  THR A 283     4052   4428   3280    248   -508     95       C  
ATOM   2350  C   THR A 283      -2.744 -16.681 -34.097  1.00 32.64           C  
ANISOU 2350  C   THR A 283     4206   4655   3542    316   -511     94       C  
ATOM   2351  O   THR A 283      -2.099 -15.713 -33.688  1.00 31.64           O  
ANISOU 2351  O   THR A 283     4108   4480   3434    360   -490    100       O  
ATOM   2352  CB  THR A 283      -1.791 -18.962 -34.104  1.00 30.87           C  
ANISOU 2352  CB  THR A 283     4034   4422   3272    195   -461     66       C  
ATOM   2353  OG1 THR A 283      -1.031 -18.552 -32.958  1.00 28.18           O  
ANISOU 2353  OG1 THR A 283     3699   4044   2963    220   -412     55       O  
ATOM   2354  CG2 THR A 283      -1.024 -20.045 -34.895  1.00 27.08           C  
ANISOU 2354  CG2 THR A 283     3623   3918   2746    135   -450     62       C  
ATOM   2355  N   ASN A 284      -4.035 -16.850 -33.835  1.00 34.60           N  
ANISOU 2355  N   ASN A 284     4370   4970   3806    323   -535     85       N  
ATOM   2356  CA  ASN A 284      -4.662 -16.216 -32.684  1.00 35.24           C  
ANISOU 2356  CA  ASN A 284     4384   5074   3934    377   -516     70       C  
ATOM   2357  C   ASN A 284      -5.372 -17.341 -31.979  1.00 34.36           C  
ANISOU 2357  C   ASN A 284     4205   5024   3825    322   -495     43       C  
ATOM   2358  O   ASN A 284      -6.244 -17.996 -32.556  1.00 34.88           O  
ANISOU 2358  O   ASN A 284     4227   5149   3875    284   -533     45       O  
ATOM   2359  CB  ASN A 284      -5.633 -15.083 -33.060  1.00 38.84           C  
ANISOU 2359  CB  ASN A 284     4792   5555   4411    456   -567     87       C  
ATOM   2360  CG  ASN A 284      -6.101 -14.251 -31.827  1.00 41.81           C  
ANISOU 2360  CG  ASN A 284     5113   5937   4835    526   -536     68       C  
ATOM   2361  OD1 ASN A 284      -5.631 -14.454 -30.697  1.00 39.72           O  
ANISOU 2361  OD1 ASN A 284     4854   5654   4583    512   -477     44       O  
ATOM   2362  ND2 ASN A 284      -7.026 -13.316 -32.057  1.00 36.95           N  
ANISOU 2362  ND2 ASN A 284     4448   5348   4244    605   -577     79       N  
ATOM   2363  N   GLN A 285      -4.973 -17.573 -30.736  1.00 32.16           N  
ANISOU 2363  N   GLN A 285     3925   4729   3564    312   -437     19       N  
ATOM   2364  CA  GLN A 285      -5.425 -18.732 -29.997  1.00 31.17           C  
ANISOU 2364  CA  GLN A 285     3758   4649   3434    247   -410     -5       C  
ATOM   2365  C   GLN A 285      -6.546 -18.384 -29.027  1.00 30.74           C  
ANISOU 2365  C   GLN A 285     3609   4657   3414    278   -393    -23       C  
ATOM   2366  O   GLN A 285      -6.637 -17.242 -28.573  1.00 34.15           O  
ANISOU 2366  O   GLN A 285     4024   5075   3876    356   -383    -25       O  
ATOM   2367  CB  GLN A 285      -4.241 -19.369 -29.264  1.00 29.71           C  
ANISOU 2367  CB  GLN A 285     3641   4408   3240    207   -358    -18       C  
ATOM   2368  CG  GLN A 285      -3.137 -19.881 -30.178  1.00 31.12           C  
ANISOU 2368  CG  GLN A 285     3906   4533   3386    174   -366     -5       C  
ATOM   2369  CD  GLN A 285      -3.532 -21.112 -30.979  1.00 33.92           C  
ANISOU 2369  CD  GLN A 285     4268   4918   3703    103   -391     -6       C  
ATOM   2370  OE1 GLN A 285      -4.701 -21.499 -31.016  1.00 35.81           O  
ANISOU 2370  OE1 GLN A 285     4443   5223   3940     76   -415    -11       O  
ATOM   2371  NE2 GLN A 285      -2.549 -21.732 -31.633  1.00 31.18           N  
ANISOU 2371  NE2 GLN A 285     3999   4523   3324     71   -386     -2       N  
ATOM   2372  N   PRO A 286      -7.420 -19.361 -28.721  1.00 29.77           N  
ANISOU 2372  N   PRO A 286     3423   4604   3284    217   -389    -38       N  
ATOM   2373  CA  PRO A 286      -8.420 -19.176 -27.654  1.00 28.65           C  
ANISOU 2373  CA  PRO A 286     3188   4528   3171    234   -357    -61       C  
ATOM   2374  C   PRO A 286      -7.799 -19.139 -26.256  1.00 28.49           C  
ANISOU 2374  C   PRO A 286     3199   4468   3159    234   -289    -83       C  
ATOM   2375  O   PRO A 286      -8.389 -18.588 -25.329  1.00 27.36           O  
ANISOU 2375  O   PRO A 286     2997   4356   3041    275   -256   -102       O  
ATOM   2376  CB  PRO A 286      -9.313 -20.408 -27.778  1.00 28.87           C  
ANISOU 2376  CB  PRO A 286     3159   4632   3177    144   -369    -68       C  
ATOM   2377  CG  PRO A 286      -9.025 -20.977 -29.123  1.00 30.97           C  
ANISOU 2377  CG  PRO A 286     3478   4881   3408    100   -424    -46       C  
ATOM   2378  CD  PRO A 286      -7.639 -20.603 -29.483  1.00 27.56           C  
ANISOU 2378  CD  PRO A 286     3154   4352   2967    129   -418    -34       C  
ATOM   2379  N   SER A 287      -6.616 -19.729 -26.113  1.00 30.08           N  
ANISOU 2379  N   SER A 287     3491   4601   3338    190   -270    -82       N  
ATOM   2380  CA  SER A 287      -5.928 -19.799 -24.826  1.00 29.18           C  
ANISOU 2380  CA  SER A 287     3415   4446   3226    182   -214   -100       C  
ATOM   2381  C   SER A 287      -4.420 -19.759 -25.032  1.00 29.01           C  
ANISOU 2381  C   SER A 287     3494   4335   3193    182   -212    -87       C  
ATOM   2382  O   SER A 287      -3.908 -20.241 -26.050  1.00 27.08           O  
ANISOU 2382  O   SER A 287     3294   4067   2929    156   -241    -71       O  
ATOM   2383  CB  SER A 287      -6.337 -21.081 -24.085  1.00 29.72           C  
ANISOU 2383  CB  SER A 287     3466   4553   3274     94   -185   -117       C  
ATOM   2384  OG  SER A 287      -5.620 -21.245 -22.879  1.00 31.52           O  
ANISOU 2384  OG  SER A 287     3742   4738   3497     78   -138   -131       O  
ATOM   2385  N   TYR A 288      -3.714 -19.182 -24.064  1.00 30.21           N  
ANISOU 2385  N   TYR A 288     3681   4440   3358    211   -177    -96       N  
ATOM   2386  CA  TYR A 288      -2.250 -19.131 -24.104  1.00 29.89           C  
ANISOU 2386  CA  TYR A 288     3725   4321   3310    209   -172    -84       C  
ATOM   2387  C   TYR A 288      -1.575 -19.848 -22.934  1.00 30.64           C  
ANISOU 2387  C   TYR A 288     3858   4389   3395    163   -134    -98       C  
ATOM   2388  O   TYR A 288      -0.396 -19.627 -22.654  1.00 32.67           O  
ANISOU 2388  O   TYR A 288     4174   4587   3654    170   -126    -91       O  
ATOM   2389  CB  TYR A 288      -1.748 -17.691 -24.287  1.00 28.64           C  
ANISOU 2389  CB  TYR A 288     3592   4118   3172    281   -180    -73       C  
ATOM   2390  CG  TYR A 288      -1.949 -17.213 -25.713  1.00 29.92           C  
ANISOU 2390  CG  TYR A 288     3753   4284   3333    312   -227    -49       C  
ATOM   2391  CD1 TYR A 288      -3.026 -16.397 -26.054  1.00 29.34           C  
ANISOU 2391  CD1 TYR A 288     3624   4249   3276    368   -251    -47       C  
ATOM   2392  CD2 TYR A 288      -1.079 -17.610 -26.727  1.00 24.75           C  
ANISOU 2392  CD2 TYR A 288     3151   3595   2656    285   -246    -29       C  
ATOM   2393  CE1 TYR A 288      -3.226 -15.975 -27.371  1.00 25.24           C  
ANISOU 2393  CE1 TYR A 288     3108   3731   2751    394   -301    -22       C  
ATOM   2394  CE2 TYR A 288      -1.274 -17.199 -28.041  1.00 26.65           C  
ANISOU 2394  CE2 TYR A 288     3398   3840   2888    306   -289     -7       C  
ATOM   2395  CZ  TYR A 288      -2.342 -16.382 -28.355  1.00 26.80           C  
ANISOU 2395  CZ  TYR A 288     3367   3893   2922    359   -319     -2       C  
ATOM   2396  OH  TYR A 288      -2.522 -15.979 -29.663  1.00 28.51           O  
ANISOU 2396  OH  TYR A 288     3596   4110   3125    379   -367     24       O  
ATOM   2397  N   SER A 289      -2.320 -20.728 -22.272  1.00 31.48           N  
ANISOU 2397  N   SER A 289     3932   4539   3489    113   -115   -114       N  
ATOM   2398  CA  SER A 289      -1.723 -21.637 -21.305  1.00 32.60           C  
ANISOU 2398  CA  SER A 289     4120   4655   3614     59    -88   -122       C  
ATOM   2399  C   SER A 289      -0.805 -22.584 -22.067  1.00 32.97           C  
ANISOU 2399  C   SER A 289     4226   4660   3641     23   -109   -107       C  
ATOM   2400  O   SER A 289      -1.056 -22.885 -23.240  1.00 34.25           O  
ANISOU 2400  O   SER A 289     4381   4837   3794     15   -138    -98       O  
ATOM   2401  CB  SER A 289      -2.794 -22.430 -20.557  1.00 32.75           C  
ANISOU 2401  CB  SER A 289     4095   4732   3617      3    -65   -141       C  
ATOM   2402  OG  SER A 289      -3.195 -23.573 -21.294  1.00 36.03           O  
ANISOU 2402  OG  SER A 289     4507   5173   4009    -59    -87   -135       O  
ATOM   2403  N   LEU A 290       0.259 -23.040 -21.411  1.00 32.56           N  
ANISOU 2403  N   LEU A 290     4234   4557   3582      4    -95   -106       N  
ATOM   2404  CA  LEU A 290       1.227 -23.918 -22.055  1.00 30.84           C  
ANISOU 2404  CA  LEU A 290     4073   4296   3350    -18   -110    -94       C  
ATOM   2405  C   LEU A 290       0.597 -25.244 -22.468  1.00 31.17           C  
ANISOU 2405  C   LEU A 290     4120   4361   3363    -80   -120    -99       C  
ATOM   2406  O   LEU A 290       0.979 -25.812 -23.496  1.00 31.70           O  
ANISOU 2406  O   LEU A 290     4219   4409   3416    -90   -139    -92       O  
ATOM   2407  CB  LEU A 290       2.439 -24.159 -21.154  1.00 31.14           C  
ANISOU 2407  CB  LEU A 290     4164   4279   3388    -21    -96    -91       C  
ATOM   2408  CG  LEU A 290       3.623 -24.876 -21.813  1.00 30.75           C  
ANISOU 2408  CG  LEU A 290     4169   4182   3333    -24   -108    -79       C  
ATOM   2409  CD1 LEU A 290       4.126 -24.110 -23.049  1.00 29.39           C  
ANISOU 2409  CD1 LEU A 290     3992   4001   3172     20   -122    -66       C  
ATOM   2410  CD2 LEU A 290       4.744 -25.079 -20.802  1.00 30.08           C  
ANISOU 2410  CD2 LEU A 290     4125   4052   3253    -23    -99    -75       C  
ATOM   2411  N   ASP A 291      -0.360 -25.718 -21.664  1.00 29.43           N  
ANISOU 2411  N   ASP A 291     3871   4180   3131   -126   -104   -113       N  
ATOM   2412  CA  ASP A 291      -1.148 -26.919 -21.958  1.00 32.50           C  
ANISOU 2412  CA  ASP A 291     4260   4599   3489   -197   -114   -118       C  
ATOM   2413  C   ASP A 291      -1.801 -26.791 -23.312  1.00 30.12           C  
ANISOU 2413  C   ASP A 291     3923   4335   3186   -193   -146   -113       C  
ATOM   2414  O   ASP A 291      -1.761 -27.705 -24.124  1.00 27.81           O  
ANISOU 2414  O   ASP A 291     3668   4031   2867   -234   -167   -110       O  
ATOM   2415  CB  ASP A 291      -2.286 -27.088 -20.942  1.00 35.97           C  
ANISOU 2415  CB  ASP A 291     4650   5095   3921   -242    -89   -133       C  
ATOM   2416  CG  ASP A 291      -1.950 -28.043 -19.824  1.00 41.27           C  
ANISOU 2416  CG  ASP A 291     5380   5735   4567   -298    -67   -137       C  
ATOM   2417  OD1 ASP A 291      -1.072 -28.917 -20.009  1.00 42.40           O  
ANISOU 2417  OD1 ASP A 291     5599   5817   4693   -317    -80   -129       O  
ATOM   2418  OD2 ASP A 291      -2.592 -27.915 -18.753  1.00 46.60           O  
ANISOU 2418  OD2 ASP A 291     6024   6445   5237   -322    -37   -149       O  
ATOM   2419  N   TYR A 292      -2.426 -25.641 -23.526  1.00 29.66           N  
ANISOU 2419  N   TYR A 292     3797   4320   3153   -144   -151   -111       N  
ATOM   2420  CA  TYR A 292      -3.193 -25.406 -24.722  1.00 29.56           C  
ANISOU 2420  CA  TYR A 292     3741   4352   3139   -137   -187   -104       C  
ATOM   2421  C   TYR A 292      -2.292 -25.303 -25.952  1.00 27.52           C  
ANISOU 2421  C   TYR A 292     3537   4046   2873   -110   -214    -89       C  
ATOM   2422  O   TYR A 292      -2.564 -25.939 -26.972  1.00 24.87           O  
ANISOU 2422  O   TYR A 292     3217   3721   2511   -145   -243    -84       O  
ATOM   2423  CB  TYR A 292      -4.046 -24.150 -24.570  1.00 30.94           C  
ANISOU 2423  CB  TYR A 292     3831   4580   3345    -79   -188   -106       C  
ATOM   2424  CG  TYR A 292      -5.114 -24.093 -25.609  1.00 31.68           C  
ANISOU 2424  CG  TYR A 292     3865   4736   3436    -84   -229    -99       C  
ATOM   2425  CD1 TYR A 292      -4.882 -23.495 -26.848  1.00 28.97           C  
ANISOU 2425  CD1 TYR A 292     3534   4378   3094    -41   -269    -81       C  
ATOM   2426  CD2 TYR A 292      -6.357 -24.678 -25.371  1.00 30.77           C  
ANISOU 2426  CD2 TYR A 292     3681   4698   3312   -140   -231   -109       C  
ATOM   2427  CE1 TYR A 292      -5.883 -23.471 -27.824  1.00 33.11           C  
ANISOU 2427  CE1 TYR A 292     4006   4963   3612    -50   -315    -72       C  
ATOM   2428  CE2 TYR A 292      -7.349 -24.660 -26.332  1.00 33.63           C  
ANISOU 2428  CE2 TYR A 292     3983   5125   3671   -151   -275   -101       C  
ATOM   2429  CZ  TYR A 292      -7.112 -24.054 -27.545  1.00 31.77           C  
ANISOU 2429  CZ  TYR A 292     3762   4872   3437   -103   -320    -82       C  
ATOM   2430  OH  TYR A 292      -8.117 -24.048 -28.470  1.00 38.45           O  
ANISOU 2430  OH  TYR A 292     4549   5783   4278   -116   -371    -72       O  
ATOM   2431  N   ILE A 293      -1.220 -24.516 -25.849  1.00 24.73           N  
ANISOU 2431  N   ILE A 293     3217   3642   2539    -54   -202    -81       N  
ATOM   2432  CA  ILE A 293      -0.306 -24.324 -26.977  1.00 22.85           C  
ANISOU 2432  CA  ILE A 293     3027   3361   2292    -28   -219    -65       C  
ATOM   2433  C   ILE A 293       0.457 -25.616 -27.295  1.00 24.50           C  
ANISOU 2433  C   ILE A 293     3307   3529   2472    -72   -214    -69       C  
ATOM   2434  O   ILE A 293       0.643 -25.956 -28.471  1.00 24.68           O  
ANISOU 2434  O   ILE A 293     3364   3542   2472    -81   -233    -63       O  
ATOM   2435  CB  ILE A 293       0.660 -23.136 -26.741  1.00 21.61           C  
ANISOU 2435  CB  ILE A 293     2884   3164   2163     35   -205    -55       C  
ATOM   2436  CG1 ILE A 293      -0.120 -21.855 -26.388  1.00 22.51           C  
ANISOU 2436  CG1 ILE A 293     2940   3310   2305     85   -209    -54       C  
ATOM   2437  CG2 ILE A 293       1.561 -22.901 -27.955  1.00 23.27           C  
ANISOU 2437  CG2 ILE A 293     3141   3339   2362     55   -218    -39       C  
ATOM   2438  CD1 ILE A 293      -0.993 -21.283 -27.503  1.00 22.84           C  
ANISOU 2438  CD1 ILE A 293     2944   3391   2345    109   -248    -43       C  
ATOM   2439  N   SER A 294       0.874 -26.333 -26.251  1.00 25.26           N  
ANISOU 2439  N   SER A 294     3431   3599   2568    -98   -189    -79       N  
ATOM   2440  CA  SER A 294       1.527 -27.636 -26.403  1.00 28.08           C  
ANISOU 2440  CA  SER A 294     3859   3913   2898   -135   -185    -84       C  
ATOM   2441  C   SER A 294       0.673 -28.628 -27.167  1.00 27.44           C  
ANISOU 2441  C   SER A 294     3791   3855   2780   -196   -208    -90       C  
ATOM   2442  O   SER A 294       1.161 -29.307 -28.068  1.00 27.59           O  
ANISOU 2442  O   SER A 294     3868   3841   2773   -207   -216    -92       O  
ATOM   2443  CB  SER A 294       1.888 -28.243 -25.040  1.00 28.47           C  
ANISOU 2443  CB  SER A 294     3933   3935   2950   -157   -162    -91       C  
ATOM   2444  OG  SER A 294       3.021 -27.607 -24.500  1.00 31.70           O  
ANISOU 2444  OG  SER A 294     4354   4307   3385   -108   -146    -83       O  
ATOM   2445  N   GLU A 295      -0.598 -28.723 -26.790  1.00 29.26           N  
ANISOU 2445  N   GLU A 295     3967   4143   3006   -238   -216    -96       N  
ATOM   2446  CA  GLU A 295      -1.537 -29.616 -27.469  1.00 31.70           C  
ANISOU 2446  CA  GLU A 295     4280   4484   3279   -307   -243   -102       C  
ATOM   2447  C   GLU A 295      -1.719 -29.208 -28.936  1.00 28.93           C  
ANISOU 2447  C   GLU A 295     3925   4151   2917   -289   -277    -93       C  
ATOM   2448  O   GLU A 295      -1.779 -30.062 -29.827  1.00 26.97           O  
ANISOU 2448  O   GLU A 295     3729   3889   2630   -332   -298    -96       O  
ATOM   2449  CB  GLU A 295      -2.877 -29.664 -26.714  1.00 34.95           C  
ANISOU 2449  CB  GLU A 295     4618   4968   3694   -354   -242   -109       C  
ATOM   2450  CG  GLU A 295      -4.117 -30.025 -27.559  1.00 47.48           C  
ANISOU 2450  CG  GLU A 295     6164   6619   5257   -412   -280   -109       C  
ATOM   2451  CD  GLU A 295      -4.301 -31.519 -27.781  1.00 56.73           C  
ANISOU 2451  CD  GLU A 295     7404   7771   6380   -505   -291   -117       C  
ATOM   2452  OE1 GLU A 295      -3.338 -32.197 -28.215  1.00 60.55           O  
ANISOU 2452  OE1 GLU A 295     7984   8181   6841   -505   -290   -120       O  
ATOM   2453  OE2 GLU A 295      -5.425 -32.017 -27.536  1.00 60.63           O  
ANISOU 2453  OE2 GLU A 295     7855   8323   6858   -580   -301   -122       O  
ATOM   2454  N   PHE A 296      -1.790 -27.904 -29.182  1.00 26.44           N  
ANISOU 2454  N   PHE A 296     3557   3859   2631   -225   -285    -81       N  
ATOM   2455  CA  PHE A 296      -1.982 -27.402 -30.539  1.00 27.05           C  
ANISOU 2455  CA  PHE A 296     3632   3952   2696   -206   -321    -68       C  
ATOM   2456  C   PHE A 296      -0.753 -27.684 -31.409  1.00 25.47           C  
ANISOU 2456  C   PHE A 296     3518   3687   2473   -190   -314    -65       C  
ATOM   2457  O   PHE A 296      -0.878 -28.188 -32.513  1.00 23.60           O  
ANISOU 2457  O   PHE A 296     3321   3448   2197   -220   -338    -65       O  
ATOM   2458  CB  PHE A 296      -2.299 -25.903 -30.517  1.00 27.53           C  
ANISOU 2458  CB  PHE A 296     3624   4043   2793   -137   -331    -54       C  
ATOM   2459  CG  PHE A 296      -2.525 -25.305 -31.883  1.00 30.98           C  
ANISOU 2459  CG  PHE A 296     4062   4494   3216   -114   -374    -37       C  
ATOM   2460  CD1 PHE A 296      -3.805 -25.280 -32.447  1.00 33.25           C  
ANISOU 2460  CD1 PHE A 296     4293   4849   3493   -138   -420    -32       C  
ATOM   2461  CD2 PHE A 296      -1.467 -24.757 -32.601  1.00 31.26           C  
ANISOU 2461  CD2 PHE A 296     4153   4480   3246    -72   -369    -24       C  
ATOM   2462  CE1 PHE A 296      -4.020 -24.718 -33.710  1.00 35.39           C  
ANISOU 2462  CE1 PHE A 296     4569   5131   3747   -117   -467    -12       C  
ATOM   2463  CE2 PHE A 296      -1.674 -24.190 -33.867  1.00 34.32           C  
ANISOU 2463  CE2 PHE A 296     4550   4878   3613    -55   -409     -5       C  
ATOM   2464  CZ  PHE A 296      -2.948 -24.173 -34.421  1.00 33.80           C  
ANISOU 2464  CZ  PHE A 296     4434   4874   3535    -76   -461      1       C  
ATOM   2465  N   GLU A 297       0.430 -27.370 -30.891  1.00 25.61           N  
ANISOU 2465  N   GLU A 297     3562   3655   2512   -146   -279    -64       N  
ATOM   2466  CA  GLU A 297       1.665 -27.457 -31.672  1.00 24.68           C  
ANISOU 2466  CA  GLU A 297     3512   3485   2381   -120   -264    -60       C  
ATOM   2467  C   GLU A 297       2.229 -28.870 -31.820  1.00 26.84           C  
ANISOU 2467  C   GLU A 297     3862   3714   2622   -157   -249    -77       C  
ATOM   2468  O   GLU A 297       2.790 -29.199 -32.863  1.00 27.47           O  
ANISOU 2468  O   GLU A 297     3999   3767   2673   -155   -247    -79       O  
ATOM   2469  CB  GLU A 297       2.736 -26.553 -31.070  1.00 21.74           C  
ANISOU 2469  CB  GLU A 297     3132   3083   2046    -62   -235    -51       C  
ATOM   2470  CG  GLU A 297       2.422 -25.063 -31.149  1.00 25.70           C  
ANISOU 2470  CG  GLU A 297     3581   3609   2573    -16   -248    -34       C  
ATOM   2471  CD  GLU A 297       2.461 -24.515 -32.568  1.00 25.39           C  
ANISOU 2471  CD  GLU A 297     3562   3574   2512     -2   -272    -18       C  
ATOM   2472  OE1 GLU A 297       3.312 -24.955 -33.373  1.00 27.18           O  
ANISOU 2472  OE1 GLU A 297     3847   3769   2711     -7   -259    -19       O  
ATOM   2473  OE2 GLU A 297       1.643 -23.629 -32.874  1.00 26.93           O  
ANISOU 2473  OE2 GLU A 297     3716   3803   2714     18   -303     -6       O  
ATOM   2474  N   LEU A 298       2.086 -29.688 -30.778  1.00 26.08           N  
ANISOU 2474  N   LEU A 298     3774   3607   2530   -190   -237    -88       N  
ATOM   2475  CA  LEU A 298       2.820 -30.945 -30.670  1.00 28.17           C  
ANISOU 2475  CA  LEU A 298     4116   3814   2772   -209   -220   -102       C  
ATOM   2476  C   LEU A 298       1.919 -32.170 -30.591  1.00 30.56           C  
ANISOU 2476  C   LEU A 298     4452   4121   3037   -287   -237   -115       C  
ATOM   2477  O   LEU A 298       2.416 -33.296 -30.703  1.00 30.69           O  
ANISOU 2477  O   LEU A 298     4550   4085   3027   -306   -229   -128       O  
ATOM   2478  CB  LEU A 298       3.729 -30.930 -29.426  1.00 27.01           C  
ANISOU 2478  CB  LEU A 298     3971   3632   2659   -176   -190   -100       C  
ATOM   2479  CG  LEU A 298       4.686 -29.754 -29.197  1.00 24.43           C  
ANISOU 2479  CG  LEU A 298     3611   3299   2372   -108   -172    -87       C  
ATOM   2480  CD1 LEU A 298       5.180 -29.740 -27.755  1.00 17.09           C  
ANISOU 2480  CD1 LEU A 298     2671   2350   1472    -96   -155    -85       C  
ATOM   2481  CD2 LEU A 298       5.854 -29.788 -30.192  1.00 23.43           C  
ANISOU 2481  CD2 LEU A 298     3527   3137   2237    -70   -155    -85       C  
ATOM   2482  N   ASN A 299       0.613 -31.941 -30.397  1.00 31.80           N  
ANISOU 2482  N   ASN A 299     4547   4341   3193   -330   -262   -113       N  
ATOM   2483  CA AASN A 299      -0.379 -33.008 -30.207  0.50 35.05           C  
ANISOU 2483  CA AASN A 299     4975   4770   3571   -418   -280   -123       C  
ATOM   2484  CA BASN A 299      -0.367 -33.017 -30.210  0.50 34.61           C  
ANISOU 2484  CA BASN A 299     4922   4714   3516   -418   -279   -124       C  
ATOM   2485  C   ASN A 299      -0.111 -33.843 -28.947  1.00 36.85           C  
ANISOU 2485  C   ASN A 299     5241   4961   3801   -445   -256   -131       C  
ATOM   2486  O   ASN A 299      -0.366 -35.051 -28.916  1.00 39.83           O  
ANISOU 2486  O   ASN A 299     5683   5310   4140   -512   -264   -141       O  
ATOM   2487  CB AASN A 299      -0.504 -33.896 -31.462  0.50 35.23           C  
ANISOU 2487  CB AASN A 299     5073   4772   3540   -463   -304   -133       C  
ATOM   2488  CB BASN A 299      -0.448 -33.921 -31.452  0.50 34.22           C  
ANISOU 2488  CB BASN A 299     4950   4641   3413   -461   -303   -133       C  
ATOM   2489  CG AASN A 299      -1.780 -34.723 -31.474  0.50 36.97           C  
ANISOU 2489  CG AASN A 299     5291   5030   3724   -563   -335   -140       C  
ATOM   2490  CG BASN A 299      -1.173 -33.262 -32.604  0.50 34.15           C  
ANISOU 2490  CG BASN A 299     4899   4687   3391   -466   -340   -125       C  
ATOM   2491  OD1AASN A 299      -2.718 -34.450 -30.722  0.50 37.35           O  
ANISOU 2491  OD1AASN A 299     5260   5139   3791   -595   -340   -135       O  
ATOM   2492  OD1BASN A 299      -2.392 -33.093 -32.566  0.50 33.88           O  
ANISOU 2492  OD1BASN A 299     4797   4720   3355   -511   -370   -120       O  
ATOM   2493  ND2AASN A 299      -1.820 -35.743 -32.328  0.50 36.85           N  
ANISOU 2493  ND2AASN A 299     5364   4980   3656   -616   -353   -152       N  
ATOM   2494  ND2BASN A 299      -0.429 -32.891 -33.643  0.50 33.30           N  
ANISOU 2494  ND2BASN A 299     4829   4551   3271   -419   -338   -122       N  
ATOM   2495  N   VAL A 300       0.396 -33.190 -27.900  1.00 37.70           N  
ANISOU 2495  N   VAL A 300     5313   5063   3948   -398   -231   -124       N  
ATOM   2496  CA  VAL A 300       0.626 -33.865 -26.617  1.00 41.65           C  
ANISOU 2496  CA  VAL A 300     5845   5530   4449   -422   -212   -127       C  
ATOM   2497  C   VAL A 300      -0.548 -33.641 -25.658  1.00 44.24           C  
ANISOU 2497  C   VAL A 300     6104   5922   4783   -472   -209   -127       C  
ATOM   2498  O   VAL A 300      -1.140 -32.557 -25.631  1.00 44.50           O  
ANISOU 2498  O   VAL A 300     6048   6018   4843   -446   -209   -123       O  
ATOM   2499  CB  VAL A 300       1.960 -33.435 -25.930  1.00 40.58           C  
ANISOU 2499  CB  VAL A 300     5724   5346   4348   -349   -187   -120       C  
ATOM   2500  CG1 VAL A 300       3.159 -34.031 -26.651  1.00 40.08           C  
ANISOU 2500  CG1 VAL A 300     5740   5215   4274   -312   -183   -123       C  
ATOM   2501  CG2 VAL A 300       2.075 -31.910 -25.827  1.00 40.83           C  
ANISOU 2501  CG2 VAL A 300     5676   5417   4422   -287   -179   -110       C  
ATOM   2502  N   GLY A 301      -0.880 -34.667 -24.879  1.00 46.61           N  
ANISOU 2502  N   GLY A 301     6447   6207   5056   -542   -204   -132       N  
ATOM   2503  CA  GLY A 301      -1.981 -34.579 -23.922  1.00 50.87           C  
ANISOU 2503  CA  GLY A 301     6926   6809   5595   -599   -193   -134       C  
ATOM   2504  C   GLY A 301      -1.671 -33.601 -22.805  1.00 53.11           C  
ANISOU 2504  C   GLY A 301     7159   7104   5916   -545   -164   -130       C  
ATOM   2505  O   GLY A 301      -0.510 -33.434 -22.429  1.00 51.54           O  
ANISOU 2505  O   GLY A 301     7002   6847   5734   -489   -154   -125       O  
ATOM   2506  N   LYS A 302      -2.707 -32.947 -22.280  1.00 57.19           N  
ANISOU 2506  N   LYS A 302     7585   7698   6445   -561   -151   -134       N  
ATOM   2507  CA  LYS A 302      -2.554 -32.014 -21.151  1.00 60.54           C  
ANISOU 2507  CA  LYS A 302     7966   8137   6899   -517   -119   -135       C  
ATOM   2508  C   LYS A 302      -1.899 -32.680 -19.927  1.00 61.54           C  
ANISOU 2508  C   LYS A 302     8168   8207   7009   -542   -100   -133       C  
ATOM   2509  O   LYS A 302      -1.977 -33.903 -19.750  1.00 61.47           O  
ANISOU 2509  O   LYS A 302     8228   8167   6962   -613   -106   -133       O  
ATOM   2510  CB  LYS A 302      -3.904 -31.375 -20.779  1.00 62.00           C  
ANISOU 2510  CB  LYS A 302     8046   8418   7095   -536   -103   -143       C  
ATOM   2511  CG  LYS A 302      -4.915 -32.325 -20.111  1.00 67.15           C  
ANISOU 2511  CG  LYS A 302     8692   9112   7711   -642    -89   -150       C  
ATOM   2512  CD  LYS A 302      -6.363 -31.847 -20.265  1.00 72.37           C  
ANISOU 2512  CD  LYS A 302     9233   9881   8381   -666    -85   -158       C  
ATOM   2513  CE  LYS A 302      -6.938 -32.224 -21.633  1.00 74.85           C  
ANISOU 2513  CE  LYS A 302     9527  10227   8684   -698   -130   -154       C  
ATOM   2514  NZ  LYS A 302      -8.366 -31.828 -21.788  1.00 75.80           N  
ANISOU 2514  NZ  LYS A 302     9525  10461   8816   -724   -132   -159       N  
ATOM   2515  N   LEU A 303      -1.242 -31.874 -19.098  1.00 62.29           N  
ANISOU 2515  N   LEU A 303     8255   8283   7129   -486    -81   -131       N  
ATOM   2516  CA  LEU A 303      -0.643 -32.381 -17.866  1.00 64.68           C  
ANISOU 2516  CA  LEU A 303     8624   8536   7414   -507    -67   -127       C  
ATOM   2517  C   LEU A 303      -1.721 -32.637 -16.813  1.00 65.78           C  
ANISOU 2517  C   LEU A 303     8740   8727   7528   -582    -38   -136       C  
ATOM   2518  O   LEU A 303      -2.348 -31.703 -16.306  1.00 66.26           O  
ANISOU 2518  O   LEU A 303     8726   8846   7605   -565    -11   -146       O  
ATOM   2519  CB  LEU A 303       0.458 -31.440 -17.363  1.00 64.66           C  
ANISOU 2519  CB  LEU A 303     8625   8498   7444   -428    -61   -121       C  
ATOM   2520  CG  LEU A 303       1.923 -31.800 -17.675  1.00 64.60           C  
ANISOU 2520  CG  LEU A 303     8688   8411   7445   -383    -83   -107       C  
ATOM   2521  CD1 LEU A 303       2.076 -32.743 -18.868  1.00 63.58           C  
ANISOU 2521  CD1 LEU A 303     8602   8254   7301   -396   -106   -106       C  
ATOM   2522  CD2 LEU A 303       2.753 -30.534 -17.891  1.00 63.24           C  
ANISOU 2522  CD2 LEU A 303     8481   8233   7315   -300    -84   -102       C  
ATOM   2523  N   LYS A 304      -1.925 -33.917 -16.507  1.00 66.55           N  
ANISOU 2523  N   LYS A 304     8906   8799   7582   -666    -43   -133       N  
ATOM   2524  CA  LYS A 304      -3.073 -34.382 -15.733  1.00 67.96           C  
ANISOU 2524  CA  LYS A 304     9065   9032   7726   -759    -17   -140       C  
ATOM   2525  C   LYS A 304      -2.731 -34.559 -14.254  1.00 67.06           C  
ANISOU 2525  C   LYS A 304     9006   8887   7588   -784      7   -136       C  
ATOM   2526  O   LYS A 304      -1.826 -35.322 -13.911  1.00 66.41           O  
ANISOU 2526  O   LYS A 304     9025   8722   7486   -791    -12   -123       O  
ATOM   2527  CB  LYS A 304      -3.582 -35.705 -16.328  1.00 69.32           C  
ANISOU 2527  CB  LYS A 304     9287   9194   7857   -851    -39   -137       C  
ATOM   2528  CG  LYS A 304      -5.085 -35.960 -16.198  1.00 73.59           C  
ANISOU 2528  CG  LYS A 304     9761   9827   8374   -947    -20   -147       C  
ATOM   2529  CD  LYS A 304      -5.422 -36.922 -15.057  1.00 76.22           C  
ANISOU 2529  CD  LYS A 304    10159  10147   8654  -1052      1   -143       C  
ATOM   2530  CE  LYS A 304      -5.840 -36.185 -13.790  1.00 77.50           C  
ANISOU 2530  CE  LYS A 304    10264  10364   8818  -1052     53   -152       C  
ATOM   2531  NZ  LYS A 304      -5.930 -37.093 -12.610  1.00 77.59           N  
ANISOU 2531  NZ  LYS A 304    10360  10346   8773  -1147     73   -145       N  
ATOM   2532  N   TYR A 305      -3.460 -33.852 -13.389  1.00 66.91           N  
ANISOU 2532  N   TYR A 305     8921   8933   7570   -795     49   -148       N  
ATOM   2533  CA  TYR A 305      -3.328 -34.012 -11.935  1.00 66.51           C  
ANISOU 2533  CA  TYR A 305     8921   8863   7486   -833     78   -147       C  
ATOM   2534  C   TYR A 305      -4.644 -33.768 -11.189  1.00 65.93           C  
ANISOU 2534  C   TYR A 305     8775   8883   7392   -896    131   -165       C  
ATOM   2535  O   TYR A 305      -5.543 -33.103 -11.709  1.00 65.97           O  
ANISOU 2535  O   TYR A 305     8671   8970   7423   -877    148   -180       O  
ATOM   2536  CB  TYR A 305      -2.212 -33.117 -11.377  1.00 67.05           C  
ANISOU 2536  CB  TYR A 305     9011   8885   7581   -746     76   -144       C  
ATOM   2537  CG  TYR A 305      -2.408 -31.629 -11.598  1.00 68.15           C  
ANISOU 2537  CG  TYR A 305     9053   9074   7766   -664     96   -159       C  
ATOM   2538  CD1 TYR A 305      -3.105 -30.852 -10.672  1.00 68.53           C  
ANISOU 2538  CD1 TYR A 305     9051   9180   7810   -666    145   -178       C  
ATOM   2539  CD2 TYR A 305      -1.879 -30.996 -12.722  1.00 68.80           C  
ANISOU 2539  CD2 TYR A 305     9104   9144   7894   -582     67   -155       C  
ATOM   2540  CE1 TYR A 305      -3.284 -29.487 -10.863  1.00 69.84           C  
ANISOU 2540  CE1 TYR A 305     9138   9382   8016   -585    162   -193       C  
ATOM   2541  CE2 TYR A 305      -2.051 -29.625 -12.924  1.00 70.88           C  
ANISOU 2541  CE2 TYR A 305     9291   9445   8197   -507     81   -167       C  
ATOM   2542  CZ  TYR A 305      -2.755 -28.879 -11.988  1.00 70.87           C  
ANISOU 2542  CZ  TYR A 305     9242   9494   8191   -506    127   -186       C  
ATOM   2543  OH  TYR A 305      -2.929 -27.527 -12.175  1.00 71.93           O  
ANISOU 2543  OH  TYR A 305     9309   9656   8363   -427    140   -198       O  
ATOM   2544  N   ASP A 306      -4.738 -34.310  -9.973  1.00 65.42           N  
ANISOU 2544  N   ASP A 306     8773   8806   7279   -967    157   -162       N  
ATOM   2545  CA  ASP A 306      -5.929 -34.178  -9.119  1.00 65.20           C  
ANISOU 2545  CA  ASP A 306     8687   8865   7223  -1036    217   -180       C  
ATOM   2546  C   ASP A 306      -5.813 -33.023  -8.123  1.00 62.86           C  
ANISOU 2546  C   ASP A 306     8361   8587   6935   -979    261   -196       C  
ATOM   2547  O   ASP A 306      -4.761 -32.822  -7.508  1.00 61.60           O  
ANISOU 2547  O   ASP A 306     8279   8355   6772   -940    247   -187       O  
ATOM   2548  CB  ASP A 306      -6.187 -35.479  -8.345  1.00 67.00           C  
ANISOU 2548  CB  ASP A 306     9007   9069   7381  -1163    226   -167       C  
ATOM   2549  CG  ASP A 306      -6.637 -36.623  -9.243  1.00 71.03           C  
ANISOU 2549  CG  ASP A 306     9538   9578   7872  -1242    193   -157       C  
ATOM   2550  OD1 ASP A 306      -5.870 -37.601  -9.382  1.00 70.81           O  
ANISOU 2550  OD1 ASP A 306     9628   9455   7819  -1265    150   -137       O  
ATOM   2551  OD2 ASP A 306      -7.753 -36.547  -9.805  1.00 72.91           O  
ANISOU 2551  OD2 ASP A 306     9676   9908   8118  -1280    210   -169       O  
ATOM   2552  N   GLY A 307      -6.904 -32.278  -7.962  1.00 61.11           N  
ANISOU 2552  N   GLY A 307     8029   8465   6727   -974    314   -221       N  
ATOM   2553  CA  GLY A 307      -6.970 -31.181  -6.993  1.00 59.15           C  
ANISOU 2553  CA  GLY A 307     7752   8242   6482   -924    365   -243       C  
ATOM   2554  C   GLY A 307      -6.334 -29.890  -7.480  1.00 56.49           C  
ANISOU 2554  C   GLY A 307     7379   7881   6204   -795    347   -250       C  
ATOM   2555  O   GLY A 307      -5.718 -29.863  -8.551  1.00 55.73           O  
ANISOU 2555  O   GLY A 307     7287   7745   6144   -743    293   -234       O  
ATOM   2556  N   PRO A 308      -6.478 -28.803  -6.698  1.00 55.18           N  
ANISOU 2556  N   PRO A 308     7185   7739   6043   -743    393   -273       N  
ATOM   2557  CA  PRO A 308      -5.888 -27.515  -7.075  1.00 53.87           C  
ANISOU 2557  CA  PRO A 308     6995   7546   5928   -625    378   -280       C  
ATOM   2558  C   PRO A 308      -4.363 -27.559  -7.051  1.00 52.51           C  
ANISOU 2558  C   PRO A 308     6926   7266   5758   -594    324   -256       C  
ATOM   2559  O   PRO A 308      -3.779 -28.282  -6.238  1.00 51.70           O  
ANISOU 2559  O   PRO A 308     6918   7113   5613   -650    316   -243       O  
ATOM   2560  CB  PRO A 308      -6.403 -26.560  -5.994  1.00 54.92           C  
ANISOU 2560  CB  PRO A 308     7101   7719   6048   -600    446   -313       C  
ATOM   2561  CG  PRO A 308      -6.701 -27.433  -4.820  1.00 55.48           C  
ANISOU 2561  CG  PRO A 308     7228   7799   6051   -706    487   -315       C  
ATOM   2562  CD  PRO A 308      -7.191 -28.726  -5.409  1.00 56.28           C  
ANISOU 2562  CD  PRO A 308     7320   7928   6137   -796    466   -296       C  
ATOM   2563  N   ILE A 309      -3.733 -26.791  -7.939  1.00 51.49           N  
ANISOU 2563  N   ILE A 309     6777   7107   5680   -506    287   -250       N  
ATOM   2564  CA  ILE A 309      -2.273 -26.678  -7.993  1.00 50.10           C  
ANISOU 2564  CA  ILE A 309     6680   6840   5514   -468    238   -228       C  
ATOM   2565  C   ILE A 309      -1.700 -26.249  -6.631  1.00 49.04           C  
ANISOU 2565  C   ILE A 309     6615   6667   5349   -471    257   -235       C  
ATOM   2566  O   ILE A 309      -0.565 -26.585  -6.291  1.00 47.19           O  
ANISOU 2566  O   ILE A 309     6463   6362   5103   -477    219   -213       O  
ATOM   2567  CB  ILE A 309      -1.813 -25.709  -9.126  1.00 50.80           C  
ANISOU 2567  CB  ILE A 309     6727   6916   5661   -374    206   -224       C  
ATOM   2568  CG1 ILE A 309      -0.281 -25.705  -9.256  1.00 50.85           C  
ANISOU 2568  CG1 ILE A 309     6806   6836   5678   -344    157   -199       C  
ATOM   2569  CG2 ILE A 309      -2.391 -24.294  -8.915  1.00 51.25           C  
ANISOU 2569  CG2 ILE A 309     6722   7011   5740   -307    244   -251       C  
ATOM   2570  CD1 ILE A 309       0.255 -25.044 -10.519  1.00 55.07           C  
ANISOU 2570  CD1 ILE A 309     7309   7355   6262   -271    122   -189       C  
ATOM   2571  N   SER A 310      -2.513 -25.533  -5.855  1.00 48.94           N  
ANISOU 2571  N   SER A 310     6568   6703   5322   -466    316   -265       N  
ATOM   2572  CA  SER A 310      -2.138 -25.083  -4.519  1.00 47.81           C  
ANISOU 2572  CA  SER A 310     6492   6531   5142   -475    342   -277       C  
ATOM   2573  C   SER A 310      -1.944 -26.236  -3.536  1.00 46.47           C  
ANISOU 2573  C   SER A 310     6410   6336   4909   -571    343   -262       C  
ATOM   2574  O   SER A 310      -1.395 -26.040  -2.450  1.00 45.54           O  
ANISOU 2574  O   SER A 310     6368   6179   4754   -587    347   -263       O  
ATOM   2575  CB  SER A 310      -3.179 -24.100  -3.978  1.00 50.40           C  
ANISOU 2575  CB  SER A 310     6760   6923   5466   -446    414   -317       C  
ATOM   2576  OG  SER A 310      -4.413 -24.747  -3.712  1.00 55.64           O  
ANISOU 2576  OG  SER A 310     7374   7666   6102   -512    466   -332       O  
ATOM   2577  N   LYS A 311      -2.389 -27.432  -3.916  1.00 44.35           N  
ANISOU 2577  N   LYS A 311     6137   6088   4625   -638    335   -248       N  
ATOM   2578  CA  LYS A 311      -2.211 -28.616  -3.070  1.00 43.44           C  
ANISOU 2578  CA  LYS A 311     6115   5942   4449   -733    329   -230       C  
ATOM   2579  C   LYS A 311      -1.382 -29.733  -3.717  1.00 42.18           C  
ANISOU 2579  C   LYS A 311     6015   5718   4295   -752    260   -194       C  
ATOM   2580  O   LYS A 311      -1.136 -30.763  -3.082  1.00 42.85           O  
ANISOU 2580  O   LYS A 311     6188   5763   4330   -823    244   -174       O  
ATOM   2581  CB  LYS A 311      -3.566 -29.155  -2.603  1.00 45.10           C  
ANISOU 2581  CB  LYS A 311     6290   6229   4615   -819    393   -248       C  
ATOM   2582  CG  LYS A 311      -4.304 -28.225  -1.649  1.00 48.85           C  
ANISOU 2582  CG  LYS A 311     6731   6761   5068   -812    470   -285       C  
ATOM   2583  CD  LYS A 311      -5.665 -28.785  -1.286  1.00 55.88           C  
ANISOU 2583  CD  LYS A 311     7571   7740   5919   -899    537   -302       C  
ATOM   2584  CE  LYS A 311      -6.443 -27.843  -0.373  1.00 58.49           C  
ANISOU 2584  CE  LYS A 311     7859   8135   6231   -883    622   -344       C  
ATOM   2585  NZ  LYS A 311      -7.802 -28.389  -0.066  1.00 61.41           N  
ANISOU 2585  NZ  LYS A 311     8164   8604   6565   -970    693   -361       N  
ATOM   2586  N   LEU A 312      -0.932 -29.524  -4.956  1.00 38.05           N  
ANISOU 2586  N   LEU A 312     5450   5180   3829   -685    219   -184       N  
ATOM   2587  CA  LEU A 312      -0.214 -30.564  -5.698  1.00 37.10           C  
ANISOU 2587  CA  LEU A 312     5378   5002   3715   -694    160   -155       C  
ATOM   2588  C   LEU A 312       1.121 -30.976  -5.084  1.00 36.03           C  
ANISOU 2588  C   LEU A 312     5346   4779   3563   -689    112   -129       C  
ATOM   2589  O   LEU A 312       1.424 -32.168  -5.015  1.00 35.16           O  
ANISOU 2589  O   LEU A 312     5309   4624   3425   -737     81   -107       O  
ATOM   2590  CB  LEU A 312      -0.014 -30.173  -7.170  1.00 37.32           C  
ANISOU 2590  CB  LEU A 312     5339   5036   3804   -622    133   -154       C  
ATOM   2591  CG  LEU A 312       0.458 -31.290  -8.113  1.00 39.38           C  
ANISOU 2591  CG  LEU A 312     5639   5254   4072   -634     85   -132       C  
ATOM   2592  CD1 LEU A 312      -0.386 -32.563  -7.974  1.00 39.99           C  
ANISOU 2592  CD1 LEU A 312     5748   5346   4101   -734     96   -129       C  
ATOM   2593  CD2 LEU A 312       0.457 -30.817  -9.563  1.00 39.38           C  
ANISOU 2593  CD2 LEU A 312     5567   5274   4124   -571     69   -135       C  
ATOM   2594  N   ARG A 313       1.923 -29.998  -4.661  1.00 33.69           N  
ANISOU 2594  N   ARG A 313     5057   4459   3285   -632    101   -129       N  
ATOM   2595  CA  ARG A 313       3.189 -30.289  -3.994  1.00 34.15           C  
ANISOU 2595  CA  ARG A 313     5204   4443   3329   -627     52   -103       C  
ATOM   2596  C   ARG A 313       2.962 -31.180  -2.771  1.00 35.49           C  
ANISOU 2596  C   ARG A 313     5464   4593   3428   -715     59    -94       C  
ATOM   2597  O   ARG A 313       3.623 -32.208  -2.609  1.00 35.13           O  
ANISOU 2597  O   ARG A 313     5499   4488   3363   -738     12    -65       O  
ATOM   2598  CB  ARG A 313       3.903 -28.999  -3.589  1.00 33.38           C  
ANISOU 2598  CB  ARG A 313     5097   4334   3253   -568     46   -110       C  
ATOM   2599  CG  ARG A 313       5.266 -29.206  -2.950  1.00 33.17           C  
ANISOU 2599  CG  ARG A 313     5149   4237   3216   -560    -13    -81       C  
ATOM   2600  CD  ARG A 313       5.929 -27.868  -2.621  1.00 32.54           C  
ANISOU 2600  CD  ARG A 313     5056   4150   3157   -510    -20    -88       C  
ATOM   2601  NE  ARG A 313       7.148 -28.052  -1.832  1.00 31.73           N  
ANISOU 2601  NE  ARG A 313     5028   3990   3039   -515    -77    -61       N  
ATOM   2602  CZ  ARG A 313       7.179 -28.204  -0.510  1.00 32.08           C  
ANISOU 2602  CZ  ARG A 313     5150   4016   3023   -568    -78    -58       C  
ATOM   2603  NH1 ARG A 313       6.056 -28.191   0.201  1.00 30.13           N  
ANISOU 2603  NH1 ARG A 313     4917   3804   2725   -623    -18    -82       N  
ATOM   2604  NH2 ARG A 313       8.343 -28.377   0.104  1.00 33.93           N  
ANISOU 2604  NH2 ARG A 313     5446   4199   3247   -567   -141    -29       N  
ATOM   2605  N   GLU A 314       2.010 -30.778  -1.932  1.00 36.92           N  
ANISOU 2605  N   GLU A 314     5634   4824   3569   -760    119   -118       N  
ATOM   2606  CA  GLU A 314       1.688 -31.473  -0.686  1.00 38.92           C  
ANISOU 2606  CA  GLU A 314     5973   5068   3746   -851    137   -113       C  
ATOM   2607  C   GLU A 314       1.140 -32.886  -0.934  1.00 36.84           C  
ANISOU 2607  C   GLU A 314     5746   4801   3451   -929    133    -98       C  
ATOM   2608  O   GLU A 314       1.545 -33.832  -0.266  1.00 36.98           O  
ANISOU 2608  O   GLU A 314     5868   4762   3420   -984    102    -71       O  
ATOM   2609  CB  GLU A 314       0.698 -30.626   0.126  1.00 41.17           C  
ANISOU 2609  CB  GLU A 314     6223   5420   4001   -875    215   -149       C  
ATOM   2610  CG  GLU A 314       0.316 -31.157   1.506  1.00 49.97           C  
ANISOU 2610  CG  GLU A 314     7424   6532   5029   -971    247   -148       C  
ATOM   2611  CD  GLU A 314      -0.559 -30.170   2.285  1.00 58.06           C  
ANISOU 2611  CD  GLU A 314     8410   7623   6027   -979    330   -189       C  
ATOM   2612  OE1 GLU A 314      -0.483 -30.156   3.536  1.00 62.21           O  
ANISOU 2612  OE1 GLU A 314     9018   8133   6487  -1030    349   -192       O  
ATOM   2613  OE2 GLU A 314      -1.316 -29.399   1.648  1.00 60.69           O  
ANISOU 2613  OE2 GLU A 314     8633   8022   6404   -932    376   -220       O  
ATOM   2614  N   SER A 315       0.236 -33.022  -1.900  1.00 34.93           N  
ANISOU 2614  N   SER A 315     5422   4615   3235   -936    160   -112       N  
ATOM   2615  CA  SER A 315      -0.413 -34.306  -2.165  1.00 36.00           C  
ANISOU 2615  CA  SER A 315     5588   4753   3337  -1022    161   -101       C  
ATOM   2616  C   SER A 315       0.411 -35.245  -3.042  1.00 35.77           C  
ANISOU 2616  C   SER A 315     5610   4650   3329   -999     92    -73       C  
ATOM   2617  O   SER A 315       0.387 -36.461  -2.839  1.00 37.23           O  
ANISOU 2617  O   SER A 315     5884   4793   3471  -1069     71    -53       O  
ATOM   2618  CB  SER A 315      -1.809 -34.111  -2.762  1.00 35.18           C  
ANISOU 2618  CB  SER A 315     5376   4748   3245  -1052    218   -129       C  
ATOM   2619  OG  SER A 315      -1.763 -33.391  -3.977  1.00 37.09           O  
ANISOU 2619  OG  SER A 315     5520   5014   3556   -965    206   -140       O  
ATOM   2620  N   ASN A 316       1.138 -34.680  -4.007  1.00 34.05           N  
ANISOU 2620  N   ASN A 316     5343   4418   3178   -902     60    -73       N  
ATOM   2621  CA  ASN A 316       1.927 -35.470  -4.949  1.00 31.58           C  
ANISOU 2621  CA  ASN A 316     5067   4043   2891   -868      3    -52       C  
ATOM   2622  C   ASN A 316       3.153 -34.712  -5.450  1.00 29.87           C  
ANISOU 2622  C   ASN A 316     4823   3792   2733   -759    -35    -45       C  
ATOM   2623  O   ASN A 316       3.190 -34.256  -6.600  1.00 28.82           O  
ANISOU 2623  O   ASN A 316     4617   3682   2650   -701    -37    -54       O  
ATOM   2624  CB  ASN A 316       1.056 -35.921  -6.129  1.00 31.14           C  
ANISOU 2624  CB  ASN A 316     4958   4026   2848   -892     15    -63       C  
ATOM   2625  CG  ASN A 316       1.653 -37.106  -6.888  1.00 32.83           C  
ANISOU 2625  CG  ASN A 316     5245   4167   3062   -891    -36    -43       C  
ATOM   2626  OD1 ASN A 316       2.847 -37.404  -6.788  1.00 34.69           O  
ANISOU 2626  OD1 ASN A 316     5546   4327   3308   -840    -83    -22       O  
ATOM   2627  ND2 ASN A 316       0.816 -37.787  -7.648  1.00 30.49           N  
ANISOU 2627  ND2 ASN A 316     4939   3894   2754   -945    -28    -50       N  
ATOM   2628  N   HIS A 317       4.157 -34.603  -4.582  1.00 28.80           N  
ANISOU 2628  N   HIS A 317     4750   3606   2588   -737    -68    -27       N  
ATOM   2629  CA  HIS A 317       5.399 -33.895  -4.879  1.00 27.79           C  
ANISOU 2629  CA  HIS A 317     4600   3448   2511   -646   -106    -17       C  
ATOM   2630  C   HIS A 317       6.144 -34.506  -6.057  1.00 26.74           C  
ANISOU 2630  C   HIS A 317     4467   3274   2418   -592   -147     -3       C  
ATOM   2631  O   HIS A 317       6.776 -33.791  -6.830  1.00 27.51           O  
ANISOU 2631  O   HIS A 317     4505   3378   2569   -517   -157     -6       O  
ATOM   2632  CB  HIS A 317       6.307 -33.865  -3.640  1.00 29.24           C  
ANISOU 2632  CB  HIS A 317     4859   3584   2668   -648   -141      4       C  
ATOM   2633  CG  HIS A 317       7.653 -33.255  -3.886  1.00 26.89           C  
ANISOU 2633  CG  HIS A 317     4541   3257   2420   -565   -187     18       C  
ATOM   2634  ND1 HIS A 317       8.805 -34.007  -3.960  1.00 26.16           N  
ANISOU 2634  ND1 HIS A 317     4500   3099   2339   -530   -249     48       N  
ATOM   2635  CD2 HIS A 317       8.031 -31.969  -4.085  1.00 26.07           C  
ANISOU 2635  CD2 HIS A 317     4369   3179   2356   -510   -180      7       C  
ATOM   2636  CE1 HIS A 317       9.835 -33.210  -4.182  1.00 23.29           C  
ANISOU 2636  CE1 HIS A 317     4094   2733   2023   -462   -276     55       C  
ATOM   2637  NE2 HIS A 317       9.392 -31.969  -4.265  1.00 22.46           N  
ANISOU 2637  NE2 HIS A 317     3920   2679   1933   -452   -236     31       N  
ATOM   2638  N   GLN A 318       6.059 -35.827  -6.190  1.00 26.92           N  
ANISOU 2638  N   GLN A 318     4563   3253   2412   -632   -167     10       N  
ATOM   2639  CA  GLN A 318       6.682 -36.534  -7.300  1.00 28.20           C  
ANISOU 2639  CA  GLN A 318     4738   3372   2604   -584   -200     19       C  
ATOM   2640  C   GLN A 318       6.203 -35.990  -8.653  1.00 27.37           C  
ANISOU 2640  C   GLN A 318     4539   3319   2539   -551   -173     -4       C  
ATOM   2641  O   GLN A 318       7.013 -35.715  -9.533  1.00 30.04           O  
ANISOU 2641  O   GLN A 318     4845   3645   2925   -476   -191     -2       O  
ATOM   2642  CB  GLN A 318       6.431 -38.045  -7.190  1.00 28.17           C  
ANISOU 2642  CB  GLN A 318     4838   3313   2553   -644   -219     32       C  
ATOM   2643  CG  GLN A 318       6.879 -38.858  -8.418  1.00 28.17           C  
ANISOU 2643  CG  GLN A 318     4859   3267   2576   -601   -244     34       C  
ATOM   2644  CD  GLN A 318       8.388 -38.955  -8.571  1.00 27.29           C  
ANISOU 2644  CD  GLN A 318     4768   3097   2503   -506   -292     53       C  
ATOM   2645  OE1 GLN A 318       9.120 -39.053  -7.586  1.00 26.69           O  
ANISOU 2645  OE1 GLN A 318     4742   2982   2417   -494   -326     75       O  
ATOM   2646  NE2 GLN A 318       8.860 -38.943  -9.815  1.00 26.97           N  
ANISOU 2646  NE2 GLN A 318     4689   3052   2505   -439   -295     44       N  
ATOM   2647  N   ARG A 319       4.893 -35.822  -8.799  1.00 28.24           N  
ANISOU 2647  N   ARG A 319     4606   3491   2631   -608   -130    -24       N  
ATOM   2648  CA  ARG A 319       4.303 -35.331 -10.044  1.00 29.02           C  
ANISOU 2648  CA  ARG A 319     4618   3644   2764   -585   -109    -43       C  
ATOM   2649  C   ARG A 319       4.516 -33.827 -10.217  1.00 27.32           C  
ANISOU 2649  C   ARG A 319     4315   3473   2595   -518    -93    -54       C  
ATOM   2650  O   ARG A 319       4.646 -33.336 -11.342  1.00 25.80           O  
ANISOU 2650  O   ARG A 319     4064   3297   2440   -465    -95    -60       O  
ATOM   2651  CB  ARG A 319       2.813 -35.685 -10.110  1.00 29.68           C  
ANISOU 2651  CB  ARG A 319     4679   3784   2813   -671    -74    -59       C  
ATOM   2652  CG  ARG A 319       2.177 -35.412 -11.460  1.00 34.42           C  
ANISOU 2652  CG  ARG A 319     5203   4435   3442   -655    -65    -75       C  
ATOM   2653  CD  ARG A 319       1.061 -36.386 -11.770  1.00 41.16           C  
ANISOU 2653  CD  ARG A 319     6073   5312   4256   -748    -56    -81       C  
ATOM   2654  NE  ARG A 319       1.559 -37.693 -12.195  1.00 44.24           N  
ANISOU 2654  NE  ARG A 319     6562   5625   4623   -768    -92    -68       N  
ATOM   2655  CZ  ARG A 319       0.789 -38.766 -12.356  1.00 49.52           C  
ANISOU 2655  CZ  ARG A 319     7279   6288   5247   -858    -93    -69       C  
ATOM   2656  NH1 ARG A 319      -0.517 -38.691 -12.129  1.00 51.63           N  
ANISOU 2656  NH1 ARG A 319     7493   6633   5491   -939    -61    -80       N  
ATOM   2657  NH2 ARG A 319       1.319 -39.919 -12.737  1.00 49.77           N  
ANISOU 2657  NH2 ARG A 319     7413   6240   5259   -867   -127    -59       N  
ATOM   2658  N   TYR A 320       4.560 -33.117  -9.093  1.00 26.38           N  
ANISOU 2658  N   TYR A 320     4193   3365   2465   -523    -79    -55       N  
ATOM   2659  CA  TYR A 320       4.800 -31.675  -9.057  1.00 26.61           C  
ANISOU 2659  CA  TYR A 320     4156   3424   2530   -465    -66    -65       C  
ATOM   2660  C   TYR A 320       6.109 -31.322  -9.738  1.00 25.27           C  
ANISOU 2660  C   TYR A 320     3978   3217   2406   -387   -102    -51       C  
ATOM   2661  O   TYR A 320       6.155 -30.424 -10.577  1.00 24.09           O  
ANISOU 2661  O   TYR A 320     3763   3095   2295   -337    -94    -59       O  
ATOM   2662  CB  TYR A 320       4.847 -31.226  -7.600  1.00 27.37           C  
ANISOU 2662  CB  TYR A 320     4285   3518   2596   -490    -53    -66       C  
ATOM   2663  CG  TYR A 320       4.835 -29.737  -7.327  1.00 29.16           C  
ANISOU 2663  CG  TYR A 320     4457   3777   2845   -448    -30    -82       C  
ATOM   2664  CD1 TYR A 320       3.689 -28.972  -7.541  1.00 28.58           C  
ANISOU 2664  CD1 TYR A 320     4312   3769   2778   -447     18   -109       C  
ATOM   2665  CD2 TYR A 320       5.948 -29.109  -6.768  1.00 29.97           C  
ANISOU 2665  CD2 TYR A 320     4585   3842   2959   -412    -58    -70       C  
ATOM   2666  CE1 TYR A 320       3.664 -27.605  -7.238  1.00 27.17           C  
ANISOU 2666  CE1 TYR A 320     4096   3611   2617   -405     39   -125       C  
ATOM   2667  CE2 TYR A 320       5.932 -27.744  -6.459  1.00 30.71           C  
ANISOU 2667  CE2 TYR A 320     4644   3958   3068   -379    -38    -86       C  
ATOM   2668  CZ  TYR A 320       4.788 -27.000  -6.698  1.00 30.25           C  
ANISOU 2668  CZ  TYR A 320     4522   3956   3015   -373     12   -114       C  
ATOM   2669  OH  TYR A 320       4.772 -25.653  -6.385  1.00 30.15           O  
ANISOU 2669  OH  TYR A 320     4485   3956   3015   -336     32   -131       O  
ATOM   2670  N   ILE A 321       7.166 -32.048  -9.376  1.00 26.74           N  
ANISOU 2670  N   ILE A 321     4231   3343   2587   -378   -142    -28       N  
ATOM   2671  CA  ILE A 321       8.500 -31.830  -9.935  1.00 24.22           C  
ANISOU 2671  CA  ILE A 321     3901   2990   2310   -306   -176    -13       C  
ATOM   2672  C   ILE A 321       8.571 -32.286 -11.393  1.00 26.56           C  
ANISOU 2672  C   ILE A 321     4176   3285   2631   -274   -178    -16       C  
ATOM   2673  O   ILE A 321       9.048 -31.539 -12.258  1.00 26.06           O  
ANISOU 2673  O   ILE A 321     4058   3237   2608   -220   -177    -18       O  
ATOM   2674  CB  ILE A 321       9.596 -32.505  -9.067  1.00 24.47           C  
ANISOU 2674  CB  ILE A 321     4005   2962   2330   -301   -221     13       C  
ATOM   2675  CG1 ILE A 321       9.604 -31.908  -7.650  1.00 23.59           C  
ANISOU 2675  CG1 ILE A 321     3917   2854   2191   -332   -222     16       C  
ATOM   2676  CG2 ILE A 321      10.989 -32.385  -9.707  1.00 22.06           C  
ANISOU 2676  CG2 ILE A 321     3680   2631   2073   -226   -255     29       C  
ATOM   2677  CD1 ILE A 321       9.736 -30.376  -7.582  1.00 23.15           C  
ANISOU 2677  CD1 ILE A 321     3799   2835   2163   -302   -206      4       C  
ATOM   2678  N   SER A 322       8.079 -33.496 -11.670  1.00 25.98           N  
ANISOU 2678  N   SER A 322     4152   3191   2529   -313   -180    -17       N  
ATOM   2679  CA  SER A 322       8.068 -34.016 -13.040  1.00 26.45           C  
ANISOU 2679  CA  SER A 322     4203   3244   2602   -291   -181    -23       C  
ATOM   2680  C   SER A 322       7.343 -33.082 -14.016  1.00 26.29           C  
ANISOU 2680  C   SER A 322     4100   3286   2603   -279   -153    -41       C  
ATOM   2681  O   SER A 322       7.775 -32.920 -15.152  1.00 28.63           O  
ANISOU 2681  O   SER A 322     4371   3582   2926   -232   -156    -42       O  
ATOM   2682  CB  SER A 322       7.437 -35.409 -13.097  1.00 26.59           C  
ANISOU 2682  CB  SER A 322     4294   3233   2577   -351   -186    -25       C  
ATOM   2683  OG  SER A 322       8.265 -36.383 -12.491  1.00 28.07           O  
ANISOU 2683  OG  SER A 322     4568   3349   2749   -346   -219     -6       O  
ATOM   2684  N   TYR A 323       6.249 -32.470 -13.569  1.00 26.89           N  
ANISOU 2684  N   TYR A 323     4136   3415   2667   -318   -126    -54       N  
ATOM   2685  CA  TYR A 323       5.472 -31.574 -14.427  1.00 28.20           C  
ANISOU 2685  CA  TYR A 323     4223   3641   2853   -304   -104    -69       C  
ATOM   2686  C   TYR A 323       6.169 -30.242 -14.614  1.00 26.49           C  
ANISOU 2686  C   TYR A 323     3956   3432   2676   -237   -104    -66       C  
ATOM   2687  O   TYR A 323       5.962 -29.586 -15.622  1.00 28.45           O  
ANISOU 2687  O   TYR A 323     4153   3708   2947   -205    -98    -72       O  
ATOM   2688  CB  TYR A 323       4.045 -31.394 -13.895  1.00 29.67           C  
ANISOU 2688  CB  TYR A 323     4375   3885   3014   -362    -74    -85       C  
ATOM   2689  CG  TYR A 323       3.116 -32.560 -14.230  1.00 37.42           C  
ANISOU 2689  CG  TYR A 323     5380   4876   3960   -433    -72    -90       C  
ATOM   2690  CD1 TYR A 323       1.746 -32.490 -13.955  1.00 40.38           C  
ANISOU 2690  CD1 TYR A 323     5711   5317   4314   -491    -43   -105       C  
ATOM   2691  CD2 TYR A 323       3.603 -33.729 -14.837  1.00 38.78           C  
ANISOU 2691  CD2 TYR A 323     5620   4996   4119   -442    -98    -82       C  
ATOM   2692  CE1 TYR A 323       0.891 -33.554 -14.265  1.00 40.68           C  
ANISOU 2692  CE1 TYR A 323     5769   5368   4318   -567    -44   -108       C  
ATOM   2693  CE2 TYR A 323       2.753 -34.797 -15.149  1.00 40.30           C  
ANISOU 2693  CE2 TYR A 323     5844   5193   4275   -515    -99    -87       C  
ATOM   2694  CZ  TYR A 323       1.402 -34.698 -14.863  1.00 41.43           C  
ANISOU 2694  CZ  TYR A 323     5941   5404   4397   -582    -74    -99       C  
ATOM   2695  OH  TYR A 323       0.560 -35.748 -15.168  1.00 47.06           O  
ANISOU 2695  OH  TYR A 323     6684   6126   5072   -664    -77   -102       O  
ATOM   2696  N   ASN A 324       6.988 -29.849 -13.637  1.00 25.72           N  
ANISOU 2696  N   ASN A 324     3879   3309   2584   -221   -113    -56       N  
ATOM   2697  CA  ASN A 324       7.845 -28.674 -13.765  1.00 25.19           C  
ANISOU 2697  CA  ASN A 324     3778   3240   2553   -165   -119    -50       C  
ATOM   2698  C   ASN A 324       8.935 -28.922 -14.805  1.00 25.00           C  
ANISOU 2698  C   ASN A 324     3753   3189   2555   -118   -139    -37       C  
ATOM   2699  O   ASN A 324       9.227 -28.045 -15.610  1.00 23.70           O  
ANISOU 2699  O   ASN A 324     3545   3040   2419    -79   -135    -37       O  
ATOM   2700  CB  ASN A 324       8.455 -28.295 -12.408  1.00 24.52           C  
ANISOU 2700  CB  ASN A 324     3722   3133   2460   -171   -129    -42       C  
ATOM   2701  CG  ASN A 324       9.348 -27.058 -12.477  1.00 25.70           C  
ANISOU 2701  CG  ASN A 324     3841   3280   2643   -125   -139    -35       C  
ATOM   2702  OD1 ASN A 324      10.530 -27.123 -12.154  1.00 28.21           O  
ANISOU 2702  OD1 ASN A 324     4179   3566   2973   -107   -167    -17       O  
ATOM   2703  ND2 ASN A 324       8.783 -25.931 -12.877  1.00 24.88           N  
ANISOU 2703  ND2 ASN A 324     3691   3210   2554   -106   -117    -48       N  
ATOM   2704  N   ILE A 325       9.529 -30.118 -14.786  1.00 23.77           N  
ANISOU 2704  N   ILE A 325     3651   2992   2391   -121   -159    -27       N  
ATOM   2705  CA  ILE A 325      10.539 -30.502 -15.778  1.00 22.45           C  
ANISOU 2705  CA  ILE A 325     3484   2799   2246    -73   -172    -19       C  
ATOM   2706  C   ILE A 325       9.905 -30.591 -17.181  1.00 23.05           C  
ANISOU 2706  C   ILE A 325     3538   2899   2321    -70   -155    -32       C  
ATOM   2707  O   ILE A 325      10.459 -30.067 -18.148  1.00 23.57           O  
ANISOU 2707  O   ILE A 325     3572   2973   2412    -28   -150    -30       O  
ATOM   2708  CB  ILE A 325      11.239 -31.848 -15.417  1.00 22.17           C  
ANISOU 2708  CB  ILE A 325     3517   2709   2198    -71   -197     -8       C  
ATOM   2709  CG1 ILE A 325      12.009 -31.733 -14.096  1.00 21.78           C  
ANISOU 2709  CG1 ILE A 325     3489   2636   2151    -69   -224     10       C  
ATOM   2710  CG2 ILE A 325      12.168 -32.315 -16.559  1.00 19.67           C  
ANISOU 2710  CG2 ILE A 325     3200   2370   1904    -16   -201     -5       C  
ATOM   2711  CD1 ILE A 325      12.378 -33.103 -13.475  1.00 20.95           C  
ANISOU 2711  CD1 ILE A 325     3464   2475   2022    -79   -253     23       C  
ATOM   2712  N   ILE A 326       8.741 -31.237 -17.275  1.00 21.81           N  
ANISOU 2712  N   ILE A 326     3399   2754   2133   -119   -147    -44       N  
ATOM   2713  CA  ILE A 326       8.038 -31.396 -18.559  1.00 23.60           C  
ANISOU 2713  CA  ILE A 326     3610   3005   2353   -126   -138    -56       C  
ATOM   2714  C   ILE A 326       7.639 -30.053 -19.181  1.00 24.23           C  
ANISOU 2714  C   ILE A 326     3619   3133   2454   -103   -125    -60       C  
ATOM   2715  O   ILE A 326       7.767 -29.876 -20.389  1.00 27.02           O  
ANISOU 2715  O   ILE A 326     3958   3495   2815    -78   -124    -61       O  
ATOM   2716  CB  ILE A 326       6.821 -32.352 -18.438  1.00 22.73           C  
ANISOU 2716  CB  ILE A 326     3530   2903   2202   -197   -136    -67       C  
ATOM   2717  CG1 ILE A 326       7.314 -33.791 -18.207  1.00 19.51           C  
ANISOU 2717  CG1 ILE A 326     3209   2433   1770   -213   -152    -63       C  
ATOM   2718  CG2 ILE A 326       5.944 -32.299 -19.704  1.00 23.26           C  
ANISOU 2718  CG2 ILE A 326     3568   3009   2261   -211   -131    -79       C  
ATOM   2719  CD1 ILE A 326       6.223 -34.775 -17.778  1.00 20.96           C  
ANISOU 2719  CD1 ILE A 326     3439   2617   1909   -296   -152    -69       C  
ATOM   2720  N   ALA A 327       7.190 -29.111 -18.350  1.00 23.48           N  
ANISOU 2720  N   ALA A 327     3488   3067   2366   -108   -116    -62       N  
ATOM   2721  CA  ALA A 327       6.820 -27.768 -18.811  1.00 24.56           C  
ANISOU 2721  CA  ALA A 327     3565   3242   2524    -80   -107    -65       C  
ATOM   2722  C   ALA A 327       7.959 -27.082 -19.553  1.00 23.06           C  
ANISOU 2722  C   ALA A 327     3364   3035   2362    -27   -112    -52       C  
ATOM   2723  O   ALA A 327       7.748 -26.482 -20.605  1.00 26.83           O  
ANISOU 2723  O   ALA A 327     3813   3533   2847     -6   -111    -52       O  
ATOM   2724  CB  ALA A 327       6.354 -26.905 -17.641  1.00 23.63           C  
ANISOU 2724  CB  ALA A 327     3425   3144   2408    -87    -94    -70       C  
ATOM   2725  N   VAL A 328       9.164 -27.186 -19.004  1.00 22.94           N  
ANISOU 2725  N   VAL A 328     3372   2986   2360     -9   -121    -41       N  
ATOM   2726  CA  VAL A 328      10.374 -26.629 -19.620  1.00 22.50           C  
ANISOU 2726  CA  VAL A 328     3302   2916   2329     34   -124    -28       C  
ATOM   2727  C   VAL A 328      10.683 -27.288 -20.960  1.00 20.94           C  
ANISOU 2727  C   VAL A 328     3116   2713   2129     50   -120    -28       C  
ATOM   2728  O   VAL A 328      10.947 -26.604 -21.945  1.00 21.59           O  
ANISOU 2728  O   VAL A 328     3174   2808   2222     74   -113    -24       O  
ATOM   2729  CB  VAL A 328      11.601 -26.774 -18.678  1.00 23.82           C  
ANISOU 2729  CB  VAL A 328     3487   3053   2511     45   -139    -14       C  
ATOM   2730  CG1 VAL A 328      12.883 -26.342 -19.386  1.00 22.18           C  
ANISOU 2730  CG1 VAL A 328     3258   2840   2331     84   -140      0       C  
ATOM   2731  CG2 VAL A 328      11.388 -25.975 -17.388  1.00 22.39           C  
ANISOU 2731  CG2 VAL A 328     3302   2875   2329     27   -143    -14       C  
ATOM   2732  N   TYR A 329      10.648 -28.616 -20.986  1.00 21.67           N  
ANISOU 2732  N   TYR A 329     3251   2781   2202     35   -125    -34       N  
ATOM   2733  CA  TYR A 329      10.913 -29.386 -22.201  1.00 21.81           C  
ANISOU 2733  CA  TYR A 329     3293   2786   2209     50   -119    -40       C  
ATOM   2734  C   TYR A 329       9.908 -29.078 -23.310  1.00 23.41           C  
ANISOU 2734  C   TYR A 329     3479   3021   2394     34   -113    -49       C  
ATOM   2735  O   TYR A 329      10.265 -29.052 -24.492  1.00 24.29           O  
ANISOU 2735  O   TYR A 329     3592   3133   2502     55   -104    -50       O  
ATOM   2736  CB  TYR A 329      10.899 -30.889 -21.886  1.00 21.91           C  
ANISOU 2736  CB  TYR A 329     3367   2759   2199     31   -127    -46       C  
ATOM   2737  CG  TYR A 329      11.263 -31.786 -23.059  1.00 22.90           C  
ANISOU 2737  CG  TYR A 329     3531   2860   2310     50   -119    -56       C  
ATOM   2738  CD1 TYR A 329      12.334 -31.478 -23.900  1.00 23.87           C  
ANISOU 2738  CD1 TYR A 329     3636   2981   2451    102   -104    -52       C  
ATOM   2739  CD2 TYR A 329      10.549 -32.956 -23.305  1.00 27.13           C  
ANISOU 2739  CD2 TYR A 329     4126   3374   2809     13   -125    -69       C  
ATOM   2740  CE1 TYR A 329      12.669 -32.310 -24.973  1.00 26.98           C  
ANISOU 2740  CE1 TYR A 329     4071   3351   2828    122    -91    -65       C  
ATOM   2741  CE2 TYR A 329      10.874 -33.791 -24.364  1.00 28.24           C  
ANISOU 2741  CE2 TYR A 329     4312   3485   2931     30   -117    -81       C  
ATOM   2742  CZ  TYR A 329      11.936 -33.464 -25.192  1.00 29.12           C  
ANISOU 2742  CZ  TYR A 329     4406   3595   3062     88    -98    -80       C  
ATOM   2743  OH  TYR A 329      12.257 -34.296 -26.241  1.00 33.10           O  
ANISOU 2743  OH  TYR A 329     4961   4070   3544    107    -84    -96       O  
ATOM   2744  N   ARG A 330       8.650 -28.856 -22.936  1.00 23.11           N  
ANISOU 2744  N   ARG A 330     3423   3013   2344     -3   -117    -56       N  
ATOM   2745  CA  ARG A 330       7.623 -28.572 -23.936  1.00 25.54           C  
ANISOU 2745  CA  ARG A 330     3709   3358   2636    -18   -119    -62       C  
ATOM   2746  C   ARG A 330       7.886 -27.282 -24.701  1.00 24.03           C  
ANISOU 2746  C   ARG A 330     3480   3186   2464     20   -117    -52       C  
ATOM   2747  O   ARG A 330       7.599 -27.206 -25.893  1.00 28.45           O  
ANISOU 2747  O   ARG A 330     4040   3760   3009     22   -120    -53       O  
ATOM   2748  CB  ARG A 330       6.217 -28.616 -23.332  1.00 25.97           C  
ANISOU 2748  CB  ARG A 330     3741   3448   2677    -63   -124    -71       C  
ATOM   2749  CG  ARG A 330       5.722 -30.039 -23.157  1.00 30.45           C  
ANISOU 2749  CG  ARG A 330     4356   4001   3211   -116   -129    -81       C  
ATOM   2750  CD  ARG A 330       4.345 -30.069 -22.579  1.00 39.49           C  
ANISOU 2750  CD  ARG A 330     5471   5191   4343   -168   -129    -89       C  
ATOM   2751  NE  ARG A 330       3.812 -31.427 -22.552  1.00 44.72           N  
ANISOU 2751  NE  ARG A 330     6182   5841   4968   -231   -136    -97       N  
ATOM   2752  CZ  ARG A 330       2.570 -31.740 -22.189  1.00 45.65           C  
ANISOU 2752  CZ  ARG A 330     6279   6001   5066   -293   -136   -105       C  
ATOM   2753  NH1 ARG A 330       1.709 -30.793 -21.817  1.00 41.50           N  
ANISOU 2753  NH1 ARG A 330     5678   5536   4556   -292   -127   -108       N  
ATOM   2754  NH2 ARG A 330       2.191 -33.010 -22.205  1.00 45.53           N  
ANISOU 2754  NH2 ARG A 330     6319   5967   5014   -356   -144   -111       N  
ATOM   2755  N   VAL A 331       8.460 -26.287 -24.035  1.00 21.80           N  
ANISOU 2755  N   VAL A 331     3173   2901   2209     46   -112    -42       N  
ATOM   2756  CA  VAL A 331       8.875 -25.060 -24.719  1.00 22.40           C  
ANISOU 2756  CA  VAL A 331     3225   2986   2301     78   -110    -30       C  
ATOM   2757  C   VAL A 331      10.040 -25.345 -25.677  1.00 22.73           C  
ANISOU 2757  C   VAL A 331     3287   3008   2342     99   -100    -23       C  
ATOM   2758  O   VAL A 331      10.053 -24.844 -26.793  1.00 22.03           O  
ANISOU 2758  O   VAL A 331     3195   2930   2245    110    -97    -18       O  
ATOM   2759  CB  VAL A 331       9.224 -23.924 -23.738  1.00 23.30           C  
ANISOU 2759  CB  VAL A 331     3317   3096   2440     93   -110    -22       C  
ATOM   2760  CG1 VAL A 331       9.539 -22.645 -24.497  1.00 23.35           C  
ANISOU 2760  CG1 VAL A 331     3307   3106   2457    119   -110     -8       C  
ATOM   2761  CG2 VAL A 331       8.069 -23.683 -22.780  1.00 24.48           C  
ANISOU 2761  CG2 VAL A 331     3449   3267   2588     76   -112    -33       C  
ATOM   2762  N   LEU A 332      10.986 -26.183 -25.253  1.00 24.10           N  
ANISOU 2762  N   LEU A 332     3482   3153   2521    106    -93    -24       N  
ATOM   2763  CA  LEU A 332      12.068 -26.645 -26.134  1.00 24.65           C  
ANISOU 2763  CA  LEU A 332     3569   3207   2590    131    -77    -22       C  
ATOM   2764  C   LEU A 332      11.545 -27.358 -27.392  1.00 25.11           C  
ANISOU 2764  C   LEU A 332     3659   3267   2614    121    -71    -35       C  
ATOM   2765  O   LEU A 332      12.043 -27.122 -28.491  1.00 26.96           O  
ANISOU 2765  O   LEU A 332     3898   3506   2840    137    -55    -33       O  
ATOM   2766  CB  LEU A 332      13.042 -27.553 -25.369  1.00 24.43           C  
ANISOU 2766  CB  LEU A 332     3558   3148   2576    146    -75    -23       C  
ATOM   2767  CG  LEU A 332      13.859 -26.912 -24.242  1.00 28.05           C  
ANISOU 2767  CG  LEU A 332     3987   3603   3067    157    -84     -8       C  
ATOM   2768  CD1 LEU A 332      14.630 -27.981 -23.472  1.00 26.29           C  
ANISOU 2768  CD1 LEU A 332     3788   3350   2853    172    -92     -7       C  
ATOM   2769  CD2 LEU A 332      14.810 -25.842 -24.791  1.00 25.05           C  
ANISOU 2769  CD2 LEU A 332     3571   3239   2708    178    -71      7       C  
ATOM   2770  N   GLN A 333      10.531 -28.208 -27.220  1.00 24.73           N  
ANISOU 2770  N   GLN A 333     3637   3218   2543     88    -85    -49       N  
ATOM   2771  CA  GLN A 333       9.924 -28.941 -28.329  1.00 23.82           C  
ANISOU 2771  CA  GLN A 333     3559   3103   2389     67    -86    -62       C  
ATOM   2772  C   GLN A 333       9.168 -28.034 -29.283  1.00 23.87           C  
ANISOU 2772  C   GLN A 333     3542   3145   2382     59    -96    -56       C  
ATOM   2773  O   GLN A 333       9.201 -28.240 -30.493  1.00 23.34           O  
ANISOU 2773  O   GLN A 333     3503   3079   2287     58    -92    -60       O  
ATOM   2774  CB  GLN A 333       8.977 -30.017 -27.812  1.00 23.16           C  
ANISOU 2774  CB  GLN A 333     3507   3011   2283     23   -102    -75       C  
ATOM   2775  CG  GLN A 333       9.665 -31.170 -27.130  1.00 24.90           C  
ANISOU 2775  CG  GLN A 333     3774   3184   2502     28    -97    -82       C  
ATOM   2776  CD  GLN A 333       8.673 -32.140 -26.526  1.00 25.94           C  
ANISOU 2776  CD  GLN A 333     3940   3306   2608    -27   -114    -91       C  
ATOM   2777  OE1 GLN A 333       8.480 -33.240 -27.038  1.00 31.34           O  
ANISOU 2777  OE1 GLN A 333     4686   3962   3259    -49   -117   -105       O  
ATOM   2778  NE2 GLN A 333       8.030 -31.732 -25.438  1.00 26.05           N  
ANISOU 2778  NE2 GLN A 333     3921   3344   2634    -52   -123    -86       N  
ATOM   2779  N   ILE A 334       8.467 -27.043 -28.742  1.00 24.27           N  
ANISOU 2779  N   ILE A 334     3547   3225   2450     55   -111    -47       N  
ATOM   2780  CA  ILE A 334       7.804 -26.065 -29.591  1.00 24.83           C  
ANISOU 2780  CA  ILE A 334     3594   3327   2513     58   -125    -37       C  
ATOM   2781  C   ILE A 334       8.869 -25.348 -30.430  1.00 25.85           C  
ANISOU 2781  C   ILE A 334     3731   3446   2646     89   -108    -24       C  
ATOM   2782  O   ILE A 334       8.715 -25.203 -31.649  1.00 27.47           O  
ANISOU 2782  O   ILE A 334     3955   3660   2823     86   -112    -20       O  
ATOM   2783  CB  ILE A 334       6.921 -25.066 -28.772  1.00 22.84           C  
ANISOU 2783  CB  ILE A 334     3290   3103   2284     60   -141    -31       C  
ATOM   2784  CG1 ILE A 334       5.759 -25.809 -28.093  1.00 22.56           C  
ANISOU 2784  CG1 ILE A 334     3243   3090   2239     22   -153    -46       C  
ATOM   2785  CG2 ILE A 334       6.382 -23.966 -29.676  1.00 23.42           C  
ANISOU 2785  CG2 ILE A 334     3344   3202   2354     76   -159    -18       C  
ATOM   2786  CD1 ILE A 334       5.064 -25.014 -26.982  1.00 21.18           C  
ANISOU 2786  CD1 ILE A 334     3019   2939   2089     28   -155    -46       C  
ATOM   2787  N   ASP A 335       9.961 -24.937 -29.785  1.00 25.11           N  
ANISOU 2787  N   ASP A 335     3624   3335   2582    113    -90    -15       N  
ATOM   2788  CA  ASP A 335      11.025 -24.233 -30.493  1.00 26.00           C  
ANISOU 2788  CA  ASP A 335     3737   3443   2699    134    -70     -1       C  
ATOM   2789  C   ASP A 335      11.772 -25.064 -31.532  1.00 23.88           C  
ANISOU 2789  C   ASP A 335     3505   3164   2405    139    -44    -10       C  
ATOM   2790  O   ASP A 335      12.166 -24.528 -32.563  1.00 23.83           O  
ANISOU 2790  O   ASP A 335     3508   3164   2382    144    -30      0       O  
ATOM   2791  CB  ASP A 335      12.047 -23.582 -29.562  1.00 25.09           C  
ANISOU 2791  CB  ASP A 335     3594   3317   2621    151    -60     11       C  
ATOM   2792  CG  ASP A 335      12.914 -22.570 -30.308  1.00 30.54           C  
ANISOU 2792  CG  ASP A 335     4279   4012   3314    161    -44     30       C  
ATOM   2793  OD1 ASP A 335      12.343 -21.582 -30.822  1.00 30.58           O  
ANISOU 2793  OD1 ASP A 335     4286   4026   3309    157    -58     42       O  
ATOM   2794  OD2 ASP A 335      14.142 -22.778 -30.425  1.00 28.88           O  
ANISOU 2794  OD2 ASP A 335     4063   3796   3113    171    -17     33       O  
ATOM   2795  N   ALA A 336      11.990 -26.348 -31.250  1.00 21.25           N  
ANISOU 2795  N   ALA A 336     3197   2809   2066    140    -35    -28       N  
ATOM   2796  CA  ALA A 336      12.585 -27.251 -32.235  1.00 21.89           C  
ANISOU 2796  CA  ALA A 336     3321   2875   2119    150     -8    -42       C  
ATOM   2797  C   ALA A 336      11.705 -27.323 -33.481  1.00 23.55           C  
ANISOU 2797  C   ALA A 336     3568   3097   2282    124    -19    -48       C  
ATOM   2798  O   ALA A 336      12.197 -27.525 -34.592  1.00 23.20           O  
ANISOU 2798  O   ALA A 336     3558   3050   2208    130      6    -54       O  
ATOM   2799  CB  ALA A 336      12.811 -28.646 -31.643  1.00 20.57           C  
ANISOU 2799  CB  ALA A 336     3186   2675   1953    156     -4    -61       C  
ATOM   2800  N   LYS A 337      10.402 -27.137 -33.281  1.00 26.45           N  
ANISOU 2800  N   LYS A 337     3925   3483   2641     94    -56    -46       N  
ATOM   2801  CA  LYS A 337       9.431 -27.110 -34.372  1.00 25.68           C  
ANISOU 2801  CA  LYS A 337     3852   3403   2500     66    -79    -47       C  
ATOM   2802  C   LYS A 337       9.365 -25.733 -35.061  1.00 25.67           C  
ANISOU 2802  C   LYS A 337     3832   3426   2498     75    -89    -23       C  
ATOM   2803  O   LYS A 337       9.616 -25.627 -36.273  1.00 26.50           O  
ANISOU 2803  O   LYS A 337     3972   3531   2565     72    -79    -21       O  
ATOM   2804  CB  LYS A 337       8.053 -27.525 -33.858  1.00 24.32           C  
ANISOU 2804  CB  LYS A 337     3669   3249   2323     30   -117    -54       C  
ATOM   2805  CG  LYS A 337       6.997 -27.530 -34.934  1.00 27.63           C  
ANISOU 2805  CG  LYS A 337     4105   3692   2699     -3   -150    -54       C  
ATOM   2806  CD  LYS A 337       5.622 -27.855 -34.400  1.00 28.38           C  
ANISOU 2806  CD  LYS A 337     4174   3817   2793    -42   -187    -59       C  
ATOM   2807  CE  LYS A 337       4.605 -27.795 -35.547  1.00 31.90           C  
ANISOU 2807  CE  LYS A 337     4630   4293   3197    -75   -227    -55       C  
ATOM   2808  NZ  LYS A 337       3.210 -27.510 -35.101  1.00 30.73           N  
ANISOU 2808  NZ  LYS A 337     4421   4194   3060   -100   -268    -49       N  
ATOM   2809  N   ARG A 338       9.040 -24.694 -34.287  1.00 23.38           N  
ANISOU 2809  N   ARG A 338     3492   3150   2243     86   -106     -7       N  
ATOM   2810  CA  ARG A 338       8.810 -23.351 -34.825  1.00 20.98           C  
ANISOU 2810  CA  ARG A 338     3175   2861   1937     96   -124     17       C  
ATOM   2811  C   ARG A 338      10.085 -22.610 -35.186  1.00 22.27           C  
ANISOU 2811  C   ARG A 338     3345   3010   2106    114    -91     32       C  
ATOM   2812  O   ARG A 338      10.117 -21.886 -36.186  1.00 21.54           O  
ANISOU 2812  O   ARG A 338     3274   2922   1988    111    -96     49       O  
ATOM   2813  CB  ARG A 338       7.975 -22.497 -33.857  1.00 22.61           C  
ANISOU 2813  CB  ARG A 338     3331   3082   2178    107   -153     26       C  
ATOM   2814  CG  ARG A 338       6.492 -22.890 -33.759  1.00 19.36           C  
ANISOU 2814  CG  ARG A 338     2899   2700   1756     87   -190     17       C  
ATOM   2815  CD  ARG A 338       5.730 -22.713 -35.086  1.00 18.63           C  
ANISOU 2815  CD  ARG A 338     2827   2628   1623     74   -224     26       C  
ATOM   2816  NE  ARG A 338       4.292 -22.779 -34.858  1.00 19.79           N  
ANISOU 2816  NE  ARG A 338     2934   2814   1773     61   -265     23       N  
ATOM   2817  CZ  ARG A 338       3.377 -22.094 -35.539  1.00 22.21           C  
ANISOU 2817  CZ  ARG A 338     3225   3149   2067     67   -308     39       C  
ATOM   2818  NH1 ARG A 338       3.728 -21.279 -36.534  1.00 22.19           N  
ANISOU 2818  NH1 ARG A 338     3254   3134   2044     84   -319     61       N  
ATOM   2819  NH2 ARG A 338       2.097 -22.222 -35.215  1.00 20.05           N  
ANISOU 2819  NH2 ARG A 338     2901   2917   1801     57   -342     34       N  
ATOM   2820  N   GLN A 339      11.122 -22.770 -34.361  1.00 22.33           N  
ANISOU 2820  N   GLN A 339     3334   3003   2147    128    -61     29       N  
ATOM   2821  CA  GLN A 339      12.458 -22.198 -34.614  1.00 22.44           C  
ANISOU 2821  CA  GLN A 339     3346   3011   2170    139    -26     42       C  
ATOM   2822  C   GLN A 339      12.487 -20.667 -34.491  1.00 23.19           C  
ANISOU 2822  C   GLN A 339     3424   3107   2279    141    -40     69       C  
ATOM   2823  O   GLN A 339      13.163 -19.980 -35.264  1.00 22.96           O  
ANISOU 2823  O   GLN A 339     3410   3078   2235    135    -22     86       O  
ATOM   2824  CB  GLN A 339      13.041 -22.698 -35.955  1.00 21.88           C  
ANISOU 2824  CB  GLN A 339     3316   2940   2056    134      7     36       C  
ATOM   2825  CG  GLN A 339      13.055 -24.245 -36.061  1.00 26.82           C  
ANISOU 2825  CG  GLN A 339     3970   3555   2664    136     23      6       C  
ATOM   2826  CD  GLN A 339      13.727 -24.817 -37.318  1.00 32.68           C  
ANISOU 2826  CD  GLN A 339     4758   4294   3363    137     65     -6       C  
ATOM   2827  OE1 GLN A 339      13.690 -26.026 -37.543  1.00 37.20           O  
ANISOU 2827  OE1 GLN A 339     5368   4852   3915    140     77    -32       O  
ATOM   2828  NE2 GLN A 339      14.342 -23.962 -38.128  1.00 35.72           N  
ANISOU 2828  NE2 GLN A 339     5149   4692   3732    133     89     11       N  
ATOM   2829  N   PHE A 340      11.760 -20.149 -33.499  1.00 23.65           N  
ANISOU 2829  N   PHE A 340     3747   2627   2611   -109   -210    224       N  
ATOM   2830  CA  PHE A 340      11.691 -18.706 -33.261  1.00 24.29           C  
ANISOU 2830  CA  PHE A 340     3758   2735   2734    -95   -209    237       C  
ATOM   2831  C   PHE A 340      12.970 -18.152 -32.653  1.00 23.36           C  
ANISOU 2831  C   PHE A 340     3626   2639   2610    -43   -166    213       C  
ATOM   2832  O   PHE A 340      13.306 -16.990 -32.878  1.00 25.08           O  
ANISOU 2832  O   PHE A 340     3812   2876   2841    -34   -166    216       O  
ATOM   2833  CB  PHE A 340      10.470 -18.314 -32.398  1.00 24.02           C  
ANISOU 2833  CB  PHE A 340     3659   2703   2765   -105   -215    267       C  
ATOM   2834  CG  PHE A 340       9.134 -18.632 -33.029  1.00 25.89           C  
ANISOU 2834  CG  PHE A 340     3887   2921   3028   -162   -266    306       C  
ATOM   2835  CD1 PHE A 340       8.959 -18.587 -34.411  1.00 24.91           C  
ANISOU 2835  CD1 PHE A 340     3797   2790   2878   -206   -319    320       C  
ATOM   2836  CD2 PHE A 340       8.035 -18.955 -32.229  1.00 28.08           C  
ANISOU 2836  CD2 PHE A 340     4124   3187   3360   -173   -264    334       C  
ATOM   2837  CE1 PHE A 340       7.715 -18.884 -34.989  1.00 24.87           C  
ANISOU 2837  CE1 PHE A 340     3784   2766   2899   -267   -380    363       C  
ATOM   2838  CE2 PHE A 340       6.791 -19.249 -32.793  1.00 23.95           C  
ANISOU 2838  CE2 PHE A 340     3581   2646   2873   -229   -318    380       C  
ATOM   2839  CZ  PHE A 340       6.635 -19.213 -34.180  1.00 25.47           C  
ANISOU 2839  CZ  PHE A 340     3807   2832   3039   -279   -382    396       C  
ATOM   2840  N   ILE A 341      13.684 -18.966 -31.879  1.00 23.86           N  
ANISOU 2840  N   ILE A 341     3712   2697   2656    -11   -135    193       N  
ATOM   2841  CA  ILE A 341      14.967 -18.517 -31.316  1.00 23.82           C  
ANISOU 2841  CA  ILE A 341     3692   2710   2649     33   -106    178       C  
ATOM   2842  C   ILE A 341      15.977 -18.301 -32.456  1.00 23.60           C  
ANISOU 2842  C   ILE A 341     3689   2685   2594     41    -97    170       C  
ATOM   2843  O   ILE A 341      16.616 -17.239 -32.543  1.00 21.90           O  
ANISOU 2843  O   ILE A 341     3440   2490   2390     56    -92    171       O  
ATOM   2844  CB  ILE A 341      15.524 -19.486 -30.227  1.00 24.91           C  
ANISOU 2844  CB  ILE A 341     3847   2839   2778     63    -81    167       C  
ATOM   2845  CG1 ILE A 341      14.531 -19.648 -29.061  1.00 25.58           C  
ANISOU 2845  CG1 ILE A 341     3916   2918   2887     55    -81    175       C  
ATOM   2846  CG2 ILE A 341      16.882 -19.002 -29.700  1.00 27.56           C  
ANISOU 2846  CG2 ILE A 341     4163   3192   3116    101    -64    162       C  
ATOM   2847  CD1 ILE A 341      14.302 -18.385 -28.246  1.00 31.49           C  
ANISOU 2847  CD1 ILE A 341     4619   3681   3666     61    -76    182       C  
ATOM   2848  N   ASN A 342      16.089 -19.300 -33.334  1.00 22.40           N  
ANISOU 2848  N   ASN A 342     3599   2507   2404     30    -92    164       N  
ATOM   2849  CA  ASN A 342      16.911 -19.214 -34.554  1.00 23.58           C  
ANISOU 2849  CA  ASN A 342     3789   2647   2521     33    -74    157       C  
ATOM   2850  C   ASN A 342      16.574 -17.977 -35.392  1.00 21.36           C  
ANISOU 2850  C   ASN A 342     3488   2381   2246      7   -101    168       C  
ATOM   2851  O   ASN A 342      17.468 -17.266 -35.840  1.00 19.20           O  
ANISOU 2851  O   ASN A 342     3206   2119   1971     26    -80    166       O  
ATOM   2852  CB  ASN A 342      16.747 -20.491 -35.398  1.00 25.11           C  
ANISOU 2852  CB  ASN A 342     4074   2800   2666     12    -67    149       C  
ATOM   2853  CG  ASN A 342      17.560 -20.462 -36.691  1.00 29.97           C  
ANISOU 2853  CG  ASN A 342     4751   3396   3242     15    -36    142       C  
ATOM   2854  OD1 ASN A 342      18.780 -20.631 -36.670  1.00 31.67           O  
ANISOU 2854  OD1 ASN A 342     4969   3607   3459     61     19    136       O  
ATOM   2855  ND2 ASN A 342      16.876 -20.283 -37.826  1.00 28.44           N  
ANISOU 2855  ND2 ASN A 342     4609   3185   3012    -36    -69    146       N  
ATOM   2856  N   LEU A 343      15.280 -17.726 -35.582  1.00 21.72           N  
ANISOU 2856  N   LEU A 343     3523   2426   2303    -36   -148    185       N  
ATOM   2857  CA  LEU A 343      14.803 -16.542 -36.303  1.00 20.67           C  
ANISOU 2857  CA  LEU A 343     3364   2305   2183    -63   -180    203       C  
ATOM   2858  C   LEU A 343      15.265 -15.249 -35.636  1.00 21.79           C  
ANISOU 2858  C   LEU A 343     3435   2479   2365    -32   -165    205       C  
ATOM   2859  O   LEU A 343      15.747 -14.334 -36.305  1.00 25.21           O  
ANISOU 2859  O   LEU A 343     3861   2923   2795    -30   -163    207       O  
ATOM   2860  CB  LEU A 343      13.273 -16.561 -36.419  1.00 20.18           C  
ANISOU 2860  CB  LEU A 343     3287   2236   2146   -113   -235    232       C  
ATOM   2861  CG  LEU A 343      12.545 -15.295 -36.922  1.00 23.80           C  
ANISOU 2861  CG  LEU A 343     3698   2707   2639   -139   -275    263       C  
ATOM   2862  CD1 LEU A 343      12.794 -15.048 -38.421  1.00 21.23           C  
ANISOU 2862  CD1 LEU A 343     3431   2369   2265   -171   -300    266       C  
ATOM   2863  CD2 LEU A 343      11.050 -15.422 -36.634  1.00 22.61           C  
ANISOU 2863  CD2 LEU A 343     3507   2548   2537   -176   -318    300       C  
ATOM   2864  N   SER A 344      15.110 -15.180 -34.317  1.00 20.87           N  
ANISOU 2864  N   SER A 344     3274   2373   2283    -10   -153    204       N  
ATOM   2865  CA  SER A 344      15.480 -13.994 -33.552  1.00 21.20           C  
ANISOU 2865  CA  SER A 344     3262   2437   2357     14   -140    205       C  
ATOM   2866  C   SER A 344      16.957 -13.683 -33.681  1.00 19.33           C  
ANISOU 2866  C   SER A 344     3026   2212   2104     44   -114    191       C  
ATOM   2867  O   SER A 344      17.327 -12.537 -33.936  1.00 20.47           O  
ANISOU 2867  O   SER A 344     3143   2372   2261     47   -114    195       O  
ATOM   2868  CB  SER A 344      15.115 -14.167 -32.079  1.00 20.96           C  
ANISOU 2868  CB  SER A 344     3207   2406   2351     29   -126    204       C  
ATOM   2869  OG  SER A 344      13.715 -14.283 -31.937  1.00 21.83           O  
ANISOU 2869  OG  SER A 344     3301   2504   2490      3   -142    224       O  
ATOM   2870  N   LEU A 345      17.791 -14.708 -33.511  1.00 17.72           N  
ANISOU 2870  N   LEU A 345     2852   2000   1881     67    -90    179       N  
ATOM   2871  CA  LEU A 345      19.239 -14.566 -33.628  1.00 19.18           C  
ANISOU 2871  CA  LEU A 345     3032   2193   2064     98    -62    175       C  
ATOM   2872  C   LEU A 345      19.632 -14.093 -35.045  1.00 21.19           C  
ANISOU 2872  C   LEU A 345     3307   2444   2300     90    -53    177       C  
ATOM   2873  O   LEU A 345      20.378 -13.111 -35.191  1.00 22.62           O  
ANISOU 2873  O   LEU A 345     3456   2642   2497    101    -44    183       O  
ATOM   2874  CB  LEU A 345      19.940 -15.881 -33.250  1.00 20.52           C  
ANISOU 2874  CB  LEU A 345     3228   2346   2222    125    -36    170       C  
ATOM   2875  CG  LEU A 345      19.954 -16.339 -31.783  1.00 21.82           C  
ANISOU 2875  CG  LEU A 345     3374   2513   2402    141    -41    170       C  
ATOM   2876  CD1 LEU A 345      20.396 -17.806 -31.678  1.00 18.07           C  
ANISOU 2876  CD1 LEU A 345     2937   2015   1913    162    -17    167       C  
ATOM   2877  CD2 LEU A 345      20.828 -15.438 -30.889  1.00 18.53           C  
ANISOU 2877  CD2 LEU A 345     2909   2118   2012    158    -47    179       C  
ATOM   2878  N   ASP A 346      19.100 -14.761 -36.072  1.00 20.48           N  
ANISOU 2878  N   ASP A 346     3277   2330   2174     65    -56    174       N  
ATOM   2879  CA  ASP A 346      19.285 -14.340 -37.470  1.00 25.28           C  
ANISOU 2879  CA  ASP A 346     3923   2927   2753     47    -51    177       C  
ATOM   2880  C   ASP A 346      18.985 -12.856 -37.715  1.00 25.76           C  
ANISOU 2880  C   ASP A 346     3940   3012   2836     31    -78    189       C  
ATOM   2881  O   ASP A 346      19.818 -12.152 -38.272  1.00 26.74           O  
ANISOU 2881  O   ASP A 346     4058   3142   2959     43    -55    190       O  
ATOM   2882  CB  ASP A 346      18.424 -15.183 -38.418  1.00 27.06           C  
ANISOU 2882  CB  ASP A 346     4229   3121   2932      6    -71    175       C  
ATOM   2883  CG  ASP A 346      19.050 -16.525 -38.747  1.00 33.05           C  
ANISOU 2883  CG  ASP A 346     5062   3844   3652     22    -25    161       C  
ATOM   2884  OD1 ASP A 346      20.132 -16.839 -38.211  1.00 36.60           O  
ANISOU 2884  OD1 ASP A 346     5490   4296   4120     70     23    157       O  
ATOM   2885  OD2 ASP A 346      18.458 -17.272 -39.552  1.00 37.37           O  
ANISOU 2885  OD2 ASP A 346     5691   4358   4151    -14    -39    157       O  
ATOM   2886  N   MET A 347      17.797 -12.400 -37.307  1.00 26.89           N  
ANISOU 2886  N   MET A 347     4051   3164   3003      6   -120    200       N  
ATOM   2887  CA  MET A 347      17.361 -11.011 -37.525  1.00 26.71           C  
ANISOU 2887  CA  MET A 347     3986   3157   3006     -8   -145    216       C  
ATOM   2888  C   MET A 347      18.195 -10.059 -36.690  1.00 24.98           C  
ANISOU 2888  C   MET A 347     3712   2961   2818     23   -123    212       C  
ATOM   2889  O   MET A 347      18.640  -9.022 -37.188  1.00 23.79           O  
ANISOU 2889  O   MET A 347     3546   2820   2672     23   -120    217       O  
ATOM   2890  CB  MET A 347      15.886 -10.817 -37.164  1.00 29.00           C  
ANISOU 2890  CB  MET A 347     4246   3445   3326    -36   -186    237       C  
ATOM   2891  CG  MET A 347      14.868 -11.541 -38.040  1.00 39.43           C  
ANISOU 2891  CG  MET A 347     5612   4744   4626    -81   -227    252       C  
ATOM   2892  SD  MET A 347      13.163 -11.381 -37.399  1.00 51.48           S  
ANISOU 2892  SD  MET A 347     7080   6268   6213   -107   -269    288       S  
ATOM   2893  CE  MET A 347      12.999  -9.595 -37.216  1.00 41.52           C  
ANISOU 2893  CE  MET A 347     5747   5024   5003    -95   -267    309       C  
ATOM   2894  N   GLY A 348      18.396 -10.420 -35.419  1.00 23.17           N  
ANISOU 2894  N   GLY A 348     3461   2737   2606     45   -111    204       N  
ATOM   2895  CA  GLY A 348      19.207  -9.636 -34.490  1.00 20.09           C  
ANISOU 2895  CA  GLY A 348     3030   2363   2239     68    -99    202       C  
ATOM   2896  C   GLY A 348      20.614  -9.365 -34.998  1.00 20.72           C  
ANISOU 2896  C   GLY A 348     3106   2451   2315     86    -77    202       C  
ATOM   2897  O   GLY A 348      21.062  -8.212 -35.047  1.00 21.89           O  
ANISOU 2897  O   GLY A 348     3225   2612   2479     85    -78    208       O  
ATOM   2898  N   TYR A 349      21.313 -10.421 -35.395  1.00 21.65           N  
ANISOU 2898  N   TYR A 349     3253   2558   2416    102    -51    198       N  
ATOM   2899  CA  TYR A 349      22.686 -10.258 -35.881  1.00 23.01           C  
ANISOU 2899  CA  TYR A 349     3416   2732   2595    124    -18    205       C  
ATOM   2900  C   TYR A 349      22.755  -9.549 -37.238  1.00 23.83           C  
ANISOU 2900  C   TYR A 349     3540   2833   2683    110     -7    209       C  
ATOM   2901  O   TYR A 349      23.679  -8.778 -37.490  1.00 25.60           O  
ANISOU 2901  O   TYR A 349     3735   3066   2925    120     11    219       O  
ATOM   2902  CB  TYR A 349      23.445 -11.582 -35.883  1.00 20.04           C  
ANISOU 2902  CB  TYR A 349     3064   2339   2214    153     19    205       C  
ATOM   2903  CG  TYR A 349      23.824 -12.041 -34.494  1.00 22.31           C  
ANISOU 2903  CG  TYR A 349     3318   2633   2526    172      8    210       C  
ATOM   2904  CD1 TYR A 349      24.631 -11.256 -33.677  1.00 22.44           C  
ANISOU 2904  CD1 TYR A 349     3280   2668   2577    179     -7    225       C  
ATOM   2905  CD2 TYR A 349      23.369 -13.264 -33.994  1.00 18.43           C  
ANISOU 2905  CD2 TYR A 349     2856   2126   2020    177      8    202       C  
ATOM   2906  CE1 TYR A 349      24.967 -11.671 -32.397  1.00 21.04           C  
ANISOU 2906  CE1 TYR A 349     3082   2494   2417    189    -27    233       C  
ATOM   2907  CE2 TYR A 349      23.705 -13.689 -32.723  1.00 17.72           C  
ANISOU 2907  CE2 TYR A 349     2743   2041   1949    193     -5    209       C  
ATOM   2908  CZ  TYR A 349      24.499 -12.894 -31.930  1.00 20.38           C  
ANISOU 2908  CZ  TYR A 349     3030   2396   2318    197    -24    225       C  
ATOM   2909  OH  TYR A 349      24.838 -13.328 -30.671  1.00 18.93           O  
ANISOU 2909  OH  TYR A 349     2833   2213   2147    206    -45    234       O  
ATOM   2910  N   TYR A 350      21.759  -9.783 -38.086  1.00 24.79           N  
ANISOU 2910  N   TYR A 350     3710   2939   2771     82    -22    204       N  
ATOM   2911  CA  TYR A 350      21.662  -9.091 -39.372  1.00 24.96           C  
ANISOU 2911  CA  TYR A 350     3760   2953   2769     61    -22    210       C  
ATOM   2912  C   TYR A 350      21.570  -7.556 -39.211  1.00 24.02           C  
ANISOU 2912  C   TYR A 350     3588   2858   2680     52    -44    220       C  
ATOM   2913  O   TYR A 350      22.255  -6.812 -39.913  1.00 22.31           O  
ANISOU 2913  O   TYR A 350     3371   2644   2463     54    -25    227       O  
ATOM   2914  CB  TYR A 350      20.471  -9.636 -40.175  1.00 26.10           C  
ANISOU 2914  CB  TYR A 350     3968   3076   2873     22    -53    209       C  
ATOM   2915  CG  TYR A 350      20.369  -9.076 -41.574  1.00 26.17           C  
ANISOU 2915  CG  TYR A 350     4025   3071   2846     -6    -58    217       C  
ATOM   2916  CD1 TYR A 350      21.148  -9.587 -42.612  1.00 27.45           C  
ANISOU 2916  CD1 TYR A 350     4261   3205   2964     -1    -10    211       C  
ATOM   2917  CD2 TYR A 350      19.501  -8.025 -41.854  1.00 22.49           C  
ANISOU 2917  CD2 TYR A 350     3537   2617   2393    -36   -107    234       C  
ATOM   2918  CE1 TYR A 350      21.062  -9.055 -43.904  1.00 30.12           C  
ANISOU 2918  CE1 TYR A 350     4657   3526   3262    -31    -13    218       C  
ATOM   2919  CE2 TYR A 350      19.406  -7.492 -43.130  1.00 27.23           C  
ANISOU 2919  CE2 TYR A 350     4184   3202   2958    -65   -118    245       C  
ATOM   2920  CZ  TYR A 350      20.181  -8.007 -44.149  1.00 27.83           C  
ANISOU 2920  CZ  TYR A 350     4341   3250   2982    -64    -73    235       C  
ATOM   2921  OH  TYR A 350      20.077  -7.460 -45.405  1.00 29.89           O  
ANISOU 2921  OH  TYR A 350     4661   3493   3202    -96    -83    246       O  
ATOM   2922  N   ALA A 351      20.726  -7.100 -38.287  1.00 23.64           N  
ANISOU 2922  N   ALA A 351     3502   2823   2659     43    -79    223       N  
ATOM   2923  CA  ALA A 351      20.492  -5.667 -38.053  1.00 22.85           C  
ANISOU 2923  CA  ALA A 351     3359   2736   2586     35    -96    232       C  
ATOM   2924  C   ALA A 351      21.567  -5.037 -37.180  1.00 24.54           C  
ANISOU 2924  C   ALA A 351     3530   2965   2827     56    -80    230       C  
ATOM   2925  O   ALA A 351      21.748  -3.811 -37.188  1.00 23.68           O  
ANISOU 2925  O   ALA A 351     3396   2865   2735     50    -85    237       O  
ATOM   2926  CB  ALA A 351      19.125  -5.457 -37.409  1.00 23.35           C  
ANISOU 2926  CB  ALA A 351     3403   2798   2671     21   -127    239       C  
ATOM   2927  N   LYS A 352      22.260  -5.894 -36.427  1.00 25.99           N  
ANISOU 2927  N   LYS A 352     3710   3151   3016     77    -66    224       N  
ATOM   2928  CA  LYS A 352      23.213  -5.502 -35.384  1.00 26.63           C  
ANISOU 2928  CA  LYS A 352     3754   3243   3123     90    -67    228       C  
ATOM   2929  C   LYS A 352      22.523  -4.713 -34.273  1.00 24.43           C  
ANISOU 2929  C   LYS A 352     3460   2966   2856     78    -91    225       C  
ATOM   2930  O   LYS A 352      22.800  -3.529 -34.047  1.00 24.08           O  
ANISOU 2930  O   LYS A 352     3396   2926   2825     69    -99    229       O  
ATOM   2931  CB  LYS A 352      24.406  -4.747 -35.978  1.00 30.04           C  
ANISOU 2931  CB  LYS A 352     4161   3682   3569     95    -49    241       C  
ATOM   2932  CG  LYS A 352      25.250  -5.607 -36.895  1.00 30.32           C  
ANISOU 2932  CG  LYS A 352     4212   3708   3598    115     -8    248       C  
ATOM   2933  CD  LYS A 352      26.253  -4.777 -37.662  1.00 32.61           C  
ANISOU 2933  CD  LYS A 352     4481   4002   3906    118     17    265       C  
ATOM   2934  CE  LYS A 352      26.966  -5.650 -38.669  1.00 32.28           C  
ANISOU 2934  CE  LYS A 352     4468   3942   3857    140     74    272       C  
ATOM   2935  NZ  LYS A 352      27.817  -4.862 -39.573  1.00 29.28           N  
ANISOU 2935  NZ  LYS A 352     4076   3560   3490    142    110    288       N  
ATOM   2936  N   ILE A 353      21.606  -5.398 -33.602  1.00 23.20           N  
ANISOU 2936  N   ILE A 353     3320   2801   2694     77    -98    217       N  
ATOM   2937  CA  ILE A 353      20.810  -4.846 -32.510  1.00 22.00           C  
ANISOU 2937  CA  ILE A 353     3166   2640   2551     69   -107    213       C  
ATOM   2938  C   ILE A 353      20.872  -5.805 -31.327  1.00 23.50           C  
ANISOU 2938  C   ILE A 353     3370   2824   2734     78   -109    206       C  
ATOM   2939  O   ILE A 353      21.302  -6.959 -31.474  1.00 22.15           O  
ANISOU 2939  O   ILE A 353     3208   2654   2554     91   -105    204       O  
ATOM   2940  CB  ILE A 353      19.317  -4.697 -32.922  1.00 21.97           C  
ANISOU 2940  CB  ILE A 353     3166   2626   2556     57   -109    219       C  
ATOM   2941  CG1 ILE A 353      18.766  -6.020 -33.486  1.00 22.43           C  
ANISOU 2941  CG1 ILE A 353     3244   2680   2600     56   -113    219       C  
ATOM   2942  CG2 ILE A 353      19.145  -3.573 -33.922  1.00 20.96           C  
ANISOU 2942  CG2 ILE A 353     3025   2502   2439     46   -113    231       C  
ATOM   2943  CD1 ILE A 353      17.293  -5.987 -33.859  1.00 19.42           C  
ANISOU 2943  CD1 ILE A 353     2858   2286   2234     38   -126    234       C  
ATOM   2944  N   GLN A 354      20.419  -5.341 -30.164  1.00 23.36           N  
ANISOU 2944  N   GLN A 354     3363   2794   2719     72   -109    202       N  
ATOM   2945  CA  GLN A 354      20.168  -6.242 -29.048  1.00 23.72           C  
ANISOU 2945  CA  GLN A 354     3433   2826   2753     77   -108    195       C  
ATOM   2946  C   GLN A 354      19.169  -7.271 -29.562  1.00 23.62           C  
ANISOU 2946  C   GLN A 354     3424   2808   2740     81    -99    195       C  
ATOM   2947  O   GLN A 354      18.214  -6.896 -30.247  1.00 24.32           O  
ANISOU 2947  O   GLN A 354     3502   2893   2843     72    -95    202       O  
ATOM   2948  CB  GLN A 354      19.567  -5.487 -27.866  1.00 23.21           C  
ANISOU 2948  CB  GLN A 354     3392   2739   2687     68    -97    191       C  
ATOM   2949  CG  GLN A 354      20.392  -4.319 -27.354  1.00 26.89           C  
ANISOU 2949  CG  GLN A 354     3867   3203   3147     54   -110    191       C  
ATOM   2950  CD  GLN A 354      19.852  -3.773 -26.047  1.00 32.52           C  
ANISOU 2950  CD  GLN A 354     4628   3883   3846     43    -93    184       C  
ATOM   2951  OE1 GLN A 354      20.461  -3.950 -24.990  1.00 33.05           O  
ANISOU 2951  OE1 GLN A 354     4733   3939   3887     32   -111    180       O  
ATOM   2952  NE2 GLN A 354      18.695  -3.120 -26.106  1.00 31.64           N  
ANISOU 2952  NE2 GLN A 354     4520   3751   3752     46    -56    185       N  
ATOM   2953  N   ILE A 355      19.377  -8.552 -29.253  1.00 22.77           N  
ANISOU 2953  N   ILE A 355     3333   2699   2620     91    -99    190       N  
ATOM   2954  CA  ILE A 355      18.482  -9.612 -29.764  1.00 24.36           C  
ANISOU 2954  CA  ILE A 355     3546   2892   2818     89    -95    190       C  
ATOM   2955  C   ILE A 355      17.016  -9.371 -29.400  1.00 24.32           C  
ANISOU 2955  C   ILE A 355     3537   2870   2832     77    -86    197       C  
ATOM   2956  O   ILE A 355      16.126  -9.611 -30.212  1.00 25.64           O  
ANISOU 2956  O   ILE A 355     3697   3034   3010     65    -93    208       O  
ATOM   2957  CB  ILE A 355      18.916 -11.050 -29.328  1.00 24.64           C  
ANISOU 2957  CB  ILE A 355     3605   2923   2837    103    -93    184       C  
ATOM   2958  CG1 ILE A 355      20.398 -11.301 -29.643  1.00 25.52           C  
ANISOU 2958  CG1 ILE A 355     3709   3045   2943    120    -94    187       C  
ATOM   2959  CG2 ILE A 355      18.036 -12.127 -30.003  1.00 20.74           C  
ANISOU 2959  CG2 ILE A 355     3129   2417   2335     95    -91    184       C  
ATOM   2960  CD1 ILE A 355      20.778 -11.107 -31.119  1.00 27.72           C  
ANISOU 2960  CD1 ILE A 355     3982   3331   3221    121    -85    190       C  
ATOM   2961  N   GLN A 356      16.766  -8.878 -28.191  1.00 24.20           N  
ANISOU 2961  N   GLN A 356     3531   2841   2822     80    -71    195       N  
ATOM   2962  CA  GLN A 356      15.398  -8.624 -27.763  1.00 23.33           C  
ANISOU 2962  CA  GLN A 356     3416   2709   2740     74    -47    206       C  
ATOM   2963  C   GLN A 356      14.713  -7.521 -28.586  1.00 23.13           C  
ANISOU 2963  C   GLN A 356     3357   2684   2749     66    -46    225       C  
ATOM   2964  O   GLN A 356      13.499  -7.383 -28.532  1.00 23.73           O  
ANISOU 2964  O   GLN A 356     3413   2742   2862     62    -29    246       O  
ATOM   2965  CB  GLN A 356      15.321  -8.339 -26.251  1.00 23.97           C  
ANISOU 2965  CB  GLN A 356     3529   2765   2812     80    -18    198       C  
ATOM   2966  CG  GLN A 356      15.967  -7.022 -25.773  1.00 22.63           C  
ANISOU 2966  CG  GLN A 356     3375   2592   2633     77    -14    192       C  
ATOM   2967  CD  GLN A 356      17.443  -7.173 -25.410  1.00 27.73           C  
ANISOU 2967  CD  GLN A 356     4040   3252   3243     75    -46    180       C  
ATOM   2968  OE1 GLN A 356      18.155  -8.029 -25.959  1.00 24.38           O  
ANISOU 2968  OE1 GLN A 356     3602   2850   2812     81    -71    180       O  
ATOM   2969  NE2 GLN A 356      17.915  -6.331 -24.483  1.00 22.83           N  
ANISOU 2969  NE2 GLN A 356     3456   2615   2603     65    -45    174       N  
ATOM   2970  N   SER A 357      15.479  -6.749 -29.359  1.00 22.10           N  
ANISOU 2970  N   SER A 357     3214   2571   2611     63    -63    223       N  
ATOM   2971  CA  SER A 357      14.865  -5.709 -30.194  1.00 20.99           C  
ANISOU 2971  CA  SER A 357     3044   2431   2502     55    -65    244       C  
ATOM   2972  C   SER A 357      14.188  -6.261 -31.462  1.00 20.98           C  
ANISOU 2972  C   SER A 357     3026   2436   2512     38    -95    263       C  
ATOM   2973  O   SER A 357      13.612  -5.482 -32.235  1.00 19.92           O  
ANISOU 2973  O   SER A 357     2865   2299   2404     27   -106    287       O  
ATOM   2974  CB  SER A 357      15.869  -4.621 -30.576  1.00 20.61           C  
ANISOU 2974  CB  SER A 357     2992   2396   2442     55    -72    237       C  
ATOM   2975  OG  SER A 357      16.422  -3.995 -29.437  1.00 21.90           O  
ANISOU 2975  OG  SER A 357     3177   2549   2595     61    -54    223       O  
ATOM   2976  N   VAL A 358      14.239  -7.582 -31.674  1.00 19.98           N  
ANISOU 2976  N   VAL A 358     2919   2311   2362     33   -109    256       N  
ATOM   2977  CA  VAL A 358      13.522  -8.210 -32.813  1.00 22.05           C  
ANISOU 2977  CA  VAL A 358     3182   2572   2626      8   -142    275       C  
ATOM   2978  C   VAL A 358      12.012  -8.007 -32.722  1.00 21.45           C  
ANISOU 2978  C   VAL A 358     3068   2478   2605     -7   -148    312       C  
ATOM   2979  O   VAL A 358      11.324  -8.056 -33.735  1.00 24.27           O  
ANISOU 2979  O   VAL A 358     3414   2832   2976    -35   -186    340       O  
ATOM   2980  CB  VAL A 358      13.812  -9.734 -32.992  1.00 22.37           C  
ANISOU 2980  CB  VAL A 358     3263   2610   2628      3   -152    259       C  
ATOM   2981  CG1 VAL A 358      15.272  -9.975 -33.349  1.00 22.19           C  
ANISOU 2981  CG1 VAL A 358     3270   2600   2562     19   -143    233       C  
ATOM   2982  CG2 VAL A 358      13.380 -10.548 -31.734  1.00 20.61           C  
ANISOU 2982  CG2 VAL A 358     3042   2373   2414     14   -131    254       C  
ATOM   2983  N   PHE A 359      11.507  -7.794 -31.507  1.00 21.21           N  
ANISOU 2983  N   PHE A 359     3022   2432   2607     10   -109    316       N  
ATOM   2984  CA  PHE A 359      10.091  -7.506 -31.284  1.00 21.97           C  
ANISOU 2984  CA  PHE A 359     3072   2505   2770      4    -98    358       C  
ATOM   2985  C   PHE A 359       9.674  -6.162 -31.883  1.00 22.96           C  
ANISOU 2985  C   PHE A 359     3156   2627   2938      1   -102    390       C  
ATOM   2986  O   PHE A 359       8.481  -5.903 -32.062  1.00 22.47           O  
ANISOU 2986  O   PHE A 359     3046   2549   2943     -8   -106    438       O  
ATOM   2987  CB  PHE A 359       9.766  -7.508 -29.786  1.00 23.72           C  
ANISOU 2987  CB  PHE A 359     3298   2703   3010     28    -38    352       C  
ATOM   2988  CG  PHE A 359       9.784  -8.879 -29.161  1.00 25.06           C  
ANISOU 2988  CG  PHE A 359     3499   2868   3155     27    -33    335       C  
ATOM   2989  CD1 PHE A 359       8.871  -9.856 -29.565  1.00 21.31           C  
ANISOU 2989  CD1 PHE A 359     3006   2386   2704      4    -59    362       C  
ATOM   2990  CD2 PHE A 359      10.712  -9.193 -28.164  1.00 23.29           C  
ANISOU 2990  CD2 PHE A 359     3322   2645   2882     46     -9    297       C  
ATOM   2991  CE1 PHE A 359       8.875 -11.127 -28.990  1.00 19.75           C  
ANISOU 2991  CE1 PHE A 359     2840   2183   2484      3    -53    346       C  
ATOM   2992  CE2 PHE A 359      10.728 -10.469 -27.579  1.00 21.01           C  
ANISOU 2992  CE2 PHE A 359     3063   2351   2571     46     -5    284       C  
ATOM   2993  CZ  PHE A 359       9.810 -11.438 -27.996  1.00 19.44           C  
ANISOU 2993  CZ  PHE A 359     2847   2143   2395     27    -24    307       C  
ATOM   2994  N   SER A 360      10.662  -5.324 -32.201  1.00 21.37           N  
ANISOU 2994  N   SER A 360     2971   2442   2706      9   -103    368       N  
ATOM   2995  CA  SER A 360      10.418  -3.974 -32.686  1.00 20.00           C  
ANISOU 2995  CA  SER A 360     2767   2265   2568     10   -102    393       C  
ATOM   2996  C   SER A 360      10.996  -3.769 -34.096  1.00 22.04           C  
ANISOU 2996  C   SER A 360     3035   2545   2793    -11   -153    393       C  
ATOM   2997  O   SER A 360      12.202  -3.521 -34.256  1.00 20.55           O  
ANISOU 2997  O   SER A 360     2877   2374   2557     -4   -150    359       O  
ATOM   2998  CB  SER A 360      11.017  -2.963 -31.710  1.00 18.34           C  
ANISOU 2998  CB  SER A 360     2572   2045   2351     37    -50    369       C  
ATOM   2999  OG  SER A 360      11.138  -1.685 -32.315  1.00 21.47           O  
ANISOU 2999  OG  SER A 360     2951   2443   2765     37    -53    383       O  
ATOM   3000  N   PRO A 361      10.142  -3.881 -35.128  1.00 22.40           N  
ANISOU 3000  N   PRO A 361     3059   2588   2865    -40   -201    434       N  
ATOM   3001  CA  PRO A 361      10.617  -3.667 -36.503  1.00 21.44           C  
ANISOU 3001  CA  PRO A 361     2960   2480   2706    -65   -248    436       C  
ATOM   3002  C   PRO A 361      11.151  -2.250 -36.729  1.00 22.00           C  
ANISOU 3002  C   PRO A 361     3021   2557   2782    -51   -232    435       C  
ATOM   3003  O   PRO A 361      12.043  -2.059 -37.561  1.00 21.64           O  
ANISOU 3003  O   PRO A 361     3008   2525   2688    -60   -247    417       O  
ATOM   3004  CB  PRO A 361       9.370  -3.913 -37.358  1.00 21.21           C  
ANISOU 3004  CB  PRO A 361     2905   2439   2715   -104   -307    492       C  
ATOM   3005  CG  PRO A 361       8.203  -3.723 -36.417  1.00 23.79           C  
ANISOU 3005  CG  PRO A 361     3168   2745   3127    -89   -279    531       C  
ATOM   3006  CD  PRO A 361       8.705  -4.211 -35.080  1.00 23.42           C  
ANISOU 3006  CD  PRO A 361     3141   2697   3060    -56   -217    485       C  
ATOM   3007  N   ILE A 362      10.620  -1.266 -36.004  1.00 24.17           N  
ANISOU 3007  N   ILE A 362     3254   2816   3114    -30   -195    454       N  
ATOM   3008  CA  ILE A 362      11.137   0.108 -36.126  1.00 25.14           C  
ANISOU 3008  CA  ILE A 362     3372   2939   3240    -16   -175    451       C  
ATOM   3009  C   ILE A 362      12.611   0.149 -35.712  1.00 25.19           C  
ANISOU 3009  C   ILE A 362     3423   2963   3187     -3   -151    397       C  
ATOM   3010  O   ILE A 362      13.453   0.685 -36.434  1.00 26.83           O  
ANISOU 3010  O   ILE A 362     3646   3185   3365     -9   -162    386       O  
ATOM   3011  CB  ILE A 362      10.269   1.147 -35.357  1.00 24.59           C  
ANISOU 3011  CB  ILE A 362     3260   2840   3244      7   -129    483       C  
ATOM   3012  CG1 ILE A 362       9.016   1.484 -36.173  1.00 24.70           C  
ANISOU 3012  CG1 ILE A 362     3218   2840   3327     -9   -165    551       C  
ATOM   3013  CG2 ILE A 362      11.055   2.441 -35.063  1.00 26.81           C  
ANISOU 3013  CG2 ILE A 362     3557   3117   3513     25    -92    462       C  
ATOM   3014  CD1 ILE A 362       7.956   2.296 -35.435  1.00 22.21           C  
ANISOU 3014  CD1 ILE A 362     2850   2488   3102     18   -111    595       C  
ATOM   3015  N   LYS A 363      12.919  -0.445 -34.564  1.00 25.75           N  
ANISOU 3015  N   LYS A 363     3510   3030   3243     13   -119    368       N  
ATOM   3016  CA  LYS A 363      14.293  -0.527 -34.085  1.00 26.31           C  
ANISOU 3016  CA  LYS A 363     3616   3115   3264     23   -105    326       C  
ATOM   3017  C   LYS A 363      15.156  -1.328 -35.059  1.00 24.95           C  
ANISOU 3017  C   LYS A 363     3467   2967   3045     11   -136    311       C  
ATOM   3018  O   LYS A 363      16.293  -0.950 -35.344  1.00 23.49           O  
ANISOU 3018  O   LYS A 363     3295   2796   2834     13   -133    294       O  
ATOM   3019  CB  LYS A 363      14.347  -1.151 -32.675  1.00 26.24           C  
ANISOU 3019  CB  LYS A 363     3627   3096   3248     37    -75    304       C  
ATOM   3020  CG  LYS A 363      15.759  -1.295 -32.092  1.00 25.09           C  
ANISOU 3020  CG  LYS A 363     3512   2964   3057     43    -72    269       C  
ATOM   3021  CD  LYS A 363      16.516   0.036 -31.981  1.00 27.57           C  
ANISOU 3021  CD  LYS A 363     3830   3276   3367     42    -63    263       C  
ATOM   3022  CE  LYS A 363      15.938   0.949 -30.916  1.00 31.32           C  
ANISOU 3022  CE  LYS A 363     4318   3717   3863     49    -24    266       C  
ATOM   3023  NZ  LYS A 363      16.874   2.076 -30.574  1.00 30.85           N  
ANISOU 3023  NZ  LYS A 363     4282   3654   3786     42    -20    253       N  
ATOM   3024  N   THR A 364      14.601  -2.433 -35.556  1.00 23.09           N  
ANISOU 3024  N   THR A 364     3239   2731   2802     -3   -160    319       N  
ATOM   3025  CA  THR A 364      15.296  -3.303 -36.494  1.00 23.25           C  
ANISOU 3025  CA  THR A 364     3297   2763   2775    -14   -180    306       C  
ATOM   3026  C   THR A 364      15.662  -2.553 -37.777  1.00 23.04           C  
ANISOU 3026  C   THR A 364     3279   2741   2732    -29   -197    316       C  
ATOM   3027  O   THR A 364      16.808  -2.581 -38.206  1.00 24.09           O  
ANISOU 3027  O   THR A 364     3436   2885   2832    -23   -183    297       O  
ATOM   3028  CB  THR A 364      14.474  -4.590 -36.798  1.00 24.31           C  
ANISOU 3028  CB  THR A 364     3448   2887   2901    -33   -205    316       C  
ATOM   3029  OG1 THR A 364      14.196  -5.283 -35.573  1.00 25.04           O  
ANISOU 3029  OG1 THR A 364     3533   2974   3007    -18   -185    305       O  
ATOM   3030  CG2 THR A 364      15.242  -5.533 -37.717  1.00 24.52           C  
ANISOU 3030  CG2 THR A 364     3529   2917   2871    -43   -214    298       C  
ATOM   3031  N   TRP A 365      14.699  -1.860 -38.373  1.00 23.27           N  
ANISOU 3031  N   TRP A 365     3288   2762   2791    -47   -224    351       N  
ATOM   3032  CA  TRP A 365      14.973  -1.117 -39.598  1.00 21.77           C  
ANISOU 3032  CA  TRP A 365     3113   2575   2584    -65   -243    364       C  
ATOM   3033  C   TRP A 365      15.814   0.128 -39.373  1.00 23.09           C  
ANISOU 3033  C   TRP A 365     3263   2750   2759    -46   -214    353       C  
ATOM   3034  O   TRP A 365      16.567   0.541 -40.267  1.00 20.68           O  
ANISOU 3034  O   TRP A 365     2981   2451   2425    -53   -214    350       O  
ATOM   3035  CB  TRP A 365      13.693  -0.793 -40.356  1.00 21.38           C  
ANISOU 3035  CB  TRP A 365     3046   2512   2565    -94   -292    412       C  
ATOM   3036  CG  TRP A 365      13.157  -1.987 -41.093  1.00 23.63           C  
ANISOU 3036  CG  TRP A 365     3371   2788   2820   -129   -337    423       C  
ATOM   3037  CD1 TRP A 365      12.010  -2.678 -40.813  1.00 21.97           C  
ANISOU 3037  CD1 TRP A 365     3139   2565   2642   -146   -367    450       C  
ATOM   3038  CD2 TRP A 365      13.758  -2.642 -42.219  1.00 22.24           C  
ANISOU 3038  CD2 TRP A 365     3269   2607   2573   -154   -353    409       C  
ATOM   3039  NE1 TRP A 365      11.853  -3.706 -41.708  1.00 24.19           N  
ANISOU 3039  NE1 TRP A 365     3480   2837   2874   -185   -411    453       N  
ATOM   3040  CE2 TRP A 365      12.913  -3.714 -42.576  1.00 21.26           C  
ANISOU 3040  CE2 TRP A 365     3174   2468   2436   -189   -399    426       C  
ATOM   3041  CE3 TRP A 365      14.929  -2.421 -42.966  1.00 22.87           C  
ANISOU 3041  CE3 TRP A 365     3399   2691   2600   -150   -328    385       C  
ATOM   3042  CZ2 TRP A 365      13.194  -4.570 -43.653  1.00 22.84           C  
ANISOU 3042  CZ2 TRP A 365     3464   2653   2564   -224   -422    417       C  
ATOM   3043  CZ3 TRP A 365      15.217  -3.273 -44.029  1.00 22.66           C  
ANISOU 3043  CZ3 TRP A 365     3455   2647   2505   -177   -341    377       C  
ATOM   3044  CH2 TRP A 365      14.349  -4.336 -44.364  1.00 25.57           C  
ANISOU 3044  CH2 TRP A 365     3865   2998   2854   -215   -388    391       C  
ATOM   3045  N   ASP A 366      15.712   0.720 -38.183  1.00 21.98           N  
ANISOU 3045  N   ASP A 366     3092   2607   2654    -25   -185    348       N  
ATOM   3046  CA  ASP A 366      16.548   1.871 -37.880  1.00 23.09           C  
ANISOU 3046  CA  ASP A 366     3225   2751   2798    -14   -161    337       C  
ATOM   3047  C   ASP A 366      18.023   1.476 -37.917  1.00 23.90           C  
ANISOU 3047  C   ASP A 366     3350   2870   2861     -7   -147    308       C  
ATOM   3048  O   ASP A 366      18.842   2.200 -38.475  1.00 25.00           O  
ANISOU 3048  O   ASP A 366     3492   3016   2990    -10   -141    307       O  
ATOM   3049  CB  ASP A 366      16.187   2.499 -36.532  1.00 25.18           C  
ANISOU 3049  CB  ASP A 366     3471   2999   3097      3   -130    335       C  
ATOM   3050  CG  ASP A 366      16.762   3.888 -36.370  1.00 26.94           C  
ANISOU 3050  CG  ASP A 366     3692   3217   3327      7   -112    332       C  
ATOM   3051  OD1 ASP A 366      16.787   4.649 -37.357  1.00 27.21           O  
ANISOU 3051  OD1 ASP A 366     3720   3253   3364     -3   -125    349       O  
ATOM   3052  OD2 ASP A 366      17.204   4.222 -35.257  1.00 29.31           O  
ANISOU 3052  OD2 ASP A 366     4004   3509   3625     15    -87    313       O  
ATOM   3053  N   ALA A 367      18.345   0.310 -37.357  1.00 23.65           N  
ANISOU 3053  N   ALA A 367     3331   2843   2812      2   -141    289       N  
ATOM   3054  CA  ALA A 367      19.727  -0.173 -37.306  1.00 23.24           C  
ANISOU 3054  CA  ALA A 367     3290   2804   2735     12   -125    270       C  
ATOM   3055  C   ALA A 367      20.259  -0.697 -38.642  1.00 23.89           C  
ANISOU 3055  C   ALA A 367     3402   2890   2787      6   -122    271       C  
ATOM   3056  O   ALA A 367      21.434  -0.503 -38.959  1.00 26.41           O  
ANISOU 3056  O   ALA A 367     3720   3215   3098     14   -101    267       O  
ATOM   3057  CB  ALA A 367      19.870  -1.232 -36.244  1.00 23.06           C  
ANISOU 3057  CB  ALA A 367     3272   2781   2709     25   -119    254       C  
ATOM   3058  N   ILE A 368      19.414  -1.391 -39.402  1.00 24.97           N  
ANISOU 3058  N   ILE A 368     3568   3016   2905     -9   -141    279       N  
ATOM   3059  CA  ILE A 368      19.778  -1.831 -40.751  1.00 23.35           C  
ANISOU 3059  CA  ILE A 368     3411   2803   2659    -22   -138    281       C  
ATOM   3060  C   ILE A 368      20.141  -0.613 -41.622  1.00 24.85           C  
ANISOU 3060  C   ILE A 368     3601   2995   2847    -32   -135    293       C  
ATOM   3061  O   ILE A 368      21.219  -0.554 -42.207  1.00 24.78           O  
ANISOU 3061  O   ILE A 368     3610   2986   2820    -24   -102    288       O  
ATOM   3062  CB  ILE A 368      18.640  -2.659 -41.405  1.00 23.02           C  
ANISOU 3062  CB  ILE A 368     3409   2744   2593    -49   -173    292       C  
ATOM   3063  CG1 ILE A 368      18.453  -3.988 -40.651  1.00 22.84           C  
ANISOU 3063  CG1 ILE A 368     3394   2718   2565    -40   -169    277       C  
ATOM   3064  CG2 ILE A 368      18.935  -2.911 -42.896  1.00 21.37           C  
ANISOU 3064  CG2 ILE A 368     3269   2519   2330    -72   -172    295       C  
ATOM   3065  CD1 ILE A 368      17.149  -4.733 -40.954  1.00 22.71           C  
ANISOU 3065  CD1 ILE A 368     3401   2686   2541    -71   -212    293       C  
ATOM   3066  N   ILE A 369      19.246   0.369 -41.672  1.00 24.03           N  
ANISOU 3066  N   ILE A 369     3474   2889   2768    -46   -164    314       N  
ATOM   3067  CA  ILE A 369      19.451   1.553 -42.501  1.00 22.89           C  
ANISOU 3067  CA  ILE A 369     3330   2743   2623    -57   -166    329       C  
ATOM   3068  C   ILE A 369      20.686   2.354 -42.047  1.00 23.83           C  
ANISOU 3068  C   ILE A 369     3422   2874   2757    -38   -130    317       C  
ATOM   3069  O   ILE A 369      21.476   2.813 -42.879  1.00 20.67           O  
ANISOU 3069  O   ILE A 369     3039   2474   2341    -42   -111    320       O  
ATOM   3070  CB  ILE A 369      18.154   2.411 -42.590  1.00 21.84           C  
ANISOU 3070  CB  ILE A 369     3172   2602   2523    -74   -205    360       C  
ATOM   3071  CG1 ILE A 369      17.066   1.614 -43.320  1.00 21.41           C  
ANISOU 3071  CG1 ILE A 369     3149   2535   2452   -103   -252    382       C  
ATOM   3072  CG2 ILE A 369      18.413   3.738 -43.317  1.00 18.09           C  
ANISOU 3072  CG2 ILE A 369     2695   2125   2052    -82   -205    376       C  
ATOM   3073  CD1 ILE A 369      15.645   2.105 -43.106  1.00 23.74           C  
ANISOU 3073  CD1 ILE A 369     3400   2820   2799   -114   -292    421       C  
ATOM   3074  N   PHE A 370      20.874   2.471 -40.733  1.00 25.10           N  
ANISOU 3074  N   PHE A 370     3547   3043   2948    -22   -122    305       N  
ATOM   3075  CA  PHE A 370      22.050   3.157 -40.191  1.00 23.64           C  
ANISOU 3075  CA  PHE A 370     3337   2868   2779    -12    -99    298       C  
ATOM   3076  C   PHE A 370      23.358   2.481 -40.589  1.00 23.82           C  
ANISOU 3076  C   PHE A 370     3367   2896   2786     -1    -70    292       C  
ATOM   3077  O   PHE A 370      24.282   3.168 -41.024  1.00 26.47           O  
ANISOU 3077  O   PHE A 370     3693   3235   3128     -2    -51    300       O  
ATOM   3078  CB  PHE A 370      21.959   3.332 -38.668  1.00 23.14           C  
ANISOU 3078  CB  PHE A 370     3248   2805   2739     -4   -103    288       C  
ATOM   3079  CG  PHE A 370      23.298   3.574 -37.994  1.00 20.98           C  
ANISOU 3079  CG  PHE A 370     2956   2540   2475      0    -92    282       C  
ATOM   3080  CD1 PHE A 370      23.811   2.642 -37.099  1.00 26.06           C  
ANISOU 3080  CD1 PHE A 370     3595   3189   3119     11    -92    273       C  
ATOM   3081  CD2 PHE A 370      24.031   4.727 -38.251  1.00 21.65           C  
ANISOU 3081  CD2 PHE A 370     3029   2627   2572    -10    -87    291       C  
ATOM   3082  CE1 PHE A 370      25.040   2.848 -36.474  1.00 29.24           C  
ANISOU 3082  CE1 PHE A 370     3976   3598   3537      9    -94    277       C  
ATOM   3083  CE2 PHE A 370      25.260   4.947 -37.634  1.00 27.44           C  
ANISOU 3083  CE2 PHE A 370     3739   3366   3319    -13    -87    293       C  
ATOM   3084  CZ  PHE A 370      25.769   4.006 -36.742  1.00 27.51           C  
ANISOU 3084  CZ  PHE A 370     3740   3381   3332     -5    -93    288       C  
ATOM   3085  N   ASN A 371      23.442   1.156 -40.440  1.00 22.87           N  
ANISOU 3085  N   ASN A 371     3263   2775   2651     11    -61    283       N  
ATOM   3086  CA  ASN A 371      24.648   0.407 -40.859  1.00 24.66           C  
ANISOU 3086  CA  ASN A 371     3498   3000   2870     28    -22    283       C  
ATOM   3087  C   ASN A 371      24.930   0.488 -42.363  1.00 25.66           C  
ANISOU 3087  C   ASN A 371     3669   3114   2967     21      7    290       C  
ATOM   3088  O   ASN A 371      26.089   0.596 -42.779  1.00 26.14           O  
ANISOU 3088  O   ASN A 371     3721   3172   3037     33     50    299       O  
ATOM   3089  CB  ASN A 371      24.602  -1.055 -40.397  1.00 22.34           C  
ANISOU 3089  CB  ASN A 371     3218   2702   2566     44    -15    272       C  
ATOM   3090  CG  ASN A 371      24.985  -1.211 -38.930  1.00 27.25           C  
ANISOU 3090  CG  ASN A 371     3797   3336   3220     56    -27    268       C  
ATOM   3091  OD1 ASN A 371      26.164  -1.280 -38.596  1.00 29.83           O  
ANISOU 3091  OD1 ASN A 371     4093   3669   3571     70    -10    279       O  
ATOM   3092  ND2 ASN A 371      23.989  -1.264 -38.051  1.00 24.51           N  
ANISOU 3092  ND2 ASN A 371     3449   2990   2874     49    -58    259       N  
ATOM   3093  N   SER A 372      23.871   0.448 -43.167  1.00 24.77           N  
ANISOU 3093  N   SER A 372     3602   2988   2819     -1    -17    291       N  
ATOM   3094  CA  SER A 372      23.994   0.578 -44.613  1.00 25.81           C  
ANISOU 3094  CA  SER A 372     3793   3101   2911    -16      2    299       C  
ATOM   3095  C   SER A 372      24.521   1.963 -44.987  1.00 27.96           C  
ANISOU 3095  C   SER A 372     4042   3380   3201    -21     12    313       C  
ATOM   3096  O   SER A 372      25.426   2.087 -45.811  1.00 28.19           O  
ANISOU 3096  O   SER A 372     4095   3398   3218    -17     59    319       O  
ATOM   3097  CB  SER A 372      22.639   0.331 -45.281  1.00 27.42           C  
ANISOU 3097  CB  SER A 372     4050   3291   3078    -48    -46    305       C  
ATOM   3098  OG  SER A 372      22.737   0.391 -46.697  1.00 27.56           O  
ANISOU 3098  OG  SER A 372     4142   3285   3044    -70    -33    313       O  
ATOM   3099  N   LEU A 373      23.963   3.002 -44.365  1.00 29.38           N  
ANISOU 3099  N   LEU A 373     4177   3573   3412    -30    -26    319       N  
ATOM   3100  CA  LEU A 373      24.370   4.382 -44.650  1.00 29.46           C  
ANISOU 3100  CA  LEU A 373     4167   3587   3441    -38    -20    331       C  
ATOM   3101  C   LEU A 373      25.782   4.694 -44.141  1.00 30.32           C  
ANISOU 3101  C   LEU A 373     4231   3707   3584    -21     16    332       C  
ATOM   3102  O   LEU A 373      26.559   5.357 -44.832  1.00 29.35           O  
ANISOU 3102  O   LEU A 373     4109   3580   3464    -24     46    344       O  
ATOM   3103  CB  LEU A 373      23.350   5.377 -44.081  1.00 27.45           C  
ANISOU 3103  CB  LEU A 373     3882   3336   3212    -49    -64    339       C  
ATOM   3104  CG  LEU A 373      22.010   5.465 -44.816  1.00 27.93           C  
ANISOU 3104  CG  LEU A 373     3974   3383   3255    -71   -105    356       C  
ATOM   3105  CD1 LEU A 373      21.045   6.374 -44.080  1.00 26.90           C  
ANISOU 3105  CD1 LEU A 373     3802   3252   3166    -72   -135    368       C  
ATOM   3106  CD2 LEU A 373      22.175   5.925 -46.276  1.00 25.58           C  
ANISOU 3106  CD2 LEU A 373     3726   3072   2921    -91   -102    372       C  
ATOM   3107  N   LYS A 374      26.105   4.205 -42.943  1.00 31.32           N  
ANISOU 3107  N   LYS A 374     4318   3845   3738     -6     12    324       N  
ATOM   3108  CA  LYS A 374      27.440   4.363 -42.351  1.00 32.37           C  
ANISOU 3108  CA  LYS A 374     4402   3987   3909      5     33    332       C  
ATOM   3109  C   LYS A 374      28.558   3.812 -43.243  1.00 33.58           C  
ANISOU 3109  C   LYS A 374     4564   4132   4064     21     92    346       C  
ATOM   3110  O   LYS A 374      29.642   4.408 -43.334  1.00 33.41           O  
ANISOU 3110  O   LYS A 374     4505   4113   4077     22    117    366       O  
ATOM   3111  CB  LYS A 374      27.500   3.713 -40.966  1.00 32.01           C  
ANISOU 3111  CB  LYS A 374     4326   3951   3884     14     11    324       C  
ATOM   3112  CG  LYS A 374      28.815   3.950 -40.227  1.00 32.48           C  
ANISOU 3112  CG  LYS A 374     4333   4021   3989     17     13    341       C  
ATOM   3113  CD  LYS A 374      28.717   3.545 -38.768  1.00 32.05           C  
ANISOU 3113  CD  LYS A 374     4259   3972   3946     16    -24    334       C  
ATOM   3114  CE  LYS A 374      30.047   3.023 -38.267  1.00 32.69           C  
ANISOU 3114  CE  LYS A 374     4294   4060   4069     26    -18    358       C  
ATOM   3115  NZ  LYS A 374      30.280   1.635 -38.748  1.00 36.69           N  
ANISOU 3115  NZ  LYS A 374     4809   4561   4572     57     23    360       N  
ATOM   3116  N   GLU A 375      28.285   2.687 -43.899  1.00 33.27           N  
ANISOU 3116  N   GLU A 375     4576   4078   3988     32    119    337       N  
ATOM   3117  CA  GLU A 375      29.217   2.074 -44.851  1.00 37.39           C  
ANISOU 3117  CA  GLU A 375     5125   4578   4502     51    190    349       C  
ATOM   3118  C   GLU A 375      29.680   3.039 -45.947  1.00 35.36           C  
ANISOU 3118  C   GLU A 375     4886   4310   4238     40    225    364       C  
ATOM   3119  O   GLU A 375      30.801   2.927 -46.444  1.00 37.19           O  
ANISOU 3119  O   GLU A 375     5109   4529   4493     58    292    383       O  
ATOM   3120  CB  GLU A 375      28.594   0.823 -45.485  1.00 39.56           C  
ANISOU 3120  CB  GLU A 375     5479   4830   4722     55    207    332       C  
ATOM   3121  CG  GLU A 375      29.046  -0.499 -44.857  1.00 50.32           C  
ANISOU 3121  CG  GLU A 375     6829   6188   6101     86    234    330       C  
ATOM   3122  CD  GLU A 375      30.315  -1.083 -45.506  1.00 58.86           C  
ANISOU 3122  CD  GLU A 375     7920   7244   7200    117    326    348       C  
ATOM   3123  OE1 GLU A 375      30.686  -0.667 -46.633  1.00 60.76           O  
ANISOU 3123  OE1 GLU A 375     8203   7463   7420    114    377    357       O  
ATOM   3124  OE2 GLU A 375      30.939  -1.974 -44.887  1.00 61.12           O  
ANISOU 3124  OE2 GLU A 375     8172   7529   7523    148    352    357       O  
ATOM   3125  N   GLN A 376      28.821   3.986 -46.308  1.00 32.33           N  
ANISOU 3125  N   GLN A 376     4525   3928   3829     12    183    359       N  
ATOM   3126  CA  GLN A 376      29.134   4.954 -47.354  1.00 33.70           C  
ANISOU 3126  CA  GLN A 376     4724   4090   3991     -2    210    373       C  
ATOM   3127  C   GLN A 376      29.521   6.317 -46.773  1.00 32.82           C  
ANISOU 3127  C   GLN A 376     4544   3997   3927    -13    186    386       C  
ATOM   3128  O   GLN A 376      29.538   7.316 -47.492  1.00 32.82           O  
ANISOU 3128  O   GLN A 376     4561   3991   3918    -30    191    397       O  
ATOM   3129  CB  GLN A 376      27.941   5.112 -48.304  1.00 35.42           C  
ANISOU 3129  CB  GLN A 376     5021   4292   4145    -29    177    367       C  
ATOM   3130  CG  GLN A 376      27.411   3.808 -48.906  1.00 38.66           C  
ANISOU 3130  CG  GLN A 376     5513   4678   4496    -31    186    355       C  
ATOM   3131  CD  GLN A 376      25.950   3.909 -49.306  1.00 43.14           C  
ANISOU 3131  CD  GLN A 376     6132   5240   5020    -66    115    353       C  
ATOM   3132  OE1 GLN A 376      25.090   3.235 -48.735  1.00 46.95           O  
ANISOU 3132  OE1 GLN A 376     6611   5729   5500    -69     71    344       O  
ATOM   3133  NE2 GLN A 376      25.658   4.766 -50.283  1.00 47.30           N  
ANISOU 3133  NE2 GLN A 376     6701   5753   5517    -92    102    368       N  
ATOM   3134  N   ASN A 377      29.831   6.344 -45.475  1.00 32.80           N  
ANISOU 3134  N   ASN A 377     4475   4016   3972     -7    158    386       N  
ATOM   3135  CA  ASN A 377      30.089   7.589 -44.728  1.00 32.31           C  
ANISOU 3135  CA  ASN A 377     4359   3967   3949    -24    125    395       C  
ATOM   3136  C   ASN A 377      28.911   8.574 -44.791  1.00 31.53           C  
ANISOU 3136  C   ASN A 377     4285   3866   3827    -46     80    385       C  
ATOM   3137  O   ASN A 377      29.084   9.798 -44.806  1.00 31.44           O  
ANISOU 3137  O   ASN A 377     4259   3854   3833    -63     71    395       O  
ATOM   3138  CB  ASN A 377      31.413   8.249 -45.165  1.00 33.26           C  
ANISOU 3138  CB  ASN A 377     4445   4085   4109    -26    168    423       C  
ATOM   3139  CG  ASN A 377      32.632   7.357 -44.923  1.00 35.25           C  
ANISOU 3139  CG  ASN A 377     4651   4338   4406     -2    211    444       C  
ATOM   3140  OD1 ASN A 377      32.740   6.677 -43.900  1.00 32.78           O  
ANISOU 3140  OD1 ASN A 377     4304   4035   4115      7    185    442       O  
ATOM   3141  ND2 ASN A 377      33.563   7.370 -45.870  1.00 34.53           N  
ANISOU 3141  ND2 ASN A 377     4557   4230   4332     10    282    468       N  
ATOM   3142  N   LYS A 378      27.702   8.029 -44.830  1.00 30.95           N  
ANISOU 3142  N   LYS A 378     4249   3790   3722    -46     53    371       N  
ATOM   3143  CA  LYS A 378      26.514   8.860 -44.786  1.00 30.80           C  
ANISOU 3143  CA  LYS A 378     4242   3766   3694    -61     11    370       C  
ATOM   3144  C   LYS A 378      25.983   8.957 -43.365  1.00 30.70           C  
ANISOU 3144  C   LYS A 378     4198   3760   3708    -59    -22    358       C  
ATOM   3145  O   LYS A 378      26.197   8.061 -42.551  1.00 30.77           O  
ANISOU 3145  O   LYS A 378     4192   3777   3723    -47    -23    347       O  
ATOM   3146  CB  LYS A 378      25.454   8.360 -45.764  1.00 32.87           C  
ANISOU 3146  CB  LYS A 378     4560   4016   3914    -69     -3    372       C  
ATOM   3147  CG  LYS A 378      25.819   8.630 -47.217  1.00 32.82           C  
ANISOU 3147  CG  LYS A 378     4604   3994   3873    -80     24    386       C  
ATOM   3148  CD  LYS A 378      24.719   8.170 -48.168  1.00 37.74           C  
ANISOU 3148  CD  LYS A 378     5292   4601   4447    -98     -6    392       C  
ATOM   3149  CE  LYS A 378      25.156   8.322 -49.627  1.00 40.27           C  
ANISOU 3149  CE  LYS A 378     5682   4899   4720   -113     26    403       C  
ATOM   3150  NZ  LYS A 378      24.011   8.121 -50.563  1.00 45.96           N  
ANISOU 3150  NZ  LYS A 378     6472   5600   5390   -143    -22    416       N  
ATOM   3151  N   VAL A 379      25.304  10.064 -43.079  1.00 29.70           N  
ANISOU 3151  N   VAL A 379     4067   3625   3593    -70    -44    363       N  
ATOM   3152  CA  VAL A 379      24.883  10.404 -41.727  1.00 28.32           C  
ANISOU 3152  CA  VAL A 379     3874   3447   3440    -69    -62    353       C  
ATOM   3153  C   VAL A 379      23.354  10.436 -41.636  1.00 27.99           C  
ANISOU 3153  C   VAL A 379     3844   3392   3400    -65    -81    357       C  
ATOM   3154  O   VAL A 379      22.695  11.113 -42.431  1.00 29.41           O  
ANISOU 3154  O   VAL A 379     4033   3560   3580    -71    -89    375       O  
ATOM   3155  CB  VAL A 379      25.477  11.773 -41.316  1.00 29.44           C  
ANISOU 3155  CB  VAL A 379     4003   3580   3603    -85    -60    358       C  
ATOM   3156  CG1 VAL A 379      24.974  12.198 -39.959  1.00 28.33           C  
ANISOU 3156  CG1 VAL A 379     3864   3424   3474    -88    -73    347       C  
ATOM   3157  CG2 VAL A 379      27.008  11.719 -41.337  1.00 28.85           C  
ANISOU 3157  CG2 VAL A 379     3904   3517   3539    -93    -47    364       C  
ATOM   3158  N   ILE A 380      22.796   9.717 -40.664  1.00 25.63           N  
ANISOU 3158  N   ILE A 380     3540   3092   3106    -54    -89    345       N  
ATOM   3159  CA  ILE A 380      21.342   9.623 -40.516  1.00 24.19           C  
ANISOU 3159  CA  ILE A 380     3359   2896   2936    -48   -102    355       C  
ATOM   3160  C   ILE A 380      20.752  10.909 -39.943  1.00 24.93           C  
ANISOU 3160  C   ILE A 380     3448   2966   3061    -48    -94    364       C  
ATOM   3161  O   ILE A 380      21.416  11.593 -39.159  1.00 22.31           O  
ANISOU 3161  O   ILE A 380     3120   2626   2732    -52    -80    352       O  
ATOM   3162  CB  ILE A 380      20.905   8.379 -39.664  1.00 24.75           C  
ANISOU 3162  CB  ILE A 380     3429   2970   3005    -36   -106    340       C  
ATOM   3163  CG1 ILE A 380      21.309   8.524 -38.192  1.00 20.52           C  
ANISOU 3163  CG1 ILE A 380     2891   2428   2477    -32    -94    321       C  
ATOM   3164  CG2 ILE A 380      21.458   7.081 -40.277  1.00 25.75           C  
ANISOU 3164  CG2 ILE A 380     3567   3115   3102    -35   -108    332       C  
ATOM   3165  CD1 ILE A 380      21.024   7.274 -37.350  1.00 23.11           C  
ANISOU 3165  CD1 ILE A 380     3222   2759   2798    -21    -96    306       C  
ATOM   3166  N   PRO A 381      19.504  11.245 -40.336  1.00 25.66           N  
ANISOU 3166  N   PRO A 381     3532   3041   3176    -43   -102    391       N  
ATOM   3167  CA  PRO A 381      18.858  12.455 -39.808  1.00 26.61           C  
ANISOU 3167  CA  PRO A 381     3647   3130   3333    -36    -83    405       C  
ATOM   3168  C   PRO A 381      18.395  12.233 -38.379  1.00 27.24           C  
ANISOU 3168  C   PRO A 381     3731   3191   3429    -21    -57    391       C  
ATOM   3169  O   PRO A 381      18.238  11.085 -37.962  1.00 29.90           O  
ANISOU 3169  O   PRO A 381     4066   3540   3756    -16    -64    379       O  
ATOM   3170  CB  PRO A 381      17.644  12.645 -40.732  1.00 25.88           C  
ANISOU 3170  CB  PRO A 381     3537   3028   3270    -34   -103    448       C  
ATOM   3171  CG  PRO A 381      17.311  11.260 -41.209  1.00 27.64           C  
ANISOU 3171  CG  PRO A 381     3758   3270   3474    -40   -135    450       C  
ATOM   3172  CD  PRO A 381      18.617  10.486 -41.242  1.00 24.41           C  
ANISOU 3172  CD  PRO A 381     3370   2887   3016    -47   -131    414       C  
ATOM   3173  N   GLN A 382      18.169  13.315 -37.645  1.00 26.55           N  
ANISOU 3173  N   GLN A 382     3656   3069   3362    -15    -25    393       N  
ATOM   3174  CA  GLN A 382      17.649  13.218 -36.293  1.00 30.26           C  
ANISOU 3174  CA  GLN A 382     4145   3509   3843     -2     10    381       C  
ATOM   3175  C   GLN A 382      16.183  12.821 -36.301  1.00 31.81           C  
ANISOU 3175  C   GLN A 382     4311   3689   4087     21     23    412       C  
ATOM   3176  O   GLN A 382      15.418  13.266 -37.155  1.00 33.54           O  
ANISOU 3176  O   GLN A 382     4499   3901   4345     27     14    452       O  
ATOM   3177  CB  GLN A 382      17.815  14.546 -35.548  1.00 30.97           C  
ANISOU 3177  CB  GLN A 382     4273   3556   3936     -4     49    374       C  
ATOM   3178  CG  GLN A 382      17.424  14.483 -34.068  1.00 31.16           C  
ANISOU 3178  CG  GLN A 382     4341   3541   3959      6     94    357       C  
ATOM   3179  CD  GLN A 382      17.679  15.784 -33.314  1.00 34.62           C  
ANISOU 3179  CD  GLN A 382     4837   3929   4386     -3    134    346       C  
ATOM   3180  OE1 GLN A 382      17.555  16.883 -33.869  1.00 32.59           O  
ANISOU 3180  OE1 GLN A 382     4578   3653   4151     -1    147    364       O  
ATOM   3181  NE2 GLN A 382      18.032  15.660 -32.032  1.00 36.59           N  
ANISOU 3181  NE2 GLN A 382     5150   4154   4600    -16    151    316       N  
ATOM   3182  N   GLY A 383      15.802  11.985 -35.338  1.00 34.02           N  
ANISOU 3182  N   GLY A 383     4600   3961   4367     32     41    399       N  
ATOM   3183  CA  GLY A 383      14.393  11.704 -35.072  1.00 34.51           C  
ANISOU 3183  CA  GLY A 383     4632   3997   4483     55     66    432       C  
ATOM   3184  C   GLY A 383      13.625  12.973 -34.734  1.00 36.57           C  
ANISOU 3184  C   GLY A 383     4894   4205   4795     75    123    460       C  
ATOM   3185  O   GLY A 383      14.086  13.802 -33.945  1.00 35.99           O  
ANISOU 3185  O   GLY A 383     4872   4100   4702     76    164    437       O  
ATOM   3186  N   ARG A 384      12.461  13.130 -35.357  1.00 37.57           N  
ANISOU 3186  N   ARG A 384     4966   4319   4989     91    122    514       N  
ATOM   3187  CA  ARG A 384      11.583  14.264 -35.098  1.00 40.81           C  
ANISOU 3187  CA  ARG A 384     5365   4675   5467    118    182    554       C  
ATOM   3188  C   ARG A 384      10.252  13.838 -34.469  1.00 40.70           C  
ANISOU 3188  C   ARG A 384     5315   4626   5525    148    230    592       C  
ATOM   3189  O   ARG A 384       9.900  12.648 -34.454  1.00 38.34           O  
ANISOU 3189  O   ARG A 384     4988   4351   5228    143    202    596       O  
ATOM   3190  CB  ARG A 384      11.336  15.053 -36.384  1.00 41.91           C  
ANISOU 3190  CB  ARG A 384     5463   4820   5641    114    146    599       C  
ATOM   3191  CG  ARG A 384      12.504  15.910 -36.800  1.00 48.49           C  
ANISOU 3191  CG  ARG A 384     6338   5665   6421     93    131    569       C  
ATOM   3192  CD  ARG A 384      12.345  16.435 -38.221  1.00 56.89           C  
ANISOU 3192  CD  ARG A 384     7365   6744   7507     82     80    612       C  
ATOM   3193  NE  ARG A 384      13.170  17.627 -38.452  1.00 65.67           N  
ANISOU 3193  NE  ARG A 384     8513   7846   8592     73     92    596       N  
ATOM   3194  CZ  ARG A 384      14.480  17.615 -38.710  1.00 67.84           C  
ANISOU 3194  CZ  ARG A 384     8825   8153   8798     45     66    553       C  
ATOM   3195  NH1 ARG A 384      15.153  16.466 -38.777  1.00 67.94           N  
ANISOU 3195  NH1 ARG A 384     8845   8210   8762     27     29    520       N  
ATOM   3196  NH2 ARG A 384      15.123  18.762 -38.902  1.00 68.80           N  
ANISOU 3196  NH2 ARG A 384     8975   8260   8907     36     79    546       N  
ATOM   3197  N   SER A 385       9.534  14.830 -33.947  1.00 39.62           N  
ANISOU 3197  N   SER A 385     5179   4428   5448    180    309    622       N  
ATOM   3198  CA  SER A 385       8.222  14.646 -33.350  1.00 41.47           C  
ANISOU 3198  CA  SER A 385     5373   4616   5767    215    374    670       C  
ATOM   3199  C   SER A 385       7.136  14.864 -34.402  1.00 40.00           C  
ANISOU 3199  C   SER A 385     5089   4430   5681    226    342    755       C  
ATOM   3200  O   SER A 385       7.138  15.883 -35.107  1.00 38.54           O  
ANISOU 3200  O   SER A 385     4888   4234   5520    228    332    784       O  
ATOM   3201  CB  SER A 385       8.040  15.634 -32.187  1.00 43.16           C  
ANISOU 3201  CB  SER A 385     5649   4754   5994    247    490    660       C  
ATOM   3202  OG  SER A 385       6.871  15.350 -31.441  1.00 46.65           O  
ANISOU 3202  OG  SER A 385     6065   5147   6513    284    570    699       O  
ATOM   3203  N   HIS A 386       6.213  13.909 -34.507  1.00 39.30           N  
ANISOU 3203  N   HIS A 386     4933   4349   5648    228    320    798       N  
ATOM   3204  CA  HIS A 386       5.098  14.025 -35.460  1.00 39.06           C  
ANISOU 3204  CA  HIS A 386     4804   4315   5721    232    278    890       C  
ATOM   3205  C   HIS A 386       3.760  13.674 -34.817  1.00 39.66           C  
ANISOU 3205  C   HIS A 386     4813   4347   5907    265    340    953       C  
ATOM   3206  O   HIS A 386       3.676  12.699 -34.059  1.00 39.81           O  
ANISOU 3206  O   HIS A 386     4848   4371   5908    265    362    926       O  
ATOM   3207  CB  HIS A 386       5.303  13.115 -36.676  1.00 38.03           C  
ANISOU 3207  CB  HIS A 386     4646   4249   5554    183    150    897       C  
ATOM   3208  CG  HIS A 386       6.668  13.195 -37.284  1.00 37.76           C  
ANISOU 3208  CG  HIS A 386     4678   4260   5408    150     95    832       C  
ATOM   3209  ND1 HIS A 386       7.048  14.213 -38.132  1.00 39.63           N  
ANISOU 3209  ND1 HIS A 386     4922   4500   5637    141     69    845       N  
ATOM   3210  CD2 HIS A 386       7.735  12.368 -37.185  1.00 35.70           C  
ANISOU 3210  CD2 HIS A 386     4476   4043   5047    124     64    760       C  
ATOM   3211  CE1 HIS A 386       8.295  14.015 -38.521  1.00 39.68           C  
ANISOU 3211  CE1 HIS A 386     4987   4547   5542    112     28    782       C  
ATOM   3212  NE2 HIS A 386       8.736  12.903 -37.958  1.00 37.87           N  
ANISOU 3212  NE2 HIS A 386     4787   4342   5258    103     25    732       N  
ATOM   3213  N   PRO A 387       2.703  14.451 -35.134  1.00 39.90           N  
ANISOU 3213  N   PRO A 387     4766   4335   6060    294    369   1043       N  
ATOM   3214  CA  PRO A 387       1.359  14.062 -34.710  1.00 40.02           C  
ANISOU 3214  CA  PRO A 387     4695   4311   6199    322    417   1122       C  
ATOM   3215  C   PRO A 387       0.841  12.895 -35.549  1.00 39.58           C  
ANISOU 3215  C   PRO A 387     4565   4305   6170    279    298   1167       C  
ATOM   3216  O   PRO A 387       1.065  12.861 -36.763  1.00 38.43           O  
ANISOU 3216  O   PRO A 387     4401   4201   5998    238    183   1185       O  
ATOM   3217  CB  PRO A 387       0.528  15.322 -34.980  1.00 38.65           C  
ANISOU 3217  CB  PRO A 387     4456   4081   6148    363    469   1210       C  
ATOM   3218  CG  PRO A 387       1.231  15.993 -36.107  1.00 39.42           C  
ANISOU 3218  CG  PRO A 387     4571   4213   6192    332    381   1200       C  
ATOM   3219  CD  PRO A 387       2.696  15.730 -35.876  1.00 39.90           C  
ANISOU 3219  CD  PRO A 387     4748   4317   6095    303    361   1083       C  
ATOM   3220  N   VAL A 388       0.170  11.948 -34.897  1.00 39.71           N  
ANISOU 3220  N   VAL A 388     4547   4311   6231    286    327   1185       N  
ATOM   3221  CA  VAL A 388      -0.467  10.834 -35.587  1.00 41.18           C  
ANISOU 3221  CA  VAL A 388     4661   4532   6454    244    221   1238       C  
ATOM   3222  C   VAL A 388      -1.558  11.362 -36.519  1.00 42.89           C  
ANISOU 3222  C   VAL A 388     4761   4730   6805    241    167   1361       C  
ATOM   3223  O   VAL A 388      -2.400  12.161 -36.107  1.00 43.56           O  
ANISOU 3223  O   VAL A 388     4782   4756   7014    291    257   1432       O  
ATOM   3224  CB  VAL A 388      -1.040   9.799 -34.587  1.00 42.02           C  
ANISOU 3224  CB  VAL A 388     4750   4621   6593    257    278   1238       C  
ATOM   3225  CG1 VAL A 388      -1.742   8.650 -35.314  1.00 44.13           C  
ANISOU 3225  CG1 VAL A 388     4942   4921   6903    208    164   1297       C  
ATOM   3226  CG2 VAL A 388       0.073   9.245 -33.696  1.00 40.92           C  
ANISOU 3226  CG2 VAL A 388     4729   4502   6318    256    319   1120       C  
ATOM   3227  N   GLN A 389      -1.502  10.935 -37.779  1.00 42.59           N  
ANISOU 3227  N   GLN A 389     4704   4740   6739    181     22   1386       N  
ATOM   3228  CA  GLN A 389      -2.483  11.303 -38.806  1.00 43.13           C  
ANISOU 3228  CA  GLN A 389     4668   4798   6922    160    -63   1507       C  
ATOM   3229  C   GLN A 389      -2.928  10.069 -39.602  1.00 41.31           C  
ANISOU 3229  C   GLN A 389     4402   4605   6689     90   -203   1547       C  
ATOM   3230  O   GLN A 389      -2.099   9.222 -39.939  1.00 39.36           O  
ANISOU 3230  O   GLN A 389     4240   4406   6311     45   -269   1469       O  
ATOM   3231  CB  GLN A 389      -1.893  12.328 -39.778  1.00 43.32           C  
ANISOU 3231  CB  GLN A 389     4725   4834   6901    147   -115   1504       C  
ATOM   3232  CG  GLN A 389      -1.747  13.742 -39.237  1.00 50.91           C  
ANISOU 3232  CG  GLN A 389     5697   5748   7901    211      5   1500       C  
ATOM   3233  CD  GLN A 389      -1.494  14.759 -40.346  1.00 55.85           C  
ANISOU 3233  CD  GLN A 389     6323   6378   8518    195    -61   1531       C  
ATOM   3234  OE1 GLN A 389      -0.579  14.602 -41.160  1.00 58.63           O  
ANISOU 3234  OE1 GLN A 389     6748   6778   8751    148   -148   1475       O  
ATOM   3235  NE2 GLN A 389      -2.310  15.809 -40.382  1.00 57.95           N  
ANISOU 3235  NE2 GLN A 389     6510   6591   8916    237    -14   1624       N  
ATOM   3236  N   PRO A 390      -4.231   9.971 -39.924  1.00 35.73           N  
ANISOU 3236  N   PRO A 390     5243   3917   4415   -110    669     27       N  
ATOM   3237  CA  PRO A 390      -4.704   8.848 -40.743  1.00 34.49           C  
ANISOU 3237  CA  PRO A 390     5061   3824   4221    -69    590     87       C  
ATOM   3238  C   PRO A 390      -4.268   8.998 -42.205  1.00 33.10           C  
ANISOU 3238  C   PRO A 390     4826   3685   4065    -16    525    171       C  
ATOM   3239  O   PRO A 390      -4.020  10.116 -42.665  1.00 33.70           O  
ANISOU 3239  O   PRO A 390     4862   3722   4221      2    556    201       O  
ATOM   3240  CB  PRO A 390      -6.235   8.948 -40.637  1.00 36.56           C  
ANISOU 3240  CB  PRO A 390     5279   4042   4572    -54    656     97       C  
ATOM   3241  CG  PRO A 390      -6.515   9.979 -39.550  1.00 38.80           C  
ANISOU 3241  CG  PRO A 390     5579   4237   4927    -97    776     25       C  
ATOM   3242  CD  PRO A 390      -5.331  10.893 -39.582  1.00 37.93           C  
ANISOU 3242  CD  PRO A 390     5480   4109   4820   -110    782     12       C  
ATOM   3243  N   TYR A 391      -4.160   7.879 -42.915  1.00 29.96           N  
ANISOU 3243  N   TYR A 391     4427   3362   3596      3    439    207       N  
ATOM   3244  CA  TYR A 391      -3.839   7.888 -44.346  1.00 29.17           C  
ANISOU 3244  CA  TYR A 391     4276   3306   3501     41    380    284       C  
ATOM   3245  C   TYR A 391      -4.487   6.665 -45.019  1.00 29.37           C  
ANISOU 3245  C   TYR A 391     4285   3397   3478     57    319    320       C  
ATOM   3246  O   TYR A 391      -4.789   5.685 -44.329  1.00 27.63           O  
ANISOU 3246  O   TYR A 391     4104   3191   3201     38    310    277       O  
ATOM   3247  CB  TYR A 391      -2.316   7.951 -44.580  1.00 28.31           C  
ANISOU 3247  CB  TYR A 391     4195   3225   3335     30    337    269       C  
ATOM   3248  CG  TYR A 391      -1.547   6.676 -44.268  1.00 26.72           C  
ANISOU 3248  CG  TYR A 391     4047   3078   3026      8    272    230       C  
ATOM   3249  CD1 TYR A 391      -1.105   6.403 -42.977  1.00 29.19           C  
ANISOU 3249  CD1 TYR A 391     4424   3375   3292    -35    280    161       C  
ATOM   3250  CD2 TYR A 391      -1.249   5.756 -45.273  1.00 25.69           C  
ANISOU 3250  CD2 TYR A 391     3900   3013   2847     24    203    263       C  
ATOM   3251  CE1 TYR A 391      -0.394   5.239 -42.690  1.00 28.51           C  
ANISOU 3251  CE1 TYR A 391     4378   3333   3122    -53    215    138       C  
ATOM   3252  CE2 TYR A 391      -0.542   4.594 -44.997  1.00 25.28           C  
ANISOU 3252  CE2 TYR A 391     3888   2999   2719      7    150    229       C  
ATOM   3253  CZ  TYR A 391      -0.118   4.342 -43.704  1.00 26.93           C  
ANISOU 3253  CZ  TYR A 391     4154   3186   2891    -28    152    172       C  
ATOM   3254  OH  TYR A 391       0.576   3.184 -43.425  1.00 28.00           O  
ANISOU 3254  OH  TYR A 391     4320   3354   2964    -44     93    150       O  
ATOM   3255  N   PRO A 392      -4.714   6.720 -46.354  1.00 27.29           N  
ANISOU 3255  N   PRO A 392     3963   3171   3233     85    279    398       N  
ATOM   3256  CA  PRO A 392      -5.470   5.656 -47.038  1.00 26.38           C  
ANISOU 3256  CA  PRO A 392     3826   3117   3080     93    230    433       C  
ATOM   3257  C   PRO A 392      -4.669   4.398 -47.361  1.00 24.70           C  
ANISOU 3257  C   PRO A 392     3651   2974   2758     79    165    407       C  
ATOM   3258  O   PRO A 392      -3.460   4.470 -47.587  1.00 23.77           O  
ANISOU 3258  O   PRO A 392     3554   2872   2605     71    142    392       O  
ATOM   3259  CB  PRO A 392      -5.933   6.330 -48.332  1.00 26.13           C  
ANISOU 3259  CB  PRO A 392     3720   3101   3107    116    212    531       C  
ATOM   3260  CG  PRO A 392      -4.904   7.361 -48.606  1.00 27.06           C  
ANISOU 3260  CG  PRO A 392     3837   3196   3250    118    223    543       C  
ATOM   3261  CD  PRO A 392      -4.366   7.821 -47.272  1.00 27.74           C  
ANISOU 3261  CD  PRO A 392     3972   3216   3350    103    282    462       C  
ATOM   3262  N   GLY A 393      -5.368   3.264 -47.401  1.00 24.53           N  
ANISOU 3262  N   GLY A 393     3634   2991   2697     75    139    401       N  
ATOM   3263  CA  GLY A 393      -4.757   1.961 -47.625  1.00 23.56           C  
ANISOU 3263  CA  GLY A 393     3542   2923   2486     60     87    371       C  
ATOM   3264  C   GLY A 393      -5.151   1.327 -48.948  1.00 25.73           C  
ANISOU 3264  C   GLY A 393     3777   3267   2731     60     44    418       C  
ATOM   3265  O   GLY A 393      -5.188   1.989 -49.988  1.00 24.90           O  
ANISOU 3265  O   GLY A 393     3628   3185   2647     65     32    478       O  
ATOM   3266  N   ALA A 394      -5.455   0.036 -48.900  1.00 23.47           N  
ANISOU 3266  N   ALA A 394     3508   3017   2394     49     20    391       N  
ATOM   3267  CA  ALA A 394      -5.696  -0.752 -50.101  1.00 24.93           C  
ANISOU 3267  CA  ALA A 394     3665   3272   2535     36    -20    416       C  
ATOM   3268  C   ALA A 394      -7.123  -0.632 -50.663  1.00 25.85           C  
ANISOU 3268  C   ALA A 394     3729   3412   2682     39    -23    476       C  
ATOM   3269  O   ALA A 394      -8.048  -0.188 -49.973  1.00 26.15           O  
ANISOU 3269  O   ALA A 394     3753   3404   2780     56      9    487       O  
ATOM   3270  CB  ALA A 394      -5.367  -2.206 -49.824  1.00 22.33           C  
ANISOU 3270  CB  ALA A 394     3372   2965   2148     20    -39    358       C  
ATOM   3271  N   PHE A 395      -7.283  -1.044 -51.918  1.00 23.71           N  
ANISOU 3271  N   PHE A 395     3428   3212   2369     18    -61    513       N  
ATOM   3272  CA  PHE A 395      -8.595  -1.171 -52.523  1.00 25.21           C  
ANISOU 3272  CA  PHE A 395     3567   3438   2573     11    -79    569       C  
ATOM   3273  C   PHE A 395      -9.131  -2.572 -52.281  1.00 26.28           C  
ANISOU 3273  C   PHE A 395     3721   3600   2663     -4    -87    521       C  
ATOM   3274  O   PHE A 395      -8.403  -3.559 -52.419  1.00 26.46           O  
ANISOU 3274  O   PHE A 395     3779   3651   2623    -25    -98    467       O  
ATOM   3275  CB  PHE A 395      -8.545  -0.872 -54.025  1.00 23.74           C  
ANISOU 3275  CB  PHE A 395     3341   3323   2355    -18   -121    639       C  
ATOM   3276  CG  PHE A 395      -9.862  -1.078 -54.735  1.00 27.56           C  
ANISOU 3276  CG  PHE A 395     3770   3856   2844    -36   -153    705       C  
ATOM   3277  CD1 PHE A 395     -10.861  -0.107 -54.674  1.00 27.95           C  
ANISOU 3277  CD1 PHE A 395     3761   3871   2986    -12   -151    785       C  
ATOM   3278  CD2 PHE A 395     -10.094  -2.234 -55.480  1.00 27.72           C  
ANISOU 3278  CD2 PHE A 395     3793   3956   2783    -81   -185    687       C  
ATOM   3279  CE1 PHE A 395     -12.078  -0.292 -55.329  1.00 31.75           C  
ANISOU 3279  CE1 PHE A 395     4184   4399   3480    -30   -189    853       C  
ATOM   3280  CE2 PHE A 395     -11.310  -2.431 -56.138  1.00 29.80           C  
ANISOU 3280  CE2 PHE A 395     4005   4271   3046   -104   -220    749       C  
ATOM   3281  CZ  PHE A 395     -12.303  -1.462 -56.062  1.00 32.30           C  
ANISOU 3281  CZ  PHE A 395     4261   4556   3457    -78   -227    836       C  
ATOM   3282  N   VAL A 396     -10.402  -2.638 -51.891  1.00 27.56           N  
ANISOU 3282  N   VAL A 396     3857   3746   2870      6    -76    540       N  
ATOM   3283  CA  VAL A 396     -11.149  -3.893 -51.799  1.00 28.20           C  
ANISOU 3283  CA  VAL A 396     3942   3856   2915    -11    -84    508       C  
ATOM   3284  C   VAL A 396     -12.411  -3.767 -52.665  1.00 28.71           C  
ANISOU 3284  C   VAL A 396     3938   3966   3003    -24   -112    582       C  
ATOM   3285  O   VAL A 396     -13.192  -2.812 -52.524  1.00 28.89           O  
ANISOU 3285  O   VAL A 396     3913   3952   3110     -1   -100    641       O  
ATOM   3286  CB  VAL A 396     -11.500  -4.258 -50.329  1.00 27.71           C  
ANISOU 3286  CB  VAL A 396     3920   3729   2881      7    -40    451       C  
ATOM   3287  CG1 VAL A 396     -12.108  -5.651 -50.247  1.00 25.28           C  
ANISOU 3287  CG1 VAL A 396     3624   3451   2532    -13    -49    413       C  
ATOM   3288  CG2 VAL A 396     -10.250  -4.187 -49.446  1.00 26.64           C  
ANISOU 3288  CG2 VAL A 396     3847   3548   2728     14    -22    395       C  
ATOM   3289  N   LYS A 397     -12.571  -4.711 -53.592  1.00 29.64           N  
ANISOU 3289  N   LYS A 397     4048   4163   3049    -64   -149    580       N  
ATOM   3290  CA  LYS A 397     -13.704  -4.731 -54.519  1.00 28.88           C  
ANISOU 3290  CA  LYS A 397     3889   4127   2958    -91   -188    651       C  
ATOM   3291  C   LYS A 397     -14.917  -5.359 -53.839  1.00 29.13           C  
ANISOU 3291  C   LYS A 397     3906   4137   3026    -81   -171    632       C  
ATOM   3292  O   LYS A 397     -14.784  -6.376 -53.158  1.00 29.84           O  
ANISOU 3292  O   LYS A 397     4043   4212   3084    -83   -147    553       O  
ATOM   3293  CB  LYS A 397     -13.345  -5.525 -55.782  1.00 28.74           C  
ANISOU 3293  CB  LYS A 397     3876   4208   2837   -153   -229    645       C  
ATOM   3294  CG  LYS A 397     -14.455  -5.567 -56.845  1.00 32.50           C  
ANISOU 3294  CG  LYS A 397     4288   4762   3298   -197   -280    723       C  
ATOM   3295  CD  LYS A 397     -14.098  -6.463 -58.025  1.00 30.82           C  
ANISOU 3295  CD  LYS A 397     4090   4649   2970   -273   -310    698       C  
ATOM   3296  CE  LYS A 397     -15.297  -6.695 -58.953  1.00 31.57           C  
ANISOU 3296  CE  LYS A 397     4128   4828   3040   -327   -364    766       C  
ATOM   3297  NZ  LYS A 397     -15.659  -5.479 -59.733  1.00 30.77           N  
ANISOU 3297  NZ  LYS A 397     3967   4756   2968   -338   -417    893       N  
ATOM   3298  N   GLU A 398     -16.087  -4.747 -54.025  1.00 29.63           N  
ANISOU 3298  N   GLU A 398     3899   4196   3165    -72   -184    709       N  
ATOM   3299  CA  GLU A 398     -17.356  -5.295 -53.537  1.00 31.08           C  
ANISOU 3299  CA  GLU A 398     4053   4364   3391    -68   -170    700       C  
ATOM   3300  C   GLU A 398     -17.806  -6.488 -54.400  1.00 29.71           C  
ANISOU 3300  C   GLU A 398     3871   4282   3135   -122   -214    691       C  
ATOM   3301  O   GLU A 398     -18.207  -6.306 -55.550  1.00 32.15           O  
ANISOU 3301  O   GLU A 398     4127   4664   3423   -160   -270    765       O  
ATOM   3302  CB  GLU A 398     -18.440  -4.196 -53.513  1.00 31.79           C  
ANISOU 3302  CB  GLU A 398     4059   4413   3607    -41   -169    790       C  
ATOM   3303  CG  GLU A 398     -19.738  -4.581 -52.776  1.00 34.27           C  
ANISOU 3303  CG  GLU A 398     4341   4686   3993    -28   -136    774       C  
ATOM   3304  CD  GLU A 398     -19.581  -4.620 -51.251  1.00 36.68           C  
ANISOU 3304  CD  GLU A 398     4704   4898   4336      4    -53    686       C  
ATOM   3305  OE1 GLU A 398     -19.360  -3.551 -50.636  1.00 35.94           O  
ANISOU 3305  OE1 GLU A 398     4607   4728   4321     37     -7    693       O  
ATOM   3306  OE2 GLU A 398     -19.683  -5.721 -50.666  1.00 35.14           O  
ANISOU 3306  OE2 GLU A 398     4559   4705   4088     -9    -32    610       O  
ATOM   3307  N   PRO A 399     -17.743  -7.717 -53.851  1.00 28.25           N  
ANISOU 3307  N   PRO A 399     3737   4095   2902   -132   -188    602       N  
ATOM   3308  CA  PRO A 399     -18.191  -8.853 -54.665  1.00 26.93           C  
ANISOU 3308  CA  PRO A 399     3559   4011   2662   -188   -221    587       C  
ATOM   3309  C   PRO A 399     -19.719  -8.961 -54.723  1.00 28.59           C  
ANISOU 3309  C   PRO A 399     3703   4234   2928   -195   -236    632       C  
ATOM   3310  O   PRO A 399     -20.413  -8.490 -53.817  1.00 28.37           O  
ANISOU 3310  O   PRO A 399     3652   4132   2995   -152   -200    642       O  
ATOM   3311  CB  PRO A 399     -17.616 -10.055 -53.918  1.00 25.33           C  
ANISOU 3311  CB  PRO A 399     3429   3782   2414   -188   -180    480       C  
ATOM   3312  CG  PRO A 399     -17.639  -9.620 -52.480  1.00 25.76           C  
ANISOU 3312  CG  PRO A 399     3512   3737   2540   -133   -129    456       C  
ATOM   3313  CD  PRO A 399     -17.372  -8.129 -52.482  1.00 24.60           C  
ANISOU 3313  CD  PRO A 399     3339   3556   2453   -101   -130    519       C  
ATOM   3314  N   ILE A 400     -20.233  -9.575 -55.786  1.00 29.11           N  
ANISOU 3314  N   ILE A 400     3734   4391   2934   -254   -285    655       N  
ATOM   3315  CA  ILE A 400     -21.647  -9.931 -55.860  1.00 29.87           C  
ANISOU 3315  CA  ILE A 400     3771   4508   3072   -270   -302    685       C  
ATOM   3316  C   ILE A 400     -21.847 -11.233 -55.075  1.00 29.27           C  
ANISOU 3316  C   ILE A 400     3742   4407   2972   -272   -254    582       C  
ATOM   3317  O   ILE A 400     -21.312 -12.276 -55.459  1.00 28.56           O  
ANISOU 3317  O   ILE A 400     3697   4363   2791   -314   -254    517       O  
ATOM   3318  CB  ILE A 400     -22.125 -10.091 -57.326  1.00 30.76           C  
ANISOU 3318  CB  ILE A 400     3829   4737   3121   -345   -380    752       C  
ATOM   3319  CG1 ILE A 400     -21.952  -8.770 -58.089  1.00 33.64           C  
ANISOU 3319  CG1 ILE A 400     4145   5125   3513   -346   -432    867       C  
ATOM   3320  CG2 ILE A 400     -23.585 -10.583 -57.379  1.00 30.51           C  
ANISOU 3320  CG2 ILE A 400     3733   4729   3130   -366   -400    776       C  
ATOM   3321  CD1 ILE A 400     -22.012  -8.912 -59.615  1.00 37.58           C  
ANISOU 3321  CD1 ILE A 400     4615   5750   3912   -436   -511    928       C  
ATOM   3322  N   PRO A 401     -22.605 -11.178 -53.962  1.00 29.57           N  
ANISOU 3322  N   PRO A 401     3771   4367   3097   -229   -208    566       N  
ATOM   3323  CA  PRO A 401     -22.756 -12.402 -53.167  1.00 28.90           C  
ANISOU 3323  CA  PRO A 401     3738   4256   2988   -233   -162    474       C  
ATOM   3324  C   PRO A 401     -23.385 -13.480 -54.027  1.00 27.98           C  
ANISOU 3324  C   PRO A 401     3596   4223   2812   -295   -195    461       C  
ATOM   3325  O   PRO A 401     -24.418 -13.245 -54.649  1.00 30.74           O  
ANISOU 3325  O   PRO A 401     3870   4618   3193   -318   -236    526       O  
ATOM   3326  CB  PRO A 401     -23.695 -11.983 -52.030  1.00 26.50           C  
ANISOU 3326  CB  PRO A 401     3411   3867   2793   -190   -112    478       C  
ATOM   3327  CG  PRO A 401     -23.594 -10.495 -51.969  1.00 31.41           C  
ANISOU 3327  CG  PRO A 401     3994   4446   3495   -150   -112    548       C  
ATOM   3328  CD  PRO A 401     -23.369 -10.054 -53.391  1.00 30.41           C  
ANISOU 3328  CD  PRO A 401     3820   4404   3329   -181   -189    627       C  
ATOM   3329  N   ASN A 402     -22.745 -14.641 -54.090  1.00 26.41           N  
ANISOU 3329  N   ASN A 402     3457   4046   2533   -325   -179    380       N  
ATOM   3330  CA  ASN A 402     -23.168 -15.686 -55.016  1.00 27.48           C  
ANISOU 3330  CA  ASN A 402     3575   4266   2601   -396   -204    356       C  
ATOM   3331  C   ASN A 402     -22.323 -16.930 -54.815  1.00 26.85           C  
ANISOU 3331  C   ASN A 402     3567   4176   2459   -415   -165    254       C  
ATOM   3332  O   ASN A 402     -21.285 -16.877 -54.162  1.00 24.79           O  
ANISOU 3332  O   ASN A 402     3363   3856   2200   -378   -135    218       O  
ATOM   3333  CB  ASN A 402     -23.032 -15.194 -56.469  1.00 27.39           C  
ANISOU 3333  CB  ASN A 402     3522   4354   2531   -451   -271    421       C  
ATOM   3334  CG  ASN A 402     -24.028 -15.864 -57.435  1.00 33.99           C  
ANISOU 3334  CG  ASN A 402     4307   5285   3322   -529   -314    435       C  
ATOM   3335  OD1 ASN A 402     -24.654 -16.882 -57.120  1.00 38.39           O  
ANISOU 3335  OD1 ASN A 402     4868   5839   3880   -547   -288    378       O  
ATOM   3336  ND2 ASN A 402     -24.167 -15.284 -58.621  1.00 30.78           N  
ANISOU 3336  ND2 ASN A 402     3853   4968   2875   -582   -382    515       N  
ATOM   3337  N   ARG A 403     -22.786 -18.051 -55.359  1.00 27.11           N  
ANISOU 3337  N   ARG A 403     3592   4264   2446   -474   -166    210       N  
ATOM   3338  CA  ARG A 403     -21.921 -19.194 -55.585  1.00 29.85           C  
ANISOU 3338  CA  ARG A 403     3991   4619   2732   -510   -136    121       C  
ATOM   3339  C   ARG A 403     -21.072 -18.881 -56.816  1.00 31.38           C  
ANISOU 3339  C   ARG A 403     4183   4886   2853   -560   -166    132       C  
ATOM   3340  O   ARG A 403     -21.507 -18.137 -57.700  1.00 32.00           O  
ANISOU 3340  O   ARG A 403     4214   5037   2908   -593   -219    205       O  
ATOM   3341  CB  ARG A 403     -22.740 -20.466 -55.816  1.00 31.45           C  
ANISOU 3341  CB  ARG A 403     4182   4854   2913   -564   -120     67       C  
ATOM   3342  CG  ARG A 403     -23.602 -20.441 -57.077  1.00 33.66           C  
ANISOU 3342  CG  ARG A 403     4399   5245   3143   -642   -172    106       C  
ATOM   3343  CD  ARG A 403     -24.368 -21.729 -57.242  1.00 36.76           C  
ANISOU 3343  CD  ARG A 403     4784   5666   3516   -698   -150     43       C  
ATOM   3344  NE  ARG A 403     -25.464 -21.827 -56.286  1.00 37.68           N  
ANISOU 3344  NE  ARG A 403     4879   5729   3709   -656   -135     56       N  
ATOM   3345  CZ  ARG A 403     -26.326 -22.838 -56.233  1.00 39.20           C  
ANISOU 3345  CZ  ARG A 403     5057   5933   3903   -693   -115     11       C  
ATOM   3346  NH1 ARG A 403     -26.219 -23.859 -57.075  1.00 39.64           N  
ANISOU 3346  NH1 ARG A 403     5120   6052   3889   -773   -106    -53       N  
ATOM   3347  NH2 ARG A 403     -27.298 -22.828 -55.334  1.00 38.85           N  
ANISOU 3347  NH2 ARG A 403     4993   5836   3933   -653    -97     25       N  
ATOM   3348  N   TYR A 404     -19.857 -19.425 -56.848  1.00 31.14           N  
ANISOU 3348  N   TYR A 404     4203   4834   2794   -566   -131     64       N  
ATOM   3349  CA  TYR A 404     -18.968 -19.319 -58.003  1.00 29.51           C  
ANISOU 3349  CA  TYR A 404     4004   4694   2517   -623   -142     52       C  
ATOM   3350  C   TYR A 404     -18.315 -20.676 -58.232  1.00 30.75           C  
ANISOU 3350  C   TYR A 404     4194   4844   2644   -668    -88    -57       C  
ATOM   3351  O   TYR A 404     -17.592 -21.180 -57.366  1.00 28.91           O  
ANISOU 3351  O   TYR A 404     4000   4525   2458   -621    -46   -107       O  
ATOM   3352  CB  TYR A 404     -17.913 -18.233 -57.780  1.00 27.49           C  
ANISOU 3352  CB  TYR A 404     3767   4399   2280   -572   -149     89       C  
ATOM   3353  CG  TYR A 404     -18.485 -16.832 -57.748  1.00 26.87           C  
ANISOU 3353  CG  TYR A 404     3649   4329   2233   -537   -198    196       C  
ATOM   3354  CD1 TYR A 404     -18.696 -16.113 -58.930  1.00 26.03           C  
ANISOU 3354  CD1 TYR A 404     3501   4311   2077   -590   -251    267       C  
ATOM   3355  CD2 TYR A 404     -18.821 -16.227 -56.538  1.00 26.83           C  
ANISOU 3355  CD2 TYR A 404     3643   4239   2310   -457   -188    228       C  
ATOM   3356  CE1 TYR A 404     -19.225 -14.828 -58.905  1.00 26.61           C  
ANISOU 3356  CE1 TYR A 404     3529   4383   2196   -556   -296    373       C  
ATOM   3357  CE2 TYR A 404     -19.346 -14.937 -56.500  1.00 28.37           C  
ANISOU 3357  CE2 TYR A 404     3795   4431   2553   -425   -222    322       C  
ATOM   3358  CZ  TYR A 404     -19.545 -14.246 -57.684  1.00 28.37           C  
ANISOU 3358  CZ  TYR A 404     3749   4514   2517   -470   -278    397       C  
ATOM   3359  OH  TYR A 404     -20.071 -12.978 -57.641  1.00 28.56           O  
ANISOU 3359  OH  TYR A 404     3722   4524   2605   -436   -311    497       O  
ATOM   3360  N   LYS A 405     -18.586 -21.260 -59.399  1.00 30.71           N  
ANISOU 3360  N   LYS A 405     4172   4930   2566   -765    -90    -89       N  
ATOM   3361  CA  LYS A 405     -18.244 -22.652 -59.674  1.00 31.03           C  
ANISOU 3361  CA  LYS A 405     4234   4967   2588   -819    -31   -199       C  
ATOM   3362  C   LYS A 405     -16.743 -22.855 -59.927  1.00 31.31           C  
ANISOU 3362  C   LYS A 405     4304   4970   2621   -826     15   -262       C  
ATOM   3363  O   LYS A 405     -16.069 -23.561 -59.174  1.00 31.58           O  
ANISOU 3363  O   LYS A 405     4365   4915   2718   -784     64   -320       O  
ATOM   3364  CB  LYS A 405     -19.082 -23.164 -60.846  1.00 31.53           C  
ANISOU 3364  CB  LYS A 405     4267   5142   2570   -931    -45   -217       C  
ATOM   3365  CG  LYS A 405     -19.124 -24.680 -60.990  1.00 36.79           C  
ANISOU 3365  CG  LYS A 405     4946   5799   3231   -988     22   -330       C  
ATOM   3366  CD  LYS A 405     -19.957 -25.078 -62.201  1.00 39.09           C  
ANISOU 3366  CD  LYS A 405     5209   6213   3430  -1111      4   -347       C  
ATOM   3367  CE  LYS A 405     -20.090 -26.591 -62.335  1.00 44.19           C  
ANISOU 3367  CE  LYS A 405     5865   6848   4077  -1173     76   -465       C  
ATOM   3368  NZ  LYS A 405     -20.895 -26.987 -63.538  1.00 46.15           N  
ANISOU 3368  NZ  LYS A 405     6088   7223   4225  -1306     60   -487       N  
ATOM   3369  N   TYR A 406     -16.230 -22.232 -60.983  1.00 31.70           N  
ANISOU 3369  N   TYR A 406     4349   5092   2602   -882     -2   -245       N  
ATOM   3370  CA  TYR A 406     -14.819 -22.314 -61.324  1.00 32.49           C  
ANISOU 3370  CA  TYR A 406     4475   5168   2700   -895     43   -303       C  
ATOM   3371  C   TYR A 406     -14.151 -20.972 -61.077  1.00 32.81           C  
ANISOU 3371  C   TYR A 406     4522   5187   2757   -832      6   -226       C  
ATOM   3372  O   TYR A 406     -14.611 -19.939 -61.568  1.00 34.39           O  
ANISOU 3372  O   TYR A 406     4700   5453   2912   -846    -53   -139       O  
ATOM   3373  CB  TYR A 406     -14.637 -22.758 -62.784  1.00 31.69           C  
ANISOU 3373  CB  TYR A 406     4371   5165   2503  -1024     70   -363       C  
ATOM   3374  CG  TYR A 406     -15.094 -24.182 -63.036  1.00 33.38           C  
ANISOU 3374  CG  TYR A 406     4584   5390   2710  -1093    125   -461       C  
ATOM   3375  CD1 TYR A 406     -16.295 -24.445 -63.699  1.00 35.46           C  
ANISOU 3375  CD1 TYR A 406     4823   5751   2900  -1175     95   -450       C  
ATOM   3376  CD2 TYR A 406     -14.332 -25.266 -62.600  1.00 31.77           C  
ANISOU 3376  CD2 TYR A 406     4396   5095   2580  -1076    206   -562       C  
ATOM   3377  CE1 TYR A 406     -16.724 -25.758 -63.925  1.00 36.68           C  
ANISOU 3377  CE1 TYR A 406     4975   5913   3047  -1242    150   -545       C  
ATOM   3378  CE2 TYR A 406     -14.747 -26.579 -62.826  1.00 34.40           C  
ANISOU 3378  CE2 TYR A 406     4725   5429   2916  -1138    264   -655       C  
ATOM   3379  CZ  TYR A 406     -15.943 -26.818 -63.486  1.00 36.02           C  
ANISOU 3379  CZ  TYR A 406     4911   5733   3040  -1222    238   -650       C  
ATOM   3380  OH  TYR A 406     -16.357 -28.117 -63.700  1.00 38.14           O  
ANISOU 3380  OH  TYR A 406     5176   6002   3313  -1288    299   -746       O  
ATOM   3381  N   VAL A 407     -13.063 -20.994 -60.312  1.00 33.06           N  
ANISOU 3381  N   VAL A 407     4579   5124   2858   -765     37   -254       N  
ATOM   3382  CA  VAL A 407     -12.350 -19.770 -59.940  1.00 31.09           C  
ANISOU 3382  CA  VAL A 407     4337   4841   2633   -701      9   -191       C  
ATOM   3383  C   VAL A 407     -10.840 -19.959 -60.046  1.00 32.02           C  
ANISOU 3383  C   VAL A 407     4475   4912   2778   -698     56   -253       C  
ATOM   3384  O   VAL A 407     -10.292 -20.944 -59.539  1.00 30.83           O  
ANISOU 3384  O   VAL A 407     4337   4690   2689   -681    104   -324       O  
ATOM   3385  CB  VAL A 407     -12.704 -19.312 -58.492  1.00 28.24           C  
ANISOU 3385  CB  VAL A 407     3985   4399   2349   -598    -16   -136       C  
ATOM   3386  CG1 VAL A 407     -11.960 -18.030 -58.125  1.00 27.51           C  
ANISOU 3386  CG1 VAL A 407     3901   4273   2280   -539    -41    -77       C  
ATOM   3387  CG2 VAL A 407     -14.185 -19.099 -58.340  1.00 24.64           C  
ANISOU 3387  CG2 VAL A 407     3502   3978   1883   -596    -54    -78       C  
ATOM   3388  N   MET A 408     -10.185 -19.006 -60.710  1.00 32.01           N  
ANISOU 3388  N   MET A 408     4475   4949   2739   -717     42   -221       N  
ATOM   3389  CA  MET A 408      -8.728 -18.908 -60.726  1.00 32.87           C  
ANISOU 3389  CA  MET A 408     4598   5008   2884   -702     79   -264       C  
ATOM   3390  C   MET A 408      -8.324 -17.606 -60.060  1.00 31.23           C  
ANISOU 3390  C   MET A 408     4397   4761   2709   -624     37   -184       C  
ATOM   3391  O   MET A 408      -8.822 -16.532 -60.426  1.00 30.15           O  
ANISOU 3391  O   MET A 408     4249   4679   2528   -628    -10   -102       O  
ATOM   3392  CB  MET A 408      -8.178 -18.869 -62.153  1.00 33.76           C  
ANISOU 3392  CB  MET A 408     4710   5200   2920   -803    110   -305       C  
ATOM   3393  CG  MET A 408      -8.624 -19.975 -63.072  1.00 43.48           C  
ANISOU 3393  CG  MET A 408     5935   6493   4092   -908    154   -384       C  
ATOM   3394  SD  MET A 408      -7.502 -20.073 -64.484  1.00 52.38           S  
ANISOU 3394  SD  MET A 408     7070   7674   5156  -1021    221   -466       S  
ATOM   3395  CE  MET A 408      -6.129 -20.871 -63.653  1.00 45.86           C  
ANISOU 3395  CE  MET A 408     6245   6706   4473   -953    297   -557       C  
ATOM   3396  N   SER A 409      -7.404 -17.680 -59.109  1.00 28.72           N  
ANISOU 3396  N   SER A 409     4093   4347   2471   -556     53   -204       N  
ATOM   3397  CA  SER A 409      -6.894 -16.458 -58.500  1.00 27.71           C  
ANISOU 3397  CA  SER A 409     3974   4183   2373   -490     20   -139       C  
ATOM   3398  C   SER A 409      -5.479 -16.147 -58.971  1.00 29.41           C  
ANISOU 3398  C   SER A 409     4191   4383   2599   -503     47   -171       C  
ATOM   3399  O   SER A 409      -4.713 -17.049 -59.333  1.00 29.89           O  
ANISOU 3399  O   SER A 409     4249   4423   2683   -537     99   -253       O  
ATOM   3400  CB  SER A 409      -6.972 -16.511 -56.969  1.00 23.82           C  
ANISOU 3400  CB  SER A 409     3497   3600   1954   -407      4   -120       C  
ATOM   3401  OG  SER A 409      -6.049 -17.440 -56.440  1.00 19.83           O  
ANISOU 3401  OG  SER A 409     3001   3021   1513   -389     37   -183       O  
ATOM   3402  N   PHE A 410      -5.161 -14.856 -58.982  1.00 28.83           N  
ANISOU 3402  N   PHE A 410     4120   4317   2517   -477     17   -108       N  
ATOM   3403  CA  PHE A 410      -3.827 -14.366 -59.282  1.00 28.92           C  
ANISOU 3403  CA  PHE A 410     4134   4307   2546   -478     38   -127       C  
ATOM   3404  C   PHE A 410      -3.387 -13.415 -58.172  1.00 30.99           C  
ANISOU 3404  C   PHE A 410     4407   4501   2865   -395      7    -75       C  
ATOM   3405  O   PHE A 410      -4.205 -12.706 -57.580  1.00 30.91           O  
ANISOU 3405  O   PHE A 410     4400   4490   2856   -355    -31     -8       O  
ATOM   3406  CB  PHE A 410      -3.804 -13.667 -60.643  1.00 28.22           C  
ANISOU 3406  CB  PHE A 410     4039   4310   2374   -550     38   -104       C  
ATOM   3407  CG  PHE A 410      -4.099 -14.587 -61.805  1.00 28.23           C  
ANISOU 3407  CG  PHE A 410     4035   4386   2306   -651     74   -165       C  
ATOM   3408  CD1 PHE A 410      -5.406 -14.989 -62.083  1.00 28.20           C  
ANISOU 3408  CD1 PHE A 410     4023   4444   2248   -688     50   -144       C  
ATOM   3409  CD2 PHE A 410      -3.066 -15.053 -62.621  1.00 28.64           C  
ANISOU 3409  CD2 PHE A 410     4088   4445   2349   -714    137   -248       C  
ATOM   3410  CE1 PHE A 410      -5.681 -15.847 -63.147  1.00 30.33           C  
ANISOU 3410  CE1 PHE A 410     4290   4786   2447   -790     85   -206       C  
ATOM   3411  CE2 PHE A 410      -3.330 -15.908 -63.692  1.00 30.44           C  
ANISOU 3411  CE2 PHE A 410     4315   4742   2509   -818    181   -315       C  
ATOM   3412  CZ  PHE A 410      -4.638 -16.302 -63.960  1.00 31.64           C  
ANISOU 3412  CZ  PHE A 410     4462   4960   2598   -859    153   -294       C  
ATOM   3413  N   ASP A 411      -2.089 -13.408 -57.893  1.00 31.69           N  
ANISOU 3413  N   ASP A 411     4500   4533   3010   -374     28   -111       N  
ATOM   3414  CA  ASP A 411      -1.545 -12.632 -56.793  1.00 32.80           C  
ANISOU 3414  CA  ASP A 411     4651   4606   3204   -304      1    -74       C  
ATOM   3415  C   ASP A 411      -0.194 -12.008 -57.153  1.00 32.63           C  
ANISOU 3415  C   ASP A 411     4624   4568   3205   -307     18    -87       C  
ATOM   3416  O   ASP A 411       0.650 -12.646 -57.778  1.00 32.72           O  
ANISOU 3416  O   ASP A 411     4622   4574   3234   -343     59   -152       O  
ATOM   3417  CB  ASP A 411      -1.393 -13.526 -55.559  1.00 35.80           C  
ANISOU 3417  CB  ASP A 411     5042   4908   3653   -261     -3   -100       C  
ATOM   3418  CG  ASP A 411      -0.625 -12.858 -54.459  1.00 38.73           C  
ANISOU 3418  CG  ASP A 411     5428   5213   4077   -205    -28    -73       C  
ATOM   3419  OD1 ASP A 411       0.536 -13.241 -54.222  1.00 43.48           O  
ANISOU 3419  OD1 ASP A 411     6021   5762   4738   -196    -19   -108       O  
ATOM   3420  OD2 ASP A 411      -1.160 -11.911 -53.851  1.00 45.39           O  
ANISOU 3420  OD2 ASP A 411     6287   6055   4906   -175    -56    -17       O  
ATOM   3421  N   LEU A 412      -0.002 -10.758 -56.747  1.00 30.62           N  
ANISOU 3421  N   LEU A 412     4378   4300   2956   -270     -9    -31       N  
ATOM   3422  CA  LEU A 412       1.273 -10.083 -56.910  1.00 30.35           C  
ANISOU 3422  CA  LEU A 412     4340   4241   2951   -265      2    -39       C  
ATOM   3423  C   LEU A 412       2.250 -10.504 -55.822  1.00 29.99           C  
ANISOU 3423  C   LEU A 412     4295   4109   2989   -221     -2    -70       C  
ATOM   3424  O   LEU A 412       1.905 -10.507 -54.638  1.00 29.14           O  
ANISOU 3424  O   LEU A 412     4205   3959   2907   -177    -34    -44       O  
ATOM   3425  CB  LEU A 412       1.070  -8.570 -56.887  1.00 30.74           C  
ANISOU 3425  CB  LEU A 412     4395   4307   2979   -245    -23     35       C  
ATOM   3426  CG  LEU A 412       0.543  -7.992 -58.201  1.00 31.43           C  
ANISOU 3426  CG  LEU A 412     4471   4478   2991   -299    -21     73       C  
ATOM   3427  CD1 LEU A 412      -0.292  -6.750 -57.953  1.00 29.91           C  
ANISOU 3427  CD1 LEU A 412     4277   4295   2791   -270    -56    164       C  
ATOM   3428  CD2 LEU A 412       1.706  -7.699 -59.142  1.00 27.91           C  
ANISOU 3428  CD2 LEU A 412     4020   4050   2535   -341     12     43       C  
ATOM   3429  N   THR A 413       3.460 -10.877 -56.239  1.00 29.11           N  
ANISOU 3429  N   THR A 413     4165   3973   2922   -239     30   -124       N  
ATOM   3430  CA  THR A 413       4.539 -11.246 -55.331  1.00 28.48           C  
ANISOU 3430  CA  THR A 413     4075   3811   2934   -203     21   -147       C  
ATOM   3431  C   THR A 413       4.981 -10.041 -54.504  1.00 29.30           C  
ANISOU 3431  C   THR A 413     4194   3885   3052   -161    -17    -97       C  
ATOM   3432  O   THR A 413       5.341  -8.995 -55.060  1.00 28.44           O  
ANISOU 3432  O   THR A 413     4084   3801   2919   -171     -7    -79       O  
ATOM   3433  CB  THR A 413       5.754 -11.773 -56.124  1.00 30.10           C  
ANISOU 3433  CB  THR A 413     4246   3997   3193   -236     72   -215       C  
ATOM   3434  OG1 THR A 413       5.386 -12.972 -56.817  1.00 34.81           O  
ANISOU 3434  OG1 THR A 413     4829   4612   3786   -280    117   -273       O  
ATOM   3435  CG2 THR A 413       6.946 -12.063 -55.201  1.00 25.00           C  
ANISOU 3435  CG2 THR A 413     3579   3262   2657   -197     55   -227       C  
ATOM   3436  N   SER A 414       4.949 -10.200 -53.181  1.00 29.04           N  
ANISOU 3436  N   SER A 414     4177   3800   3055   -122    -57    -75       N  
ATOM   3437  CA  SER A 414       5.457  -9.194 -52.234  1.00 27.63           C  
ANISOU 3437  CA  SER A 414     4015   3587   2895    -90    -91    -39       C  
ATOM   3438  C   SER A 414       5.172  -7.760 -52.683  1.00 24.60           C  
ANISOU 3438  C   SER A 414     3643   3243   2463    -92    -84     -1       C  
ATOM   3439  O   SER A 414       6.091  -6.999 -53.014  1.00 24.94           O  
ANISOU 3439  O   SER A 414     3673   3279   2523    -95    -75     -3       O  
ATOM   3440  CB  SER A 414       6.953  -9.407 -52.003  1.00 27.41           C  
ANISOU 3440  CB  SER A 414     3961   3505   2949    -85    -97    -66       C  
ATOM   3441  OG  SER A 414       7.401  -8.655 -50.892  1.00 37.45           O  
ANISOU 3441  OG  SER A 414     5251   4741   4238    -60   -139    -32       O  
ATOM   3442  N   LEU A 415       3.893  -7.399 -52.690  1.00 23.63           N  
ANISOU 3442  N   LEU A 415     3536   3155   2286    -90    -88     36       N  
ATOM   3443  CA  LEU A 415       3.445  -6.184 -53.376  1.00 23.07           C  
ANISOU 3443  CA  LEU A 415     3464   3126   2176    -97    -78     79       C  
ATOM   3444  C   LEU A 415       4.056  -4.880 -52.863  1.00 21.08           C  
ANISOU 3444  C   LEU A 415     3220   2842   1947    -75    -84    105       C  
ATOM   3445  O   LEU A 415       4.711  -4.175 -53.624  1.00 20.35           O  
ANISOU 3445  O   LEU A 415     3114   2765   1854    -89    -68    110       O  
ATOM   3446  CB  LEU A 415       1.915  -6.077 -53.427  1.00 21.50           C  
ANISOU 3446  CB  LEU A 415     3271   2963   1934    -96    -84    120       C  
ATOM   3447  CG  LEU A 415       1.459  -4.800 -54.155  1.00 24.01           C  
ANISOU 3447  CG  LEU A 415     3578   3319   2226   -103    -79    177       C  
ATOM   3448  CD1 LEU A 415       1.815  -4.850 -55.645  1.00 20.99           C  
ANISOU 3448  CD1 LEU A 415     3175   2996   1804   -151    -62    172       C  
ATOM   3449  CD2 LEU A 415      -0.012  -4.493 -53.963  1.00 20.75           C  
ANISOU 3449  CD2 LEU A 415     3162   2922   1798    -92    -89    228       C  
ATOM   3450  N   TYR A 416       3.838  -4.547 -51.595  1.00 19.34           N  
ANISOU 3450  N   TYR A 416     3024   2579   1744    -48   -104    120       N  
ATOM   3451  CA  TYR A 416       4.294  -3.245 -51.107  1.00 19.95           C  
ANISOU 3451  CA  TYR A 416     3111   2628   1840    -34   -103    142       C  
ATOM   3452  C   TYR A 416       5.818  -3.071 -51.184  1.00 20.24           C  
ANISOU 3452  C   TYR A 416     3136   2639   1914    -39   -105    114       C  
ATOM   3453  O   TYR A 416       6.277  -1.997 -51.554  1.00 19.78           O  
ANISOU 3453  O   TYR A 416     3070   2581   1863    -40    -90    129       O  
ATOM   3454  CB  TYR A 416       3.736  -2.923 -49.710  1.00 19.44           C  
ANISOU 3454  CB  TYR A 416     3080   2525   1781    -18   -115    153       C  
ATOM   3455  CG  TYR A 416       2.282  -2.475 -49.704  1.00 18.94           C  
ANISOU 3455  CG  TYR A 416     3020   2477   1699    -10    -98    190       C  
ATOM   3456  CD1 TYR A 416       1.458  -2.673 -50.817  1.00 18.33           C  
ANISOU 3456  CD1 TYR A 416     2917   2451   1598    -18    -90    215       C  
ATOM   3457  CD2 TYR A 416       1.719  -1.889 -48.567  1.00 19.33           C  
ANISOU 3457  CD2 TYR A 416     3096   2489   1759     -1    -89    198       C  
ATOM   3458  CE1 TYR A 416       0.127  -2.282 -50.809  1.00 18.16           C  
ANISOU 3458  CE1 TYR A 416     2888   2440   1572    -10    -80    254       C  
ATOM   3459  CE2 TYR A 416       0.383  -1.506 -48.542  1.00 21.55           C  
ANISOU 3459  CE2 TYR A 416     3372   2776   2041      7    -68    229       C  
ATOM   3460  CZ  TYR A 416      -0.404  -1.704 -49.666  1.00 20.32           C  
ANISOU 3460  CZ  TYR A 416     3182   2667   1871      6    -67    261       C  
ATOM   3461  OH  TYR A 416      -1.723  -1.326 -49.650  1.00 21.78           O  
ANISOU 3461  OH  TYR A 416     3352   2854   2069     15    -51    297       O  
ATOM   3462  N   PRO A 417       6.600  -4.127 -50.856  1.00 22.22           N  
ANISOU 3462  N   PRO A 417     3379   2865   2197    -42   -122     75       N  
ATOM   3463  CA  PRO A 417       8.050  -4.004 -51.031  1.00 22.15           C  
ANISOU 3463  CA  PRO A 417     3348   2831   2237    -47   -122     49       C  
ATOM   3464  C   PRO A 417       8.461  -3.882 -52.498  1.00 23.48           C  
ANISOU 3464  C   PRO A 417     3486   3034   2399    -71    -82     32       C  
ATOM   3465  O   PRO A 417       9.420  -3.158 -52.803  1.00 22.25           O  
ANISOU 3465  O   PRO A 417     3318   2868   2268    -76    -69     26       O  
ATOM   3466  CB  PRO A 417       8.591  -5.307 -50.419  1.00 21.85           C  
ANISOU 3466  CB  PRO A 417     3299   2756   2247    -45   -150     21       C  
ATOM   3467  CG  PRO A 417       7.544  -5.693 -49.408  1.00 20.83           C  
ANISOU 3467  CG  PRO A 417     3206   2622   2088    -35   -177     43       C  
ATOM   3468  CD  PRO A 417       6.256  -5.355 -50.107  1.00 21.83           C  
ANISOU 3468  CD  PRO A 417     3341   2797   2155    -38   -147     62       C  
ATOM   3469  N   SER A 418       7.744  -4.573 -53.387  1.00 21.46           N  
ANISOU 3469  N   SER A 418     3224   2823   2106    -91    -61     23       N  
ATOM   3470  CA  SER A 418       7.981  -4.447 -54.826  1.00 22.05           C  
ANISOU 3470  CA  SER A 418     3280   2945   2155   -129    -20      9       C  
ATOM   3471  C   SER A 418       7.589  -3.075 -55.379  1.00 23.19           C  
ANISOU 3471  C   SER A 418     3432   3124   2255   -136    -12     62       C  
ATOM   3472  O   SER A 418       8.187  -2.611 -56.351  1.00 22.15           O  
ANISOU 3472  O   SER A 418     3287   3016   2112   -166     17     57       O  
ATOM   3473  CB  SER A 418       7.263  -5.553 -55.601  1.00 21.91           C  
ANISOU 3473  CB  SER A 418     3255   2971   2099   -161      0    -16       C  
ATOM   3474  OG  SER A 418       7.694  -6.826 -55.141  1.00 24.92           O  
ANISOU 3474  OG  SER A 418     3622   3311   2536   -155     -1    -66       O  
ATOM   3475  N   ILE A 419       6.586  -2.429 -54.775  1.00 23.08           N  
ANISOU 3475  N   ILE A 419     3436   3110   2222   -110    -33    115       N  
ATOM   3476  CA  ILE A 419       6.223  -1.065 -55.182  1.00 22.36           C  
ANISOU 3476  CA  ILE A 419     3346   3037   2113   -110    -26    174       C  
ATOM   3477  C   ILE A 419       7.358  -0.126 -54.768  1.00 22.72           C  
ANISOU 3477  C   ILE A 419     3391   3036   2204    -97    -20    167       C  
ATOM   3478  O   ILE A 419       7.765   0.746 -55.535  1.00 22.92           O  
ANISOU 3478  O   ILE A 419     3407   3077   2224   -113      0    189       O  
ATOM   3479  CB  ILE A 419       4.870  -0.583 -54.584  1.00 21.14           C  
ANISOU 3479  CB  ILE A 419     3202   2880   1950    -85    -42    228       C  
ATOM   3480  CG1 ILE A 419       3.684  -1.369 -55.165  1.00 18.83           C  
ANISOU 3480  CG1 ILE A 419     2903   2641   1611   -103    -50    244       C  
ATOM   3481  CG2 ILE A 419       4.667   0.910 -54.850  1.00 20.01           C  
ANISOU 3481  CG2 ILE A 419     3051   2733   1817    -78    -33    290       C  
ATOM   3482  CD1 ILE A 419       2.351  -1.161 -54.390  1.00 16.95           C  
ANISOU 3482  CD1 ILE A 419     2672   2389   1379    -75    -64    284       C  
ATOM   3483  N   ILE A 420       7.881  -0.345 -53.563  1.00 21.51           N  
ANISOU 3483  N   ILE A 420     3250   2831   2094    -72    -39    139       N  
ATOM   3484  CA  ILE A 420       9.008   0.421 -53.054  1.00 21.80           C  
ANISOU 3484  CA  ILE A 420     3286   2823   2175    -64    -39    126       C  
ATOM   3485  C   ILE A 420      10.204   0.329 -54.004  1.00 24.19           C  
ANISOU 3485  C   ILE A 420     3562   3134   2496    -89    -14     93       C  
ATOM   3486  O   ILE A 420      10.825   1.350 -54.328  1.00 24.42           O  
ANISOU 3486  O   ILE A 420     3585   3155   2539    -95      4    104       O  
ATOM   3487  CB  ILE A 420       9.398  -0.020 -51.616  1.00 20.59           C  
ANISOU 3487  CB  ILE A 420     3148   2620   2056    -47    -74    101       C  
ATOM   3488  CG1 ILE A 420       8.336   0.469 -50.619  1.00 19.98           C  
ANISOU 3488  CG1 ILE A 420     3102   2528   1959    -31    -83    131       C  
ATOM   3489  CG2 ILE A 420      10.790   0.517 -51.243  1.00 19.51           C  
ANISOU 3489  CG2 ILE A 420     3001   2445   1968    -49    -79     79       C  
ATOM   3490  CD1 ILE A 420       8.411  -0.144 -49.222  1.00 13.79           C  
ANISOU 3490  CD1 ILE A 420     2345   1710   1185    -28   -119    112       C  
ATOM   3491  N   ARG A 421      10.507  -0.888 -54.456  1.00 22.13           N  
ANISOU 3491  N   ARG A 421     3284   2884   2242   -106     -8     49       N  
ATOM   3492  CA  ARG A 421      11.634  -1.114 -55.360  1.00 24.48           C  
ANISOU 3492  CA  ARG A 421     3552   3184   2565   -136     27      5       C  
ATOM   3493  C   ARG A 421      11.357  -0.557 -56.763  1.00 25.15           C  
ANISOU 3493  C   ARG A 421     3637   3328   2591   -176     66     25       C  
ATOM   3494  O   ARG A 421      12.203   0.133 -57.324  1.00 27.86           O  
ANISOU 3494  O   ARG A 421     3970   3670   2947   -196     94     18       O  
ATOM   3495  CB  ARG A 421      11.992  -2.603 -55.421  1.00 21.59           C  
ANISOU 3495  CB  ARG A 421     3164   2805   2236   -146     32    -52       C  
ATOM   3496  CG  ARG A 421      12.388  -3.220 -54.071  1.00 23.33           C  
ANISOU 3496  CG  ARG A 421     3379   2964   2521   -112    -15    -63       C  
ATOM   3497  CD  ARG A 421      12.377  -4.737 -54.145  1.00 23.01           C  
ANISOU 3497  CD  ARG A 421     3317   2911   2515   -118    -11   -103       C  
ATOM   3498  NE  ARG A 421      13.317  -5.234 -55.149  1.00 23.40           N  
ANISOU 3498  NE  ARG A 421     3325   2954   2612   -150     42   -162       N  
ATOM   3499  CZ  ARG A 421      13.195  -6.390 -55.797  1.00 28.06           C  
ANISOU 3499  CZ  ARG A 421     3894   3551   3215   -175     79   -209       C  
ATOM   3500  NH1 ARG A 421      12.159  -7.207 -55.559  1.00 19.54           N  
ANISOU 3500  NH1 ARG A 421     2832   2487   2103   -171     64   -202       N  
ATOM   3501  NH2 ARG A 421      14.114  -6.725 -56.694  1.00 23.29           N  
ANISOU 3501  NH2 ARG A 421     3253   2936   2660   -210    139   -270       N  
ATOM   3502  N   GLN A 422      10.170  -0.843 -57.306  1.00 24.84           N  
ANISOU 3502  N   GLN A 422     3609   3343   2487   -193     64     54       N  
ATOM   3503  CA  GLN A 422       9.761  -0.379 -58.642  1.00 23.56           C  
ANISOU 3503  CA  GLN A 422     3448   3248   2255   -242     89     86       C  
ATOM   3504  C   GLN A 422       9.711   1.147 -58.759  1.00 24.10           C  
ANISOU 3504  C   GLN A 422     3523   3316   2318   -234     86    154       C  
ATOM   3505  O   GLN A 422      10.204   1.720 -59.731  1.00 25.36           O  
ANISOU 3505  O   GLN A 422     3678   3504   2455   -274    115    165       O  
ATOM   3506  CB  GLN A 422       8.399  -0.967 -59.027  1.00 22.03           C  
ANISOU 3506  CB  GLN A 422     3263   3111   1997   -260     74    114       C  
ATOM   3507  CG  GLN A 422       7.721  -0.277 -60.223  1.00 24.49           C  
ANISOU 3507  CG  GLN A 422     3578   3496   2232   -308     78    179       C  
ATOM   3508  CD  GLN A 422       6.854  -1.221 -61.053  1.00 26.99           C  
ANISOU 3508  CD  GLN A 422     3896   3884   2476   -360     79    173       C  
ATOM   3509  OE1 GLN A 422       6.959  -2.444 -60.935  1.00 29.45           O  
ANISOU 3509  OE1 GLN A 422     4204   4190   2795   -370     94    103       O  
ATOM   3510  NE2 GLN A 422       5.998  -0.651 -61.903  1.00 20.71           N  
ANISOU 3510  NE2 GLN A 422     3101   3155   1612   -399     62    248       N  
ATOM   3511  N   VAL A 423       9.106   1.797 -57.774  1.00 22.31           N  
ANISOU 3511  N   VAL A 423     3305   3055   2116   -186     57    199       N  
ATOM   3512  CA  VAL A 423       8.952   3.252 -57.814  1.00 23.63           C  
ANISOU 3512  CA  VAL A 423     3474   3212   2294   -174     59    265       C  
ATOM   3513  C   VAL A 423      10.220   3.970 -57.334  1.00 23.62           C  
ANISOU 3513  C   VAL A 423     3470   3155   2350   -160     75    236       C  
ATOM   3514  O   VAL A 423      10.458   5.112 -57.722  1.00 24.01           O  
ANISOU 3514  O   VAL A 423     3516   3199   2408   -166     92    277       O  
ATOM   3515  CB  VAL A 423       7.694   3.727 -57.028  1.00 21.58           C  
ANISOU 3515  CB  VAL A 423     3220   2933   2044   -135     35    322       C  
ATOM   3516  CG1 VAL A 423       7.523   5.239 -57.115  1.00 22.65           C  
ANISOU 3516  CG1 VAL A 423     3349   3048   2209   -123     45    391       C  
ATOM   3517  CG2 VAL A 423       6.442   3.031 -57.559  1.00 22.54           C  
ANISOU 3517  CG2 VAL A 423     3339   3113   2113   -151     16    353       C  
ATOM   3518  N   ASN A 424      11.035   3.273 -56.533  1.00 22.54           N  
ANISOU 3518  N   ASN A 424     3332   2978   2256   -144     68    171       N  
ATOM   3519  CA  ASN A 424      12.220   3.835 -55.874  1.00 23.14           C  
ANISOU 3519  CA  ASN A 424     3402   2998   2391   -130     71    141       C  
ATOM   3520  C   ASN A 424      11.832   4.806 -54.753  1.00 24.49           C  
ANISOU 3520  C   ASN A 424     3590   3126   2588    -97     56    173       C  
ATOM   3521  O   ASN A 424      12.285   5.952 -54.713  1.00 24.54           O  
ANISOU 3521  O   ASN A 424     3596   3108   2621    -95     75    190       O  
ATOM   3522  CB  ASN A 424      13.203   4.470 -56.883  1.00 24.62           C  
ANISOU 3522  CB  ASN A 424     3574   3195   2585   -163    111    134       C  
ATOM   3523  CG  ASN A 424      14.624   4.594 -56.331  1.00 28.17           C  
ANISOU 3523  CG  ASN A 424     4008   3593   3104   -157    115     82       C  
ATOM   3524  OD1 ASN A 424      15.077   3.764 -55.535  1.00 30.28           O  
ANISOU 3524  OD1 ASN A 424     4266   3829   3412   -142     89     39       O  
ATOM   3525  ND2 ASN A 424      15.331   5.634 -56.755  1.00 28.88           N  
ANISOU 3525  ND2 ASN A 424     4091   3672   3212   -171    144     91       N  
ATOM   3526  N   ILE A 425      11.002   4.317 -53.831  1.00 25.38           N  
ANISOU 3526  N   ILE A 425     3720   3228   2693    -75     29    176       N  
ATOM   3527  CA  ILE A 425      10.473   5.123 -52.730  1.00 24.93           C  
ANISOU 3527  CA  ILE A 425     3684   3132   2655    -52     24    197       C  
ATOM   3528  C   ILE A 425      11.404   5.058 -51.523  1.00 26.09           C  
ANISOU 3528  C   ILE A 425     3842   3232   2837    -49      3    151       C  
ATOM   3529  O   ILE A 425      11.596   4.001 -50.921  1.00 25.75           O  
ANISOU 3529  O   ILE A 425     3804   3185   2794    -49    -30    120       O  
ATOM   3530  CB  ILE A 425       9.015   4.703 -52.362  1.00 24.83           C  
ANISOU 3530  CB  ILE A 425     3686   3134   2615    -37     12    224       C  
ATOM   3531  CG1 ILE A 425       8.080   4.946 -53.551  1.00 24.71           C  
ANISOU 3531  CG1 ILE A 425     3653   3165   2570    -44     25    282       C  
ATOM   3532  CG2 ILE A 425       8.499   5.473 -51.148  1.00 22.06           C  
ANISOU 3532  CG2 ILE A 425     3356   2735   2289    -21     19    232       C  
ATOM   3533  CD1 ILE A 425       6.781   4.155 -53.505  1.00 24.77           C  
ANISOU 3533  CD1 ILE A 425     3665   3201   2545    -38      9    301       C  
ATOM   3534  N   SER A 426      11.973   6.211 -51.179  1.00 26.12           N  
ANISOU 3534  N   SER A 426     3848   3202   2873    -51     21    152       N  
ATOM   3535  CA  SER A 426      12.952   6.325 -50.101  1.00 26.27           C  
ANISOU 3535  CA  SER A 426     3876   3182   2923    -59      0    112       C  
ATOM   3536  C   SER A 426      12.922   7.786 -49.648  1.00 27.25           C  
ANISOU 3536  C   SER A 426     4013   3271   3070    -62     33    123       C  
ATOM   3537  O   SER A 426      12.468   8.647 -50.405  1.00 28.64           O  
ANISOU 3537  O   SER A 426     4179   3450   3253    -55     72    162       O  
ATOM   3538  CB  SER A 426      14.348   5.944 -50.609  1.00 25.86           C  
ANISOU 3538  CB  SER A 426     3794   3130   2904    -72     -9     78       C  
ATOM   3539  OG  SER A 426      15.202   5.517 -49.554  1.00 27.72           O  
ANISOU 3539  OG  SER A 426     4028   3336   3166    -80    -52     45       O  
ATOM   3540  N   PRO A 427      13.363   8.071 -48.407  1.00 25.91           N  
ANISOU 3540  N   PRO A 427     3866   3068   2913    -77     18     92       N  
ATOM   3541  CA  PRO A 427      13.427   9.453 -47.939  1.00 26.13           C  
ANISOU 3541  CA  PRO A 427     3905   3057   2967    -87     58     91       C  
ATOM   3542  C   PRO A 427      14.324  10.341 -48.801  1.00 26.92           C  
ANISOU 3542  C   PRO A 427     3977   3147   3106    -90     89     96       C  
ATOM   3543  O   PRO A 427      14.007  11.504 -49.015  1.00 28.63           O  
ANISOU 3543  O   PRO A 427     4192   3339   3349    -87    138    119       O  
ATOM   3544  CB  PRO A 427      14.019   9.321 -46.525  1.00 27.07           C  
ANISOU 3544  CB  PRO A 427     4052   3154   3080   -118     24     47       C  
ATOM   3545  CG  PRO A 427      14.544   7.910 -46.436  1.00 28.09           C  
ANISOU 3545  CG  PRO A 427     4171   3307   3195   -119    -41     35       C  
ATOM   3546  CD  PRO A 427      13.636   7.124 -47.314  1.00 26.93           C  
ANISOU 3546  CD  PRO A 427     4013   3193   3026    -91    -36     63       C  
ATOM   3547  N   GLU A 428      15.434   9.800 -49.297  1.00 27.90           N  
ANISOU 3547  N   GLU A 428     4075   3285   3240    -97     66     75       N  
ATOM   3548  CA  GLU A 428      16.388  10.628 -50.021  1.00 27.83           C  
ANISOU 3548  CA  GLU A 428     4041   3264   3268   -106     98     72       C  
ATOM   3549  C   GLU A 428      16.145  10.667 -51.538  1.00 28.13           C  
ANISOU 3549  C   GLU A 428     4059   3336   3296    -99    129    110       C  
ATOM   3550  O   GLU A 428      16.837  11.400 -52.261  1.00 28.87           O  
ANISOU 3550  O   GLU A 428     4134   3423   3414   -110    162    115       O  
ATOM   3551  CB  GLU A 428      17.837  10.242 -49.667  1.00 27.92           C  
ANISOU 3551  CB  GLU A 428     4033   3264   3311   -125     64     24       C  
ATOM   3552  CG  GLU A 428      18.422   9.056 -50.423  1.00 26.03           C  
ANISOU 3552  CG  GLU A 428     3761   3050   3080   -122     42      9       C  
ATOM   3553  CD  GLU A 428      17.956   7.719 -49.882  1.00 30.05           C  
ANISOU 3553  CD  GLU A 428     4277   3573   3566   -114     -8      4       C  
ATOM   3554  OE1 GLU A 428      16.826   7.643 -49.352  1.00 28.98           O  
ANISOU 3554  OE1 GLU A 428     4175   3445   3390   -104    -15     25       O  
ATOM   3555  OE2 GLU A 428      18.726   6.740 -49.993  1.00 33.43           O  
ANISOU 3555  OE2 GLU A 428     4675   4001   4025   -116    -37    -21       O  
ATOM   3556  N   THR A 429      15.157   9.902 -52.011  1.00 26.25           N  
ANISOU 3556  N   THR A 429     3823   3135   3015    -87    118    138       N  
ATOM   3557  CA  THR A 429      14.847   9.866 -53.451  1.00 26.95           C  
ANISOU 3557  CA  THR A 429     3896   3266   3078    -93    141    177       C  
ATOM   3558  C   THR A 429      13.673  10.749 -53.879  1.00 26.23           C  
ANISOU 3558  C   THR A 429     3809   3179   2979    -83    166    250       C  
ATOM   3559  O   THR A 429      13.346  10.804 -55.057  1.00 27.38           O  
ANISOU 3559  O   THR A 429     3943   3364   3097    -96    177    295       O  
ATOM   3560  CB  THR A 429      14.643   8.433 -53.999  1.00 25.41           C  
ANISOU 3560  CB  THR A 429     3695   3118   2843    -99    118    162       C  
ATOM   3561  OG1 THR A 429      13.592   7.787 -53.274  1.00 28.04           O  
ANISOU 3561  OG1 THR A 429     4046   3456   3152    -81     89    170       O  
ATOM   3562  CG2 THR A 429      15.923   7.635 -53.875  1.00 22.07           C  
ANISOU 3562  CG2 THR A 429     3252   2684   2450   -111    104     98       C  
ATOM   3563  N   ILE A 430      13.048  11.441 -52.933  1.00 28.97           N  
ANISOU 3563  N   ILE A 430     4170   3484   3354    -66    175    261       N  
ATOM   3564  CA  ILE A 430      11.946  12.344 -53.267  1.00 28.56           C  
ANISOU 3564  CA  ILE A 430     4111   3422   3321    -52    202    333       C  
ATOM   3565  C   ILE A 430      12.445  13.437 -54.203  1.00 29.47           C  
ANISOU 3565  C   ILE A 430     4206   3528   3464    -65    237    375       C  
ATOM   3566  O   ILE A 430      13.404  14.141 -53.884  1.00 31.34           O  
ANISOU 3566  O   ILE A 430     4443   3726   3739    -73    260    343       O  
ATOM   3567  CB  ILE A 430      11.296  12.951 -52.009  1.00 28.90           C  
ANISOU 3567  CB  ILE A 430     4169   3408   3405    -37    222    323       C  
ATOM   3568  CG1 ILE A 430      10.598  11.846 -51.197  1.00 27.80           C  
ANISOU 3568  CG1 ILE A 430     4051   3283   3228    -29    189    294       C  
ATOM   3569  CG2 ILE A 430      10.304  14.038 -52.399  1.00 27.03           C  
ANISOU 3569  CG2 ILE A 430     3911   3143   3217    -21    260    399       C  
ATOM   3570  CD1 ILE A 430      10.189  12.256 -49.784  1.00 23.12           C  
ANISOU 3570  CD1 ILE A 430     3484   2639   2662    -29    209    260       C  
ATOM   3571  N   ALA A 431      11.797  13.555 -55.362  1.00 30.27           N  
ANISOU 3571  N   ALA A 431     4291   3669   3543    -71    236    450       N  
ATOM   3572  CA  ALA A 431      12.213  14.488 -56.415  1.00 31.01           C  
ANISOU 3572  CA  ALA A 431     4367   3766   3650    -91    262    505       C  
ATOM   3573  C   ALA A 431      11.289  15.693 -56.534  1.00 31.58           C  
ANISOU 3573  C   ALA A 431     4419   3799   3782    -74    285    594       C  
ATOM   3574  O   ALA A 431      11.686  16.741 -57.041  1.00 33.96           O  
ANISOU 3574  O   ALA A 431     4706   4075   4121    -84    315    637       O  
ATOM   3575  CB  ALA A 431      12.308  13.762 -57.755  1.00 30.66           C  
ANISOU 3575  CB  ALA A 431     4319   3800   3531   -128    245    528       C  
ATOM   3576  N   GLY A 432      10.055  15.535 -56.069  1.00 31.85           N  
ANISOU 3576  N   GLY A 432     4448   3824   3831    -48    273    625       N  
ATOM   3577  CA  GLY A 432       9.050  16.590 -56.174  1.00 29.68           C  
ANISOU 3577  CA  GLY A 432     4142   3505   3630    -27    294    715       C  
ATOM   3578  C   GLY A 432       7.661  16.004 -56.294  1.00 29.64           C  
ANISOU 3578  C   GLY A 432     4121   3530   3609    -13    262    767       C  
ATOM   3579  O   GLY A 432       7.438  14.847 -55.923  1.00 27.43           O  
ANISOU 3579  O   GLY A 432     3863   3288   3272    -12    233    715       O  
ATOM   3580  N   THR A 433       6.733  16.807 -56.813  1.00 30.01           N  
ANISOU 3580  N   THR A 433     4128   3558   3716     -2    265    875       N  
ATOM   3581  CA  THR A 433       5.334  16.410 -56.978  1.00 30.10           C  
ANISOU 3581  CA  THR A 433     4113   3592   3732     12    234    940       C  
ATOM   3582  C   THR A 433       4.809  16.767 -58.365  1.00 30.98           C  
ANISOU 3582  C   THR A 433     4187   3750   3833    -11    197   1072       C  
ATOM   3583  O   THR A 433       5.325  17.678 -59.016  1.00 30.39           O  
ANISOU 3583  O   THR A 433     4099   3662   3786    -27    211   1130       O  
ATOM   3584  CB  THR A 433       4.395  17.072 -55.915  1.00 31.67           C  
ANISOU 3584  CB  THR A 433     4287   3699   4047     53    276    944       C  
ATOM   3585  OG1 THR A 433       4.413  18.503 -56.049  1.00 28.19           O  
ANISOU 3585  OG1 THR A 433     3810   3183   3719     65    321   1009       O  
ATOM   3586  CG2 THR A 433       4.811  16.692 -54.504  1.00 29.11           C  
ANISOU 3586  CG2 THR A 433     4006   3336   3719     63    309    817       C  
ATOM   3587  N   PHE A 434       3.787  16.038 -58.811  1.00 31.15           N  
ANISOU 3587  N   PHE A 434     4192   3830   3812    -18    148   1123       N  
ATOM   3588  CA  PHE A 434       3.041  16.402 -60.017  1.00 34.02           C  
ANISOU 3588  CA  PHE A 434     4514   4238   4175    -42    104   1265       C  
ATOM   3589  C   PHE A 434       1.578  16.658 -59.667  1.00 34.97           C  
ANISOU 3589  C   PHE A 434     4580   4317   4390     -4     94   1340       C  
ATOM   3590  O   PHE A 434       1.121  16.303 -58.576  1.00 34.48           O  
ANISOU 3590  O   PHE A 434     4523   4210   4367     32    119   1269       O  
ATOM   3591  CB  PHE A 434       3.178  15.340 -61.131  1.00 31.85           C  
ANISOU 3591  CB  PHE A 434     4263   4085   3754   -103     49   1273       C  
ATOM   3592  CG  PHE A 434       2.591  13.993 -60.782  1.00 31.18           C  
ANISOU 3592  CG  PHE A 434     4195   4049   3605   -101     22   1210       C  
ATOM   3593  CD1 PHE A 434       3.369  13.019 -60.163  1.00 26.57           C  
ANISOU 3593  CD1 PHE A 434     3659   3475   2963   -100     40   1076       C  
ATOM   3594  CD2 PHE A 434       1.269  13.687 -61.102  1.00 30.40           C  
ANISOU 3594  CD2 PHE A 434     4059   3984   3507   -103    -25   1290       C  
ATOM   3595  CE1 PHE A 434       2.837  11.770 -59.849  1.00 28.01           C  
ANISOU 3595  CE1 PHE A 434     3855   3696   3090    -99     17   1022       C  
ATOM   3596  CE2 PHE A 434       0.726  12.441 -60.786  1.00 27.60           C  
ANISOU 3596  CE2 PHE A 434     3720   3672   3094   -103    -46   1231       C  
ATOM   3597  CZ  PHE A 434       1.514  11.478 -60.163  1.00 26.04           C  
ANISOU 3597  CZ  PHE A 434     3574   3482   2839   -101    -24   1096       C  
ATOM   3598  N   LYS A 435       0.855  17.283 -60.592  1.00 37.25           N  
ANISOU 3598  N   LYS A 435     4816   4619   4720    -17     56   1486       N  
ATOM   3599  CA  LYS A 435      -0.561  17.578 -60.404  1.00 38.50           C  
ANISOU 3599  CA  LYS A 435     4908   4736   4985     16     40   1575       C  
ATOM   3600  C   LYS A 435      -1.374  16.306 -60.633  1.00 38.36           C  
ANISOU 3600  C   LYS A 435     4894   4805   4875     -3    -18   1569       C  
ATOM   3601  O   LYS A 435      -1.301  15.704 -61.707  1.00 39.95           O  
ANISOU 3601  O   LYS A 435     5109   5113   4957    -60    -78   1611       O  
ATOM   3602  CB  LYS A 435      -0.998  18.695 -61.353  1.00 38.05           C  
ANISOU 3602  CB  LYS A 435     4784   4662   5011      6     11   1747       C  
ATOM   3603  CG  LYS A 435      -2.334  19.336 -61.006  1.00 43.19           C  
ANISOU 3603  CG  LYS A 435     5351   5232   5829     53     14   1842       C  
ATOM   3604  CD  LYS A 435      -2.418  20.793 -61.503  1.00 49.61           C  
ANISOU 3604  CD  LYS A 435     6098   5970   6780     63     23   1983       C  
ATOM   3605  CE  LYS A 435      -2.619  20.896 -63.017  1.00 47.22           C  
ANISOU 3605  CE  LYS A 435     5769   5761   6411      3    -72   2147       C  
ATOM   3606  NZ  LYS A 435      -2.939  22.288 -63.434  1.00 48.32           N  
ANISOU 3606  NZ  LYS A 435     5829   5819   6711     18    -72   2306       N  
ATOM   3607  N   VAL A 436      -2.146  15.908 -59.622  1.00 37.51           N  
ANISOU 3607  N   VAL A 436     4777   4653   4823     39      5   1514       N  
ATOM   3608  CA  VAL A 436      -2.838  14.614 -59.638  1.00 37.56           C  
ANISOU 3608  CA  VAL A 436     4794   4732   4744     26    -38   1483       C  
ATOM   3609  C   VAL A 436      -4.224  14.667 -60.269  1.00 37.89           C  
ANISOU 3609  C   VAL A 436     4764   4800   4832     21    -97   1617       C  
ATOM   3610  O   VAL A 436      -5.034  15.540 -59.954  1.00 40.41           O  
ANISOU 3610  O   VAL A 436     5016   5035   5303     62    -78   1692       O  
ATOM   3611  CB  VAL A 436      -2.952  13.971 -58.220  1.00 37.45           C  
ANISOU 3611  CB  VAL A 436     4815   4669   4746     64     12   1348       C  
ATOM   3612  CG1 VAL A 436      -1.598  13.818 -57.601  1.00 37.54           C  
ANISOU 3612  CG1 VAL A 436     4894   4663   4705     62     56   1223       C  
ATOM   3613  CG2 VAL A 436      -3.854  14.799 -57.299  1.00 41.20           C  
ANISOU 3613  CG2 VAL A 436     5238   5031   5387    116     66   1369       C  
ATOM   3614  N   ALA A 437      -4.475  13.718 -61.163  1.00 37.15           N  
ANISOU 3614  N   ALA A 437     4682   4822   4612    -32   -166   1643       N  
ATOM   3615  CA  ALA A 437      -5.795  13.481 -61.719  1.00 37.81           C  
ANISOU 3615  CA  ALA A 437     4704   4949   4713    -46   -232   1753       C  
ATOM   3616  C   ALA A 437      -6.506  12.458 -60.817  1.00 39.39           C  
ANISOU 3616  C   ALA A 437     4915   5143   4910    -18   -217   1660       C  
ATOM   3617  O   ALA A 437      -5.851  11.800 -60.015  1.00 37.55           O  
ANISOU 3617  O   ALA A 437     4746   4898   4625     -5   -171   1520       O  
ATOM   3618  CB  ALA A 437      -5.660  12.951 -63.124  1.00 36.89           C  
ANISOU 3618  CB  ALA A 437     4602   4966   4448   -131   -310   1818       C  
ATOM   3619  N   PRO A 438      -7.846  12.336 -60.925  1.00 40.62           N  
ANISOU 3619  N   PRO A 438     5004   5303   5128    -10   -257   1741       N  
ATOM   3620  CA  PRO A 438      -8.529  11.302 -60.146  1.00 41.60           C  
ANISOU 3620  CA  PRO A 438     5140   5428   5238      9   -244   1654       C  
ATOM   3621  C   PRO A 438      -8.015   9.911 -60.477  1.00 41.69           C  
ANISOU 3621  C   PRO A 438     5224   5546   5070    -41   -269   1561       C  
ATOM   3622  O   PRO A 438      -7.691   9.633 -61.634  1.00 41.11           O  
ANISOU 3622  O   PRO A 438     5164   5572   4885   -107   -324   1606       O  
ATOM   3623  CB  PRO A 438      -9.989  11.446 -60.573  1.00 42.83           C  
ANISOU 3623  CB  PRO A 438     5204   5592   5477     10   -299   1784       C  
ATOM   3624  CG  PRO A 438     -10.117  12.893 -60.935  1.00 43.01           C  
ANISOU 3624  CG  PRO A 438     5156   5547   5638     30   -303   1918       C  
ATOM   3625  CD  PRO A 438      -8.802  13.251 -61.579  1.00 42.71           C  
ANISOU 3625  CD  PRO A 438     5173   5548   5507     -8   -305   1915       C  
ATOM   3626  N   LEU A 439      -7.942   9.058 -59.454  1.00 40.34           N  
ANISOU 3626  N   LEU A 439     5098   5351   4877    -16   -226   1430       N  
ATOM   3627  CA  LEU A 439      -7.372   7.720 -59.569  1.00 39.71           C  
ANISOU 3627  CA  LEU A 439     5087   5350   4651    -55   -236   1326       C  
ATOM   3628  C   LEU A 439      -7.945   6.895 -60.720  1.00 41.23           C  
ANISOU 3628  C   LEU A 439     5266   5661   4741   -121   -308   1379       C  
ATOM   3629  O   LEU A 439      -7.204   6.174 -61.396  1.00 41.71           O  
ANISOU 3629  O   LEU A 439     5373   5801   4673   -177   -322   1332       O  
ATOM   3630  CB  LEU A 439      -7.527   6.957 -58.248  1.00 39.75           C  
ANISOU 3630  CB  LEU A 439     5127   5304   4672    -15   -187   1206       C  
ATOM   3631  CG  LEU A 439      -6.818   5.600 -58.161  1.00 39.31           C  
ANISOU 3631  CG  LEU A 439     5141   5306   4491    -44   -187   1090       C  
ATOM   3632  CD1 LEU A 439      -5.299   5.759 -58.079  1.00 36.90           C  
ANISOU 3632  CD1 LEU A 439     4888   4988   4143    -50   -157   1021       C  
ATOM   3633  CD2 LEU A 439      -7.347   4.798 -56.985  1.00 38.50           C  
ANISOU 3633  CD2 LEU A 439     5058   5163   4407    -13   -157   1006       C  
ATOM   3634  N   HIS A 440      -9.254   6.994 -60.944  1.00 42.79           N  
ANISOU 3634  N   HIS A 440     5396   5867   4996   -119   -350   1473       N  
ATOM   3635  CA  HIS A 440      -9.881   6.267 -62.056  1.00 45.31           C  
ANISOU 3635  CA  HIS A 440     5697   6303   5216   -190   -425   1533       C  
ATOM   3636  C   HIS A 440      -9.320   6.661 -63.424  1.00 43.30           C  
ANISOU 3636  C   HIS A 440     5446   6134   4873   -265   -476   1617       C  
ATOM   3637  O   HIS A 440      -9.312   5.849 -64.351  1.00 43.52           O  
ANISOU 3637  O   HIS A 440     5496   6273   4767   -346   -519   1614       O  
ATOM   3638  CB  HIS A 440     -11.418   6.341 -62.011  1.00 48.69           C  
ANISOU 3638  CB  HIS A 440     6043   6721   5734   -174   -466   1625       C  
ATOM   3639  CG  HIS A 440     -12.051   5.135 -61.381  1.00 55.84           C  
ANISOU 3639  CG  HIS A 440     6965   7638   6614   -166   -453   1534       C  
ATOM   3640  ND1 HIS A 440     -12.362   5.067 -60.037  1.00 59.70           N  
ANISOU 3640  ND1 HIS A 440     7457   8029   7197    -96   -387   1456       N  
ATOM   3641  CD2 HIS A 440     -12.396   3.933 -61.906  1.00 58.65           C  
ANISOU 3641  CD2 HIS A 440     7339   8092   6855   -224   -491   1502       C  
ATOM   3642  CE1 HIS A 440     -12.885   3.884 -59.767  1.00 60.45           C  
ANISOU 3642  CE1 HIS A 440     7569   8159   7238   -109   -390   1388       C  
ATOM   3643  NE2 HIS A 440     -12.915   3.176 -60.883  1.00 60.09           N  
ANISOU 3643  NE2 HIS A 440     7531   8230   7069   -184   -451   1413       N  
ATOM   3644  N   ASP A 441      -8.828   7.896 -63.526  1.00 41.86           N  
ANISOU 3644  N   ASP A 441     5246   5897   4762   -244   -464   1685       N  
ATOM   3645  CA  ASP A 441      -8.173   8.383 -64.741  1.00 42.09           C  
ANISOU 3645  CA  ASP A 441     5285   5996   4711   -314   -502   1762       C  
ATOM   3646  C   ASP A 441      -6.854   7.667 -65.023  1.00 39.89           C  
ANISOU 3646  C   ASP A 441     5093   5771   4292   -362   -466   1639       C  
ATOM   3647  O   ASP A 441      -6.528   7.399 -66.186  1.00 41.58           O  
ANISOU 3647  O   ASP A 441     5329   6089   4381   -453   -503   1668       O  
ATOM   3648  CB  ASP A 441      -7.954   9.897 -64.674  1.00 43.17           C  
ANISOU 3648  CB  ASP A 441     5381   6048   4974   -273   -488   1860       C  
ATOM   3649  CG  ASP A 441      -9.249  10.684 -64.797  1.00 46.74           C  
ANISOU 3649  CG  ASP A 441     5734   6463   5564   -247   -538   2018       C  
ATOM   3650  OD1 ASP A 441     -10.324  10.076 -64.991  1.00 48.28           O  
ANISOU 3650  OD1 ASP A 441     5889   6706   5749   -266   -591   2059       O  
ATOM   3651  OD2 ASP A 441      -9.187  11.925 -64.699  1.00 50.38           O  
ANISOU 3651  OD2 ASP A 441     6149   6841   6151   -209   -524   2104       O  
ATOM   3652  N   TYR A 442      -6.101   7.362 -63.965  1.00 35.89           N  
ANISOU 3652  N   TYR A 442     4633   5195   3810   -306   -394   1502       N  
ATOM   3653  CA  TYR A 442      -4.889   6.556 -64.105  1.00 32.64           C  
ANISOU 3653  CA  TYR A 442     4293   4822   3287   -344   -357   1376       C  
ATOM   3654  C   TYR A 442      -5.227   5.093 -64.390  1.00 32.85           C  
ANISOU 3654  C   TYR A 442     4345   4931   3207   -394   -373   1305       C  
ATOM   3655  O   TYR A 442      -4.608   4.473 -65.253  1.00 33.72           O  
ANISOU 3655  O   TYR A 442     4492   5122   3198   -472   -373   1263       O  
ATOM   3656  CB  TYR A 442      -3.964   6.707 -62.889  1.00 30.64           C  
ANISOU 3656  CB  TYR A 442     4076   4468   3099   -273   -285   1265       C  
ATOM   3657  CG  TYR A 442      -3.481   8.128 -62.688  1.00 28.52           C  
ANISOU 3657  CG  TYR A 442     3789   4123   2925   -235   -261   1321       C  
ATOM   3658  CD1 TYR A 442      -2.589   8.719 -63.589  1.00 31.99           C  
ANISOU 3658  CD1 TYR A 442     4242   4594   3317   -283   -262   1358       C  
ATOM   3659  CD2 TYR A 442      -3.933   8.892 -61.614  1.00 28.55           C  
ANISOU 3659  CD2 TYR A 442     3762   4020   3066   -158   -230   1335       C  
ATOM   3660  CE1 TYR A 442      -2.156  10.038 -63.421  1.00 28.42           C  
ANISOU 3660  CE1 TYR A 442     3772   4069   2957   -249   -238   1412       C  
ATOM   3661  CE2 TYR A 442      -3.503  10.211 -61.436  1.00 29.78           C  
ANISOU 3661  CE2 TYR A 442     3899   4101   3316   -127   -201   1383       C  
ATOM   3662  CZ  TYR A 442      -2.617  10.770 -62.342  1.00 28.64           C  
ANISOU 3662  CZ  TYR A 442     3767   3989   3125   -170   -207   1423       C  
ATOM   3663  OH  TYR A 442      -2.198  12.066 -62.167  1.00 32.55           O  
ANISOU 3663  OH  TYR A 442     4243   4407   3718   -140   -175   1470       O  
ATOM   3664  N   ILE A 443      -6.226   4.557 -63.686  1.00 33.26           N  
ANISOU 3664  N   ILE A 443     4373   4959   3304   -355   -381   1290       N  
ATOM   3665  CA  ILE A 443      -6.676   3.178 -63.890  1.00 31.50           C  
ANISOU 3665  CA  ILE A 443     4167   4806   2993   -398   -395   1226       C  
ATOM   3666  C   ILE A 443      -7.097   2.936 -65.339  1.00 33.84           C  
ANISOU 3666  C   ILE A 443     4451   5227   3178   -503   -457   1303       C  
ATOM   3667  O   ILE A 443      -6.797   1.886 -65.911  1.00 32.63           O  
ANISOU 3667  O   ILE A 443     4336   5152   2910   -575   -450   1228       O  
ATOM   3668  CB  ILE A 443      -7.824   2.790 -62.915  1.00 31.46           C  
ANISOU 3668  CB  ILE A 443     4132   4753   3068   -339   -396   1216       C  
ATOM   3669  CG1 ILE A 443      -7.310   2.785 -61.466  1.00 32.16           C  
ANISOU 3669  CG1 ILE A 443     4252   4733   3235   -256   -330   1116       C  
ATOM   3670  CG2 ILE A 443      -8.402   1.412 -63.273  1.00 27.92           C  
ANISOU 3670  CG2 ILE A 443     3696   4386   2528   -393   -417   1167       C  
ATOM   3671  CD1 ILE A 443      -8.383   3.012 -60.399  1.00 30.79           C  
ANISOU 3671  CD1 ILE A 443     4040   4482   3176   -188   -319   1134       C  
ATOM   3672  N   ASN A 444      -7.772   3.921 -65.927  1.00 37.32           N  
ANISOU 3672  N   ASN A 444     4836   5686   3656   -518   -515   1454       N  
ATOM   3673  CA  ASN A 444      -8.280   3.806 -67.293  1.00 41.79           C  
ANISOU 3673  CA  ASN A 444     5385   6376   4118   -625   -589   1552       C  
ATOM   3674  C   ASN A 444      -7.363   4.390 -68.365  1.00 42.57           C  
ANISOU 3674  C   ASN A 444     5511   6532   4131   -703   -597   1597       C  
ATOM   3675  O   ASN A 444      -7.746   4.496 -69.535  1.00 44.86           O  
ANISOU 3675  O   ASN A 444     5787   6925   4332   -801   -663   1698       O  
ATOM   3676  CB  ASN A 444      -9.702   4.378 -67.386  1.00 44.17           C  
ANISOU 3676  CB  ASN A 444     5602   6676   4506   -609   -663   1704       C  
ATOM   3677  CG  ASN A 444     -10.701   3.562 -66.577  1.00 47.89           C  
ANISOU 3677  CG  ASN A 444     6049   7120   5027   -562   -660   1653       C  
ATOM   3678  OD1 ASN A 444     -10.960   2.398 -66.890  1.00 48.61           O  
ANISOU 3678  OD1 ASN A 444     6164   7288   5017   -620   -669   1588       O  
ATOM   3679  ND2 ASN A 444     -11.240   4.159 -65.513  1.00 46.91           N  
ANISOU 3679  ND2 ASN A 444     5879   6882   5061   -461   -637   1675       N  
ATOM   3680  N   ALA A 445      -6.152   4.766 -67.957  1.00 41.92           N  
ANISOU 3680  N   ALA A 445     5469   6385   4074   -664   -530   1523       N  
ATOM   3681  CA  ALA A 445      -5.120   5.245 -68.881  1.00 42.29           C  
ANISOU 3681  CA  ALA A 445     5550   6477   4040   -736   -520   1540       C  
ATOM   3682  C   ALA A 445      -5.526   6.494 -69.684  1.00 43.93           C  
ANISOU 3682  C   ALA A 445     5713   6710   4270   -769   -588   1725       C  
ATOM   3683  O   ALA A 445      -5.114   6.659 -70.837  1.00 44.25           O  
ANISOU 3683  O   ALA A 445     5776   6839   4198   -873   -611   1773       O  
ATOM   3684  CB  ALA A 445      -4.667   4.106 -69.822  1.00 41.74           C  
ANISOU 3684  CB  ALA A 445     5535   6522   3802   -854   -507   1452       C  
ATOM   3685  N   VAL A 446      -6.326   7.368 -69.074  1.00 44.59           N  
ANISOU 3685  N   VAL A 446     5729   6712   4502   -685   -615   1827       N  
ATOM   3686  CA  VAL A 446      -6.752   8.610 -69.742  1.00 46.11           C  
ANISOU 3686  CA  VAL A 446     5865   6908   4747   -704   -680   2015       C  
ATOM   3687  C   VAL A 446      -6.093   9.874 -69.179  1.00 45.27           C  
ANISOU 3687  C   VAL A 446     5747   6684   4772   -625   -633   2041       C  
ATOM   3688  O   VAL A 446      -6.069  10.914 -69.843  1.00 46.72           O  
ANISOU 3688  O   VAL A 446     5899   6871   4981   -652   -671   2180       O  
ATOM   3689  CB  VAL A 446      -8.298   8.770 -69.783  1.00 47.93           C  
ANISOU 3689  CB  VAL A 446     6010   7146   5056   -691   -762   2152       C  
ATOM   3690  CG1 VAL A 446      -8.922   7.695 -70.664  1.00 47.52           C  
ANISOU 3690  CG1 VAL A 446     5969   7235   4854   -799   -826   2159       C  
ATOM   3691  CG2 VAL A 446      -8.901   8.744 -68.376  1.00 48.67           C  
ANISOU 3691  CG2 VAL A 446     6066   7118   5309   -567   -719   2096       C  
ATOM   3692  N   ALA A 447      -5.559   9.786 -67.964  1.00 42.62           N  
ANISOU 3692  N   ALA A 447     5434   6246   4514   -533   -551   1912       N  
ATOM   3693  CA  ALA A 447      -4.835  10.912 -67.383  1.00 41.82           C  
ANISOU 3693  CA  ALA A 447     5329   6035   4527   -465   -497   1914       C  
ATOM   3694  C   ALA A 447      -3.509  11.142 -68.106  1.00 41.50           C  
ANISOU 3694  C   ALA A 447     5345   6034   4389   -528   -470   1884       C  
ATOM   3695  O   ALA A 447      -2.921  10.205 -68.665  1.00 37.93           O  
ANISOU 3695  O   ALA A 447     4949   5669   3792   -602   -460   1797       O  
ATOM   3696  CB  ALA A 447      -4.604  10.697 -65.904  1.00 39.00           C  
ANISOU 3696  CB  ALA A 447     4987   5569   4261   -367   -421   1780       C  
ATOM   3697  N   GLU A 448      -3.058  12.397 -68.105  1.00 42.92           N  
ANISOU 3697  N   GLU A 448     5506   6146   4656   -500   -453   1956       N  
ATOM   3698  CA  GLU A 448      -1.777  12.756 -68.704  1.00 44.76           C  
ANISOU 3698  CA  GLU A 448     5788   6401   4817   -552   -419   1930       C  
ATOM   3699  C   GLU A 448      -0.624  12.074 -67.964  1.00 42.02           C  
ANISOU 3699  C   GLU A 448     5504   6021   4440   -523   -336   1738       C  
ATOM   3700  O   GLU A 448      -0.709  11.816 -66.755  1.00 38.56           O  
ANISOU 3700  O   GLU A 448     5065   5504   4084   -439   -297   1648       O  
ATOM   3701  CB  GLU A 448      -1.587  14.280 -68.766  1.00 47.20           C  
ANISOU 3701  CB  GLU A 448     6058   6632   5243   -520   -414   2048       C  
ATOM   3702  CG  GLU A 448      -1.399  14.995 -67.420  1.00 50.99           C  
ANISOU 3702  CG  GLU A 448     6516   6963   5893   -405   -346   1994       C  
ATOM   3703  CD  GLU A 448      -1.213  16.514 -67.568  1.00 57.93           C  
ANISOU 3703  CD  GLU A 448     7354   7763   6892   -382   -336   2113       C  
ATOM   3704  OE1 GLU A 448      -1.002  16.993 -68.712  1.00 58.29           O  
ANISOU 3704  OE1 GLU A 448     7399   7871   6878   -457   -378   2226       O  
ATOM   3705  OE2 GLU A 448      -1.272  17.228 -66.537  1.00 56.48           O  
ANISOU 3705  OE2 GLU A 448     7141   7457   6864   -294   -283   2092       O  
ATOM   3706  N   ARG A 449       0.437  11.767 -68.706  1.00 40.69           N  
ANISOU 3706  N   ARG A 449     5390   5917   4155   -599   -311   1679       N  
ATOM   3707  CA  ARG A 449       1.623  11.138 -68.137  1.00 39.12           C  
ANISOU 3707  CA  ARG A 449     5242   5687   3933   -581   -237   1508       C  
ATOM   3708  C   ARG A 449       2.206  12.048 -67.041  1.00 36.23           C  
ANISOU 3708  C   ARG A 449     4867   5194   3705   -485   -184   1476       C  
ATOM   3709  O   ARG A 449       2.467  13.227 -67.292  1.00 37.19           O  
ANISOU 3709  O   ARG A 449     4970   5277   3883   -482   -180   1562       O  
ATOM   3710  CB  ARG A 449       2.646  10.855 -69.246  1.00 40.30           C  
ANISOU 3710  CB  ARG A 449     5441   5920   3951   -685   -214   1469       C  
ATOM   3711  CG  ARG A 449       3.641   9.767 -68.901  1.00 42.41           C  
ANISOU 3711  CG  ARG A 449     5754   6187   4172   -690   -150   1290       C  
ATOM   3712  CD  ARG A 449       4.287   9.154 -70.144  1.00 45.92           C  
ANISOU 3712  CD  ARG A 449     6241   6735   4470   -814   -130   1247       C  
ATOM   3713  NE  ARG A 449       5.221   8.090 -69.767  1.00 45.88           N  
ANISOU 3713  NE  ARG A 449     6269   6716   4448   -812    -63   1075       N  
ATOM   3714  CZ  ARG A 449       6.542   8.229 -69.702  1.00 43.78           C  
ANISOU 3714  CZ  ARG A 449     6025   6411   4200   -813      2    988       C  
ATOM   3715  NH1 ARG A 449       7.110   9.382 -70.013  1.00 46.99           N  
ANISOU 3715  NH1 ARG A 449     6430   6793   4631   -821     15   1051       N  
ATOM   3716  NH2 ARG A 449       7.304   7.205 -69.340  1.00 44.11           N  
ANISOU 3716  NH2 ARG A 449     6085   6434   4241   -809     57    841       N  
ATOM   3717  N   PRO A 450       2.384  11.511 -65.818  1.00 34.20           N  
ANISOU 3717  N   PRO A 450     4621   4871   3501   -414   -146   1356       N  
ATOM   3718  CA  PRO A 450       2.863  12.325 -64.690  1.00 33.01           C  
ANISOU 3718  CA  PRO A 450     4464   4604   3475   -332    -97   1319       C  
ATOM   3719  C   PRO A 450       4.222  12.983 -64.923  1.00 32.85           C  
ANISOU 3719  C   PRO A 450     4468   4558   3454   -350    -51   1287       C  
ATOM   3720  O   PRO A 450       4.383  14.175 -64.640  1.00 33.97           O  
ANISOU 3720  O   PRO A 450     4588   4626   3693   -314    -30   1340       O  
ATOM   3721  CB  PRO A 450       2.944  11.315 -63.540  1.00 31.21           C  
ANISOU 3721  CB  PRO A 450     4258   4343   3256   -284    -72   1185       C  
ATOM   3722  CG  PRO A 450       1.939  10.285 -63.887  1.00 31.45           C  
ANISOU 3722  CG  PRO A 450     4284   4448   3220   -312   -118   1199       C  
ATOM   3723  CD  PRO A 450       1.998  10.155 -65.381  1.00 31.46           C  
ANISOU 3723  CD  PRO A 450     4291   4554   3107   -408   -151   1262       C  
ATOM   3724  N   SER A 451       5.185  12.223 -65.442  1.00 31.70           N  
ANISOU 3724  N   SER A 451     4364   4470   3211   -406    -29   1199       N  
ATOM   3725  CA  SER A 451       6.543  12.733 -65.634  1.00 31.53           C  
ANISOU 3725  CA  SER A 451     4365   4424   3191   -425     20   1152       C  
ATOM   3726  C   SER A 451       7.274  12.021 -66.758  1.00 32.60           C  
ANISOU 3726  C   SER A 451     4535   4651   3201   -520     33   1106       C  
ATOM   3727  O   SER A 451       7.106  10.811 -66.957  1.00 31.58           O  
ANISOU 3727  O   SER A 451     4423   4581   2996   -553     27   1040       O  
ATOM   3728  CB  SER A 451       7.370  12.605 -64.346  1.00 29.67           C  
ANISOU 3728  CB  SER A 451     4142   4103   3029   -358     67   1028       C  
ATOM   3729  OG  SER A 451       8.682  13.120 -64.532  1.00 27.06           O  
ANISOU 3729  OG  SER A 451     3828   3748   2708   -376    113    985       O  
ATOM   3730  N   ASP A 452       8.091  12.792 -67.469  1.00 32.20           N  
ANISOU 3730  N   ASP A 452     4494   4606   3134   -565     59   1136       N  
ATOM   3731  CA  ASP A 452       9.022  12.271 -68.467  1.00 34.46           C  
ANISOU 3731  CA  ASP A 452     4816   4963   3316   -659     94   1075       C  
ATOM   3732  C   ASP A 452      10.453  12.191 -67.908  1.00 30.79           C  
ANISOU 3732  C   ASP A 452     4365   4435   2899   -633    162    945       C  
ATOM   3733  O   ASP A 452      11.396  11.900 -68.633  1.00 31.47           O  
ANISOU 3733  O   ASP A 452     4474   4557   2924   -702    206    883       O  
ATOM   3734  CB  ASP A 452       8.989  13.147 -69.725  1.00 36.57           C  
ANISOU 3734  CB  ASP A 452     5086   5286   3522   -742     78   1198       C  
ATOM   3735  CG  ASP A 452       7.727  12.954 -70.553  1.00 44.27           C  
ANISOU 3735  CG  ASP A 452     6051   6353   4415   -801      6   1318       C  
ATOM   3736  OD1 ASP A 452       7.265  11.802 -70.694  1.00 49.22           O  
ANISOU 3736  OD1 ASP A 452     6690   7042   4969   -832    -10   1265       O  
ATOM   3737  OD2 ASP A 452       7.206  13.956 -71.089  1.00 49.14           O  
ANISOU 3737  OD2 ASP A 452     6647   6980   5045   -821    -37   1468       O  
ATOM   3738  N   VAL A 453      10.604  12.440 -66.610  1.00 30.39           N  
ANISOU 3738  N   VAL A 453     4300   4291   2958   -539    171    902       N  
ATOM   3739  CA  VAL A 453      11.925  12.491 -65.971  1.00 28.71           C  
ANISOU 3739  CA  VAL A 453     4093   4012   2803   -510    224    793       C  
ATOM   3740  C   VAL A 453      12.020  11.549 -64.770  1.00 27.88           C  
ANISOU 3740  C   VAL A 453     3987   3864   2743   -449    223    687       C  
ATOM   3741  O   VAL A 453      12.996  10.809 -64.632  1.00 29.82           O  
ANISOU 3741  O   VAL A 453     4240   4103   2988   -459    256    579       O  
ATOM   3742  CB  VAL A 453      12.280  13.932 -65.517  1.00 28.54           C  
ANISOU 3742  CB  VAL A 453     4056   3910   2877   -467    242    843       C  
ATOM   3743  CG1 VAL A 453      13.626  13.968 -64.785  1.00 29.93           C  
ANISOU 3743  CG1 VAL A 453     4237   4021   3116   -439    290    730       C  
ATOM   3744  CG2 VAL A 453      12.307  14.882 -66.707  1.00 29.70           C  
ANISOU 3744  CG2 VAL A 453     4204   4094   2986   -530    245    951       C  
ATOM   3745  N   TYR A 454      11.000  11.575 -63.914  1.00 25.93           N  
ANISOU 3745  N   TYR A 454     3727   3587   2539   -388    186    722       N  
ATOM   3746  CA  TYR A 454      11.045  10.890 -62.627  1.00 25.07           C  
ANISOU 3746  CA  TYR A 454     3619   3427   2478   -327    182    637       C  
ATOM   3747  C   TYR A 454      10.076   9.729 -62.556  1.00 24.74           C  
ANISOU 3747  C   TYR A 454     3581   3431   2389   -327    148    627       C  
ATOM   3748  O   TYR A 454       9.194   9.600 -63.404  1.00 24.83           O  
ANISOU 3748  O   TYR A 454     3588   3508   2338   -366    121    697       O  
ATOM   3749  CB  TYR A 454      10.743  11.876 -61.500  1.00 24.00           C  
ANISOU 3749  CB  TYR A 454     3472   3208   2440   -259    181    667       C  
ATOM   3750  CG  TYR A 454      11.694  13.045 -61.455  1.00 23.07           C  
ANISOU 3750  CG  TYR A 454     3350   3038   2379   -256    219    671       C  
ATOM   3751  CD1 TYR A 454      13.053  12.852 -61.206  1.00 22.89           C  
ANISOU 3751  CD1 TYR A 454     3336   2991   2372   -263    250    577       C  
ATOM   3752  CD2 TYR A 454      11.237  14.347 -61.664  1.00 23.78           C  
ANISOU 3752  CD2 TYR A 454     3423   3097   2517   -246    224    772       C  
ATOM   3753  CE1 TYR A 454      13.940  13.932 -61.158  1.00 27.96           C  
ANISOU 3753  CE1 TYR A 454     3972   3583   3067   -263    286    578       C  
ATOM   3754  CE2 TYR A 454      12.113  15.433 -61.617  1.00 28.75           C  
ANISOU 3754  CE2 TYR A 454     4048   3674   3203   -245    263    774       C  
ATOM   3755  CZ  TYR A 454      13.456  15.219 -61.361  1.00 29.85           C  
ANISOU 3755  CZ  TYR A 454     4200   3794   3348   -255    294    674       C  
ATOM   3756  OH  TYR A 454      14.318  16.292 -61.318  1.00 38.21           O  
ANISOU 3756  OH  TYR A 454     5253   4802   4463   -256    333    674       O  
ATOM   3757  N   SER A 455      10.259   8.889 -61.540  1.00 24.23           N  
ANISOU 3757  N   SER A 455     3521   3332   2353   -287    146    542       N  
ATOM   3758  CA  SER A 455       9.419   7.720 -61.326  1.00 26.36           C  
ANISOU 3758  CA  SER A 455     3794   3634   2587   -282    118    520       C  
ATOM   3759  C   SER A 455       8.254   8.086 -60.399  1.00 26.56           C  
ANISOU 3759  C   SER A 455     3811   3622   2657   -225     89    572       C  
ATOM   3760  O   SER A 455       8.461   8.659 -59.326  1.00 26.64           O  
ANISOU 3760  O   SER A 455     3823   3561   2740   -177     98    556       O  
ATOM   3761  CB  SER A 455      10.251   6.567 -60.751  1.00 25.79           C  
ANISOU 3761  CB  SER A 455     3729   3541   2527   -274    130    406       C  
ATOM   3762  OG  SER A 455       9.416   5.531 -60.251  1.00 26.42           O  
ANISOU 3762  OG  SER A 455     3813   3633   2592   -255    103    386       O  
ATOM   3763  N   CYS A 456       7.035   7.748 -60.811  1.00 25.98           N  
ANISOU 3763  N   CYS A 456     3729   3597   2544   -237     57    630       N  
ATOM   3764  CA  CYS A 456       5.846   8.299 -60.161  1.00 26.22           C  
ANISOU 3764  CA  CYS A 456     3742   3593   2627   -190     37    697       C  
ATOM   3765  C   CYS A 456       4.897   7.306 -59.498  1.00 25.32           C  
ANISOU 3765  C   CYS A 456     3631   3485   2505   -166     14    671       C  
ATOM   3766  O   CYS A 456       4.870   6.119 -59.831  1.00 24.86           O  
ANISOU 3766  O   CYS A 456     3584   3478   2384   -195      3    624       O  
ATOM   3767  CB  CYS A 456       5.062   9.151 -61.159  1.00 26.47           C  
ANISOU 3767  CB  CYS A 456     3747   3661   2649   -217     15    822       C  
ATOM   3768  SG  CYS A 456       6.067  10.375 -61.983  1.00 31.29           S  
ANISOU 3768  SG  CYS A 456     4355   4265   3268   -249     41    869       S  
ATOM   3769  N   SER A 457       4.125   7.829 -58.549  1.00 25.65           N  
ANISOU 3769  N   SER A 457     3662   3470   2616   -116     13    699       N  
ATOM   3770  CA  SER A 457       2.970   7.149 -57.979  1.00 25.47           C  
ANISOU 3770  CA  SER A 457     3634   3449   2596    -94     -6    699       C  
ATOM   3771  C   SER A 457       1.771   8.075 -58.133  1.00 25.45           C  
ANISOU 3771  C   SER A 457     3591   3430   2648    -76    -17    805       C  
ATOM   3772  O   SER A 457       1.915   9.283 -57.968  1.00 27.47           O  
ANISOU 3772  O   SER A 457     3830   3631   2975    -56      6    848       O  
ATOM   3773  CB  SER A 457       3.202   6.842 -56.499  1.00 24.80           C  
ANISOU 3773  CB  SER A 457     3573   3297   2551    -53     12    618       C  
ATOM   3774  OG  SER A 457       1.980   6.510 -55.852  1.00 28.24           O  
ANISOU 3774  OG  SER A 457     4002   3720   3007    -28      3    630       O  
ATOM   3775  N   PRO A 458       0.580   7.513 -58.435  1.00 26.13           N  
ANISOU 3775  N   PRO A 458     3657   3559   2711    -84    -50    848       N  
ATOM   3776  CA  PRO A 458      -0.662   8.273 -58.643  1.00 26.61           C  
ANISOU 3776  CA  PRO A 458     3668   3608   2835    -69    -67    958       C  
ATOM   3777  C   PRO A 458      -1.125   9.135 -57.456  1.00 27.70           C  
ANISOU 3777  C   PRO A 458     3788   3643   3093    -10    -28    961       C  
ATOM   3778  O   PRO A 458      -2.149   9.816 -57.563  1.00 29.05           O  
ANISOU 3778  O   PRO A 458     3909   3789   3341      7    -35   1050       O  
ATOM   3779  CB  PRO A 458      -1.701   7.175 -58.937  1.00 25.59           C  
ANISOU 3779  CB  PRO A 458     3530   3543   2651    -88   -107    966       C  
ATOM   3780  CG  PRO A 458      -1.113   5.944 -58.386  1.00 27.49           C  
ANISOU 3780  CG  PRO A 458     3818   3794   2834    -92    -94    847       C  
ATOM   3781  CD  PRO A 458       0.350   6.070 -58.624  1.00 25.78           C  
ANISOU 3781  CD  PRO A 458     3632   3577   2587   -111    -72    795       C  
ATOM   3782  N   ASN A 459      -0.390   9.117 -56.344  1.00 25.74           N  
ANISOU 3782  N   ASN A 459     3578   3337   2866     14     13    866       N  
ATOM   3783  CA  ASN A 459      -0.682  10.048 -55.253  1.00 24.92           C  
ANISOU 3783  CA  ASN A 459     3463   3136   2870     55     62    859       C  
ATOM   3784  C   ASN A 459      -0.072  11.430 -55.497  1.00 24.64           C  
ANISOU 3784  C   ASN A 459     3409   3051   2901     60     92    903       C  
ATOM   3785  O   ASN A 459      -0.363  12.381 -54.765  1.00 23.59           O  
ANISOU 3785  O   ASN A 459     3257   2833   2872     89    140    910       O  
ATOM   3786  CB  ASN A 459      -0.256   9.480 -53.891  1.00 25.11           C  
ANISOU 3786  CB  ASN A 459     3538   3121   2883     67     91    744       C  
ATOM   3787  CG  ASN A 459       1.235   9.603 -53.633  1.00 25.57           C  
ANISOU 3787  CG  ASN A 459     3635   3168   2914     56    105    676       C  
ATOM   3788  OD1 ASN A 459       2.058   9.429 -54.536  1.00 28.58           O  
ANISOU 3788  OD1 ASN A 459     4021   3597   3242     31     83    682       O  
ATOM   3789  ND2 ASN A 459       1.592   9.882 -52.382  1.00 25.33           N  
ANISOU 3789  ND2 ASN A 459     3633   3072   2917     67    142    608       N  
ATOM   3790  N   GLY A 460       0.760  11.537 -56.534  1.00 23.38           N  
ANISOU 3790  N   GLY A 460     3255   2942   2686     28     70    930       N  
ATOM   3791  CA  GLY A 460       1.409  12.810 -56.881  1.00 23.20           C  
ANISOU 3791  CA  GLY A 460     3217   2879   2720     28     96    976       C  
ATOM   3792  C   GLY A 460       2.892  12.884 -56.585  1.00 22.88           C  
ANISOU 3792  C   GLY A 460     3218   2824   2650     17    123    890       C  
ATOM   3793  O   GLY A 460       3.521  13.904 -56.836  1.00 23.49           O  
ANISOU 3793  O   GLY A 460     3286   2866   2771     14    148    917       O  
ATOM   3794  N   MET A 461       3.461  11.808 -56.054  1.00 23.69           N  
ANISOU 3794  N   MET A 461     3363   2950   2686     10    116    789       N  
ATOM   3795  CA  MET A 461       4.877  11.811 -55.688  1.00 25.06           C  
ANISOU 3795  CA  MET A 461     3571   3107   2843      0    136    707       C  
ATOM   3796  C   MET A 461       5.797  11.378 -56.831  1.00 26.69           C  
ANISOU 3796  C   MET A 461     3786   3382   2974    -41    116    703       C  
ATOM   3797  O   MET A 461       5.439  10.516 -57.646  1.00 27.49           O  
ANISOU 3797  O   MET A 461     3885   3555   3004    -68     84    721       O  
ATOM   3798  CB  MET A 461       5.111  10.962 -54.435  1.00 25.86           C  
ANISOU 3798  CB  MET A 461     3709   3188   2928     12    137    607       C  
ATOM   3799  CG  MET A 461       4.517  11.575 -53.156  1.00 26.57           C  
ANISOU 3799  CG  MET A 461     3802   3201   3093     40    174    588       C  
ATOM   3800  SD  MET A 461       5.324  13.126 -52.668  1.00 29.82           S  
ANISOU 3800  SD  MET A 461     4211   3530   3589     43    232    577       S  
ATOM   3801  CE  MET A 461       6.925  12.515 -52.132  1.00 31.65           C  
ANISOU 3801  CE  MET A 461     4487   3774   3764     21    218    474       C  
ATOM   3802  N   MET A 462       6.973  12.000 -56.888  1.00 26.67           N  
ANISOU 3802  N   MET A 462     3791   3353   2988    -51    143    676       N  
ATOM   3803  CA  MET A 462       7.974  11.720 -57.915  1.00 27.37           C  
ANISOU 3803  CA  MET A 462     3888   3494   3019    -93    140    662       C  
ATOM   3804  C   MET A 462       9.296  11.342 -57.264  1.00 27.56           C  
ANISOU 3804  C   MET A 462     3934   3493   3045    -94    155    559       C  
ATOM   3805  O   MET A 462       9.651  11.879 -56.208  1.00 27.26           O  
ANISOU 3805  O   MET A 462     3904   3390   3065    -69    175    522       O  
ATOM   3806  CB  MET A 462       8.182  12.937 -58.813  1.00 29.48           C  
ANISOU 3806  CB  MET A 462     4135   3757   3310   -112    157    744       C  
ATOM   3807  CG  MET A 462       6.928  13.418 -59.530  1.00 31.11           C  
ANISOU 3807  CG  MET A 462     4309   3986   3525   -116    133    867       C  
ATOM   3808  SD  MET A 462       7.279  14.560 -60.880  1.00 32.96           S  
ANISOU 3808  SD  MET A 462     4525   4240   3759   -159    138    974       S  
ATOM   3809  CE  MET A 462       8.034  15.944 -60.023  1.00 34.21           C  
ANISOU 3809  CE  MET A 462     4677   4289   4034   -120    196    954       C  
ATOM   3810  N   TYR A 463      10.022  10.418 -57.891  1.00 26.08           N  
ANISOU 3810  N   TYR A 463     3754   3355   2800   -127    148    511       N  
ATOM   3811  CA  TYR A 463      11.258   9.889 -57.309  1.00 26.81           C  
ANISOU 3811  CA  TYR A 463     3858   3424   2905   -127    155    416       C  
ATOM   3812  C   TYR A 463      12.393   9.821 -58.321  1.00 27.85           C  
ANISOU 3812  C   TYR A 463     3984   3584   3015   -171    179    390       C  
ATOM   3813  O   TYR A 463      12.148   9.606 -59.514  1.00 26.36           O  
ANISOU 3813  O   TYR A 463     3792   3455   2768   -212    182    424       O  
ATOM   3814  CB  TYR A 463      11.010   8.505 -56.692  1.00 24.80           C  
ANISOU 3814  CB  TYR A 463     3614   3182   2627   -117    127    359       C  
ATOM   3815  CG  TYR A 463       9.960   8.519 -55.607  1.00 25.11           C  
ANISOU 3815  CG  TYR A 463     3663   3191   2686    -80    110    374       C  
ATOM   3816  CD1 TYR A 463       8.610   8.318 -55.918  1.00 25.56           C  
ANISOU 3816  CD1 TYR A 463     3715   3280   2717    -75     95    430       C  
ATOM   3817  CD2 TYR A 463      10.304   8.758 -54.278  1.00 22.34           C  
ANISOU 3817  CD2 TYR A 463     3328   2782   2379    -58    110    331       C  
ATOM   3818  CE1 TYR A 463       7.634   8.341 -54.938  1.00 23.48           C  
ANISOU 3818  CE1 TYR A 463     3458   2985   2478    -44     88    439       C  
ATOM   3819  CE2 TYR A 463       9.327   8.782 -53.280  1.00 25.48           C  
ANISOU 3819  CE2 TYR A 463     3739   3153   2790    -34    104    338       C  
ATOM   3820  CZ  TYR A 463       7.996   8.573 -53.627  1.00 24.35           C  
ANISOU 3820  CZ  TYR A 463     3588   3037   2629    -25     97    390       C  
ATOM   3821  OH  TYR A 463       7.020   8.596 -52.672  1.00 24.61           O  
ANISOU 3821  OH  TYR A 463     3630   3039   2681     -4     99    393       O  
ATOM   3822  N   TYR A 464      13.628   9.998 -57.838  1.00 27.88           N  
ANISOU 3822  N   TYR A 464     3986   3545   3063   -168    195    329       N  
ATOM   3823  CA  TYR A 464      14.811   9.932 -58.701  1.00 27.18           C  
ANISOU 3823  CA  TYR A 464     3887   3472   2967   -208    226    292       C  
ATOM   3824  C   TYR A 464      14.948   8.547 -59.330  1.00 26.92           C  
ANISOU 3824  C   TYR A 464     3851   3489   2888   -240    225    243       C  
ATOM   3825  O   TYR A 464      14.559   7.532 -58.731  1.00 24.53           O  
ANISOU 3825  O   TYR A 464     3551   3187   2583   -220    197    211       O  
ATOM   3826  CB  TYR A 464      16.093  10.273 -57.927  1.00 27.68           C  
ANISOU 3826  CB  TYR A 464     3942   3477   3099   -196    238    230       C  
ATOM   3827  CG  TYR A 464      16.152  11.667 -57.336  1.00 31.94           C  
ANISOU 3827  CG  TYR A 464     4484   3963   3689   -175    252    263       C  
ATOM   3828  CD1 TYR A 464      16.581  11.867 -56.023  1.00 34.68           C  
ANISOU 3828  CD1 TYR A 464     4834   4254   4087   -150    239    219       C  
ATOM   3829  CD2 TYR A 464      15.784  12.789 -58.083  1.00 34.38           C  
ANISOU 3829  CD2 TYR A 464     4791   4275   3995   -186    278    338       C  
ATOM   3830  CE1 TYR A 464      16.639  13.148 -55.466  1.00 36.13           C  
ANISOU 3830  CE1 TYR A 464     5022   4388   4318   -138    261    238       C  
ATOM   3831  CE2 TYR A 464      15.843  14.072 -57.539  1.00 36.01           C  
ANISOU 3831  CE2 TYR A 464     4996   4424   4261   -168    299    363       C  
ATOM   3832  CZ  TYR A 464      16.269  14.244 -56.229  1.00 37.83           C  
ANISOU 3832  CZ  TYR A 464     5232   4599   4541   -145    295    308       C  
ATOM   3833  OH  TYR A 464      16.323  15.510 -55.684  1.00 39.98           O  
ANISOU 3833  OH  TYR A 464     5505   4814   4873   -134    325    323       O  
ATOM   3834  N   LYS A 465      15.502   8.515 -60.535  1.00 26.43           N  
ANISOU 3834  N   LYS A 465     3784   3466   2792   -294    261    234       N  
ATOM   3835  CA  LYS A 465      15.690   7.271 -61.274  1.00 29.18           C  
ANISOU 3835  CA  LYS A 465     4129   3860   3098   -337    277    179       C  
ATOM   3836  C   LYS A 465      17.167   6.921 -61.477  1.00 31.30           C  
ANISOU 3836  C   LYS A 465     4376   4101   3414   -361    321     92       C  
ATOM   3837  O   LYS A 465      17.484   5.840 -61.982  1.00 28.76           O  
ANISOU 3837  O   LYS A 465     4045   3801   3082   -396    346     28       O  
ATOM   3838  CB  LYS A 465      15.010   7.351 -62.635  1.00 28.48           C  
ANISOU 3838  CB  LYS A 465     4054   3850   2916   -400    290    233       C  
ATOM   3839  CG  LYS A 465      13.502   7.404 -62.590  1.00 30.21           C  
ANISOU 3839  CG  LYS A 465     4284   4105   3089   -384    244    316       C  
ATOM   3840  CD  LYS A 465      12.908   7.311 -63.997  1.00 27.91           C  
ANISOU 3840  CD  LYS A 465     4004   3902   2698   -461    249    367       C  
ATOM   3841  CE  LYS A 465      12.889   5.872 -64.484  1.00 26.79           C  
ANISOU 3841  CE  LYS A 465     3867   3809   2504   -507    265    292       C  
ATOM   3842  NZ  LYS A 465      12.038   5.715 -65.686  1.00 32.68           N  
ANISOU 3842  NZ  LYS A 465     4627   4649   3142   -583    256    348       N  
ATOM   3843  N   ASP A 466      18.060   7.827 -61.083  1.00 31.76           N  
ANISOU 3843  N   ASP A 466     4424   4109   3533   -345    334     85       N  
ATOM   3844  CA  ASP A 466      19.485   7.640 -61.334  1.00 36.03           C  
ANISOU 3844  CA  ASP A 466     4939   4622   4129   -370    378      9       C  
ATOM   3845  C   ASP A 466      20.124   6.586 -60.434  1.00 36.74           C  
ANISOU 3845  C   ASP A 466     4999   4664   4296   -339    358    -66       C  
ATOM   3846  O   ASP A 466      21.089   5.939 -60.829  1.00 39.29           O  
ANISOU 3846  O   ASP A 466     5292   4973   4664   -366    397   -137       O  
ATOM   3847  CB  ASP A 466      20.241   8.971 -61.228  1.00 36.07           C  
ANISOU 3847  CB  ASP A 466     4940   4589   4177   -366    398     28       C  
ATOM   3848  CG  ASP A 466      20.343   9.479 -59.805  1.00 40.52           C  
ANISOU 3848  CG  ASP A 466     5500   5091   4806   -306    355     33       C  
ATOM   3849  OD1 ASP A 466      19.290   9.721 -59.173  1.00 42.61           O  
ANISOU 3849  OD1 ASP A 466     5784   5355   5049   -272    316     85       O  
ATOM   3850  OD2 ASP A 466      21.484   9.644 -59.319  1.00 44.62           O  
ANISOU 3850  OD2 ASP A 466     5994   5562   5399   -300    363    -16       O  
ATOM   3851  N   ARG A 467      19.578   6.415 -59.234  1.00 37.56           N  
ANISOU 3851  N   ARG A 467     5109   4741   4419   -286    299    -47       N  
ATOM   3852  CA  ARG A 467      20.188   5.565 -58.218  1.00 38.84           C  
ANISOU 3852  CA  ARG A 467     5245   4855   4658   -255    265    -99       C  
ATOM   3853  C   ARG A 467      19.142   5.032 -57.241  1.00 37.09           C  
ANISOU 3853  C   ARG A 467     5044   4635   4415   -216    206    -71       C  
ATOM   3854  O   ARG A 467      18.156   5.710 -56.935  1.00 35.44           O  
ANISOU 3854  O   ARG A 467     4867   4439   4159   -198    187    -13       O  
ATOM   3855  CB  ARG A 467      21.280   6.337 -57.455  1.00 41.10           C  
ANISOU 3855  CB  ARG A 467     5511   5084   5021   -239    255   -114       C  
ATOM   3856  CG  ARG A 467      20.767   7.582 -56.716  1.00 48.20           C  
ANISOU 3856  CG  ARG A 467     6441   5971   5902   -214    231    -58       C  
ATOM   3857  CD  ARG A 467      21.887   8.452 -56.143  1.00 56.89           C  
ANISOU 3857  CD  ARG A 467     7523   7021   7070   -212    232    -78       C  
ATOM   3858  NE  ARG A 467      21.554   9.877 -56.247  1.00 64.60           N  
ANISOU 3858  NE  ARG A 467     8525   7996   8024   -212    255    -30       N  
ATOM   3859  CZ  ARG A 467      20.963  10.602 -55.296  1.00 68.50           C  
ANISOU 3859  CZ  ARG A 467     9044   8468   8514   -189    231      3       C  
ATOM   3860  NH1 ARG A 467      20.634  10.055 -54.127  1.00 67.87           N  
ANISOU 3860  NH1 ARG A 467     8974   8373   8438   -167    179     -8       N  
ATOM   3861  NH2 ARG A 467      20.704  11.887 -55.516  1.00 68.52           N  
ANISOU 3861  NH2 ARG A 467     9062   8461   8512   -191    263     45       N  
ATOM   3862  N   ASP A 468      19.373   3.813 -56.758  1.00 36.12           N  
ANISOU 3862  N   ASP A 468     4899   4491   4334   -204    182   -112       N  
ATOM   3863  CA  ASP A 468      18.523   3.193 -55.750  1.00 33.26           C  
ANISOU 3863  CA  ASP A 468     4555   4124   3958   -171    125    -92       C  
ATOM   3864  C   ASP A 468      18.654   3.916 -54.420  1.00 30.38           C  
ANISOU 3864  C   ASP A 468     4205   3720   3619   -143     78    -69       C  
ATOM   3865  O   ASP A 468      19.765   4.201 -53.963  1.00 30.25           O  
ANISOU 3865  O   ASP A 468     4163   3663   3667   -143     67    -93       O  
ATOM   3866  CB  ASP A 468      18.913   1.727 -55.563  1.00 36.78           C  
ANISOU 3866  CB  ASP A 468     4968   4548   4460   -169    112   -140       C  
ATOM   3867  CG  ASP A 468      18.543   0.858 -56.756  1.00 42.70           C  
ANISOU 3867  CG  ASP A 468     5711   5338   5175   -202    162   -170       C  
ATOM   3868  OD1 ASP A 468      17.370   0.889 -57.193  1.00 42.78           O  
ANISOU 3868  OD1 ASP A 468     5755   5401   5099   -211    165   -135       O  
ATOM   3869  OD2 ASP A 468      19.431   0.125 -57.248  1.00 49.35           O  
ANISOU 3869  OD2 ASP A 468     6511   6158   6082   -224    199   -229       O  
ATOM   3870  N   GLY A 469      17.515   4.222 -53.808  1.00 32.69           N  
ANISOU 3870  N   GLY A 469     5005   4033   3381   -420    458    497       N  
ATOM   3871  CA  GLY A 469      17.482   4.695 -52.428  1.00 28.83           C  
ANISOU 3871  CA  GLY A 469     4392   3563   3000   -417    350    471       C  
ATOM   3872  C   GLY A 469      17.838   3.592 -51.447  1.00 28.62           C  
ANISOU 3872  C   GLY A 469     4231   3586   3058   -408    281    412       C  
ATOM   3873  O   GLY A 469      17.748   2.395 -51.773  1.00 25.83           O  
ANISOU 3873  O   GLY A 469     3881   3274   2658   -392    287    396       O  
ATOM   3874  N   VAL A 470      18.237   3.996 -50.243  1.00 26.36           N  
ANISOU 3874  N   VAL A 470     3841   3287   2887   -416    208    380       N  
ATOM   3875  CA  VAL A 470      18.624   3.061 -49.187  1.00 24.34           C  
ANISOU 3875  CA  VAL A 470     3480   3059   2708   -403    119    326       C  
ATOM   3876  C   VAL A 470      17.467   2.146 -48.753  1.00 25.42           C  
ANISOU 3876  C   VAL A 470     3659   3272   2726   -356     22    324       C  
ATOM   3877  O   VAL A 470      17.689   0.996 -48.372  1.00 27.98           O  
ANISOU 3877  O   VAL A 470     3938   3625   3069   -341    -12    292       O  
ATOM   3878  CB  VAL A 470      19.243   3.811 -47.968  1.00 25.56           C  
ANISOU 3878  CB  VAL A 470     3550   3167   2994   -418     38    291       C  
ATOM   3879  CG1 VAL A 470      18.251   4.792 -47.341  1.00 20.82           C  
ANISOU 3879  CG1 VAL A 470     3018   2574   2319   -402    -38    313       C  
ATOM   3880  CG2 VAL A 470      19.787   2.829 -46.923  1.00 25.40           C  
ANISOU 3880  CG2 VAL A 470     3444   3155   3052   -400    -68    235       C  
ATOM   3881  N   VAL A 471      16.236   2.649 -48.817  1.00 25.52           N  
ANISOU 3881  N   VAL A 471     3755   3307   2634   -333    -18    356       N  
ATOM   3882  CA  VAL A 471      15.068   1.826 -48.498  1.00 23.00           C  
ANISOU 3882  CA  VAL A 471     3466   3043   2228   -293    -88    349       C  
ATOM   3883  C   VAL A 471      14.850   0.714 -49.541  1.00 21.92           C  
ANISOU 3883  C   VAL A 471     3363   2943   2021   -281    -47    352       C  
ATOM   3884  O   VAL A 471      14.781  -0.448 -49.162  1.00 23.56           O  
ANISOU 3884  O   VAL A 471     3538   3187   2227   -265    -74    322       O  
ATOM   3885  CB  VAL A 471      13.797   2.683 -48.215  1.00 23.81           C  
ANISOU 3885  CB  VAL A 471     3624   3143   2281   -270   -142    370       C  
ATOM   3886  CG1 VAL A 471      12.542   1.838 -48.243  1.00 22.10           C  
ANISOU 3886  CG1 VAL A 471     3431   2967   1998   -233   -187    361       C  
ATOM   3887  CG2 VAL A 471      13.923   3.387 -46.854  1.00 25.56           C  
ANISOU 3887  CG2 VAL A 471     3816   3334   2562   -277   -194    348       C  
ATOM   3888  N   PRO A 472      14.766   1.051 -50.853  1.00 21.59           N  
ANISOU 3888  N   PRO A 472     3404   2885   1913   -288     19    388       N  
ATOM   3889  CA  PRO A 472      14.721  -0.043 -51.838  1.00 23.23           C  
ANISOU 3889  CA  PRO A 472     3659   3117   2051   -281     62    383       C  
ATOM   3890  C   PRO A 472      15.893  -1.021 -51.712  1.00 25.71           C  
ANISOU 3890  C   PRO A 472     3889   3432   2446   -301    128    346       C  
ATOM   3891  O   PRO A 472      15.701  -2.240 -51.788  1.00 27.14           O  
ANISOU 3891  O   PRO A 472     4060   3652   2600   -284    115    321       O  
ATOM   3892  CB  PRO A 472      14.794   0.689 -53.184  1.00 20.70           C  
ANISOU 3892  CB  PRO A 472     3466   2749   1652   -294    140    428       C  
ATOM   3893  CG  PRO A 472      14.144   2.009 -52.912  1.00 20.33           C  
ANISOU 3893  CG  PRO A 472     3452   2675   1596   -284     81    462       C  
ATOM   3894  CD  PRO A 472      14.450   2.354 -51.475  1.00 20.90           C  
ANISOU 3894  CD  PRO A 472     3401   2753   1785   -293     38    435       C  
ATOM   3895  N   THR A 473      17.090  -0.487 -51.503  1.00 26.11           N  
ANISOU 3895  N   THR A 473     3873   3433   2615   -335    194    338       N  
ATOM   3896  CA  THR A 473      18.295  -1.304 -51.427  1.00 26.99           C  
ANISOU 3896  CA  THR A 473     3886   3524   2845   -354    256    298       C  
ATOM   3897  C   THR A 473      18.238  -2.319 -50.285  1.00 25.83           C  
ANISOU 3897  C   THR A 473     3656   3417   2740   -325    145    258       C  
ATOM   3898  O   THR A 473      18.507  -3.497 -50.494  1.00 26.37           O  
ANISOU 3898  O   THR A 473     3697   3502   2820   -317    169    233       O  
ATOM   3899  CB  THR A 473      19.543  -0.416 -51.330  1.00 27.07           C  
ANISOU 3899  CB  THR A 473     3817   3455   3014   -397    333    287       C  
ATOM   3900  OG1 THR A 473      19.708   0.272 -52.574  1.00 32.58           O  
ANISOU 3900  OG1 THR A 473     4613   4101   3663   -427    479    324       O  
ATOM   3901  CG2 THR A 473      20.797  -1.244 -51.048  1.00 28.90           C  
ANISOU 3901  CG2 THR A 473     3910   3652   3418   -410    367    233       C  
ATOM   3902  N   GLU A 474      17.874  -1.860 -49.094  1.00 23.88           N  
ANISOU 3902  N   GLU A 474     3390   3177   2509   -311     31    253       N  
ATOM   3903  CA  GLU A 474      17.865  -2.727 -47.923  1.00 24.72           C  
ANISOU 3903  CA  GLU A 474     3452   3299   2640   -283    -72    219       C  
ATOM   3904  C   GLU A 474      16.674  -3.667 -47.877  1.00 23.43           C  
ANISOU 3904  C   GLU A 474     3350   3194   2359   -250   -104    222       C  
ATOM   3905  O   GLU A 474      16.803  -4.796 -47.419  1.00 22.44           O  
ANISOU 3905  O   GLU A 474     3199   3080   2245   -231   -137    196       O  
ATOM   3906  CB  GLU A 474      17.966  -1.909 -46.634  1.00 26.42           C  
ANISOU 3906  CB  GLU A 474     3653   3482   2902   -281   -173    208       C  
ATOM   3907  CG  GLU A 474      19.333  -1.233 -46.443  1.00 28.98           C  
ANISOU 3907  CG  GLU A 474     3885   3737   3391   -312   -172    184       C  
ATOM   3908  CD  GLU A 474      20.510  -2.199 -46.579  1.00 32.45           C  
ANISOU 3908  CD  GLU A 474     4219   4147   3965   -314   -155    144       C  
ATOM   3909  OE1 GLU A 474      21.495  -1.832 -47.261  1.00 36.92           O  
ANISOU 3909  OE1 GLU A 474     4706   4660   4663   -349    -59    132       O  
ATOM   3910  OE2 GLU A 474      20.457  -3.319 -46.017  1.00 30.88           O  
ANISOU 3910  OE2 GLU A 474     4016   3965   3750   -282   -228    123       O  
ATOM   3911  N   ILE A 475      15.524  -3.207 -48.370  1.00 23.47           N  
ANISOU 3911  N   ILE A 475     3430   3223   2266   -243    -99    251       N  
ATOM   3912  CA  ILE A 475      14.339  -4.054 -48.455  1.00 23.13           C  
ANISOU 3912  CA  ILE A 475     3428   3221   2140   -215   -125    245       C  
ATOM   3913  C   ILE A 475      14.539  -5.211 -49.463  1.00 23.41           C  
ANISOU 3913  C   ILE A 475     3469   3281   2147   -214    -69    234       C  
ATOM   3914  O   ILE A 475      13.990  -6.292 -49.263  1.00 22.72           O  
ANISOU 3914  O   ILE A 475     3380   3219   2032   -193    -92    212       O  
ATOM   3915  CB  ILE A 475      13.038  -3.223 -48.734  1.00 24.33           C  
ANISOU 3915  CB  ILE A 475     3640   3376   2227   -203   -152    270       C  
ATOM   3916  CG1 ILE A 475      11.816  -3.881 -48.092  1.00 23.93           C  
ANISOU 3916  CG1 ILE A 475     3595   3341   2155   -175   -199    247       C  
ATOM   3917  CG2 ILE A 475      12.804  -3.012 -50.227  1.00 21.76           C  
ANISOU 3917  CG2 ILE A 475     3379   3053   1836   -206   -115    295       C  
ATOM   3918  CD1 ILE A 475      10.546  -3.037 -48.168  1.00 23.31           C  
ANISOU 3918  CD1 ILE A 475     3545   3248   2063   -160   -233    259       C  
ATOM   3919  N   THR A 476      15.337  -4.974 -50.512  1.00 22.26           N  
ANISOU 3919  N   THR A 476     3334   3114   2009   -238     17    246       N  
ATOM   3920  CA  THR A 476      15.648  -5.978 -51.549  1.00 24.40           C  
ANISOU 3920  CA  THR A 476     3628   3394   2250   -242     94    232       C  
ATOM   3921  C   THR A 476      16.442  -7.167 -50.982  1.00 26.29           C  
ANISOU 3921  C   THR A 476     3778   3634   2576   -237    100    193       C  
ATOM   3922  O   THR A 476      16.165  -8.328 -51.311  1.00 25.27           O  
ANISOU 3922  O   THR A 476     3662   3531   2411   -223    110    173       O  
ATOM   3923  CB  THR A 476      16.440  -5.350 -52.740  1.00 26.27           C  
ANISOU 3923  CB  THR A 476     3916   3583   2480   -276    218    253       C  
ATOM   3924  OG1 THR A 476      15.628  -4.378 -53.416  1.00 23.57           O  
ANISOU 3924  OG1 THR A 476     3689   3233   2032   -273    204    293       O  
ATOM   3925  CG2 THR A 476      16.883  -6.423 -53.754  1.00 28.75           C  
ANISOU 3925  CG2 THR A 476     4266   3892   2768   -284    320    231       C  
ATOM   3926  N   LYS A 477      17.425  -6.868 -50.133  1.00 27.07           N  
ANISOU 3926  N   LYS A 477     3789   3698   2799   -246     80    180       N  
ATOM   3927  CA  LYS A 477      18.250  -7.903 -49.500  1.00 28.38           C  
ANISOU 3927  CA  LYS A 477     3868   3848   3067   -234     56    143       C  
ATOM   3928  C   LYS A 477      17.416  -8.867 -48.656  1.00 27.06           C  
ANISOU 3928  C   LYS A 477     3725   3716   2839   -197    -33    132       C  
ATOM   3929  O   LYS A 477      17.587 -10.081 -48.748  1.00 28.20           O  
ANISOU 3929  O   LYS A 477     3849   3867   2997   -183    -20    109       O  
ATOM   3930  CB  LYS A 477      19.370  -7.271 -48.657  1.00 29.12           C  
ANISOU 3930  CB  LYS A 477     3868   3884   3312   -244     10    126       C  
ATOM   3931  CG  LYS A 477      20.453  -6.570 -49.483  1.00 31.59           C  
ANISOU 3931  CG  LYS A 477     4123   4139   3741   -285    128    122       C  
ATOM   3932  CD  LYS A 477      21.386  -5.728 -48.617  1.00 32.86           C  
ANISOU 3932  CD  LYS A 477     4187   4236   4062   -297     62    101       C  
ATOM   3933  CE  LYS A 477      22.334  -4.910 -49.481  1.00 41.05           C  
ANISOU 3933  CE  LYS A 477     5169   5206   5224   -345    205     97       C  
ATOM   3934  NZ  LYS A 477      23.180  -3.976 -48.683  1.00 43.22           N  
ANISOU 3934  NZ  LYS A 477     5343   5411   5670   -361    136     72       N  
ATOM   3935  N   VAL A 478      16.513  -8.328 -47.840  1.00 27.00           N  
ANISOU 3935  N   VAL A 478     3766   3720   2772   -185   -108    147       N  
ATOM   3936  CA  VAL A 478      15.682  -9.167 -46.972  1.00 25.73           C  
ANISOU 3936  CA  VAL A 478     3642   3573   2560   -155   -165    136       C  
ATOM   3937  C   VAL A 478      14.629  -9.887 -47.806  1.00 26.45           C  
ANISOU 3937  C   VAL A 478     3772   3705   2571   -149   -122    133       C  
ATOM   3938  O   VAL A 478      14.357 -11.072 -47.574  1.00 29.07           O  
ANISOU 3938  O   VAL A 478     4108   4045   2893   -132   -124    113       O  
ATOM   3939  CB  VAL A 478      15.046  -8.370 -45.791  1.00 25.78           C  
ANISOU 3939  CB  VAL A 478     3699   3559   2536   -147   -234    145       C  
ATOM   3940  CG1 VAL A 478      14.158  -9.271 -44.928  1.00 25.22           C  
ANISOU 3940  CG1 VAL A 478     3686   3485   2412   -121   -256    132       C  
ATOM   3941  CG2 VAL A 478      16.132  -7.739 -44.921  1.00 21.73           C  
ANISOU 3941  CG2 VAL A 478     3158   2997   2101   -150   -301    139       C  
ATOM   3942  N   PHE A 479      14.058  -9.190 -48.789  1.00 25.36           N  
ANISOU 3942  N   PHE A 479     3670   3585   2381   -162    -92    151       N  
ATOM   3943  CA  PHE A 479      13.154  -9.830 -49.744  1.00 25.99           C  
ANISOU 3943  CA  PHE A 479     3790   3693   2394   -155    -73    142       C  
ATOM   3944  C   PHE A 479      13.776 -11.061 -50.430  1.00 28.23           C  
ANISOU 3944  C   PHE A 479     4059   3984   2683   -157    -17    118       C  
ATOM   3945  O   PHE A 479      13.102 -12.079 -50.588  1.00 26.62           O  
ANISOU 3945  O   PHE A 479     3867   3797   2451   -144    -23     93       O  
ATOM   3946  CB  PHE A 479      12.643  -8.862 -50.818  1.00 25.63           C  
ANISOU 3946  CB  PHE A 479     3804   3648   2285   -164    -69    167       C  
ATOM   3947  CG  PHE A 479      11.962  -9.567 -51.969  1.00 29.32           C  
ANISOU 3947  CG  PHE A 479     4329   4130   2681   -156    -67    151       C  
ATOM   3948  CD1 PHE A 479      10.691 -10.124 -51.810  1.00 29.93           C  
ANISOU 3948  CD1 PHE A 479     4404   4218   2751   -135   -128    125       C  
ATOM   3949  CD2 PHE A 479      12.612  -9.725 -53.189  1.00 26.86           C  
ANISOU 3949  CD2 PHE A 479     4077   3811   2319   -171      2    154       C  
ATOM   3950  CE1 PHE A 479      10.071 -10.804 -52.866  1.00 36.34           C  
ANISOU 3950  CE1 PHE A 479     5266   5035   3508   -127   -149    101       C  
ATOM   3951  CE2 PHE A 479      11.996 -10.405 -54.255  1.00 28.96           C  
ANISOU 3951  CE2 PHE A 479     4420   4080   2501   -163     -9    134       C  
ATOM   3952  CZ  PHE A 479      10.729 -10.939 -54.097  1.00 31.21           C  
ANISOU 3952  CZ  PHE A 479     4697   4380   2783   -139    -98    106       C  
ATOM   3953  N   ASN A 480      15.037 -10.941 -50.861  1.00 28.23           N  
ANISOU 3953  N   ASN A 480     4030   3963   2734   -176     48    119       N  
ATOM   3954  CA  ASN A 480      15.754 -12.056 -51.488  1.00 31.72           C  
ANISOU 3954  CA  ASN A 480     4451   4399   3204   -180    122     92       C  
ATOM   3955  C   ASN A 480      16.004 -13.238 -50.538  1.00 30.98           C  
ANISOU 3955  C   ASN A 480     4297   4302   3174   -157     84     65       C  
ATOM   3956  O   ASN A 480      15.982 -14.385 -50.965  1.00 32.10           O  
ANISOU 3956  O   ASN A 480     4439   4450   3307   -150    119     40       O  
ATOM   3957  CB  ASN A 480      17.071 -11.588 -52.126  1.00 31.52           C  
ANISOU 3957  CB  ASN A 480     4395   4329   3250   -209    224     94       C  
ATOM   3958  CG  ASN A 480      16.862 -10.865 -53.460  1.00 34.73           C  
ANISOU 3958  CG  ASN A 480     4909   4726   3560   -232    304    116       C  
ATOM   3959  OD1 ASN A 480      15.866 -11.077 -54.155  1.00 35.32           O  
ANISOU 3959  OD1 ASN A 480     5083   4827   3512   -222    281    119       O  
ATOM   3960  ND2 ASN A 480      17.817 -10.011 -53.822  1.00 32.35           N  
ANISOU 3960  ND2 ASN A 480     4595   4375   3319   -262    395    129       N  
ATOM   3961  N   GLN A 481      16.250 -12.952 -49.263  1.00 30.21           N  
ANISOU 3961  N   GLN A 481     4162   4184   3132   -143      8     71       N  
ATOM   3962  CA  GLN A 481      16.316 -13.992 -48.234  1.00 31.25           C  
ANISOU 3962  CA  GLN A 481     4278   4300   3296   -114    -48     54       C  
ATOM   3963  C   GLN A 481      14.957 -14.665 -48.075  1.00 29.58           C  
ANISOU 3963  C   GLN A 481     4127   4115   2998   -101    -58     48       C  
ATOM   3964  O   GLN A 481      14.868 -15.890 -47.982  1.00 29.40           O  
ANISOU 3964  O   GLN A 481     4103   4088   2980    -86    -46     27       O  
ATOM   3965  CB  GLN A 481      16.716 -13.408 -46.886  1.00 30.23           C  
ANISOU 3965  CB  GLN A 481     4144   4133   3212   -101   -143     63       C  
ATOM   3966  CG  GLN A 481      18.099 -12.809 -46.813  1.00 35.41           C  
ANISOU 3966  CG  GLN A 481     4718   4744   3992   -110   -161     56       C  
ATOM   3967  CD  GLN A 481      18.331 -12.097 -45.489  1.00 39.17           C  
ANISOU 3967  CD  GLN A 481     5212   5178   4492    -97   -279     62       C  
ATOM   3968  OE1 GLN A 481      17.544 -12.241 -44.546  1.00 39.24           O  
ANISOU 3968  OE1 GLN A 481     5309   5184   4417    -76   -337     70       O  
ATOM   3969  NE2 GLN A 481      19.405 -11.315 -45.414  1.00 41.14           N  
ANISOU 3969  NE2 GLN A 481     5386   5385   4861   -110   -308     52       N  
ATOM   3970  N   ARG A 482      13.901 -13.855 -48.038  1.00 28.84           N  
ANISOU 3970  N   ARG A 482     4077   4038   2845   -107    -75     63       N  
ATOM   3971  CA  ARG A 482      12.543 -14.374 -47.918  1.00 26.79           C  
ANISOU 3971  CA  ARG A 482     3852   3787   2539    -98    -77     49       C  
ATOM   3972  C   ARG A 482      12.272 -15.376 -49.031  1.00 27.07           C  
ANISOU 3972  C   ARG A 482     3885   3846   2555   -101    -36     21       C  
ATOM   3973  O   ARG A 482      11.797 -16.489 -48.771  1.00 25.39           O  
ANISOU 3973  O   ARG A 482     3674   3625   2349    -90    -25     -4       O  
ATOM   3974  CB  ARG A 482      11.518 -13.238 -47.938  1.00 25.03           C  
ANISOU 3974  CB  ARG A 482     3655   3569   2288   -104    -99     63       C  
ATOM   3975  CG  ARG A 482      10.080 -13.671 -47.640  1.00 25.43           C  
ANISOU 3975  CG  ARG A 482     3718   3607   2337    -96    -98     39       C  
ATOM   3976  CD  ARG A 482       9.275 -13.868 -48.914  1.00 27.27           C  
ANISOU 3976  CD  ARG A 482     3945   3862   2554    -99   -106     17       C  
ATOM   3977  NE  ARG A 482       7.949 -14.424 -48.652  1.00 24.17           N  
ANISOU 3977  NE  ARG A 482     3536   3444   2202    -92   -106    -20       N  
ATOM   3978  CZ  ARG A 482       6.856 -14.107 -49.341  1.00 26.21           C  
ANISOU 3978  CZ  ARG A 482     3780   3696   2482    -89   -149    -41       C  
ATOM   3979  NH1 ARG A 482       6.917 -13.211 -50.327  1.00 27.11           N  
ANISOU 3979  NH1 ARG A 482     3920   3827   2552    -89   -203    -22       N  
ATOM   3980  NH2 ARG A 482       5.691 -14.669 -49.033  1.00 24.13           N  
ANISOU 3980  NH2 ARG A 482     3480   3395   2295    -85   -141    -85       N  
ATOM   3981  N   LYS A 483      12.620 -14.981 -50.253  1.00 27.04           N  
ANISOU 3981  N   LYS A 483     3891   3859   2523   -116     -6     26       N  
ATOM   3982  CA  LYS A 483      12.344 -15.759 -51.459  1.00 29.71           C  
ANISOU 3982  CA  LYS A 483     4259   4211   2818   -121     27     -2       C  
ATOM   3983  C   LYS A 483      13.008 -17.139 -51.437  1.00 29.81           C  
ANISOU 3983  C   LYS A 483     4240   4215   2869   -115     75    -30       C  
ATOM   3984  O   LYS A 483      12.401 -18.131 -51.846  1.00 30.48           O  
ANISOU 3984  O   LYS A 483     4341   4306   2935   -111     82    -64       O  
ATOM   3985  CB  LYS A 483      12.748 -14.963 -52.714  1.00 30.52           C  
ANISOU 3985  CB  LYS A 483     4417   4315   2863   -140     64     15       C  
ATOM   3986  CG  LYS A 483      12.352 -15.630 -54.035  1.00 37.38           C  
ANISOU 3986  CG  LYS A 483     5361   5186   3654   -143     84    -14       C  
ATOM   3987  CD  LYS A 483      12.731 -14.785 -55.251  1.00 45.57           C  
ANISOU 3987  CD  LYS A 483     6500   6207   4608   -161    129      7       C  
ATOM   3988  CE  LYS A 483      12.300 -15.472 -56.547  1.00 50.27           C  
ANISOU 3988  CE  LYS A 483     7207   6793   5101   -161    135    -25       C  
ATOM   3989  NZ  LYS A 483      12.512 -14.610 -57.751  1.00 54.79           N  
ANISOU 3989  NZ  LYS A 483     7927   7333   5559   -174    171      0       N  
ATOM   3990  N   GLU A 484      14.245 -17.198 -50.951  1.00 30.84           N  
ANISOU 3990  N   GLU A 484     4321   4325   3071   -113     99    -21       N  
ATOM   3991  CA  GLU A 484      14.957 -18.462 -50.807  1.00 33.41           C  
ANISOU 3991  CA  GLU A 484     4606   4630   3459   -101    132    -47       C  
ATOM   3992  C   GLU A 484      14.189 -19.411 -49.876  1.00 33.06           C  
ANISOU 3992  C   GLU A 484     4571   4578   3413    -78     91    -59       C  
ATOM   3993  O   GLU A 484      13.926 -20.565 -50.228  1.00 33.86           O  
ANISOU 3993  O   GLU A 484     4677   4678   3512    -73    123    -90       O  
ATOM   3994  CB  GLU A 484      16.371 -18.215 -50.269  1.00 35.42           C  
ANISOU 3994  CB  GLU A 484     4789   4846   3822    -96    132    -39       C  
ATOM   3995  CG  GLU A 484      17.282 -19.452 -50.273  1.00 40.22           C  
ANISOU 3995  CG  GLU A 484     5339   5419   4522    -80    167    -69       C  
ATOM   3996  CD  GLU A 484      18.589 -19.240 -49.508  1.00 48.96           C  
ANISOU 3996  CD  GLU A 484     6360   6472   5771    -65    123    -68       C  
ATOM   3997  OE1 GLU A 484      18.791 -18.144 -48.937  1.00 51.34           O  
ANISOU 3997  OE1 GLU A 484     6652   6764   6092    -69     64    -45       O  
ATOM   3998  OE2 GLU A 484      19.420 -20.174 -49.473  1.00 50.71           O  
ANISOU 3998  OE2 GLU A 484     6519   6651   6098    -48    139    -94       O  
ATOM   3999  N   HIS A 485      13.815 -18.911 -48.700  1.00 30.33           N  
ANISOU 3999  N   HIS A 485     4240   4217   3065    -66     32    -37       N  
ATOM   4000  CA  HIS A 485      13.129 -19.733 -47.702  1.00 27.06           C  
ANISOU 4000  CA  HIS A 485     3860   3775   2648    -47     17    -45       C  
ATOM   4001  C   HIS A 485      11.734 -20.167 -48.145  1.00 26.77           C  
ANISOU 4001  C   HIS A 485     3842   3751   2578    -57     45    -72       C  
ATOM   4002  O   HIS A 485      11.319 -21.310 -47.878  1.00 24.92           O  
ANISOU 4002  O   HIS A 485     3618   3493   2359    -49     73    -96       O  
ATOM   4003  CB  HIS A 485      13.093 -19.021 -46.356  1.00 27.50           C  
ANISOU 4003  CB  HIS A 485     3957   3796   2695    -35    -38    -17       C  
ATOM   4004  CG  HIS A 485      14.442 -18.877 -45.722  1.00 28.11           C  
ANISOU 4004  CG  HIS A 485     4018   3839   2824    -17    -97     -2       C  
ATOM   4005  ND1 HIS A 485      15.100 -19.933 -45.128  1.00 32.37           N  
ANISOU 4005  ND1 HIS A 485     4566   4331   3402     13   -125     -9       N  
ATOM   4006  CD2 HIS A 485      15.253 -17.802 -45.582  1.00 28.59           C  
ANISOU 4006  CD2 HIS A 485     4050   3895   2920    -22   -144     15       C  
ATOM   4007  CE1 HIS A 485      16.260 -19.517 -44.654  1.00 30.03           C  
ANISOU 4007  CE1 HIS A 485     4240   4000   3171     29   -203      0       C  
ATOM   4008  NE2 HIS A 485      16.378 -18.228 -44.918  1.00 33.89           N  
ANISOU 4008  NE2 HIS A 485     4701   4513   3663      5   -211     12       N  
ATOM   4009  N   LYS A 486      11.027 -19.280 -48.847  1.00 23.69           N  
ANISOU 4009  N   LYS A 486     3453   3390   2157    -74     32    -72       N  
ATOM   4010  CA  LYS A 486       9.729 -19.647 -49.403  1.00 25.21           C  
ANISOU 4010  CA  LYS A 486     3647   3585   2346    -80     33   -109       C  
ATOM   4011  C   LYS A 486       9.871 -20.817 -50.381  1.00 23.37           C  
ANISOU 4011  C   LYS A 486     3410   3362   2108    -83     62   -148       C  
ATOM   4012  O   LYS A 486       9.067 -21.741 -50.352  1.00 25.36           O  
ANISOU 4012  O   LYS A 486     3653   3594   2389    -83     74   -187       O  
ATOM   4013  CB  LYS A 486       9.000 -18.461 -50.053  1.00 24.46           C  
ANISOU 4013  CB  LYS A 486     3559   3508   2227    -89    -15   -104       C  
ATOM   4014  CG  LYS A 486       7.536 -18.784 -50.352  1.00 26.50           C  
ANISOU 4014  CG  LYS A 486     3799   3746   2522    -90    -41   -149       C  
ATOM   4015  CD  LYS A 486       6.799 -17.709 -51.141  1.00 29.41           C  
ANISOU 4015  CD  LYS A 486     4176   4121   2876    -91   -116   -150       C  
ATOM   4016  CE  LYS A 486       5.320 -18.098 -51.281  1.00 30.88           C  
ANISOU 4016  CE  LYS A 486     4317   4269   3146    -88   -156   -207       C  
ATOM   4017  NZ  LYS A 486       4.438 -17.096 -51.980  1.00 28.61           N  
ANISOU 4017  NZ  LYS A 486     4028   3969   2874    -79   -259   -216       N  
ATOM   4018  N   GLY A 487      10.905 -20.776 -51.218  1.00 25.38           N  
ANISOU 4018  N   GLY A 487     3672   3636   2334    -89     85   -141       N  
ATOM   4019  CA  GLY A 487      11.217 -21.874 -52.141  1.00 25.79           C  
ANISOU 4019  CA  GLY A 487     3733   3689   2376    -93    130   -179       C  
ATOM   4020  C   GLY A 487      11.397 -23.201 -51.418  1.00 26.57           C  
ANISOU 4020  C   GLY A 487     3803   3759   2533    -79    163   -198       C  
ATOM   4021  O   GLY A 487      10.830 -24.214 -51.824  1.00 29.07           O  
ANISOU 4021  O   GLY A 487     4124   4067   2855    -81    180   -241       O  
ATOM   4022  N   TYR A 488      12.174 -23.190 -50.336  1.00 26.67           N  
ANISOU 4022  N   TYR A 488     3794   3749   2589    -62    161   -166       N  
ATOM   4023  CA  TYR A 488      12.340 -24.372 -49.484  1.00 26.89           C  
ANISOU 4023  CA  TYR A 488     3819   3735   2663    -40    177   -174       C  
ATOM   4024  C   TYR A 488      11.019 -24.839 -48.910  1.00 25.23           C  
ANISOU 4024  C   TYR A 488     3635   3500   2452    -42    183   -192       C  
ATOM   4025  O   TYR A 488      10.753 -26.049 -48.877  1.00 26.09           O  
ANISOU 4025  O   TYR A 488     3745   3579   2587    -37    222   -221       O  
ATOM   4026  CB  TYR A 488      13.330 -24.128 -48.333  1.00 26.09           C  
ANISOU 4026  CB  TYR A 488     3715   3598   2598    -15    137   -135       C  
ATOM   4027  CG  TYR A 488      14.728 -23.736 -48.763  1.00 29.14           C  
ANISOU 4027  CG  TYR A 488     4048   3988   3036    -13    135   -127       C  
ATOM   4028  CD1 TYR A 488      15.290 -24.229 -49.945  1.00 31.66           C  
ANISOU 4028  CD1 TYR A 488     4332   4318   3380    -25    205   -157       C  
ATOM   4029  CD2 TYR A 488      15.498 -22.882 -47.973  1.00 32.23           C  
ANISOU 4029  CD2 TYR A 488     4425   4358   3463     -1     72    -95       C  
ATOM   4030  CE1 TYR A 488      16.580 -23.865 -50.336  1.00 33.96           C  
ANISOU 4030  CE1 TYR A 488     4564   4593   3746    -28    233   -156       C  
ATOM   4031  CE2 TYR A 488      16.786 -22.512 -48.352  1.00 34.11           C  
ANISOU 4031  CE2 TYR A 488     4591   4583   3785     -2     77    -97       C  
ATOM   4032  CZ  TYR A 488      17.321 -23.006 -49.529  1.00 35.25           C  
ANISOU 4032  CZ  TYR A 488     4691   4734   3970    -17    168   -127       C  
ATOM   4033  OH  TYR A 488      18.595 -22.641 -49.896  1.00 39.32           O  
ANISOU 4033  OH  TYR A 488     5127   5218   4595    -23    201   -135       O  
ATOM   4034  N   MET A 489      10.199 -23.887 -48.458  1.00 24.28           N  
ANISOU 4034  N   MET A 489     3528   3379   2316    -50    157   -177       N  
ATOM   4035  CA  MET A 489       8.914 -24.214 -47.842  1.00 25.58           C  
ANISOU 4035  CA  MET A 489     3708   3502   2510    -55    186   -199       C  
ATOM   4036  C   MET A 489       7.964 -24.906 -48.821  1.00 26.46           C  
ANISOU 4036  C   MET A 489     3781   3616   2654    -72    200   -259       C  
ATOM   4037  O   MET A 489       7.352 -25.919 -48.481  1.00 26.30           O  
ANISOU 4037  O   MET A 489     3759   3548   2685    -75    251   -292       O  
ATOM   4038  CB  MET A 489       8.244 -22.974 -47.249  1.00 26.12           C  
ANISOU 4038  CB  MET A 489     3789   3562   2573    -61    167   -178       C  
ATOM   4039  CG  MET A 489       6.864 -23.258 -46.652  1.00 26.86           C  
ANISOU 4039  CG  MET A 489     3884   3595   2727    -72    223   -210       C  
ATOM   4040  SD  MET A 489       5.852 -21.792 -46.394  1.00 39.31           S  
ANISOU 4040  SD  MET A 489     5442   5160   4333    -84    207   -207       S  
ATOM   4041  CE  MET A 489       5.257 -21.413 -48.042  1.00 28.21           C  
ANISOU 4041  CE  MET A 489     3957   3806   2953    -93    122   -247       C  
ATOM   4042  N   LEU A 490       7.843 -24.348 -50.023  1.00 26.37           N  
ANISOU 4042  N   LEU A 490     3754   3652   2615    -83    150   -276       N  
ATOM   4043  CA  LEU A 490       6.947 -24.894 -51.040  1.00 28.33           C  
ANISOU 4043  CA  LEU A 490     3981   3896   2886    -95    126   -338       C  
ATOM   4044  C   LEU A 490       7.383 -26.268 -51.554  1.00 27.77           C  
ANISOU 4044  C   LEU A 490     3915   3819   2817    -96    168   -374       C  
ATOM   4045  O   LEU A 490       6.538 -27.133 -51.805  1.00 27.35           O  
ANISOU 4045  O   LEU A 490     3838   3733   2819   -105    174   -432       O  
ATOM   4046  CB  LEU A 490       6.772 -23.914 -52.205  1.00 28.00           C  
ANISOU 4046  CB  LEU A 490     3959   3892   2787   -100     44   -342       C  
ATOM   4047  CG  LEU A 490       5.938 -22.652 -51.955  1.00 31.78           C  
ANISOU 4047  CG  LEU A 490     4420   4365   3289   -100    -16   -327       C  
ATOM   4048  CD1 LEU A 490       5.866 -21.801 -53.216  1.00 32.42           C  
ANISOU 4048  CD1 LEU A 490     4549   4474   3297    -99   -106   -328       C  
ATOM   4049  CD2 LEU A 490       4.531 -22.990 -51.478  1.00 32.99           C  
ANISOU 4049  CD2 LEU A 490     4510   4461   3565   -104    -19   -379       C  
ATOM   4050  N   ALA A 491       8.692 -26.468 -51.704  1.00 27.18           N  
ANISOU 4050  N   ALA A 491     3861   3765   2699    -87    200   -346       N  
ATOM   4051  CA  ALA A 491       9.216 -27.772 -52.112  1.00 28.63           C  
ANISOU 4051  CA  ALA A 491     4047   3935   2896    -84    252   -378       C  
ATOM   4052  C   ALA A 491       8.916 -28.834 -51.053  1.00 28.74           C  
ANISOU 4052  C   ALA A 491     4047   3894   2979    -75    301   -386       C  
ATOM   4053  O   ALA A 491       8.568 -29.964 -51.393  1.00 30.11           O  
ANISOU 4053  O   ALA A 491     4212   4039   3187    -81    334   -435       O  
ATOM   4054  CB  ALA A 491      10.710 -27.695 -52.396  1.00 28.04           C  
ANISOU 4054  CB  ALA A 491     3979   3877   2797    -75    287   -349       C  
ATOM   4055  N   ALA A 492       9.034 -28.464 -49.775  1.00 28.02           N  
ANISOU 4055  N   ALA A 492     3970   3776   2900    -60    307   -337       N  
ATOM   4056  CA  ALA A 492       8.674 -29.358 -48.663  1.00 29.94           C  
ANISOU 4056  CA  ALA A 492     4239   3948   3189    -50    362   -336       C  
ATOM   4057  C   ALA A 492       7.189 -29.725 -48.683  1.00 29.88           C  
ANISOU 4057  C   ALA A 492     4208   3900   3245    -74    398   -389       C  
ATOM   4058  O   ALA A 492       6.804 -30.865 -48.386  1.00 31.08           O  
ANISOU 4058  O   ALA A 492     4365   3993   3451    -77    464   -419       O  
ATOM   4059  CB  ALA A 492       9.056 -28.731 -47.325  1.00 29.08           C  
ANISOU 4059  CB  ALA A 492     4187   3809   3054    -30    352   -274       C  
ATOM   4060  N   GLN A 493       6.369 -28.745 -49.039  1.00 27.38           N  
ANISOU 4060  N   GLN A 493     3858   3606   2940    -91    353   -404       N  
ATOM   4061  CA  GLN A 493       4.929 -28.916 -49.178  1.00 28.56           C  
ANISOU 4061  CA  GLN A 493     3954   3710   3187   -113    366   -466       C  
ATOM   4062  C   GLN A 493       4.581 -29.838 -50.368  1.00 28.87           C  
ANISOU 4062  C   GLN A 493     3953   3753   3262   -126    338   -541       C  
ATOM   4063  O   GLN A 493       3.745 -30.744 -50.249  1.00 27.59           O  
ANISOU 4063  O   GLN A 493     3753   3526   3203   -141    387   -598       O  
ATOM   4064  CB  GLN A 493       4.293 -27.526 -49.318  1.00 28.04           C  
ANISOU 4064  CB  GLN A 493     3859   3666   3130   -119    299   -461       C  
ATOM   4065  CG  GLN A 493       2.783 -27.458 -49.496  1.00 32.21           C  
ANISOU 4065  CG  GLN A 493     4307   4139   3793   -138    288   -530       C  
ATOM   4066  CD  GLN A 493       2.300 -26.014 -49.581  1.00 37.49           C  
ANISOU 4066  CD  GLN A 493     4950   4825   4471   -136    215   -516       C  
ATOM   4067  OE1 GLN A 493       1.852 -25.559 -50.634  1.00 38.30           O  
ANISOU 4067  OE1 GLN A 493     5017   4950   4587   -135    101   -551       O  
ATOM   4068  NE2 GLN A 493       2.423 -25.278 -48.476  1.00 35.64           N  
ANISOU 4068  NE2 GLN A 493     4749   4572   4221   -132    273   -464       N  
ATOM   4069  N   ARG A 494       5.226 -29.606 -51.507  1.00 28.02           N  
ANISOU 4069  N   ARG A 494     3865   3710   3071   -122    267   -543       N  
ATOM   4070  CA  ARG A 494       5.042 -30.466 -52.679  1.00 30.39           C  
ANISOU 4070  CA  ARG A 494     4161   4010   3374   -132    237   -612       C  
ATOM   4071  C   ARG A 494       5.484 -31.901 -52.392  1.00 30.96           C  
ANISOU 4071  C   ARG A 494     4240   4046   3478   -131    329   -628       C  
ATOM   4072  O   ARG A 494       4.814 -32.846 -52.796  1.00 33.16           O  
ANISOU 4072  O   ARG A 494     4490   4282   3825   -146    337   -699       O  
ATOM   4073  CB  ARG A 494       5.801 -29.924 -53.892  1.00 28.06           C  
ANISOU 4073  CB  ARG A 494     3927   3777   2958   -129    174   -603       C  
ATOM   4074  CG  ARG A 494       5.203 -28.672 -54.507  1.00 29.06           C  
ANISOU 4074  CG  ARG A 494     4066   3927   3048   -130     63   -604       C  
ATOM   4075  CD  ARG A 494       5.877 -28.364 -55.846  1.00 31.05           C  
ANISOU 4075  CD  ARG A 494     4415   4217   3166   -129     19   -606       C  
ATOM   4076  NE  ARG A 494       7.302 -28.061 -55.695  1.00 25.12           N  
ANISOU 4076  NE  ARG A 494     3700   3502   2341   -123    101   -540       N  
ATOM   4077  CZ  ARG A 494       7.794 -26.844 -55.475  1.00 29.46           C  
ANISOU 4077  CZ  ARG A 494     4265   4082   2846   -118     92   -477       C  
ATOM   4078  NH1 ARG A 494       6.985 -25.795 -55.388  1.00 25.41           N  
ANISOU 4078  NH1 ARG A 494     3744   3572   2336   -116      7   -465       N  
ATOM   4079  NH2 ARG A 494       9.104 -26.672 -55.362  1.00 29.18           N  
ANISOU 4079  NH2 ARG A 494     4245   4066   2778   -115    167   -432       N  
ATOM   4080  N   ASN A 495       6.614 -32.044 -51.702  1.00 30.63           N  
ANISOU 4080  N   ASN A 495     4233   4012   3394   -110    386   -566       N  
ATOM   4081  CA  ASN A 495       7.119 -33.345 -51.272  1.00 30.80           C  
ANISOU 4081  CA  ASN A 495     4266   3987   3447    -99    466   -568       C  
ATOM   4082  C   ASN A 495       6.163 -34.058 -50.323  1.00 31.65           C  
ANISOU 4082  C   ASN A 495     4364   4012   3651   -108    537   -588       C  
ATOM   4083  O   ASN A 495       6.024 -35.291 -50.380  1.00 30.97           O  
ANISOU 4083  O   ASN A 495     4274   3875   3618   -113    596   -628       O  
ATOM   4084  CB  ASN A 495       8.506 -33.204 -50.626  1.00 30.93           C  
ANISOU 4084  CB  ASN A 495     4318   4016   3419    -68    483   -496       C  
ATOM   4085  CG  ASN A 495       9.601 -32.930 -51.644  1.00 30.77           C  
ANISOU 4085  CG  ASN A 495     4297   4050   3343    -63    461   -493       C  
ATOM   4086  OD1 ASN A 495       9.479 -33.288 -52.815  1.00 31.45           O  
ANISOU 4086  OD1 ASN A 495     4386   4153   3410    -80    462   -547       O  
ATOM   4087  ND2 ASN A 495      10.676 -32.287 -51.201  1.00 33.42           N  
ANISOU 4087  ND2 ASN A 495     4637   4403   3659    -42    447   -434       N  
ATOM   4088  N   GLY A 496       5.521 -33.278 -49.450  1.00 31.48           N  
ANISOU 4088  N   GLY A 496     4345   3965   3652   -113    548   -561       N  
ATOM   4089  CA  GLY A 496       4.497 -33.790 -48.539  1.00 31.07           C  
ANISOU 4089  CA  GLY A 496     4291   3816   3700   -128    644   -583       C  
ATOM   4090  C   GLY A 496       3.352 -34.462 -49.282  1.00 33.68           C  
ANISOU 4090  C   GLY A 496     4536   4106   4153   -160    650   -681       C  
ATOM   4091  O   GLY A 496       2.903 -35.544 -48.894  1.00 36.41           O  
ANISOU 4091  O   GLY A 496     4879   4368   4588   -173    748   -716       O  
ATOM   4092  N   GLU A 497       2.901 -33.831 -50.368  1.00 33.00           N  
ANISOU 4092  N   GLU A 497     4391   4071   4077   -172    537   -728       N  
ATOM   4093  CA  GLU A 497       1.796 -34.351 -51.183  1.00 34.48           C  
ANISOU 4093  CA  GLU A 497     4494   4216   4389   -198    496   -831       C  
ATOM   4094  C   GLU A 497       2.157 -35.639 -51.928  1.00 35.43           C  
ANISOU 4094  C   GLU A 497     4627   4331   4502   -202    504   -881       C  
ATOM   4095  O   GLU A 497       1.296 -36.488 -52.154  1.00 34.88           O  
ANISOU 4095  O   GLU A 497     4497   4192   4565   -226    523   -965       O  
ATOM   4096  CB  GLU A 497       1.276 -33.284 -52.152  1.00 33.59           C  
ANISOU 4096  CB  GLU A 497     4342   4150   4271   -199    341   -864       C  
ATOM   4097  CG  GLU A 497       0.698 -32.035 -51.467  1.00 33.55           C  
ANISOU 4097  CG  GLU A 497     4302   4133   4311   -198    333   -831       C  
ATOM   4098  CD  GLU A 497      -0.415 -32.334 -50.442  1.00 35.23           C  
ANISOU 4098  CD  GLU A 497     4442   4232   4713   -221    455   -868       C  
ATOM   4099  OE1 GLU A 497      -1.295 -33.179 -50.714  1.00 32.82           O  
ANISOU 4099  OE1 GLU A 497     4055   3850   4566   -244    472   -958       O  
ATOM   4100  OE2 GLU A 497      -0.413 -31.703 -49.363  1.00 33.92           O  
ANISOU 4100  OE2 GLU A 497     4305   4042   4540   -218    541   -811       O  
ATOM   4101  N   ILE A 498       3.429 -35.781 -52.296  1.00 35.67           N  
ANISOU 4101  N   ILE A 498     4729   4426   4396   -181    496   -835       N  
ATOM   4102  CA  ILE A 498       3.918 -37.020 -52.902  1.00 38.18           C  
ANISOU 4102  CA  ILE A 498     5068   4733   4705   -182    527   -875       C  
ATOM   4103  C   ILE A 498       3.869 -38.183 -51.899  1.00 38.30           C  
ANISOU 4103  C   ILE A 498     5086   4663   4804   -182    661   -870       C  
ATOM   4104  O   ILE A 498       3.527 -39.311 -52.259  1.00 41.89           O  
ANISOU 4104  O   ILE A 498     5518   5065   5333   -199    697   -938       O  
ATOM   4105  CB  ILE A 498       5.343 -36.851 -53.491  1.00 37.82           C  
ANISOU 4105  CB  ILE A 498     5091   4762   4518   -158    510   -829       C  
ATOM   4106  CG1 ILE A 498       5.329 -35.828 -54.633  1.00 37.19           C  
ANISOU 4106  CG1 ILE A 498     5037   4747   4345   -163    395   -844       C  
ATOM   4107  CG2 ILE A 498       5.887 -38.192 -53.991  1.00 34.69           C  
ANISOU 4107  CG2 ILE A 498     4715   4339   4126   -158    567   -870       C  
ATOM   4108  CD1 ILE A 498       6.707 -35.349 -55.051  1.00 35.39           C  
ANISOU 4108  CD1 ILE A 498     4873   4581   3992   -145    406   -787       C  
ATOM   4109  N   ILE A 499       4.207 -37.901 -50.645  1.00 36.56           N  
ANISOU 4109  N   ILE A 499     4908   4419   4564   -164    731   -790       N  
ATOM   4110  CA  ILE A 499       4.119 -38.899 -49.588  1.00 37.29           C  
ANISOU 4110  CA  ILE A 499     5040   4413   4717   -161    859   -773       C  
ATOM   4111  C   ILE A 499       2.656 -39.251 -49.273  1.00 40.08           C  
ANISOU 4111  C   ILE A 499     5332   4668   5229   -200    936   -842       C  
ATOM   4112  O   ILE A 499       2.330 -40.429 -49.093  1.00 40.13           O  
ANISOU 4112  O   ILE A 499     5336   4588   5323   -215   1032   -882       O  
ATOM   4113  CB  ILE A 499       4.882 -38.464 -48.315  1.00 35.61           C  
ANISOU 4113  CB  ILE A 499     4924   4186   4420   -126    896   -669       C  
ATOM   4114  CG1 ILE A 499       6.365 -38.238 -48.637  1.00 34.42           C  
ANISOU 4114  CG1 ILE A 499     4805   4113   4159    -88    821   -615       C  
ATOM   4115  CG2 ILE A 499       4.734 -39.505 -47.216  1.00 34.93           C  
ANISOU 4115  CG2 ILE A 499     4917   3979   4376   -120   1027   -649       C  
ATOM   4116  CD1 ILE A 499       7.083 -37.321 -47.650  1.00 33.20           C  
ANISOU 4116  CD1 ILE A 499     4721   3971   3922    -55    789   -524       C  
ATOM   4117  N   LYS A 500       1.783 -38.240 -49.213  1.00 40.13           N  
ANISOU 4117  N   LYS A 500     5280   4676   5290   -218    902   -860       N  
ATOM   4118  CA  LYS A 500       0.341 -38.483 -49.038  1.00 41.92           C  
ANISOU 4118  CA  LYS A 500     5415   4799   5712   -258    969   -942       C  
ATOM   4119  C   LYS A 500      -0.231 -39.393 -50.140  1.00 44.08           C  
ANISOU 4119  C   LYS A 500     5598   5050   6102   -284    917  -1054       C  
ATOM   4120  O   LYS A 500      -0.932 -40.361 -49.840  1.00 46.29           O  
ANISOU 4120  O   LYS A 500     5835   5220   6534   -312   1029  -1114       O  
ATOM   4121  CB  LYS A 500      -0.447 -37.172 -48.965  1.00 40.68           C  
ANISOU 4121  CB  LYS A 500     5191   4651   5612   -268    914   -951       C  
ATOM   4122  CG  LYS A 500      -0.226 -36.361 -47.699  1.00 39.19           C  
ANISOU 4122  CG  LYS A 500     5089   4445   5356   -254   1001   -861       C  
ATOM   4123  CD  LYS A 500      -1.059 -35.082 -47.714  1.00 37.97           C  
ANISOU 4123  CD  LYS A 500     4855   4294   5278   -265    949   -880       C  
ATOM   4124  CE  LYS A 500      -0.530 -34.054 -46.718  1.00 36.66           C  
ANISOU 4124  CE  LYS A 500     4793   4150   4986   -244    984   -782       C  
ATOM   4125  NZ  LYS A 500      -1.247 -32.740 -46.817  1.00 35.30           N  
ANISOU 4125  NZ  LYS A 500     4543   3990   4879   -250    922   -797       N  
ATOM   4126  N   GLU A 501       0.088 -39.091 -51.402  1.00 44.89           N  
ANISOU 4126  N   GLU A 501     5684   5245   6127   -275    755  -1085       N  
ATOM   4127  CA  GLU A 501      -0.346 -39.906 -52.548  1.00 47.96           C  
ANISOU 4127  CA  GLU A 501     6018   5616   6589   -295    677  -1194       C  
ATOM   4128  C   GLU A 501       0.094 -41.359 -52.415  1.00 47.91           C  
ANISOU 4128  C   GLU A 501     6048   5558   6595   -299    790  -1207       C  
ATOM   4129  O   GLU A 501      -0.685 -42.273 -52.675  1.00 48.52           O  
ANISOU 4129  O   GLU A 501     6058   5552   6827   -329    817  -1302       O  
ATOM   4130  CB  GLU A 501       0.179 -39.336 -53.875  1.00 49.23           C  
ANISOU 4130  CB  GLU A 501     6222   5882   6603   -278    500  -1204       C  
ATOM   4131  CG  GLU A 501      -0.580 -38.118 -54.418  1.00 54.79           C  
ANISOU 4131  CG  GLU A 501     6876   6609   7333   -278    342  -1234       C  
ATOM   4132  CD  GLU A 501      -1.876 -38.469 -55.150  1.00 60.99           C  
ANISOU 4132  CD  GLU A 501     7555   7315   8301   -304    229  -1367       C  
ATOM   4133  OE1 GLU A 501      -2.159 -39.671 -55.366  1.00 62.63           O  
ANISOU 4133  OE1 GLU A 501     7732   7458   8608   -325    270  -1444       O  
ATOM   4134  OE2 GLU A 501      -2.613 -37.525 -55.516  1.00 62.95           O  
ANISOU 4134  OE2 GLU A 501     7749   7560   8607   -300     89  -1399       O  
ATOM   4135  N   ALA A 502       1.342 -41.557 -52.000  1.00 48.07           N  
ANISOU 4135  N   ALA A 502     6171   5622   6470   -267    849  -1116       N  
ATOM   4136  CA  ALA A 502       1.915 -42.891 -51.838  1.00 49.27           C  
ANISOU 4136  CA  ALA A 502     6369   5727   6624   -261    949  -1115       C  
ATOM   4137  C   ALA A 502       1.262 -43.677 -50.698  1.00 51.81           C  
ANISOU 4137  C   ALA A 502     6688   5917   7080   -279   1116  -1117       C  
ATOM   4138  O   ALA A 502       1.131 -44.904 -50.776  1.00 52.63           O  
ANISOU 4138  O   ALA A 502     6786   5946   7265   -294   1193  -1166       O  
ATOM   4139  CB  ALA A 502       3.408 -42.794 -51.626  1.00 46.97           C  
ANISOU 4139  CB  ALA A 502     6173   5503   6170   -216    953  -1018       C  
ATOM   4140  N   LEU A 503       0.845 -42.966 -49.651  1.00 52.75           N  
ANISOU 4140  N   LEU A 503     6822   5997   7222   -281   1183  -1066       N  
ATOM   4141  CA  LEU A 503       0.211 -43.582 -48.484  1.00 54.27           C  
ANISOU 4141  CA  LEU A 503     7045   6047   7527   -300   1370  -1059       C  
ATOM   4142  C   LEU A 503      -1.094 -44.318 -48.787  1.00 56.97           C  
ANISOU 4142  C   LEU A 503     7264   6277   8103   -354   1437  -1182       C  
ATOM   4143  O   LEU A 503      -1.566 -45.094 -47.958  1.00 57.87           O  
ANISOU 4143  O   LEU A 503     7407   6257   8325   -376   1618  -1189       O  
ATOM   4144  CB  LEU A 503      -0.019 -42.543 -47.383  1.00 53.08           C  
ANISOU 4144  CB  LEU A 503     6949   5873   7347   -295   1430   -988       C  
ATOM   4145  CG  LEU A 503       1.110 -42.382 -46.363  1.00 51.90           C  
ANISOU 4145  CG  LEU A 503     6972   5733   7013   -247   1466   -862       C  
ATOM   4146  CD1 LEU A 503       1.010 -41.039 -45.650  1.00 50.43           C  
ANISOU 4146  CD1 LEU A 503     6829   5570   6763   -238   1455   -802       C  
ATOM   4147  CD2 LEU A 503       1.103 -43.534 -45.365  1.00 51.41           C  
ANISOU 4147  CD2 LEU A 503     7030   5527   6975   -245   1644   -835       C  
ATOM   4148  N   HIS A 504      -1.672 -44.070 -49.962  1.00 59.37           N  
ANISOU 4148  N   HIS A 504     7442   6626   8490   -375   1289  -1280       N  
ATOM   4149  CA  HIS A 504      -2.885 -44.770 -50.383  1.00 63.98           C  
ANISOU 4149  CA  HIS A 504     7889   7101   9319   -424   1312  -1414       C  
ATOM   4150  C   HIS A 504      -2.589 -46.230 -50.706  1.00 65.36           C  
ANISOU 4150  C   HIS A 504     8088   7228   9519   -432   1370  -1456       C  
ATOM   4151  O   HIS A 504      -3.458 -47.090 -50.567  1.00 66.76           O  
ANISOU 4151  O   HIS A 504     8187   7273   9904   -474   1476  -1542       O  
ATOM   4152  CB  HIS A 504      -3.546 -44.080 -51.580  1.00 65.15           C  
ANISOU 4152  CB  HIS A 504     7914   7302   9538   -434   1096  -1509       C  
ATOM   4153  CG  HIS A 504      -3.995 -42.678 -51.300  1.00 67.97           C  
ANISOU 4153  CG  HIS A 504     8226   7687   9911   -428   1037  -1481       C  
ATOM   4154  ND1 HIS A 504      -4.453 -42.272 -50.064  1.00 70.42           N  
ANISOU 4154  ND1 HIS A 504     8534   7916  10305   -440   1206  -1438       N  
ATOM   4155  CD2 HIS A 504      -4.073 -41.591 -52.104  1.00 68.56           C  
ANISOU 4155  CD2 HIS A 504     8269   7854   9929   -411    834  -1493       C  
ATOM   4156  CE1 HIS A 504      -4.779 -40.993 -50.115  1.00 70.21           C  
ANISOU 4156  CE1 HIS A 504     8461   7934  10280   -430   1109  -1425       C  
ATOM   4157  NE2 HIS A 504      -4.559 -40.556 -51.342  1.00 69.82           N  
ANISOU 4157  NE2 HIS A 504     8391   7990  10148   -411    879  -1456       N  
ATOM   4158  N   ASN A 505      -1.354 -46.495 -51.128  1.00 65.95           N  
ANISOU 4158  N   ASN A 505     8264   7398   9395   -394   1310  -1400       N  
ATOM   4159  CA  ASN A 505      -0.883 -47.854 -51.389  1.00 67.44           C  
ANISOU 4159  CA  ASN A 505     8492   7546   9584   -394   1371  -1425       C  
ATOM   4160  C   ASN A 505       0.419 -48.163 -50.642  1.00 66.21           C  
ANISOU 4160  C   ASN A 505     8483   7413   9260   -345   1453  -1300       C  
ATOM   4161  O   ASN A 505       1.489 -48.219 -51.257  1.00 65.61           O  
ANISOU 4161  O   ASN A 505     8457   7428   9043   -311   1370  -1271       O  
ATOM   4162  CB  ASN A 505      -0.705 -48.083 -52.896  1.00 68.58           C  
ANISOU 4162  CB  ASN A 505     8602   7763   9691   -397   1204  -1513       C  
ATOM   4163  CG  ASN A 505      -2.028 -48.118 -53.644  1.00 72.60           C  
ANISOU 4163  CG  ASN A 505     8973   8214  10396   -443   1108  -1656       C  
ATOM   4164  OD1 ASN A 505      -2.402 -47.153 -54.315  1.00 73.60           O  
ANISOU 4164  OD1 ASN A 505     9055   8402  10507   -442    940  -1690       O  
ATOM   4165  ND2 ASN A 505      -2.748 -49.232 -53.525  1.00 74.14           N  
ANISOU 4165  ND2 ASN A 505     9100   8280  10790   -482   1208  -1744       N  
ATOM   4166  N   PRO A 506       0.336 -48.358 -49.309  1.00 65.99           N  
ANISOU 4166  N   PRO A 506     8533   7286   9252   -339   1615  -1229       N  
ATOM   4167  CA  PRO A 506       1.553 -48.663 -48.562  1.00 65.52           C  
ANISOU 4167  CA  PRO A 506     8624   7230   9040   -285   1662  -1113       C  
ATOM   4168  C   PRO A 506       1.941 -50.136 -48.663  1.00 67.15           C  
ANISOU 4168  C   PRO A 506     8869   7361   9283   -279   1741  -1134       C  
ATOM   4169  O   PRO A 506       1.115 -51.018 -48.414  1.00 69.39           O  
ANISOU 4169  O   PRO A 506     9130   7517   9718   -318   1873  -1192       O  
ATOM   4170  CB  PRO A 506       1.190 -48.287 -47.123  1.00 65.08           C  
ANISOU 4170  CB  PRO A 506     8665   7079   8981   -284   1796  -1037       C  
ATOM   4171  CG  PRO A 506      -0.297 -48.400 -47.047  1.00 66.21           C  
ANISOU 4171  CG  PRO A 506     8705   7116   9338   -348   1905  -1132       C  
ATOM   4172  CD  PRO A 506      -0.852 -48.277 -48.437  1.00 66.78           C  
ANISOU 4172  CD  PRO A 506     8601   7258   9515   -381   1762  -1253       C  
ATOM   4173  N   ASN A 507       3.191 -50.390 -49.039  1.00 67.70           N  
ANISOU 4173  N   ASN A 507     8988   7501   9232   -231   1668  -1090       N  
ATOM   4174  CA  ASN A 507       3.710 -51.751 -49.148  1.00 69.35           C  
ANISOU 4174  CA  ASN A 507     9238   7643   9470   -216   1733  -1103       C  
ATOM   4175  C   ASN A 507       3.912 -52.369 -47.771  1.00 71.24           C  
ANISOU 4175  C   ASN A 507     9619   7750   9699   -186   1869  -1014       C  
ATOM   4176  O   ASN A 507       4.120 -51.658 -46.788  1.00 70.70           O  
ANISOU 4176  O   ASN A 507     9649   7672   9541   -158   1875   -921       O  
ATOM   4177  CB  ASN A 507       5.021 -51.771 -49.940  1.00 68.01           C  
ANISOU 4177  CB  ASN A 507     9072   7576   9193   -172   1624  -1085       C  
ATOM   4178  CG  ASN A 507       4.881 -51.153 -51.324  1.00 67.33           C  
ANISOU 4178  CG  ASN A 507     8891   7607   9084   -199   1500  -1167       C  
ATOM   4179  OD1 ASN A 507       4.252 -50.101 -51.493  1.00 63.30           O  
ANISOU 4179  OD1 ASN A 507     8334   7155   8563   -222   1430  -1181       O  
ATOM   4180  ND2 ASN A 507       5.478 -51.800 -52.323  1.00 64.47           N  
ANISOU 4180  ND2 ASN A 507     8515   7272   8707   -194   1473  -1220       N  
ATOM   4181  N   LEU A 508       3.832 -53.693 -47.695  1.00 73.42           N  
ANISOU 4181  N   LEU A 508     9923   7913  10059   -192   1977  -1045       N  
ATOM   4182  CA  LEU A 508       3.997 -54.372 -46.417  1.00 75.03           C  
ANISOU 4182  CA  LEU A 508    10291   7971  10245   -163   2110   -960       C  
ATOM   4183  C   LEU A 508       5.400 -54.944 -46.275  1.00 75.54           C  
ANISOU 4183  C   LEU A 508    10449   8037  10217    -86   2049   -886       C  
ATOM   4184  O   LEU A 508       5.750 -55.940 -46.915  1.00 77.05           O  
ANISOU 4184  O   LEU A 508    10600   8209  10467    -81   2058   -935       O  
ATOM   4185  CB  LEU A 508       2.926 -55.445 -46.223  1.00 76.39           C  
ANISOU 4185  CB  LEU A 508    10454   7986  10585   -219   2294  -1032       C  
ATOM   4186  CG  LEU A 508       1.545 -54.984 -45.746  1.00 77.54           C  
ANISOU 4186  CG  LEU A 508    10561   8052  10847   -284   2418  -1074       C  
ATOM   4187  CD1 LEU A 508       0.576 -56.152 -45.805  1.00 78.27           C  
ANISOU 4187  CD1 LEU A 508    10604   7990  11144   -344   2592  -1168       C  
ATOM   4188  CD2 LEU A 508       1.590 -54.383 -44.335  1.00 75.93           C  
ANISOU 4188  CD2 LEU A 508    10541   7776  10532   -257   2505   -957       C  
ATOM   4189  N   SER A 509       6.197 -54.284 -45.437  1.00 75.19           N  
ANISOU 4189  N   SER A 509    10523   8008  10038    -26   1978   -774       N  
ATOM   4190  CA  SER A 509       7.603 -54.625 -45.230  1.00 75.26           C  
ANISOU 4190  CA  SER A 509    10606   8016   9975     57   1884   -700       C  
ATOM   4191  C   SER A 509       8.173 -53.863 -44.038  1.00 74.75           C  
ANISOU 4191  C   SER A 509    10698   7927   9776    116   1815   -581       C  
ATOM   4192  O   SER A 509       7.556 -52.915 -43.539  1.00 75.21           O  
ANISOU 4192  O   SER A 509    10793   8002   9781     90   1831   -559       O  
ATOM   4193  CB  SER A 509       8.425 -54.299 -46.482  1.00 74.55           C  
ANISOU 4193  CB  SER A 509    10366   8075   9885     67   1753   -747       C  
ATOM   4194  OG  SER A 509       8.316 -52.926 -46.814  1.00 74.18           O  
ANISOU 4194  OG  SER A 509    10249   8160   9776     48   1660   -748       O  
ATOM   4195  N   VAL A 510       9.349 -54.290 -43.585  1.00 74.36           N  
ANISOU 4195  N   VAL A 510    10743   7829   9681    197   1730   -509       N  
ATOM   4196  CA  VAL A 510      10.106 -53.544 -42.585  1.00 73.89           C  
ANISOU 4196  CA  VAL A 510    10823   7754   9497    264   1609   -403       C  
ATOM   4197  C   VAL A 510      11.233 -52.804 -43.299  1.00 72.11           C  
ANISOU 4197  C   VAL A 510    10457   7670   9270    299   1432   -406       C  
ATOM   4198  O   VAL A 510      12.148 -53.419 -43.856  1.00 71.92           O  
ANISOU 4198  O   VAL A 510    10358   7652   9316    338   1376   -424       O  
ATOM   4199  CB  VAL A 510      10.651 -54.448 -41.445  1.00 75.93           C  
ANISOU 4199  CB  VAL A 510    11307   7834   9708    340   1607   -316       C  
ATOM   4200  CG1 VAL A 510      11.521 -53.641 -40.478  1.00 76.75           C  
ANISOU 4200  CG1 VAL A 510    11556   7921   9685    416   1437   -216       C  
ATOM   4201  CG2 VAL A 510       9.502 -55.106 -40.690  1.00 77.45           C  
ANISOU 4201  CG2 VAL A 510    11663   7870   9894    299   1814   -309       C  
ATOM   4202  N   ASP A 511      11.136 -51.477 -43.289  1.00 69.23           N  
ANISOU 4202  N   ASP A 511    10056   7410   8837    282   1361   -392       N  
ATOM   4203  CA  ASP A 511      12.094 -50.608 -43.961  1.00 66.77           C  
ANISOU 4203  CA  ASP A 511     9613   7231   8526    304   1216   -397       C  
ATOM   4204  C   ASP A 511      12.319 -49.336 -43.151  1.00 64.88           C  
ANISOU 4204  C   ASP A 511     9452   7021   8180    328   1109   -326       C  
ATOM   4205  O   ASP A 511      11.694 -49.137 -42.104  1.00 65.67           O  
ANISOU 4205  O   ASP A 511     9715   7040   8196    325   1155   -276       O  
ATOM   4206  CB  ASP A 511      11.607 -50.268 -45.377  1.00 66.08           C  
ANISOU 4206  CB  ASP A 511     9338   7278   8490    233   1254   -494       C  
ATOM   4207  CG  ASP A 511      10.128 -49.906 -45.424  1.00 64.62           C  
ANISOU 4207  CG  ASP A 511     9146   7107   8298    157   1354   -537       C  
ATOM   4208  OD1 ASP A 511       9.596 -49.373 -44.427  1.00 64.53           O  
ANISOU 4208  OD1 ASP A 511     9247   7049   8223    155   1379   -485       O  
ATOM   4209  OD2 ASP A 511       9.494 -50.154 -46.470  1.00 64.22           O  
ANISOU 4209  OD2 ASP A 511     8980   7106   8314    101   1406   -628       O  
ATOM   4210  N   GLU A 512      13.214 -48.484 -43.637  1.00 61.89           N  
ANISOU 4210  N   GLU A 512     8962   6747   7807    348    981   -324       N  
ATOM   4211  CA  GLU A 512      13.522 -47.224 -42.972  1.00 59.82           C  
ANISOU 4211  CA  GLU A 512     8753   6520   7457    369    866   -266       C  
ATOM   4212  C   GLU A 512      13.171 -46.026 -43.858  1.00 56.39           C  
ANISOU 4212  C   GLU A 512     8175   6239   7012    311    862   -309       C  
ATOM   4213  O   GLU A 512      13.226 -46.131 -45.087  1.00 55.17           O  
ANISOU 4213  O   GLU A 512     7870   6168   6923    277    893   -377       O  
ATOM   4214  CB  GLU A 512      14.998 -47.184 -42.558  1.00 61.65           C  
ANISOU 4214  CB  GLU A 512     8996   6711   7716    455    695   -216       C  
ATOM   4215  CG  GLU A 512      15.323 -47.997 -41.297  1.00 66.83           C  
ANISOU 4215  CG  GLU A 512     9862   7197   8334    529    642   -146       C  
ATOM   4216  CD  GLU A 512      14.742 -47.389 -40.020  1.00 69.62           C  
ANISOU 4216  CD  GLU A 512    10441   7481   8530    535    630    -77       C  
ATOM   4217  OE1 GLU A 512      14.021 -48.107 -39.291  1.00 69.30           O  
ANISOU 4217  OE1 GLU A 512    10587   7318   8426    532    741    -50       O  
ATOM   4218  OE2 GLU A 512      15.002 -46.193 -39.747  1.00 70.34           O  
ANISOU 4218  OE2 GLU A 512    10532   7632   8564    539    524    -53       O  
ATOM   4219  N   PRO A 513      12.792 -44.887 -43.239  1.00 54.40           N  
ANISOU 4219  N   PRO A 513     7986   6015   6670    299    826   -270       N  
ATOM   4220  CA  PRO A 513      12.553 -43.672 -44.012  1.00 52.43           C  
ANISOU 4220  CA  PRO A 513     7612   5903   6408    253    802   -301       C  
ATOM   4221  C   PRO A 513      13.810 -43.276 -44.775  1.00 52.35           C  
ANISOU 4221  C   PRO A 513     7473   5969   6449    279    699   -311       C  
ATOM   4222  O   PRO A 513      14.918 -43.450 -44.264  1.00 54.98           O  
ANISOU 4222  O   PRO A 513     7832   6246   6811    343    598   -271       O  
ATOM   4223  CB  PRO A 513      12.234 -42.627 -42.936  1.00 51.89           C  
ANISOU 4223  CB  PRO A 513     7664   5816   6237    258    761   -241       C  
ATOM   4224  CG  PRO A 513      12.752 -43.197 -41.667  1.00 52.94           C  
ANISOU 4224  CG  PRO A 513     7983   5811   6320    324    713   -172       C  
ATOM   4225  CD  PRO A 513      12.566 -44.662 -41.801  1.00 53.78           C  
ANISOU 4225  CD  PRO A 513     8113   5831   6488    329    810   -196       C  
ATOM   4226  N   LEU A 514      13.634 -42.777 -45.995  1.00 50.45           N  
ANISOU 4226  N   LEU A 514     7101   5840   6229    231    725   -368       N  
ATOM   4227  CA  LEU A 514      14.750 -42.338 -46.827  1.00 50.34           C  
ANISOU 4227  CA  LEU A 514     6970   5891   6265    243    669   -385       C  
ATOM   4228  C   LEU A 514      15.427 -41.125 -46.211  1.00 49.69           C  
ANISOU 4228  C   LEU A 514     6896   5832   6153    271    551   -329       C  
ATOM   4229  O   LEU A 514      14.755 -40.231 -45.702  1.00 48.40           O  
ANISOU 4229  O   LEU A 514     6790   5695   5905    251    532   -301       O  
ATOM   4230  CB  LEU A 514      14.252 -41.975 -48.227  1.00 50.01           C  
ANISOU 4230  CB  LEU A 514     6836   5952   6215    181    731   -454       C  
ATOM   4231  CG  LEU A 514      14.144 -43.014 -49.343  1.00 51.30           C  
ANISOU 4231  CG  LEU A 514     6948   6113   6430    157    821   -531       C  
ATOM   4232  CD1 LEU A 514      13.734 -44.408 -48.862  1.00 51.59           C  
ANISOU 4232  CD1 LEU A 514     7040   6050   6510    169    883   -542       C  
ATOM   4233  CD2 LEU A 514      13.172 -42.490 -50.384  1.00 51.93           C  
ANISOU 4233  CD2 LEU A 514     7000   6276   6455     94    852   -590       C  
ATOM   4234  N   ASP A 515      16.755 -41.106 -46.256  1.00 50.80           N  
ANISOU 4234  N   ASP A 515     6970   5951   6380    316    474   -319       N  
ATOM   4235  CA  ASP A 515      17.524 -39.964 -45.782  1.00 51.00           C  
ANISOU 4235  CA  ASP A 515     6976   5991   6409    342    353   -279       C  
ATOM   4236  C   ASP A 515      17.577 -38.923 -46.895  1.00 48.97           C  
ANISOU 4236  C   ASP A 515     6609   5847   6149    290    392   -313       C  
ATOM   4237  O   ASP A 515      18.433 -38.993 -47.785  1.00 49.63           O  
ANISOU 4237  O   ASP A 515     6580   5946   6331    288    425   -351       O  
ATOM   4238  CB  ASP A 515      18.934 -40.397 -45.361  1.00 54.82           C  
ANISOU 4238  CB  ASP A 515     7418   6386   7025    414    245   -264       C  
ATOM   4239  CG  ASP A 515      19.751 -39.254 -44.763  1.00 60.18           C  
ANISOU 4239  CG  ASP A 515     8076   7061   7729    444     97   -229       C  
ATOM   4240  OD1 ASP A 515      20.990 -39.266 -44.941  1.00 62.25           O  
ANISOU 4240  OD1 ASP A 515     8220   7283   8147    481     28   -245       O  
ATOM   4241  OD2 ASP A 515      19.164 -38.350 -44.119  1.00 60.96           O  
ANISOU 4241  OD2 ASP A 515     8268   7187   7706    429     52   -191       O  
ATOM   4242  N   VAL A 516      16.649 -37.970 -46.842  1.00 44.29           N  
ANISOU 4242  N   VAL A 516     6058   5321   5449    249    399   -301       N  
ATOM   4243  CA  VAL A 516      16.506 -36.967 -47.893  1.00 41.32           C  
ANISOU 4243  CA  VAL A 516     5609   5046   5046    200    434   -328       C  
ATOM   4244  C   VAL A 516      16.449 -35.534 -47.361  1.00 40.03           C  
ANISOU 4244  C   VAL A 516     5466   4922   4823    194    356   -285       C  
ATOM   4245  O   VAL A 516      16.042 -35.286 -46.220  1.00 39.33           O  
ANISOU 4245  O   VAL A 516     5471   4796   4676    212    298   -241       O  
ATOM   4246  CB  VAL A 516      15.253 -37.232 -48.769  1.00 41.14           C  
ANISOU 4246  CB  VAL A 516     5598   5074   4958    145    530   -378       C  
ATOM   4247  CG1 VAL A 516      15.448 -38.475 -49.619  1.00 43.26           C  
ANISOU 4247  CG1 VAL A 516     5832   5318   5287    141    613   -435       C  
ATOM   4248  CG2 VAL A 516      13.995 -37.358 -47.905  1.00 40.18           C  
ANISOU 4248  CG2 VAL A 516     5568   4925   4775    134    538   -360       C  
ATOM   4249  N   ASP A 517      16.861 -34.594 -48.207  1.00 38.33           N  
ANISOU 4249  N   ASP A 517     5174   4773   4617    167    365   -299       N  
ATOM   4250  CA  ASP A 517      16.716 -33.173 -47.920  1.00 35.49           C  
ANISOU 4250  CA  ASP A 517     4824   4459   4200    153    307   -266       C  
ATOM   4251  C   ASP A 517      15.350 -32.725 -48.440  1.00 33.40           C  
ANISOU 4251  C   ASP A 517     4597   4261   3833    104    357   -282       C  
ATOM   4252  O   ASP A 517      15.137 -32.592 -49.650  1.00 32.22           O  
ANISOU 4252  O   ASP A 517     4415   4163   3664     69    415   -321       O  
ATOM   4253  CB  ASP A 517      17.857 -32.367 -48.563  1.00 34.38           C  
ANISOU 4253  CB  ASP A 517     4586   4341   4135    148    301   -273       C  
ATOM   4254  CG  ASP A 517      17.931 -30.937 -48.047  1.00 34.89           C  
ANISOU 4254  CG  ASP A 517     4659   4433   4166    142    222   -233       C  
ATOM   4255  OD1 ASP A 517      19.046 -30.381 -47.998  1.00 39.51           O  
ANISOU 4255  OD1 ASP A 517     5168   4996   4847    156    179   -228       O  
ATOM   4256  OD2 ASP A 517      16.884 -30.363 -47.676  1.00 34.05           O  
ANISOU 4256  OD2 ASP A 517     4625   4361   3951    124    207   -212       O  
ATOM   4257  N   TYR A 518      14.422 -32.505 -47.517  1.00 31.54           N  
ANISOU 4257  N   TYR A 518     4438   4009   3536    103    333   -255       N  
ATOM   4258  CA  TYR A 518      13.044 -32.167 -47.873  1.00 30.47           C  
ANISOU 4258  CA  TYR A 518     4322   3913   3341     62    373   -277       C  
ATOM   4259  C   TYR A 518      12.874 -30.765 -48.482  1.00 30.07           C  
ANISOU 4259  C   TYR A 518     4242   3937   3247     34    344   -272       C  
ATOM   4260  O   TYR A 518      11.821 -30.463 -49.032  1.00 29.87           O  
ANISOU 4260  O   TYR A 518     4216   3944   3189      3    361   -300       O  
ATOM   4261  CB  TYR A 518      12.123 -32.346 -46.663  1.00 29.95           C  
ANISOU 4261  CB  TYR A 518     4345   3788   3247     68    385   -255       C  
ATOM   4262  CG  TYR A 518      11.992 -33.779 -46.199  1.00 28.56           C  
ANISOU 4262  CG  TYR A 518     4217   3531   3103     86    438   -265       C  
ATOM   4263  CD1 TYR A 518      12.820 -34.288 -45.206  1.00 31.65           C  
ANISOU 4263  CD1 TYR A 518     4679   3845   3500    135    395   -223       C  
ATOM   4264  CD2 TYR A 518      11.042 -34.625 -46.755  1.00 27.28           C  
ANISOU 4264  CD2 TYR A 518     4035   3359   2970     56    520   -319       C  
ATOM   4265  CE1 TYR A 518      12.701 -35.610 -44.777  1.00 32.70           C  
ANISOU 4265  CE1 TYR A 518     4873   3894   3657    155    444   -228       C  
ATOM   4266  CE2 TYR A 518      10.915 -35.940 -46.334  1.00 27.42           C  
ANISOU 4266  CE2 TYR A 518     4100   3296   3022     71    580   -329       C  
ATOM   4267  CZ  TYR A 518      11.746 -36.425 -45.349  1.00 30.99           C  
ANISOU 4267  CZ  TYR A 518     4633   3673   3470    120    547   -279       C  
ATOM   4268  OH  TYR A 518      11.624 -37.733 -44.932  1.00 37.29           O  
ANISOU 4268  OH  TYR A 518     5492   4381   4296    137    607   -284       O  
ATOM   4269  N   ARG A 519      13.915 -29.935 -48.406  1.00 29.42           N  
ANISOU 4269  N   ARG A 519     4131   3869   3177     47    297   -241       N  
ATOM   4270  CA  ARG A 519      13.880 -28.571 -48.953  1.00 31.06           C  
ANISOU 4270  CA  ARG A 519     4319   4137   3346     22    275   -231       C  
ATOM   4271  C   ARG A 519      13.972 -28.531 -50.476  1.00 31.70           C  
ANISOU 4271  C   ARG A 519     4372   4262   3410     -7    329   -270       C  
ATOM   4272  O   ARG A 519      13.844 -27.460 -51.076  1.00 32.76           O  
ANISOU 4272  O   ARG A 519     4512   4439   3497    -29    319   -262       O  
ATOM   4273  CB  ARG A 519      15.011 -27.711 -48.362  1.00 32.11           C  
ANISOU 4273  CB  ARG A 519     4428   4258   3516     42    213   -190       C  
ATOM   4274  CG  ARG A 519      14.936 -27.473 -46.835  1.00 34.08           C  
ANISOU 4274  CG  ARG A 519     4742   4458   3750     71    136   -149       C  
ATOM   4275  CD  ARG A 519      16.181 -26.740 -46.326  1.00 34.90           C  
ANISOU 4275  CD  ARG A 519     4813   4538   3911     94     50   -122       C  
ATOM   4276  NE  ARG A 519      17.405 -27.482 -46.642  1.00 38.83           N  
ANISOU 4276  NE  ARG A 519     5233   4998   4524    118     48   -142       N  
ATOM   4277  CZ  ARG A 519      18.629 -26.960 -46.684  1.00 40.65           C  
ANISOU 4277  CZ  ARG A 519     5380   5206   4860    129      2   -142       C  
ATOM   4278  NH1 ARG A 519      18.830 -25.666 -46.436  1.00 38.74           N  
ANISOU 4278  NH1 ARG A 519     5128   4981   4612    117    -51   -121       N  
ATOM   4279  NH2 ARG A 519      19.656 -27.741 -46.986  1.00 39.94           N  
ANISOU 4279  NH2 ARG A 519     5207   5069   4902    152     14   -169       N  
ATOM   4280  N   PHE A 520      14.206 -29.686 -51.097  1.00 31.90           N  
ANISOU 4280  N   PHE A 520     4386   4269   3466     -6    388   -311       N  
ATOM   4281  CA  PHE A 520      14.344 -29.774 -52.554  1.00 34.14           C  
ANISOU 4281  CA  PHE A 520     4676   4577   3717    -32    451   -353       C  
ATOM   4282  C   PHE A 520      13.411 -30.833 -53.114  1.00 33.65           C  
ANISOU 4282  C   PHE A 520     4646   4509   3630    -45    477   -408       C  
ATOM   4283  O   PHE A 520      13.240 -31.899 -52.511  1.00 32.70           O  
ANISOU 4283  O   PHE A 520     4514   4348   3561    -29    490   -419       O  
ATOM   4284  CB  PHE A 520      15.799 -30.066 -52.962  1.00 36.33           C  
ANISOU 4284  CB  PHE A 520     4906   4825   4074    -23    519   -361       C  
ATOM   4285  CG  PHE A 520      16.773 -29.020 -52.491  1.00 40.10           C  
ANISOU 4285  CG  PHE A 520     5333   5296   4608    -14    490   -320       C  
ATOM   4286  CD1 PHE A 520      17.009 -27.872 -53.256  1.00 41.49           C  
ANISOU 4286  CD1 PHE A 520     5522   5500   4741    -42    522   -311       C  
ATOM   4287  CD2 PHE A 520      17.429 -29.159 -51.266  1.00 37.87           C  
ANISOU 4287  CD2 PHE A 520     5001   4970   4419     24    422   -290       C  
ATOM   4288  CE1 PHE A 520      17.893 -26.879 -52.812  1.00 40.61           C  
ANISOU 4288  CE1 PHE A 520     5356   5376   4699    -38    499   -278       C  
ATOM   4289  CE2 PHE A 520      18.315 -28.175 -50.812  1.00 40.19           C  
ANISOU 4289  CE2 PHE A 520     5243   5250   4780     33    375   -260       C  
ATOM   4290  CZ  PHE A 520      18.550 -27.034 -51.589  1.00 39.42           C  
ANISOU 4290  CZ  PHE A 520     5137   5182   4657     -1    420   -256       C  
ATOM   4291  N   ASP A 521      12.808 -30.526 -54.261  1.00 32.83           N  
ANISOU 4291  N   ASP A 521     4591   4435   3449    -73    477   -443       N  
ATOM   4292  CA  ASP A 521      11.857 -31.426 -54.922  1.00 32.86           C  
ANISOU 4292  CA  ASP A 521     4628   4428   3430    -87    477   -507       C  
ATOM   4293  C   ASP A 521      12.417 -32.843 -55.059  1.00 31.73           C  
ANISOU 4293  C   ASP A 521     4469   4242   3343    -79    555   -544       C  
ATOM   4294  O   ASP A 521      13.573 -33.026 -55.450  1.00 32.87           O  
ANISOU 4294  O   ASP A 521     4606   4373   3511    -73    627   -544       O  
ATOM   4295  CB  ASP A 521      11.449 -30.853 -56.285  1.00 35.02           C  
ANISOU 4295  CB  ASP A 521     4982   4725   3597   -111    451   -540       C  
ATOM   4296  CG  ASP A 521      10.543 -29.633 -56.153  1.00 38.12           C  
ANISOU 4296  CG  ASP A 521     5388   5148   3948   -116    352   -515       C  
ATOM   4297  OD1 ASP A 521       9.380 -29.800 -55.731  1.00 40.90           O  
ANISOU 4297  OD1 ASP A 521     5709   5489   4341   -117    289   -538       O  
ATOM   4298  OD2 ASP A 521      10.987 -28.507 -56.461  1.00 40.18           O  
ANISOU 4298  OD2 ASP A 521     5685   5433   4151   -120    344   -477       O  
ATOM   4299  N   PHE A 522      11.613 -33.845 -54.708  1.00 30.16           N  
ANISOU 4299  N   PHE A 522     4259   4013   3188    -78    551   -578       N  
ATOM   4300  CA  PHE A 522      12.081 -35.228 -54.787  1.00 31.86           C  
ANISOU 4300  CA  PHE A 522     4462   4182   3463    -68    624   -613       C  
ATOM   4301  C   PHE A 522      12.448 -35.589 -56.225  1.00 32.13           C  
ANISOU 4301  C   PHE A 522     4547   4217   3445    -88    680   -672       C  
ATOM   4302  O   PHE A 522      11.681 -35.326 -57.148  1.00 32.27           O  
ANISOU 4302  O   PHE A 522     4629   4252   3380   -112    639   -715       O  
ATOM   4303  CB  PHE A 522      11.037 -36.218 -54.251  1.00 30.52           C  
ANISOU 4303  CB  PHE A 522     4280   3971   3347    -71    620   -646       C  
ATOM   4304  CG  PHE A 522      10.872 -36.194 -52.753  1.00 30.84           C  
ANISOU 4304  CG  PHE A 522     4300   3979   3439    -49    610   -590       C  
ATOM   4305  CD1 PHE A 522      11.905 -35.767 -51.921  1.00 30.10           C  
ANISOU 4305  CD1 PHE A 522     4199   3880   3359    -16    599   -522       C  
ATOM   4306  CD2 PHE A 522       9.685 -36.634 -52.172  1.00 30.02           C  
ANISOU 4306  CD2 PHE A 522     4195   3833   3376    -60    615   -610       C  
ATOM   4307  CE1 PHE A 522      11.748 -35.758 -50.533  1.00 31.10           C  
ANISOU 4307  CE1 PHE A 522     4347   3963   3507      7    581   -471       C  
ATOM   4308  CE2 PHE A 522       9.517 -36.630 -50.790  1.00 28.53           C  
ANISOU 4308  CE2 PHE A 522     4025   3598   3217    -42    629   -559       C  
ATOM   4309  CZ  PHE A 522      10.547 -36.193 -49.967  1.00 30.06           C  
ANISOU 4309  CZ  PHE A 522     4241   3789   3392     -7    606   -487       C  
ATOM   4310  N   SER A 523      13.631 -36.174 -56.397  1.00 34.16           N  
ANISOU 4310  N   SER A 523     4784   4442   3754    -74    770   -676       N  
ATOM   4311  CA  SER A 523      14.069 -36.724 -57.682  1.00 36.46           C  
ANISOU 4311  CA  SER A 523     5134   4712   4008    -92    860   -738       C  
ATOM   4312  C   SER A 523      13.207 -37.925 -58.089  1.00 37.66           C  
ANISOU 4312  C   SER A 523     5319   4835   4155   -105    859   -811       C  
ATOM   4313  O   SER A 523      12.361 -38.377 -57.316  1.00 37.68           O  
ANISOU 4313  O   SER A 523     5281   4827   4207   -100    805   -811       O  
ATOM   4314  CB  SER A 523      15.542 -37.140 -57.598  1.00 36.54           C  
ANISOU 4314  CB  SER A 523     5086   4677   4122    -72    969   -729       C  
ATOM   4315  OG  SER A 523      15.708 -38.274 -56.760  1.00 38.12           O  
ANISOU 4315  OG  SER A 523     5218   4829   4437    -42    975   -729       O  
ATOM   4316  N   ASP A 524      13.426 -38.435 -59.298  1.00 40.95           N  
ANISOU 4316  N   ASP A 524     5817   5227   4515   -125    928   -876       N  
ATOM   4317  CA  ASP A 524      12.714 -39.624 -59.777  1.00 44.38           C  
ANISOU 4317  CA  ASP A 524     6287   5625   4950   -138    929   -956       C  
ATOM   4318  C   ASP A 524      13.064 -40.896 -58.997  1.00 44.63           C  
ANISOU 4318  C   ASP A 524     6232   5606   5119   -116    992   -960       C  
ATOM   4319  O   ASP A 524      12.167 -41.665 -58.648  1.00 44.76           O  
ANISOU 4319  O   ASP A 524     6228   5599   5180   -120    954   -992       O  
ATOM   4320  CB  ASP A 524      12.928 -39.826 -61.282  1.00 46.03           C  
ANISOU 4320  CB  ASP A 524     6634   5811   5045   -164    990  -1027       C  
ATOM   4321  CG  ASP A 524      12.214 -38.768 -62.125  1.00 50.42           C  
ANISOU 4321  CG  ASP A 524     7316   6400   5443   -185    889  -1037       C  
ATOM   4322  OD1 ASP A 524      11.342 -38.042 -61.593  1.00 50.07           O  
ANISOU 4322  OD1 ASP A 524     7231   6395   5399   -182    759  -1006       O  
ATOM   4323  OD2 ASP A 524      12.526 -38.663 -63.331  1.00 53.13           O  
ANISOU 4323  OD2 ASP A 524     7810   6718   5660   -203    942  -1078       O  
ATOM   4324  N   GLU A 525      14.355 -41.105 -58.720  1.00 46.01           N  
ANISOU 4324  N   GLU A 525     6354   5751   5375    -90   1085   -929       N  
ATOM   4325  CA  GLU A 525      14.812 -42.266 -57.935  1.00 46.57           C  
ANISOU 4325  CA  GLU A 525     6349   5763   5583    -58   1131   -924       C  
ATOM   4326  C   GLU A 525      14.224 -42.265 -56.521  1.00 45.37           C  
ANISOU 4326  C   GLU A 525     6146   5610   5484    -35   1044   -865       C  
ATOM   4327  O   GLU A 525      13.912 -43.327 -55.972  1.00 45.42           O  
ANISOU 4327  O   GLU A 525     6135   5563   5559    -22   1058   -877       O  
ATOM   4328  CB  GLU A 525      16.350 -42.375 -57.900  1.00 48.34           C  
ANISOU 4328  CB  GLU A 525     6512   5945   5911    -29   1226   -905       C  
ATOM   4329  CG  GLU A 525      17.094 -41.236 -57.172  1.00 51.32           C  
ANISOU 4329  CG  GLU A 525     6824   6345   6330     -6   1181   -827       C  
ATOM   4330  CD  GLU A 525      18.590 -41.173 -57.507  1.00 56.35           C  
ANISOU 4330  CD  GLU A 525     7396   6932   7082      9   1287   -832       C  
ATOM   4331  OE1 GLU A 525      19.039 -40.153 -58.099  1.00 52.98           O  
ANISOU 4331  OE1 GLU A 525     6986   6528   6614    -13   1332   -826       O  
ATOM   4332  OE2 GLU A 525      19.315 -42.143 -57.178  1.00 57.27           O  
ANISOU 4332  OE2 GLU A 525     7441   6976   7343     44   1332   -845       O  
ATOM   4333  N   ILE A 526      14.061 -41.070 -55.950  1.00 43.18           N  
ANISOU 4333  N   ILE A 526     5858   5381   5166    -31    967   -803       N  
ATOM   4334  CA  ILE A 526      13.418 -40.919 -54.646  1.00 41.53           C  
ANISOU 4334  CA  ILE A 526     5630   5166   4983    -14    897   -749       C  
ATOM   4335  C   ILE A 526      11.921 -41.232 -54.730  1.00 41.10           C  
ANISOU 4335  C   ILE A 526     5601   5110   4905    -47    869   -796       C  
ATOM   4336  O   ILE A 526      11.395 -41.994 -53.906  1.00 39.61           O  
ANISOU 4336  O   ILE A 526     5405   4866   4777    -39    884   -792       O  
ATOM   4337  CB  ILE A 526      13.668 -39.516 -54.038  1.00 41.32           C  
ANISOU 4337  CB  ILE A 526     5591   5186   4921     -4    827   -677       C  
ATOM   4338  CG1 ILE A 526      15.122 -39.403 -53.556  1.00 41.96           C  
ANISOU 4338  CG1 ILE A 526     5623   5240   5081     37    837   -630       C  
ATOM   4339  CG2 ILE A 526      12.708 -39.245 -52.883  1.00 40.79           C  
ANISOU 4339  CG2 ILE A 526     5537   5112   4849      0    768   -636       C  
ATOM   4340  CD1 ILE A 526      15.624 -37.963 -53.381  1.00 41.77           C  
ANISOU 4340  CD1 ILE A 526     5580   5262   5030     39    785   -579       C  
ATOM   4341  N   LYS A 527      11.245 -40.661 -55.728  1.00 41.30           N  
ANISOU 4341  N   LYS A 527     5660   5181   4852    -82    829   -842       N  
ATOM   4342  CA  LYS A 527       9.821 -40.933 -55.953  1.00 43.39           C  
ANISOU 4342  CA  LYS A 527     5930   5432   5123   -113    782   -904       C  
ATOM   4343  C   LYS A 527       9.513 -42.428 -56.079  1.00 45.27           C  
ANISOU 4343  C   LYS A 527     6161   5601   5437   -121    842   -970       C  
ATOM   4344  O   LYS A 527       8.500 -42.899 -55.564  1.00 45.38           O  
ANISOU 4344  O   LYS A 527     6146   5572   5526   -135    837   -995       O  
ATOM   4345  CB  LYS A 527       9.298 -40.179 -57.178  1.00 43.25           C  
ANISOU 4345  CB  LYS A 527     5967   5460   5008   -141    706   -952       C  
ATOM   4346  CG  LYS A 527       8.649 -38.840 -56.851  1.00 45.98           C  
ANISOU 4346  CG  LYS A 527     6301   5850   5320   -145    611   -912       C  
ATOM   4347  CD  LYS A 527       8.215 -38.084 -58.107  1.00 48.19           C  
ANISOU 4347  CD  LYS A 527     6656   6163   5493   -164    519   -955       C  
ATOM   4348  CE  LYS A 527       9.367 -37.284 -58.698  1.00 49.47           C  
ANISOU 4348  CE  LYS A 527     6888   6366   5543   -157    555   -911       C  
ATOM   4349  NZ  LYS A 527       8.885 -36.208 -59.599  1.00 50.00           N  
ANISOU 4349  NZ  LYS A 527     7042   6462   5494   -169    454   -922       N  
ATOM   4350  N   GLU A 528      10.393 -43.168 -56.752  1.00 48.16           N  
ANISOU 4350  N   GLU A 528     6552   5949   5799   -114    912  -1001       N  
ATOM   4351  CA  GLU A 528      10.177 -44.601 -56.964  1.00 50.67           C  
ANISOU 4351  CA  GLU A 528     6867   6198   6186   -122    973  -1068       C  
ATOM   4352  C   GLU A 528      10.383 -45.413 -55.689  1.00 49.13           C  
ANISOU 4352  C   GLU A 528     6632   5939   6098    -92   1030  -1020       C  
ATOM   4353  O   GLU A 528       9.650 -46.372 -55.446  1.00 48.79           O  
ANISOU 4353  O   GLU A 528     6578   5832   6127   -105   1061  -1062       O  
ATOM   4354  CB  GLU A 528      11.047 -45.136 -58.105  1.00 53.42           C  
ANISOU 4354  CB  GLU A 528     7265   6535   6496   -125   1043  -1121       C  
ATOM   4355  CG  GLU A 528      10.710 -44.555 -59.485  1.00 60.20           C  
ANISOU 4355  CG  GLU A 528     8215   7431   7226   -158    993  -1184       C  
ATOM   4356  CD  GLU A 528       9.296 -44.885 -59.952  1.00 65.36           C  
ANISOU 4356  CD  GLU A 528     8891   8066   7879   -191    900  -1270       C  
ATOM   4357  OE1 GLU A 528       8.465 -43.949 -60.040  1.00 67.43           O  
ANISOU 4357  OE1 GLU A 528     9159   8364   8098   -204    784  -1269       O  
ATOM   4358  OE2 GLU A 528       9.015 -46.075 -60.226  1.00 66.35           O  
ANISOU 4358  OE2 GLU A 528     9018   8131   8062   -204    937  -1344       O  
ATOM   4359  N   LYS A 529      11.368 -45.021 -54.881  1.00 48.95           N  
ANISOU 4359  N   LYS A 529     6594   5920   6085    -50   1037   -933       N  
ATOM   4360  CA  LYS A 529      11.624 -45.668 -53.592  1.00 50.61           C  
ANISOU 4360  CA  LYS A 529     6799   6058   6371    -12   1065   -875       C  
ATOM   4361  C   LYS A 529      10.470 -45.466 -52.609  1.00 49.95           C  
ANISOU 4361  C   LYS A 529     6732   5949   6298    -25   1047   -850       C  
ATOM   4362  O   LYS A 529      10.116 -46.384 -51.867  1.00 49.81           O  
ANISOU 4362  O   LYS A 529     6736   5846   6344    -17   1102   -844       O  
ATOM   4363  CB  LYS A 529      12.929 -45.166 -52.969  1.00 51.66           C  
ANISOU 4363  CB  LYS A 529     6919   6195   6515     39   1040   -794       C  
ATOM   4364  CG  LYS A 529      14.188 -45.857 -53.472  1.00 53.97           C  
ANISOU 4364  CG  LYS A 529     7180   6453   6875     67   1095   -814       C  
ATOM   4365  CD  LYS A 529      15.431 -45.253 -52.820  1.00 55.44           C  
ANISOU 4365  CD  LYS A 529     7329   6631   7104    118   1047   -741       C  
ATOM   4366  CE  LYS A 529      16.700 -45.631 -53.566  1.00 57.66           C  
ANISOU 4366  CE  LYS A 529     7550   6884   7472    136   1112   -775       C  
ATOM   4367  NZ  LYS A 529      17.826 -44.697 -53.269  1.00 57.94           N  
ANISOU 4367  NZ  LYS A 529     7526   6930   7560    168   1064   -726       N  
ATOM   4368  N   ILE A 530       9.899 -44.262 -52.613  1.00 49.80           N  
ANISOU 4368  N   ILE A 530     6707   5993   6222    -45    983   -835       N  
ATOM   4369  CA  ILE A 530       8.737 -43.928 -51.786  1.00 50.32           C  
ANISOU 4369  CA  ILE A 530     6778   6030   6310    -64    980   -821       C  
ATOM   4370  C   ILE A 530       7.538 -44.833 -52.101  1.00 52.17           C  
ANISOU 4370  C   ILE A 530     6987   6204   6630   -106   1028   -909       C  
ATOM   4371  O   ILE A 530       6.837 -45.283 -51.190  1.00 51.88           O  
ANISOU 4371  O   ILE A 530     6964   6086   6664   -113   1095   -901       O  
ATOM   4372  CB  ILE A 530       8.362 -42.427 -51.923  1.00 49.59           C  
ANISOU 4372  CB  ILE A 530     6671   6018   6153    -79    897   -801       C  
ATOM   4373  CG1 ILE A 530       9.364 -41.560 -51.159  1.00 48.42           C  
ANISOU 4373  CG1 ILE A 530     6550   5900   5947    -39    862   -705       C  
ATOM   4374  CG2 ILE A 530       6.947 -42.145 -51.406  1.00 49.19           C  
ANISOU 4374  CG2 ILE A 530     6602   5931   6157   -111    905   -822       C  
ATOM   4375  CD1 ILE A 530       9.275 -40.087 -51.489  1.00 44.71           C  
ANISOU 4375  CD1 ILE A 530     6066   5515   5408    -51    784   -686       C  
ATOM   4376  N   LYS A 531       7.331 -45.110 -53.388  1.00 54.22           N  
ANISOU 4376  N   LYS A 531     7221   6493   6888   -133    998   -997       N  
ATOM   4377  CA  LYS A 531       6.268 -46.009 -53.853  1.00 57.01           C  
ANISOU 4377  CA  LYS A 531     7541   6785   7336   -173   1021  -1097       C  
ATOM   4378  C   LYS A 531       6.394 -47.458 -53.352  1.00 57.10           C  
ANISOU 4378  C   LYS A 531     7565   6696   7435   -165   1134  -1108       C  
ATOM   4379  O   LYS A 531       5.439 -48.234 -53.451  1.00 57.77           O  
ANISOU 4379  O   LYS A 531     7615   6708   7626   -200   1173  -1184       O  
ATOM   4380  CB  LYS A 531       6.188 -45.997 -55.384  1.00 58.47           C  
ANISOU 4380  CB  LYS A 531     7730   7015   7470   -196    945  -1187       C  
ATOM   4381  CG  LYS A 531       5.635 -44.704 -55.967  1.00 61.89           C  
ANISOU 4381  CG  LYS A 531     8159   7518   7839   -212    821  -1201       C  
ATOM   4382  CD  LYS A 531       5.231 -44.886 -57.421  1.00 65.59           C  
ANISOU 4382  CD  LYS A 531     8658   7995   8269   -238    733  -1307       C  
ATOM   4383  CE  LYS A 531       4.452 -43.681 -57.928  1.00 69.27           C  
ANISOU 4383  CE  LYS A 531     9123   8503   8693   -250    587  -1327       C  
ATOM   4384  NZ  LYS A 531       3.917 -43.897 -59.308  1.00 73.75           N  
ANISOU 4384  NZ  LYS A 531     9743   9058   9222   -272    471  -1438       N  
ATOM   4385  N   LYS A 532       7.560 -47.814 -52.815  1.00 55.45           N  
ANISOU 4385  N   LYS A 532     7400   6473   7197   -119   1179  -1035       N  
ATOM   4386  CA  LYS A 532       7.805 -49.170 -52.324  1.00 54.91           C  
ANISOU 4386  CA  LYS A 532     7357   6303   7202   -102   1276  -1035       C  
ATOM   4387  C   LYS A 532       7.895 -49.240 -50.796  1.00 53.87           C  
ANISOU 4387  C   LYS A 532     7291   6095   7081    -68   1327   -939       C  
ATOM   4388  O   LYS A 532       8.227 -50.285 -50.233  1.00 53.85           O  
ANISOU 4388  O   LYS A 532     7337   5999   7123    -42   1399   -917       O  
ATOM   4389  CB  LYS A 532       9.067 -49.761 -52.977  1.00 56.23           C  
ANISOU 4389  CB  LYS A 532     7532   6482   7351    -70   1287  -1041       C  
ATOM   4390  CG  LYS A 532       8.929 -50.022 -54.480  1.00 59.35           C  
ANISOU 4390  CG  LYS A 532     7904   6914   7731   -107   1272  -1148       C  
ATOM   4391  CD  LYS A 532      10.216 -50.578 -55.093  1.00 63.75           C  
ANISOU 4391  CD  LYS A 532     8473   7469   8279    -77   1315  -1156       C  
ATOM   4392  CE  LYS A 532      10.050 -50.835 -56.594  1.00 65.24           C  
ANISOU 4392  CE  LYS A 532     8678   7682   8429   -116   1314  -1266       C  
ATOM   4393  NZ  LYS A 532      11.276 -51.384 -57.242  1.00 64.72           N  
ANISOU 4393  NZ  LYS A 532     8628   7600   8362    -93   1387  -1284       N  
ATOM   4394  N   LEU A 533       7.577 -48.132 -50.127  1.00 53.01           N  
ANISOU 4394  N   LEU A 533     7200   6017   6924    -68   1290   -883       N  
ATOM   4395  CA  LEU A 533       7.725 -48.036 -48.671  1.00 51.92           C  
ANISOU 4395  CA  LEU A 533     7160   5806   6761    -33   1327   -788       C  
ATOM   4396  C   LEU A 533       6.464 -48.369 -47.873  1.00 51.41           C  
ANISOU 4396  C   LEU A 533     7133   5633   6766    -69   1442   -801       C  
ATOM   4397  O   LEU A 533       5.340 -48.232 -48.361  1.00 51.62           O  
ANISOU 4397  O   LEU A 533     7078   5663   6872   -125   1466   -881       O  
ATOM   4398  CB  LEU A 533       8.241 -46.649 -48.265  1.00 50.87           C  
ANISOU 4398  CB  LEU A 533     7048   5751   6529     -8   1232   -713       C  
ATOM   4399  CG  LEU A 533       9.697 -46.299 -48.582  1.00 50.59           C  
ANISOU 4399  CG  LEU A 533     7000   5782   6440     41   1140   -671       C  
ATOM   4400  CD1 LEU A 533       9.929 -44.825 -48.313  1.00 50.05           C  
ANISOU 4400  CD1 LEU A 533     6933   5793   6292     49   1052   -617       C  
ATOM   4401  CD2 LEU A 533      10.678 -47.158 -47.786  1.00 48.28           C  
ANISOU 4401  CD2 LEU A 533     6783   5399   6163    103   1146   -612       C  
ATOM   4402  N   SER A 534       6.684 -48.799 -46.633  1.00 51.44           N  
ANISOU 4402  N   SER A 534     7269   5530   6747    -35   1512   -725       N  
ATOM   4403  CA  SER A 534       5.622 -49.135 -45.698  1.00 51.99           C  
ANISOU 4403  CA  SER A 534     7414   5469   6871    -66   1657   -723       C  
ATOM   4404  C   SER A 534       4.954 -47.884 -45.146  1.00 52.84           C  
ANISOU 4404  C   SER A 534     7536   5598   6945    -87   1659   -698       C  
ATOM   4405  O   SER A 534       5.529 -46.792 -45.191  1.00 51.21           O  
ANISOU 4405  O   SER A 534     7323   5493   6643    -62   1539   -653       O  
ATOM   4406  CB  SER A 534       6.189 -49.957 -44.541  1.00 53.16           C  
ANISOU 4406  CB  SER A 534     7744   5484   6970    -14   1724   -639       C  
ATOM   4407  OG  SER A 534       7.112 -49.194 -43.783  1.00 53.08           O  
ANISOU 4407  OG  SER A 534     7844   5498   6825     46   1620   -538       O  
ATOM   4408  N   ALA A 535       3.746 -48.058 -44.614  1.00 53.17           N  
ANISOU 4408  N   ALA A 535     7592   5530   7081   -135   1809   -731       N  
ATOM   4409  CA  ALA A 535       3.000 -46.970 -43.994  1.00 52.59           C  
ANISOU 4409  CA  ALA A 535     7537   5445   7002   -159   1849   -715       C  
ATOM   4410  C   ALA A 535       3.784 -46.308 -42.863  1.00 51.90           C  
ANISOU 4410  C   ALA A 535     7633   5345   6742   -104   1815   -596       C  
ATOM   4411  O   ALA A 535       3.724 -45.091 -42.699  1.00 52.27           O  
ANISOU 4411  O   ALA A 535     7671   5459   6732   -105   1752   -571       O  
ATOM   4412  CB  ALA A 535       1.650 -47.468 -43.493  1.00 53.80           C  
ANISOU 4412  CB  ALA A 535     7688   5443   7309   -218   2057   -771       C  
ATOM   4413  N   LYS A 536       4.524 -47.113 -42.102  1.00 52.14           N  
ANISOU 4413  N   LYS A 536     7835   5283   6693    -55   1843   -526       N  
ATOM   4414  CA  LYS A 536       5.306 -46.623 -40.965  1.00 52.12           C  
ANISOU 4414  CA  LYS A 536     8036   5242   6524      4   1788   -415       C  
ATOM   4415  C   LYS A 536       6.413 -45.661 -41.401  1.00 49.66           C  
ANISOU 4415  C   LYS A 536     7659   5084   6124     48   1572   -380       C  
ATOM   4416  O   LYS A 536       6.563 -44.581 -40.826  1.00 47.45           O  
ANISOU 4416  O   LYS A 536     7447   4831   5749     63   1513   -330       O  
ATOM   4417  CB  LYS A 536       5.895 -47.792 -40.170  1.00 53.95           C  
ANISOU 4417  CB  LYS A 536     8466   5332   6700     56   1833   -354       C  
ATOM   4418  CG  LYS A 536       6.583 -47.376 -38.873  1.00 59.49           C  
ANISOU 4418  CG  LYS A 536     9422   5957   7225    120   1773   -244       C  
ATOM   4419  CD  LYS A 536       7.170 -48.569 -38.128  1.00 61.97           C  
ANISOU 4419  CD  LYS A 536     9947   6117   7483    179   1793   -183       C  
ATOM   4420  CE  LYS A 536       7.986 -48.107 -36.928  1.00 64.62           C  
ANISOU 4420  CE  LYS A 536    10540   6380   7632    254   1672    -77       C  
ATOM   4421  NZ  LYS A 536       8.357 -49.241 -36.030  1.00 69.05           N  
ANISOU 4421  NZ  LYS A 536    11362   6754   8121    311   1706    -12       N  
ATOM   4422  N   SER A 537       7.181 -46.065 -42.414  1.00 48.15           N  
ANISOU 4422  N   SER A 537     7339   4982   5972     67   1469   -411       N  
ATOM   4423  CA  SER A 537       8.258 -45.238 -42.952  1.00 44.59           C  
ANISOU 4423  CA  SER A 537     6808   4665   5469    102   1290   -389       C  
ATOM   4424  C   SER A 537       7.724 -43.997 -43.666  1.00 41.78           C  
ANISOU 4424  C   SER A 537     6317   4437   5122     56   1248   -430       C  
ATOM   4425  O   SER A 537       8.299 -42.914 -43.544  1.00 39.14           O  
ANISOU 4425  O   SER A 537     5983   4175   4713     78   1138   -387       O  
ATOM   4426  CB  SER A 537       9.150 -46.054 -43.884  1.00 45.46           C  
ANISOU 4426  CB  SER A 537     6820   4816   5635    126   1232   -420       C  
ATOM   4427  OG  SER A 537       9.900 -47.004 -43.148  1.00 50.39           O  
ANISOU 4427  OG  SER A 537     7572   5329   6245    186   1225   -367       O  
ATOM   4428  N   LEU A 538       6.625 -44.161 -44.399  1.00 39.85           N  
ANISOU 4428  N   LEU A 538     5958   4206   4976     -5   1325   -515       N  
ATOM   4429  CA  LEU A 538       5.995 -43.046 -45.109  1.00 39.49           C  
ANISOU 4429  CA  LEU A 538     5791   4263   4952    -45   1275   -560       C  
ATOM   4430  C   LEU A 538       5.475 -41.998 -44.142  1.00 40.35           C  
ANISOU 4430  C   LEU A 538     5973   4343   5014    -52   1304   -515       C  
ATOM   4431  O   LEU A 538       5.634 -40.801 -44.380  1.00 40.56           O  
ANISOU 4431  O   LEU A 538     5954   4465   4992    -51   1208   -500       O  
ATOM   4432  CB  LEU A 538       4.864 -43.532 -46.015  1.00 38.21           C  
ANISOU 4432  CB  LEU A 538     5499   4092   4925   -104   1333   -668       C  
ATOM   4433  CG  LEU A 538       5.281 -44.337 -47.253  1.00 40.82           C  
ANISOU 4433  CG  LEU A 538     5744   4474   5293   -106   1285   -732       C  
ATOM   4434  CD1 LEU A 538       4.067 -44.961 -47.925  1.00 41.58           C  
ANISOU 4434  CD1 LEU A 538     5741   4526   5533   -162   1343   -842       C  
ATOM   4435  CD2 LEU A 538       6.085 -43.489 -48.245  1.00 36.83           C  
ANISOU 4435  CD2 LEU A 538     5178   4109   4708    -91   1142   -729       C  
ATOM   4436  N   ASN A 539       4.870 -42.455 -43.048  1.00 40.57           N  
ANISOU 4436  N   ASN A 539     6128   4231   5055    -60   1448   -494       N  
ATOM   4437  CA  ASN A 539       4.365 -41.557 -42.017  1.00 43.10           C  
ANISOU 4437  CA  ASN A 539     6552   4498   5326    -68   1509   -452       C  
ATOM   4438  C   ASN A 539       5.460 -40.739 -41.356  1.00 41.96           C  
ANISOU 4438  C   ASN A 539     6529   4392   5021    -12   1383   -360       C  
ATOM   4439  O   ASN A 539       5.294 -39.536 -41.151  1.00 41.48           O  
ANISOU 4439  O   ASN A 539     6464   4379   4917    -19   1343   -343       O  
ATOM   4440  CB  ASN A 539       3.556 -42.316 -40.965  1.00 44.63           C  
ANISOU 4440  CB  ASN A 539     6891   4509   5557    -88   1719   -448       C  
ATOM   4441  CG  ASN A 539       2.125 -42.550 -41.395  1.00 45.63           C  
ANISOU 4441  CG  ASN A 539     6876   4584   5878   -159   1861   -548       C  
ATOM   4442  OD1 ASN A 539       1.591 -43.649 -41.239  1.00 50.72           O  
ANISOU 4442  OD1 ASN A 539     7541   5110   6622   -184   2010   -585       O  
ATOM   4443  ND2 ASN A 539       1.496 -41.518 -41.947  1.00 40.54           N  
ANISOU 4443  ND2 ASN A 539     6081   4018   5304   -191   1810   -596       N  
ATOM   4444  N   GLU A 540       6.577 -41.393 -41.045  1.00 41.26           N  
ANISOU 4444  N   GLU A 540     6539   4277   4859     45   1312   -306       N  
ATOM   4445  CA  GLU A 540       7.733 -40.702 -40.490  1.00 41.56           C  
ANISOU 4445  CA  GLU A 540     6673   4345   4774    103   1160   -229       C  
ATOM   4446  C   GLU A 540       8.294 -39.675 -41.487  1.00 39.14           C  
ANISOU 4446  C   GLU A 540     6192   4203   4476    101   1014   -247       C  
ATOM   4447  O   GLU A 540       8.680 -38.569 -41.095  1.00 37.36           O  
ANISOU 4447  O   GLU A 540     6002   4017   4176    117    925   -205       O  
ATOM   4448  CB  GLU A 540       8.805 -41.703 -40.039  1.00 42.61           C  
ANISOU 4448  CB  GLU A 540     6923   4402   4866    169   1097   -181       C  
ATOM   4449  CG  GLU A 540      10.063 -41.079 -39.405  1.00 50.47           C  
ANISOU 4449  CG  GLU A 540     8013   5403   5759    237    913   -108       C  
ATOM   4450  CD  GLU A 540       9.768 -40.091 -38.270  1.00 56.91           C  
ANISOU 4450  CD  GLU A 540     9006   6164   6451    241    911    -57       C  
ATOM   4451  OE1 GLU A 540       8.776 -40.283 -37.530  1.00 60.74           O  
ANISOU 4451  OE1 GLU A 540     9639   6540   6900    213   1074    -52       O  
ATOM   4452  OE2 GLU A 540      10.541 -39.119 -38.113  1.00 58.17           O  
ANISOU 4452  OE2 GLU A 540     9163   6383   6558    271    754    -26       O  
ATOM   4453  N   MET A 541       8.317 -40.040 -42.769  1.00 35.65           N  
ANISOU 4453  N   MET A 541     5579   3846   4121     79   1000   -310       N  
ATOM   4454  CA  MET A 541       8.755 -39.127 -43.824  1.00 34.01           C  
ANISOU 4454  CA  MET A 541     5225   3779   3918     70    891   -332       C  
ATOM   4455  C   MET A 541       7.811 -37.931 -43.961  1.00 33.19           C  
ANISOU 4455  C   MET A 541     5071   3727   3812     27    901   -351       C  
ATOM   4456  O   MET A 541       8.257 -36.801 -44.173  1.00 31.51           O  
ANISOU 4456  O   MET A 541     4822   3598   3553     33    805   -328       O  
ATOM   4457  CB  MET A 541       8.894 -39.856 -45.163  1.00 34.15           C  
ANISOU 4457  CB  MET A 541     5111   3853   4011     53    892   -400       C  
ATOM   4458  CG  MET A 541      10.062 -40.836 -45.227  1.00 31.70           C  
ANISOU 4458  CG  MET A 541     4816   3512   3716     99    861   -383       C  
ATOM   4459  SD  MET A 541      10.391 -41.464 -46.887  1.00 33.40           S  
ANISOU 4459  SD  MET A 541     4887   3801   4001     79    863   -464       S  
ATOM   4460  CE  MET A 541      10.888 -39.964 -47.753  1.00 31.23           C  
ANISOU 4460  CE  MET A 541     4527   3660   3678     67    766   -464       C  
ATOM   4461  N   LEU A 542       6.511 -38.191 -43.831  1.00 31.89           N  
ANISOU 4461  N   LEU A 542     4898   3502   3717    -16   1021   -396       N  
ATOM   4462  CA  LEU A 542       5.509 -37.143 -43.923  1.00 30.95           C  
ANISOU 4462  CA  LEU A 542     4719   3409   3632    -55   1038   -424       C  
ATOM   4463  C   LEU A 542       5.676 -36.169 -42.765  1.00 31.13           C  
ANISOU 4463  C   LEU A 542     4867   3401   3560    -36   1032   -354       C  
ATOM   4464  O   LEU A 542       5.611 -34.957 -42.968  1.00 29.12           O  
ANISOU 4464  O   LEU A 542     4563   3219   3282    -43    964   -347       O  
ATOM   4465  CB  LEU A 542       4.088 -37.725 -43.968  1.00 30.03           C  
ANISOU 4465  CB  LEU A 542     4551   3208   3653   -104   1176   -497       C  
ATOM   4466  CG  LEU A 542       2.895 -36.759 -44.007  1.00 32.22           C  
ANISOU 4466  CG  LEU A 542     4747   3480   4015   -144   1208   -539       C  
ATOM   4467  CD1 LEU A 542       3.016 -35.703 -45.126  1.00 28.43           C  
ANISOU 4467  CD1 LEU A 542     4142   3137   3522   -147   1050   -560       C  
ATOM   4468  CD2 LEU A 542       1.570 -37.525 -44.112  1.00 33.23           C  
ANISOU 4468  CD2 LEU A 542     4796   3504   4325   -192   1344   -627       C  
ATOM   4469  N   PHE A 543       5.896 -36.711 -41.563  1.00 32.65           N  
ANISOU 4469  N   PHE A 543     5238   3478   3690    -10   1101   -302       N  
ATOM   4470  CA  PHE A 543       6.184 -35.911 -40.378  1.00 32.96           C  
ANISOU 4470  CA  PHE A 543     5443   3469   3612     16   1084   -234       C  
ATOM   4471  C   PHE A 543       7.394 -35.011 -40.607  1.00 33.26           C  
ANISOU 4471  C   PHE A 543     5451   3612   3572     53    898   -191       C  
ATOM   4472  O   PHE A 543       7.361 -33.823 -40.275  1.00 33.94           O  
ANISOU 4472  O   PHE A 543     5559   3729   3607     51    854   -168       O  
ATOM   4473  CB  PHE A 543       6.391 -36.805 -39.141  1.00 36.26           C  
ANISOU 4473  CB  PHE A 543     6092   3734   3952     48   1163   -183       C  
ATOM   4474  CG  PHE A 543       6.716 -36.035 -37.878  1.00 37.48           C  
ANISOU 4474  CG  PHE A 543     6458   3820   3961     78   1133   -114       C  
ATOM   4475  CD1 PHE A 543       5.713 -35.375 -37.169  1.00 39.61           C  
ANISOU 4475  CD1 PHE A 543     6817   4017   4216     42   1271   -119       C  
ATOM   4476  CD2 PHE A 543       8.027 -35.963 -37.405  1.00 39.27           C  
ANISOU 4476  CD2 PHE A 543     6796   4046   4079    143    962    -51       C  
ATOM   4477  CE1 PHE A 543       6.010 -34.648 -36.004  1.00 41.06           C  
ANISOU 4477  CE1 PHE A 543     7220   4131   4251     69   1245    -59       C  
ATOM   4478  CE2 PHE A 543       8.338 -35.244 -36.242  1.00 37.99           C  
ANISOU 4478  CE2 PHE A 543     6844   3813   3776    173    910      6       C  
ATOM   4479  CZ  PHE A 543       7.325 -34.587 -35.541  1.00 39.48           C  
ANISOU 4479  CZ  PHE A 543     7145   3933   3924    136   1055      4       C  
ATOM   4480  N   ARG A 544       8.449 -35.576 -41.192  1.00 33.09           N  
ANISOU 4480  N   ARG A 544     5373   3640   3560     86    799   -186       N  
ATOM   4481  CA  ARG A 544       9.680 -34.829 -41.471  1.00 32.90           C  
ANISOU 4481  CA  ARG A 544     5300   3701   3500    119    636   -156       C  
ATOM   4482  C   ARG A 544       9.503 -33.763 -42.556  1.00 32.71           C  
ANISOU 4482  C   ARG A 544     5113   3805   3508     84    594   -189       C  
ATOM   4483  O   ARG A 544       9.997 -32.638 -42.414  1.00 32.85           O  
ANISOU 4483  O   ARG A 544     5128   3872   3483     94    505   -159       O  
ATOM   4484  CB  ARG A 544      10.830 -35.782 -41.810  1.00 32.70           C  
ANISOU 4484  CB  ARG A 544     5246   3671   3509    162    566   -151       C  
ATOM   4485  CG  ARG A 544      11.355 -36.564 -40.606  1.00 34.23           C  
ANISOU 4485  CG  ARG A 544     5624   3733   3648    217    541    -99       C  
ATOM   4486  CD  ARG A 544      12.241 -37.728 -41.044  1.00 36.65           C  
ANISOU 4486  CD  ARG A 544     5881   4019   4025    254    502   -108       C  
ATOM   4487  NE  ARG A 544      12.558 -38.617 -39.929  1.00 38.24           N  
ANISOU 4487  NE  ARG A 544     6273   4077   4178    308    485    -61       N  
ATOM   4488  CZ  ARG A 544      13.445 -39.610 -39.970  1.00 41.74           C  
ANISOU 4488  CZ  ARG A 544     6716   4467   4674    358    423    -54       C  
ATOM   4489  NH1 ARG A 544      14.137 -39.869 -41.074  1.00 40.49           N  
ANISOU 4489  NH1 ARG A 544     6368   4386   4628    359    390    -95       N  
ATOM   4490  NH2 ARG A 544      13.642 -40.349 -38.892  1.00 42.59           N  
ANISOU 4490  NH2 ARG A 544     7028   4433   4723    410    399     -6       N  
ATOM   4491  N   ALA A 545       8.794 -34.119 -43.627  1.00 31.21           N  
ANISOU 4491  N   ALA A 545     4803   3661   3393     45    651   -252       N  
ATOM   4492  CA  ALA A 545       8.428 -33.168 -44.676  1.00 29.47           C  
ANISOU 4492  CA  ALA A 545     4460   3544   3195     13    612   -286       C  
ATOM   4493  C   ALA A 545       7.690 -31.982 -44.070  1.00 28.74           C  
ANISOU 4493  C   ALA A 545     4399   3445   3077     -4    621   -269       C  
ATOM   4494  O   ALA A 545       8.005 -30.829 -44.367  1.00 26.53           O  
ANISOU 4494  O   ALA A 545     4079   3237   2764     -5    543   -251       O  
ATOM   4495  CB  ALA A 545       7.557 -33.844 -45.736  1.00 27.85           C  
ANISOU 4495  CB  ALA A 545     4157   3354   3071    -24    664   -363       C  
ATOM   4496  N   GLN A 546       6.715 -32.284 -43.216  1.00 29.24           N  
ANISOU 4496  N   GLN A 546     4535   3411   3163    -20    734   -276       N  
ATOM   4497  CA  GLN A 546       5.887 -31.265 -42.572  1.00 30.49           C  
ANISOU 4497  CA  GLN A 546     4727   3539   3318    -39    778   -269       C  
ATOM   4498  C   GLN A 546       6.662 -30.407 -41.576  1.00 28.96           C  
ANISOU 4498  C   GLN A 546     4661   3334   3010     -8    716   -199       C  
ATOM   4499  O   GLN A 546       6.377 -29.215 -41.445  1.00 30.38           O  
ANISOU 4499  O   GLN A 546     4829   3541   3173    -20    694   -191       O  
ATOM   4500  CB  GLN A 546       4.655 -31.897 -41.912  1.00 31.60           C  
ANISOU 4500  CB  GLN A 546     4917   3556   3535    -68    949   -303       C  
ATOM   4501  CG  GLN A 546       3.636 -32.444 -42.927  1.00 34.85           C  
ANISOU 4501  CG  GLN A 546     5171   3974   4098   -107    995   -390       C  
ATOM   4502  CD  GLN A 546       2.487 -33.228 -42.292  1.00 40.00           C  
ANISOU 4502  CD  GLN A 546     5853   4485   4861   -139   1182   -433       C  
ATOM   4503  OE1 GLN A 546       1.420 -33.362 -42.891  1.00 41.56           O  
ANISOU 4503  OE1 GLN A 546     5914   4663   5214   -176   1225   -511       O  
ATOM   4504  NE2 GLN A 546       2.703 -33.752 -41.084  1.00 38.06           N  
ANISOU 4504  NE2 GLN A 546     5791   4129   4543   -124   1290   -385       N  
ATOM   4505  N   ARG A 547       7.636 -31.002 -40.883  1.00 27.02           N  
ANISOU 4505  N   ARG A 547     4537   3038   2690     34    676   -153       N  
ATOM   4506  CA  ARG A 547       8.531 -30.224 -40.020  1.00 25.95           C  
ANISOU 4506  CA  ARG A 547     4519   2890   2452     70    573    -94       C  
ATOM   4507  C   ARG A 547       9.429 -29.294 -40.841  1.00 25.90           C  
ANISOU 4507  C   ARG A 547     4382   3003   2454     77    432    -88       C  
ATOM   4508  O   ARG A 547       9.620 -28.132 -40.482  1.00 26.04           O  
ANISOU 4508  O   ARG A 547     4426   3042   2427     79    372    -63       O  
ATOM   4509  CB  ARG A 547       9.360 -31.126 -39.096  1.00 25.61           C  
ANISOU 4509  CB  ARG A 547     4642   2748   2340    121    534    -50       C  
ATOM   4510  CG  ARG A 547       8.597 -31.636 -37.872  1.00 27.00           C  
ANISOU 4510  CG  ARG A 547     5033   2774   2451    120    669    -33       C  
ATOM   4511  CD  ARG A 547       8.157 -30.473 -36.984  1.00 30.12           C  
ANISOU 4511  CD  ARG A 547     5552   3128   2764    109    696    -11       C  
ATOM   4512  NE  ARG A 547       7.348 -30.886 -35.842  1.00 33.43           N  
ANISOU 4512  NE  ARG A 547     6194   3390   3118    100    863      1       N  
ATOM   4513  CZ  ARG A 547       7.850 -31.224 -34.657  1.00 37.98           C  
ANISOU 4513  CZ  ARG A 547     7036   3841   3555    144    836     53       C  
ATOM   4514  NH1 ARG A 547       9.166 -31.218 -34.462  1.00 39.02           N  
ANISOU 4514  NH1 ARG A 547     7218   3988   3619    203    625     93       N  
ATOM   4515  NH2 ARG A 547       7.041 -31.572 -33.666  1.00 35.96           N  
ANISOU 4515  NH2 ARG A 547     7001   3429   3231    130   1020     62       N  
ATOM   4516  N   THR A 548       9.953 -29.801 -41.953  1.00 25.64           N  
ANISOU 4516  N   THR A 548     4219   3041   2483     78    396   -114       N  
ATOM   4517  CA  THR A 548      10.718 -28.975 -42.890  1.00 27.77           C  
ANISOU 4517  CA  THR A 548     4365   3413   2771     75    303   -116       C  
ATOM   4518  C   THR A 548       9.874 -27.816 -43.435  1.00 26.64           C  
ANISOU 4518  C   THR A 548     4154   3335   2632     36    319   -134       C  
ATOM   4519  O   THR A 548      10.342 -26.676 -43.476  1.00 26.82           O  
ANISOU 4519  O   THR A 548     4157   3403   2630     37    248   -110       O  
ATOM   4520  CB  THR A 548      11.315 -29.807 -44.053  1.00 28.45           C  
ANISOU 4520  CB  THR A 548     4342   3547   2920     76    300   -149       C  
ATOM   4521  OG1 THR A 548      12.146 -30.843 -43.519  1.00 29.82           O  
ANISOU 4521  OG1 THR A 548     4570   3653   3107    118    275   -132       O  
ATOM   4522  CG2 THR A 548      12.160 -28.928 -44.966  1.00 27.22           C  
ANISOU 4522  CG2 THR A 548     4085   3476   2780     71    233   -149       C  
ATOM   4523  N   GLU A 549       8.629 -28.105 -43.818  1.00 26.75           N  
ANISOU 4523  N   GLU A 549     4131   3342   2690      4    405   -177       N  
ATOM   4524  CA  GLU A 549       7.707 -27.063 -44.285  1.00 26.58           C  
ANISOU 4524  CA  GLU A 549     4046   3362   2693    -27    408   -199       C  
ATOM   4525  C   GLU A 549       7.476 -25.959 -43.250  1.00 26.15           C  
ANISOU 4525  C   GLU A 549     4067   3272   2595    -26    409   -163       C  
ATOM   4526  O   GLU A 549       7.477 -24.784 -43.602  1.00 25.71           O  
ANISOU 4526  O   GLU A 549     3967   3272   2530    -34    354   -155       O  
ATOM   4527  CB  GLU A 549       6.369 -27.662 -44.731  1.00 27.81           C  
ANISOU 4527  CB  GLU A 549     4141   3487   2938    -57    489   -262       C  
ATOM   4528  CG  GLU A 549       5.364 -26.614 -45.229  1.00 31.21           C  
ANISOU 4528  CG  GLU A 549     4494   3944   3419    -82    470   -291       C  
ATOM   4529  CD  GLU A 549       4.038 -27.209 -45.667  1.00 36.90           C  
ANISOU 4529  CD  GLU A 549     5135   4619   4264   -109    528   -365       C  
ATOM   4530  OE1 GLU A 549       3.960 -28.449 -45.861  1.00 40.35           O  
ANISOU 4530  OE1 GLU A 549     5565   5025   4742   -113    575   -399       O  
ATOM   4531  OE2 GLU A 549       3.074 -26.428 -45.825  1.00 37.05           O  
ANISOU 4531  OE2 GLU A 549     5092   4627   4358   -125    520   -395       O  
ATOM   4532  N   VAL A 550       7.280 -26.346 -41.986  1.00 25.77           N  
ANISOU 4532  N   VAL A 550     4153   3125   2513    -15    477   -143       N  
ATOM   4533  CA  VAL A 550       7.064 -25.391 -40.887  1.00 26.71           C  
ANISOU 4533  CA  VAL A 550     4384   3192   2575    -13    494   -112       C  
ATOM   4534  C   VAL A 550       8.282 -24.486 -40.659  1.00 27.36           C  
ANISOU 4534  C   VAL A 550     4496   3317   2582     13    359    -66       C  
ATOM   4535  O   VAL A 550       8.135 -23.273 -40.477  1.00 28.62           O  
ANISOU 4535  O   VAL A 550     4657   3495   2722      4    332    -54       O  
ATOM   4536  CB  VAL A 550       6.680 -26.109 -39.558  1.00 26.04           C  
ANISOU 4536  CB  VAL A 550     4481   2968   2444     -5    608    -99       C  
ATOM   4537  CG1 VAL A 550       6.775 -25.142 -38.361  1.00 26.51           C  
ANISOU 4537  CG1 VAL A 550     4702   2965   2405      5    604    -60       C  
ATOM   4538  CG2 VAL A 550       5.274 -26.712 -39.651  1.00 24.70           C  
ANISOU 4538  CG2 VAL A 550     4271   2733   2379    -42    775   -152       C  
ATOM   4539  N   ALA A 551       9.473 -25.087 -40.650  1.00 27.06           N  
ANISOU 4539  N   ALA A 551     4476   3284   2521     46    273    -45       N  
ATOM   4540  CA  ALA A 551      10.731 -24.342 -40.535  1.00 28.03           C  
ANISOU 4540  CA  ALA A 551     4594   3439   2616     71    135    -13       C  
ATOM   4541  C   ALA A 551      10.840 -23.306 -41.658  1.00 28.93           C  
ANISOU 4541  C   ALA A 551     4560   3659   2775     46     99    -24       C  
ATOM   4542  O   ALA A 551      11.192 -22.139 -41.418  1.00 26.99           O  
ANISOU 4542  O   ALA A 551     4319   3430   2506     45     36     -4       O  
ATOM   4543  CB  ALA A 551      11.923 -25.300 -40.575  1.00 27.50           C  
ANISOU 4543  CB  ALA A 551     4523   3355   2570    109     58     -4       C  
ATOM   4544  N   GLY A 552      10.529 -23.742 -42.880  1.00 26.73           N  
ANISOU 4544  N   GLY A 552     4165   3440   2550     26    139    -58       N  
ATOM   4545  CA  GLY A 552      10.518 -22.850 -44.038  1.00 26.90           C  
ANISOU 4545  CA  GLY A 552     4078   3548   2594      2    115    -69       C  
ATOM   4546  C   GLY A 552       9.498 -21.740 -43.862  1.00 26.79           C  
ANISOU 4546  C   GLY A 552     4071   3537   2570    -19    134    -69       C  
ATOM   4547  O   GLY A 552       9.775 -20.562 -44.158  1.00 25.95           O  
ANISOU 4547  O   GLY A 552     3935   3473   2454    -27     84    -51       O  
ATOM   4548  N   MET A 553       8.321 -22.118 -43.364  1.00 23.95           N  
ANISOU 4548  N   MET A 553     3749   3122   2229    -30    217    -90       N  
ATOM   4549  CA  MET A 553       7.255 -21.165 -43.086  1.00 23.98           C  
ANISOU 4549  CA  MET A 553     3753   3105   2254    -49    254    -99       C  
ATOM   4550  C   MET A 553       7.710 -20.084 -42.112  1.00 23.15           C  
ANISOU 4550  C   MET A 553     3734   2976   2086    -39    218    -58       C  
ATOM   4551  O   MET A 553       7.465 -18.907 -42.351  1.00 24.80           O  
ANISOU 4551  O   MET A 553     3905   3215   2303    -51    190    -53       O  
ATOM   4552  CB  MET A 553       5.998 -21.869 -42.557  1.00 26.64           C  
ANISOU 4552  CB  MET A 553     4117   3358   2649    -63    376   -136       C  
ATOM   4553  CG  MET A 553       4.848 -20.915 -42.181  1.00 34.28           C  
ANISOU 4553  CG  MET A 553     5074   4281   3671    -82    436   -153       C  
ATOM   4554  SD  MET A 553       4.186 -20.008 -43.600  1.00 42.80           S  
ANISOU 4554  SD  MET A 553     5992   5436   4834    -96    357   -185       S  
ATOM   4555  CE  MET A 553       2.873 -21.094 -44.152  1.00 43.95           C  
ANISOU 4555  CE  MET A 553     6041   5532   5127   -115    425   -264       C  
ATOM   4556  N   THR A 554       8.370 -20.476 -41.026  1.00 21.70           N  
ANISOU 4556  N   THR A 554     3676   2731   1838    -16    208    -32       N  
ATOM   4557  CA  THR A 554       8.827 -19.497 -40.036  1.00 21.98           C  
ANISOU 4557  CA  THR A 554     3815   2730   1805     -5    156      1       C  
ATOM   4558  C   THR A 554       9.802 -18.510 -40.669  1.00 23.00           C  
ANISOU 4558  C   THR A 554     3857   2938   1943     -4     41     18       C  
ATOM   4559  O   THR A 554       9.637 -17.291 -40.537  1.00 22.19           O  
ANISOU 4559  O   THR A 554     3754   2846   1832    -16     22     27       O  
ATOM   4560  CB  THR A 554       9.484 -20.161 -38.811  1.00 21.95           C  
ANISOU 4560  CB  THR A 554     3983   2636   1720     27    128     25       C  
ATOM   4561  OG1 THR A 554       8.519 -20.971 -38.127  1.00 24.73           O  
ANISOU 4561  OG1 THR A 554     4447   2896   2054     22    264     12       O  
ATOM   4562  CG2 THR A 554      10.008 -19.108 -37.849  1.00 22.83           C  
ANISOU 4562  CG2 THR A 554     4210   2707   1756     40     48     51       C  
ATOM   4563  N   ALA A 555      10.796 -19.048 -41.374  1.00 22.39           N  
ANISOU 4563  N   ALA A 555     3705   2907   1896      8    -19     20       N  
ATOM   4564  CA  ALA A 555      11.840 -18.233 -41.973  1.00 23.72           C  
ANISOU 4564  CA  ALA A 555     3791   3131   2092      6   -104     32       C  
ATOM   4565  C   ALA A 555      11.282 -17.248 -43.005  1.00 24.76           C  
ANISOU 4565  C   ALA A 555     3834   3329   2245    -23    -79     27       C  
ATOM   4566  O   ALA A 555      11.634 -16.066 -42.995  1.00 25.80           O  
ANISOU 4566  O   ALA A 555     3953   3476   2376    -31   -123     44       O  
ATOM   4567  CB  ALA A 555      12.915 -19.122 -42.595  1.00 23.44           C  
ANISOU 4567  CB  ALA A 555     3683   3114   2107     21   -137     25       C  
ATOM   4568  N   GLN A 556      10.396 -17.731 -43.873  1.00 22.63           N  
ANISOU 4568  N   GLN A 556     3513   3090   1996    -38    -19      1       N  
ATOM   4569  CA  GLN A 556       9.864 -16.904 -44.951  1.00 21.89           C  
ANISOU 4569  CA  GLN A 556     3353   3049   1917    -58    -19     -5       C  
ATOM   4570  C   GLN A 556       8.804 -15.905 -44.485  1.00 23.98           C  
ANISOU 4570  C   GLN A 556     3638   3288   2185    -67     -5     -4       C  
ATOM   4571  O   GLN A 556       8.871 -14.732 -44.851  1.00 25.46           O  
ANISOU 4571  O   GLN A 556     3804   3501   2369    -75    -40     13       O  
ATOM   4572  CB  GLN A 556       9.365 -17.761 -46.134  1.00 19.75           C  
ANISOU 4572  CB  GLN A 556     3029   2810   1667    -66      8    -39       C  
ATOM   4573  CG  GLN A 556       8.009 -18.466 -45.941  1.00 19.82           C  
ANISOU 4573  CG  GLN A 556     3036   2781   1715    -70     61    -77       C  
ATOM   4574  CD  GLN A 556       6.811 -17.600 -46.327  1.00 24.06           C  
ANISOU 4574  CD  GLN A 556     3536   3316   2292    -81     50    -95       C  
ATOM   4575  OE1 GLN A 556       6.957 -16.560 -46.979  1.00 23.51           O  
ANISOU 4575  OE1 GLN A 556     3449   3283   2202    -84     -4    -77       O  
ATOM   4576  NE2 GLN A 556       5.620 -18.029 -45.923  1.00 18.26           N  
ANISOU 4576  NE2 GLN A 556     2785   2525   1627    -86    106   -133       N  
ATOM   4577  N   ILE A 557       7.839 -16.352 -43.673  1.00 25.00           N  
ANISOU 4577  N   ILE A 557     3811   3356   2331    -67     61    -24       N  
ATOM   4578  CA  ILE A 557       6.704 -15.490 -43.338  1.00 25.03           C  
ANISOU 4578  CA  ILE A 557     3814   3323   2372    -78     98    -35       C  
ATOM   4579  C   ILE A 557       7.112 -14.312 -42.462  1.00 24.96           C  
ANISOU 4579  C   ILE A 557     3874   3292   2319    -76     75     -4       C  
ATOM   4580  O   ILE A 557       6.519 -13.230 -42.538  1.00 25.33           O  
ANISOU 4580  O   ILE A 557     3896   3334   2394    -85     75     -4       O  
ATOM   4581  CB  ILE A 557       5.483 -16.258 -42.742  1.00 25.99           C  
ANISOU 4581  CB  ILE A 557     3954   3367   2554    -84    207    -75       C  
ATOM   4582  CG1 ILE A 557       4.204 -15.406 -42.894  1.00 26.78           C  
ANISOU 4582  CG1 ILE A 557     3991   3436   2749    -97    239   -104       C  
ATOM   4583  CG2 ILE A 557       5.736 -16.691 -41.284  1.00 24.23           C  
ANISOU 4583  CG2 ILE A 557     3874   3061   2269    -77    274    -60       C  
ATOM   4584  CD1 ILE A 557       2.902 -16.164 -42.668  1.00 30.66           C  
ANISOU 4584  CD1 ILE A 557     4445   3847   3357   -109    348   -160       C  
ATOM   4585  N   ASN A 558       8.139 -14.521 -41.649  1.00 22.80           N  
ANISOU 4585  N   ASN A 558     3685   2997   1982    -63     42     20       N  
ATOM   4586  CA  ASN A 558       8.598 -13.478 -40.753  1.00 22.94           C  
ANISOU 4586  CA  ASN A 558     3782   2982   1954    -60      2     43       C  
ATOM   4587  C   ASN A 558       9.568 -12.521 -41.432  1.00 22.27           C  
ANISOU 4587  C   ASN A 558     3626   2958   1876    -64    -89     65       C  
ATOM   4588  O   ASN A 558       9.699 -11.374 -41.016  1.00 22.08           O  
ANISOU 4588  O   ASN A 558     3630   2920   1840    -70   -119     78       O  
ATOM   4589  CB  ASN A 558       9.142 -14.088 -39.467  1.00 22.06           C  
ANISOU 4589  CB  ASN A 558     3818   2795   1770    -40     -9     52       C  
ATOM   4590  CG  ASN A 558       8.034 -14.641 -38.600  1.00 24.31           C  
ANISOU 4590  CG  ASN A 558     4211   2990   2035    -43    118     34       C  
ATOM   4591  OD1 ASN A 558       7.221 -13.877 -38.079  1.00 21.65           O  
ANISOU 4591  OD1 ASN A 558     3922   2604   1702    -57    189     25       O  
ATOM   4592  ND2 ASN A 558       7.966 -15.974 -38.471  1.00 20.18           N  
ANISOU 4592  ND2 ASN A 558     3725   2436   1505    -33    163     25       N  
ATOM   4593  N   ARG A 559      10.211 -12.979 -42.505  1.00 21.89           N  
ANISOU 4593  N   ARG A 559     3491   2972   1855    -65   -118     66       N  
ATOM   4594  CA  ARG A 559      10.973 -12.065 -43.361  1.00 22.35           C  
ANISOU 4594  CA  ARG A 559     3479   3078   1934    -76   -165     84       C  
ATOM   4595  C   ARG A 559      10.020 -11.206 -44.190  1.00 23.29           C  
ANISOU 4595  C   ARG A 559     3558   3226   2066    -91   -143     85       C  
ATOM   4596  O   ARG A 559      10.261 -10.008 -44.379  1.00 23.11           O  
ANISOU 4596  O   ARG A 559     3524   3211   2045   -101   -170    105       O  
ATOM   4597  CB  ARG A 559      11.999 -12.812 -44.219  1.00 22.13           C  
ANISOU 4597  CB  ARG A 559     3387   3086   1933    -75   -178     81       C  
ATOM   4598  CG  ARG A 559      13.290 -13.113 -43.446  1.00 23.16           C  
ANISOU 4598  CG  ARG A 559     3531   3180   2088    -58   -241     84       C  
ATOM   4599  CD  ARG A 559      14.148 -14.191 -44.111  1.00 26.66           C  
ANISOU 4599  CD  ARG A 559     3911   3638   2580    -50   -234     71       C  
ATOM   4600  NE  ARG A 559      15.387 -14.412 -43.362  1.00 23.43           N  
ANISOU 4600  NE  ARG A 559     3497   3179   2224    -29   -316     68       N  
ATOM   4601  CZ  ARG A 559      15.519 -15.262 -42.342  1.00 26.96           C  
ANISOU 4601  CZ  ARG A 559     4019   3571   2653      2   -368     64       C  
ATOM   4602  NH1 ARG A 559      14.490 -16.002 -41.937  1.00 22.23           N  
ANISOU 4602  NH1 ARG A 559     3506   2959   1982     11   -317     63       N  
ATOM   4603  NH2 ARG A 559      16.691 -15.376 -41.724  1.00 24.50           N  
ANISOU 4603  NH2 ARG A 559     3699   3205   2404     27   -475     58       N  
ATOM   4604  N   LYS A 560       8.919 -11.815 -44.643  1.00 21.94           N  
ANISOU 4604  N   LYS A 560     3365   3058   1912    -90   -103     61       N  
ATOM   4605  CA  LYS A 560       7.814 -11.067 -45.250  1.00 20.37           C  
ANISOU 4605  CA  LYS A 560     3133   2863   1745    -95   -104     53       C  
ATOM   4606  C   LYS A 560       7.249 -10.026 -44.265  1.00 18.72           C  
ANISOU 4606  C   LYS A 560     2958   2602   1552    -97    -87     58       C  
ATOM   4607  O   LYS A 560       7.053  -8.868 -44.625  1.00 17.04           O  
ANISOU 4607  O   LYS A 560     2727   2394   1352   -100   -117     74       O  
ATOM   4608  CB  LYS A 560       6.716 -12.024 -45.737  1.00 20.16           C  
ANISOU 4608  CB  LYS A 560     3068   2828   1764    -91    -77     12       C  
ATOM   4609  CG  LYS A 560       5.421 -11.338 -46.169  1.00 23.32           C  
ANISOU 4609  CG  LYS A 560     3423   3205   2233    -89    -95     -9       C  
ATOM   4610  CD  LYS A 560       4.330 -12.347 -46.528  1.00 22.10           C  
ANISOU 4610  CD  LYS A 560     3215   3024   2157    -86    -78    -63       C  
ATOM   4611  CE  LYS A 560       2.987 -11.641 -46.736  1.00 26.79           C  
ANISOU 4611  CE  LYS A 560     3746   3570   2863    -80   -104    -94       C  
ATOM   4612  NZ  LYS A 560       1.888 -12.559 -47.212  1.00 26.44           N  
ANISOU 4612  NZ  LYS A 560     3627   3489   2931    -77   -110   -158       N  
ATOM   4613  N   LEU A 561       7.011 -10.433 -43.020  1.00 17.27           N  
ANISOU 4613  N   LEU A 561     2841   2360   1363    -94    -33     45       N  
ATOM   4614  CA  LEU A 561       6.487  -9.508 -42.013  1.00 21.01           C  
ANISOU 4614  CA  LEU A 561     3370   2770   1842    -98      5     44       C  
ATOM   4615  C   LEU A 561       7.434  -8.323 -41.800  1.00 21.46           C  
ANISOU 4615  C   LEU A 561     3455   2841   1857   -102    -61     77       C  
ATOM   4616  O   LEU A 561       6.984  -7.176 -41.720  1.00 22.58           O  
ANISOU 4616  O   LEU A 561     3592   2964   2025   -107    -58     82       O  
ATOM   4617  CB  LEU A 561       6.183 -10.225 -40.684  1.00 20.16           C  
ANISOU 4617  CB  LEU A 561     3372   2581   1707    -95     90     27       C  
ATOM   4618  CG  LEU A 561       5.719  -9.363 -39.495  1.00 26.59           C  
ANISOU 4618  CG  LEU A 561     4286   3310   2505   -101    152     22       C  
ATOM   4619  CD1 LEU A 561       4.384  -8.660 -39.763  1.00 25.16           C  
ANISOU 4619  CD1 LEU A 561     4029   3096   2436   -110    219     -5       C  
ATOM   4620  CD2 LEU A 561       5.630 -10.206 -38.214  1.00 28.08           C  
ANISOU 4620  CD2 LEU A 561     4632   3408   2629    -97    238     11       C  
ATOM   4621  N   LEU A 562       8.734  -8.607 -41.733  1.00 19.96           N  
ANISOU 4621  N   LEU A 562     3284   2676   1625    -98   -120     95       N  
ATOM   4622  CA  LEU A 562       9.750  -7.567 -41.572  1.00 21.30           C  
ANISOU 4622  CA  LEU A 562     3461   2850   1783   -105   -189    118       C  
ATOM   4623  C   LEU A 562       9.767  -6.548 -42.722  1.00 21.65           C  
ANISOU 4623  C   LEU A 562     3425   2939   1860   -118   -206    137       C  
ATOM   4624  O   LEU A 562       9.825  -5.336 -42.482  1.00 22.84           O  
ANISOU 4624  O   LEU A 562     3589   3071   2018   -127   -224    150       O  
ATOM   4625  CB  LEU A 562      11.146  -8.189 -41.367  1.00 21.32           C  
ANISOU 4625  CB  LEU A 562     3469   2857   1774    -97   -255    122       C  
ATOM   4626  CG  LEU A 562      12.275  -7.250 -40.911  1.00 25.22           C  
ANISOU 4626  CG  LEU A 562     3973   3329   2282   -102   -337    131       C  
ATOM   4627  CD1 LEU A 562      11.963  -6.563 -39.564  1.00 25.55           C  
ANISOU 4627  CD1 LEU A 562     4138   3298   2273    -99   -355    124       C  
ATOM   4628  CD2 LEU A 562      13.601  -7.994 -40.823  1.00 24.02           C  
ANISOU 4628  CD2 LEU A 562     3794   3170   2162    -90   -411    124       C  
ATOM   4629  N   ILE A 563       9.716  -7.021 -43.964  1.00 19.23           N  
ANISOU 4629  N   ILE A 563     3056   2684   1567   -119   -201    140       N  
ATOM   4630  CA  ILE A 563       9.723  -6.089 -45.092  1.00 22.51           C  
ANISOU 4630  CA  ILE A 563     3434   3127   1991   -128   -216    163       C  
ATOM   4631  C   ILE A 563       8.410  -5.310 -45.226  1.00 23.83           C  
ANISOU 4631  C   ILE A 563     3598   3272   2183   -121   -213    160       C  
ATOM   4632  O   ILE A 563       8.416  -4.110 -45.521  1.00 22.68           O  
ANISOU 4632  O   ILE A 563     3454   3119   2045   -126   -233    184       O  
ATOM   4633  CB  ILE A 563      10.193  -6.723 -46.443  1.00 24.36           C  
ANISOU 4633  CB  ILE A 563     3637   3408   2210   -131   -210    168       C  
ATOM   4634  CG1 ILE A 563       9.323  -7.902 -46.881  1.00 19.36           C  
ANISOU 4634  CG1 ILE A 563     2994   2790   1574   -118   -197    139       C  
ATOM   4635  CG2 ILE A 563      11.661  -7.137 -46.356  1.00 20.98           C  
ANISOU 4635  CG2 ILE A 563     3190   2986   1794   -141   -207    170       C  
ATOM   4636  CD1 ILE A 563       9.782  -8.500 -48.195  1.00 18.61           C  
ANISOU 4636  CD1 ILE A 563     2892   2731   1448   -122   -190    140       C  
ATOM   4637  N   ASN A 564       7.293  -5.984 -44.969  1.00 22.57           N  
ANISOU 4637  N   ASN A 564     3430   3091   2056   -110   -184    128       N  
ATOM   4638  CA  ASN A 564       6.017  -5.295 -44.875  1.00 21.20           C  
ANISOU 4638  CA  ASN A 564     3235   2874   1946   -102   -175    114       C  
ATOM   4639  C   ASN A 564       5.961  -4.276 -43.726  1.00 22.48           C  
ANISOU 4639  C   ASN A 564     3441   2983   2118   -108   -146    118       C  
ATOM   4640  O   ASN A 564       5.271  -3.265 -43.830  1.00 22.08           O  
ANISOU 4640  O   ASN A 564     3370   2900   2118   -104   -152    120       O  
ATOM   4641  CB  ASN A 564       4.887  -6.301 -44.768  1.00 22.05           C  
ANISOU 4641  CB  ASN A 564     3307   2952   2118    -93   -134     68       C  
ATOM   4642  CG  ASN A 564       4.590  -6.975 -46.092  1.00 23.29           C  
ANISOU 4642  CG  ASN A 564     3415   3147   2286    -83   -189     55       C  
ATOM   4643  OD1 ASN A 564       5.005  -6.501 -47.150  1.00 23.67           O  
ANISOU 4643  OD1 ASN A 564     3471   3233   2290    -80   -254     83       O  
ATOM   4644  ND2 ASN A 564       3.871  -8.086 -46.040  1.00 20.46           N  
ANISOU 4644  ND2 ASN A 564     3022   2769   1983    -80   -156     11       N  
ATOM   4645  N   SER A 565       6.712  -4.535 -42.651  1.00 21.81           N  
ANISOU 4645  N   SER A 565     3425   2880   1981   -116   -124    118       N  
ATOM   4646  CA  SER A 565       6.775  -3.627 -41.506  1.00 21.84           C  
ANISOU 4646  CA  SER A 565     3501   2826   1972   -123   -103    118       C  
ATOM   4647  C   SER A 565       7.589  -2.375 -41.789  1.00 21.45           C  
ANISOU 4647  C   SER A 565     3444   2794   1912   -133   -164    149       C  
ATOM   4648  O   SER A 565       7.420  -1.366 -41.101  1.00 23.87           O  
ANISOU 4648  O   SER A 565     3793   3052   2225   -139   -153    148       O  
ATOM   4649  CB  SER A 565       7.336  -4.338 -40.278  1.00 22.43           C  
ANISOU 4649  CB  SER A 565     3681   2862   1978   -123    -86    106       C  
ATOM   4650  OG  SER A 565       6.465  -5.375 -39.871  1.00 26.50           O  
ANISOU 4650  OG  SER A 565     4224   3339   2506   -117     -1     77       O  
ATOM   4651  N   LEU A 566       8.475  -2.446 -42.784  1.00 21.21           N  
ANISOU 4651  N   LEU A 566     3366   2822   1870   -138   -213    174       N  
ATOM   4652  CA  LEU A 566       9.207  -1.272 -43.246  1.00 22.43           C  
ANISOU 4652  CA  LEU A 566     3506   2985   2033   -152   -249    204       C  
ATOM   4653  C   LEU A 566       8.265  -0.315 -43.958  1.00 22.37           C  
ANISOU 4653  C   LEU A 566     3474   2966   2059   -146   -248    220       C  
ATOM   4654  O   LEU A 566       8.330   0.888 -43.723  1.00 23.74           O  
ANISOU 4654  O   LEU A 566     3662   3108   2249   -153   -255    234       O  
ATOM   4655  CB  LEU A 566      10.404  -1.631 -44.146  1.00 20.74           C  
ANISOU 4655  CB  LEU A 566     3253   2816   1811   -164   -270    222       C  
ATOM   4656  CG  LEU A 566      11.202  -0.439 -44.714  1.00 21.82           C  
ANISOU 4656  CG  LEU A 566     3374   2948   1970   -185   -279    252       C  
ATOM   4657  CD1 LEU A 566      11.724   0.507 -43.619  1.00 15.48           C  
ANISOU 4657  CD1 LEU A 566     2594   2096   1192   -198   -307    244       C  
ATOM   4658  CD2 LEU A 566      12.351  -0.894 -45.602  1.00 23.39           C  
ANISOU 4658  CD2 LEU A 566     3535   3173   2179   -200   -262    262       C  
ATOM   4659  N   TYR A 567       7.400  -0.843 -44.826  1.00 22.33           N  
ANISOU 4659  N   TYR A 567     3435   2980   2070   -129   -251    215       N  
ATOM   4660  CA  TYR A 567       6.294  -0.035 -45.346  1.00 23.47           C  
ANISOU 4660  CA  TYR A 567     3557   3093   2266   -111   -273    219       C  
ATOM   4661  C   TYR A 567       5.502   0.562 -44.171  1.00 23.11           C  
ANISOU 4661  C   TYR A 567     3518   2980   2282   -109   -228    193       C  
ATOM   4662  O   TYR A 567       5.253   1.764 -44.134  1.00 22.64           O  
ANISOU 4662  O   TYR A 567     3461   2884   2256   -107   -239    207       O  
ATOM   4663  CB  TYR A 567       5.354  -0.822 -46.281  1.00 21.49           C  
ANISOU 4663  CB  TYR A 567     3267   2854   2044    -88   -306    201       C  
ATOM   4664  CG  TYR A 567       3.934  -0.334 -46.126  1.00 20.79           C  
ANISOU 4664  CG  TYR A 567     3132   2702   2064    -66   -316    174       C  
ATOM   4665  CD1 TYR A 567       3.006  -1.066 -45.384  1.00 20.35           C  
ANISOU 4665  CD1 TYR A 567     3034   2606   2093    -62   -258    121       C  
ATOM   4666  CD2 TYR A 567       3.545   0.908 -46.634  1.00 21.72           C  
ANISOU 4666  CD2 TYR A 567     3249   2786   2217    -50   -372    198       C  
ATOM   4667  CE1 TYR A 567       1.711  -0.593 -45.183  1.00 24.13           C  
ANISOU 4667  CE1 TYR A 567     3450   3008   2709    -44   -250     86       C  
ATOM   4668  CE2 TYR A 567       2.255   1.393 -46.435  1.00 22.87           C  
ANISOU 4668  CE2 TYR A 567     3337   2860   2494    -27   -384    167       C  
ATOM   4669  CZ  TYR A 567       1.346   0.638 -45.711  1.00 24.22           C  
ANISOU 4669  CZ  TYR A 567     3446   2988   2767    -24   -319    108       C  
ATOM   4670  OH  TYR A 567       0.070   1.110 -45.520  1.00 27.10           O  
ANISOU 4670  OH  TYR A 567     3733   3266   3296     -3   -317     68       O  
ATOM   4671  N   GLY A 568       5.118  -0.281 -43.214  1.00 22.65           N  
ANISOU 4671  N   GLY A 568     3474   2896   2235   -110   -166    155       N  
ATOM   4672  CA  GLY A 568       4.356   0.176 -42.047  1.00 23.12           C  
ANISOU 4672  CA  GLY A 568     3565   2875   2346   -112    -90    124       C  
ATOM   4673  C   GLY A 568       5.066   1.245 -41.233  1.00 24.74           C  
ANISOU 4673  C   GLY A 568     3842   3051   2506   -128    -89    138       C  
ATOM   4674  O   GLY A 568       4.439   2.196 -40.749  1.00 23.60           O  
ANISOU 4674  O   GLY A 568     3710   2843   2415   -127    -50    126       O  
ATOM   4675  N   ALA A 569       6.381   1.093 -41.091  1.00 24.61           N  
ANISOU 4675  N   ALA A 569     3868   3074   2407   -142   -135    158       N  
ATOM   4676  CA  ALA A 569       7.177   2.025 -40.314  1.00 24.93           C  
ANISOU 4676  CA  ALA A 569     3975   3084   2413   -158   -157    164       C  
ATOM   4677  C   ALA A 569       7.090   3.430 -40.900  1.00 26.71           C  
ANISOU 4677  C   ALA A 569     4162   3301   2687   -162   -180    190       C  
ATOM   4678  O   ALA A 569       6.989   4.408 -40.160  1.00 28.36           O  
ANISOU 4678  O   ALA A 569     4417   3451   2906   -170   -162    181       O  
ATOM   4679  CB  ALA A 569       8.614   1.552 -40.226  1.00 25.68           C  
ANISOU 4679  CB  ALA A 569     4089   3215   2452   -169   -222    174       C  
ATOM   4680  N   LEU A 570       7.070   3.522 -42.230  1.00 26.57           N  
ANISOU 4680  N   LEU A 570     4075   3330   2691   -155   -216    222       N  
ATOM   4681  CA  LEU A 570       6.943   4.806 -42.924  1.00 24.83           C  
ANISOU 4681  CA  LEU A 570     3834   3093   2507   -153   -241    254       C  
ATOM   4682  C   LEU A 570       5.675   5.551 -42.517  1.00 24.67           C  
ANISOU 4682  C   LEU A 570     3806   3004   2565   -136   -209    235       C  
ATOM   4683  O   LEU A 570       5.574   6.769 -42.713  1.00 24.05           O  
ANISOU 4683  O   LEU A 570     3727   2890   2521   -135   -223    256       O  
ATOM   4684  CB  LEU A 570       6.962   4.610 -44.448  1.00 23.98           C  
ANISOU 4684  CB  LEU A 570     3691   3031   2388   -141   -284    291       C  
ATOM   4685  CG  LEU A 570       8.239   4.068 -45.103  1.00 22.80           C  
ANISOU 4685  CG  LEU A 570     3546   2937   2180   -161   -293    313       C  
ATOM   4686  CD1 LEU A 570       7.970   3.729 -46.558  1.00 19.43           C  
ANISOU 4686  CD1 LEU A 570     3119   2540   1725   -144   -319    339       C  
ATOM   4687  CD2 LEU A 570       9.414   5.041 -44.994  1.00 20.39           C  
ANISOU 4687  CD2 LEU A 570     3255   2615   1878   -191   -289    334       C  
ATOM   4688  N   GLY A 571       4.717   4.808 -41.961  1.00 24.07           N  
ANISOU 4688  N   GLY A 571     3719   2898   2528   -124   -154    193       N  
ATOM   4689  CA  GLY A 571       3.474   5.383 -41.442  1.00 24.15           C  
ANISOU 4689  CA  GLY A 571     3709   2823   2643   -110    -94    160       C  
ATOM   4690  C   GLY A 571       3.340   5.387 -39.922  1.00 23.89           C  
ANISOU 4690  C   GLY A 571     3762   2720   2595   -127     10    118       C  
ATOM   4691  O   GLY A 571       2.241   5.587 -39.403  1.00 22.98           O  
ANISOU 4691  O   GLY A 571     3632   2522   2576   -119     99     78       O  
ATOM   4692  N   ASN A 572       4.448   5.160 -39.209  1.00 24.40           N  
ANISOU 4692  N   ASN A 572     3922   2804   2544   -149     -1    122       N  
ATOM   4693  CA  ASN A 572       4.479   5.304 -37.744  1.00 24.25           C  
ANISOU 4693  CA  ASN A 572     4034   2707   2474   -164     74     86       C  
ATOM   4694  C   ASN A 572       5.352   6.480 -37.285  1.00 24.16           C  
ANISOU 4694  C   ASN A 572     4089   2674   2417   -182     24     97       C  
ATOM   4695  O   ASN A 572       6.518   6.562 -37.666  1.00 24.78           O  
ANISOU 4695  O   ASN A 572     4155   2809   2450   -192    -73    124       O  
ATOM   4696  CB  ASN A 572       4.948   4.015 -37.073  1.00 23.88           C  
ANISOU 4696  CB  ASN A 572     4077   2668   2328   -168     88     71       C  
ATOM   4697  CG  ASN A 572       5.018   4.143 -35.552  1.00 28.05           C  
ANISOU 4697  CG  ASN A 572     4787   3101   2772   -180    155     36       C  
ATOM   4698  OD1 ASN A 572       5.843   4.887 -35.015  1.00 30.96           O  
ANISOU 4698  OD1 ASN A 572     5238   3449   3076   -192     92     38       O  
ATOM   4699  ND2 ASN A 572       4.141   3.431 -34.858  1.00 26.67           N  
ANISOU 4699  ND2 ASN A 572     4684   2854   2597   -178    287      1       N  
ATOM   4700  N   VAL A 573       4.792   7.369 -36.455  1.00 25.93           N  
ANISOU 4700  N   VAL A 573     4380   2806   2667   -188     99     68       N  
ATOM   4701  CA  VAL A 573       5.467   8.631 -36.062  1.00 26.92           C  
ANISOU 4701  CA  VAL A 573     4560   2899   2769   -205     55     72       C  
ATOM   4702  C   VAL A 573       6.834   8.452 -35.372  1.00 28.02           C  
ANISOU 4702  C   VAL A 573     4807   3047   2793   -224    -36     66       C  
ATOM   4703  O   VAL A 573       7.688   9.332 -35.452  1.00 31.30           O  
ANISOU 4703  O   VAL A 573     5215   3465   3213   -240   -116     77       O  
ATOM   4704  CB  VAL A 573       4.546   9.593 -35.221  1.00 27.75           C  
ANISOU 4704  CB  VAL A 573     4730   2889   2924   -208    167     34       C  
ATOM   4705  CG1 VAL A 573       3.324  10.051 -36.043  1.00 26.44           C  
ANISOU 4705  CG1 VAL A 573     4423   2705   2917   -185    219     40       C  
ATOM   4706  CG2 VAL A 573       4.115   8.967 -33.873  1.00 24.96           C  
ANISOU 4706  CG2 VAL A 573     4543   2445   2496   -214    287    -18       C  
ATOM   4707  N   TRP A 574       7.036   7.303 -34.730  1.00 28.50           N  
ANISOU 4707  N   TRP A 574     4961   3103   2766   -220    -33     47       N  
ATOM   4708  CA  TRP A 574       8.294   6.981 -34.042  1.00 31.22           C  
ANISOU 4708  CA  TRP A 574     5410   3442   3010   -227   -145     36       C  
ATOM   4709  C   TRP A 574       9.459   6.552 -34.952  1.00 28.37           C  
ANISOU 4709  C   TRP A 574     4930   3175   2675   -229   -269     67       C  
ATOM   4710  O   TRP A 574      10.606   6.539 -34.514  1.00 28.40           O  
ANISOU 4710  O   TRP A 574     4978   3166   2646   -236   -384     54       O  
ATOM   4711  CB  TRP A 574       8.040   5.943 -32.935  1.00 34.42           C  
ANISOU 4711  CB  TRP A 574     5992   3784   3302   -217    -95      5       C  
ATOM   4712  CG  TRP A 574       7.035   6.448 -31.952  1.00 41.76           C  
ANISOU 4712  CG  TRP A 574     7065   4598   4202   -222     47    -32       C  
ATOM   4713  CD1 TRP A 574       5.710   6.123 -31.893  1.00 43.98           C  
ANISOU 4713  CD1 TRP A 574     7340   4835   4535   -218    222    -48       C  
ATOM   4714  CD2 TRP A 574       7.259   7.419 -30.921  1.00 44.97           C  
ANISOU 4714  CD2 TRP A 574     7636   4908   4542   -236     39    -65       C  
ATOM   4715  NE1 TRP A 574       5.099   6.815 -30.874  1.00 47.85           N  
ANISOU 4715  NE1 TRP A 574     7982   5202   4996   -228    342    -88       N  
ATOM   4716  CE2 TRP A 574       6.026   7.619 -30.263  1.00 47.56           C  
ANISOU 4716  CE2 TRP A 574     8064   5134   4874   -239    231    -97       C  
ATOM   4717  CE3 TRP A 574       8.385   8.130 -30.482  1.00 48.25           C  
ANISOU 4717  CE3 TRP A 574     8123   5304   4907   -247   -112    -76       C  
ATOM   4718  CZ2 TRP A 574       5.886   8.500 -29.181  1.00 51.56           C  
ANISOU 4718  CZ2 TRP A 574     8758   5520   5312   -253    286   -138       C  
ATOM   4719  CZ3 TRP A 574       8.247   9.010 -29.404  1.00 51.35           C  
ANISOU 4719  CZ3 TRP A 574     8700   5579   5230   -259    -80   -118       C  
ATOM   4720  CH2 TRP A 574       7.004   9.187 -28.769  1.00 52.22           C  
ANISOU 4720  CH2 TRP A 574     8926   5592   5323   -262    123   -147       C  
ATOM   4721  N   PHE A 575       9.172   6.230 -36.212  1.00 25.76           N  
ANISOU 4721  N   PHE A 575     4451   2924   2413   -222   -247    103       N  
ATOM   4722  CA  PHE A 575      10.213   5.861 -37.177  1.00 24.81           C  
ANISOU 4722  CA  PHE A 575     4222   2881   2323   -227   -328    131       C  
ATOM   4723  C   PHE A 575      11.015   7.090 -37.619  1.00 26.30           C  
ANISOU 4723  C   PHE A 575     4350   3067   2576   -250   -380    146       C  
ATOM   4724  O   PHE A 575      10.441   8.118 -37.961  1.00 28.66           O  
ANISOU 4724  O   PHE A 575     4624   3348   2917   -255   -336    162       O  
ATOM   4725  CB  PHE A 575       9.578   5.179 -38.386  1.00 22.84           C  
ANISOU 4725  CB  PHE A 575     3866   2703   2108   -213   -281    160       C  
ATOM   4726  CG  PHE A 575      10.556   4.472 -39.292  1.00 20.44           C  
ANISOU 4726  CG  PHE A 575     3481   2470   1816   -216   -334    182       C  
ATOM   4727  CD1 PHE A 575      11.589   3.700 -38.775  1.00 22.63           C  
ANISOU 4727  CD1 PHE A 575     3785   2748   2066   -218   -401    163       C  
ATOM   4728  CD2 PHE A 575      10.409   4.544 -40.671  1.00 20.47           C  
ANISOU 4728  CD2 PHE A 575     3392   2528   1858   -215   -316    218       C  
ATOM   4729  CE1 PHE A 575      12.481   3.025 -39.624  1.00 22.65           C  
ANISOU 4729  CE1 PHE A 575     3699   2804   2101   -221   -433    177       C  
ATOM   4730  CE2 PHE A 575      11.287   3.869 -41.527  1.00 21.36           C  
ANISOU 4730  CE2 PHE A 575     3444   2694   1979   -221   -338    234       C  
ATOM   4731  CZ  PHE A 575      12.323   3.111 -41.001  1.00 20.54           C  
ANISOU 4731  CZ  PHE A 575     3344   2590   1869   -226   -387    212       C  
ATOM   4732  N   ARG A 576      12.341   6.976 -37.597  1.00 25.10           N  
ANISOU 4732  N   ARG A 576     4128   2909   2500   -431   -166    -84       N  
ATOM   4733  CA  ARG A 576      13.239   8.039 -38.048  1.00 25.26           C  
ANISOU 4733  CA  ARG A 576     4118   2911   2570   -428   -141   -101       C  
ATOM   4734  C   ARG A 576      12.859   8.558 -39.454  1.00 27.12           C  
ANISOU 4734  C   ARG A 576     4304   3130   2871   -352    -76    -84       C  
ATOM   4735  O   ARG A 576      12.967   9.753 -39.734  1.00 25.92           O  
ANISOU 4735  O   ARG A 576     4141   2949   2757   -351    -12   -102       O  
ATOM   4736  CB  ARG A 576      14.682   7.519 -38.044  1.00 24.96           C  
ANISOU 4736  CB  ARG A 576     4048   2888   2548   -440   -233    -85       C  
ATOM   4737  CG  ARG A 576      15.768   8.592 -38.159  1.00 23.72           C  
ANISOU 4737  CG  ARG A 576     3869   2713   2429   -461   -219   -110       C  
ATOM   4738  CD  ARG A 576      17.178   7.985 -38.148  1.00 20.32           C  
ANISOU 4738  CD  ARG A 576     3399   2296   2027   -471   -314    -91       C  
ATOM   4739  NE  ARG A 576      17.474   7.237 -36.916  1.00 23.31           N  
ANISOU 4739  NE  ARG A 576     3810   2697   2350   -538   -405    -77       N  
ATOM   4740  CZ  ARG A 576      17.915   7.772 -35.781  1.00 23.91           C  
ANISOU 4740  CZ  ARG A 576     3927   2782   2376   -626   -429   -100       C  
ATOM   4741  NH1 ARG A 576      18.127   9.081 -35.689  1.00 22.51           N  
ANISOU 4741  NH1 ARG A 576     3762   2586   2204   -657   -363   -148       N  
ATOM   4742  NH2 ARG A 576      18.149   6.993 -34.728  1.00 23.59           N  
ANISOU 4742  NH2 ARG A 576     3917   2768   2280   -689   -522    -75       N  
ATOM   4743  N   TYR A 577      12.390   7.658 -40.316  1.00 25.53           N  
ANISOU 4743  N   TYR A 577     4074   2947   2680   -296    -93    -48       N  
ATOM   4744  CA  TYR A 577      12.081   8.005 -41.708  1.00 26.00           C  
ANISOU 4744  CA  TYR A 577     4087   3003   2789   -234    -48    -23       C  
ATOM   4745  C   TYR A 577      10.580   8.052 -42.002  1.00 26.00           C  
ANISOU 4745  C   TYR A 577     4093   2999   2786   -205      7     -5       C  
ATOM   4746  O   TYR A 577      10.158   7.891 -43.149  1.00 26.96           O  
ANISOU 4746  O   TYR A 577     4179   3135   2932   -157     20     29       O  
ATOM   4747  CB  TYR A 577      12.815   7.059 -42.668  1.00 26.04           C  
ANISOU 4747  CB  TYR A 577     4046   3034   2815   -199   -101      0       C  
ATOM   4748  CG  TYR A 577      14.274   6.914 -42.320  1.00 26.45           C  
ANISOU 4748  CG  TYR A 577     4083   3083   2884   -227   -158    -14       C  
ATOM   4749  CD1 TYR A 577      14.739   5.788 -41.632  1.00 26.97           C  
ANISOU 4749  CD1 TYR A 577     4153   3161   2932   -248   -238     -9       C  
ATOM   4750  CD2 TYR A 577      15.188   7.913 -42.650  1.00 25.63           C  
ANISOU 4750  CD2 TYR A 577     3956   2962   2821   -234   -134    -29       C  
ATOM   4751  CE1 TYR A 577      16.082   5.663 -41.292  1.00 27.22           C  
ANISOU 4751  CE1 TYR A 577     4162   3188   2992   -275   -298    -14       C  
ATOM   4752  CE2 TYR A 577      16.530   7.795 -42.316  1.00 26.05           C  
ANISOU 4752  CE2 TYR A 577     3989   3011   2897   -261   -189    -42       C  
ATOM   4753  CZ  TYR A 577      16.968   6.675 -41.639  1.00 26.54           C  
ANISOU 4753  CZ  TYR A 577     4052   3086   2947   -281   -272    -33       C  
ATOM   4754  OH  TYR A 577      18.296   6.564 -41.318  1.00 27.00           O  
ANISOU 4754  OH  TYR A 577     4081   3138   3040   -308   -332    -37       O  
ATOM   4755  N   TYR A 578       9.788   8.262 -40.950  1.00 24.24           N  
ANISOU 4755  N   TYR A 578     3916   2760   2534   -240     37    -29       N  
ATOM   4756  CA  TYR A 578       8.366   8.517 -41.066  1.00 23.89           C  
ANISOU 4756  CA  TYR A 578     3873   2700   2503   -219    101    -19       C  
ATOM   4757  C   TYR A 578       8.089   9.567 -42.126  1.00 24.28           C  
ANISOU 4757  C   TYR A 578     3877   2725   2622   -177    161      9       C  
ATOM   4758  O   TYR A 578       8.623  10.670 -42.077  1.00 23.00           O  
ANISOU 4758  O   TYR A 578     3709   2530   2498   -191    201     -7       O  
ATOM   4759  CB  TYR A 578       7.826   9.025 -39.727  1.00 25.82           C  
ANISOU 4759  CB  TYR A 578     4172   2915   2724   -278    150    -66       C  
ATOM   4760  CG  TYR A 578       6.383   9.490 -39.756  1.00 24.57           C  
ANISOU 4760  CG  TYR A 578     4009   2725   2603   -260    232    -63       C  
ATOM   4761  CD1 TYR A 578       6.069  10.850 -39.737  1.00 24.20           C  
ANISOU 4761  CD1 TYR A 578     3949   2623   2623   -264    322    -81       C  
ATOM   4762  CD2 TYR A 578       5.331   8.565 -39.794  1.00 24.13           C  
ANISOU 4762  CD2 TYR A 578     3957   2688   2525   -240    222    -44       C  
ATOM   4763  CE1 TYR A 578       4.737  11.286 -39.753  1.00 26.30           C  
ANISOU 4763  CE1 TYR A 578     4200   2849   2942   -246    400    -75       C  
ATOM   4764  CE2 TYR A 578       4.001   8.983 -39.804  1.00 26.07           C  
ANISOU 4764  CE2 TYR A 578     4191   2900   2815   -224    296    -40       C  
ATOM   4765  CZ  TYR A 578       3.713  10.347 -39.785  1.00 27.36           C  
ANISOU 4765  CZ  TYR A 578     4336   3005   3054   -226    385    -55       C  
ATOM   4766  OH  TYR A 578       2.405  10.764 -39.788  1.00 30.15           O  
ANISOU 4766  OH  TYR A 578     4667   3317   3470   -209    460    -48       O  
ATOM   4767  N   ASP A 579       7.247   9.217 -43.084  1.00 24.68           N  
ANISOU 4767  N   ASP A 579     3895   2793   2691   -129    165     56       N  
ATOM   4768  CA  ASP A 579       6.839  10.160 -44.105  1.00 25.49           C  
ANISOU 4768  CA  ASP A 579     3952   2875   2857    -93    214     98       C  
ATOM   4769  C   ASP A 579       5.559   9.664 -44.750  1.00 25.39           C  
ANISOU 4769  C   ASP A 579     3915   2882   2851    -57    217    146       C  
ATOM   4770  O   ASP A 579       5.555   8.640 -45.444  1.00 22.10           O  
ANISOU 4770  O   ASP A 579     3486   2515   2397    -39    166    169       O  
ATOM   4771  CB  ASP A 579       7.937  10.355 -45.153  1.00 25.59           C  
ANISOU 4771  CB  ASP A 579     3931   2907   2883    -78    189    120       C  
ATOM   4772  CG  ASP A 579       7.729  11.608 -45.993  1.00 27.51           C  
ANISOU 4772  CG  ASP A 579     4137   3121   3196    -55    244    162       C  
ATOM   4773  OD1 ASP A 579       8.737  12.207 -46.442  1.00 27.68           O  
ANISOU 4773  OD1 ASP A 579     4143   3135   3237    -60    246    162       O  
ATOM   4774  OD2 ASP A 579       6.556  11.997 -46.197  1.00 25.82           O  
ANISOU 4774  OD2 ASP A 579     3904   2887   3022    -35    283    199       O  
ATOM   4775  N   LEU A 580       4.477  10.401 -44.507  1.00 25.54           N  
ANISOU 4775  N   LEU A 580     3923   2857   2922    -50    281    156       N  
ATOM   4776  CA  LEU A 580       3.158  10.041 -45.027  1.00 25.93           C  
ANISOU 4776  CA  LEU A 580     3943   2918   2990    -19    287    204       C  
ATOM   4777  C   LEU A 580       3.030  10.169 -46.549  1.00 25.73           C  
ANISOU 4777  C   LEU A 580     3863   2924   2988     17    266    281       C  
ATOM   4778  O   LEU A 580       2.184   9.513 -47.156  1.00 25.35           O  
ANISOU 4778  O   LEU A 580     3793   2912   2928     36    242    323       O  
ATOM   4779  CB  LEU A 580       2.056  10.820 -44.303  1.00 27.09           C  
ANISOU 4779  CB  LEU A 580     4087   3001   3204    -24    367    192       C  
ATOM   4780  CG  LEU A 580       1.108  10.048 -43.366  1.00 30.52           C  
ANISOU 4780  CG  LEU A 580     4554   3435   3607    -42    378    157       C  
ATOM   4781  CD1 LEU A 580       1.687   8.757 -42.756  1.00 23.16           C  
ANISOU 4781  CD1 LEU A 580     3677   2552   2571    -71    312    117       C  
ATOM   4782  CD2 LEU A 580       0.569  10.960 -42.285  1.00 29.34           C  
ANISOU 4782  CD2 LEU A 580     4422   3212   3514    -73    471    107       C  
ATOM   4783  N   ARG A 581       3.877  10.993 -47.159  1.00 25.11           N  
ANISOU 4783  N   ARG A 581     3766   2837   2939     20    273    300       N  
ATOM   4784  CA  ARG A 581       3.966  11.061 -48.628  1.00 25.00           C  
ANISOU 4784  CA  ARG A 581     3708   2862   2927     40    246    371       C  
ATOM   4785  C   ARG A 581       4.458   9.726 -49.204  1.00 25.39           C  
ANISOU 4785  C   ARG A 581     3769   2985   2894     33    181    361       C  
ATOM   4786  O   ARG A 581       3.975   9.271 -50.251  1.00 25.18           O  
ANISOU 4786  O   ARG A 581     3715   3007   2844     42    155    412       O  
ATOM   4787  CB  ARG A 581       4.908  12.183 -49.077  1.00 23.29           C  
ANISOU 4787  CB  ARG A 581     3476   2619   2753     36    270    385       C  
ATOM   4788  CG  ARG A 581       4.548  13.593 -48.581  1.00 27.30           C  
ANISOU 4788  CG  ARG A 581     3969   3046   3359     40    344    392       C  
ATOM   4789  CD  ARG A 581       5.655  14.606 -48.921  1.00 29.69           C  
ANISOU 4789  CD  ARG A 581     4263   3322   3695     31    366    393       C  
ATOM   4790  NE  ARG A 581       6.885  14.363 -48.155  1.00 30.45           N  
ANISOU 4790  NE  ARG A 581     4403   3422   3746      1    354    310       N  
ATOM   4791  CZ  ARG A 581       8.009  15.065 -48.286  1.00 30.40           C  
ANISOU 4791  CZ  ARG A 581     4395   3397   3756    -13    367    293       C  
ATOM   4792  NH1 ARG A 581       8.075  16.069 -49.154  1.00 30.81           N  
ANISOU 4792  NH1 ARG A 581     4411   3426   3870      0    398    351       N  
ATOM   4793  NH2 ARG A 581       9.070  14.766 -47.548  1.00 24.54           N  
ANISOU 4793  NH2 ARG A 581     3688   2661   2975    -43    347    222       N  
ATOM   4794  N   ASN A 582       5.419   9.104 -48.523  1.00 23.41           N  
ANISOU 4794  N   ASN A 582     3554   2740   2601     14    156    297       N  
ATOM   4795  CA  ASN A 582       5.942   7.805 -48.954  1.00 25.61           C  
ANISOU 4795  CA  ASN A 582     3838   3073   2818      8    102    280       C  
ATOM   4796  C   ASN A 582       4.986   6.634 -48.679  1.00 24.30           C  
ANISOU 4796  C   ASN A 582     3684   2935   2615     13     78    276       C  
ATOM   4797  O   ASN A 582       4.773   5.783 -49.553  1.00 24.49           O  
ANISOU 4797  O   ASN A 582     3691   3008   2605     16     50    295       O  
ATOM   4798  CB  ASN A 582       7.342   7.545 -48.364  1.00 25.80           C  
ANISOU 4798  CB  ASN A 582     3885   3089   2829    -12     79    223       C  
ATOM   4799  CG  ASN A 582       8.439   8.381 -49.042  1.00 27.63           C  
ANISOU 4799  CG  ASN A 582     4096   3314   3090    -17     93    228       C  
ATOM   4800  OD1 ASN A 582       8.242   8.945 -50.126  1.00 24.11           O  
ANISOU 4800  OD1 ASN A 582     3621   2881   2659     -8    112    276       O  
ATOM   4801  ND2 ASN A 582       9.601   8.457 -48.400  1.00 24.43           N  
ANISOU 4801  ND2 ASN A 582     3705   2888   2689    -36     80    181       N  
ATOM   4802  N   ALA A 583       4.397   6.596 -47.482  1.00 23.31           N  
ANISOU 4802  N   ALA A 583     3587   2776   2492      7     93    249       N  
ATOM   4803  CA  ALA A 583       3.449   5.526 -47.138  1.00 21.17           C  
ANISOU 4803  CA  ALA A 583     3330   2526   2188      9     76    244       C  
ATOM   4804  C   ALA A 583       2.238   5.552 -48.081  1.00 23.39           C  
ANISOU 4804  C   ALA A 583     3572   2831   2485     30     85    303       C  
ATOM   4805  O   ALA A 583       1.796   4.506 -48.576  1.00 24.12           O  
ANISOU 4805  O   ALA A 583     3658   2969   2539     32     54    312       O  
ATOM   4806  CB  ALA A 583       3.012   5.628 -45.669  1.00 17.37           C  
ANISOU 4806  CB  ALA A 583     2891   2002   1707    -10    101    204       C  
ATOM   4807  N   THR A 584       1.739   6.761 -48.349  1.00 22.07           N  
ANISOU 4807  N   THR A 584     3376   2632   2379     43    126    345       N  
ATOM   4808  CA  THR A 584       0.593   6.971 -49.233  1.00 22.46           C  
ANISOU 4808  CA  THR A 584     3379   2699   2457     61    130    416       C  
ATOM   4809  C   THR A 584       0.932   6.693 -50.703  1.00 23.41           C  
ANISOU 4809  C   THR A 584     3471   2884   2542     57     91    463       C  
ATOM   4810  O   THR A 584       0.096   6.162 -51.442  1.00 23.96           O  
ANISOU 4810  O   THR A 584     3515   2998   2589     57     67    506       O  
ATOM   4811  CB  THR A 584      -0.002   8.396 -49.053  1.00 24.06           C  
ANISOU 4811  CB  THR A 584     3551   2837   2756     76    187    454       C  
ATOM   4812  OG1 THR A 584      -0.312   8.607 -47.663  1.00 26.22           O  
ANISOU 4812  OG1 THR A 584     3856   3052   3057     68    235    396       O  
ATOM   4813  CG2 THR A 584      -1.273   8.568 -49.873  1.00 24.44           C  
ANISOU 4813  CG2 THR A 584     3542   2898   2847     95    183    537       C  
ATOM   4814  N   ALA A 585       2.151   7.026 -51.122  1.00 21.53           N  
ANISOU 4814  N   ALA A 585     3237   2651   2292     46     86    452       N  
ATOM   4815  CA  ALA A 585       2.599   6.678 -52.475  1.00 23.27           C  
ANISOU 4815  CA  ALA A 585     3439   2934   2467     29     57    481       C  
ATOM   4816  C   ALA A 585       2.531   5.168 -52.715  1.00 22.47           C  
ANISOU 4816  C   ALA A 585     3351   2889   2298     15     22    447       C  
ATOM   4817  O   ALA A 585       2.117   4.730 -53.783  1.00 24.36           O  
ANISOU 4817  O   ALA A 585     3570   3187   2499     -3      2    483       O  
ATOM   4818  CB  ALA A 585       4.012   7.209 -52.746  1.00 20.37           C  
ANISOU 4818  CB  ALA A 585     3079   2559   2103     17     65    460       C  
ATOM   4819  N   ILE A 586       2.943   4.387 -51.721  1.00 21.11           N  
ANISOU 4819  N   ILE A 586     3212   2697   2111     16     14    380       N  
ATOM   4820  CA  ILE A 586       2.869   2.925 -51.798  1.00 21.43           C  
ANISOU 4820  CA  ILE A 586     3263   2775   2103      5    -14    345       C  
ATOM   4821  C   ILE A 586       1.424   2.423 -51.904  1.00 22.35           C  
ANISOU 4821  C   ILE A 586     3368   2917   2205     10    -21    375       C  
ATOM   4822  O   ILE A 586       1.106   1.658 -52.814  1.00 24.52           O  
ANISOU 4822  O   ILE A 586     3629   3249   2440     -8    -39    386       O  
ATOM   4823  CB  ILE A 586       3.562   2.254 -50.579  1.00 21.40           C  
ANISOU 4823  CB  ILE A 586     3294   2737   2098      6    -26    280       C  
ATOM   4824  CG1 ILE A 586       5.062   2.589 -50.574  1.00 20.33           C  
ANISOU 4824  CG1 ILE A 586     3162   2584   1980     -3    -28    250       C  
ATOM   4825  CG2 ILE A 586       3.318   0.731 -50.576  1.00 16.62           C  
ANISOU 4825  CG2 ILE A 586     2697   2161   1458     -2    -53    251       C  
ATOM   4826  CD1 ILE A 586       5.686   2.521 -49.191  1.00 16.20           C  
ANISOU 4826  CD1 ILE A 586     2671   2015   1470     -5    -40    207       C  
ATOM   4827  N   THR A 587       0.558   2.854 -50.980  1.00 24.23           N  
ANISOU 4827  N   THR A 587     3613   3113   2480     28     -2    384       N  
ATOM   4828  CA  THR A 587      -0.827   2.353 -50.927  1.00 23.39           C  
ANISOU 4828  CA  THR A 587     3495   3022   2371     34     -5    407       C  
ATOM   4829  C   THR A 587      -1.666   2.803 -52.127  1.00 24.01           C  
ANISOU 4829  C   THR A 587     3524   3140   2458     31    -13    485       C  
ATOM   4830  O   THR A 587      -2.492   2.036 -52.646  1.00 24.05           O  
ANISOU 4830  O   THR A 587     3513   3193   2433     21    -35    504       O  
ATOM   4831  CB  THR A 587      -1.561   2.712 -49.598  1.00 25.73           C  
ANISOU 4831  CB  THR A 587     3809   3258   2710     48     28    390       C  
ATOM   4832  OG1 THR A 587      -1.789   4.125 -49.509  1.00 22.60           O  
ANISOU 4832  OG1 THR A 587     3390   2815   2383     62     67    426       O  
ATOM   4833  CG2 THR A 587      -0.775   2.234 -48.384  1.00 22.95           C  
ANISOU 4833  CG2 THR A 587     3509   2875   2335     38     27    320       C  
ATOM   4834  N   THR A 588      -1.431   4.031 -52.584  1.00 23.41           N  
ANISOU 4834  N   THR A 588     3423   3047   2423     37      1    535       N  
ATOM   4835  CA  THR A 588      -2.145   4.558 -53.742  1.00 22.92           C  
ANISOU 4835  CA  THR A 588     3313   3023   2374     30    -16    626       C  
ATOM   4836  C   THR A 588      -1.736   3.825 -55.033  1.00 23.15           C  
ANISOU 4836  C   THR A 588     3339   3137   2319    -11    -53    635       C  
ATOM   4837  O   THR A 588      -2.601   3.404 -55.796  1.00 24.45           O  
ANISOU 4837  O   THR A 588     3478   3359   2454    -32    -81    681       O  
ATOM   4838  CB  THR A 588      -2.001   6.082 -53.842  1.00 22.86           C  
ANISOU 4838  CB  THR A 588     3278   2966   2443     45     10    683       C  
ATOM   4839  OG1 THR A 588      -2.294   6.650 -52.558  1.00 27.03           O  
ANISOU 4839  OG1 THR A 588     3814   3412   3044     74     57    652       O  
ATOM   4840  CG2 THR A 588      -2.981   6.658 -54.864  1.00 24.88           C  
ANISOU 4840  CG2 THR A 588     3474   3250   2730     41    -13    794       C  
ATOM   4841  N   PHE A 589      -0.433   3.651 -55.249  1.00 22.67           N  
ANISOU 4841  N   PHE A 589     3305   3086   2224    -28    -48    586       N  
ATOM   4842  CA  PHE A 589       0.084   2.849 -56.371  1.00 22.10           C  
ANISOU 4842  CA  PHE A 589     3235   3087   2074    -74    -67    570       C  
ATOM   4843  C   PHE A 589      -0.569   1.464 -56.346  1.00 22.87           C  
ANISOU 4843  C   PHE A 589     3341   3224   2126    -88    -84    534       C  
ATOM   4844  O   PHE A 589      -0.968   0.941 -57.385  1.00 23.19           O  
ANISOU 4844  O   PHE A 589     3367   3335   2108   -130   -103    555       O  
ATOM   4845  CB  PHE A 589       1.616   2.722 -56.277  1.00 21.08           C  
ANISOU 4845  CB  PHE A 589     3132   2940   1936    -82    -49    502       C  
ATOM   4846  CG  PHE A 589       2.278   2.166 -57.525  1.00 19.08           C  
ANISOU 4846  CG  PHE A 589     2879   2754   1618   -136    -51    484       C  
ATOM   4847  CD1 PHE A 589       2.362   0.792 -57.740  1.00 17.53           C  
ANISOU 4847  CD1 PHE A 589     2692   2592   1375   -162    -53    422       C  
ATOM   4848  CD2 PHE A 589       2.851   3.021 -58.462  1.00 19.71           C  
ANISOU 4848  CD2 PHE A 589     2948   2855   1685   -164    -43    524       C  
ATOM   4849  CE1 PHE A 589       2.984   0.273 -58.892  1.00 17.12           C  
ANISOU 4849  CE1 PHE A 589     2640   2597   1268   -220    -41    394       C  
ATOM   4850  CE2 PHE A 589       3.471   2.515 -59.616  1.00 23.02           C  
ANISOU 4850  CE2 PHE A 589     3371   3337   2040   -225    -34    500       C  
ATOM   4851  CZ  PHE A 589       3.539   1.137 -59.826  1.00 17.79           C  
ANISOU 4851  CZ  PHE A 589     2718   2709   1333   -254    -30    430       C  
ATOM   4852  N   GLY A 590      -0.696   0.893 -55.149  1.00 24.39           N  
ANISOU 4852  N   GLY A 590     3556   3371   2342    -58    -76    480       N  
ATOM   4853  CA  GLY A 590      -1.344  -0.413 -54.955  1.00 25.54           C  
ANISOU 4853  CA  GLY A 590     3709   3540   2454    -67    -88    444       C  
ATOM   4854  C   GLY A 590      -2.779  -0.453 -55.459  1.00 25.62           C  
ANISOU 4854  C   GLY A 590     3687   3591   2455    -76   -106    506       C  
ATOM   4855  O   GLY A 590      -3.179  -1.393 -56.164  1.00 23.30           O  
ANISOU 4855  O   GLY A 590     3387   3358   2106   -112   -123    497       O  
ATOM   4856  N   GLN A 591      -3.544   0.577 -55.109  1.00 25.18           N  
ANISOU 4856  N   GLN A 591     3608   3500   2460    -47   -101    567       N  
ATOM   4857  CA  GLN A 591      -4.940   0.689 -55.521  1.00 26.05           C  
ANISOU 4857  CA  GLN A 591     3676   3639   2584    -51   -122    638       C  
ATOM   4858  C   GLN A 591      -5.043   0.779 -57.032  1.00 26.49           C  
ANISOU 4858  C   GLN A 591     3702   3777   2585   -100   -157    702       C  
ATOM   4859  O   GLN A 591      -5.924   0.174 -57.627  1.00 26.82           O  
ANISOU 4859  O   GLN A 591     3722   3878   2590   -130   -186    729       O  
ATOM   4860  CB  GLN A 591      -5.606   1.917 -54.888  1.00 28.29           C  
ANISOU 4860  CB  GLN A 591     3929   3854   2965    -10   -101    693       C  
ATOM   4861  CG  GLN A 591      -5.915   1.787 -53.391  1.00 30.58           C  
ANISOU 4861  CG  GLN A 591     4245   4070   3304     25    -62    636       C  
ATOM   4862  CD  GLN A 591      -7.031   2.730 -52.929  1.00 34.81           C  
ANISOU 4862  CD  GLN A 591     4738   4549   3940     55    -36    690       C  
ATOM   4863  OE1 GLN A 591      -7.664   3.411 -53.737  1.00 40.39           O  
ANISOU 4863  OE1 GLN A 591     5387   5270   4688     54    -55    780       O  
ATOM   4864  NE2 GLN A 591      -7.280   2.758 -51.629  1.00 35.38           N  
ANISOU 4864  NE2 GLN A 591     4834   4554   4055     76      9    637       N  
ATOM   4865  N   MET A 592      -4.131   1.541 -57.637  1.00 27.81           N  
ANISOU 4865  N   MET A 592     3871   3951   2744   -115   -154    725       N  
ATOM   4866  CA  MET A 592      -4.031   1.656 -59.087  1.00 28.56           C  
ANISOU 4866  CA  MET A 592     3949   4129   2773   -175   -184    782       C  
ATOM   4867  C   MET A 592      -3.665   0.324 -59.738  1.00 27.91           C  
ANISOU 4867  C   MET A 592     3893   4118   2593   -232   -188    712       C  
ATOM   4868  O   MET A 592      -4.296  -0.076 -60.707  1.00 28.98           O  
ANISOU 4868  O   MET A 592     4012   4334   2666   -288   -219    749       O  
ATOM   4869  CB  MET A 592      -3.000   2.721 -59.484  1.00 29.28           C  
ANISOU 4869  CB  MET A 592     4044   4204   2877   -179   -171    808       C  
ATOM   4870  CG  MET A 592      -2.807   2.836 -61.000  1.00 28.92           C  
ANISOU 4870  CG  MET A 592     3990   4248   2751   -254   -198    864       C  
ATOM   4871  SD  MET A 592      -1.495   3.957 -61.513  1.00 30.39           S  
ANISOU 4871  SD  MET A 592     4187   4419   2942   -268   -176    885       S  
ATOM   4872  CE  MET A 592      -0.049   3.158 -60.819  1.00 34.31           C  
ANISOU 4872  CE  MET A 592     4732   4876   3427   -254   -126    738       C  
ATOM   4873  N   ALA A 593      -2.651  -0.350 -59.200  1.00 26.43           N  
ANISOU 4873  N   ALA A 593     3743   3899   2399   -222   -155    611       N  
ATOM   4874  CA  ALA A 593      -2.119  -1.571 -59.810  1.00 28.51           C  
ANISOU 4874  CA  ALA A 593     4028   4215   2590   -275   -144    535       C  
ATOM   4875  C   ALA A 593      -3.183  -2.666 -59.888  1.00 29.32           C  
ANISOU 4875  C   ALA A 593     4124   4359   2658   -297   -160    521       C  
ATOM   4876  O   ALA A 593      -3.315  -3.338 -60.913  1.00 28.64           O  
ANISOU 4876  O   ALA A 593     4036   4350   2495   -366   -166    508       O  
ATOM   4877  CB  ALA A 593      -0.895  -2.070 -59.040  1.00 25.10           C  
ANISOU 4877  CB  ALA A 593     3626   3723   2187   -248   -109    439       C  
ATOM   4878  N   LEU A 594      -3.946  -2.813 -58.803  1.00 28.78           N  
ANISOU 4878  N   LEU A 594     4052   4240   2644   -243   -164    520       N  
ATOM   4879  CA  LEU A 594      -5.019  -3.800 -58.716  1.00 29.25           C  
ANISOU 4879  CA  LEU A 594     4104   4328   2683   -255   -177    508       C  
ATOM   4880  C   LEU A 594      -6.147  -3.520 -59.718  1.00 29.40           C  
ANISOU 4880  C   LEU A 594     4083   4423   2665   -299   -218    596       C  
ATOM   4881  O   LEU A 594      -6.528  -4.397 -60.499  1.00 30.65           O  
ANISOU 4881  O   LEU A 594     4238   4654   2753   -360   -230    579       O  
ATOM   4882  CB  LEU A 594      -5.577  -3.858 -57.281  1.00 27.72           C  
ANISOU 4882  CB  LEU A 594     3916   4057   2558   -189   -167    493       C  
ATOM   4883  CG  LEU A 594      -6.648  -4.922 -57.023  1.00 31.41           C  
ANISOU 4883  CG  LEU A 594     4379   4543   3014   -196   -174    472       C  
ATOM   4884  CD1 LEU A 594      -6.087  -6.312 -57.324  1.00 30.07           C  
ANISOU 4884  CD1 LEU A 594     4234   4400   2791   -235   -159    385       C  
ATOM   4885  CD2 LEU A 594      -7.179  -4.841 -55.600  1.00 28.97           C  
ANISOU 4885  CD2 LEU A 594     4080   4156   2772   -138   -158    461       C  
ATOM   4886  N   GLN A 595      -6.669  -2.298 -59.686  1.00 28.41           N  
ANISOU 4886  N   GLN A 595     3924   4279   2593   -271   -240    692       N  
ATOM   4887  CA  GLN A 595      -7.755  -1.894 -60.568  1.00 30.99           C  
ANISOU 4887  CA  GLN A 595     4202   4669   2904   -308   -289    796       C  
ATOM   4888  C   GLN A 595      -7.322  -1.778 -62.036  1.00 30.96           C  
ANISOU 4888  C   GLN A 595     4198   4759   2806   -393   -315    833       C  
ATOM   4889  O   GLN A 595      -8.109  -2.062 -62.932  1.00 33.05           O  
ANISOU 4889  O   GLN A 595     4438   5108   3012   -456   -358    885       O  
ATOM   4890  CB  GLN A 595      -8.423  -0.621 -60.046  1.00 29.26           C  
ANISOU 4890  CB  GLN A 595     3939   4387   2792   -250   -299    889       C  
ATOM   4891  CG  GLN A 595      -9.252  -0.887 -58.789  1.00 31.30           C  
ANISOU 4891  CG  GLN A 595     4190   4576   3129   -190   -277    860       C  
ATOM   4892  CD  GLN A 595      -9.576   0.370 -58.005  1.00 32.98           C  
ANISOU 4892  CD  GLN A 595     4371   4698   3461   -127   -257    914       C  
ATOM   4893  OE1 GLN A 595     -10.667   0.927 -58.125  1.00 34.66           O  
ANISOU 4893  OE1 GLN A 595     4524   4903   3742   -115   -279   1001       O  
ATOM   4894  NE2 GLN A 595      -8.625   0.824 -57.197  1.00 34.01           N  
ANISOU 4894  NE2 GLN A 595     4540   4759   3626    -89   -213    861       N  
ATOM   4895  N   TRP A 596      -6.071  -1.385 -62.269  1.00 30.46           N  
ANISOU 4895  N   TRP A 596     4164   4684   2726   -402   -288    804       N  
ATOM   4896  CA  TRP A 596      -5.486  -1.388 -63.615  1.00 29.19           C  
ANISOU 4896  CA  TRP A 596     4015   4610   2466   -492   -296    816       C  
ATOM   4897  C   TRP A 596      -5.483  -2.801 -64.208  1.00 30.41           C  
ANISOU 4897  C   TRP A 596     4192   4837   2524   -567   -283    730       C  
ATOM   4898  O   TRP A 596      -5.863  -2.996 -65.357  1.00 31.10           O  
ANISOU 4898  O   TRP A 596     4273   5022   2520   -658   -313    768       O  
ATOM   4899  CB  TRP A 596      -4.059  -0.820 -63.587  1.00 25.46           C  
ANISOU 4899  CB  TRP A 596     3571   4097   2004   -481   -255    778       C  
ATOM   4900  CG  TRP A 596      -3.299  -0.957 -64.872  1.00 25.56           C  
ANISOU 4900  CG  TRP A 596     3606   4191   1916   -577   -246    763       C  
ATOM   4901  CD1 TRP A 596      -2.739  -2.097 -65.372  1.00 27.35           C  
ANISOU 4901  CD1 TRP A 596     3862   4461   2067   -641   -208    660       C  
ATOM   4902  CD2 TRP A 596      -2.990   0.085 -65.810  1.00 24.98           C  
ANISOU 4902  CD2 TRP A 596     3525   4158   1808   -624   -265    851       C  
ATOM   4903  NE1 TRP A 596      -2.116  -1.840 -66.566  1.00 26.57           N  
ANISOU 4903  NE1 TRP A 596     3779   4433   1885   -731   -199    670       N  
ATOM   4904  CE2 TRP A 596      -2.249  -0.509 -66.862  1.00 28.53           C  
ANISOU 4904  CE2 TRP A 596     4007   4683   2150   -724   -237    790       C  
ATOM   4905  CE3 TRP A 596      -3.269   1.460 -65.868  1.00 26.36           C  
ANISOU 4905  CE3 TRP A 596     3668   4309   2037   -596   -300    975       C  
ATOM   4906  CZ2 TRP A 596      -1.781   0.227 -67.974  1.00 26.27           C  
ANISOU 4906  CZ2 TRP A 596     3728   4456   1796   -801   -245    851       C  
ATOM   4907  CZ3 TRP A 596      -2.805   2.196 -66.981  1.00 29.88           C  
ANISOU 4907  CZ3 TRP A 596     4118   4812   2423   -667   -314   1044       C  
ATOM   4908  CH2 TRP A 596      -2.065   1.570 -68.012  1.00 25.68           C  
ANISOU 4908  CH2 TRP A 596     3624   4361   1770   -771   -287    981       C  
ATOM   4909  N   ILE A 597      -5.051  -3.782 -63.420  1.00 30.15           N  
ANISOU 4909  N   ILE A 597     4187   4755   2515   -534   -238    617       N  
ATOM   4910  CA  ILE A 597      -4.952  -5.144 -63.922  1.00 30.60           C  
ANISOU 4910  CA  ILE A 597     4264   4864   2498   -601   -213    525       C  
ATOM   4911  C   ILE A 597      -6.304  -5.867 -64.010  1.00 33.31           C  
ANISOU 4911  C   ILE A 597     4586   5256   2816   -625   -246    544       C  
ATOM   4912  O   ILE A 597      -6.442  -6.826 -64.770  1.00 33.88           O  
ANISOU 4912  O   ILE A 597     4668   5399   2808   -707   -236    492       O  
ATOM   4913  CB  ILE A 597      -3.877  -5.963 -63.160  1.00 29.36           C  
ANISOU 4913  CB  ILE A 597     4138   4635   2384   -564   -152    402       C  
ATOM   4914  CG1 ILE A 597      -3.145  -6.899 -64.124  1.00 25.04           C  
ANISOU 4914  CG1 ILE A 597     3610   4140   1762   -654   -107    311       C  
ATOM   4915  CG2 ILE A 597      -4.452  -6.678 -61.925  1.00 27.39           C  
ANISOU 4915  CG2 ILE A 597     3888   4320   2197   -496   -150    365       C  
ATOM   4916  CD1 ILE A 597      -2.407  -6.176 -65.217  1.00 22.76           C  
ANISOU 4916  CD1 ILE A 597     3329   3904   1413   -722    -97    335       C  
ATOM   4917  N   GLU A 598      -7.286  -5.400 -63.235  1.00 34.37           N  
ANISOU 4917  N   GLU A 598     4690   5348   3021   -558   -280    611       N  
ATOM   4918  CA  GLU A 598      -8.662  -5.879 -63.330  1.00 33.76           C  
ANISOU 4918  CA  GLU A 598     4582   5314   2932   -578   -318    648       C  
ATOM   4919  C   GLU A 598      -9.191  -5.513 -64.708  1.00 35.62           C  
ANISOU 4919  C   GLU A 598     4791   5661   3082   -672   -373    739       C  
ATOM   4920  O   GLU A 598      -9.726  -6.367 -65.419  1.00 35.21           O  
ANISOU 4920  O   GLU A 598     4737   5692   2949   -753   -388    719       O  
ATOM   4921  CB  GLU A 598      -9.537  -5.252 -62.233  1.00 35.08           C  
ANISOU 4921  CB  GLU A 598     4717   5406   3208   -487   -335    708       C  
ATOM   4922  CG  GLU A 598     -11.024  -5.636 -62.285  1.00 36.01           C  
ANISOU 4922  CG  GLU A 598     4792   5560   3331   -500   -375    755       C  
ATOM   4923  CD  GLU A 598     -11.904  -4.865 -61.294  1.00 39.83           C  
ANISOU 4923  CD  GLU A 598     5235   5966   3934   -416   -385    821       C  
ATOM   4924  OE1 GLU A 598     -11.456  -3.847 -60.714  1.00 39.55           O  
ANISOU 4924  OE1 GLU A 598     5199   5857   3972   -356   -368    848       O  
ATOM   4925  OE2 GLU A 598     -13.066  -5.284 -61.097  1.00 41.99           O  
ANISOU 4925  OE2 GLU A 598     5475   6249   4230   -414   -405    840       O  
ATOM   4926  N   ARG A 599      -9.019  -4.245 -65.084  1.00 35.47           N  
ANISOU 4926  N   ARG A 599     4753   5645   3080   -668   -404    840       N  
ATOM   4927  CA  ARG A 599      -9.414  -3.768 -66.407  1.00 37.40           C  
ANISOU 4927  CA  ARG A 599     4973   5994   3241   -762   -464    943       C  
ATOM   4928  C   ARG A 599      -8.766  -4.592 -67.528  1.00 38.28           C  
ANISOU 4928  C   ARG A 599     5128   6203   3214   -883   -441    868       C  
ATOM   4929  O   ARG A 599      -9.451  -5.008 -68.462  1.00 40.68           O  
ANISOU 4929  O   ARG A 599     5420   6612   3424   -982   -482    901       O  
ATOM   4930  CB  ARG A 599      -9.107  -2.273 -66.572  1.00 36.69           C  
ANISOU 4930  CB  ARG A 599     4862   5878   3202   -734   -491   1056       C  
ATOM   4931  CG  ARG A 599      -9.469  -1.744 -67.954  1.00 39.77           C  
ANISOU 4931  CG  ARG A 599     5229   6379   3504   -838   -561   1177       C  
ATOM   4932  CD  ARG A 599      -9.343  -0.230 -68.069  1.00 39.09           C  
ANISOU 4932  CD  ARG A 599     5110   6256   3486   -804   -594   1308       C  
ATOM   4933  NE  ARG A 599      -7.984   0.257 -67.839  1.00 38.10           N  
ANISOU 4933  NE  ARG A 599     5027   6073   3376   -773   -533   1251       N  
ATOM   4934  CZ  ARG A 599      -6.989   0.196 -68.720  1.00 37.82           C  
ANISOU 4934  CZ  ARG A 599     5035   6096   3237   -855   -510   1216       C  
ATOM   4935  NH1 ARG A 599      -7.172  -0.352 -69.913  1.00 37.40           N  
ANISOU 4935  NH1 ARG A 599     4998   6167   3047   -982   -538   1225       N  
ATOM   4936  NH2 ARG A 599      -5.799   0.684 -68.397  1.00 39.03           N  
ANISOU 4936  NH2 ARG A 599     5219   6185   3425   -816   -454   1166       N  
ATOM   4937  N   LYS A 600      -7.460  -4.843 -67.410  1.00 37.02           N  
ANISOU 4937  N   LYS A 600     5015   6007   3046   -879   -371    764       N  
ATOM   4938  CA  LYS A 600      -6.708  -5.593 -68.422  1.00 36.12           C  
ANISOU 4938  CA  LYS A 600     4940   5968   2816   -992   -328    677       C  
ATOM   4939  C   LYS A 600      -7.148  -7.049 -68.547  1.00 35.16           C  
ANISOU 4939  C   LYS A 600     4830   5887   2644  -1046   -302    577       C  
ATOM   4940  O   LYS A 600      -7.310  -7.559 -69.653  1.00 35.85           O  
ANISOU 4940  O   LYS A 600     4929   6079   2613  -1170   -304    560       O  
ATOM   4941  CB  LYS A 600      -5.195  -5.516 -68.158  1.00 35.21           C  
ANISOU 4941  CB  LYS A 600     4861   5785   2730   -963   -253    586       C  
ATOM   4942  CG  LYS A 600      -4.583  -4.136 -68.356  1.00 35.55           C  
ANISOU 4942  CG  LYS A 600     4902   5811   2795   -944   -269    670       C  
ATOM   4943  CD  LYS A 600      -4.438  -3.783 -69.833  1.00 40.56           C  
ANISOU 4943  CD  LYS A 600     5549   6560   3303  -1075   -288    723       C  
ATOM   4944  CE  LYS A 600      -3.714  -2.458 -70.015  1.00 40.63           C  
ANISOU 4944  CE  LYS A 600     5558   6542   3336  -1057   -295    799       C  
ATOM   4945  NZ  LYS A 600      -3.322  -2.247 -71.439  1.00 41.84           N  
ANISOU 4945  NZ  LYS A 600     5737   6804   3358  -1195   -296    825       N  
ATOM   4946  N   VAL A 601      -7.332  -7.714 -67.411  1.00 35.12           N  
ANISOU 4946  N   VAL A 601     4822   5797   2724   -958   -274    512       N  
ATOM   4947  CA  VAL A 601      -7.730  -9.117 -67.396  1.00 34.40           C  
ANISOU 4947  CA  VAL A 601     4739   5727   2603   -997   -244    415       C  
ATOM   4948  C   VAL A 601      -9.126  -9.269 -67.998  1.00 36.80           C  
ANISOU 4948  C   VAL A 601     5013   6127   2845  -1063   -311    490       C  
ATOM   4949  O   VAL A 601      -9.360 -10.170 -68.811  1.00 37.33           O  
ANISOU 4949  O   VAL A 601     5091   6277   2816  -1171   -297    433       O  
ATOM   4950  CB  VAL A 601      -7.642  -9.724 -65.972  1.00 32.98           C  
ANISOU 4950  CB  VAL A 601     4563   5432   2535   -885   -207    344       C  
ATOM   4951  CG1 VAL A 601      -8.390 -11.044 -65.887  1.00 30.52           C  
ANISOU 4951  CG1 VAL A 601     4250   5141   2206   -916   -192    275       C  
ATOM   4952  CG2 VAL A 601      -6.181  -9.926 -65.581  1.00 32.87           C  
ANISOU 4952  CG2 VAL A 601     4581   5343   2567   -851   -137    248       C  
ATOM   4953  N   ASN A 602     -10.037  -8.375 -67.613  1.00 37.76           N  
ANISOU 4953  N   ASN A 602     5090   6233   3023  -1003   -381    615       N  
ATOM   4954  CA  ASN A 602     -11.374  -8.336 -68.202  1.00 39.44           C  
ANISOU 4954  CA  ASN A 602     5260   6533   3191  -1062   -459    711       C  
ATOM   4955  C   ASN A 602     -11.319  -8.126 -69.707  1.00 42.13           C  
ANISOU 4955  C   ASN A 602     5608   7007   3393  -1206   -497    761       C  
ATOM   4956  O   ASN A 602     -11.905  -8.904 -70.462  1.00 47.01           O  
ANISOU 4956  O   ASN A 602     6226   7722   3913  -1313   -514    741       O  
ATOM   4957  CB  ASN A 602     -12.254  -7.273 -67.531  1.00 37.65           C  
ANISOU 4957  CB  ASN A 602     4977   6254   3075   -968   -521    843       C  
ATOM   4958  CG  ASN A 602     -12.880  -7.763 -66.232  1.00 35.70           C  
ANISOU 4958  CG  ASN A 602     4715   5915   2933   -868   -499    800       C  
ATOM   4959  OD1 ASN A 602     -13.015  -8.972 -66.009  1.00 33.58           O  
ANISOU 4959  OD1 ASN A 602     4467   5649   2641   -885   -461    698       O  
ATOM   4960  ND2 ASN A 602     -13.278  -6.825 -65.374  1.00 25.55           N  
ANISOU 4960  ND2 ASN A 602     3395   4548   1767   -767   -517    877       N  
ATOM   4961  N   GLU A 603     -10.592  -7.094 -70.136  1.00 42.72           N  
ANISOU 4961  N   GLU A 603     5692   7085   3454  -1215   -507    824       N  
ATOM   4962  CA  GLU A 603     -10.430  -6.785 -71.562  1.00 42.82           C  
ANISOU 4962  CA  GLU A 603     5718   7222   3328  -1357   -542    880       C  
ATOM   4963  C   GLU A 603      -9.860  -7.971 -72.334  1.00 42.48           C  
ANISOU 4963  C   GLU A 603     5728   7252   3161  -1481   -472    737       C  
ATOM   4964  O   GLU A 603     -10.328  -8.280 -73.427  1.00 45.35           O  
ANISOU 4964  O   GLU A 603     6096   7741   3393  -1622   -507    760       O  
ATOM   4965  CB  GLU A 603      -9.538  -5.552 -71.767  1.00 42.64           C  
ANISOU 4965  CB  GLU A 603     5705   7173   3322  -1336   -543    947       C  
ATOM   4966  CG  GLU A 603     -10.177  -4.215 -71.387  1.00 44.14           C  
ANISOU 4966  CG  GLU A 603     5838   7320   3615  -1252   -622   1115       C  
ATOM   4967  CD  GLU A 603      -9.241  -3.012 -71.593  1.00 46.69           C  
ANISOU 4967  CD  GLU A 603     6172   7611   3957  -1234   -616   1176       C  
ATOM   4968  OE1 GLU A 603      -8.058  -3.204 -71.956  1.00 42.67           O  
ANISOU 4968  OE1 GLU A 603     5717   7110   3387  -1279   -549   1084       O  
ATOM   4969  OE2 GLU A 603      -9.696  -1.864 -71.396  1.00 47.60           O  
ANISOU 4969  OE2 GLU A 603     6238   7690   4157  -1176   -676   1316       O  
ATOM   4970  N   TYR A 604      -8.854  -8.632 -71.762  1.00 41.15           N  
ANISOU 4970  N   TYR A 604     5597   7002   3038  -1434   -372    591       N  
ATOM   4971  CA  TYR A 604      -8.245  -9.803 -72.391  1.00 40.25           C  
ANISOU 4971  CA  TYR A 604     5526   6932   2836  -1542   -287    440       C  
ATOM   4972  C   TYR A 604      -9.240 -10.960 -72.525  1.00 41.96           C  
ANISOU 4972  C   TYR A 604     5732   7203   3007  -1601   -293    390       C  
ATOM   4973  O   TYR A 604      -9.407 -11.513 -73.613  1.00 43.50           O  
ANISOU 4973  O   TYR A 604     5947   7511   3069  -1752   -284    353       O  
ATOM   4974  CB  TYR A 604      -6.994 -10.258 -71.630  1.00 40.00           C  
ANISOU 4974  CB  TYR A 604     5521   6783   2894  -1463   -184    305       C  
ATOM   4975  CG  TYR A 604      -6.376 -11.535 -72.167  1.00 40.59           C  
ANISOU 4975  CG  TYR A 604     5630   6881   2912  -1561    -84    141       C  
ATOM   4976  CD1 TYR A 604      -6.529 -12.751 -71.488  1.00 40.01           C  
ANISOU 4976  CD1 TYR A 604     5553   6747   2902  -1521    -32     31       C  
ATOM   4977  CD2 TYR A 604      -5.646 -11.531 -73.358  1.00 40.98           C  
ANISOU 4977  CD2 TYR A 604     5713   7009   2847  -1698    -36     93       C  
ATOM   4978  CE1 TYR A 604      -5.966 -13.931 -71.984  1.00 39.99           C  
ANISOU 4978  CE1 TYR A 604     5575   6755   2864  -1611     68   -122       C  
ATOM   4979  CE2 TYR A 604      -5.082 -12.703 -73.865  1.00 42.15           C  
ANISOU 4979  CE2 TYR A 604     5891   7172   2954  -1794     69    -67       C  
ATOM   4980  CZ  TYR A 604      -5.246 -13.896 -73.175  1.00 44.13           C  
ANISOU 4980  CZ  TYR A 604     6131   7355   3282  -1747    121   -174       C  
ATOM   4981  OH  TYR A 604      -4.684 -15.047 -73.681  1.00 45.61           O  
ANISOU 4981  OH  TYR A 604     6339   7546   3443  -1841    232   -333       O  
ATOM   4982  N   LEU A 605      -9.902 -11.320 -71.426  1.00 40.29           N  
ANISOU 4982  N   LEU A 605     5493   6913   2903  -1489   -304    386       N  
ATOM   4983  CA  LEU A 605     -10.793 -12.477 -71.433  1.00 41.03           C  
ANISOU 4983  CA  LEU A 605     5577   7043   2971  -1534   -299    327       C  
ATOM   4984  C   LEU A 605     -12.053 -12.284 -72.301  1.00 43.36           C  
ANISOU 4984  C   LEU A 605     5839   7468   3166  -1636   -397    437       C  
ATOM   4985  O   LEU A 605     -12.542 -13.239 -72.904  1.00 42.65           O  
ANISOU 4985  O   LEU A 605     5757   7459   2989  -1746   -385    375       O  
ATOM   4986  CB  LEU A 605     -11.134 -12.924 -70.005  1.00 37.71           C  
ANISOU 4986  CB  LEU A 605     5137   6501   2688  -1391   -282    293       C  
ATOM   4987  CG  LEU A 605     -10.035 -13.687 -69.248  1.00 35.22           C  
ANISOU 4987  CG  LEU A 605     4854   6076   2451  -1327   -179    151       C  
ATOM   4988  CD1 LEU A 605     -10.473 -14.007 -67.833  1.00 34.91           C  
ANISOU 4988  CD1 LEU A 605     4797   5928   2538  -1195   -178    143       C  
ATOM   4989  CD2 LEU A 605      -9.605 -14.970 -69.950  1.00 35.29           C  
ANISOU 4989  CD2 LEU A 605     4893   6126   2392  -1440    -94      6       C  
ATOM   4990  N   ASN A 606     -12.558 -11.052 -72.362  1.00 45.22           N  
ANISOU 4990  N   ASN A 606     6037   7721   3424  -1603   -492    602       N  
ATOM   4991  CA  ASN A 606     -13.653 -10.699 -73.263  1.00 50.24           C  
ANISOU 4991  CA  ASN A 606     6636   8482   3972  -1704   -598    732       C  
ATOM   4992  C   ASN A 606     -13.271 -10.895 -74.726  1.00 54.87           C  
ANISOU 4992  C   ASN A 606     7263   9209   4376  -1893   -595    711       C  
ATOM   4993  O   ASN A 606     -14.116 -11.224 -75.560  1.00 55.78           O  
ANISOU 4993  O   ASN A 606     7366   9447   4383  -2019   -655    752       O  
ATOM   4994  CB  ASN A 606     -14.088  -9.250 -73.037  1.00 50.42           C  
ANISOU 4994  CB  ASN A 606     6605   8478   4074  -1626   -692    915       C  
ATOM   4995  CG  ASN A 606     -15.164  -9.122 -71.977  1.00 50.29           C  
ANISOU 4995  CG  ASN A 606     6527   8384   4198  -1502   -734    976       C  
ATOM   4996  OD1 ASN A 606     -16.301  -9.544 -72.186  1.00 47.95           O  
ANISOU 4996  OD1 ASN A 606     6190   8147   3881  -1547   -791   1016       O  
ATOM   4997  ND2 ASN A 606     -14.815  -8.522 -70.836  1.00 46.72           N  
ANISOU 4997  ND2 ASN A 606     6065   7797   3889  -1351   -704    981       N  
ATOM   4998  N   GLU A 607     -11.989 -10.684 -75.015  1.00 58.91           N  
ANISOU 4998  N   GLU A 607     7825   9702   4857  -1914   -523    646       N  
ATOM   4999  CA  GLU A 607     -11.410 -10.876 -76.340  1.00 63.51           C  
ANISOU 4999  CA  GLU A 607     8458  10403   5271  -2093   -493    601       C  
ATOM   5000  C   GLU A 607     -11.238 -12.366 -76.649  1.00 64.86           C  
ANISOU 5000  C   GLU A 607     8667  10605   5373  -2191   -395    417       C  
ATOM   5001  O   GLU A 607     -11.505 -12.805 -77.768  1.00 68.02           O  
ANISOU 5001  O   GLU A 607     9089  11138   5615  -2368   -401    395       O  
ATOM   5002  CB  GLU A 607     -10.075 -10.122 -76.419  1.00 64.79           C  
ANISOU 5002  CB  GLU A 607     8655  10516   5448  -2068   -440    588       C  
ATOM   5003  CG  GLU A 607      -9.115 -10.515 -77.543  1.00 70.62           C  
ANISOU 5003  CG  GLU A 607     9457  11335   6042  -2231   -357    481       C  
ATOM   5004  CD  GLU A 607      -7.665 -10.145 -77.221  1.00 75.14           C  
ANISOU 5004  CD  GLU A 607    10059  11808   6682  -2164   -266    408       C  
ATOM   5005  OE1 GLU A 607      -6.758 -10.924 -77.588  1.00 78.04           O  
ANISOU 5005  OE1 GLU A 607    10470  12172   7009  -2238   -149    249       O  
ATOM   5006  OE2 GLU A 607      -7.427  -9.086 -76.591  1.00 74.74           O  
ANISOU 5006  OE2 GLU A 607     9986  11678   6732  -2039   -305    505       O  
ATOM   5007  N   VAL A 608     -10.799 -13.134 -75.655  1.00 65.38           N  
ANISOU 5007  N   VAL A 608     8737  10547   5556  -2082   -304    287       N  
ATOM   5008  CA  VAL A 608     -10.635 -14.587 -75.790  1.00 67.34           C  
ANISOU 5008  CA  VAL A 608     9013  10799   5776  -2153   -202    110       C  
ATOM   5009  C   VAL A 608     -11.968 -15.302 -76.063  1.00 69.07           C  
ANISOU 5009  C   VAL A 608     9207  11104   5933  -2229   -255    124       C  
ATOM   5010  O   VAL A 608     -12.031 -16.206 -76.901  1.00 69.49           O  
ANISOU 5010  O   VAL A 608     9288  11244   5870  -2382   -205     22       O  
ATOM   5011  CB  VAL A 608      -9.961 -15.197 -74.530  1.00 66.03           C  
ANISOU 5011  CB  VAL A 608     8846  10468   5773  -2001   -111     -5       C  
ATOM   5012  CG1 VAL A 608      -9.980 -16.719 -74.571  1.00 66.27           C  
ANISOU 5012  CG1 VAL A 608     8891  10490   5798  -2061    -15   -172       C  
ATOM   5013  CG2 VAL A 608      -8.536 -14.701 -74.397  1.00 66.08           C  
ANISOU 5013  CG2 VAL A 608     8878  10399   5828  -1954    -44    -48       C  
ATOM   5014  N   CYS A 609     -13.022 -14.878 -75.363  1.00 69.45           N  
ANISOU 5014  N   CYS A 609     9202  11126   6061  -2126   -352    246       N  
ATOM   5015  CA  CYS A 609     -14.329 -15.545 -75.408  1.00 70.15           C  
ANISOU 5015  CA  CYS A 609     9257  11275   6123  -2170   -404    262       C  
ATOM   5016  C   CYS A 609     -15.305 -14.936 -76.420  1.00 71.58           C  
ANISOU 5016  C   CYS A 609     9409  11608   6181  -2294   -532    414       C  
ATOM   5017  O   CYS A 609     -16.301 -15.563 -76.782  1.00 72.06           O  
ANISOU 5017  O   CYS A 609     9449  11751   6180  -2380   -572    416       O  
ATOM   5018  CB  CYS A 609     -14.959 -15.562 -74.010  1.00 69.67           C  
ANISOU 5018  CB  CYS A 609     9150  11091   6230  -1991   -426    294       C  
ATOM   5019  SG  CYS A 609     -13.929 -16.346 -72.739  1.00 66.59           S  
ANISOU 5019  SG  CYS A 609     8789  10526   5985  -1850   -293    132       S  
ATOM   5020  N   GLY A 610     -15.018 -13.713 -76.859  1.00 71.81           N  
ANISOU 5020  N   GLY A 610     9434  11671   6180  -2303   -598    546       N  
ATOM   5021  CA  GLY A 610     -15.801 -13.047 -77.897  1.00 73.14           C  
ANISOU 5021  CA  GLY A 610     9577  11985   6228  -2430   -725    705       C  
ATOM   5022  C   GLY A 610     -16.974 -12.211 -77.412  1.00 73.82           C  
ANISOU 5022  C   GLY A 610     9578  12053   6416  -2333   -857    894       C  
ATOM   5023  O   GLY A 610     -17.963 -12.053 -78.137  1.00 74.17           O  
ANISOU 5023  O   GLY A 610     9585  12217   6381  -2438   -968   1011       O  
ATOM   5024  N   THR A 611     -16.865 -11.666 -76.199  1.00 72.51           N  
ANISOU 5024  N   THR A 611     9382  11739   6429  -2141   -846    923       N  
ATOM   5025  CA  THR A 611     -17.935 -10.848 -75.612  1.00 72.58           C  
ANISOU 5025  CA  THR A 611     9306  11706   6564  -2034   -951   1089       C  
ATOM   5026  C   THR A 611     -17.545  -9.377 -75.431  1.00 72.99           C  
ANISOU 5026  C   THR A 611     9334  11700   6698  -1947   -997   1229       C  
ATOM   5027  O   THR A 611     -16.466  -8.952 -75.856  1.00 71.75           O  
ANISOU 5027  O   THR A 611     9228  11551   6484  -1980   -958   1209       O  
ATOM   5028  CB  THR A 611     -18.431 -11.428 -74.270  1.00 71.64           C  
ANISOU 5028  CB  THR A 611     9159  11463   6599  -1886   -906   1018       C  
ATOM   5029  OG1 THR A 611     -17.310 -11.834 -73.474  1.00 71.74           O  
ANISOU 5029  OG1 THR A 611     9228  11360   6671  -1796   -782    869       O  
ATOM   5030  CG2 THR A 611     -19.341 -12.627 -74.507  1.00 72.82           C  
ANISOU 5030  CG2 THR A 611     9297  11684   6687  -1973   -910    951       C  
ATOM   5031  N   GLU A 612     -18.443  -8.608 -74.811  1.00 73.95           N  
ANISOU 5031  N   GLU A 612     9375  11763   6960  -1839  -1075   1368       N  
ATOM   5032  CA  GLU A 612     -18.213  -7.191 -74.514  1.00 74.79           C  
ANISOU 5032  CA  GLU A 612     9447  11797   7175  -1742  -1115   1505       C  
ATOM   5033  C   GLU A 612     -18.888  -6.807 -73.195  1.00 72.59           C  
ANISOU 5033  C   GLU A 612     9101  11378   7101  -1568  -1116   1544       C  
ATOM   5034  O   GLU A 612     -20.074  -7.079 -72.992  1.00 73.11           O  
ANISOU 5034  O   GLU A 612     9103  11455   7219  -1559  -1170   1593       O  
ATOM   5035  CB  GLU A 612     -18.728  -6.302 -75.657  1.00 77.69           C  
ANISOU 5035  CB  GLU A 612     9768  12281   7469  -1852  -1247   1701       C  
ATOM   5036  CG  GLU A 612     -18.484  -4.798 -75.466  1.00 81.66           C  
ANISOU 5036  CG  GLU A 612    10231  12712   8086  -1764  -1290   1854       C  
ATOM   5037  CD  GLU A 612     -19.201  -3.931 -76.505  1.00 87.99           C  
ANISOU 5037  CD  GLU A 612    10969  13618   8844  -1862  -1436   2074       C  
ATOM   5038  OE1 GLU A 612     -19.149  -4.256 -77.715  1.00 89.45           O  
ANISOU 5038  OE1 GLU A 612    11190  13957   8841  -2039  -1483   2093       O  
ATOM   5039  OE2 GLU A 612     -19.809  -2.911 -76.110  1.00 89.57           O  
ANISOU 5039  OE2 GLU A 612    11083  13747   9202  -1767  -1503   2230       O  
ATOM   5040  N   GLY A 613     -18.122  -6.183 -72.303  1.00 69.38           N  
ANISOU 5040  N   GLY A 613     8710  10842   6808  -1437  -1053   1517       N  
ATOM   5041  CA  GLY A 613     -18.655  -5.684 -71.037  1.00 66.34           C  
ANISOU 5041  CA  GLY A 613     8270  10320   6616  -1279  -1043   1551       C  
ATOM   5042  C   GLY A 613     -18.830  -6.709 -69.925  1.00 63.09           C  
ANISOU 5042  C   GLY A 613     7877   9827   6265  -1200   -961   1405       C  
ATOM   5043  O   GLY A 613     -19.251  -6.356 -68.819  1.00 62.96           O  
ANISOU 5043  O   GLY A 613     7823   9697   6402  -1075   -941   1419       O  
ATOM   5044  N   GLU A 614     -18.511  -7.972 -70.206  1.00 59.65           N  
ANISOU 5044  N   GLU A 614     7501   9447   5715  -1276   -909   1265       N  
ATOM   5045  CA  GLU A 614     -18.608  -9.025 -69.193  1.00 57.78           C  
ANISOU 5045  CA  GLU A 614     7288   9136   5532  -1209   -830   1125       C  
ATOM   5046  C   GLU A 614     -17.498  -8.955 -68.144  1.00 53.53           C  
ANISOU 5046  C   GLU A 614     6802   8470   5067  -1098   -735   1024       C  
ATOM   5047  O   GLU A 614     -16.318  -8.798 -68.472  1.00 51.68           O  
ANISOU 5047  O   GLU A 614     6620   8238   4778  -1120   -694    977       O  
ATOM   5048  CB  GLU A 614     -18.655 -10.410 -69.834  1.00 59.13           C  
ANISOU 5048  CB  GLU A 614     7499   9400   5570  -1328   -803   1009       C  
ATOM   5049  CG  GLU A 614     -20.019 -10.744 -70.434  1.00 66.53           C  
ANISOU 5049  CG  GLU A 614     8376  10437   6466  -1412   -888   1083       C  
ATOM   5050  CD  GLU A 614     -20.495 -12.149 -70.087  1.00 71.07           C  
ANISOU 5050  CD  GLU A 614     8965  11012   7025  -1431   -837    955       C  
ATOM   5051  OE1 GLU A 614     -21.184 -12.763 -70.933  1.00 75.91           O  
ANISOU 5051  OE1 GLU A 614     9564  11742   7538  -1555   -882    960       O  
ATOM   5052  OE2 GLU A 614     -20.187 -12.636 -68.971  1.00 70.58           O  
ANISOU 5052  OE2 GLU A 614     8930  10837   7050  -1328   -755    852       O  
ATOM   5053  N   ALA A 615     -17.895  -9.063 -66.881  1.00 49.34           N  
ANISOU 5053  N   ALA A 615     6255   7830   4663   -983   -700    994       N  
ATOM   5054  CA  ALA A 615     -16.955  -9.006 -65.772  1.00 47.28           C  
ANISOU 5054  CA  ALA A 615     6039   7448   4476   -878   -619    907       C  
ATOM   5055  C   ALA A 615     -16.463 -10.403 -65.415  1.00 44.87           C  
ANISOU 5055  C   ALA A 615     5793   7127   4130   -891   -542    747       C  
ATOM   5056  O   ALA A 615     -17.212 -11.215 -64.881  1.00 46.99           O  
ANISOU 5056  O   ALA A 615     6050   7375   4427   -874   -528    702       O  
ATOM   5057  CB  ALA A 615     -17.594  -8.331 -64.563  1.00 46.07           C  
ANISOU 5057  CB  ALA A 615     5844   7184   4477   -757   -617    959       C  
ATOM   5058  N   PHE A 616     -15.202 -10.679 -65.729  1.00 42.08           N  
ANISOU 5058  N   PHE A 616     5496   6776   3715   -922   -489    663       N  
ATOM   5059  CA  PHE A 616     -14.577 -11.944 -65.366  1.00 37.92           C  
ANISOU 5059  CA  PHE A 616     5019   6216   3171   -926   -410    514       C  
ATOM   5060  C   PHE A 616     -13.982 -11.878 -63.963  1.00 34.17           C  
ANISOU 5060  C   PHE A 616     4569   5608   2806   -803   -358    464       C  
ATOM   5061  O   PHE A 616     -14.028 -12.862 -63.229  1.00 32.39           O  
ANISOU 5061  O   PHE A 616     4363   5331   2613   -773   -313    377       O  
ATOM   5062  CB  PHE A 616     -13.492 -12.328 -66.372  1.00 37.64           C  
ANISOU 5062  CB  PHE A 616     5028   6242   3031  -1022   -371    441       C  
ATOM   5063  CG  PHE A 616     -14.023 -12.839 -67.680  1.00 39.00           C  
ANISOU 5063  CG  PHE A 616     5194   6549   3076  -1166   -400    443       C  
ATOM   5064  CD1 PHE A 616     -14.186 -14.208 -67.893  1.00 39.16           C  
ANISOU 5064  CD1 PHE A 616     5233   6599   3048  -1233   -352    328       C  
ATOM   5065  CD2 PHE A 616     -14.343 -11.958 -68.709  1.00 38.36           C  
ANISOU 5065  CD2 PHE A 616     5089   6565   2920  -1242   -475    561       C  
ATOM   5066  CE1 PHE A 616     -14.666 -14.692 -69.118  1.00 39.66           C  
ANISOU 5066  CE1 PHE A 616     5294   6792   2983  -1380   -374    322       C  
ATOM   5067  CE2 PHE A 616     -14.824 -12.433 -69.931  1.00 41.09           C  
ANISOU 5067  CE2 PHE A 616     5433   7045   3134  -1390   -507    565       C  
ATOM   5068  CZ  PHE A 616     -14.985 -13.803 -70.132  1.00 38.10           C  
ANISOU 5068  CZ  PHE A 616     5075   6699   2701  -1461   -454    441       C  
ATOM   5069  N   VAL A 617     -13.413 -10.728 -63.606  1.00 31.74           N  
ANISOU 5069  N   VAL A 617     4260   5246   2551   -739   -365    521       N  
ATOM   5070  CA  VAL A 617     -12.903 -10.509 -62.252  1.00 32.13           C  
ANISOU 5070  CA  VAL A 617     4331   5175   2701   -630   -325    488       C  
ATOM   5071  C   VAL A 617     -14.097 -10.278 -61.329  1.00 30.91           C  
ANISOU 5071  C   VAL A 617     4140   4971   2632   -563   -345    539       C  
ATOM   5072  O   VAL A 617     -14.846  -9.319 -61.509  1.00 33.22           O  
ANISOU 5072  O   VAL A 617     4384   5277   2961   -552   -393    646       O  
ATOM   5073  CB  VAL A 617     -11.929  -9.305 -62.175  1.00 32.19           C  
ANISOU 5073  CB  VAL A 617     4349   5143   2738   -589   -323    530       C  
ATOM   5074  CG1 VAL A 617     -11.324  -9.184 -60.767  1.00 30.10           C  
ANISOU 5074  CG1 VAL A 617     4112   4760   2564   -490   -279    483       C  
ATOM   5075  CG2 VAL A 617     -10.825  -9.438 -63.204  1.00 30.07           C  
ANISOU 5075  CG2 VAL A 617     4110   4930   2384   -664   -303    488       C  
ATOM   5076  N   LEU A 618     -14.291 -11.178 -60.371  1.00 28.69           N  
ANISOU 5076  N   LEU A 618     3880   4632   2389   -525   -305    463       N  
ATOM   5077  CA  LEU A 618     -15.433 -11.094 -59.451  1.00 28.55           C  
ANISOU 5077  CA  LEU A 618     3832   4565   2450   -470   -312    495       C  
ATOM   5078  C   LEU A 618     -15.060 -10.391 -58.152  1.00 28.35           C  
ANISOU 5078  C   LEU A 618     3826   4431   2516   -377   -281    495       C  
ATOM   5079  O   LEU A 618     -15.913  -9.850 -57.447  1.00 29.08           O  
ANISOU 5079  O   LEU A 618     3887   4475   2686   -329   -283    541       O  
ATOM   5080  CB  LEU A 618     -15.988 -12.493 -59.155  1.00 27.30           C  
ANISOU 5080  CB  LEU A 618     3686   4410   2276   -491   -286    416       C  
ATOM   5081  CG  LEU A 618     -15.078 -13.493 -58.429  1.00 28.70           C  
ANISOU 5081  CG  LEU A 618     3922   4527   2456   -469   -227    305       C  
ATOM   5082  CD1 LEU A 618     -15.582 -13.747 -57.023  1.00 28.92           C  
ANISOU 5082  CD1 LEU A 618     3962   4468   2559   -401   -201    285       C  
ATOM   5083  CD2 LEU A 618     -15.006 -14.812 -59.193  1.00 31.56           C  
ANISOU 5083  CD2 LEU A 618     4296   4948   2746   -548   -208    227       C  
ATOM   5084  N   TYR A 619     -13.772 -10.416 -57.837  1.00 28.63           N  
ANISOU 5084  N   TYR A 619     3909   4424   2543   -357   -248    439       N  
ATOM   5085  CA  TYR A 619     -13.296  -9.940 -56.559  1.00 25.95           C  
ANISOU 5085  CA  TYR A 619     3599   3987   2275   -282   -216    423       C  
ATOM   5086  C   TYR A 619     -11.827  -9.625 -56.612  1.00 25.13           C  
ANISOU 5086  C   TYR A 619     3531   3861   2155   -274   -200    393       C  
ATOM   5087  O   TYR A 619     -11.087 -10.150 -57.449  1.00 24.88           O  
ANISOU 5087  O   TYR A 619     3514   3878   2063   -324   -197    353       O  
ATOM   5088  CB  TYR A 619     -13.529 -11.009 -55.485  1.00 25.85           C  
ANISOU 5088  CB  TYR A 619     3618   3921   2282   -259   -182    350       C  
ATOM   5089  CG  TYR A 619     -13.169 -10.565 -54.081  1.00 22.60           C  
ANISOU 5089  CG  TYR A 619     3240   3414   1934   -195   -152    335       C  
ATOM   5090  CD1 TYR A 619     -12.138 -11.184 -53.370  1.00 19.17           C  
ANISOU 5090  CD1 TYR A 619     2859   2932   1495   -180   -127    267       C  
ATOM   5091  CD2 TYR A 619     -13.866  -9.525 -53.466  1.00 22.49           C  
ANISOU 5091  CD2 TYR A 619     3202   3357   1987   -155   -148    390       C  
ATOM   5092  CE1 TYR A 619     -11.812 -10.775 -52.067  1.00 19.91           C  
ANISOU 5092  CE1 TYR A 619     2986   2945   1633   -134   -105    256       C  
ATOM   5093  CE2 TYR A 619     -13.550  -9.110 -52.177  1.00 22.09           C  
ANISOU 5093  CE2 TYR A 619     3187   3223   1985   -110   -114    368       C  
ATOM   5094  CZ  TYR A 619     -12.529  -9.733 -51.488  1.00 20.23           C  
ANISOU 5094  CZ  TYR A 619     3008   2950   1727   -103    -96    303       C  
ATOM   5095  OH  TYR A 619     -12.254  -9.308 -50.214  1.00 23.92           O  
ANISOU 5095  OH  TYR A 619     3514   3344   2232    -71    -69    286       O  
ATOM   5096  N   GLY A 620     -11.410  -8.783 -55.678  1.00 24.57           N  
ANISOU 5096  N   GLY A 620     3476   3716   2145   -216   -184    405       N  
ATOM   5097  CA  GLY A 620     -10.010  -8.523 -55.444  1.00 24.33           C  
ANISOU 5097  CA  GLY A 620     3481   3649   2113   -200   -167    369       C  
ATOM   5098  C   GLY A 620      -9.824  -7.754 -54.157  1.00 25.48           C  
ANISOU 5098  C   GLY A 620     3646   3708   2326   -139   -147    375       C  
ATOM   5099  O   GLY A 620     -10.679  -6.948 -53.777  1.00 25.76           O  
ANISOU 5099  O   GLY A 620     3656   3719   2414   -113   -146    427       O  
ATOM   5100  N   ASP A 621      -8.696  -8.001 -53.496  1.00 25.31           N  
ANISOU 5100  N   ASP A 621     3668   3640   2309   -122   -128    320       N  
ATOM   5101  CA  ASP A 621      -8.359  -7.333 -52.252  1.00 26.56           C  
ANISOU 5101  CA  ASP A 621     3854   3722   2518    -79   -110    316       C  
ATOM   5102  C   ASP A 621      -6.868  -7.000 -52.229  1.00 26.33           C  
ANISOU 5102  C   ASP A 621     3849   3671   2486    -74   -108    292       C  
ATOM   5103  O   ASP A 621      -6.031  -7.906 -52.160  1.00 23.91           O  
ANISOU 5103  O   ASP A 621     3565   3359   2161    -85   -107    238       O  
ATOM   5104  CB  ASP A 621      -8.728  -8.233 -51.066  1.00 27.29           C  
ANISOU 5104  CB  ASP A 621     3980   3770   2620    -67    -94    270       C  
ATOM   5105  CG  ASP A 621      -8.375  -7.618 -49.715  1.00 29.40           C  
ANISOU 5105  CG  ASP A 621     4283   3964   2923    -38    -74    259       C  
ATOM   5106  OD1 ASP A 621      -7.647  -6.603 -49.662  1.00 29.16           O  
ANISOU 5106  OD1 ASP A 621     4256   3913   2911    -25    -71    275       O  
ATOM   5107  OD2 ASP A 621      -8.829  -8.171 -48.694  1.00 27.72           O  
ANISOU 5107  OD2 ASP A 621     4099   3716   2716    -34    -60    232       O  
ATOM   5108  N   THR A 622      -6.554  -5.701 -52.275  1.00 25.48           N  
ANISOU 5108  N   THR A 622     3730   3546   2406    -57   -105    333       N  
ATOM   5109  CA  THR A 622      -5.163  -5.188 -52.189  1.00 24.47           C  
ANISOU 5109  CA  THR A 622     3621   3392   2283    -50   -101    315       C  
ATOM   5110  C   THR A 622      -4.288  -5.505 -53.410  1.00 25.78           C  
ANISOU 5110  C   THR A 622     3777   3609   2408    -84   -110    301       C  
ATOM   5111  O   THR A 622      -3.900  -4.591 -54.144  1.00 27.88           O  
ANISOU 5111  O   THR A 622     4027   3896   2672    -92   -113    338       O  
ATOM   5112  CB  THR A 622      -4.452  -5.644 -50.892  1.00 23.00           C  
ANISOU 5112  CB  THR A 622     3481   3145   2112    -33    -94    261       C  
ATOM   5113  OG1 THR A 622      -5.257  -5.278 -49.761  1.00 24.10           O  
ANISOU 5113  OG1 THR A 622     3637   3240   2282    -13    -77    269       O  
ATOM   5114  CG2 THR A 622      -3.066  -5.000 -50.763  1.00 21.62           C  
ANISOU 5114  CG2 THR A 622     3319   2943   1952    -26    -93    249       C  
ATOM   5115  N   ASP A 623      -3.996  -6.787 -53.626  1.00 25.70           N  
ANISOU 5115  N   ASP A 623     3776   3617   2370   -107   -109    246       N  
ATOM   5116  CA  ASP A 623      -3.019  -7.207 -54.627  1.00 28.82           C  
ANISOU 5116  CA  ASP A 623     4165   4047   2736   -144   -102    212       C  
ATOM   5117  C   ASP A 623      -3.410  -8.476 -55.378  1.00 29.47           C  
ANISOU 5117  C   ASP A 623     4240   4180   2778   -188    -96    174       C  
ATOM   5118  O   ASP A 623      -2.630  -8.990 -56.179  1.00 27.54           O  
ANISOU 5118  O   ASP A 623     3991   3960   2514   -226    -78    130       O  
ATOM   5119  CB  ASP A 623      -1.667  -7.456 -53.954  1.00 31.08           C  
ANISOU 5119  CB  ASP A 623     4474   4276   3060   -125    -94    162       C  
ATOM   5120  CG  ASP A 623      -1.682  -8.668 -53.038  1.00 32.94           C  
ANISOU 5120  CG  ASP A 623     4727   4471   3317   -113    -95    117       C  
ATOM   5121  OD1 ASP A 623      -0.628  -9.325 -52.913  1.00 36.54           O  
ANISOU 5121  OD1 ASP A 623     5187   4897   3801   -116    -90     71       O  
ATOM   5122  OD2 ASP A 623      -2.733  -8.964 -52.434  1.00 33.83           O  
ANISOU 5122  OD2 ASP A 623     4849   4577   3426   -102   -101    129       O  
ATOM   5123  N   SER A 624      -4.599  -8.995 -55.104  1.00 28.52           N  
ANISOU 5123  N   SER A 624     4115   4071   2650   -187   -104    183       N  
ATOM   5124  CA  SER A 624      -5.011 -10.251 -55.703  1.00 30.86           C  
ANISOU 5124  CA  SER A 624     4405   4410   2912   -231    -94    140       C  
ATOM   5125  C   SER A 624      -6.328 -10.080 -56.433  1.00 31.47           C  
ANISOU 5125  C   SER A 624     4455   4556   2946   -263   -114    191       C  
ATOM   5126  O   SER A 624      -7.168  -9.277 -56.015  1.00 32.33           O  
ANISOU 5126  O   SER A 624     4552   4656   3078   -232   -133    253       O  
ATOM   5127  CB  SER A 624      -5.164 -11.313 -54.625  1.00 30.90           C  
ANISOU 5127  CB  SER A 624     4431   4360   2951   -206    -86     96       C  
ATOM   5128  OG  SER A 624      -6.279 -10.995 -53.812  1.00 38.83           O  
ANISOU 5128  OG  SER A 624     5437   5346   3969   -176    -99    136       O  
ATOM   5129  N   ILE A 625      -6.499 -10.823 -57.525  1.00 29.19           N  
ANISOU 5129  N   ILE A 625     4154   4335   2600   -328   -107    163       N  
ATOM   5130  CA  ILE A 625      -7.770 -10.855 -58.234  1.00 28.59           C  
ANISOU 5130  CA  ILE A 625     4051   4333   2479   -369   -133    208       C  
ATOM   5131  C   ILE A 625      -8.315 -12.280 -58.308  1.00 28.57           C  
ANISOU 5131  C   ILE A 625     4051   4350   2455   -404   -115    145       C  
ATOM   5132  O   ILE A 625      -7.555 -13.249 -58.344  1.00 25.68           O  
ANISOU 5132  O   ILE A 625     3701   3963   2092   -422    -79     65       O  
ATOM   5133  CB  ILE A 625      -7.691 -10.229 -59.660  1.00 31.19           C  
ANISOU 5133  CB  ILE A 625     4361   4750   2739   -436   -151    252       C  
ATOM   5134  CG1 ILE A 625      -6.681 -10.971 -60.545  1.00 28.55           C  
ANISOU 5134  CG1 ILE A 625     4043   4450   2355   -502   -113    172       C  
ATOM   5135  CG2 ILE A 625      -7.369  -8.728 -59.583  1.00 31.98           C  
ANISOU 5135  CG2 ILE A 625     4452   4830   2868   -399   -172    330       C  
ATOM   5136  CD1 ILE A 625      -6.750 -10.596 -62.008  1.00 27.24           C  
ANISOU 5136  CD1 ILE A 625     3866   4386   2100   -592   -128    206       C  
ATOM   5137  N   TYR A 626      -9.639 -12.387 -58.333  1.00 28.02           N  
ANISOU 5137  N   TYR A 626     3959   4314   2375   -413   -140    184       N  
ATOM   5138  CA  TYR A 626     -10.316 -13.667 -58.433  1.00 26.96           C  
ANISOU 5138  CA  TYR A 626     3822   4202   2219   -449   -125    132       C  
ATOM   5139  C   TYR A 626     -11.137 -13.684 -59.704  1.00 28.14           C  
ANISOU 5139  C   TYR A 626     3941   4459   2294   -530   -153    165       C  
ATOM   5140  O   TYR A 626     -12.039 -12.867 -59.888  1.00 29.29           O  
ANISOU 5140  O   TYR A 626     4053   4637   2438   -527   -198    253       O  
ATOM   5141  CB  TYR A 626     -11.180 -13.909 -57.194  1.00 25.00           C  
ANISOU 5141  CB  TYR A 626     3576   3894   2029   -392   -127    140       C  
ATOM   5142  CG  TYR A 626     -10.344 -14.158 -55.971  1.00 23.85           C  
ANISOU 5142  CG  TYR A 626     3467   3653   1941   -333   -101     98       C  
ATOM   5143  CD1 TYR A 626      -9.755 -13.097 -55.275  1.00 23.69           C  
ANISOU 5143  CD1 TYR A 626     3461   3580   1960   -279   -108    134       C  
ATOM   5144  CD2 TYR A 626     -10.109 -15.454 -55.521  1.00 24.54           C  
ANISOU 5144  CD2 TYR A 626     3575   3703   2045   -336    -71     26       C  
ATOM   5145  CE1 TYR A 626      -8.964 -13.321 -54.160  1.00 20.19           C  
ANISOU 5145  CE1 TYR A 626     3052   3057   1562   -235    -92    100       C  
ATOM   5146  CE2 TYR A 626      -9.329 -15.686 -54.409  1.00 24.59           C  
ANISOU 5146  CE2 TYR A 626     3613   3626   2104   -288    -58      1       C  
ATOM   5147  CZ  TYR A 626      -8.759 -14.614 -53.733  1.00 25.00           C  
ANISOU 5147  CZ  TYR A 626     3680   3634   2185   -240    -72     39       C  
ATOM   5148  OH  TYR A 626      -7.976 -14.843 -52.624  1.00 30.36           O  
ANISOU 5148  OH  TYR A 626     4390   4237   2909   -203    -66     19       O  
ATOM   5149  N   VAL A 627     -10.791 -14.618 -60.584  1.00 29.60           N  
ANISOU 5149  N   VAL A 627     4134   4694   2419   -608   -124     94       N  
ATOM   5150  CA  VAL A 627     -11.320 -14.669 -61.935  1.00 28.97           C  
ANISOU 5150  CA  VAL A 627     4034   4727   2246   -708   -147    114       C  
ATOM   5151  C   VAL A 627     -12.252 -15.861 -62.077  1.00 30.37           C  
ANISOU 5151  C   VAL A 627     4202   4939   2398   -756   -137     66       C  
ATOM   5152  O   VAL A 627     -11.881 -16.993 -61.762  1.00 29.56           O  
ANISOU 5152  O   VAL A 627     4119   4795   2317   -759    -83    -30       O  
ATOM   5153  CB  VAL A 627     -10.174 -14.778 -62.965  1.00 30.84           C  
ANISOU 5153  CB  VAL A 627     4290   5005   2421   -781   -111     59       C  
ATOM   5154  CG1 VAL A 627     -10.710 -14.690 -64.386  1.00 31.95           C  
ANISOU 5154  CG1 VAL A 627     4417   5274   2449   -898   -140     90       C  
ATOM   5155  CG2 VAL A 627      -9.121 -13.683 -62.718  1.00 31.78           C  
ANISOU 5155  CG2 VAL A 627     4422   5078   2576   -728   -113     94       C  
ATOM   5156  N   SER A 628     -13.468 -15.585 -62.537  1.00 31.41           N  
ANISOU 5156  N   SER A 628     4299   5143   2494   -792   -190    138       N  
ATOM   5157  CA  SER A 628     -14.450 -16.609 -62.857  1.00 33.87           C  
ANISOU 5157  CA  SER A 628     4595   5507   2768   -853   -190    102       C  
ATOM   5158  C   SER A 628     -14.052 -17.342 -64.137  1.00 34.71           C  
ANISOU 5158  C   SER A 628     4716   5701   2772   -978   -160     30       C  
ATOM   5159  O   SER A 628     -13.848 -16.716 -65.182  1.00 36.71           O  
ANISOU 5159  O   SER A 628     4964   6037   2946  -1050   -189     73       O  
ATOM   5160  CB  SER A 628     -15.831 -15.966 -63.021  1.00 35.12           C  
ANISOU 5160  CB  SER A 628     4702   5717   2923   -858   -264    212       C  
ATOM   5161  OG  SER A 628     -16.792 -16.914 -63.426  1.00 35.66           O  
ANISOU 5161  OG  SER A 628     4753   5847   2950   -927   -269    182       O  
ATOM   5162  N   ALA A 629     -13.949 -18.667 -64.047  1.00 34.93           N  
ANISOU 5162  N   ALA A 629     4760   5708   2804  -1008    -98    -81       N  
ATOM   5163  CA  ALA A 629     -13.465 -19.487 -65.158  1.00 34.97           C  
ANISOU 5163  CA  ALA A 629     4783   5779   2727  -1127    -45   -176       C  
ATOM   5164  C   ALA A 629     -14.543 -20.363 -65.811  1.00 35.72           C  
ANISOU 5164  C   ALA A 629     4861   5960   2752  -1227    -50   -207       C  
ATOM   5165  O   ALA A 629     -14.230 -21.190 -66.676  1.00 36.00           O  
ANISOU 5165  O   ALA A 629     4911   6046   2721  -1335      5   -303       O  
ATOM   5166  CB  ALA A 629     -12.284 -20.340 -64.700  1.00 34.44           C  
ANISOU 5166  CB  ALA A 629     4744   5616   2725  -1098     44   -293       C  
ATOM   5167  N   ASP A 630     -15.802 -20.174 -65.411  1.00 35.20           N  
ANISOU 5167  N   ASP A 630     4761   5909   2704  -1196   -112   -131       N  
ATOM   5168  CA  ASP A 630     -16.918 -20.960 -65.951  1.00 36.41           C  
ANISOU 5168  CA  ASP A 630     4892   6142   2799  -1286   -125   -152       C  
ATOM   5169  C   ASP A 630     -16.878 -21.034 -67.468  1.00 37.60           C  
ANISOU 5169  C   ASP A 630     5047   6428   2810  -1442   -134   -168       C  
ATOM   5170  O   ASP A 630     -16.987 -22.121 -68.048  1.00 36.74           O  
ANISOU 5170  O   ASP A 630     4949   6364   2645  -1542    -82   -269       O  
ATOM   5171  CB  ASP A 630     -18.271 -20.371 -65.529  1.00 37.37           C  
ANISOU 5171  CB  ASP A 630     4965   6279   2953  -1240   -209    -36       C  
ATOM   5172  CG  ASP A 630     -18.554 -20.532 -64.049  1.00 38.77           C  
ANISOU 5172  CG  ASP A 630     5141   6334   3254  -1111   -190    -38       C  
ATOM   5173  OD1 ASP A 630     -17.607 -20.796 -63.273  1.00 35.88           O  
ANISOU 5173  OD1 ASP A 630     4811   5869   2951  -1041   -131    -98       O  
ATOM   5174  OD2 ASP A 630     -19.738 -20.387 -63.667  1.00 41.11           O  
ANISOU 5174  OD2 ASP A 630     5398   6636   3585  -1085   -235     24       O  
ATOM   5175  N   LYS A 631     -16.728 -19.869 -68.096  1.00 35.38           N  
ANISOU 5175  N   LYS A 631     4758   6211   2474  -1467   -198    -67       N  
ATOM   5176  CA  LYS A 631     -16.766 -19.757 -69.551  1.00 36.73           C  
ANISOU 5176  CA  LYS A 631     4934   6524   2500  -1623   -223    -56       C  
ATOM   5177  C   LYS A 631     -15.580 -20.439 -70.230  1.00 37.14           C  
ANISOU 5177  C   LYS A 631     5034   6585   2491  -1712   -123   -193       C  
ATOM   5178  O   LYS A 631     -15.709 -20.921 -71.348  1.00 39.59           O  
ANISOU 5178  O   LYS A 631     5358   7005   2680  -1865   -108   -243       O  
ATOM   5179  CB  LYS A 631     -16.842 -18.289 -69.976  1.00 36.64           C  
ANISOU 5179  CB  LYS A 631     4901   6565   2456  -1620   -318     97       C  
ATOM   5180  CG  LYS A 631     -18.160 -17.623 -69.645  1.00 38.59           C  
ANISOU 5180  CG  LYS A 631     5085   6829   2747  -1571   -421    238       C  
ATOM   5181  CD  LYS A 631     -18.134 -16.156 -70.035  1.00 41.94           C  
ANISOU 5181  CD  LYS A 631     5484   7289   3160  -1560   -507    391       C  
ATOM   5182  CE  LYS A 631     -19.534 -15.576 -70.052  1.00 45.98           C  
ANISOU 5182  CE  LYS A 631     5923   7845   3701  -1552   -616    536       C  
ATOM   5183  NZ  LYS A 631     -20.125 -15.477 -68.682  1.00 49.36           N  
ANISOU 5183  NZ  LYS A 631     6318   8153   4285  -1404   -611    555       N  
ATOM   5184  N   ILE A 632     -14.432 -20.479 -69.552  1.00 37.52           N  
ANISOU 5184  N   ILE A 632     5109   6519   2629  -1623    -53   -255       N  
ATOM   5185  CA  ILE A 632     -13.242 -21.146 -70.099  1.00 37.19           C  
ANISOU 5185  CA  ILE A 632     5104   6464   2560  -1694     54   -391       C  
ATOM   5186  C   ILE A 632     -13.477 -22.651 -70.098  1.00 37.85           C  
ANISOU 5186  C   ILE A 632     5193   6531   2657  -1748    136   -527       C  
ATOM   5187  O   ILE A 632     -13.240 -23.323 -71.102  1.00 37.55           O  
ANISOU 5187  O   ILE A 632     5174   6562   2530  -1889    201   -627       O  
ATOM   5188  CB  ILE A 632     -11.936 -20.787 -69.323  1.00 35.48           C  
ANISOU 5188  CB  ILE A 632     4905   6122   2453  -1578    102   -414       C  
ATOM   5189  CG1 ILE A 632     -11.771 -19.267 -69.188  1.00 33.83           C  
ANISOU 5189  CG1 ILE A 632     4689   5919   2247  -1512     22   -277       C  
ATOM   5190  CG2 ILE A 632     -10.700 -21.423 -69.987  1.00 31.91           C  
ANISOU 5190  CG2 ILE A 632     4483   5659   1983  -1660    215   -552       C  
ATOM   5191  CD1 ILE A 632     -11.729 -18.512 -70.500  1.00 39.25           C  
ANISOU 5191  CD1 ILE A 632     5383   6733   2796  -1635    -19   -219       C  
ATOM   5192  N   ILE A 633     -13.963 -23.165 -68.969  1.00 37.57           N  
ANISOU 5192  N   ILE A 633     5141   6403   2731  -1641    138   -532       N  
ATOM   5193  CA  ILE A 633     -14.351 -24.563 -68.875  1.00 38.54           C  
ANISOU 5193  CA  ILE A 633     5262   6505   2876  -1683    206   -645       C  
ATOM   5194  C   ILE A 633     -15.423 -24.888 -69.922  1.00 40.77           C  
ANISOU 5194  C   ILE A 633     5534   6931   3027  -1831    174   -645       C  
ATOM   5195  O   ILE A 633     -15.324 -25.900 -70.616  1.00 40.85           O  
ANISOU 5195  O   ILE A 633     5559   6978   2986  -1950    253   -768       O  
ATOM   5196  CB  ILE A 633     -14.842 -24.932 -67.450  1.00 37.58           C  
ANISOU 5196  CB  ILE A 633     5125   6268   2886  -1544    197   -625       C  
ATOM   5197  CG1 ILE A 633     -13.684 -24.882 -66.436  1.00 36.17           C  
ANISOU 5197  CG1 ILE A 633     4961   5948   2835  -1419    242   -649       C  
ATOM   5198  CG2 ILE A 633     -15.533 -26.299 -67.441  1.00 36.49           C  
ANISOU 5198  CG2 ILE A 633     4980   6129   2757  -1598    249   -720       C  
ATOM   5199  CD1 ILE A 633     -12.510 -25.804 -66.762  1.00 35.21           C  
ANISOU 5199  CD1 ILE A 633     4856   5771   2750  -1465    358   -788       C  
ATOM   5200  N   ASP A 634     -16.419 -24.010 -70.042  1.00 42.32           N  
ANISOU 5200  N   ASP A 634     5702   7204   3172  -1829     58   -507       N  
ATOM   5201  CA  ASP A 634     -17.559 -24.224 -70.937  1.00 46.21           C  
ANISOU 5201  CA  ASP A 634     6174   7835   3547  -1961      3   -481       C  
ATOM   5202  C   ASP A 634     -17.199 -24.163 -72.418  1.00 47.74           C  
ANISOU 5202  C   ASP A 634     6394   8164   3581  -2141     15   -515       C  
ATOM   5203  O   ASP A 634     -17.886 -24.763 -73.244  1.00 48.81           O  
ANISOU 5203  O   ASP A 634     6528   8409   3611  -2284     11   -554       O  
ATOM   5204  CB  ASP A 634     -18.683 -23.227 -70.642  1.00 46.76           C  
ANISOU 5204  CB  ASP A 634     6197   7943   3627  -1903   -129   -311       C  
ATOM   5205  CG  ASP A 634     -19.434 -23.543 -69.357  1.00 49.12           C  
ANISOU 5205  CG  ASP A 634     6467   8141   4056  -1772   -137   -294       C  
ATOM   5206  OD1 ASP A 634     -19.164 -24.586 -68.720  1.00 45.93           O  
ANISOU 5206  OD1 ASP A 634     6081   7647   3724  -1734    -49   -407       O  
ATOM   5207  OD2 ASP A 634     -20.308 -22.732 -68.984  1.00 53.64           O  
ANISOU 5207  OD2 ASP A 634     6997   8722   4664  -1710   -230   -164       O  
ATOM   5208  N   LYS A 635     -16.135 -23.434 -72.751  1.00 47.67           N  
ANISOU 5208  N   LYS A 635     6412   8150   3549  -2142     31   -503       N  
ATOM   5209  CA  LYS A 635     -15.689 -23.329 -74.140  1.00 50.20           C  
ANISOU 5209  CA  LYS A 635     6765   8596   3715  -2317     51   -538       C  
ATOM   5210  C   LYS A 635     -15.132 -24.640 -74.703  1.00 50.44           C  
ANISOU 5210  C   LYS A 635     6829   8628   3709  -2439    191   -732       C  
ATOM   5211  O   LYS A 635     -15.144 -24.848 -75.917  1.00 50.57           O  
ANISOU 5211  O   LYS A 635     6870   8769   3575  -2621    212   -781       O  
ATOM   5212  CB  LYS A 635     -14.686 -22.190 -74.326  1.00 50.74           C  
ANISOU 5212  CB  LYS A 635     6852   8653   3774  -2285     36   -474       C  
ATOM   5213  CG  LYS A 635     -15.191 -21.088 -75.241  1.00 57.88           C  
ANISOU 5213  CG  LYS A 635     7748   9698   4547  -2375    -83   -325       C  
ATOM   5214  CD  LYS A 635     -14.086 -20.617 -76.175  1.00 63.71           C  
ANISOU 5214  CD  LYS A 635     8531  10487   5188  -2474    -39   -353       C  
ATOM   5215  CE  LYS A 635     -14.630 -20.136 -77.524  1.00 68.90           C  
ANISOU 5215  CE  LYS A 635     9196  11328   5653  -2659   -122   -268       C  
ATOM   5216  NZ  LYS A 635     -15.091 -18.718 -77.496  1.00 71.28           N  
ANISOU 5216  NZ  LYS A 635     9464  11666   5954  -2602   -266    -59       N  
ATOM   5217  N   VAL A 636     -14.644 -25.515 -73.825  1.00 50.05           N  
ANISOU 5217  N   VAL A 636     6780   8438   3800  -2343    289   -842       N  
ATOM   5218  CA  VAL A 636     -14.230 -26.853 -74.249  1.00 51.72           C  
ANISOU 5218  CA  VAL A 636     7011   8631   4009  -2446    428  -1028       C  
ATOM   5219  C   VAL A 636     -15.349 -27.854 -73.970  1.00 53.07           C  
ANISOU 5219  C   VAL A 636     7160   8808   4198  -2464    429  -1067       C  
ATOM   5220  O   VAL A 636     -15.542 -28.804 -74.732  1.00 54.50           O  
ANISOU 5220  O   VAL A 636     7353   9049   4305  -2613    504  -1188       O  
ATOM   5221  CB  VAL A 636     -12.859 -27.310 -73.637  1.00 51.02           C  
ANISOU 5221  CB  VAL A 636     6934   8384   4068  -2356    552  -1138       C  
ATOM   5222  CG1 VAL A 636     -12.055 -26.127 -73.128  1.00 48.93           C  
ANISOU 5222  CG1 VAL A 636     6671   8060   3861  -2231    504  -1039       C  
ATOM   5223  CG2 VAL A 636     -13.032 -28.354 -72.553  1.00 50.88           C  
ANISOU 5223  CG2 VAL A 636     6894   8232   4205  -2249    606  -1203       C  
ATOM   5224  N   GLY A 637     -16.096 -27.614 -72.892  1.00 52.16           N  
ANISOU 5224  N   GLY A 637     7011   8630   4176  -2320    349   -967       N  
ATOM   5225  CA  GLY A 637     -17.199 -28.481 -72.489  1.00 53.76           C  
ANISOU 5225  CA  GLY A 637     7189   8828   4410  -2317    343   -990       C  
ATOM   5226  C   GLY A 637     -16.752 -29.462 -71.426  1.00 53.67           C  
ANISOU 5226  C   GLY A 637     7176   8653   4564  -2206    441  -1088       C  
ATOM   5227  O   GLY A 637     -15.738 -30.132 -71.596  1.00 53.58           O  
ANISOU 5227  O   GLY A 637     7185   8577   4597  -2235    560  -1216       O  
ATOM   5228  N   GLU A 638     -17.509 -29.548 -70.332  1.00 54.05           N  
ANISOU 5228  N   GLU A 638     7198   8631   4707  -2083    392  -1025       N  
ATOM   5229  CA  GLU A 638     -17.165 -30.434 -69.211  1.00 55.22           C  
ANISOU 5229  CA  GLU A 638     7344   8622   5013  -1971    469  -1095       C  
ATOM   5230  C   GLU A 638     -17.021 -31.907 -69.603  1.00 56.79           C  
ANISOU 5230  C   GLU A 638     7550   8797   5231  -2069    596  -1263       C  
ATOM   5231  O   GLU A 638     -16.278 -32.652 -68.959  1.00 56.81           O  
ANISOU 5231  O   GLU A 638     7555   8666   5365  -2002    687  -1343       O  
ATOM   5232  CB  GLU A 638     -18.185 -30.300 -68.075  1.00 55.70           C  
ANISOU 5232  CB  GLU A 638     7379   8634   5148  -1850    394  -1000       C  
ATOM   5233  CG  GLU A 638     -17.929 -29.140 -67.118  1.00 56.00           C  
ANISOU 5233  CG  GLU A 638     7414   8606   5255  -1697    319   -872       C  
ATOM   5234  CD  GLU A 638     -18.987 -29.023 -66.027  1.00 60.02           C  
ANISOU 5234  CD  GLU A 638     7900   9071   5833  -1592    257   -789       C  
ATOM   5235  OE1 GLU A 638     -18.712 -28.388 -64.982  1.00 56.00           O  
ANISOU 5235  OE1 GLU A 638     7394   8473   5410  -1459    226   -717       O  
ATOM   5236  OE2 GLU A 638     -20.099 -29.567 -66.211  1.00 64.78           O  
ANISOU 5236  OE2 GLU A 638     8481   9727   6404  -1649    242   -799       O  
ATOM   5237  N   SER A 639     -17.720 -32.312 -70.663  1.00 57.85           N  
ANISOU 5237  N   SER A 639     7684   9060   5238  -2232    603  -1314       N  
ATOM   5238  CA  SER A 639     -17.764 -33.707 -71.108  1.00 58.05           C  
ANISOU 5238  CA  SER A 639     7712   9075   5268  -2344    724  -1477       C  
ATOM   5239  C   SER A 639     -16.427 -34.210 -71.649  1.00 58.15           C  
ANISOU 5239  C   SER A 639     7748   9036   5310  -2407    861  -1618       C  
ATOM   5240  O   SER A 639     -16.181 -35.417 -71.682  1.00 58.07           O  
ANISOU 5240  O   SER A 639     7735   8956   5373  -2451    985  -1759       O  
ATOM   5241  CB  SER A 639     -18.853 -33.888 -72.170  1.00 60.16           C  
ANISOU 5241  CB  SER A 639     7976   9510   5372  -2517    686  -1488       C  
ATOM   5242  OG  SER A 639     -20.135 -33.597 -71.639  1.00 60.30           O  
ANISOU 5242  OG  SER A 639     7963   9562   5388  -2459    572  -1372       O  
ATOM   5243  N   LYS A 640     -15.574 -33.279 -72.068  1.00 57.52           N  
ANISOU 5243  N   LYS A 640     7687   8986   5184  -2412    843  -1579       N  
ATOM   5244  CA  LYS A 640     -14.271 -33.605 -72.651  1.00 57.88           C  
ANISOU 5244  CA  LYS A 640     7750   8988   5252  -2477    972  -1706       C  
ATOM   5245  C   LYS A 640     -13.193 -33.952 -71.620  1.00 55.65           C  
ANISOU 5245  C   LYS A 640     7455   8517   5174  -2326   1043  -1741       C  
ATOM   5246  O   LYS A 640     -12.111 -34.414 -71.995  1.00 56.04           O  
ANISOU 5246  O   LYS A 640     7507   8503   5281  -2371   1166  -1860       O  
ATOM   5247  CB  LYS A 640     -13.785 -32.458 -73.554  1.00 61.02           C  
ANISOU 5247  CB  LYS A 640     8174   9497   5513  -2551    926  -1650       C  
ATOM   5248  CG  LYS A 640     -13.990 -32.659 -75.070  1.00 65.68           C  
ANISOU 5248  CG  LYS A 640     8792  10248   5916  -2784    968  -1735       C  
ATOM   5249  CD  LYS A 640     -15.423 -33.069 -75.454  1.00 72.68           C  
ANISOU 5249  CD  LYS A 640     9670  11254   6691  -2887    909  -1720       C  
ATOM   5250  CE  LYS A 640     -16.431 -31.930 -75.285  1.00 74.28           C  
ANISOU 5250  CE  LYS A 640     9857  11554   6812  -2836    724  -1521       C  
ATOM   5251  NZ  LYS A 640     -16.304 -30.897 -76.358  1.00 75.88           N  
ANISOU 5251  NZ  LYS A 640    10083  11905   6841  -2954    655  -1447       N  
ATOM   5252  N   PHE A 641     -13.482 -33.734 -70.333  1.00 51.81           N  
ANISOU 5252  N   PHE A 641     6951   7938   4796  -2156    968  -1637       N  
ATOM   5253  CA  PHE A 641     -12.508 -34.006 -69.265  1.00 48.41           C  
ANISOU 5253  CA  PHE A 641     6506   7332   4554  -2010   1014  -1647       C  
ATOM   5254  C   PHE A 641     -12.637 -35.412 -68.680  1.00 48.68           C  
ANISOU 5254  C   PHE A 641     6519   7249   4727  -1987   1104  -1741       C  
ATOM   5255  O   PHE A 641     -13.739 -35.884 -68.410  1.00 47.06           O  
ANISOU 5255  O   PHE A 641     6307   7067   4505  -1993   1075  -1727       O  
ATOM   5256  CB  PHE A 641     -12.586 -32.952 -68.153  1.00 44.22           C  
ANISOU 5256  CB  PHE A 641     5974   6760   4067  -1844    890  -1485       C  
ATOM   5257  CG  PHE A 641     -12.236 -31.562 -68.610  1.00 40.14           C  
ANISOU 5257  CG  PHE A 641     5473   6326   3451  -1847    814  -1393       C  
ATOM   5258  CD1 PHE A 641     -13.221 -30.586 -68.722  1.00 37.85           C  
ANISOU 5258  CD1 PHE A 641     5186   6147   3048  -1847    689  -1265       C  
ATOM   5259  CD2 PHE A 641     -10.925 -31.231 -68.943  1.00 38.85           C  
ANISOU 5259  CD2 PHE A 641     5319   6127   3317  -1852    870  -1433       C  
ATOM   5260  CE1 PHE A 641     -12.906 -29.300 -69.152  1.00 37.23           C  
ANISOU 5260  CE1 PHE A 641     5119   6140   2886  -1850    619  -1175       C  
ATOM   5261  CE2 PHE A 641     -10.595 -29.942 -69.376  1.00 35.01           C  
ANISOU 5261  CE2 PHE A 641     4848   5715   2739  -1857    802  -1348       C  
ATOM   5262  CZ  PHE A 641     -11.588 -28.976 -69.477  1.00 34.46           C  
ANISOU 5262  CZ  PHE A 641     4782   5754   2557  -1856    676  -1216       C  
ATOM   5263  N   ARG A 642     -11.495 -36.068 -68.492  1.00 49.84           N  
ANISOU 5263  N   ARG A 642     6651   7265   5019  -1960   1215  -1833       N  
ATOM   5264  CA  ARG A 642     -11.442 -37.434 -67.973  1.00 50.81           C  
ANISOU 5264  CA  ARG A 642     6748   7260   5298  -1939   1312  -1925       C  
ATOM   5265  C   ARG A 642     -11.817 -37.466 -66.498  1.00 48.34           C  
ANISOU 5265  C   ARG A 642     6425   6847   5096  -1775   1233  -1815       C  
ATOM   5266  O   ARG A 642     -12.584 -38.332 -66.064  1.00 47.83           O  
ANISOU 5266  O   ARG A 642     6350   6746   5077  -1769   1249  -1836       O  
ATOM   5267  CB  ARG A 642     -10.033 -38.011 -68.143  1.00 53.23           C  
ANISOU 5267  CB  ARG A 642     7031   7444   5751  -1945   1446  -2038       C  
ATOM   5268  CG  ARG A 642      -9.622 -38.336 -69.570  1.00 58.92           C  
ANISOU 5268  CG  ARG A 642     7759   8235   6394  -2124   1569  -2189       C  
ATOM   5269  CD  ARG A 642      -8.116 -38.560 -69.635  1.00 62.31           C  
ANISOU 5269  CD  ARG A 642     8161   8539   6974  -2103   1681  -2270       C  
ATOM   5270  NE  ARG A 642      -7.393 -37.356 -70.046  1.00 67.18           N  
ANISOU 5270  NE  ARG A 642     8798   9216   7510  -2104   1636  -2217       N  
ATOM   5271  CZ  ARG A 642      -6.260 -36.921 -69.496  1.00 68.46           C  
ANISOU 5271  CZ  ARG A 642     8941   9275   7797  -1995   1631  -2177       C  
ATOM   5272  NH1 ARG A 642      -5.709 -37.568 -68.475  1.00 69.23           N  
ANISOU 5272  NH1 ARG A 642     8995   9202   8107  -1874   1659  -2172       N  
ATOM   5273  NH2 ARG A 642      -5.680 -35.821 -69.959  1.00 67.13           N  
ANISOU 5273  NH2 ARG A 642     8793   9173   7540  -2009   1594  -2134       N  
ATOM   5274  N   ASP A 643     -11.253 -36.519 -65.744  1.00 45.33           N  
ANISOU 5274  N   ASP A 643     6048   6423   4753  -1650   1151  -1701       N  
ATOM   5275  CA  ASP A 643     -11.442 -36.395 -64.300  1.00 42.70           C  
ANISOU 5275  CA  ASP A 643     5712   5995   4516  -1497   1072  -1590       C  
ATOM   5276  C   ASP A 643     -11.103 -34.967 -63.841  1.00 41.61           C  
ANISOU 5276  C   ASP A 643     5591   5881   4338  -1404    962  -1459       C  
ATOM   5277  O   ASP A 643     -10.723 -34.119 -64.655  1.00 41.42           O  
ANISOU 5277  O   ASP A 643     5579   5942   4218  -1456    947  -1453       O  
ATOM   5278  CB  ASP A 643     -10.583 -37.426 -63.547  1.00 42.36           C  
ANISOU 5278  CB  ASP A 643     5640   5777   4678  -1430   1153  -1641       C  
ATOM   5279  CG  ASP A 643      -9.129 -37.439 -64.009  1.00 45.89           C  
ANISOU 5279  CG  ASP A 643     6067   6160   5209  -1445   1235  -1711       C  
ATOM   5280  OD1 ASP A 643      -8.560 -36.364 -64.300  1.00 45.89           O  
ANISOU 5280  OD1 ASP A 643     6080   6211   5145  -1435   1191  -1665       O  
ATOM   5281  OD2 ASP A 643      -8.544 -38.538 -64.082  1.00 52.71           O  
ANISOU 5281  OD2 ASP A 643     6897   6916   6214  -1468   1349  -1815       O  
ATOM   5282  N   THR A 644     -11.224 -34.716 -62.538  1.00 38.62           N  
ANISOU 5282  N   THR A 644     5217   5426   4033  -1274    889  -1357       N  
ATOM   5283  CA  THR A 644     -10.977 -33.394 -61.977  1.00 36.43           C  
ANISOU 5283  CA  THR A 644     4955   5161   3724  -1184    788  -1234       C  
ATOM   5284  C   THR A 644      -9.570 -32.901 -62.329  1.00 37.82           C  
ANISOU 5284  C   THR A 644     5126   5306   3937  -1177    818  -1255       C  
ATOM   5285  O   THR A 644      -9.402 -31.781 -62.834  1.00 36.51           O  
ANISOU 5285  O   THR A 644     4974   5223   3675  -1192    770  -1207       O  
ATOM   5286  CB  THR A 644     -11.181 -33.376 -60.438  1.00 34.63           C  
ANISOU 5286  CB  THR A 644     4734   4838   3586  -1054    726  -1141       C  
ATOM   5287  OG1 THR A 644     -12.470 -33.913 -60.105  1.00 30.22           O  
ANISOU 5287  OG1 THR A 644     4178   4301   3003  -1064    710  -1131       O  
ATOM   5288  CG2 THR A 644     -11.083 -31.956 -59.900  1.00 32.83           C  
ANISOU 5288  CG2 THR A 644     4526   4637   3312   -974    625  -1020       C  
ATOM   5289  N   ASN A 645      -8.568 -33.747 -62.093  1.00 37.38           N  
ANISOU 5289  N   ASN A 645     5046   5129   4029  -1157    899  -1324       N  
ATOM   5290  CA  ASN A 645      -7.182 -33.350 -62.320  1.00 37.44           C  
ANISOU 5290  CA  ASN A 645     5040   5089   4098  -1142    932  -1344       C  
ATOM   5291  C   ASN A 645      -6.941 -32.873 -63.752  1.00 37.45           C  
ANISOU 5291  C   ASN A 645     5050   5202   3978  -1261    976  -1410       C  
ATOM   5292  O   ASN A 645      -6.057 -32.053 -63.992  1.00 38.20           O  
ANISOU 5292  O   ASN A 645     5146   5302   4064  -1248    966  -1390       O  
ATOM   5293  CB  ASN A 645      -6.211 -34.470 -61.933  1.00 38.86           C  
ANISOU 5293  CB  ASN A 645     5179   5115   4471  -1114   1022  -1417       C  
ATOM   5294  CG  ASN A 645      -4.806 -33.955 -61.665  1.00 40.42           C  
ANISOU 5294  CG  ASN A 645     5358   5236   4765  -1052   1020  -1394       C  
ATOM   5295  OD1 ASN A 645      -4.599 -33.095 -60.807  1.00 39.98           O  
ANISOU 5295  OD1 ASN A 645     5316   5164   4710   -956    924  -1282       O  
ATOM   5296  ND2 ASN A 645      -3.831 -34.479 -62.405  1.00 40.66           N  
ANISOU 5296  ND2 ASN A 645     5353   5216   4880  -1110   1133  -1505       N  
ATOM   5297  N   HIS A 646      -7.756 -33.371 -64.684  1.00 38.54           N  
ANISOU 5297  N   HIS A 646     5195   5432   4017  -1381   1021  -1484       N  
ATOM   5298  CA  HIS A 646      -7.691 -32.983 -66.093  1.00 38.38           C  
ANISOU 5298  CA  HIS A 646     5190   5536   3858  -1518   1059  -1546       C  
ATOM   5299  C   HIS A 646      -8.105 -31.524 -66.345  1.00 37.30           C  
ANISOU 5299  C   HIS A 646     5082   5523   3569  -1513    943  -1427       C  
ATOM   5300  O   HIS A 646      -7.339 -30.776 -66.950  1.00 37.35           O  
ANISOU 5300  O   HIS A 646     5097   5565   3528  -1545    950  -1427       O  
ATOM   5301  CB  HIS A 646      -8.493 -33.959 -66.956  1.00 40.25           C  
ANISOU 5301  CB  HIS A 646     5427   5839   4026  -1655   1133  -1655       C  
ATOM   5302  CG  HIS A 646      -8.290 -33.785 -68.429  1.00 41.20           C  
ANISOU 5302  CG  HIS A 646     5564   6076   4014  -1817   1196  -1742       C  
ATOM   5303  ND1 HIS A 646      -9.095 -34.402 -69.363  1.00 42.95           N  
ANISOU 5303  ND1 HIS A 646     5797   6398   4126  -1965   1244  -1827       N  
ATOM   5304  CD2 HIS A 646      -7.388 -33.059 -69.131  1.00 43.39           C  
ANISOU 5304  CD2 HIS A 646     5853   6390   4243  -1862   1218  -1757       C  
ATOM   5305  CE1 HIS A 646      -8.695 -34.067 -70.576  1.00 41.16           C  
ANISOU 5305  CE1 HIS A 646     5589   6267   3783  -2100   1292  -1890       C  
ATOM   5306  NE2 HIS A 646      -7.662 -33.252 -70.464  1.00 42.52           N  
ANISOU 5306  NE2 HIS A 646     5763   6402   3991  -2039   1279  -1849       N  
ATOM   5307  N   TRP A 647      -9.281 -31.104 -65.874  1.00 36.37           N  
ANISOU 5307  N   TRP A 647     4975   5461   3384  -1473    840  -1325       N  
ATOM   5308  CA  TRP A 647      -9.643 -29.677 -65.993  1.00 35.94           C  
ANISOU 5308  CA  TRP A 647     4937   5502   3215  -1452    728  -1201       C  
ATOM   5309  C   TRP A 647      -8.723 -28.761 -65.174  1.00 35.62           C  
ANISOU 5309  C   TRP A 647     4898   5384   3250  -1328    682  -1120       C  
ATOM   5310  O   TRP A 647      -8.491 -27.613 -65.560  1.00 37.26           O  
ANISOU 5310  O   TRP A 647     5118   5656   3382  -1332    630  -1054       O  
ATOM   5311  CB  TRP A 647     -11.140 -29.394 -65.733  1.00 36.32           C  
ANISOU 5311  CB  TRP A 647     4987   5628   3185  -1442    633  -1111       C  
ATOM   5312  CG  TRP A 647     -11.641 -29.546 -64.295  1.00 33.66           C  
ANISOU 5312  CG  TRP A 647     4644   5197   2947  -1310    585  -1043       C  
ATOM   5313  CD1 TRP A 647     -12.379 -30.582 -63.793  1.00 34.54           C  
ANISOU 5313  CD1 TRP A 647     4746   5267   3110  -1303    609  -1078       C  
ATOM   5314  CD2 TRP A 647     -11.475 -28.615 -63.210  1.00 32.32           C  
ANISOU 5314  CD2 TRP A 647     4481   4972   2829  -1180    507   -930       C  
ATOM   5315  NE1 TRP A 647     -12.662 -30.370 -62.463  1.00 35.21           N  
ANISOU 5315  NE1 TRP A 647     4834   5273   3270  -1179    552   -994       N  
ATOM   5316  CE2 TRP A 647     -12.120 -29.171 -62.080  1.00 32.77           C  
ANISOU 5316  CE2 TRP A 647     4534   4955   2961  -1104    490   -905       C  
ATOM   5317  CE3 TRP A 647     -10.835 -27.373 -63.081  1.00 31.76           C  
ANISOU 5317  CE3 TRP A 647     4418   4904   2744  -1125    455   -852       C  
ATOM   5318  CZ2 TRP A 647     -12.142 -28.532 -60.842  1.00 31.50           C  
ANISOU 5318  CZ2 TRP A 647     4383   4730   2856   -984    426   -810       C  
ATOM   5319  CZ3 TRP A 647     -10.859 -26.734 -61.847  1.00 29.45           C  
ANISOU 5319  CZ3 TRP A 647     4132   4544   2514  -1002    391   -759       C  
ATOM   5320  CH2 TRP A 647     -11.505 -27.315 -60.744  1.00 30.56           C  
ANISOU 5320  CH2 TRP A 647     4272   4616   2722   -936    378   -740       C  
ATOM   5321  N   VAL A 648      -8.189 -29.277 -64.064  1.00 34.53           N  
ANISOU 5321  N   VAL A 648     4748   5110   3262  -1224    700  -1123       N  
ATOM   5322  CA  VAL A 648      -7.229 -28.525 -63.250  1.00 33.02           C  
ANISOU 5322  CA  VAL A 648     4557   4838   3151  -1114    661  -1057       C  
ATOM   5323  C   VAL A 648      -5.931 -28.270 -64.027  1.00 34.85           C  
ANISOU 5323  C   VAL A 648     4782   5063   3396  -1159    725  -1119       C  
ATOM   5324  O   VAL A 648      -5.433 -27.137 -64.041  1.00 34.98           O  
ANISOU 5324  O   VAL A 648     4809   5102   3380  -1126    676  -1052       O  
ATOM   5325  CB  VAL A 648      -6.967 -29.196 -61.878  1.00 31.17           C  
ANISOU 5325  CB  VAL A 648     4310   4464   3069  -1004    659  -1040       C  
ATOM   5326  CG1 VAL A 648      -5.854 -28.483 -61.131  1.00 26.79           C  
ANISOU 5326  CG1 VAL A 648     3753   3830   2594   -909    625   -982       C  
ATOM   5327  CG2 VAL A 648      -8.242 -29.187 -61.034  1.00 29.98           C  
ANISOU 5327  CG2 VAL A 648     4173   4327   2892   -954    587   -963       C  
ATOM   5328  N   ASP A 649      -5.406 -29.311 -64.680  1.00 35.73           N  
ANISOU 5328  N   ASP A 649     4876   5141   3560  -1238    840  -1248       N  
ATOM   5329  CA  ASP A 649      -4.264 -29.178 -65.603  1.00 39.32           C  
ANISOU 5329  CA  ASP A 649     5322   5597   4019  -1308    922  -1330       C  
ATOM   5330  C   ASP A 649      -4.564 -28.201 -66.732  1.00 37.64           C  
ANISOU 5330  C   ASP A 649     5140   5536   3625  -1406    893  -1306       C  
ATOM   5331  O   ASP A 649      -3.705 -27.408 -67.118  1.00 36.53           O  
ANISOU 5331  O   ASP A 649     5005   5408   3467  -1414    897  -1296       O  
ATOM   5332  CB  ASP A 649      -3.870 -30.539 -66.225  1.00 42.47           C  
ANISOU 5332  CB  ASP A 649     5696   5946   4496  -1399   1065  -1487       C  
ATOM   5333  CG  ASP A 649      -2.998 -31.390 -65.305  1.00 46.45           C  
ANISOU 5333  CG  ASP A 649     6156   6277   5215  -1308   1116  -1520       C  
ATOM   5334  OD1 ASP A 649      -2.362 -30.844 -64.374  1.00 50.38           O  
ANISOU 5334  OD1 ASP A 649     6645   6700   5798  -1192   1053  -1435       O  
ATOM   5335  OD2 ASP A 649      -2.944 -32.617 -65.523  1.00 49.06           O  
ANISOU 5335  OD2 ASP A 649     6460   6546   5634  -1357   1219  -1629       O  
ATOM   5336  N   PHE A 650      -5.780 -28.273 -67.268  1.00 37.94           N  
ANISOU 5336  N   PHE A 650     5195   5688   3533  -1485    861  -1295       N  
ATOM   5337  CA  PHE A 650      -6.176 -27.385 -68.357  1.00 39.17           C  
ANISOU 5337  CA  PHE A 650     5377   5994   3511  -1588    821  -1258       C  
ATOM   5338  C   PHE A 650      -6.120 -25.912 -67.935  1.00 37.58           C  
ANISOU 5338  C   PHE A 650     5186   5816   3276  -1500    708  -1113       C  
ATOM   5339  O   PHE A 650      -5.504 -25.092 -68.621  1.00 35.72           O  
ANISOU 5339  O   PHE A 650     4964   5632   2975  -1544    708  -1099       O  
ATOM   5340  CB  PHE A 650      -7.555 -27.767 -68.914  1.00 38.76           C  
ANISOU 5340  CB  PHE A 650     5334   6057   3337  -1685    794  -1259       C  
ATOM   5341  CG  PHE A 650      -8.147 -26.727 -69.815  1.00 41.26           C  
ANISOU 5341  CG  PHE A 650     5672   6529   3477  -1769    714  -1177       C  
ATOM   5342  CD1 PHE A 650      -7.656 -26.541 -71.103  1.00 43.97           C  
ANISOU 5342  CD1 PHE A 650     6036   6962   3708  -1913    768  -1238       C  
ATOM   5343  CD2 PHE A 650      -9.188 -25.918 -69.372  1.00 42.29           C  
ANISOU 5343  CD2 PHE A 650     5799   6711   3557  -1708    587  -1035       C  
ATOM   5344  CE1 PHE A 650      -8.197 -25.571 -71.941  1.00 46.52           C  
ANISOU 5344  CE1 PHE A 650     6378   7430   3867  -1996    686  -1149       C  
ATOM   5345  CE2 PHE A 650      -9.737 -24.946 -70.203  1.00 44.35           C  
ANISOU 5345  CE2 PHE A 650     6071   7108   3670  -1784    507   -946       C  
ATOM   5346  CZ  PHE A 650      -9.238 -24.772 -71.490  1.00 44.45           C  
ANISOU 5346  CZ  PHE A 650     6107   7216   3567  -1929    551   -998       C  
ATOM   5347  N   LEU A 651      -6.747 -25.594 -66.801  1.00 38.37           N  
ANISOU 5347  N   LEU A 651     5281   5874   3423  -1379    619  -1011       N  
ATOM   5348  CA  LEU A 651      -6.733 -24.234 -66.244  1.00 38.24           C  
ANISOU 5348  CA  LEU A 651     5272   5863   3396  -1286    519   -878       C  
ATOM   5349  C   LEU A 651      -5.330 -23.771 -65.854  1.00 38.52           C  
ANISOU 5349  C   LEU A 651     5304   5809   3523  -1217    544   -882       C  
ATOM   5350  O   LEU A 651      -4.961 -22.621 -66.113  1.00 38.47           O  
ANISOU 5350  O   LEU A 651     5308   5842   3468  -1209    501   -816       O  
ATOM   5351  CB  LEU A 651      -7.689 -24.112 -65.044  1.00 36.90           C  
ANISOU 5351  CB  LEU A 651     5096   5655   3269  -1178    439   -787       C  
ATOM   5352  CG  LEU A 651      -9.193 -24.178 -65.326  1.00 39.17           C  
ANISOU 5352  CG  LEU A 651     5380   6038   3463  -1226    385   -743       C  
ATOM   5353  CD1 LEU A 651      -9.979 -23.886 -64.058  1.00 37.46           C  
ANISOU 5353  CD1 LEU A 651     5158   5770   3305  -1110    312   -651       C  
ATOM   5354  CD2 LEU A 651      -9.611 -23.219 -66.450  1.00 38.49           C  
ANISOU 5354  CD2 LEU A 651     5299   6090   3234  -1317    332   -681       C  
ATOM   5355  N   ASP A 652      -4.564 -24.672 -65.238  1.00 39.24           N  
ANISOU 5355  N   ASP A 652     5377   5779   3752  -1169    609   -956       N  
ATOM   5356  CA  ASP A 652      -3.161 -24.430 -64.880  1.00 39.63           C  
ANISOU 5356  CA  ASP A 652     5415   5735   3910  -1110    641   -973       C  
ATOM   5357  C   ASP A 652      -2.342 -24.016 -66.104  1.00 40.98           C  
ANISOU 5357  C   ASP A 652     5591   5962   4018  -1208    701  -1030       C  
ATOM   5358  O   ASP A 652      -1.590 -23.033 -66.057  1.00 39.17           O  
ANISOU 5358  O   ASP A 652     5365   5724   3791  -1171    675   -982       O  
ATOM   5359  CB  ASP A 652      -2.559 -25.685 -64.223  1.00 40.91           C  
ANISOU 5359  CB  ASP A 652     5547   5764   4234  -1068    711  -1052       C  
ATOM   5360  CG  ASP A 652      -1.060 -25.569 -63.968  1.00 45.46           C  
ANISOU 5360  CG  ASP A 652     6098   6240   4934  -1022    752  -1080       C  
ATOM   5361  OD1 ASP A 652      -0.628 -24.649 -63.240  1.00 42.70           O  
ANISOU 5361  OD1 ASP A 652     5753   5859   4612   -933    682   -993       O  
ATOM   5362  OD2 ASP A 652      -0.306 -26.413 -64.501  1.00 51.64           O  
ANISOU 5362  OD2 ASP A 652     6854   6972   5795  -1077    859  -1194       O  
ATOM   5363  N   LYS A 653      -2.499 -24.768 -67.195  1.00 41.14           N  
ANISOU 5363  N   LYS A 653     5614   6041   3977  -1339    786  -1135       N  
ATOM   5364  CA  LYS A 653      -1.826 -24.460 -68.457  1.00 43.72           C  
ANISOU 5364  CA  LYS A 653     5953   6436   4224  -1458    853  -1201       C  
ATOM   5365  C   LYS A 653      -2.369 -23.163 -69.078  1.00 42.91           C  
ANISOU 5365  C   LYS A 653     5882   6466   3955  -1501    765  -1095       C  
ATOM   5366  O   LYS A 653      -1.600 -22.330 -69.543  1.00 42.94           O  
ANISOU 5366  O   LYS A 653     5896   6492   3927  -1522    771  -1080       O  
ATOM   5367  CB  LYS A 653      -1.934 -25.638 -69.430  1.00 45.02           C  
ANISOU 5367  CB  LYS A 653     6115   6630   4358  -1599    971  -1347       C  
ATOM   5368  CG  LYS A 653      -0.831 -25.683 -70.477  1.00 50.85           C  
ANISOU 5368  CG  LYS A 653     6855   7377   5087  -1707   1087  -1458       C  
ATOM   5369  CD  LYS A 653      -0.842 -26.990 -71.289  1.00 54.00           C  
ANISOU 5369  CD  LYS A 653     7248   7779   5492  -1841   1225  -1623       C  
ATOM   5370  CE  LYS A 653       0.231 -26.961 -72.390  1.00 58.50           C  
ANISOU 5370  CE  LYS A 653     7823   8363   6040  -1963   1349  -1740       C  
ATOM   5371  NZ  LYS A 653       0.260 -28.192 -73.246  1.00 59.04           N  
ANISOU 5371  NZ  LYS A 653     7887   8436   6111  -2109   1500  -1914       N  
ATOM   5372  N   PHE A 654      -3.689 -22.986 -69.054  1.00 42.90           N  
ANISOU 5372  N   PHE A 654     5891   6548   3860  -1511    681  -1017       N  
ATOM   5373  CA  PHE A 654      -4.306 -21.749 -69.535  1.00 42.99           C  
ANISOU 5373  CA  PHE A 654     5922   6676   3736  -1539    584   -896       C  
ATOM   5374  C   PHE A 654      -3.791 -20.501 -68.790  1.00 42.72           C  
ANISOU 5374  C   PHE A 654     5886   6591   3755  -1417    513   -787       C  
ATOM   5375  O   PHE A 654      -3.445 -19.498 -69.418  1.00 41.22           O  
ANISOU 5375  O   PHE A 654     5711   6462   3490  -1455    489   -736       O  
ATOM   5376  CB  PHE A 654      -5.833 -21.833 -69.448  1.00 42.25           C  
ANISOU 5376  CB  PHE A 654     5826   6657   3569  -1551    502   -825       C  
ATOM   5377  CG  PHE A 654      -6.542 -20.695 -70.127  1.00 44.08           C  
ANISOU 5377  CG  PHE A 654     6068   7016   3663  -1604    407   -705       C  
ATOM   5378  CD1 PHE A 654      -6.889 -19.548 -69.419  1.00 44.58           C  
ANISOU 5378  CD1 PHE A 654     6122   7065   3750  -1494    304   -564       C  
ATOM   5379  CD2 PHE A 654      -6.858 -20.766 -71.474  1.00 45.82           C  
ANISOU 5379  CD2 PHE A 654     6307   7371   3732  -1769    420   -731       C  
ATOM   5380  CE1 PHE A 654      -7.540 -18.495 -70.043  1.00 44.65           C  
ANISOU 5380  CE1 PHE A 654     6132   7182   3651  -1540    216   -444       C  
ATOM   5381  CE2 PHE A 654      -7.509 -19.715 -72.106  1.00 48.83           C  
ANISOU 5381  CE2 PHE A 654     6694   7870   3991  -1821    322   -605       C  
ATOM   5382  CZ  PHE A 654      -7.850 -18.578 -71.386  1.00 46.60           C  
ANISOU 5382  CZ  PHE A 654     6394   7562   3751  -1701    219   -459       C  
ATOM   5383  N   ALA A 655      -3.737 -20.569 -67.461  1.00 41.39           N  
ANISOU 5383  N   ALA A 655     5702   6313   3711  -1278    481   -751       N  
ATOM   5384  CA  ALA A 655      -3.261 -19.436 -66.661  1.00 42.14           C  
ANISOU 5384  CA  ALA A 655     5796   6355   3861  -1165    419   -656       C  
ATOM   5385  C   ALA A 655      -1.798 -19.118 -66.937  1.00 42.47           C  
ANISOU 5385  C   ALA A 655     5837   6350   3949  -1169    478   -705       C  
ATOM   5386  O   ALA A 655      -1.430 -17.954 -67.098  1.00 42.71           O  
ANISOU 5386  O   ALA A 655     5876   6405   3945  -1154    439   -635       O  
ATOM   5387  CB  ALA A 655      -3.473 -19.691 -65.186  1.00 40.34           C  
ANISOU 5387  CB  ALA A 655     5557   6022   3750  -1033    382   -621       C  
ATOM   5388  N   ARG A 656      -0.977 -20.160 -67.016  1.00 43.76           N  
ANISOU 5388  N   ARG A 656     5986   6444   4197  -1193    577   -826       N  
ATOM   5389  CA  ARG A 656       0.458 -19.996 -67.198  1.00 45.90           C  
ANISOU 5389  CA  ARG A 656     6246   6654   4541  -1192    643   -884       C  
ATOM   5390  C   ARG A 656       0.854 -19.599 -68.626  1.00 47.07           C  
ANISOU 5390  C   ARG A 656     6414   6897   4573  -1326    697   -928       C  
ATOM   5391  O   ARG A 656       1.762 -18.788 -68.809  1.00 47.89           O  
ANISOU 5391  O   ARG A 656     6520   6989   4686  -1317    705   -913       O  
ATOM   5392  CB  ARG A 656       1.193 -21.261 -66.750  1.00 47.99           C  
ANISOU 5392  CB  ARG A 656     6477   6797   4958  -1167    730   -993       C  
ATOM   5393  CG  ARG A 656       2.678 -21.069 -66.450  1.00 54.63           C  
ANISOU 5393  CG  ARG A 656     7292   7538   5927  -1116    774  -1026       C  
ATOM   5394  CD  ARG A 656       3.305 -22.312 -65.807  1.00 59.58           C  
ANISOU 5394  CD  ARG A 656     7875   8032   6732  -1071    839  -1107       C  
ATOM   5395  NE  ARG A 656       3.263 -23.483 -66.685  1.00 63.58           N  
ANISOU 5395  NE  ARG A 656     8368   8545   7243  -1181    955  -1240       N  
ATOM   5396  CZ  ARG A 656       2.442 -24.519 -66.523  1.00 64.13           C  
ANISOU 5396  CZ  ARG A 656     8433   8607   7325  -1196    972  -1275       C  
ATOM   5397  NH1 ARG A 656       1.590 -24.548 -65.508  1.00 65.81           N  
ANISOU 5397  NH1 ARG A 656     8654   8806   7547  -1108    880  -1186       N  
ATOM   5398  NH2 ARG A 656       2.476 -25.531 -67.376  1.00 66.26           N  
ANISOU 5398  NH2 ARG A 656     8692   8883   7601  -1305   1088  -1405       N  
ATOM   5399  N   GLU A 657       0.176 -20.151 -69.631  1.00 47.49           N  
ANISOU 5399  N   GLU A 657     6483   7047   4513  -1456    734   -982       N  
ATOM   5400  CA  GLU A 657       0.558 -19.906 -71.031  1.00 48.71           C  
ANISOU 5400  CA  GLU A 657     6662   7298   4548  -1605    797  -1037       C  
ATOM   5401  C   GLU A 657      -0.162 -18.728 -71.699  1.00 47.44           C  
ANISOU 5401  C   GLU A 657     6533   7274   4220  -1662    703   -916       C  
ATOM   5402  O   GLU A 657       0.368 -18.129 -72.631  1.00 47.71           O  
ANISOU 5402  O   GLU A 657     6589   7372   4168  -1753    730   -922       O  
ATOM   5403  CB  GLU A 657       0.395 -21.175 -71.879  1.00 51.82           C  
ANISOU 5403  CB  GLU A 657     7058   7725   4906  -1742    906  -1180       C  
ATOM   5404  CG  GLU A 657       1.350 -22.306 -71.506  1.00 54.99           C  
ANISOU 5404  CG  GLU A 657     7423   7989   5481  -1713   1026  -1316       C  
ATOM   5405  CD  GLU A 657       1.287 -23.485 -72.464  1.00 60.81           C  
ANISOU 5405  CD  GLU A 657     8163   8757   6185  -1864   1154  -1471       C  
ATOM   5406  OE1 GLU A 657       0.239 -23.687 -73.122  1.00 62.30           O  
ANISOU 5406  OE1 GLU A 657     8380   9064   6229  -1968   1133  -1469       O  
ATOM   5407  OE2 GLU A 657       2.295 -24.220 -72.556  1.00 62.08           O  
ANISOU 5407  OE2 GLU A 657     8294   8821   6472  -1880   1279  -1598       O  
ATOM   5408  N   ARG A 658      -1.359 -18.397 -71.224  1.00 45.91           N  
ANISOU 5408  N   ARG A 658     6337   7118   3987  -1609    594   -803       N  
ATOM   5409  CA  ARG A 658      -2.164 -17.348 -71.851  1.00 46.07           C  
ANISOU 5409  CA  ARG A 658     6376   7265   3865  -1662    498   -678       C  
ATOM   5410  C   ARG A 658      -2.314 -16.119 -70.962  1.00 45.60           C  
ANISOU 5410  C   ARG A 658     6305   7165   3856  -1526    394   -533       C  
ATOM   5411  O   ARG A 658      -1.921 -15.016 -71.344  1.00 46.47           O  
ANISOU 5411  O   ARG A 658     6427   7309   3922  -1536    364   -462       O  
ATOM   5412  CB  ARG A 658      -3.545 -17.888 -72.239  1.00 46.09           C  
ANISOU 5412  CB  ARG A 658     6380   7363   3768  -1738    456   -659       C  
ATOM   5413  CG  ARG A 658      -3.503 -19.070 -73.199  1.00 50.82           C  
ANISOU 5413  CG  ARG A 658     6994   8016   4300  -1892    559   -804       C  
ATOM   5414  CD  ARG A 658      -3.466 -18.622 -74.656  1.00 55.98           C  
ANISOU 5414  CD  ARG A 658     7682   8812   4777  -2068    569   -802       C  
ATOM   5415  NE  ARG A 658      -3.091 -19.719 -75.547  1.00 61.91           N  
ANISOU 5415  NE  ARG A 658     8450   9593   5478  -2219    698   -969       N  
ATOM   5416  CZ  ARG A 658      -1.918 -19.820 -76.168  1.00 63.49           C  
ANISOU 5416  CZ  ARG A 658     8667   9775   5680  -2295    811  -1076       C  
ATOM   5417  NH1 ARG A 658      -0.990 -18.880 -76.015  1.00 64.48           N  
ANISOU 5417  NH1 ARG A 658     8795   9856   5848  -2233    805  -1030       N  
ATOM   5418  NH2 ARG A 658      -1.673 -20.860 -76.953  1.00 63.45           N  
ANISOU 5418  NH2 ARG A 658     8677   9795   5637  -2437    937  -1235       N  
ATOM   5419  N   MET A 659      -2.873 -16.318 -69.773  1.00 42.72           N  
ANISOU 5419  N   MET A 659     5920   6727   3586  -1404    347   -494       N  
ATOM   5420  CA  MET A 659      -3.211 -15.208 -68.884  1.00 41.89           C  
ANISOU 5420  CA  MET A 659     5804   6587   3527  -1282    252   -361       C  
ATOM   5421  C   MET A 659      -2.010 -14.462 -68.295  1.00 41.06           C  
ANISOU 5421  C   MET A 659     5698   6391   3513  -1194    266   -351       C  
ATOM   5422  O   MET A 659      -1.977 -13.225 -68.309  1.00 40.05           O  
ANISOU 5422  O   MET A 659     5573   6282   3365  -1164    209   -250       O  
ATOM   5423  CB  MET A 659      -4.143 -15.683 -67.779  1.00 40.69           C  
ANISOU 5423  CB  MET A 659     5634   6381   3444  -1189    210   -334       C  
ATOM   5424  CG  MET A 659      -5.491 -16.115 -68.306  1.00 42.48           C  
ANISOU 5424  CG  MET A 659     5856   6705   3580  -1265    172   -310       C  
ATOM   5425  SD  MET A 659      -6.654 -16.452 -66.996  1.00 45.52           S  
ANISOU 5425  SD  MET A 659     6219   7030   4046  -1153    116   -261       S  
ATOM   5426  CE  MET A 659      -6.983 -14.786 -66.415  1.00 44.27           C  
ANISOU 5426  CE  MET A 659     6047   6859   3913  -1056     20   -101       C  
ATOM   5427  N   GLU A 660      -1.031 -15.208 -67.790  1.00 40.64           N  
ANISOU 5427  N   GLU A 660     5638   6239   3565  -1154    339   -452       N  
ATOM   5428  CA  GLU A 660       0.156 -14.599 -67.193  1.00 40.78           C  
ANISOU 5428  CA  GLU A 660     5650   6168   3678  -1073    351   -449       C  
ATOM   5429  C   GLU A 660       0.933 -13.700 -68.171  1.00 41.14           C  
ANISOU 5429  C   GLU A 660     5709   6265   3657  -1143    373   -439       C  
ATOM   5430  O   GLU A 660       1.271 -12.573 -67.801  1.00 39.75           O  
ANISOU 5430  O   GLU A 660     5533   6065   3503  -1079    328   -359       O  
ATOM   5431  CB  GLU A 660       1.045 -15.645 -66.496  1.00 41.01           C  
ANISOU 5431  CB  GLU A 660     5660   6080   3842  -1024    421   -553       C  
ATOM   5432  CG  GLU A 660       0.498 -16.076 -65.118  1.00 44.27           C  
ANISOU 5432  CG  GLU A 660     6061   6414   4345   -913    373   -521       C  
ATOM   5433  CD  GLU A 660       1.351 -17.120 -64.387  1.00 46.57           C  
ANISOU 5433  CD  GLU A 660     6329   6589   4778   -864    429   -607       C  
ATOM   5434  OE1 GLU A 660       2.545 -17.300 -64.719  1.00 50.36           O  
ANISOU 5434  OE1 GLU A 660     6793   7023   5316   -885    497   -679       O  
ATOM   5435  OE2 GLU A 660       0.818 -17.762 -63.458  1.00 45.66           O  
ANISOU 5435  OE2 GLU A 660     6207   6421   4719   -803    404   -598       O  
ATOM   5436  N   PRO A 661       1.191 -14.170 -69.418  1.00 41.69           N  
ANISOU 5436  N   PRO A 661     5793   6406   3641  -1279    445   -520       N  
ATOM   5437  CA  PRO A 661       1.832 -13.284 -70.411  1.00 43.10           C  
ANISOU 5437  CA  PRO A 661     5991   6647   3738  -1359    464   -503       C  
ATOM   5438  C   PRO A 661       1.057 -11.990 -70.686  1.00 42.73           C  
ANISOU 5438  C   PRO A 661     5956   6683   3597  -1362    361   -350       C  
ATOM   5439  O   PRO A 661       1.668 -10.925 -70.835  1.00 43.44           O  
ANISOU 5439  O   PRO A 661     6053   6771   3683  -1349    347   -295       O  
ATOM   5440  CB  PRO A 661       1.882 -14.147 -71.681  1.00 43.16           C  
ANISOU 5440  CB  PRO A 661     6016   6734   3647  -1522    552   -613       C  
ATOM   5441  CG  PRO A 661       1.930 -15.532 -71.183  1.00 43.30           C  
ANISOU 5441  CG  PRO A 661     6013   6676   3761  -1499    617   -726       C  
ATOM   5442  CD  PRO A 661       1.100 -15.557 -69.919  1.00 42.58           C  
ANISOU 5442  CD  PRO A 661     5905   6531   3743  -1366    529   -646       C  
ATOM   5443  N   ALA A 662      -0.268 -12.086 -70.756  1.00 41.83           N  
ANISOU 5443  N   ALA A 662     5840   6638   3416  -1381    292   -281       N  
ATOM   5444  CA  ALA A 662      -1.114 -10.909 -70.944  1.00 41.39           C  
ANISOU 5444  CA  ALA A 662     5783   6650   3294  -1375    188   -126       C  
ATOM   5445  C   ALA A 662      -1.049  -9.981 -69.736  1.00 39.93           C  
ANISOU 5445  C   ALA A 662     5578   6371   3222  -1222    132    -39       C  
ATOM   5446  O   ALA A 662      -0.983  -8.758 -69.890  1.00 40.03           O  
ANISOU 5446  O   ALA A 662     5591   6401   3220  -1207     85     63       O  
ATOM   5447  CB  ALA A 662      -2.554 -11.320 -71.233  1.00 41.70           C  
ANISOU 5447  CB  ALA A 662     5814   6775   3256  -1426    129    -78       C  
ATOM   5448  N   ILE A 663      -1.063 -10.578 -68.541  1.00 38.31           N  
ANISOU 5448  N   ILE A 663     5359   6068   3129  -1117    141    -81       N  
ATOM   5449  CA  ILE A 663      -0.968  -9.847 -67.280  1.00 34.35           C  
ANISOU 5449  CA  ILE A 663     4844   5472   2736   -979     99    -19       C  
ATOM   5450  C   ILE A 663       0.340  -9.057 -67.223  1.00 34.67           C  
ANISOU 5450  C   ILE A 663     4891   5461   2822   -951    129    -26       C  
ATOM   5451  O   ILE A 663       0.346  -7.875 -66.861  1.00 35.11           O  
ANISOU 5451  O   ILE A 663     4942   5496   2903   -892     82     66       O  
ATOM   5452  CB  ILE A 663      -1.140 -10.811 -66.060  1.00 34.65           C  
ANISOU 5452  CB  ILE A 663     4872   5420   2873   -892    111    -76       C  
ATOM   5453  CG1 ILE A 663      -2.624 -11.143 -65.876  1.00 33.08           C  
ANISOU 5453  CG1 ILE A 663     4663   5263   2644   -891     57    -26       C  
ATOM   5454  CG2 ILE A 663      -0.545 -10.220 -64.765  1.00 29.75           C  
ANISOU 5454  CG2 ILE A 663     4247   4690   2368   -768     95    -51       C  
ATOM   5455  CD1 ILE A 663      -2.908 -12.225 -64.856  1.00 32.65           C  
ANISOU 5455  CD1 ILE A 663     4603   5136   2666   -830     74    -86       C  
ATOM   5456  N   ASP A 664       1.435  -9.708 -67.610  1.00 35.81           N  
ANISOU 5456  N   ASP A 664     5042   5583   2981   -997    212   -139       N  
ATOM   5457  CA  ASP A 664       2.749  -9.072 -67.667  1.00 37.26           C  
ANISOU 5457  CA  ASP A 664     5228   5720   3208   -983    251   -161       C  
ATOM   5458  C   ASP A 664       2.772  -7.871 -68.623  1.00 36.24           C  
ANISOU 5458  C   ASP A 664     5113   5670   2985  -1047    226    -77       C  
ATOM   5459  O   ASP A 664       3.307  -6.814 -68.278  1.00 35.84           O  
ANISOU 5459  O   ASP A 664     5060   5578   2978   -991    206    -21       O  
ATOM   5460  CB  ASP A 664       3.833 -10.096 -68.041  1.00 39.62           C  
ANISOU 5460  CB  ASP A 664     5524   5985   3543  -1036    353   -304       C  
ATOM   5461  CG  ASP A 664       4.005 -11.187 -66.980  1.00 47.09           C  
ANISOU 5461  CG  ASP A 664     6449   6833   4611   -958    375   -375       C  
ATOM   5462  OD1 ASP A 664       4.330 -12.338 -67.351  1.00 52.96           O  
ANISOU 5462  OD1 ASP A 664     7185   7564   5374  -1014    451   -486       O  
ATOM   5463  OD2 ASP A 664       3.813 -10.905 -65.775  1.00 48.77           O  
ANISOU 5463  OD2 ASP A 664     6652   6978   4899   -848    319   -321       O  
ATOM   5464  N   ARG A 665       2.178  -8.027 -69.805  1.00 34.44           N  
ANISOU 5464  N   ARG A 665     4902   5556   2629  -1169    223    -64       N  
ATOM   5465  CA  ARG A 665       2.127  -6.935 -70.785  1.00 34.97           C  
ANISOU 5465  CA  ARG A 665     4983   5707   2596  -1244    192     29       C  
ATOM   5466  C   ARG A 665       1.391  -5.728 -70.207  1.00 33.10           C  
ANISOU 5466  C   ARG A 665     4729   5457   2391  -1157     95    180       C  
ATOM   5467  O   ARG A 665       1.854  -4.591 -70.330  1.00 34.15           O  
ANISOU 5467  O   ARG A 665     4863   5580   2532  -1141     79    250       O  
ATOM   5468  CB  ARG A 665       1.476  -7.383 -72.104  1.00 35.95           C  
ANISOU 5468  CB  ARG A 665     5127   5965   2567  -1400    193     26       C  
ATOM   5469  CG  ARG A 665       2.307  -8.371 -72.910  1.00 41.09           C  
ANISOU 5469  CG  ARG A 665     5800   6638   3173  -1514    305   -126       C  
ATOM   5470  CD  ARG A 665       1.770  -8.571 -74.342  1.00 46.82           C  
ANISOU 5470  CD  ARG A 665     6556   7511   3723  -1691    307   -120       C  
ATOM   5471  NE  ARG A 665       0.432  -9.168 -74.378  1.00 49.82           N  
ANISOU 5471  NE  ARG A 665     6928   7954   4047  -1719    249    -87       N  
ATOM   5472  CZ  ARG A 665       0.179 -10.479 -74.334  1.00 52.73           C  
ANISOU 5472  CZ  ARG A 665     7295   8320   4420  -1752    303   -201       C  
ATOM   5473  NH1 ARG A 665       1.171 -11.363 -74.252  1.00 50.94           N  
ANISOU 5473  NH1 ARG A 665     7071   8024   4260  -1761    418   -355       N  
ATOM   5474  NH2 ARG A 665      -1.078 -10.909 -74.373  1.00 50.06           N  
ANISOU 5474  NH2 ARG A 665     6948   8044   4029  -1776    242   -158       N  
ATOM   5475  N   GLY A 666       0.250  -5.984 -69.571  1.00 29.44           N  
ANISOU 5475  N   GLY A 666     4246   4988   1952  -1102     37    228       N  
ATOM   5476  CA  GLY A 666      -0.519  -4.936 -68.917  1.00 28.76           C  
ANISOU 5476  CA  GLY A 666     4136   4875   1918  -1014    -43    360       C  
ATOM   5477  C   GLY A 666       0.253  -4.222 -67.816  1.00 29.42           C  
ANISOU 5477  C   GLY A 666     4212   4843   2121   -895    -32    361       C  
ATOM   5478  O   GLY A 666       0.106  -3.015 -67.626  1.00 31.79           O  
ANISOU 5478  O   GLY A 666     4500   5125   2454   -850    -74    464       O  
ATOM   5479  N   PHE A 667       1.082  -4.956 -67.081  1.00 28.43           N  
ANISOU 5479  N   PHE A 667     4093   4639   2069   -846     24    250       N  
ATOM   5480  CA  PHE A 667       1.868  -4.321 -66.023  1.00 27.34           C  
ANISOU 5480  CA  PHE A 667     3951   4398   2040   -744     31    249       C  
ATOM   5481  C   PHE A 667       3.110  -3.591 -66.544  1.00 29.43           C  
ANISOU 5481  C   PHE A 667     4226   4655   2303   -772     70    236       C  
ATOM   5482  O   PHE A 667       3.500  -2.573 -65.968  1.00 27.60           O  
ANISOU 5482  O   PHE A 667     3987   4365   2133   -706     55    284       O  
ATOM   5483  CB  PHE A 667       2.224  -5.308 -64.912  1.00 23.77           C  
ANISOU 5483  CB  PHE A 667     3496   3860   1674   -676     59    156       C  
ATOM   5484  CG  PHE A 667       1.179  -5.399 -63.819  1.00 23.92           C  
ANISOU 5484  CG  PHE A 667     3505   3842   1741   -596     11    199       C  
ATOM   5485  CD1 PHE A 667       0.709  -4.244 -63.181  1.00 20.99           C  
ANISOU 5485  CD1 PHE A 667     3125   3438   1411   -530    -35    294       C  
ATOM   5486  CD2 PHE A 667       0.690  -6.638 -63.407  1.00 21.04           C  
ANISOU 5486  CD2 PHE A 667     3141   3467   1387   -591     19    140       C  
ATOM   5487  CE1 PHE A 667      -0.239  -4.320 -62.160  1.00 20.48           C  
ANISOU 5487  CE1 PHE A 667     3052   3336   1394   -463    -68    325       C  
ATOM   5488  CE2 PHE A 667      -0.251  -6.728 -62.380  1.00 18.78           C  
ANISOU 5488  CE2 PHE A 667     2848   3145   1144   -522    -19    175       C  
ATOM   5489  CZ  PHE A 667      -0.719  -5.558 -61.759  1.00 22.21           C  
ANISOU 5489  CZ  PHE A 667     3274   3549   1615   -460    -61    266       C  
ATOM   5490  N   ARG A 668       3.717  -4.100 -67.622  1.00 29.42           N  
ANISOU 5490  N   ARG A 668     4239   4708   2231   -874    125    167       N  
ATOM   5491  CA  ARG A 668       4.839  -3.403 -68.263  1.00 34.26           C  
ANISOU 5491  CA  ARG A 668     4863   5323   2830   -917    167    156       C  
ATOM   5492  C   ARG A 668       4.382  -2.046 -68.805  1.00 35.27           C  
ANISOU 5492  C   ARG A 668     4993   5503   2905   -938    112    293       C  
ATOM   5493  O   ARG A 668       5.107  -1.056 -68.707  1.00 36.10           O  
ANISOU 5493  O   ARG A 668     5097   5569   3049   -909    118    325       O  
ATOM   5494  CB  ARG A 668       5.471  -4.234 -69.394  1.00 35.60           C  
ANISOU 5494  CB  ARG A 668     5050   5549   2926  -1039    246     52       C  
ATOM   5495  CG  ARG A 668       6.142  -5.523 -68.939  1.00 40.78           C  
ANISOU 5495  CG  ARG A 668     5696   6140   3659  -1021    315    -88       C  
ATOM   5496  CD  ARG A 668       7.221  -6.014 -69.902  1.00 44.89           C  
ANISOU 5496  CD  ARG A 668     6225   6676   4154  -1122    416   -201       C  
ATOM   5497  NE  ARG A 668       6.758  -6.153 -71.283  1.00 53.43           N  
ANISOU 5497  NE  ARG A 668     7335   7880   5086  -1267    435   -200       N  
ATOM   5498  CZ  ARG A 668       6.202  -7.250 -71.799  1.00 56.66           C  
ANISOU 5498  CZ  ARG A 668     7752   8344   5432  -1348    465   -266       C  
ATOM   5499  NH1 ARG A 668       6.015  -8.335 -71.048  1.00 55.34           N  
ANISOU 5499  NH1 ARG A 668     7565   8116   5347  -1292    481   -336       N  
ATOM   5500  NH2 ARG A 668       5.827  -7.255 -73.074  1.00 54.35           N  
ANISOU 5500  NH2 ARG A 668     7490   8170   4992  -1492    478   -258       N  
ATOM   5501  N   GLU A 669       3.177  -2.013 -69.372  1.00 35.81           N  
ANISOU 5501  N   GLU A 669     5060   5656   2891   -988     55    376       N  
ATOM   5502  CA  GLU A 669       2.570  -0.765 -69.845  1.00 37.66           C  
ANISOU 5502  CA  GLU A 669     5284   5935   3088  -1004    -11    525       C  
ATOM   5503  C   GLU A 669       2.348   0.216 -68.685  1.00 35.69           C  
ANISOU 5503  C   GLU A 669     5009   5592   2960   -874    -51    601       C  
ATOM   5504  O   GLU A 669       2.557   1.420 -68.838  1.00 35.13           O  
ANISOU 5504  O   GLU A 669     4931   5508   2909   -862    -69    688       O  
ATOM   5505  CB  GLU A 669       1.253  -1.043 -70.590  1.00 38.34           C  
ANISOU 5505  CB  GLU A 669     5365   6127   3077  -1081    -73    602       C  
ATOM   5506  CG  GLU A 669       0.621   0.186 -71.259  1.00 44.08           C  
ANISOU 5506  CG  GLU A 669     6076   6910   3761  -1116   -147    768       C  
ATOM   5507  CD  GLU A 669      -0.738  -0.111 -71.892  1.00 48.88           C  
ANISOU 5507  CD  GLU A 669     6669   7619   4285  -1186   -221    853       C  
ATOM   5508  OE1 GLU A 669      -0.818  -1.022 -72.744  1.00 53.77           O  
ANISOU 5508  OE1 GLU A 669     7313   8330   4788  -1302   -201    792       O  
ATOM   5509  OE2 GLU A 669      -1.726   0.573 -71.547  1.00 50.11           O  
ANISOU 5509  OE2 GLU A 669     6783   7761   4494  -1130   -296    979       O  
ATOM   5510  N   MET A 670       1.937  -0.305 -67.529  1.00 32.57           N  
ANISOU 5510  N   MET A 670     4601   5131   2644   -784    -58    564       N  
ATOM   5511  CA  MET A 670       1.696   0.539 -66.363  1.00 31.37           C  
ANISOU 5511  CA  MET A 670     4428   4889   2603   -671    -85    620       C  
ATOM   5512  C   MET A 670       2.999   1.145 -65.838  1.00 31.06           C  
ANISOU 5512  C   MET A 670     4398   4770   2634   -623    -41    576       C  
ATOM   5513  O   MET A 670       3.043   2.325 -65.462  1.00 30.21           O  
ANISOU 5513  O   MET A 670     4277   4615   2586   -573    -57    649       O  
ATOM   5514  CB  MET A 670       0.988  -0.249 -65.259  1.00 31.57           C  
ANISOU 5514  CB  MET A 670     4444   4868   2684   -601    -97    581       C  
ATOM   5515  CG  MET A 670       0.439   0.626 -64.149  1.00 31.97           C  
ANISOU 5515  CG  MET A 670     4472   4840   2833   -502   -125    648       C  
ATOM   5516  SD  MET A 670      -0.153  -0.334 -62.758  1.00 31.82           S  
ANISOU 5516  SD  MET A 670     4454   4760   2877   -427   -124    583       S  
ATOM   5517  CE  MET A 670       1.375  -0.778 -61.947  1.00 29.53           C  
ANISOU 5517  CE  MET A 670     4191   4392   2637   -390    -71    463       C  
ATOM   5518  N   CYS A 671       4.051   0.330 -65.819  1.00 31.28           N  
ANISOU 5518  N   CYS A 671     4443   4779   2663   -640     15    457       N  
ATOM   5519  CA  CYS A 671       5.382   0.780 -65.434  1.00 32.57           C  
ANISOU 5519  CA  CYS A 671     4611   4874   2890   -608     58    407       C  
ATOM   5520  C   CYS A 671       5.844   1.963 -66.315  1.00 32.28           C  
ANISOU 5520  C   CYS A 671     4579   4867   2819   -654     63    475       C  
ATOM   5521  O   CYS A 671       6.319   2.981 -65.801  1.00 32.09           O  
ANISOU 5521  O   CYS A 671     4548   4781   2864   -600     64    509       O  
ATOM   5522  CB  CYS A 671       6.374  -0.387 -65.502  1.00 31.40           C  
ANISOU 5522  CB  CYS A 671     4472   4711   2748   -636    119    273       C  
ATOM   5523  SG  CYS A 671       8.100   0.047 -65.162  1.00 36.49           S  
ANISOU 5523  SG  CYS A 671     5114   5276   3475   -608    173    205       S  
ATOM   5524  N   GLU A 672       5.686   1.826 -67.628  1.00 32.63           N  
ANISOU 5524  N   GLU A 672     4635   5006   2756   -761     68    496       N  
ATOM   5525  CA  GLU A 672       6.058   2.892 -68.570  1.00 34.70           C  
ANISOU 5525  CA  GLU A 672     4906   5308   2971   -820     69    570       C  
ATOM   5526  C   GLU A 672       5.238   4.160 -68.344  1.00 32.54           C  
ANISOU 5526  C   GLU A 672     4610   5020   2736   -772      6    717       C  
ATOM   5527  O   GLU A 672       5.779   5.263 -68.343  1.00 32.50           O  
ANISOU 5527  O   GLU A 672     4600   4976   2771   -753     13    766       O  
ATOM   5528  CB  GLU A 672       5.918   2.417 -70.017  1.00 38.02           C  
ANISOU 5528  CB  GLU A 672     5349   5844   3253   -959     81    568       C  
ATOM   5529  CG  GLU A 672       6.914   1.331 -70.415  1.00 46.64           C  
ANISOU 5529  CG  GLU A 672     6460   6945   4314  -1022    166    417       C  
ATOM   5530  CD  GLU A 672       7.158   1.268 -71.919  1.00 57.13           C  
ANISOU 5530  CD  GLU A 672     7819   8378   5508  -1172    200    412       C  
ATOM   5531  OE1 GLU A 672       7.176   0.144 -72.471  1.00 59.88           O  
ANISOU 5531  OE1 GLU A 672     8184   8778   5791  -1254    245    317       O  
ATOM   5532  OE2 GLU A 672       7.335   2.339 -72.550  1.00 59.92           O  
ANISOU 5532  OE2 GLU A 672     8183   8764   5822  -1214    185    501       O  
ATOM   5533  N   TYR A 673       3.937   3.981 -68.134  1.00 30.96           N  
ANISOU 5533  N   TYR A 673     4389   4841   2532   -752    -52    784       N  
ATOM   5534  CA  TYR A 673       3.004   5.068 -67.843  1.00 30.17           C  
ANISOU 5534  CA  TYR A 673     4257   4717   2490   -700   -111    921       C  
ATOM   5535  C   TYR A 673       3.450   5.898 -66.641  1.00 30.28           C  
ANISOU 5535  C   TYR A 673     4257   4614   2634   -592    -91    915       C  
ATOM   5536  O   TYR A 673       3.450   7.128 -66.691  1.00 31.73           O  
ANISOU 5536  O   TYR A 673     4423   4765   2867   -572   -103   1007       O  
ATOM   5537  CB  TYR A 673       1.612   4.474 -67.612  1.00 28.95           C  
ANISOU 5537  CB  TYR A 673     4079   4592   2329   -686   -163    959       C  
ATOM   5538  CG  TYR A 673       0.468   5.453 -67.481  1.00 32.15           C  
ANISOU 5538  CG  TYR A 673     4439   4982   2794   -647   -226   1107       C  
ATOM   5539  CD1 TYR A 673       0.450   6.648 -68.198  1.00 34.71           C  
ANISOU 5539  CD1 TYR A 673     4746   5324   3120   -678   -255   1234       C  
ATOM   5540  CD2 TYR A 673      -0.630   5.154 -66.669  1.00 31.52           C  
ANISOU 5540  CD2 TYR A 673     4330   4870   2776   -584   -255   1124       C  
ATOM   5541  CE1 TYR A 673      -0.611   7.538 -68.088  1.00 35.49           C  
ANISOU 5541  CE1 TYR A 673     4793   5400   3293   -640   -312   1375       C  
ATOM   5542  CE2 TYR A 673      -1.709   6.033 -66.563  1.00 33.92           C  
ANISOU 5542  CE2 TYR A 673     4583   5154   3151   -549   -307   1258       C  
ATOM   5543  CZ  TYR A 673      -1.687   7.225 -67.280  1.00 35.14           C  
ANISOU 5543  CZ  TYR A 673     4715   5319   3318   -576   -336   1385       C  
ATOM   5544  OH  TYR A 673      -2.737   8.108 -67.185  1.00 37.54           O  
ANISOU 5544  OH  TYR A 673     4958   5593   3712   -540   -386   1523       O  
ATOM   5545  N   MET A 674       3.848   5.216 -65.573  1.00 29.06           N  
ANISOU 5545  N   MET A 674     4113   4396   2534   -530    -60    806       N  
ATOM   5546  CA  MET A 674       4.298   5.875 -64.354  1.00 29.03           C  
ANISOU 5546  CA  MET A 674     4102   4286   2640   -439    -40    785       C  
ATOM   5547  C   MET A 674       5.779   6.255 -64.386  1.00 28.34           C  
ANISOU 5547  C   MET A 674     4032   4163   2573   -445     10    723       C  
ATOM   5548  O   MET A 674       6.279   6.886 -63.444  1.00 27.82           O  
ANISOU 5548  O   MET A 674     3963   4014   2593   -381     27    705       O  
ATOM   5549  CB  MET A 674       3.982   5.002 -63.126  1.00 27.90           C  
ANISOU 5549  CB  MET A 674     3963   4094   2544   -376    -39    709       C  
ATOM   5550  CG  MET A 674       2.490   4.940 -62.787  1.00 30.38           C  
ANISOU 5550  CG  MET A 674     4253   4415   2876   -347    -83    777       C  
ATOM   5551  SD  MET A 674       1.822   6.498 -62.126  1.00 34.47           S  
ANISOU 5551  SD  MET A 674     4736   4856   3506   -278    -96    885       S  
ATOM   5552  CE  MET A 674       0.569   6.828 -63.359  1.00 33.19           C  
ANISOU 5552  CE  MET A 674     4535   4776   3298   -333   -155   1029       C  
ATOM   5553  N   ASN A 675       6.468   5.885 -65.471  1.00 28.31           N  
ANISOU 5553  N   ASN A 675     4046   4222   2489   -528     36    689       N  
ATOM   5554  CA  ASN A 675       7.911   6.132 -65.632  1.00 26.61           C  
ANISOU 5554  CA  ASN A 675     3844   3979   2289   -545     90    622       C  
ATOM   5555  C   ASN A 675       8.744   5.541 -64.484  1.00 27.12           C  
ANISOU 5555  C   ASN A 675     3910   3965   2430   -483    120    508       C  
ATOM   5556  O   ASN A 675       9.743   6.121 -64.051  1.00 24.84           O  
ANISOU 5556  O   ASN A 675     3620   3616   2203   -455    147    478       O  
ATOM   5557  CB  ASN A 675       8.214   7.634 -65.807  1.00 23.99           C  
ANISOU 5557  CB  ASN A 675     3504   3616   1995   -536     92    708       C  
ATOM   5558  CG  ASN A 675       9.582   7.885 -66.446  1.00 26.65           C  
ANISOU 5558  CG  ASN A 675     3856   3955   2313   -587    147    656       C  
ATOM   5559  OD1 ASN A 675      10.019   7.130 -67.315  1.00 24.52           O  
ANISOU 5559  OD1 ASN A 675     3604   3747   1967   -666    178    598       O  
ATOM   5560  ND2 ASN A 675      10.255   8.949 -66.021  1.00 23.11           N  
ANISOU 5560  ND2 ASN A 675     3401   3440   1940   -547    165    673       N  
ATOM   5561  N   ASN A 676       8.322   4.383 -63.990  1.00 26.69           N  
ANISOU 5561  N   ASN A 676     3856   3912   2373   -466    109    451       N  
ATOM   5562  CA  ASN A 676       8.999   3.756 -62.861  1.00 26.18           C  
ANISOU 5562  CA  ASN A 676     3790   3776   2381   -409    124    359       C  
ATOM   5563  C   ASN A 676      10.391   3.263 -63.217  1.00 27.77           C  
ANISOU 5563  C   ASN A 676     3991   3965   2594   -444    177    263       C  
ATOM   5564  O   ASN A 676      10.714   3.081 -64.400  1.00 26.55           O  
ANISOU 5564  O   ASN A 676     3843   3868   2376   -523    212    246       O  
ATOM   5565  CB  ASN A 676       8.148   2.634 -62.273  1.00 25.39           C  
ANISOU 5565  CB  ASN A 676     3690   3680   2277   -385     99    331       C  
ATOM   5566  CG  ASN A 676       6.825   3.134 -61.727  1.00 23.51           C  
ANISOU 5566  CG  ASN A 676     3446   3436   2049   -341     53    416       C  
ATOM   5567  OD1 ASN A 676       5.798   2.490 -61.907  1.00 27.59           O  
ANISOU 5567  OD1 ASN A 676     3961   3996   2524   -354     28    435       O  
ATOM   5568  ND2 ASN A 676       6.844   4.286 -61.054  1.00 20.98           N  
ANISOU 5568  ND2 ASN A 676     3122   3060   1792   -291     46    465       N  
ATOM   5569  N   LYS A 677      11.212   3.074 -62.188  1.00 28.23           N  
ANISOU 5569  N   LYS A 677     4041   3949   2737   -391    184    202       N  
ATOM   5570  CA  LYS A 677      12.623   2.739 -62.366  1.00 29.62           C  
ANISOU 5570  CA  LYS A 677     4205   4095   2955   -412    232    116       C  
ATOM   5571  C   LYS A 677      12.846   1.305 -62.858  1.00 29.54           C  
ANISOU 5571  C   LYS A 677     4186   4107   2929   -456    266     30       C  
ATOM   5572  O   LYS A 677      13.781   1.049 -63.611  1.00 30.73           O  
ANISOU 5572  O   LYS A 677     4328   4264   3083   -509    323    -33       O  
ATOM   5573  CB  LYS A 677      13.384   2.984 -61.055  1.00 31.10           C  
ANISOU 5573  CB  LYS A 677     4379   4195   3241   -343    217     87       C  
ATOM   5574  CG  LYS A 677      14.898   2.854 -61.159  1.00 34.16           C  
ANISOU 5574  CG  LYS A 677     4744   4542   3692   -358    260     12       C  
ATOM   5575  CD  LYS A 677      15.579   3.204 -59.838  1.00 37.50           C  
ANISOU 5575  CD  LYS A 677     5155   4888   4206   -296    232     -1       C  
ATOM   5576  CE  LYS A 677      17.078   2.935 -59.895  1.00 40.33           C  
ANISOU 5576  CE  LYS A 677     5480   5202   4641   -309    268    -76       C  
ATOM   5577  NZ  LYS A 677      17.368   1.466 -59.948  1.00 44.08           N  
ANISOU 5577  NZ  LYS A 677     5930   5666   5152   -320    283   -148       N  
ATOM   5578  N   GLN A 678      11.991   0.377 -62.432  1.00 29.43           N  
ANISOU 5578  N   GLN A 678     4175   4102   2906   -437    238     22       N  
ATOM   5579  CA  GLN A 678      12.177  -1.047 -62.732  1.00 29.85           C  
ANISOU 5579  CA  GLN A 678     4217   4162   2963   -471    272    -64       C  
ATOM   5580  C   GLN A 678      10.827  -1.759 -62.666  1.00 30.20           C  
ANISOU 5580  C   GLN A 678     4274   4249   2952   -471    239    -39       C  
ATOM   5581  O   GLN A 678      10.053  -1.533 -61.738  1.00 30.10           O  
ANISOU 5581  O   GLN A 678     4268   4216   2953   -411    186     13       O  
ATOM   5582  CB  GLN A 678      13.160  -1.654 -61.718  1.00 30.24           C  
ANISOU 5582  CB  GLN A 678     4238   4123   3127   -419    275   -130       C  
ATOM   5583  CG  GLN A 678      13.725  -3.029 -62.065  1.00 34.15           C  
ANISOU 5583  CG  GLN A 678     4708   4602   3666   -453    327   -228       C  
ATOM   5584  CD  GLN A 678      14.527  -3.642 -60.912  1.00 34.37           C  
ANISOU 5584  CD  GLN A 678     4702   4539   3820   -392    309   -269       C  
ATOM   5585  OE1 GLN A 678      14.769  -2.998 -59.893  1.00 35.23           O  
ANISOU 5585  OE1 GLN A 678     4811   4603   3973   -334    260   -229       O  
ATOM   5586  NE2 GLN A 678      14.933  -4.894 -61.074  1.00 35.58           N  
ANISOU 5586  NE2 GLN A 678     4824   4663   4032   -411    349   -346       N  
ATOM   5587  N   HIS A 679      10.534  -2.602 -63.654  1.00 29.39           N  
ANISOU 5587  N   HIS A 679     4175   4206   2786   -545    274    -80       N  
ATOM   5588  CA  HIS A 679       9.287  -3.379 -63.652  1.00 28.24           C  
ANISOU 5588  CA  HIS A 679     4038   4103   2588   -554    247    -66       C  
ATOM   5589  C   HIS A 679       9.361  -4.558 -62.668  1.00 27.76           C  
ANISOU 5589  C   HIS A 679     3961   3978   2607   -503    244   -127       C  
ATOM   5590  O   HIS A 679      10.172  -5.476 -62.830  1.00 26.28           O  
ANISOU 5590  O   HIS A 679     3755   3760   2472   -525    295   -216       O  
ATOM   5591  CB  HIS A 679       8.915  -3.853 -65.069  1.00 28.54           C  
ANISOU 5591  CB  HIS A 679     4088   4234   2522   -662    285    -89       C  
ATOM   5592  CG  HIS A 679       7.965  -5.012 -65.085  1.00 27.89           C  
ANISOU 5592  CG  HIS A 679     4007   4183   2406   -681    278   -116       C  
ATOM   5593  ND1 HIS A 679       6.683  -4.930 -64.585  1.00 24.27           N  
ANISOU 5593  ND1 HIS A 679     3555   3744   1922   -642    214    -42       N  
ATOM   5594  CD2 HIS A 679       8.117  -6.283 -65.526  1.00 26.61           C  
ANISOU 5594  CD2 HIS A 679     3840   4030   2242   -735    334   -212       C  
ATOM   5595  CE1 HIS A 679       6.087  -6.101 -64.713  1.00 23.56           C  
ANISOU 5595  CE1 HIS A 679     3465   3679   1810   -671    225    -90       C  
ATOM   5596  NE2 HIS A 679       6.933  -6.939 -65.287  1.00 28.18           N  
ANISOU 5596  NE2 HIS A 679     4043   4257   2408   -728    298   -193       N  
ATOM   5597  N   LEU A 680       8.524  -4.510 -61.636  1.00 28.33           N  
ANISOU 5597  N   LEU A 680     4040   4028   2696   -438    186    -77       N  
ATOM   5598  CA  LEU A 680       8.532  -5.537 -60.594  1.00 26.94           C  
ANISOU 5598  CA  LEU A 680     3854   3791   2591   -389    172   -118       C  
ATOM   5599  C   LEU A 680       7.134  -5.972 -60.166  1.00 26.39           C  
ANISOU 5599  C   LEU A 680     3799   3746   2484   -370    131    -80       C  
ATOM   5600  O   LEU A 680       6.958  -6.613 -59.124  1.00 25.70           O  
ANISOU 5600  O   LEU A 680     3709   3607   2447   -322    108    -92       O  
ATOM   5601  CB  LEU A 680       9.351  -5.071 -59.391  1.00 26.59           C  
ANISOU 5601  CB  LEU A 680     3802   3664   2637   -319    145   -110       C  
ATOM   5602  CG  LEU A 680      10.862  -4.967 -59.613  1.00 28.84           C  
ANISOU 5602  CG  LEU A 680     4061   3905   2990   -330    185   -164       C  
ATOM   5603  CD1 LEU A 680      11.503  -4.131 -58.504  1.00 23.32           C  
ANISOU 5603  CD1 LEU A 680     3360   3144   2355   -270    147   -134       C  
ATOM   5604  CD2 LEU A 680      11.511  -6.368 -59.728  1.00 26.96           C  
ANISOU 5604  CD2 LEU A 680     3792   3630   2823   -348    227   -253       C  
ATOM   5605  N   MET A 681       6.136  -5.629 -60.972  1.00 27.46           N  
ANISOU 5605  N   MET A 681     3945   3959   2529   -412    121    -31       N  
ATOM   5606  CA  MET A 681       4.783  -6.103 -60.712  1.00 28.81           C  
ANISOU 5606  CA  MET A 681     4123   4158   2664   -403     88      1       C  
ATOM   5607  C   MET A 681       4.632  -7.502 -61.311  1.00 29.36           C  
ANISOU 5607  C   MET A 681     4187   4257   2710   -459    125    -75       C  
ATOM   5608  O   MET A 681       4.282  -7.655 -62.485  1.00 30.94           O  
ANISOU 5608  O   MET A 681     4391   4536   2830   -538    147    -82       O  
ATOM   5609  CB  MET A 681       3.737  -5.118 -61.253  1.00 28.57           C  
ANISOU 5609  CB  MET A 681     4098   4195   2563   -421     53     96       C  
ATOM   5610  CG  MET A 681       3.763  -3.721 -60.599  1.00 26.28           C  
ANISOU 5610  CG  MET A 681     3809   3866   2310   -363     22    171       C  
ATOM   5611  SD  MET A 681       3.263  -3.699 -58.853  1.00 27.86           S  
ANISOU 5611  SD  MET A 681     4016   3986   2584   -271    -12    186       S  
ATOM   5612  CE  MET A 681       4.849  -3.569 -58.031  1.00 22.43           C  
ANISOU 5612  CE  MET A 681     3332   3216   1976   -235      6    131       C  
ATOM   5613  N   PHE A 682       4.926  -8.517 -60.497  1.00 30.40           N  
ANISOU 5613  N   PHE A 682     4310   4324   2915   -424    134   -131       N  
ATOM   5614  CA  PHE A 682       4.897  -9.912 -60.940  1.00 30.95           C  
ANISOU 5614  CA  PHE A 682     4370   4402   2989   -470    179   -212       C  
ATOM   5615  C   PHE A 682       3.676 -10.637 -60.379  1.00 31.01           C  
ANISOU 5615  C   PHE A 682     4384   4415   2983   -449    148   -196       C  
ATOM   5616  O   PHE A 682       3.674 -11.060 -59.226  1.00 28.53           O  
ANISOU 5616  O   PHE A 682     4069   4033   2736   -388    125   -196       O  
ATOM   5617  CB  PHE A 682       6.186 -10.652 -60.535  1.00 32.47           C  
ANISOU 5617  CB  PHE A 682     4537   4508   3291   -450    219   -290       C  
ATOM   5618  CG  PHE A 682       7.460 -10.053 -61.101  1.00 33.09           C  
ANISOU 5618  CG  PHE A 682     4603   4574   3396   -474    260   -318       C  
ATOM   5619  CD1 PHE A 682       7.493  -9.498 -62.384  1.00 33.08           C  
ANISOU 5619  CD1 PHE A 682     4611   4649   3307   -551    294   -321       C  
ATOM   5620  CD2 PHE A 682       8.639 -10.079 -60.356  1.00 33.60           C  
ANISOU 5620  CD2 PHE A 682     4643   4551   3573   -425    262   -342       C  
ATOM   5621  CE1 PHE A 682       8.672  -8.956 -62.907  1.00 33.69           C  
ANISOU 5621  CE1 PHE A 682     4679   4714   3409   -576    338   -350       C  
ATOM   5622  CE2 PHE A 682       9.825  -9.544 -60.868  1.00 34.99           C  
ANISOU 5622  CE2 PHE A 682     4802   4712   3781   -446    302   -372       C  
ATOM   5623  CZ  PHE A 682       9.842  -8.983 -62.152  1.00 35.15           C  
ANISOU 5623  CZ  PHE A 682     4836   4806   3713   -522    344   -380       C  
ATOM   5624  N   MET A 683       2.636 -10.778 -61.199  1.00 32.62           N  
ANISOU 5624  N   MET A 683     4595   4702   3097   -507    146   -180       N  
ATOM   5625  CA  MET A 683       1.397 -11.419 -60.764  1.00 32.28           C  
ANISOU 5625  CA  MET A 683     4556   4672   3036   -494    118   -163       C  
ATOM   5626  C   MET A 683       1.255 -12.854 -61.290  1.00 34.95           C  
ANISOU 5626  C   MET A 683     4886   5025   3367   -552    168   -250       C  
ATOM   5627  O   MET A 683       0.938 -13.079 -62.458  1.00 35.02           O  
ANISOU 5627  O   MET A 683     4897   5114   3297   -639    196   -275       O  
ATOM   5628  CB  MET A 683       0.194 -10.557 -61.146  1.00 31.04           C  
ANISOU 5628  CB  MET A 683     4405   4590   2797   -508     70    -73       C  
ATOM   5629  CG  MET A 683      -1.144 -11.172 -60.812  1.00 28.98           C  
ANISOU 5629  CG  MET A 683     4144   4351   2517   -502     43    -54       C  
ATOM   5630  SD  MET A 683      -2.542 -10.118 -61.229  1.00 28.07           S  
ANISOU 5630  SD  MET A 683     4020   4313   2331   -515    -18     61       S  
ATOM   5631  CE  MET A 683      -2.901  -9.401 -59.620  1.00 24.00           C  
ANISOU 5631  CE  MET A 683     3508   3712   1900   -404    -55    120       C  
ATOM   5632  N   ASP A 684       1.495 -13.816 -60.406  1.00 36.96           N  
ANISOU 5632  N   ASP A 684     5133   5202   3709   -508    179   -294       N  
ATOM   5633  CA  ASP A 684       1.425 -15.235 -60.747  1.00 40.01           C  
ANISOU 5633  CA  ASP A 684     5506   5580   4115   -554    233   -380       C  
ATOM   5634  C   ASP A 684       0.069 -15.801 -60.376  1.00 39.42           C  
ANISOU 5634  C   ASP A 684     5440   5529   4008   -547    203   -357       C  
ATOM   5635  O   ASP A 684      -0.629 -15.252 -59.517  1.00 40.41           O  
ANISOU 5635  O   ASP A 684     5578   5645   4131   -488    144   -283       O  
ATOM   5636  CB  ASP A 684       2.494 -16.024 -59.981  1.00 42.43           C  
ANISOU 5636  CB  ASP A 684     5791   5778   4552   -508    261   -434       C  
ATOM   5637  CG  ASP A 684       3.897 -15.814 -60.526  1.00 50.63           C  
ANISOU 5637  CG  ASP A 684     6809   6788   5639   -531    312   -485       C  
ATOM   5638  OD1 ASP A 684       4.043 -15.200 -61.609  1.00 53.25           O  
ANISOU 5638  OD1 ASP A 684     7149   7190   5895   -595    339   -494       O  
ATOM   5639  OD2 ASP A 684       4.857 -16.277 -59.864  1.00 54.71           O  
ANISOU 5639  OD2 ASP A 684     7300   7211   6276   -488    325   -515       O  
ATOM   5640  N   ARG A 685      -0.288 -16.918 -60.998  1.00 37.64           N  
ANISOU 5640  N   ARG A 685     5207   5329   3766   -611    251   -427       N  
ATOM   5641  CA  ARG A 685      -1.481 -17.654 -60.607  1.00 36.05           C  
ANISOU 5641  CA  ARG A 685     5009   5138   3550   -607    233   -420       C  
ATOM   5642  C   ARG A 685      -1.287 -18.222 -59.202  1.00 34.62           C  
ANISOU 5642  C   ARG A 685     4826   4852   3475   -522    216   -416       C  
ATOM   5643  O   ARG A 685      -0.212 -18.729 -58.880  1.00 34.26           O  
ANISOU 5643  O   ARG A 685     4764   4728   3524   -501    248   -462       O  
ATOM   5644  CB  ARG A 685      -1.769 -18.773 -61.612  1.00 34.90           C  
ANISOU 5644  CB  ARG A 685     4855   5037   3367   -701    298   -509       C  
ATOM   5645  CG  ARG A 685      -3.153 -19.407 -61.478  1.00 33.63           C  
ANISOU 5645  CG  ARG A 685     4699   4914   3166   -717    278   -499       C  
ATOM   5646  CD  ARG A 685      -3.145 -20.588 -60.512  1.00 35.24           C  
ANISOU 5646  CD  ARG A 685     4893   5023   3472   -669    298   -540       C  
ATOM   5647  NE  ARG A 685      -2.324 -21.691 -61.006  1.00 31.47           N  
ANISOU 5647  NE  ARG A 685     4395   4502   3058   -717    386   -649       N  
ATOM   5648  CZ  ARG A 685      -1.989 -22.757 -60.291  1.00 30.27           C  
ANISOU 5648  CZ  ARG A 685     4227   4254   3022   -681    416   -692       C  
ATOM   5649  NH1 ARG A 685      -2.397 -22.884 -59.027  1.00 29.64           N  
ANISOU 5649  NH1 ARG A 685     4155   4116   2991   -600    363   -634       N  
ATOM   5650  NH2 ARG A 685      -1.237 -23.696 -60.839  1.00 24.57           N  
ANISOU 5650  NH2 ARG A 685     3478   3488   2368   -729    504   -793       N  
ATOM   5651  N   GLU A 686      -2.323 -18.120 -58.372  1.00 33.50           N  
ANISOU 5651  N   GLU A 686     4699   4709   3320   -478    165   -357       N  
ATOM   5652  CA  GLU A 686      -2.294 -18.687 -57.029  1.00 35.09           C  
ANISOU 5652  CA  GLU A 686     4906   4823   3604   -411    146   -347       C  
ATOM   5653  C   GLU A 686      -3.183 -19.926 -56.897  1.00 34.53           C  
ANISOU 5653  C   GLU A 686     4833   4748   3541   -431    165   -383       C  
ATOM   5654  O   GLU A 686      -2.668 -21.037 -56.776  1.00 34.64           O  
ANISOU 5654  O   GLU A 686     4831   4701   3630   -437    207   -443       O  
ATOM   5655  CB  GLU A 686      -2.658 -17.640 -55.975  1.00 37.22           C  
ANISOU 5655  CB  GLU A 686     5199   5077   3867   -345     82   -260       C  
ATOM   5656  CG  GLU A 686      -1.469 -17.153 -55.154  1.00 48.03           C  
ANISOU 5656  CG  GLU A 686     6571   6373   5304   -292     63   -242       C  
ATOM   5657  CD  GLU A 686      -1.852 -16.810 -53.715  1.00 54.39           C  
ANISOU 5657  CD  GLU A 686     7404   7133   6129   -232     13   -183       C  
ATOM   5658  OE1 GLU A 686      -1.155 -15.984 -53.076  1.00 55.97           O  
ANISOU 5658  OE1 GLU A 686     7614   7298   6352   -195    -15   -149       O  
ATOM   5659  OE2 GLU A 686      -2.859 -17.370 -53.225  1.00 59.70           O  
ANISOU 5659  OE2 GLU A 686     8089   7805   6791   -228      5   -175       O  
ATOM   5660  N   ALA A 687      -4.506 -19.745 -56.934  1.00 32.00           N  
ANISOU 5660  N   ALA A 687     4522   4485   3149   -442    138   -345       N  
ATOM   5661  CA  ALA A 687      -5.435 -20.864 -56.724  1.00 29.97           C  
ANISOU 5661  CA  ALA A 687     4265   4225   2899   -458    154   -374       C  
ATOM   5662  C   ALA A 687      -6.253 -21.294 -57.945  1.00 28.79           C  
ANISOU 5662  C   ALA A 687     4103   4166   2671   -544    182   -414       C  
ATOM   5663  O   ALA A 687      -6.650 -20.476 -58.785  1.00 28.64           O  
ANISOU 5663  O   ALA A 687     4081   4234   2566   -585    162   -381       O  
ATOM   5664  CB  ALA A 687      -6.353 -20.588 -55.534  1.00 31.02           C  
ANISOU 5664  CB  ALA A 687     4418   4334   3035   -400    104   -307       C  
ATOM   5665  N   ILE A 688      -6.475 -22.602 -58.038  1.00 28.39           N  
ANISOU 5665  N   ILE A 688     4044   4094   2651   -577    229   -483       N  
ATOM   5666  CA  ILE A 688      -7.440 -23.169 -58.963  1.00 29.78           C  
ANISOU 5666  CA  ILE A 688     4210   4349   2754   -659    253   -522       C  
ATOM   5667  C   ILE A 688      -8.540 -23.841 -58.148  1.00 31.73           C  
ANISOU 5667  C   ILE A 688     4462   4572   3021   -632    237   -508       C  
ATOM   5668  O   ILE A 688      -8.292 -24.787 -57.395  1.00 32.80           O  
ANISOU 5668  O   ILE A 688     4599   4623   3242   -601    263   -540       O  
ATOM   5669  CB  ILE A 688      -6.784 -24.155 -59.945  1.00 31.23           C  
ANISOU 5669  CB  ILE A 688     4379   4535   2953   -740    338   -633       C  
ATOM   5670  CG1 ILE A 688      -5.779 -23.411 -60.836  1.00 33.03           C  
ANISOU 5670  CG1 ILE A 688     4604   4798   3148   -778    357   -648       C  
ATOM   5671  CG2 ILE A 688      -7.841 -24.828 -60.809  1.00 30.97           C  
ANISOU 5671  CG2 ILE A 688     4340   4586   2842   -832    363   -679       C  
ATOM   5672  CD1 ILE A 688      -4.995 -24.300 -61.764  1.00 36.69           C  
ANISOU 5672  CD1 ILE A 688     5052   5253   3636   -859    453   -765       C  
ATOM   5673  N   ALA A 689      -9.757 -23.327 -58.285  1.00 31.25           N  
ANISOU 5673  N   ALA A 689     4401   4585   2888   -645    193   -453       N  
ATOM   5674  CA  ALA A 689     -10.874 -23.804 -57.484  1.00 28.76           C  
ANISOU 5674  CA  ALA A 689     4089   4250   2589   -617    176   -432       C  
ATOM   5675  C   ALA A 689     -12.034 -24.270 -58.345  1.00 29.10           C  
ANISOU 5675  C   ALA A 689     4115   4381   2561   -696    183   -455       C  
ATOM   5676  O   ALA A 689     -12.284 -23.735 -59.436  1.00 30.18           O  
ANISOU 5676  O   ALA A 689     4238   4614   2614   -761    166   -442       O  
ATOM   5677  CB  ALA A 689     -11.322 -22.730 -56.501  1.00 26.55           C  
ANISOU 5677  CB  ALA A 689     3821   3950   2315   -542    116   -338       C  
ATOM   5678  N   GLY A 690     -12.730 -25.284 -57.849  1.00 29.70           N  
ANISOU 5678  N   GLY A 690     4190   4424   2670   -696    204   -486       N  
ATOM   5679  CA  GLY A 690     -13.905 -25.820 -58.518  1.00 31.06           C  
ANISOU 5679  CA  GLY A 690     4344   4673   2784   -768    209   -510       C  
ATOM   5680  C   GLY A 690     -14.463 -27.016 -57.779  1.00 31.78           C  
ANISOU 5680  C   GLY A 690     4438   4702   2933   -755    242   -550       C  
ATOM   5681  O   GLY A 690     -13.841 -27.500 -56.833  1.00 30.54           O  
ANISOU 5681  O   GLY A 690     4299   4445   2861   -697    263   -563       O  
ATOM   5682  N   PRO A 691     -15.645 -27.503 -58.204  1.00 33.45           N  
ANISOU 5682  N   PRO A 691     4634   4977   3100   -813    243   -567       N  
ATOM   5683  CA  PRO A 691     -16.221 -28.713 -57.616  1.00 33.57           C  
ANISOU 5683  CA  PRO A 691     4650   4938   3167   -812    282   -613       C  
ATOM   5684  C   PRO A 691     -15.574 -29.979 -58.179  1.00 33.65           C  
ANISOU 5684  C   PRO A 691     4657   4920   3210   -872    364   -724       C  
ATOM   5685  O   PRO A 691     -15.013 -29.946 -59.279  1.00 34.84           O  
ANISOU 5685  O   PRO A 691     4799   5123   3315   -943    392   -775       O  
ATOM   5686  CB  PRO A 691     -17.694 -28.653 -58.044  1.00 35.04           C  
ANISOU 5686  CB  PRO A 691     4812   5214   3288   -861    251   -590       C  
ATOM   5687  CG  PRO A 691     -17.821 -27.474 -58.992  1.00 36.78           C  
ANISOU 5687  CG  PRO A 691     5014   5539   3420   -899    195   -533       C  
ATOM   5688  CD  PRO A 691     -16.454 -27.001 -59.329  1.00 33.14           C  
ANISOU 5688  CD  PRO A 691     4569   5063   2959   -891    208   -544       C  
ATOM   5689  N   PRO A 692     -15.650 -31.101 -57.439  1.00 34.61           N  
ANISOU 5689  N   PRO A 692     4783   4953   3414   -850    407   -765       N  
ATOM   5690  CA  PRO A 692     -15.189 -32.361 -58.050  1.00 34.11           C  
ANISOU 5690  CA  PRO A 692     4707   4860   3392   -916    495   -876       C  
ATOM   5691  C   PRO A 692     -16.016 -32.673 -59.293  1.00 35.82           C  
ANISOU 5691  C   PRO A 692     4906   5191   3514  -1032    517   -935       C  
ATOM   5692  O   PRO A 692     -17.229 -32.449 -59.287  1.00 34.88           O  
ANISOU 5692  O   PRO A 692     4780   5138   3336  -1047    472   -894       O  
ATOM   5693  CB  PRO A 692     -15.442 -33.401 -56.949  1.00 32.75           C  
ANISOU 5693  CB  PRO A 692     4542   4582   3320   -869    522   -885       C  
ATOM   5694  CG  PRO A 692     -15.452 -32.589 -55.656  1.00 33.07           C  
ANISOU 5694  CG  PRO A 692     4607   4573   3384   -766    452   -779       C  
ATOM   5695  CD  PRO A 692     -16.080 -31.281 -56.038  1.00 31.72           C  
ANISOU 5695  CD  PRO A 692     4435   4506   3112   -770    385   -713       C  
ATOM   5696  N   LEU A 693     -15.362 -33.155 -60.353  1.00 37.87           N  
ANISOU 5696  N   LEU A 693     5156   5475   3758  -1119    586  -1030       N  
ATOM   5697  CA  LEU A 693     -16.029 -33.443 -61.624  1.00 37.90           C  
ANISOU 5697  CA  LEU A 693     5147   5596   3656  -1249    610  -1094       C  
ATOM   5698  C   LEU A 693     -17.125 -34.486 -61.445  1.00 38.39           C  
ANISOU 5698  C   LEU A 693     5199   5656   3732  -1284    638  -1136       C  
ATOM   5699  O   LEU A 693     -16.882 -35.553 -60.887  1.00 39.83           O  
ANISOU 5699  O   LEU A 693     5379   5733   4020  -1260    703  -1194       O  
ATOM   5700  CB  LEU A 693     -15.026 -33.952 -62.663  1.00 39.68           C  
ANISOU 5700  CB  LEU A 693     5369   5826   3881  -1339    703  -1208       C  
ATOM   5701  CG  LEU A 693     -15.105 -33.501 -64.132  1.00 40.61           C  
ANISOU 5701  CG  LEU A 693     5488   6087   3856  -1471    704  -1242       C  
ATOM   5702  CD1 LEU A 693     -14.840 -34.679 -65.063  1.00 41.35           C  
ANISOU 5702  CD1 LEU A 693     5574   6186   3949  -1597    824  -1395       C  
ATOM   5703  CD2 LEU A 693     -16.418 -32.815 -64.501  1.00 40.09           C  
ANISOU 5703  CD2 LEU A 693     5417   6152   3662  -1512    610  -1161       C  
ATOM   5704  N   GLY A 694     -18.326 -34.168 -61.919  1.00 37.75           N  
ANISOU 5704  N   GLY A 694     5107   5688   3549  -1340    585  -1103       N  
ATOM   5705  CA  GLY A 694     -19.458 -35.090 -61.841  1.00 39.78           C  
ANISOU 5705  CA  GLY A 694     5349   5957   3807  -1384    606  -1142       C  
ATOM   5706  C   GLY A 694     -20.280 -34.979 -60.570  1.00 39.51           C  
ANISOU 5706  C   GLY A 694     5316   5866   3829  -1283    556  -1060       C  
ATOM   5707  O   GLY A 694     -21.260 -35.704 -60.396  1.00 39.83           O  
ANISOU 5707  O   GLY A 694     5345   5910   3878  -1310    571  -1085       O  
ATOM   5708  N   SER A 695     -19.887 -34.063 -59.684  1.00 38.36           N  
ANISOU 5708  N   SER A 695     5186   5669   3721  -1173    500   -966       N  
ATOM   5709  CA  SER A 695     -20.569 -33.871 -58.405  1.00 37.08           C  
ANISOU 5709  CA  SER A 695     5031   5447   3611  -1080    460   -890       C  
ATOM   5710  C   SER A 695     -21.547 -32.697 -58.456  1.00 36.22           C  
ANISOU 5710  C   SER A 695     4905   5425   3434  -1067    371   -791       C  
ATOM   5711  O   SER A 695     -21.607 -31.974 -59.444  1.00 35.67           O  
ANISOU 5711  O   SER A 695     4817   5457   3279  -1123    332   -768       O  
ATOM   5712  CB  SER A 695     -19.542 -33.636 -57.295  1.00 36.33           C  
ANISOU 5712  CB  SER A 695     4965   5235   3604   -973    459   -851       C  
ATOM   5713  OG  SER A 695     -18.923 -32.366 -57.456  1.00 36.89           O  
ANISOU 5713  OG  SER A 695     5041   5337   3637   -939    405   -786       O  
ATOM   5714  N   LYS A 696     -22.287 -32.503 -57.369  1.00 37.05           N  
ANISOU 5714  N   LYS A 696     5012   5483   3583   -996    343   -731       N  
ATOM   5715  CA  LYS A 696     -23.230 -31.395 -57.255  1.00 38.49           C  
ANISOU 5715  CA  LYS A 696     5171   5724   3731   -972    268   -636       C  
ATOM   5716  C   LYS A 696     -22.702 -30.261 -56.360  1.00 37.65           C  
ANISOU 5716  C   LYS A 696     5085   5561   3660   -871    229   -552       C  
ATOM   5717  O   LYS A 696     -23.452 -29.347 -55.988  1.00 37.37           O  
ANISOU 5717  O   LYS A 696     5031   5543   3624   -833    180   -474       O  
ATOM   5718  CB  LYS A 696     -24.583 -31.908 -56.745  1.00 40.81           C  
ANISOU 5718  CB  LYS A 696     5445   6012   4049   -975    271   -633       C  
ATOM   5719  CG  LYS A 696     -25.301 -32.824 -57.731  1.00 43.57           C  
ANISOU 5719  CG  LYS A 696     5764   6439   4350  -1084    295   -704       C  
ATOM   5720  CD  LYS A 696     -26.397 -33.631 -57.050  1.00 49.93           C  
ANISOU 5720  CD  LYS A 696     6561   7208   5203  -1081    321   -724       C  
ATOM   5721  CE  LYS A 696     -27.129 -34.521 -58.053  1.00 51.78           C  
ANISOU 5721  CE  LYS A 696     6763   7524   5386  -1196    344   -797       C  
ATOM   5722  NZ  LYS A 696     -27.944 -35.567 -57.368  1.00 56.46           N  
ANISOU 5722  NZ  LYS A 696     7355   8060   6037  -1195    392   -840       N  
ATOM   5723  N   GLY A 697     -21.413 -30.315 -56.028  1.00 33.51           N  
ANISOU 5723  N   GLY A 697     4595   4967   3170   -831    254   -571       N  
ATOM   5724  CA  GLY A 697     -20.774 -29.251 -55.246  1.00 34.52           C  
ANISOU 5724  CA  GLY A 697     4745   5045   3324   -746    220   -500       C  
ATOM   5725  C   GLY A 697     -20.781 -27.926 -55.997  1.00 33.28           C  
ANISOU 5725  C   GLY A 697     4565   4972   3108   -755    162   -436       C  
ATOM   5726  O   GLY A 697     -20.777 -27.903 -57.228  1.00 32.96           O  
ANISOU 5726  O   GLY A 697     4502   5021   3002   -831    153   -456       O  
ATOM   5727  N   ILE A 698     -20.822 -26.821 -55.264  1.00 31.43           N  
ANISOU 5727  N   ILE A 698     4336   4709   2895   -684    123   -357       N  
ATOM   5728  CA  ILE A 698     -20.924 -25.506 -55.902  1.00 31.76           C  
ANISOU 5728  CA  ILE A 698     4350   4821   2896   -687     66   -284       C  
ATOM   5729  C   ILE A 698     -19.555 -24.883 -56.179  1.00 31.46           C  
ANISOU 5729  C   ILE A 698     4334   4774   2846   -669     61   -278       C  
ATOM   5730  O   ILE A 698     -19.460 -23.917 -56.936  1.00 33.28           O  
ANISOU 5730  O   ILE A 698     4544   5069   3033   -687     20   -228       O  
ATOM   5731  CB  ILE A 698     -21.847 -24.528 -55.121  1.00 31.13           C  
ANISOU 5731  CB  ILE A 698     4252   4724   2854   -628     30   -201       C  
ATOM   5732  CG1 ILE A 698     -21.299 -24.257 -53.713  1.00 30.66           C  
ANISOU 5732  CG1 ILE A 698     4238   4558   2855   -545     50   -189       C  
ATOM   5733  CG2 ILE A 698     -23.274 -25.071 -55.070  1.00 31.48           C  
ANISOU 5733  CG2 ILE A 698     4261   4793   2908   -658     32   -204       C  
ATOM   5734  CD1 ILE A 698     -21.994 -23.116 -52.995  1.00 29.60           C  
ANISOU 5734  CD1 ILE A 698     4088   4400   2759   -492     27   -114       C  
ATOM   5735  N   GLY A 699     -18.506 -25.443 -55.571  1.00 30.46           N  
ANISOU 5735  N   GLY A 699     4247   4565   2762   -636    101   -325       N  
ATOM   5736  CA  GLY A 699     -17.127 -25.024 -55.843  1.00 29.44           C  
ANISOU 5736  CA  GLY A 699     4135   4420   2632   -624    105   -332       C  
ATOM   5737  C   GLY A 699     -16.630 -23.912 -54.931  1.00 30.51           C  
ANISOU 5737  C   GLY A 699     4291   4501   2801   -543     75   -266       C  
ATOM   5738  O   GLY A 699     -15.578 -24.037 -54.303  1.00 29.88           O  
ANISOU 5738  O   GLY A 699     4241   4349   2765   -502     91   -281       O  
ATOM   5739  N   GLY A 700     -17.379 -22.815 -54.873  1.00 29.48           N  
ANISOU 5739  N   GLY A 700     4140   4404   2657   -522     32   -191       N  
ATOM   5740  CA  GLY A 700     -17.013 -21.671 -54.051  1.00 27.66           C  
ANISOU 5740  CA  GLY A 700     3926   4126   2458   -453     10   -131       C  
ATOM   5741  C   GLY A 700     -18.179 -20.723 -53.862  1.00 27.45           C  
ANISOU 5741  C   GLY A 700     3868   4123   2440   -434    -22    -59       C  
ATOM   5742  O   GLY A 700     -19.207 -20.851 -54.534  1.00 28.95           O  
ANISOU 5742  O   GLY A 700     4016   4378   2607   -477    -38    -45       O  
ATOM   5743  N   PHE A 701     -18.025 -19.785 -52.932  1.00 25.53           N  
ANISOU 5743  N   PHE A 701     3640   3823   2237   -373    -28    -15       N  
ATOM   5744  CA  PHE A 701     -18.984 -18.694 -52.758  1.00 25.64           C  
ANISOU 5744  CA  PHE A 701     3618   3845   2278   -350    -50     56       C  
ATOM   5745  C   PHE A 701     -18.368 -17.492 -52.045  1.00 24.63           C  
ANISOU 5745  C   PHE A 701     3510   3664   2186   -294    -52     96       C  
ATOM   5746  O   PHE A 701     -17.380 -17.629 -51.337  1.00 25.42           O  
ANISOU 5746  O   PHE A 701     3658   3707   2291   -268    -35     67       O  
ATOM   5747  CB  PHE A 701     -20.261 -19.154 -52.029  1.00 22.47           C  
ANISOU 5747  CB  PHE A 701     3206   3419   1915   -344    -30     51       C  
ATOM   5748  CG  PHE A 701     -20.052 -19.515 -50.574  1.00 23.29           C  
ANISOU 5748  CG  PHE A 701     3366   3431   2054   -305     10     20       C  
ATOM   5749  CD1 PHE A 701     -19.789 -20.829 -50.202  1.00 19.48           C  
ANISOU 5749  CD1 PHE A 701     2920   2920   1562   -320     37    -41       C  
ATOM   5750  CD2 PHE A 701     -20.149 -18.548 -49.577  1.00 24.91           C  
ANISOU 5750  CD2 PHE A 701     3585   3579   2302   -259     22     53       C  
ATOM   5751  CE1 PHE A 701     -19.614 -21.171 -48.859  1.00 24.12           C  
ANISOU 5751  CE1 PHE A 701     3560   3427   2176   -292     65    -58       C  
ATOM   5752  CE2 PHE A 701     -19.966 -18.881 -48.231  1.00 23.64           C  
ANISOU 5752  CE2 PHE A 701     3481   3342   2159   -238     56     25       C  
ATOM   5753  CZ  PHE A 701     -19.698 -20.196 -47.876  1.00 20.44           C  
ANISOU 5753  CZ  PHE A 701     3115   2914   1737   -255     73    -25       C  
ATOM   5754  N   TRP A 702     -18.976 -16.327 -52.247  1.00 24.46           N  
ANISOU 5754  N   TRP A 702     3444   3658   2191   -278    -75    164       N  
ATOM   5755  CA  TRP A 702     -18.630 -15.097 -51.547  1.00 25.27           C  
ANISOU 5755  CA  TRP A 702     3557   3706   2340   -228    -69    203       C  
ATOM   5756  C   TRP A 702     -19.878 -14.596 -50.837  1.00 25.33           C  
ANISOU 5756  C   TRP A 702     3533   3676   2416   -204    -50    235       C  
ATOM   5757  O   TRP A 702     -20.950 -14.594 -51.435  1.00 28.87           O  
ANISOU 5757  O   TRP A 702     3922   4168   2881   -225    -69    270       O  
ATOM   5758  CB  TRP A 702     -18.173 -14.035 -52.560  1.00 24.37           C  
ANISOU 5758  CB  TRP A 702     3408   3638   2212   -234   -107    262       C  
ATOM   5759  CG  TRP A 702     -16.701 -13.915 -52.722  1.00 24.33           C  
ANISOU 5759  CG  TRP A 702     3445   3626   2173   -230   -108    238       C  
ATOM   5760  CD1 TRP A 702     -15.902 -12.943 -52.193  1.00 24.83           C  
ANISOU 5760  CD1 TRP A 702     3531   3641   2264   -190   -101    255       C  
ATOM   5761  CD2 TRP A 702     -15.835 -14.789 -53.462  1.00 27.76           C  
ANISOU 5761  CD2 TRP A 702     3900   4100   2548   -270   -110    187       C  
ATOM   5762  NE1 TRP A 702     -14.592 -13.156 -52.551  1.00 28.07           N  
ANISOU 5762  NE1 TRP A 702     3972   4059   2636   -200   -105    223       N  
ATOM   5763  CE2 TRP A 702     -14.519 -14.282 -53.328  1.00 26.36           C  
ANISOU 5763  CE2 TRP A 702     3754   3893   2370   -248   -107    180       C  
ATOM   5764  CE3 TRP A 702     -16.040 -15.954 -54.217  1.00 27.66           C  
ANISOU 5764  CE3 TRP A 702     3880   4141   2487   -325   -109    142       C  
ATOM   5765  CZ2 TRP A 702     -13.410 -14.895 -53.930  1.00 26.76           C  
ANISOU 5765  CZ2 TRP A 702     3824   3963   2382   -277   -101    130       C  
ATOM   5766  CZ3 TRP A 702     -14.936 -16.566 -54.814  1.00 31.32           C  
ANISOU 5766  CZ3 TRP A 702     4366   4622   2911   -357    -97     88       C  
ATOM   5767  CH2 TRP A 702     -13.636 -16.031 -54.667  1.00 27.99           C  
ANISOU 5767  CH2 TRP A 702     3971   4166   2498   -331    -93     84       C  
ATOM   5768  N   THR A 703     -19.760 -14.166 -49.581  1.00 24.68           N  
ANISOU 5768  N   THR A 703     3488   3514   2376   -167    -10    222       N  
ATOM   5769  CA  THR A 703     -20.879 -13.472 -48.925  1.00 23.67           C  
ANISOU 5769  CA  THR A 703     3325   3343   2326   -145     20    251       C  
ATOM   5770  C   THR A 703     -20.724 -11.947 -48.961  1.00 24.43           C  
ANISOU 5770  C   THR A 703     3389   3413   2479   -114     19    308       C  
ATOM   5771  O   THR A 703     -21.695 -11.203 -48.794  1.00 25.47           O  
ANISOU 5771  O   THR A 703     3466   3517   2693    -98     37    348       O  
ATOM   5772  CB  THR A 703     -21.132 -13.935 -47.443  1.00 23.87           C  
ANISOU 5772  CB  THR A 703     3407   3293   2368   -137     79    197       C  
ATOM   5773  OG1 THR A 703     -20.362 -13.142 -46.538  1.00 23.66           O  
ANISOU 5773  OG1 THR A 703     3428   3206   2354   -113    106    189       O  
ATOM   5774  CG2 THR A 703     -20.796 -15.402 -47.232  1.00 24.97           C  
ANISOU 5774  CG2 THR A 703     3599   3441   2448   -162     80    138       C  
ATOM   5775  N   GLY A 704     -19.498 -11.482 -49.157  1.00 26.22           N  
ANISOU 5775  N   GLY A 704     3647   3641   2673   -105      3    311       N  
ATOM   5776  CA  GLY A 704     -19.198 -10.045 -49.129  1.00 25.87           C  
ANISOU 5776  CA  GLY A 704     3581   3565   2682    -75      7    360       C  
ATOM   5777  C   GLY A 704     -17.700  -9.835 -49.096  1.00 24.34           C  
ANISOU 5777  C   GLY A 704     3442   3366   2439    -69     -3    339       C  
ATOM   5778  O   GLY A 704     -16.938 -10.790 -49.266  1.00 20.90           O  
ANISOU 5778  O   GLY A 704     3049   2957   1936    -88    -19    296       O  
ATOM   5779  N   LYS A 705     -17.269  -8.592 -48.892  1.00 24.07           N  
ANISOU 5779  N   LYS A 705     3403   3295   2449    -43     10    369       N  
ATOM   5780  CA  LYS A 705     -15.836  -8.306 -48.806  1.00 24.65           C  
ANISOU 5780  CA  LYS A 705     3525   3358   2483    -37      2    350       C  
ATOM   5781  C   LYS A 705     -15.207  -9.155 -47.703  1.00 24.47           C  
ANISOU 5781  C   LYS A 705     3579   3297   2420    -43     25    278       C  
ATOM   5782  O   LYS A 705     -15.788  -9.314 -46.632  1.00 26.47           O  
ANISOU 5782  O   LYS A 705     3857   3503   2696    -42     65    250       O  
ATOM   5783  CB  LYS A 705     -15.579  -6.826 -48.527  1.00 23.86           C  
ANISOU 5783  CB  LYS A 705     3410   3209   2446    -10     24    385       C  
ATOM   5784  CG  LYS A 705     -15.872  -5.911 -49.704  1.00 24.40           C  
ANISOU 5784  CG  LYS A 705     3405   3314   2553     -5     -9    468       C  
ATOM   5785  CD  LYS A 705     -15.586  -4.469 -49.333  1.00 26.08           C  
ANISOU 5785  CD  LYS A 705     3605   3466   2840     24     21    498       C  
ATOM   5786  CE  LYS A 705     -15.912  -3.521 -50.474  1.00 25.55           C  
ANISOU 5786  CE  LYS A 705     3459   3427   2821     30    -15    594       C  
ATOM   5787  NZ  LYS A 705     -15.742  -2.125 -50.016  1.00 27.39           N  
ANISOU 5787  NZ  LYS A 705     3675   3587   3146     60     26    620       N  
ATOM   5788  N   LYS A 706     -14.046  -9.729 -48.004  1.00 24.70           N  
ANISOU 5788  N   LYS A 706     3642   3349   2392    -53     -3    252       N  
ATOM   5789  CA  LYS A 706     -13.230 -10.473 -47.041  1.00 24.68           C  
ANISOU 5789  CA  LYS A 706     3708   3310   2358    -58      5    199       C  
ATOM   5790  C   LYS A 706     -13.903 -11.737 -46.481  1.00 24.02           C  
ANISOU 5790  C   LYS A 706     3647   3219   2259    -75     17    164       C  
ATOM   5791  O   LYS A 706     -13.445 -12.297 -45.488  1.00 23.96           O  
ANISOU 5791  O   LYS A 706     3696   3174   2235    -81     25    131       O  
ATOM   5792  CB  LYS A 706     -12.736  -9.525 -45.928  1.00 26.61           C  
ANISOU 5792  CB  LYS A 706     3991   3493   2625    -44     32    194       C  
ATOM   5793  CG  LYS A 706     -11.779  -8.432 -46.455  1.00 27.71           C  
ANISOU 5793  CG  LYS A 706     4118   3637   2775    -29     17    220       C  
ATOM   5794  CD  LYS A 706     -11.176  -7.584 -45.360  1.00 29.50           C  
ANISOU 5794  CD  LYS A 706     4386   3805   3016    -24     44    206       C  
ATOM   5795  CE  LYS A 706     -10.164  -6.581 -45.915  1.00 33.65           C  
ANISOU 5795  CE  LYS A 706     4898   4335   3552    -11     29    229       C  
ATOM   5796  NZ  LYS A 706      -8.883  -7.239 -46.336  1.00 30.62           N  
ANISOU 5796  NZ  LYS A 706     4533   3976   3124    -18    -12    211       N  
ATOM   5797  N   ARG A 707     -14.972 -12.186 -47.138  1.00 25.77           N  
ANISOU 5797  N   ARG A 707     3715   3281   2793   -354    101    -80       N  
ATOM   5798  CA  ARG A 707     -15.757 -13.335 -46.683  1.00 24.44           C  
ANISOU 5798  CA  ARG A 707     3513   3112   2661   -329     82    -71       C  
ATOM   5799  C   ARG A 707     -16.073 -14.279 -47.829  1.00 23.55           C  
ANISOU 5799  C   ARG A 707     3400   3011   2538   -344     32    -66       C  
ATOM   5800  O   ARG A 707     -16.995 -14.028 -48.616  1.00 22.81           O  
ANISOU 5800  O   ARG A 707     3301   2902   2462   -346     -9    -32       O  
ATOM   5801  CB  ARG A 707     -17.059 -12.873 -46.008  1.00 23.73           C  
ANISOU 5801  CB  ARG A 707     3396   2978   2640   -301     88    -31       C  
ATOM   5802  CG  ARG A 707     -16.852 -12.257 -44.624  1.00 24.47           C  
ANISOU 5802  CG  ARG A 707     3486   3063   2748   -282    144    -46       C  
ATOM   5803  CD  ARG A 707     -18.160 -11.863 -43.961  1.00 23.10           C  
ANISOU 5803  CD  ARG A 707     3287   2841   2648   -254    159     -7       C  
ATOM   5804  NE  ARG A 707     -19.025 -13.013 -43.685  1.00 30.40           N  
ANISOU 5804  NE  ARG A 707     4179   3754   3617   -232    146      7       N  
ATOM   5805  CZ  ARG A 707     -19.030 -13.714 -42.548  1.00 31.25           C  
ANISOU 5805  CZ  ARG A 707     4276   3864   3734   -204    184     -5       C  
ATOM   5806  NH1 ARG A 707     -18.216 -13.399 -41.541  1.00 27.24           N  
ANISOU 5806  NH1 ARG A 707     3784   3381   3186   -193    226    -34       N  
ATOM   5807  NH2 ARG A 707     -19.868 -14.731 -42.411  1.00 29.56           N  
ANISOU 5807  NH2 ARG A 707     4032   3628   3571   -187    181     11       N  
ATOM   5808  N   TYR A 708     -15.305 -15.362 -47.927  1.00 22.23           N  
ANISOU 5808  N   TYR A 708     3233   2872   2339   -354     36   -103       N  
ATOM   5809  CA  TYR A 708     -15.482 -16.326 -49.015  1.00 23.74           C  
ANISOU 5809  CA  TYR A 708     3426   3077   2519   -375     -3   -112       C  
ATOM   5810  C   TYR A 708     -14.904 -17.702 -48.689  1.00 23.11           C  
ANISOU 5810  C   TYR A 708     3334   3012   2436   -371     19   -147       C  
ATOM   5811  O   TYR A 708     -14.126 -17.856 -47.745  1.00 21.60           O  
ANISOU 5811  O   TYR A 708     3138   2833   2235   -351     60   -163       O  
ATOM   5812  CB  TYR A 708     -14.878 -15.792 -50.328  1.00 23.21           C  
ANISOU 5812  CB  TYR A 708     3402   3028   2388   -410    -25   -116       C  
ATOM   5813  CG  TYR A 708     -13.383 -15.529 -50.265  1.00 23.17           C  
ANISOU 5813  CG  TYR A 708     3426   3044   2333   -427     15   -152       C  
ATOM   5814  CD1 TYR A 708     -12.889 -14.298 -49.832  1.00 23.55           C  
ANISOU 5814  CD1 TYR A 708     3489   3084   2375   -426     49   -150       C  
ATOM   5815  CD2 TYR A 708     -12.465 -16.511 -50.640  1.00 19.44           C  
ANISOU 5815  CD2 TYR A 708     2961   2597   1827   -445     25   -193       C  
ATOM   5816  CE1 TYR A 708     -11.522 -14.056 -49.766  1.00 21.52           C  
ANISOU 5816  CE1 TYR A 708     3248   2848   2081   -446     87   -192       C  
ATOM   5817  CE2 TYR A 708     -11.102 -16.278 -50.579  1.00 22.05           C  
ANISOU 5817  CE2 TYR A 708     3308   2949   2121   -459     62   -228       C  
ATOM   5818  CZ  TYR A 708     -10.637 -15.043 -50.142  1.00 23.55           C  
ANISOU 5818  CZ  TYR A 708     3508   3134   2307   -461     91   -230       C  
ATOM   5819  OH  TYR A 708      -9.280 -14.804 -50.080  1.00 28.32           O  
ANISOU 5819  OH  TYR A 708     4119   3759   2881   -479    128   -275       O  
ATOM   5820  N   ALA A 709     -15.300 -18.691 -49.487  1.00 23.70           N  
ANISOU 5820  N   ALA A 709     3399   3087   2519   -389     -7   -159       N  
ATOM   5821  CA  ALA A 709     -14.817 -20.061 -49.359  1.00 24.55           C  
ANISOU 5821  CA  ALA A 709     3496   3200   2632   -389     21   -191       C  
ATOM   5822  C   ALA A 709     -14.636 -20.662 -50.744  1.00 25.53           C  
ANISOU 5822  C   ALA A 709     3637   3339   2723   -432     -9   -222       C  
ATOM   5823  O   ALA A 709     -15.469 -20.456 -51.630  1.00 27.87           O  
ANISOU 5823  O   ALA A 709     3933   3636   3020   -453    -59   -216       O  
ATOM   5824  CB  ALA A 709     -15.791 -20.901 -48.530  1.00 25.32           C  
ANISOU 5824  CB  ALA A 709     3552   3263   2806   -359     42   -179       C  
ATOM   5825  N   LEU A 710     -13.539 -21.391 -50.924  1.00 26.31           N  
ANISOU 5825  N   LEU A 710     3751   3454   2792   -443     23   -256       N  
ATOM   5826  CA  LEU A 710     -13.211 -22.028 -52.195  1.00 26.86           C  
ANISOU 5826  CA  LEU A 710     3842   3537   2827   -487      8   -293       C  
ATOM   5827  C   LEU A 710     -12.717 -23.451 -51.987  1.00 27.28           C  
ANISOU 5827  C   LEU A 710     3880   3580   2905   -484     56   -326       C  
ATOM   5828  O   LEU A 710     -12.006 -23.741 -51.020  1.00 27.77           O  
ANISOU 5828  O   LEU A 710     3932   3642   2979   -448    103   -321       O  
ATOM   5829  CB  LEU A 710     -12.132 -21.237 -52.932  1.00 25.67           C  
ANISOU 5829  CB  LEU A 710     3739   3414   2601   -512      7   -303       C  
ATOM   5830  CG  LEU A 710     -12.457 -19.854 -53.497  1.00 29.04           C  
ANISOU 5830  CG  LEU A 710     4196   3848   2991   -522    -31   -272       C  
ATOM   5831  CD1 LEU A 710     -11.171 -19.162 -53.899  1.00 29.32           C  
ANISOU 5831  CD1 LEU A 710     4275   3899   2968   -541     -3   -285       C  
ATOM   5832  CD2 LEU A 710     -13.423 -19.932 -54.687  1.00 29.98           C  
ANISOU 5832  CD2 LEU A 710     4325   3976   3092   -546    -92   -268       C  
ATOM   5833  N   ASN A 711     -13.088 -24.333 -52.909  1.00 25.93           N  
ANISOU 5833  N   ASN A 711     3707   3403   2743   -520     45   -361       N  
ATOM   5834  CA  ASN A 711     -12.555 -25.684 -52.921  1.00 27.19           C  
ANISOU 5834  CA  ASN A 711     3858   3547   2927   -525     99   -397       C  
ATOM   5835  C   ASN A 711     -11.340 -25.761 -53.856  1.00 28.29           C  
ANISOU 5835  C   ASN A 711     4038   3711   3000   -559    111   -433       C  
ATOM   5836  O   ASN A 711     -11.495 -25.844 -55.073  1.00 28.78           O  
ANISOU 5836  O   ASN A 711     4124   3785   3024   -608     81   -465       O  
ATOM   5837  CB  ASN A 711     -13.641 -26.681 -53.324  1.00 27.58           C  
ANISOU 5837  CB  ASN A 711     3876   3567   3035   -549     94   -427       C  
ATOM   5838  CG  ASN A 711     -13.200 -28.106 -53.162  1.00 30.48           C  
ANISOU 5838  CG  ASN A 711     4231   3903   3447   -547    167   -459       C  
ATOM   5839  OD1 ASN A 711     -12.707 -28.491 -52.104  1.00 32.58           O  
ANISOU 5839  OD1 ASN A 711     4486   4150   3744   -497    225   -432       O  
ATOM   5840  ND2 ASN A 711     -13.361 -28.903 -54.214  1.00 29.30           N  
ANISOU 5840  ND2 ASN A 711     4084   3749   3301   -600    166   -517       N  
ATOM   5841  N   VAL A 712     -10.139 -25.727 -53.271  1.00 25.71           N  
ANISOU 5841  N   VAL A 712     3717   3394   2659   -533    155   -428       N  
ATOM   5842  CA  VAL A 712      -8.893 -25.548 -54.023  1.00 27.10           C  
ANISOU 5842  CA  VAL A 712     3928   3592   2775   -562    171   -457       C  
ATOM   5843  C   VAL A 712      -8.213 -26.880 -54.329  1.00 28.91           C  
ANISOU 5843  C   VAL A 712     4153   3805   3025   -572    228   -497       C  
ATOM   5844  O   VAL A 712      -8.081 -27.732 -53.448  1.00 29.43           O  
ANISOU 5844  O   VAL A 712     4188   3851   3144   -530    274   -487       O  
ATOM   5845  CB  VAL A 712      -7.901 -24.609 -53.272  1.00 25.84           C  
ANISOU 5845  CB  VAL A 712     3770   3457   2591   -532    184   -439       C  
ATOM   5846  CG1 VAL A 712      -6.572 -24.533 -53.981  1.00 23.56           C  
ANISOU 5846  CG1 VAL A 712     3509   3186   2258   -561    213   -474       C  
ATOM   5847  CG2 VAL A 712      -8.491 -23.208 -53.098  1.00 25.22           C  
ANISOU 5847  CG2 VAL A 712     3701   3388   2493   -530    140   -405       C  
ATOM   5848  N   TRP A 713      -7.785 -27.036 -55.584  1.00 28.15           N  
ANISOU 5848  N   TRP A 713     4094   3717   2884   -625    228   -539       N  
ATOM   5849  CA  TRP A 713      -7.105 -28.241 -56.055  1.00 29.64           C  
ANISOU 5849  CA  TRP A 713     4285   3888   3089   -645    287   -584       C  
ATOM   5850  C   TRP A 713      -5.608 -28.015 -56.223  1.00 29.71           C  
ANISOU 5850  C   TRP A 713     4312   3913   3063   -646    326   -598       C  
ATOM   5851  O   TRP A 713      -4.810 -28.965 -56.158  1.00 28.99           O  
ANISOU 5851  O   TRP A 713     4208   3805   3001   -637    388   -620       O  
ATOM   5852  CB  TRP A 713      -7.712 -28.714 -57.384  1.00 28.39           C  
ANISOU 5852  CB  TRP A 713     4153   3725   2908   -708    266   -633       C  
ATOM   5853  CG  TRP A 713      -9.166 -29.057 -57.254  1.00 29.51           C  
ANISOU 5853  CG  TRP A 713     4265   3852   3096   -711    230   -632       C  
ATOM   5854  CD1 TRP A 713     -10.227 -28.217 -57.448  1.00 28.97           C  
ANISOU 5854  CD1 TRP A 713     4197   3805   3007   -718    154   -610       C  
ATOM   5855  CD2 TRP A 713      -9.719 -30.322 -56.875  1.00 27.25           C  
ANISOU 5855  CD2 TRP A 713     3939   3522   2894   -706    275   -653       C  
ATOM   5856  NE1 TRP A 713     -11.405 -28.881 -57.219  1.00 28.44           N  
ANISOU 5856  NE1 TRP A 713     4087   3713   3007   -719    144   -622       N  
ATOM   5857  CE2 TRP A 713     -11.125 -30.175 -56.863  1.00 28.06           C  
ANISOU 5857  CE2 TRP A 713     4015   3622   3025   -714    221   -650       C  
ATOM   5858  CE3 TRP A 713      -9.164 -31.567 -56.543  1.00 29.96           C  
ANISOU 5858  CE3 TRP A 713     4264   3823   3297   -692    362   -674       C  
ATOM   5859  CZ2 TRP A 713     -11.992 -31.229 -56.538  1.00 26.97           C  
ANISOU 5859  CZ2 TRP A 713     3832   3439   2977   -716    254   -674       C  
ATOM   5860  CZ3 TRP A 713     -10.025 -32.618 -56.220  1.00 32.86           C  
ANISOU 5860  CZ3 TRP A 713     4593   4142   3752   -691    400   -691       C  
ATOM   5861  CH2 TRP A 713     -11.427 -32.440 -56.225  1.00 31.07           C  
ANISOU 5861  CH2 TRP A 713     4338   3911   3554   -706    347   -694       C  
ATOM   5862  N   ASP A 714      -5.241 -26.755 -56.447  1.00 28.88           N  
ANISOU 5862  N   ASP A 714     4234   3836   2902   -657    296   -586       N  
ATOM   5863  CA  ASP A 714      -3.863 -26.381 -56.691  1.00 30.10           C  
ANISOU 5863  CA  ASP A 714     4405   4005   3027   -666    333   -605       C  
ATOM   5864  C   ASP A 714      -3.583 -24.969 -56.169  1.00 31.29           C  
ANISOU 5864  C   ASP A 714     4555   4179   3152   -650    309   -578       C  
ATOM   5865  O   ASP A 714      -4.249 -24.001 -56.550  1.00 30.78           O  
ANISOU 5865  O   ASP A 714     4521   4120   3053   -668    265   -557       O  
ATOM   5866  CB  ASP A 714      -3.524 -26.516 -58.183  1.00 29.22           C  
ANISOU 5866  CB  ASP A 714     4348   3890   2862   -729    347   -649       C  
ATOM   5867  CG  ASP A 714      -2.023 -26.483 -58.454  1.00 31.98           C  
ANISOU 5867  CG  ASP A 714     4707   4242   3200   -741    407   -679       C  
ATOM   5868  OD1 ASP A 714      -1.388 -25.433 -58.227  1.00 31.66           O  
ANISOU 5868  OD1 ASP A 714     4670   4219   3140   -735    407   -668       O  
ATOM   5869  OD2 ASP A 714      -1.479 -27.504 -58.913  1.00 32.77           O  
ANISOU 5869  OD2 ASP A 714     4809   4325   3317   -758    459   -717       O  
ATOM   5870  N   MET A 715      -2.597 -24.879 -55.284  1.00 30.71           N  
ANISOU 5870  N   MET A 715     4446   4122   3101   -614    340   -580       N  
ATOM   5871  CA  MET A 715      -2.195 -23.622 -54.675  1.00 32.82           C  
ANISOU 5871  CA  MET A 715     4702   4413   3354   -601    328   -569       C  
ATOM   5872  C   MET A 715      -0.716 -23.377 -54.954  1.00 34.06           C  
ANISOU 5872  C   MET A 715     4857   4584   3500   -619    374   -609       C  
ATOM   5873  O   MET A 715       0.143 -24.151 -54.520  1.00 33.46           O  
ANISOU 5873  O   MET A 715     4741   4519   3454   -592    409   -629       O  
ATOM   5874  CB  MET A 715      -2.466 -23.645 -53.164  1.00 33.88           C  
ANISOU 5874  CB  MET A 715     4784   4564   3525   -538    314   -539       C  
ATOM   5875  CG  MET A 715      -2.148 -22.343 -52.443  1.00 36.48           C  
ANISOU 5875  CG  MET A 715     5098   4919   3841   -526    301   -537       C  
ATOM   5876  SD  MET A 715      -3.102 -20.944 -53.074  1.00 44.95           S  
ANISOU 5876  SD  MET A 715     6222   5973   4885   -565    264   -512       S  
ATOM   5877  CE  MET A 715      -4.634 -21.143 -52.177  1.00 41.88           C  
ANISOU 5877  CE  MET A 715     5811   5572   4528   -523    222   -461       C  
ATOM   5878  N   GLU A 716      -0.444 -22.292 -55.682  1.00 33.93           N  
ANISOU 5878  N   GLU A 716     4881   4564   3446   -661    377   -620       N  
ATOM   5879  CA  GLU A 716       0.899 -21.908 -56.154  1.00 36.28           C  
ANISOU 5879  CA  GLU A 716     5185   4865   3734   -691    429   -663       C  
ATOM   5880  C   GLU A 716       1.848 -23.072 -56.498  1.00 34.35           C  
ANISOU 5880  C   GLU A 716     4924   4617   3510   -695    479   -701       C  
ATOM   5881  O   GLU A 716       2.995 -23.116 -56.051  1.00 34.53           O  
ANISOU 5881  O   GLU A 716     4900   4658   3560   -680    514   -732       O  
ATOM   5882  CB  GLU A 716       1.555 -20.865 -55.223  1.00 36.93           C  
ANISOU 5882  CB  GLU A 716     5226   4973   3835   -675    434   -676       C  
ATOM   5883  CG  GLU A 716       1.718 -21.289 -53.775  1.00 41.46           C  
ANISOU 5883  CG  GLU A 716     5725   5583   4445   -613    418   -673       C  
ATOM   5884  CD  GLU A 716       1.835 -20.112 -52.796  1.00 44.83           C  
ANISOU 5884  CD  GLU A 716     6118   6037   4877   -599    403   -680       C  
ATOM   5885  OE1 GLU A 716       1.458 -20.305 -51.618  1.00 42.59           O  
ANISOU 5885  OE1 GLU A 716     5793   5782   4607   -546    373   -660       O  
ATOM   5886  OE2 GLU A 716       2.297 -19.013 -53.192  1.00 45.98           O  
ANISOU 5886  OE2 GLU A 716     6282   6173   5015   -639    426   -706       O  
ATOM   5887  N   GLY A 717       1.354 -24.002 -57.308  1.00 32.11           N  
ANISOU 5887  N   GLY A 717     4675   4310   3215   -715    483   -702       N  
ATOM   5888  CA  GLY A 717       2.176 -25.093 -57.808  1.00 30.75           C  
ANISOU 5888  CA  GLY A 717     4498   4124   3063   -726    540   -739       C  
ATOM   5889  C   GLY A 717       2.077 -26.379 -57.014  1.00 29.73           C  
ANISOU 5889  C   GLY A 717     4316   3992   2988   -675    550   -729       C  
ATOM   5890  O   GLY A 717       2.604 -27.406 -57.443  1.00 29.77           O  
ANISOU 5890  O   GLY A 717     4318   3977   3016   -683    602   -756       O  
ATOM   5891  N   THR A 718       1.417 -26.327 -55.857  1.00 28.44           N  
ANISOU 5891  N   THR A 718     4114   3846   2847   -622    510   -690       N  
ATOM   5892  CA  THR A 718       1.167 -27.525 -55.060  1.00 28.55           C  
ANISOU 5892  CA  THR A 718     4085   3851   2911   -567    524   -668       C  
ATOM   5893  C   THR A 718      -0.146 -28.161 -55.504  1.00 30.07           C  
ANISOU 5893  C   THR A 718     4308   4009   3109   -586    508   -656       C  
ATOM   5894  O   THR A 718      -1.219 -27.604 -55.285  1.00 30.91           O  
ANISOU 5894  O   THR A 718     4425   4118   3202   -586    455   -628       O  
ATOM   5895  CB  THR A 718       1.114 -27.229 -53.534  1.00 29.22           C  
ANISOU 5895  CB  THR A 718     4115   3972   3015   -494    497   -630       C  
ATOM   5896  OG1 THR A 718       2.312 -26.560 -53.125  1.00 30.74           O  
ANISOU 5896  OG1 THR A 718     4272   4207   3200   -481    504   -653       O  
ATOM   5897  CG2 THR A 718       0.967 -28.529 -52.724  1.00 25.55           C  
ANISOU 5897  CG2 THR A 718     3613   3497   2601   -427    526   -601       C  
ATOM   5898  N   ARG A 719      -0.050 -29.319 -56.142  1.00 29.76           N  
ANISOU 5898  N   ARG A 719     4277   3935   3094   -606    556   -683       N  
ATOM   5899  CA  ARG A 719      -1.220 -30.091 -56.520  1.00 33.11           C  
ANISOU 5899  CA  ARG A 719     4719   4326   3537   -626    550   -685       C  
ATOM   5900  C   ARG A 719      -1.556 -31.012 -55.355  1.00 33.76           C  
ANISOU 5900  C   ARG A 719     4751   4388   3688   -558    577   -649       C  
ATOM   5901  O   ARG A 719      -0.790 -31.927 -55.050  1.00 36.68           O  
ANISOU 5901  O   ARG A 719     5094   4741   4101   -523    640   -651       O  
ATOM   5902  CB  ARG A 719      -0.935 -30.903 -57.797  1.00 33.77           C  
ANISOU 5902  CB  ARG A 719     4838   4379   3614   -686    599   -742       C  
ATOM   5903  CG  ARG A 719      -2.151 -31.608 -58.398  1.00 33.59           C  
ANISOU 5903  CG  ARG A 719     4833   4327   3602   -725    587   -765       C  
ATOM   5904  CD  ARG A 719      -3.180 -30.602 -58.944  1.00 35.14           C  
ANISOU 5904  CD  ARG A 719     5065   4551   3735   -762    502   -759       C  
ATOM   5905  NE  ARG A 719      -2.589 -29.699 -59.927  1.00 32.48           N  
ANISOU 5905  NE  ARG A 719     4783   4240   3318   -806    488   -777       N  
ATOM   5906  CZ  ARG A 719      -2.534 -29.941 -61.235  1.00 35.81           C  
ANISOU 5906  CZ  ARG A 719     5257   4661   3690   -868    500   -827       C  
ATOM   5907  NH1 ARG A 719      -3.045 -31.063 -61.734  1.00 34.83           N  
ANISOU 5907  NH1 ARG A 719     5132   4512   3590   -900    521   -873       N  
ATOM   5908  NH2 ARG A 719      -1.971 -29.055 -62.045  1.00 31.57           N  
ANISOU 5908  NH2 ARG A 719     4773   4144   3078   -900    495   -834       N  
ATOM   5909  N   TYR A 720      -2.682 -30.757 -54.691  1.00 33.47           N  
ANISOU 5909  N   TYR A 720     4704   4351   3664   -534    533   -612       N  
ATOM   5910  CA  TYR A 720      -3.047 -31.501 -53.481  1.00 34.66           C  
ANISOU 5910  CA  TYR A 720     4813   4483   3875   -462    561   -569       C  
ATOM   5911  C   TYR A 720      -3.513 -32.920 -53.784  1.00 35.41           C  
ANISOU 5911  C   TYR A 720     4904   4517   4034   -471    624   -586       C  
ATOM   5912  O   TYR A 720      -4.203 -33.148 -54.772  1.00 36.74           O  
ANISOU 5912  O   TYR A 720     5097   4663   4201   -537    614   -629       O  
ATOM   5913  CB  TYR A 720      -4.159 -30.790 -52.708  1.00 34.17           C  
ANISOU 5913  CB  TYR A 720     4742   4431   3810   -439    505   -527       C  
ATOM   5914  CG  TYR A 720      -3.829 -29.409 -52.197  1.00 35.06           C  
ANISOU 5914  CG  TYR A 720     4854   4595   3872   -424    452   -507       C  
ATOM   5915  CD1 TYR A 720      -2.840 -29.209 -51.233  1.00 37.28           C  
ANISOU 5915  CD1 TYR A 720     5103   4914   4146   -365    466   -489       C  
ATOM   5916  CD2 TYR A 720      -4.536 -28.302 -52.652  1.00 34.75           C  
ANISOU 5916  CD2 TYR A 720     4841   4568   3793   -466    390   -508       C  
ATOM   5917  CE1 TYR A 720      -2.545 -27.933 -50.762  1.00 36.25           C  
ANISOU 5917  CE1 TYR A 720     4968   4831   3974   -358    422   -484       C  
ATOM   5918  CE2 TYR A 720      -4.257 -27.027 -52.182  1.00 37.70           C  
ANISOU 5918  CE2 TYR A 720     5214   4980   4130   -455    354   -493       C  
ATOM   5919  CZ  TYR A 720      -3.264 -26.846 -51.241  1.00 37.90           C  
ANISOU 5919  CZ  TYR A 720     5208   5040   4152   -405    371   -486       C  
ATOM   5920  OH  TYR A 720      -3.000 -25.574 -50.782  1.00 38.24           O  
ANISOU 5920  OH  TYR A 720     5247   5120   4163   -402    339   -484       O  
ATOM   5921  N   ALA A 721      -3.134 -33.865 -52.927  1.00 34.73           N  
ANISOU 5921  N   ALA A 721     4784   4407   4004   -403    690   -555       N  
ATOM   5922  CA  ALA A 721      -3.655 -35.226 -53.009  1.00 37.49           C  
ANISOU 5922  CA  ALA A 721     5126   4688   4431   -401    764   -564       C  
ATOM   5923  C   ALA A 721      -5.166 -35.217 -52.739  1.00 38.58           C  
ANISOU 5923  C   ALA A 721     5260   4798   4599   -411    737   -552       C  
ATOM   5924  O   ALA A 721      -5.924 -35.941 -53.389  1.00 39.17           O  
ANISOU 5924  O   ALA A 721     5339   4824   4718   -461    764   -594       O  
ATOM   5925  CB  ALA A 721      -2.929 -36.143 -52.020  1.00 36.80           C  
ANISOU 5925  CB  ALA A 721     5006   4581   4396   -309    844   -515       C  
ATOM   5926  N   GLU A 722      -5.581 -34.392 -51.777  1.00 37.19           N  
ANISOU 5926  N   GLU A 722     5072   4654   4403   -365    686   -500       N  
ATOM   5927  CA  GLU A 722      -6.994 -34.180 -51.458  1.00 38.62           C  
ANISOU 5927  CA  GLU A 722     5247   4816   4612   -371    654   -485       C  
ATOM   5928  C   GLU A 722      -7.314 -32.690 -51.556  1.00 36.31           C  
ANISOU 5928  C   GLU A 722     4968   4577   4250   -395    556   -478       C  
ATOM   5929  O   GLU A 722      -6.521 -31.862 -51.096  1.00 35.04           O  
ANISOU 5929  O   GLU A 722     4810   4467   4038   -364    529   -455       O  
ATOM   5930  CB  GLU A 722      -7.323 -34.674 -50.043  1.00 39.56           C  
ANISOU 5930  CB  GLU A 722     5340   4907   4783   -283    704   -418       C  
ATOM   5931  CG  GLU A 722      -7.038 -36.149 -49.791  1.00 46.21           C  
ANISOU 5931  CG  GLU A 722     6170   5687   5703   -243    815   -409       C  
ATOM   5932  CD  GLU A 722      -7.994 -37.075 -50.523  1.00 53.11           C  
ANISOU 5932  CD  GLU A 722     7039   6486   6653   -304    861   -460       C  
ATOM   5933  OE1 GLU A 722      -9.167 -36.691 -50.720  1.00 56.69           O  
ANISOU 5933  OE1 GLU A 722     7488   6932   7119   -347    814   -479       O  
ATOM   5934  OE2 GLU A 722      -7.570 -38.192 -50.897  1.00 58.12           O  
ANISOU 5934  OE2 GLU A 722     7673   7071   7340   -310    947   -485       O  
ATOM   5935  N   PRO A 723      -8.477 -32.339 -52.138  1.00 33.43           N  
ANISOU 5935  N   PRO A 723     4609   4204   3888   -448    505   -500       N  
ATOM   5936  CA  PRO A 723      -8.853 -30.924 -52.239  1.00 31.56           C  
ANISOU 5936  CA  PRO A 723     4386   4012   3593   -465    419   -486       C  
ATOM   5937  C   PRO A 723      -8.838 -30.251 -50.870  1.00 32.19           C  
ANISOU 5937  C   PRO A 723     4449   4111   3669   -395    411   -425       C  
ATOM   5938  O   PRO A 723      -9.132 -30.893 -49.859  1.00 30.82           O  
ANISOU 5938  O   PRO A 723     4253   3909   3549   -338    458   -390       O  
ATOM   5939  CB  PRO A 723     -10.281 -30.971 -52.798  1.00 30.73           C  
ANISOU 5939  CB  PRO A 723     4274   3885   3518   -510    380   -508       C  
ATOM   5940  CG  PRO A 723     -10.758 -32.383 -52.529  1.00 33.16           C  
ANISOU 5940  CG  PRO A 723     4552   4130   3916   -501    455   -522       C  
ATOM   5941  CD  PRO A 723      -9.537 -33.230 -52.643  1.00 32.76           C  
ANISOU 5941  CD  PRO A 723     4511   4067   3868   -489    528   -537       C  
ATOM   5942  N   LYS A 724      -8.490 -28.969 -50.842  1.00 33.19           N  
ANISOU 5942  N   LYS A 724     4592   4285   3735   -399    357   -415       N  
ATOM   5943  CA  LYS A 724      -8.324 -28.247 -49.589  1.00 35.81           C  
ANISOU 5943  CA  LYS A 724     4910   4643   4054   -340    349   -371       C  
ATOM   5944  C   LYS A 724      -9.178 -26.983 -49.588  1.00 35.26           C  
ANISOU 5944  C   LYS A 724     4848   4585   3964   -359    286   -356       C  
ATOM   5945  O   LYS A 724      -9.229 -26.254 -50.585  1.00 34.94           O  
ANISOU 5945  O   LYS A 724     4833   4559   3886   -412    242   -377       O  
ATOM   5946  CB  LYS A 724      -6.841 -27.917 -49.373  1.00 36.75           C  
ANISOU 5946  CB  LYS A 724     5029   4809   4125   -320    359   -380       C  
ATOM   5947  CG  LYS A 724      -6.509 -27.185 -48.076  1.00 45.72           C  
ANISOU 5947  CG  LYS A 724     6147   5986   5238   -261    350   -348       C  
ATOM   5948  CD  LYS A 724      -4.998 -27.199 -47.790  1.00 52.14           C  
ANISOU 5948  CD  LYS A 724     6945   6847   6018   -233    368   -365       C  
ATOM   5949  CE  LYS A 724      -4.560 -26.035 -46.893  1.00 56.43           C  
ANISOU 5949  CE  LYS A 724     7475   7447   6521   -207    337   -362       C  
ATOM   5950  NZ  LYS A 724      -5.191 -26.056 -45.539  1.00 57.92           N  
ANISOU 5950  NZ  LYS A 724     7648   7642   6718   -140    340   -317       N  
ATOM   5951  N   LEU A 725      -9.847 -26.728 -48.468  1.00 32.57           N  
ANISOU 5951  N   LEU A 725     4489   4236   3650   -312    288   -316       N  
ATOM   5952  CA  LEU A 725     -10.710 -25.560 -48.356  1.00 31.47           C  
ANISOU 5952  CA  LEU A 725     4353   4100   3504   -323    238   -297       C  
ATOM   5953  C   LEU A 725      -9.914 -24.299 -48.063  1.00 30.40           C  
ANISOU 5953  C   LEU A 725     4230   4009   3312   -319    216   -296       C  
ATOM   5954  O   LEU A 725      -9.192 -24.219 -47.071  1.00 30.25           O  
ANISOU 5954  O   LEU A 725     4199   4018   3276   -274    239   -288       O  
ATOM   5955  CB  LEU A 725     -11.792 -25.771 -47.288  1.00 30.29           C  
ANISOU 5955  CB  LEU A 725     4179   3917   3412   -279    258   -258       C  
ATOM   5956  CG  LEU A 725     -12.695 -27.002 -47.461  1.00 30.11           C  
ANISOU 5956  CG  LEU A 725     4137   3840   3465   -283    291   -262       C  
ATOM   5957  CD1 LEU A 725     -13.719 -27.109 -46.336  1.00 30.47           C  
ANISOU 5957  CD1 LEU A 725     4160   3847   3569   -237    320   -221       C  
ATOM   5958  CD2 LEU A 725     -13.385 -26.998 -48.817  1.00 27.63           C  
ANISOU 5958  CD2 LEU A 725     3823   3514   3159   -352    245   -298       C  
ATOM   5959  N   LYS A 726     -10.025 -23.321 -48.951  1.00 29.12           N  
ANISOU 5959  N   LYS A 726     4092   3855   3118   -367    174   -307       N  
ATOM   5960  CA  LYS A 726      -9.535 -22.001 -48.630  1.00 29.29           C  
ANISOU 5960  CA  LYS A 726     4123   3903   3101   -367    160   -305       C  
ATOM   5961  C   LYS A 726     -10.727 -21.182 -48.148  1.00 27.60           C  
ANISOU 5961  C   LYS A 726     3903   3669   2915   -355    137   -270       C  
ATOM   5962  O   LYS A 726     -11.615 -20.830 -48.935  1.00 28.04           O  
ANISOU 5962  O   LYS A 726     3969   3704   2980   -384    101   -258       O  
ATOM   5963  CB  LYS A 726      -8.849 -21.332 -49.819  1.00 28.24           C  
ANISOU 5963  CB  LYS A 726     4025   3786   2921   -419    145   -332       C  
ATOM   5964  CG  LYS A 726      -8.058 -20.104 -49.384  1.00 32.39           C  
ANISOU 5964  CG  LYS A 726     4555   4336   3416   -419    152   -342       C  
ATOM   5965  CD  LYS A 726      -7.864 -19.080 -50.487  1.00 34.20           C  
ANISOU 5965  CD  LYS A 726     4823   4560   3610   -468    138   -349       C  
ATOM   5966  CE  LYS A 726      -7.083 -17.884 -49.942  1.00 37.60           C  
ANISOU 5966  CE  LYS A 726     5252   5008   4027   -469    160   -366       C  
ATOM   5967  NZ  LYS A 726      -7.002 -16.750 -50.900  1.00 38.67           N  
ANISOU 5967  NZ  LYS A 726     5430   5126   4137   -510    160   -363       N  
ATOM   5968  N   ILE A 727     -10.753 -20.910 -46.848  1.00 24.49           N  
ANISOU 5968  N   ILE A 727     3492   3283   2532   -310    157   -253       N  
ATOM   5969  CA  ILE A 727     -11.831 -20.138 -46.248  1.00 22.69           C  
ANISOU 5969  CA  ILE A 727     3256   3030   2334   -295    146   -221       C  
ATOM   5970  C   ILE A 727     -11.250 -18.880 -45.634  1.00 23.60           C  
ANISOU 5970  C   ILE A 727     3378   3171   2418   -291    152   -230       C  
ATOM   5971  O   ILE A 727     -10.319 -18.955 -44.835  1.00 25.47           O  
ANISOU 5971  O   ILE A 727     3604   3446   2626   -265    174   -251       O  
ATOM   5972  CB  ILE A 727     -12.578 -20.936 -45.169  1.00 21.32           C  
ANISOU 5972  CB  ILE A 727     3058   2833   2208   -245    176   -193       C  
ATOM   5973  CG1 ILE A 727     -13.068 -22.284 -45.725  1.00 21.01           C  
ANISOU 5973  CG1 ILE A 727     3008   2764   2212   -251    185   -194       C  
ATOM   5974  CG2 ILE A 727     -13.748 -20.115 -44.621  1.00 20.39           C  
ANISOU 5974  CG2 ILE A 727     2933   2685   2130   -234    169   -162       C  
ATOM   5975  CD1 ILE A 727     -13.610 -23.233 -44.662  1.00 17.60           C  
ANISOU 5975  CD1 ILE A 727     2555   2302   1830   -198    234   -167       C  
ATOM   5976  N   MET A 728     -11.793 -17.727 -46.008  1.00 23.68           N  
ANISOU 5976  N   MET A 728     3402   3162   2435   -316    133   -217       N  
ATOM   5977  CA  MET A 728     -11.357 -16.463 -45.417  1.00 24.90           C  
ANISOU 5977  CA  MET A 728     3561   3329   2571   -317    148   -231       C  
ATOM   5978  C   MET A 728     -12.520 -15.674 -44.831  1.00 24.91           C  
ANISOU 5978  C   MET A 728     3556   3294   2615   -302    151   -196       C  
ATOM   5979  O   MET A 728     -13.578 -15.542 -45.457  1.00 25.14           O  
ANISOU 5979  O   MET A 728     3587   3285   2679   -311    126   -161       O  
ATOM   5980  CB  MET A 728     -10.611 -15.585 -46.440  1.00 27.11           C  
ANISOU 5980  CB  MET A 728     3869   3614   2818   -365    144   -253       C  
ATOM   5981  CG  MET A 728      -9.389 -16.224 -47.108  1.00 34.18           C  
ANISOU 5981  CG  MET A 728     4772   4542   3674   -386    149   -292       C  
ATOM   5982  SD  MET A 728      -8.129 -16.906 -45.998  1.00 45.59           S  
ANISOU 5982  SD  MET A 728     6182   6043   5096   -352    176   -335       S  
ATOM   5983  CE  MET A 728      -7.728 -15.497 -45.000  1.00 32.97           C  
ANISOU 5983  CE  MET A 728     4572   4464   3490   -352    197   -366       C  
ATOM   5984  N   GLY A 729     -12.313 -15.145 -43.630  1.00 24.75           N  
ANISOU 5984  N   GLY A 729     3526   3287   2591   -278    180   -209       N  
ATOM   5985  CA  GLY A 729     -13.256 -14.213 -43.018  1.00 24.18           C  
ANISOU 5985  CA  GLY A 729     3451   3178   2557   -268    194   -185       C  
ATOM   5986  C   GLY A 729     -14.416 -14.865 -42.306  1.00 25.13           C  
ANISOU 5986  C   GLY A 729     3553   3269   2726   -228    202   -147       C  
ATOM   5987  O   GLY A 729     -14.914 -14.332 -41.321  1.00 25.87           O  
ANISOU 5987  O   GLY A 729     3641   3346   2841   -206    230   -139       O  
ATOM   5988  N   LEU A 730     -14.843 -16.023 -42.800  1.00 24.75           N  
ANISOU 5988  N   LEU A 730     3495   3209   2699   -222    184   -128       N  
ATOM   5989  CA  LEU A 730     -15.992 -16.722 -42.242  1.00 24.80           C  
ANISOU 5989  CA  LEU A 730     3482   3178   2765   -190    199    -95       C  
ATOM   5990  C   LEU A 730     -15.710 -17.240 -40.838  1.00 26.56           C  
ANISOU 5990  C   LEU A 730     3700   3419   2971   -139    245    -97       C  
ATOM   5991  O   LEU A 730     -14.549 -17.365 -40.419  1.00 25.41           O  
ANISOU 5991  O   LEU A 730     3563   3327   2765   -126    254   -126       O  
ATOM   5992  CB  LEU A 730     -16.439 -17.877 -43.154  1.00 25.55           C  
ANISOU 5992  CB  LEU A 730     3563   3255   2889   -202    175    -87       C  
ATOM   5993  CG  LEU A 730     -16.623 -17.580 -44.646  1.00 22.96           C  
ANISOU 5993  CG  LEU A 730     3242   2925   2558   -249    122    -89       C  
ATOM   5994  CD1 LEU A 730     -17.188 -18.810 -45.335  1.00 17.89           C  
ANISOU 5994  CD1 LEU A 730     2580   2267   1951   -260    104    -92       C  
ATOM   5995  CD2 LEU A 730     -17.500 -16.351 -44.883  1.00 21.11           C  
ANISOU 5995  CD2 LEU A 730     3004   2661   2354   -257    101    -60       C  
ATOM   5996  N   GLU A 731     -16.792 -17.552 -40.131  1.00 25.98           N  
ANISOU 5996  N   GLU A 731     3614   3303   2954   -108    274    -65       N  
ATOM   5997  CA  GLU A 731     -16.756 -17.882 -38.722  1.00 26.01           C  
ANISOU 5997  CA  GLU A 731     3622   3316   2944    -53    325    -56       C  
ATOM   5998  C   GLU A 731     -15.862 -19.077 -38.387  1.00 26.65           C  
ANISOU 5998  C   GLU A 731     3708   3438   2980    -17    343    -61       C  
ATOM   5999  O   GLU A 731     -15.349 -19.177 -37.277  1.00 28.40           O  
ANISOU 5999  O   GLU A 731     3940   3699   3153     31    373    -62       O  
ATOM   6000  CB  GLU A 731     -18.179 -18.083 -38.209  1.00 25.70           C  
ANISOU 6000  CB  GLU A 731     3568   3211   2986    -31    361    -17       C  
ATOM   6001  CG  GLU A 731     -18.892 -16.773 -37.874  1.00 32.04           C  
ANISOU 6001  CG  GLU A 731     4370   3984   3820    -41    368     -9       C  
ATOM   6002  CD  GLU A 731     -19.477 -16.025 -39.086  1.00 34.66           C  
ANISOU 6002  CD  GLU A 731     4688   4286   4197    -89    319     -2       C  
ATOM   6003  OE1 GLU A 731     -19.247 -16.428 -40.258  1.00 29.35           O  
ANISOU 6003  OE1 GLU A 731     4009   3624   3518   -119    272     -9       O  
ATOM   6004  OE2 GLU A 731     -20.184 -15.018 -38.848  1.00 34.06           O  
ANISOU 6004  OE2 GLU A 731     4606   4173   4161    -92    331     12       O  
ATOM   6005  N   THR A 732     -15.665 -19.966 -39.353  1.00 24.65           N  
ANISOU 6005  N   THR A 732     3447   3178   2740    -37    325    -64       N  
ATOM   6006  CA  THR A 732     -14.736 -21.076 -39.198  1.00 25.43           C  
ANISOU 6006  CA  THR A 732     3550   3312   2802     -5    343    -69       C  
ATOM   6007  C   THR A 732     -13.318 -20.612 -38.863  1.00 26.10           C  
ANISOU 6007  C   THR A 732     3642   3475   2799      4    328   -103       C  
ATOM   6008  O   THR A 732     -12.545 -21.374 -38.290  1.00 27.71           O  
ANISOU 6008  O   THR A 732     3845   3719   2964     53    350   -100       O  
ATOM   6009  CB  THR A 732     -14.655 -21.905 -40.490  1.00 25.60           C  
ANISOU 6009  CB  THR A 732     3563   3314   2850    -44    323    -81       C  
ATOM   6010  OG1 THR A 732     -14.432 -21.022 -41.596  1.00 25.11           O  
ANISOU 6010  OG1 THR A 732     3505   3264   2770   -105    269   -109       O  
ATOM   6011  CG2 THR A 732     -15.928 -22.663 -40.716  1.00 23.26           C  
ANISOU 6011  CG2 THR A 732     3250   2949   2641    -47    345    -57       C  
ATOM   6012  N   GLN A 733     -12.988 -19.369 -39.219  1.00 25.75           N  
ANISOU 6012  N   GLN A 733     3601   3451   2731    -40    296   -136       N  
ATOM   6013  CA  GLN A 733     -11.611 -18.854 -39.140  1.00 25.20           C  
ANISOU 6013  CA  GLN A 733     3530   3452   2591    -48    279   -184       C  
ATOM   6014  C   GLN A 733     -11.362 -17.995 -37.908  1.00 25.77           C  
ANISOU 6014  C   GLN A 733     3603   3568   2622    -22    292   -205       C  
ATOM   6015  O   GLN A 733     -10.227 -17.622 -37.626  1.00 26.12           O  
ANISOU 6015  O   GLN A 733     3638   3679   2609    -22    281   -252       O  
ATOM   6016  CB  GLN A 733     -11.250 -18.054 -40.406  1.00 24.83           C  
ANISOU 6016  CB  GLN A 733     3489   3400   2545   -118    245   -215       C  
ATOM   6017  CG  GLN A 733     -11.533 -18.776 -41.739  1.00 22.85           C  
ANISOU 6017  CG  GLN A 733     3244   3113   2326   -152    226   -202       C  
ATOM   6018  CD  GLN A 733     -10.984 -20.191 -41.763  1.00 27.60           C  
ANISOU 6018  CD  GLN A 733     3837   3730   2920   -122    241   -199       C  
ATOM   6019  OE1 GLN A 733     -11.743 -21.164 -41.700  1.00 27.64           O  
ANISOU 6019  OE1 GLN A 733     3837   3695   2968   -100    261   -167       O  
ATOM   6020  NE2 GLN A 733      -9.656 -20.316 -41.826  1.00 24.52           N  
ANISOU 6020  NE2 GLN A 733     3442   3394   2481   -121    239   -234       N  
ATOM   6021  N   LYS A 734     -12.421 -17.688 -37.172  1.00 26.69           N  
ANISOU 6021  N   LYS A 734     3726   3646   2769     -2    318   -176       N  
ATOM   6022  CA  LYS A 734     -12.318 -16.780 -36.035  1.00 28.70           C  
ANISOU 6022  CA  LYS A 734     3985   3935   2986     16    336   -201       C  
ATOM   6023  C   LYS A 734     -12.074 -17.528 -34.729  1.00 28.19           C  
ANISOU 6023  C   LYS A 734     3923   3919   2868     94    363   -186       C  
ATOM   6024  O   LYS A 734     -12.758 -18.503 -34.433  1.00 29.96           O  
ANISOU 6024  O   LYS A 734     4155   4105   3121    138    394   -132       O  
ATOM   6025  CB  LYS A 734     -13.586 -15.943 -35.929  1.00 30.18           C  
ANISOU 6025  CB  LYS A 734     4180   4052   3235     -4    355   -179       C  
ATOM   6026  CG  LYS A 734     -13.725 -14.889 -37.016  1.00 36.43           C  
ANISOU 6026  CG  LYS A 734     4972   4808   4063    -72    331   -195       C  
ATOM   6027  CD  LYS A 734     -15.171 -14.382 -37.135  1.00 44.71           C  
ANISOU 6027  CD  LYS A 734     6022   5776   5191    -81    347   -153       C  
ATOM   6028  CE  LYS A 734     -15.580 -13.446 -35.998  1.00 48.06           C  
ANISOU 6028  CE  LYS A 734     6452   6191   5618    -68    389   -164       C  
ATOM   6029  NZ  LYS A 734     -14.957 -12.093 -36.121  1.00 53.79           N  
ANISOU 6029  NZ  LYS A 734     7182   6932   6325   -112    391   -216       N  
ATOM   6030  N   SER A 735     -11.107 -17.060 -33.944  1.00 28.26           N  
ANISOU 6030  N   SER A 735     3925   4011   2800    111    355   -235       N  
ATOM   6031  CA  SER A 735     -10.792 -17.675 -32.652  1.00 27.98           C  
ANISOU 6031  CA  SER A 735     3896   4041   2696    193    374   -221       C  
ATOM   6032  C   SER A 735     -11.921 -17.511 -31.637  1.00 28.92           C  
ANISOU 6032  C   SER A 735     4041   4121   2828    229    423   -185       C  
ATOM   6033  O   SER A 735     -11.963 -18.210 -30.626  1.00 28.99           O  
ANISOU 6033  O   SER A 735     4065   4160   2791    305    453   -151       O  
ATOM   6034  CB  SER A 735      -9.486 -17.125 -32.087  1.00 27.62           C  
ANISOU 6034  CB  SER A 735     3828   4105   2560    199    344   -294       C  
ATOM   6035  OG  SER A 735      -9.592 -15.740 -31.822  1.00 25.78           O  
ANISOU 6035  OG  SER A 735     3594   3875   2326    149    346   -353       O  
ATOM   6036  N   SER A 736     -12.834 -16.589 -31.928  1.00 27.51           N  
ANISOU 6036  N   SER A 736     3868   3872   2713    176    435   -189       N  
ATOM   6037  CA  SER A 736     -13.984 -16.308 -31.075  1.00 27.46           C  
ANISOU 6037  CA  SER A 736     3882   3815   2736    200    487   -159       C  
ATOM   6038  C   SER A 736     -15.150 -17.287 -31.265  1.00 24.98           C  
ANISOU 6038  C   SER A 736     3576   3412   2502    226    525    -83       C  
ATOM   6039  O   SER A 736     -16.040 -17.365 -30.426  1.00 29.02           O  
ANISOU 6039  O   SER A 736     4106   3884   3035    262    579    -50       O  
ATOM   6040  CB  SER A 736     -14.469 -14.889 -31.341  1.00 25.76           C  
ANISOU 6040  CB  SER A 736     3664   3556   2567    134    489   -194       C  
ATOM   6041  OG  SER A 736     -14.705 -14.729 -32.720  1.00 26.41           O  
ANISOU 6041  OG  SER A 736     3733   3584   2720     77    458   -184       O  
ATOM   6042  N   THR A 737     -15.147 -18.011 -32.375  1.00 22.59           N  
ANISOU 6042  N   THR A 737     3258   3078   2248    203    501    -63       N  
ATOM   6043  CA  THR A 737     -16.164 -19.001 -32.664  1.00 22.46           C  
ANISOU 6043  CA  THR A 737     3240   2981   2314    219    535     -6       C  
ATOM   6044  C   THR A 737     -15.857 -20.296 -31.899  1.00 25.00           C  
ANISOU 6044  C   THR A 737     3576   3324   2597    299    578     34       C  
ATOM   6045  O   THR A 737     -14.720 -20.768 -31.923  1.00 25.17           O  
ANISOU 6045  O   THR A 737     3597   3417   2551    324    554     21       O  
ATOM   6046  CB  THR A 737     -16.182 -19.294 -34.167  1.00 23.18           C  
ANISOU 6046  CB  THR A 737     3308   3039   2461    162    490    -11       C  
ATOM   6047  OG1 THR A 737     -16.494 -18.092 -34.879  1.00 24.16           O  
ANISOU 6047  OG1 THR A 737     3423   3141   2617     97    454    -37       O  
ATOM   6048  CG2 THR A 737     -17.189 -20.371 -34.524  1.00 20.06           C  
ANISOU 6048  CG2 THR A 737     2902   2565   2154    171    523     33       C  
ATOM   6049  N   PRO A 738     -16.871 -20.880 -31.223  1.00 20.55           N  
ANISOU 6049  N   PRO A 738     3005   2920   1883    315     64    407       N  
ATOM   6050  CA  PRO A 738     -16.663 -22.127 -30.482  1.00 21.93           C  
ANISOU 6050  CA  PRO A 738     3152   3108   2074    349     76    472       C  
ATOM   6051  C   PRO A 738     -16.016 -23.213 -31.340  1.00 22.21           C  
ANISOU 6051  C   PRO A 738     3200   3065   2174    319     75    461       C  
ATOM   6052  O   PRO A 738     -16.303 -23.321 -32.526  1.00 21.98           O  
ANISOU 6052  O   PRO A 738     3190   2978   2182    262     72    431       O  
ATOM   6053  CB  PRO A 738     -18.083 -22.528 -30.072  1.00 23.42           C  
ANISOU 6053  CB  PRO A 738     3318   3315   2266    349     87    559       C  
ATOM   6054  CG  PRO A 738     -18.808 -21.222 -29.953  1.00 21.10           C  
ANISOU 6054  CG  PRO A 738     3022   3071   1923    361     78    522       C  
ATOM   6055  CD  PRO A 738     -18.260 -20.395 -31.091  1.00 19.52           C  
ANISOU 6055  CD  PRO A 738     2868   2810   1737    321     62    439       C  
ATOM   6056  N   LYS A 739     -15.132 -23.997 -30.739  1.00 26.27           N  
ANISOU 6056  N   LYS A 739     3698   3586   2697    365     73    479       N  
ATOM   6057  CA  LYS A 739     -14.414 -25.041 -31.467  1.00 31.01           C  
ANISOU 6057  CA  LYS A 739     4305   4113   3363    357     65    452       C  
ATOM   6058  C   LYS A 739     -15.325 -26.005 -32.229  1.00 30.35           C  
ANISOU 6058  C   LYS A 739     4234   3935   3362    308     67    486       C  
ATOM   6059  O   LYS A 739     -15.074 -26.308 -33.398  1.00 30.24           O  
ANISOU 6059  O   LYS A 739     4229   3869   3391    268     59    415       O  
ATOM   6060  CB  LYS A 739     -13.461 -25.798 -30.530  1.00 33.78           C  
ANISOU 6060  CB  LYS A 739     4635   4486   3713    435     57    483       C  
ATOM   6061  CG  LYS A 739     -12.115 -25.109 -30.373  1.00 39.60           C  
ANISOU 6061  CG  LYS A 739     5354   5303   4391    467     49    390       C  
ATOM   6062  CD  LYS A 739     -11.322 -25.147 -31.684  1.00 46.13           C  
ANISOU 6062  CD  LYS A 739     6186   6095   5245    423     43    282       C  
ATOM   6063  CE  LYS A 739     -10.220 -24.094 -31.714  1.00 50.98           C  
ANISOU 6063  CE  LYS A 739     6779   6799   5792    414     44    184       C  
ATOM   6064  NZ  LYS A 739      -9.108 -24.415 -30.764  1.00 53.32           N  
ANISOU 6064  NZ  LYS A 739     7033   7170   6054    498     32    168       N  
ATOM   6065  N   ALA A 740     -16.384 -26.467 -31.570  1.00 29.57           N  
ANISOU 6065  N   ALA A 740     4127   3826   3282    306     77    589       N  
ATOM   6066  CA  ALA A 740     -17.306 -27.426 -32.173  1.00 30.92           C  
ANISOU 6066  CA  ALA A 740     4302   3907   3540    251     79    625       C  
ATOM   6067  C   ALA A 740     -18.104 -26.791 -33.305  1.00 28.91           C  
ANISOU 6067  C   ALA A 740     4051   3655   3277    185     79    563       C  
ATOM   6068  O   ALA A 740     -18.463 -27.458 -34.267  1.00 32.55           O  
ANISOU 6068  O   ALA A 740     4513   4048   3805    134     73    528       O  
ATOM   6069  CB  ALA A 740     -18.234 -28.019 -31.114  1.00 29.60           C  
ANISOU 6069  CB  ALA A 740     4115   3746   3384    253     94    761       C  
ATOM   6070  N   VAL A 741     -18.371 -25.499 -33.173  1.00 27.95           N  
ANISOU 6070  N   VAL A 741     3930   3614   3074    191     83    545       N  
ATOM   6071  CA  VAL A 741     -19.041 -24.720 -34.200  1.00 25.65           C  
ANISOU 6071  CA  VAL A 741     3648   3335   2761    145     77    495       C  
ATOM   6072  C   VAL A 741     -18.134 -24.463 -35.410  1.00 25.80           C  
ANISOU 6072  C   VAL A 741     3687   3337   2780    118     66    399       C  
ATOM   6073  O   VAL A 741     -18.600 -24.518 -36.551  1.00 24.80           O  
ANISOU 6073  O   VAL A 741     3560   3196   2666     69     59    361       O  
ATOM   6074  CB  VAL A 741     -19.571 -23.379 -33.637  1.00 26.26           C  
ANISOU 6074  CB  VAL A 741     3726   3491   2762    173     77    506       C  
ATOM   6075  CG1 VAL A 741     -20.227 -22.559 -34.738  1.00 21.93           C  
ANISOU 6075  CG1 VAL A 741     3193   2946   2194    138     63    464       C  
ATOM   6076  CG2 VAL A 741     -20.550 -23.640 -32.510  1.00 27.86           C  
ANISOU 6076  CG2 VAL A 741     3891   3743   2950    198     90    592       C  
ATOM   6077  N   GLN A 742     -16.853 -24.184 -35.170  1.00 23.42           N  
ANISOU 6077  N   GLN A 742     3392   3053   2452    146     64    359       N  
ATOM   6078  CA  GLN A 742     -15.900 -24.052 -36.270  1.00 24.95           C  
ANISOU 6078  CA  GLN A 742     3592   3250   2639    115     58    270       C  
ATOM   6079  C   GLN A 742     -15.902 -25.332 -37.102  1.00 25.63           C  
ANISOU 6079  C   GLN A 742     3662   3280   2796     94     52    232       C  
ATOM   6080  O   GLN A 742     -15.964 -25.285 -38.332  1.00 25.41           O  
ANISOU 6080  O   GLN A 742     3629   3263   2763     47     47    170       O  
ATOM   6081  CB  GLN A 742     -14.475 -23.795 -35.772  1.00 26.11           C  
ANISOU 6081  CB  GLN A 742     3732   3434   2754    150     59    229       C  
ATOM   6082  CG  GLN A 742     -14.249 -22.517 -34.974  1.00 25.93           C  
ANISOU 6082  CG  GLN A 742     3720   3466   2668    167     61    237       C  
ATOM   6083  CD  GLN A 742     -12.810 -22.407 -34.503  1.00 25.52           C  
ANISOU 6083  CD  GLN A 742     3648   3461   2589    196     62    184       C  
ATOM   6084  OE1 GLN A 742     -12.128 -23.415 -34.329  1.00 26.95           O  
ANISOU 6084  OE1 GLN A 742     3805   3636   2798    235     58    170       O  
ATOM   6085  NE2 GLN A 742     -12.336 -21.184 -34.319  1.00 23.59           N  
ANISOU 6085  NE2 GLN A 742     3410   3259   2294    178     62    149       N  
ATOM   6086  N   LYS A 743     -15.846 -26.466 -36.410  1.00 25.01           N  
ANISOU 6086  N   LYS A 743     3574   3143   2786    131     49    270       N  
ATOM   6087  CA  LYS A 743     -15.761 -27.778 -37.037  1.00 26.98           C  
ANISOU 6087  CA  LYS A 743     3811   3313   3126    122     36    227       C  
ATOM   6088  C   LYS A 743     -17.008 -28.073 -37.876  1.00 27.76           C  
ANISOU 6088  C   LYS A 743     3902   3383   3264     57     34    220       C  
ATOM   6089  O   LYS A 743     -16.897 -28.500 -39.026  1.00 27.60           O  
ANISOU 6089  O   LYS A 743     3864   3351   3272     26     22    126       O  
ATOM   6090  CB  LYS A 743     -15.574 -28.833 -35.947  1.00 28.46           C  
ANISOU 6090  CB  LYS A 743     4001   3428   3385    177     30    302       C  
ATOM   6091  CG  LYS A 743     -15.154 -30.208 -36.410  1.00 33.92           C  
ANISOU 6091  CG  LYS A 743     4687   4015   4187    193      7    250       C  
ATOM   6092  CD  LYS A 743     -14.846 -31.082 -35.189  1.00 38.83           C  
ANISOU 6092  CD  LYS A 743     5321   4566   4866    261     -2    350       C  
ATOM   6093  CE  LYS A 743     -15.095 -32.560 -35.460  1.00 41.80           C  
ANISOU 6093  CE  LYS A 743     5704   4786   5390    256    -25    351       C  
ATOM   6094  NZ  LYS A 743     -14.179 -33.105 -36.494  1.00 42.61           N  
ANISOU 6094  NZ  LYS A 743     5792   4854   5543    282    -55    198       N  
ATOM   6095  N   ALA A 744     -18.183 -27.822 -37.298  1.00 25.12           N  
ANISOU 6095  N   ALA A 744     3569   3054   2923     40     46    309       N  
ATOM   6096  CA  ALA A 744     -19.458 -28.098 -37.960  1.00 25.77           C  
ANISOU 6096  CA  ALA A 744     3631   3123   3036    -21     44    306       C  
ATOM   6097  C   ALA A 744     -19.719 -27.198 -39.164  1.00 24.99           C  
ANISOU 6097  C   ALA A 744     3527   3100   2867    -55     38    236       C  
ATOM   6098  O   ALA A 744     -20.130 -27.687 -40.227  1.00 25.43           O  
ANISOU 6098  O   ALA A 744     3559   3151   2954   -100     27    168       O  
ATOM   6099  CB  ALA A 744     -20.600 -28.006 -36.967  1.00 25.65           C  
ANISOU 6099  CB  ALA A 744     3606   3122   3016    -27     60    417       C  
ATOM   6100  N   LEU A 745     -19.469 -25.897 -39.000  1.00 21.32           N  
ANISOU 6100  N   LEU A 745     3086   2706   2311    -35     42    253       N  
ATOM   6101  CA  LEU A 745     -19.584 -24.944 -40.101  1.00 22.63           C  
ANISOU 6101  CA  LEU A 745     3256   2937   2405    -63     33    210       C  
ATOM   6102  C   LEU A 745     -18.622 -25.301 -41.244  1.00 24.46           C  
ANISOU 6102  C   LEU A 745     3474   3185   2633    -87     27    111       C  
ATOM   6103  O   LEU A 745     -18.992 -25.236 -42.418  1.00 28.12           O  
ANISOU 6103  O   LEU A 745     3919   3698   3069   -126     17     61       O  
ATOM   6104  CB  LEU A 745     -19.365 -23.497 -39.614  1.00 22.00           C  
ANISOU 6104  CB  LEU A 745     3212   2900   2248    -36     35    251       C  
ATOM   6105  CG  LEU A 745     -20.444 -22.804 -38.760  1.00 21.02           C  
ANISOU 6105  CG  LEU A 745     3093   2793   2100     -6     34    323       C  
ATOM   6106  CD1 LEU A 745     -19.969 -21.432 -38.293  1.00 18.01           C  
ANISOU 6106  CD1 LEU A 745     2749   2433   1661     26     30    335       C  
ATOM   6107  CD2 LEU A 745     -21.783 -22.678 -39.513  1.00 16.16           C  
ANISOU 6107  CD2 LEU A 745     2458   2210   1472    -30     22    328       C  
ATOM   6108  N   LYS A 746     -17.407 -25.714 -40.899  1.00 25.22           N  
ANISOU 6108  N   LYS A 746     3572   3260   2751    -60     30     77       N  
ATOM   6109  CA  LYS A 746     -16.436 -26.151 -41.899  1.00 27.30           C  
ANISOU 6109  CA  LYS A 746     3808   3555   3010    -73     24    -30       C  
ATOM   6110  C   LYS A 746     -16.932 -27.358 -42.700  1.00 28.53           C  
ANISOU 6110  C   LYS A 746     3926   3674   3239    -94      9   -105       C  
ATOM   6111  O   LYS A 746     -16.750 -27.408 -43.923  1.00 29.49           O  
ANISOU 6111  O   LYS A 746     4015   3866   3326   -125      1   -197       O  
ATOM   6112  CB  LYS A 746     -15.064 -26.439 -41.278  1.00 29.80           C  
ANISOU 6112  CB  LYS A 746     4124   3861   3339    -26     27    -58       C  
ATOM   6113  CG  LYS A 746     -13.986 -26.682 -42.333  1.00 28.84           C  
ANISOU 6113  CG  LYS A 746     3963   3806   3189    -38     22   -179       C  
ATOM   6114  CD  LYS A 746     -12.588 -26.753 -41.767  1.00 31.17           C  
ANISOU 6114  CD  LYS A 746     4246   4122   3474      9     25   -214       C  
ATOM   6115  CE  LYS A 746     -11.597 -27.058 -42.894  1.00 36.56           C  
ANISOU 6115  CE  LYS A 746     4875   4893   4123     -3     21   -347       C  
ATOM   6116  NZ  LYS A 746     -10.191 -26.709 -42.558  1.00 39.23           N  
ANISOU 6116  NZ  LYS A 746     5190   5305   4410     21     29   -387       N  
ATOM   6117  N   GLU A 747     -17.566 -28.312 -42.021  1.00 26.03           N  
ANISOU 6117  N   GLU A 747     3610   3256   3024    -83      4    -68       N  
ATOM   6118  CA  GLU A 747     -18.109 -29.490 -42.700  1.00 27.87           C  
ANISOU 6118  CA  GLU A 747     3808   3432   3350   -112    -14   -143       C  
ATOM   6119  C   GLU A 747     -19.327 -29.121 -43.570  1.00 28.78           C  
ANISOU 6119  C   GLU A 747     3898   3614   3424   -170    -16   -157       C  
ATOM   6120  O   GLU A 747     -19.520 -29.696 -44.635  1.00 30.03           O  
ANISOU 6120  O   GLU A 747     4012   3794   3604   -200    -33   -265       O  
ATOM   6121  CB  GLU A 747     -18.420 -30.615 -41.693  1.00 27.76           C  
ANISOU 6121  CB  GLU A 747     3807   3276   3465    -96    -17    -82       C  
ATOM   6122  CG  GLU A 747     -19.014 -31.900 -42.277  1.00 27.66           C  
ANISOU 6122  CG  GLU A 747     3763   3170   3577   -135    -38   -157       C  
ATOM   6123  CD  GLU A 747     -18.103 -32.626 -43.272  1.00 29.46           C  
ANISOU 6123  CD  GLU A 747     3960   3387   3847   -115    -66   -321       C  
ATOM   6124  OE1 GLU A 747     -18.592 -33.553 -43.950  1.00 33.87           O  
ANISOU 6124  OE1 GLU A 747     4484   3886   4500   -150    -87   -416       O  
ATOM   6125  OE2 GLU A 747     -16.908 -32.285 -43.393  1.00 31.33           O  
ANISOU 6125  OE2 GLU A 747     4197   3684   4024    -65    -66   -368       O  
ATOM   6126  N   CYS A 748     -20.126 -28.154 -43.121  1.00 28.63           N  
ANISOU 6126  N   CYS A 748     3899   3637   3341   -176     -4    -57       N  
ATOM   6127  CA  CYS A 748     -21.242 -27.640 -43.916  1.00 29.56           C  
ANISOU 6127  CA  CYS A 748     3992   3837   3403   -214    -12    -63       C  
ATOM   6128  C   CYS A 748     -20.741 -27.019 -45.223  1.00 28.34           C  
ANISOU 6128  C   CYS A 748     3822   3795   3150   -227    -21   -137       C  
ATOM   6129  O   CYS A 748     -21.243 -27.333 -46.303  1.00 30.30           O  
ANISOU 6129  O   CYS A 748     4023   4106   3384   -259    -36   -216       O  
ATOM   6130  CB  CYS A 748     -22.052 -26.607 -43.121  1.00 29.39           C  
ANISOU 6130  CB  CYS A 748     3997   3843   3327   -196     -2     52       C  
ATOM   6131  SG  CYS A 748     -23.099 -27.305 -41.817  1.00 32.47           S  
ANISOU 6131  SG  CYS A 748     4375   4158   3802   -201     11    142       S  
ATOM   6132  N   ILE A 749     -19.748 -26.141 -45.104  1.00 26.10           N  
ANISOU 6132  N   ILE A 749     3573   3547   2795   -206    -11   -110       N  
ATOM   6133  CA  ILE A 749     -19.059 -25.557 -46.250  1.00 24.29           C  
ANISOU 6133  CA  ILE A 749     3331   3430   2468   -227    -13   -163       C  
ATOM   6134  C   ILE A 749     -18.405 -26.624 -47.130  1.00 24.91           C  
ANISOU 6134  C   ILE A 749     3351   3537   2575   -239    -22   -305       C  
ATOM   6135  O   ILE A 749     -18.509 -26.558 -48.358  1.00 27.52           O  
ANISOU 6135  O   ILE A 749     3637   3982   2836   -268    -31   -374       O  
ATOM   6136  CB  ILE A 749     -17.994 -24.525 -45.803  1.00 23.44           C  
ANISOU 6136  CB  ILE A 749     3269   3338   2299   -215      3   -110       C  
ATOM   6137  CG1 ILE A 749     -18.662 -23.309 -45.158  1.00 22.35           C  
ANISOU 6137  CG1 ILE A 749     3185   3184   2124   -203      3      8       C  
ATOM   6138  CG2 ILE A 749     -17.129 -24.101 -46.976  1.00 22.44           C  
ANISOU 6138  CG2 ILE A 749     3119   3331   2077   -252      6   -165       C  
ATOM   6139  CD1 ILE A 749     -17.689 -22.383 -44.420  1.00 24.16           C  
ANISOU 6139  CD1 ILE A 749     3460   3396   2325   -190     17     55       C  
ATOM   6140  N   ARG A 750     -17.739 -27.602 -46.515  1.00 25.83           N  
ANISOU 6140  N   ARG A 750     3465   3560   2790   -208    -22   -350       N  
ATOM   6141  CA  ARG A 750     -17.151 -28.708 -47.278  1.00 27.44           C  
ANISOU 6141  CA  ARG A 750     3611   3773   3041   -203    -38   -502       C  
ATOM   6142  C   ARG A 750     -18.221 -29.353 -48.155  1.00 27.67           C  
ANISOU 6142  C   ARG A 750     3589   3821   3102   -239    -59   -581       C  
ATOM   6143  O   ARG A 750     -18.056 -29.454 -49.373  1.00 28.89           O  
ANISOU 6143  O   ARG A 750     3684   4096   3195   -258    -70   -695       O  
ATOM   6144  CB  ARG A 750     -16.483 -29.759 -46.371  1.00 27.49           C  
ANISOU 6144  CB  ARG A 750     3631   3642   3174   -151    -46   -525       C  
ATOM   6145  CG  ARG A 750     -15.612 -30.750 -47.163  1.00 26.87           C  
ANISOU 6145  CG  ARG A 750     3493   3581   3136   -127    -67   -698       C  
ATOM   6146  CD  ARG A 750     -15.302 -32.046 -46.406  1.00 30.25           C  
ANISOU 6146  CD  ARG A 750     3933   3837   3725    -72    -90   -728       C  
ATOM   6147  NE  ARG A 750     -16.486 -32.874 -46.161  1.00 30.43           N  
ANISOU 6147  NE  ARG A 750     3963   3724   3873   -101   -104   -705       N  
ATOM   6148  CZ  ARG A 750     -17.096 -33.635 -47.073  1.00 33.62           C  
ANISOU 6148  CZ  ARG A 750     4318   4118   4339   -136   -128   -828       C  
ATOM   6149  NH1 ARG A 750     -16.654 -33.693 -48.329  1.00 28.90           N  
ANISOU 6149  NH1 ARG A 750     3653   3650   3679   -138   -142   -990       N  
ATOM   6150  NH2 ARG A 750     -18.163 -34.344 -46.725  1.00 31.54           N  
ANISOU 6150  NH2 ARG A 750     4062   3724   4195   -175   -137   -793       N  
ATOM   6151  N   ARG A 751     -19.333 -29.738 -47.536  1.00 28.30           N  
ANISOU 6151  N   ARG A 751     3683   3801   3267   -253    -62   -521       N  
ATOM   6152  CA  ARG A 751     -20.448 -30.377 -48.244  1.00 29.92           C  
ANISOU 6152  CA  ARG A 751     3835   4018   3516   -296    -82   -595       C  
ATOM   6153  C   ARG A 751     -21.074 -29.523 -49.348  1.00 29.79           C  
ANISOU 6153  C   ARG A 751     3782   4176   3362   -325    -87   -609       C  
ATOM   6154  O   ARG A 751     -21.345 -30.035 -50.437  1.00 31.81           O  
ANISOU 6154  O   ARG A 751     3967   4512   3606   -349   -107   -739       O  
ATOM   6155  CB  ARG A 751     -21.508 -30.846 -47.248  1.00 30.91           C  
ANISOU 6155  CB  ARG A 751     3981   4015   3749   -316    -78   -507       C  
ATOM   6156  CG  ARG A 751     -21.046 -32.040 -46.436  1.00 30.16           C  
ANISOU 6156  CG  ARG A 751     3906   3743   3810   -299    -83   -516       C  
ATOM   6157  CD  ARG A 751     -21.839 -32.225 -45.159  1.00 30.31           C  
ANISOU 6157  CD  ARG A 751     3960   3651   3904   -314    -67   -372       C  
ATOM   6158  NE  ARG A 751     -21.496 -33.503 -44.535  1.00 30.34           N  
ANISOU 6158  NE  ARG A 751     3980   3480   4069   -305    -78   -378       N  
ATOM   6159  CZ  ARG A 751     -22.206 -34.623 -44.669  1.00 33.09           C  
ANISOU 6159  CZ  ARG A 751     4301   3718   4555   -360    -94   -425       C  
ATOM   6160  NH1 ARG A 751     -23.330 -34.629 -45.382  1.00 31.95           N  
ANISOU 6160  NH1 ARG A 751     4100   3638   4400   -430    -99   -480       N  
ATOM   6161  NH2 ARG A 751     -21.799 -35.739 -44.077  1.00 28.13           N  
ANISOU 6161  NH2 ARG A 751     3699   2911   4079   -346   -108   -415       N  
ATOM   6162  N   MET A 752     -21.297 -28.235 -49.069  1.00 27.39           N  
ANISOU 6162  N   MET A 752     3524   3929   2955   -317    -73   -478       N  
ATOM   6163  CA  MET A 752     -21.774 -27.269 -50.077  1.00 27.28           C  
ANISOU 6163  CA  MET A 752     3489   4076   2801   -331    -81   -461       C  
ATOM   6164  C   MET A 752     -20.881 -27.247 -51.323  1.00 28.73           C  
ANISOU 6164  C   MET A 752     3624   4401   2890   -342    -86   -565       C  
ATOM   6165  O   MET A 752     -21.363 -27.335 -52.451  1.00 29.74           O  
ANISOU 6165  O   MET A 752     3687   4663   2949   -362   -104   -641       O  
ATOM   6166  CB  MET A 752     -21.821 -25.847 -49.490  1.00 26.24           C  
ANISOU 6166  CB  MET A 752     3429   3950   2589   -309    -69   -304       C  
ATOM   6167  CG  MET A 752     -22.971 -25.579 -48.538  1.00 28.47           C  
ANISOU 6167  CG  MET A 752     3738   4163   2914   -293    -69   -206       C  
ATOM   6168  SD  MET A 752     -22.772 -24.062 -47.571  1.00 32.98           S  
ANISOU 6168  SD  MET A 752     4399   4703   3430   -251    -58    -52       S  
ATOM   6169  CE  MET A 752     -23.140 -22.809 -48.789  1.00 26.86           C  
ANISOU 6169  CE  MET A 752     3628   4068   2510   -251    -81    -10       C  
ATOM   6170  N   LEU A 753     -19.575 -27.138 -51.101  1.00 28.86           N  
ANISOU 6170  N   LEU A 753     3663   4406   2895   -328    -69   -572       N  
ATOM   6171  CA  LEU A 753     -18.623 -26.933 -52.186  1.00 29.24           C  
ANISOU 6171  CA  LEU A 753     3665   4612   2832   -342    -65   -650       C  
ATOM   6172  C   LEU A 753     -18.249 -28.221 -52.922  1.00 30.81           C  
ANISOU 6172  C   LEU A 753     3777   4850   3080   -337    -83   -848       C  
ATOM   6173  O   LEU A 753     -17.901 -28.183 -54.106  1.00 33.14           O  
ANISOU 6173  O   LEU A 753     4001   5323   3267   -353    -88   -942       O  
ATOM   6174  CB  LEU A 753     -17.354 -26.238 -51.663  1.00 27.02           C  
ANISOU 6174  CB  LEU A 753     3431   4322   2511   -335    -39   -585       C  
ATOM   6175  CG  LEU A 753     -17.431 -24.971 -50.790  1.00 25.76           C  
ANISOU 6175  CG  LEU A 753     3361   4102   2323   -335    -23   -410       C  
ATOM   6176  CD1 LEU A 753     -16.072 -24.283 -50.711  1.00 24.60           C  
ANISOU 6176  CD1 LEU A 753     3234   4003   2111   -352      1   -385       C  
ATOM   6177  CD2 LEU A 753     -18.479 -23.987 -51.252  1.00 24.33           C  
ANISOU 6177  CD2 LEU A 753     3203   3983   2058   -351    -34   -309       C  
ATOM   6178  N   GLN A 754     -18.315 -29.352 -52.226  1.00 28.83           N  
ANISOU 6178  N   GLN A 754     3529   4434   2991   -314    -95   -912       N  
ATOM   6179  CA  GLN A 754     -17.833 -30.614 -52.776  1.00 30.03           C  
ANISOU 6179  CA  GLN A 754     3608   4581   3219   -296   -118  -1108       C  
ATOM   6180  C   GLN A 754     -18.960 -31.565 -53.163  1.00 33.15           C  
ANISOU 6180  C   GLN A 754     3953   4931   3711   -320   -148  -1211       C  
ATOM   6181  O   GLN A 754     -18.799 -32.391 -54.070  1.00 32.60           O  
ANISOU 6181  O   GLN A 754     3800   4925   3661   -317   -174  -1400       O  
ATOM   6182  CB  GLN A 754     -16.883 -31.302 -51.793  1.00 30.80           C  
ANISOU 6182  CB  GLN A 754     3743   4517   3442   -246   -117  -1123       C  
ATOM   6183  CG  GLN A 754     -15.487 -30.669 -51.702  1.00 31.53           C  
ANISOU 6183  CG  GLN A 754     3843   4695   3440   -220    -95  -1105       C  
ATOM   6184  CD  GLN A 754     -14.578 -31.368 -50.697  1.00 32.13           C  
ANISOU 6184  CD  GLN A 754     3950   4622   3636   -157   -100  -1120       C  
ATOM   6185  OE1 GLN A 754     -14.814 -32.510 -50.314  1.00 36.78           O  
ANISOU 6185  OE1 GLN A 754     4540   5053   4380   -125   -127  -1181       O  
ATOM   6186  NE2 GLN A 754     -13.536 -30.677 -50.265  1.00 30.37           N  
ANISOU 6186  NE2 GLN A 754     3750   4448   3342   -139    -77  -1063       N  
ATOM   6187  N   GLU A 755     -20.100 -31.442 -52.487  1.00 33.63           N  
ANISOU 6187  N   GLU A 755     4056   4892   3830   -344   -145  -1097       N  
ATOM   6188  CA  GLU A 755     -21.141 -32.462 -52.570  1.00 36.50           C  
ANISOU 6188  CA  GLU A 755     4378   5169   4321   -377   -170  -1182       C  
ATOM   6189  C   GLU A 755     -22.520 -31.928 -52.946  1.00 35.98           C  
ANISOU 6189  C   GLU A 755     4285   5201   4185   -420   -173  -1132       C  
ATOM   6190  O   GLU A 755     -23.254 -32.591 -53.672  1.00 39.73           O  
ANISOU 6190  O   GLU A 755     4682   5720   4693   -455   -198  -1263       O  
ATOM   6191  CB  GLU A 755     -21.181 -33.282 -51.272  1.00 35.52           C  
ANISOU 6191  CB  GLU A 755     4314   4799   4384   -370   -168  -1122       C  
ATOM   6192  CG  GLU A 755     -19.957 -34.200 -51.106  1.00 39.24           C  
ANISOU 6192  CG  GLU A 755     4788   5162   4958   -319   -183  -1226       C  
ATOM   6193  CD  GLU A 755     -19.835 -34.822 -49.721  1.00 41.09           C  
ANISOU 6193  CD  GLU A 755     5096   5165   5352   -298   -179  -1122       C  
ATOM   6194  OE1 GLU A 755     -18.794 -35.457 -49.442  1.00 43.41           O  
ANISOU 6194  OE1 GLU A 755     5404   5367   5723   -240   -193  -1179       O  
ATOM   6195  OE2 GLU A 755     -20.773 -34.691 -48.913  1.00 41.05           O  
ANISOU 6195  OE2 GLU A 755     5130   5080   5388   -336   -164   -983       O  
ATOM   6196  N   GLY A 756     -22.876 -30.745 -52.458  1.00 35.20           N  
ANISOU 6196  N   GLY A 756     4243   5138   3993   -413   -152   -955       N  
ATOM   6197  CA  GLY A 756     -24.119 -30.108 -52.882  1.00 35.55           C  
ANISOU 6197  CA  GLY A 756     4259   5299   3950   -435   -160   -907       C  
ATOM   6198  C   GLY A 756     -25.134 -29.866 -51.788  1.00 37.00           C  
ANISOU 6198  C   GLY A 756     4485   5381   4191   -444   -149   -770       C  
ATOM   6199  O   GLY A 756     -24.860 -30.100 -50.602  1.00 36.84           O  
ANISOU 6199  O   GLY A 756     4526   5200   4270   -435   -130   -689       O  
ATOM   6200  N   GLU A 757     -26.314 -29.407 -52.205  1.00 36.76           N  
ANISOU 6200  N   GLU A 757     4414   5464   4090   -457   -163   -750       N  
ATOM   6201  CA  GLU A 757     -27.378 -28.981 -51.300  1.00 36.52           C  
ANISOU 6201  CA  GLU A 757     4407   5391   4078   -457   -154   -625       C  
ATOM   6202  C   GLU A 757     -27.938 -30.117 -50.439  1.00 37.25           C  
ANISOU 6202  C   GLU A 757     4484   5329   4340   -508   -145   -642       C  
ATOM   6203  O   GLU A 757     -28.142 -29.944 -49.232  1.00 34.47           O  
ANISOU 6203  O   GLU A 757     4183   4879   4036   -501   -123   -516       O  
ATOM   6204  CB  GLU A 757     -28.505 -28.311 -52.097  1.00 37.96           C  
ANISOU 6204  CB  GLU A 757     4532   5753   4140   -451   -178   -624       C  
ATOM   6205  CG  GLU A 757     -29.644 -27.736 -51.235  1.00 40.39           C  
ANISOU 6205  CG  GLU A 757     4853   6051   4444   -436   -174   -504       C  
ATOM   6206  CD  GLU A 757     -30.654 -26.932 -52.040  1.00 44.07           C  
ANISOU 6206  CD  GLU A 757     5266   6703   4775   -406   -204   -495       C  
ATOM   6207  OE1 GLU A 757     -31.092 -27.409 -53.109  1.00 48.64           O  
ANISOU 6207  OE1 GLU A 757     5754   7407   5320   -434   -229   -620       O  
ATOM   6208  OE2 GLU A 757     -31.015 -25.824 -51.600  1.00 44.02           O  
ANISOU 6208  OE2 GLU A 757     5307   6722   4698   -347   -208   -369       O  
ATOM   6209  N   GLU A 758     -28.188 -31.270 -51.061  1.00 39.04           N  
ANISOU 6209  N   GLU A 758     4638   5539   4657   -563   -163   -796       N  
ATOM   6210  CA  GLU A 758     -28.765 -32.411 -50.352  1.00 41.38           C  
ANISOU 6210  CA  GLU A 758     4916   5679   5128   -629   -158   -813       C  
ATOM   6211  C   GLU A 758     -27.851 -32.883 -49.217  1.00 39.43           C  
ANISOU 6211  C   GLU A 758     4752   5231   4997   -613   -136   -733       C  
ATOM   6212  O   GLU A 758     -28.316 -33.125 -48.099  1.00 37.66           O  
ANISOU 6212  O   GLU A 758     4556   4899   4854   -640   -115   -620       O  
ATOM   6213  CB  GLU A 758     -29.092 -33.553 -51.324  1.00 46.00           C  
ANISOU 6213  CB  GLU A 758     5407   6271   5798   -692   -188  -1016       C  
ATOM   6214  CG  GLU A 758     -29.856 -34.719 -50.696  1.00 54.86           C  
ANISOU 6214  CG  GLU A 758     6503   7232   7108   -782   -185  -1033       C  
ATOM   6215  CD  GLU A 758     -30.364 -35.728 -51.718  1.00 63.98           C  
ANISOU 6215  CD  GLU A 758     7555   8410   8345   -853   -220  -1247       C  
ATOM   6216  OE1 GLU A 758     -30.372 -36.940 -51.403  1.00 68.55           O  
ANISOU 6216  OE1 GLU A 758     8129   8798   9117   -917   -227  -1310       O  
ATOM   6217  OE2 GLU A 758     -30.764 -35.321 -52.832  1.00 68.23           O  
ANISOU 6217  OE2 GLU A 758     8014   9155   8757   -844   -242  -1354       O  
ATOM   6218  N   SER A 759     -26.553 -32.981 -49.504  1.00 37.84           N  
ANISOU 6218  N   SER A 759     4584   5002   4792   -566   -142   -788       N  
ATOM   6219  CA  SER A 759     -25.571 -33.430 -48.519  1.00 36.84           C  
ANISOU 6219  CA  SER A 759     4531   4703   4765   -534   -129   -726       C  
ATOM   6220  C   SER A 759     -25.507 -32.489 -47.322  1.00 33.63           C  
ANISOU 6220  C   SER A 759     4197   4282   4298   -496    -97   -532       C  
ATOM   6221  O   SER A 759     -25.384 -32.921 -46.171  1.00 30.63           O  
ANISOU 6221  O   SER A 759     3862   3765   4012   -494    -81   -434       O  
ATOM   6222  CB  SER A 759     -24.193 -33.549 -49.154  1.00 37.12           C  
ANISOU 6222  CB  SER A 759     4572   4757   4775   -481   -142   -833       C  
ATOM   6223  OG  SER A 759     -23.233 -33.889 -48.173  1.00 37.77           O  
ANISOU 6223  OG  SER A 759     4721   4691   4938   -438   -133   -767       O  
ATOM   6224  N   LEU A 760     -25.613 -31.201 -47.619  1.00 32.56           N  
ANISOU 6224  N   LEU A 760     4070   4295   4005   -463    -92   -479       N  
ATOM   6225  CA  LEU A 760     -25.594 -30.148 -46.617  1.00 32.89           C  
ANISOU 6225  CA  LEU A 760     4174   4345   3978   -420    -69   -320       C  
ATOM   6226  C   LEU A 760     -26.801 -30.232 -45.671  1.00 32.76           C  
ANISOU 6226  C   LEU A 760     4146   4296   4004   -450    -54   -221       C  
ATOM   6227  O   LEU A 760     -26.658 -30.037 -44.460  1.00 31.72           O  
ANISOU 6227  O   LEU A 760     4061   4102   3891   -425    -32   -103       O  
ATOM   6228  CB  LEU A 760     -25.491 -28.786 -47.321  1.00 31.23           C  
ANISOU 6228  CB  LEU A 760     3974   4288   3604   -383    -75   -300       C  
ATOM   6229  CG  LEU A 760     -25.510 -27.408 -46.639  1.00 32.33           C  
ANISOU 6229  CG  LEU A 760     4172   4462   3649   -332    -63   -164       C  
ATOM   6230  CD1 LEU A 760     -26.861 -26.768 -46.775  1.00 31.81           C  
ANISOU 6230  CD1 LEU A 760     4075   4490   3520   -330    -74   -123       C  
ATOM   6231  CD2 LEU A 760     -25.038 -27.392 -45.192  1.00 29.62           C  
ANISOU 6231  CD2 LEU A 760     3886   4008   3360   -303    -39    -66       C  
ATOM   6232  N   GLN A 761     -27.974 -30.545 -46.219  1.00 33.74           N  
ANISOU 6232  N   GLN A 761     4199   4482   4139   -504    -65   -276       N  
ATOM   6233  CA  GLN A 761     -29.197 -30.674 -45.417  1.00 34.70           C  
ANISOU 6233  CA  GLN A 761     4288   4601   4294   -545    -50   -196       C  
ATOM   6234  C   GLN A 761     -29.171 -31.891 -44.493  1.00 36.55           C  
ANISOU 6234  C   GLN A 761     4532   4669   4687   -601    -32   -155       C  
ATOM   6235  O   GLN A 761     -29.685 -31.824 -43.374  1.00 38.02           O  
ANISOU 6235  O   GLN A 761     4724   4835   4885   -612     -6    -31       O  
ATOM   6236  CB  GLN A 761     -30.439 -30.725 -46.306  1.00 35.83           C  
ANISOU 6236  CB  GLN A 761     4340   4869   4404   -594    -69   -279       C  
ATOM   6237  CG  GLN A 761     -30.724 -29.444 -47.075  1.00 33.97           C  
ANISOU 6237  CG  GLN A 761     4094   4809   4004   -532    -89   -281       C  
ATOM   6238  CD  GLN A 761     -31.655 -29.677 -48.259  1.00 35.33           C  
ANISOU 6238  CD  GLN A 761     4168   5114   4141   -572   -117   -403       C  
ATOM   6239  OE1 GLN A 761     -31.988 -28.750 -48.998  1.00 35.17           O  
ANISOU 6239  OE1 GLN A 761     4128   5246   3987   -523   -140   -408       O  
ATOM   6240  NE2 GLN A 761     -32.075 -30.918 -48.442  1.00 32.89           N  
ANISOU 6240  NE2 GLN A 761     3795   4746   3953   -660   -120   -500       N  
ATOM   6241  N   GLU A 762     -28.582 -32.991 -44.966  1.00 36.83           N  
ANISOU 6241  N   GLU A 762     4564   4588   4840   -633    -48   -257       N  
ATOM   6242  CA  GLU A 762     -28.335 -34.178 -44.138  1.00 40.54           C  
ANISOU 6242  CA  GLU A 762     5061   4867   5475   -674    -39   -212       C  
ATOM   6243  C   GLU A 762     -27.497 -33.847 -42.904  1.00 38.98           C  
ANISOU 6243  C   GLU A 762     4943   4605   5261   -605    -17    -66       C  
ATOM   6244  O   GLU A 762     -27.846 -34.221 -41.777  1.00 37.63           O  
ANISOU 6244  O   GLU A 762     4786   4362   5148   -633      7     64       O  
ATOM   6245  CB  GLU A 762     -27.596 -35.246 -44.942  1.00 43.53           C  
ANISOU 6245  CB  GLU A 762     5435   5131   5974   -685    -71   -366       C  
ATOM   6246  CG  GLU A 762     -28.418 -36.450 -45.336  1.00 52.83           C  
ANISOU 6246  CG  GLU A 762     6552   6218   7303   -791    -87   -460       C  
ATOM   6247  CD  GLU A 762     -27.546 -37.654 -45.684  1.00 60.02           C  
ANISOU 6247  CD  GLU A 762     7480   6948   8376   -788   -120   -580       C  
ATOM   6248  OE1 GLU A 762     -26.301 -37.558 -45.551  1.00 61.29           O  
ANISOU 6248  OE1 GLU A 762     7699   7066   8524   -698   -127   -580       O  
ATOM   6249  OE2 GLU A 762     -28.106 -38.699 -46.085  1.00 63.58           O  
ANISOU 6249  OE2 GLU A 762     7884   7299   8973   -874   -141   -682       O  
ATOM   6250  N   TYR A 763     -26.392 -33.142 -43.125  1.00 37.60           N  
ANISOU 6250  N   TYR A 763     4813   4472   5001   -521    -23    -87       N  
ATOM   6251  CA  TYR A 763     -25.479 -32.821 -42.042  1.00 36.95           C  
ANISOU 6251  CA  TYR A 763     4797   4343   4899   -452     -7     25       C  
ATOM   6252  C   TYR A 763     -26.091 -31.870 -41.031  1.00 36.59           C  
ANISOU 6252  C   TYR A 763     4761   4384   4759   -432     21    166       C  
ATOM   6253  O   TYR A 763     -25.971 -32.100 -39.829  1.00 35.97           O  
ANISOU 6253  O   TYR A 763     4708   4247   4711   -418     41    285       O  
ATOM   6254  CB  TYR A 763     -24.150 -32.266 -42.556  1.00 36.32           C  
ANISOU 6254  CB  TYR A 763     4751   4300   4748   -378    -19    -43       C  
ATOM   6255  CG  TYR A 763     -23.089 -32.278 -41.482  1.00 36.84           C  
ANISOU 6255  CG  TYR A 763     4875   4296   4827   -312     -9     43       C  
ATOM   6256  CD1 TYR A 763     -22.734 -31.111 -40.798  1.00 37.04           C  
ANISOU 6256  CD1 TYR A 763     4934   4403   4737   -256      9    128       C  
ATOM   6257  CD2 TYR A 763     -22.474 -33.470 -41.117  1.00 37.00           C  
ANISOU 6257  CD2 TYR A 763     4914   4164   4980   -301    -21     37       C  
ATOM   6258  CE1 TYR A 763     -21.768 -31.138 -39.787  1.00 36.87           C  
ANISOU 6258  CE1 TYR A 763     4954   4334   4721   -195     17    197       C  
ATOM   6259  CE2 TYR A 763     -21.521 -33.508 -40.120  1.00 38.56           C  
ANISOU 6259  CE2 TYR A 763     5158   4310   5183   -231    -16    118       C  
ATOM   6260  CZ  TYR A 763     -21.172 -32.350 -39.460  1.00 36.96           C  
ANISOU 6260  CZ  TYR A 763     4979   4211   4854   -180      4    195       C  
ATOM   6261  OH  TYR A 763     -20.216 -32.428 -38.482  1.00 39.68           O  
ANISOU 6261  OH  TYR A 763     5359   4519   5199   -110      7    263       O  
ATOM   6262  N   PHE A 764     -26.745 -30.813 -41.521  1.00 35.70           N  
ANISOU 6262  N   PHE A 764     4622   4414   4529   -423     20    149       N  
ATOM   6263  CA  PHE A 764     -27.371 -29.822 -40.650  1.00 35.51           C  
ANISOU 6263  CA  PHE A 764     4599   4482   4412   -391     38    256       C  
ATOM   6264  C   PHE A 764     -28.370 -30.476 -39.713  1.00 37.48           C  
ANISOU 6264  C   PHE A 764     4809   4711   4721   -449     62    348       C  
ATOM   6265  O   PHE A 764     -28.306 -30.282 -38.494  1.00 37.22           O  
ANISOU 6265  O   PHE A 764     4793   4681   4667   -419     85    462       O  
ATOM   6266  CB  PHE A 764     -28.079 -28.734 -41.460  1.00 34.85           C  
ANISOU 6266  CB  PHE A 764     4486   4541   4214   -373     23    213       C  
ATOM   6267  CG  PHE A 764     -28.957 -27.833 -40.628  1.00 34.58           C  
ANISOU 6267  CG  PHE A 764     4437   4602   4101   -339     35    301       C  
ATOM   6268  CD1 PHE A 764     -28.410 -26.752 -39.940  1.00 33.61           C  
ANISOU 6268  CD1 PHE A 764     4364   4506   3900   -258     38    360       C  
ATOM   6269  CD2 PHE A 764     -30.330 -28.067 -40.531  1.00 35.34           C  
ANISOU 6269  CD2 PHE A 764     4458   4768   4200   -388     41    313       C  
ATOM   6270  CE1 PHE A 764     -29.214 -25.912 -39.166  1.00 34.76           C  
ANISOU 6270  CE1 PHE A 764     4489   4742   3975   -215     43    421       C  
ATOM   6271  CE2 PHE A 764     -31.142 -27.235 -39.765  1.00 36.49           C  
ANISOU 6271  CE2 PHE A 764     4578   5020   4267   -346     49    380       C  
ATOM   6272  CZ  PHE A 764     -30.580 -26.155 -39.075  1.00 36.79           C  
ANISOU 6272  CZ  PHE A 764     4669   5079   4230   -254     49    430       C  
ATOM   6273  N   LYS A 765     -29.295 -31.236 -40.300  1.00 39.32           N  
ANISOU 6273  N   LYS A 765     4981   4937   5023   -536     57    293       N  
ATOM   6274  CA  LYS A 765     -30.321 -31.948 -39.558  1.00 42.10           C  
ANISOU 6274  CA  LYS A 765     5282   5274   5439   -618     82    373       C  
ATOM   6275  C   LYS A 765     -29.683 -32.748 -38.423  1.00 42.90           C  
ANISOU 6275  C   LYS A 765     5431   5240   5630   -624    102    490       C  
ATOM   6276  O   LYS A 765     -30.152 -32.697 -37.279  1.00 42.05           O  
ANISOU 6276  O   LYS A 765     5309   5172   5498   -634    133    621       O  
ATOM   6277  CB  LYS A 765     -31.100 -32.879 -40.490  1.00 45.04           C  
ANISOU 6277  CB  LYS A 765     5589   5617   5908   -724     68    270       C  
ATOM   6278  CG  LYS A 765     -32.429 -33.387 -39.930  1.00 51.21           C  
ANISOU 6278  CG  LYS A 765     6295   6433   6730   -827     95    336       C  
ATOM   6279  CD  LYS A 765     -32.886 -34.674 -40.629  1.00 57.97           C  
ANISOU 6279  CD  LYS A 765     7102   7183   7739   -951     82    243       C  
ATOM   6280  CE  LYS A 765     -33.227 -34.446 -42.102  1.00 62.23           C  
ANISOU 6280  CE  LYS A 765     7587   7817   8240   -956     47     62       C  
ATOM   6281  NZ  LYS A 765     -33.063 -35.687 -42.926  1.00 64.88           N  
ANISOU 6281  NZ  LYS A 765     7905   8013   8735  -1038     21    -71       N  
ATOM   6282  N   GLU A 766     -28.604 -33.462 -38.740  1.00 42.09           N  
ANISOU 6282  N   GLU A 766     5379   4991   5621   -608     83    441       N  
ATOM   6283  CA  GLU A 766     -27.932 -34.288 -37.748  1.00 43.80           C  
ANISOU 6283  CA  GLU A 766     5646   5068   5930   -600     92    550       C  
ATOM   6284  C   GLU A 766     -27.252 -33.449 -36.671  1.00 42.44           C  
ANISOU 6284  C   GLU A 766     5514   4961   5648   -502    109    657       C  
ATOM   6285  O   GLU A 766     -27.346 -33.772 -35.489  1.00 42.14           O  
ANISOU 6285  O   GLU A 766     5483   4907   5623   -506    133    801       O  
ATOM   6286  CB  GLU A 766     -26.938 -35.248 -38.400  1.00 45.95           C  
ANISOU 6286  CB  GLU A 766     5958   5171   6332   -591     59    454       C  
ATOM   6287  CG  GLU A 766     -26.704 -36.516 -37.588  1.00 49.58           C  
ANISOU 6287  CG  GLU A 766     6450   5443   6944   -623     59    559       C  
ATOM   6288  CD  GLU A 766     -27.978 -37.319 -37.368  1.00 53.84           C  
ANISOU 6288  CD  GLU A 766     6942   5933   7583   -758     77    623       C  
ATOM   6289  OE1 GLU A 766     -28.665 -37.655 -38.358  1.00 55.35           O  
ANISOU 6289  OE1 GLU A 766     7082   6118   7833   -839     63    496       O  
ATOM   6290  OE2 GLU A 766     -28.293 -37.621 -36.198  1.00 58.54           O  
ANISOU 6290  OE2 GLU A 766     7543   6506   8193   -789    107    800       O  
ATOM   6291  N   PHE A 767     -26.602 -32.357 -37.071  1.00 39.94           N  
ANISOU 6291  N   PHE A 767     5222   4732   5223   -419     97    589       N  
ATOM   6292  CA  PHE A 767     -25.940 -31.484 -36.101  1.00 39.65           C  
ANISOU 6292  CA  PHE A 767     5218   4763   5083   -328    109    665       C  
ATOM   6293  C   PHE A 767     -26.923 -30.848 -35.114  1.00 39.79           C  
ANISOU 6293  C   PHE A 767     5196   4911   5012   -328    138    769       C  
ATOM   6294  O   PHE A 767     -26.661 -30.813 -33.912  1.00 39.13           O  
ANISOU 6294  O   PHE A 767     5121   4850   4896   -289    157    879       O  
ATOM   6295  CB  PHE A 767     -25.068 -30.412 -36.776  1.00 37.13           C  
ANISOU 6295  CB  PHE A 767     4931   4502   4674   -256     90    568       C  
ATOM   6296  CG  PHE A 767     -24.201 -29.656 -35.806  1.00 37.24           C  
ANISOU 6296  CG  PHE A 767     4980   4561   4609   -170     98    626       C  
ATOM   6297  CD1 PHE A 767     -24.531 -28.361 -35.422  1.00 37.39           C  
ANISOU 6297  CD1 PHE A 767     4992   4703   4510   -127    105    643       C  
ATOM   6298  CD2 PHE A 767     -23.079 -30.261 -35.236  1.00 35.12           C  
ANISOU 6298  CD2 PHE A 767     4746   4211   4386   -126     95    658       C  
ATOM   6299  CE1 PHE A 767     -23.742 -27.662 -34.507  1.00 37.65           C  
ANISOU 6299  CE1 PHE A 767     5051   4780   4476    -51    110    679       C  
ATOM   6300  CE2 PHE A 767     -22.290 -29.580 -34.315  1.00 36.69           C  
ANISOU 6300  CE2 PHE A 767     4967   4468   4507    -48    101    702       C  
ATOM   6301  CZ  PHE A 767     -22.619 -28.273 -33.951  1.00 39.10           C  
ANISOU 6301  CZ  PHE A 767     5261   4897   4696    -15    109    708       C  
ATOM   6302  N   GLU A 768     -28.051 -30.366 -35.632  1.00 41.05           N  
ANISOU 6302  N   GLU A 768     5303   5169   5126   -366    139    728       N  
ATOM   6303  CA  GLU A 768     -29.132 -29.814 -34.811  1.00 40.73           C  
ANISOU 6303  CA  GLU A 768     5205   5269   5003   -368    163    804       C  
ATOM   6304  C   GLU A 768     -29.623 -30.817 -33.758  1.00 40.91           C  
ANISOU 6304  C   GLU A 768     5195   5267   5083   -436    197    939       C  
ATOM   6305  O   GLU A 768     -29.942 -30.434 -32.632  1.00 40.89           O  
ANISOU 6305  O   GLU A 768     5162   5374   4999   -407    222   1036       O  
ATOM   6306  CB  GLU A 768     -30.287 -29.364 -35.715  1.00 42.65           C  
ANISOU 6306  CB  GLU A 768     5389   5609   5208   -403    152    722       C  
ATOM   6307  CG  GLU A 768     -31.405 -28.572 -35.029  1.00 47.32           C  
ANISOU 6307  CG  GLU A 768     5912   6372   5694   -381    168    767       C  
ATOM   6308  CD  GLU A 768     -32.436 -28.035 -36.018  1.00 49.77           C  
ANISOU 6308  CD  GLU A 768     6167   6783   5959   -391    146    674       C  
ATOM   6309  OE1 GLU A 768     -32.499 -26.799 -36.202  1.00 51.73           O  
ANISOU 6309  OE1 GLU A 768     6425   7119   6110   -301    124    634       O  
ATOM   6310  OE2 GLU A 768     -33.174 -28.845 -36.621  1.00 49.20           O  
ANISOU 6310  OE2 GLU A 768     6040   6699   5953   -488    148    640       O  
ATOM   6311  N   LYS A 769     -29.668 -32.096 -34.127  1.00 41.12           N  
ANISOU 6311  N   LYS A 769     5224   5150   5248   -527    195    945       N  
ATOM   6312  CA  LYS A 769     -30.160 -33.152 -33.243  1.00 43.53           C  
ANISOU 6312  CA  LYS A 769     5504   5405   5630   -613    225   1087       C  
ATOM   6313  C   LYS A 769     -29.201 -33.483 -32.104  1.00 43.61           C  
ANISOU 6313  C   LYS A 769     5568   5358   5645   -555    235   1218       C  
ATOM   6314  O   LYS A 769     -29.635 -33.735 -30.982  1.00 44.23           O  
ANISOU 6314  O   LYS A 769     5614   5497   5693   -582    268   1369       O  
ATOM   6315  CB  LYS A 769     -30.428 -34.437 -34.034  1.00 46.60           C  
ANISOU 6315  CB  LYS A 769     5890   5627   6190   -729    213   1043       C  
ATOM   6316  CG  LYS A 769     -31.799 -34.549 -34.661  1.00 48.63           C  
ANISOU 6316  CG  LYS A 769     6059   5958   6460   -837    221    983       C  
ATOM   6317  CD  LYS A 769     -31.984 -35.946 -35.242  1.00 54.11           C  
ANISOU 6317  CD  LYS A 769     6751   6465   7343   -960    209    950       C  
ATOM   6318  CE  LYS A 769     -33.180 -36.022 -36.184  1.00 55.40           C  
ANISOU 6318  CE  LYS A 769     6826   6701   7524  -1061    205    833       C  
ATOM   6319  NZ  LYS A 769     -33.352 -37.400 -36.728  1.00 55.73           N  
ANISOU 6319  NZ  LYS A 769     6861   6550   7763  -1187    190    785       N  
ATOM   6320  N   GLU A 770     -27.901 -33.494 -32.403  1.00 42.26           N  
ANISOU 6320  N   GLU A 770     5469   5085   5502   -475    206   1162       N  
ATOM   6321  CA  GLU A 770     -26.900 -33.996 -31.465  1.00 41.76           C  
ANISOU 6321  CA  GLU A 770     5458   4946   5465   -416    205   1273       C  
ATOM   6322  C   GLU A 770     -26.186 -32.882 -30.688  1.00 40.40           C  
ANISOU 6322  C   GLU A 770     5296   4911   5142   -294    209   1289       C  
ATOM   6323  O   GLU A 770     -25.503 -33.148 -29.698  1.00 40.22           O  
ANISOU 6323  O   GLU A 770     5296   4882   5103   -239    213   1396       O  
ATOM   6324  CB  GLU A 770     -25.886 -34.898 -32.186  1.00 42.84           C  
ANISOU 6324  CB  GLU A 770     5658   4878   5743   -403    167   1202       C  
ATOM   6325  CG  GLU A 770     -26.475 -35.870 -33.233  1.00 43.75           C  
ANISOU 6325  CG  GLU A 770     5760   4851   6011   -513    151   1121       C  
ATOM   6326  CD  GLU A 770     -27.399 -36.951 -32.662  1.00 47.88           C  
ANISOU 6326  CD  GLU A 770     6259   5291   6644   -634    174   1262       C  
ATOM   6327  OE1 GLU A 770     -28.194 -37.515 -33.449  1.00 49.96           O  
ANISOU 6327  OE1 GLU A 770     6488   5488   7007   -743    169   1190       O  
ATOM   6328  OE2 GLU A 770     -27.340 -37.249 -31.450  1.00 45.25           O  
ANISOU 6328  OE2 GLU A 770     5936   4963   6295   -626    196   1443       O  
ATOM   6329  N   PHE A 771     -26.386 -31.642 -31.129  1.00 37.89           N  
ANISOU 6329  N   PHE A 771     4960   4718   4720   -255    204   1183       N  
ATOM   6330  CA  PHE A 771     -25.774 -30.439 -30.545  1.00 38.79           C  
ANISOU 6330  CA  PHE A 771     5082   4955   4700   -147    202   1164       C  
ATOM   6331  C   PHE A 771     -25.671 -30.408 -29.009  1.00 38.66           C  
ANISOU 6331  C   PHE A 771     5044   5041   4606    -99    227   1303       C  
ATOM   6332  O   PHE A 771     -24.627 -30.058 -28.460  1.00 37.76           O  
ANISOU 6332  O   PHE A 771     4957   4948   4441    -11    217   1304       O  
ATOM   6333  CB  PHE A 771     -26.527 -29.198 -31.055  1.00 39.81           C  
ANISOU 6333  CB  PHE A 771     5178   5210   4738   -136    199   1070       C  
ATOM   6334  CG  PHE A 771     -26.007 -27.896 -30.528  1.00 42.68           C  
ANISOU 6334  CG  PHE A 771     5551   5684   4983    -34    192   1034       C  
ATOM   6335  CD1 PHE A 771     -26.663 -27.242 -29.493  1.00 45.97           C  
ANISOU 6335  CD1 PHE A 771     5912   6258   5295      3    210   1085       C  
ATOM   6336  CD2 PHE A 771     -24.875 -27.302 -31.091  1.00 50.20           C  
ANISOU 6336  CD2 PHE A 771     6559   6588   5927     20    166    938       C  
ATOM   6337  CE1 PHE A 771     -26.194 -26.028 -29.004  1.00 49.58           C  
ANISOU 6337  CE1 PHE A 771     6375   6808   5654     98    198   1032       C  
ATOM   6338  CE2 PHE A 771     -24.392 -26.080 -30.615  1.00 50.88           C  
ANISOU 6338  CE2 PHE A 771     6653   6762   5917    102    158    898       C  
ATOM   6339  CZ  PHE A 771     -25.055 -25.442 -29.563  1.00 52.80           C  
ANISOU 6339  CZ  PHE A 771     6847   7147   6069    144    171    940       C  
ATOM   6340  N   ARG A 772     -26.748 -30.774 -28.324  1.00 39.88           N  
ANISOU 6340  N   ARG A 772     5138   5274   4742   -161    259   1416       N  
ATOM   6341  CA  ARG A 772     -26.810 -30.665 -26.860  1.00 41.63           C  
ANISOU 6341  CA  ARG A 772     5318   5638   4862   -119    286   1549       C  
ATOM   6342  C   ARG A 772     -25.872 -31.608 -26.095  1.00 40.65           C  
ANISOU 6342  C   ARG A 772     5235   5429   4782    -90    285   1680       C  
ATOM   6343  O   ARG A 772     -25.714 -31.481 -24.883  1.00 43.38           O  
ANISOU 6343  O   ARG A 772     5549   5904   5028    -37    302   1786       O  
ATOM   6344  CB  ARG A 772     -28.262 -30.786 -26.377  1.00 43.94           C  
ANISOU 6344  CB  ARG A 772     5522   6063   5110   -200    325   1635       C  
ATOM   6345  CG  ARG A 772     -29.097 -29.565 -26.745  1.00 48.53           C  
ANISOU 6345  CG  ARG A 772     6048   6793   5596   -176    322   1512       C  
ATOM   6346  CD  ARG A 772     -30.549 -29.900 -27.080  1.00 57.24           C  
ANISOU 6346  CD  ARG A 772     7077   7952   6721   -287    345   1528       C  
ATOM   6347  NE  ARG A 772     -31.110 -28.916 -28.012  1.00 59.92           N  
ANISOU 6347  NE  ARG A 772     7397   8344   7025   -261    322   1373       N  
ATOM   6348  CZ  ARG A 772     -31.727 -27.790 -27.649  1.00 63.51           C  
ANISOU 6348  CZ  ARG A 772     7791   8984   7355   -192    321   1320       C  
ATOM   6349  NH1 ARG A 772     -31.886 -27.493 -26.361  1.00 63.97           N  
ANISOU 6349  NH1 ARG A 772     7790   9212   7302   -144    346   1395       N  
ATOM   6350  NH2 ARG A 772     -32.192 -26.958 -28.579  1.00 60.74           N  
ANISOU 6350  NH2 ARG A 772     7435   8657   6988   -164    292   1188       N  
ATOM   6351  N   GLN A 773     -25.237 -32.533 -26.808  1.00 39.26           N  
ANISOU 6351  N   GLN A 773     5124   5044   4749   -115    260   1663       N  
ATOM   6352  CA  GLN A 773     -24.297 -33.477 -26.203  1.00 39.87           C  
ANISOU 6352  CA  GLN A 773     5248   5015   4885    -75    247   1778       C  
ATOM   6353  C   GLN A 773     -22.861 -32.956 -26.224  1.00 37.17           C  
ANISOU 6353  C   GLN A 773     4949   4672   4502     51    214   1685       C  
ATOM   6354  O   GLN A 773     -21.962 -33.581 -25.656  1.00 36.50           O  
ANISOU 6354  O   GLN A 773     4896   4530   4442    114    198   1766       O  
ATOM   6355  CB  GLN A 773     -24.336 -34.823 -26.931  1.00 41.29           C  
ANISOU 6355  CB  GLN A 773     5473   4955   5258   -158    230   1800       C  
ATOM   6356  CG  GLN A 773     -25.705 -35.453 -27.057  1.00 47.64           C  
ANISOU 6356  CG  GLN A 773     6236   5732   6132   -303    259   1876       C  
ATOM   6357  CD  GLN A 773     -25.774 -36.481 -28.185  1.00 52.69           C  
ANISOU 6357  CD  GLN A 773     6915   6135   6968   -387    232   1805       C  
ATOM   6358  OE1 GLN A 773     -26.751 -36.522 -28.937  1.00 51.91           O  
ANISOU 6358  OE1 GLN A 773     6778   6031   6913   -490    241   1734       O  
ATOM   6359  NE2 GLN A 773     -24.733 -37.310 -28.310  1.00 51.77           N  
ANISOU 6359  NE2 GLN A 773     6870   5833   6969   -336    194   1812       N  
ATOM   6360  N   LEU A 774     -22.642 -31.831 -26.900  1.00 34.11           N  
ANISOU 6360  N   LEU A 774     4560   4345   4053     85    203   1518       N  
ATOM   6361  CA  LEU A 774     -21.300 -31.265 -27.009  1.00 33.50           C  
ANISOU 6361  CA  LEU A 774     4515   4275   3937    185    175   1417       C  
ATOM   6362  C   LEU A 774     -20.803 -30.776 -25.655  1.00 34.48           C  
ANISOU 6362  C   LEU A 774     4610   4559   3932    278    183   1488       C  
ATOM   6363  O   LEU A 774     -21.567 -30.197 -24.879  1.00 34.67           O  
ANISOU 6363  O   LEU A 774     4579   4743   3851    277    209   1538       O  
ATOM   6364  CB  LEU A 774     -21.252 -30.147 -28.053  1.00 29.70           C  
ANISOU 6364  CB  LEU A 774     4040   3821   3423    183    164   1240       C  
ATOM   6365  CG  LEU A 774     -21.475 -30.597 -29.503  1.00 30.28           C  
ANISOU 6365  CG  LEU A 774     4140   3755   3610    110    149   1144       C  
ATOM   6366  CD1 LEU A 774     -21.733 -29.418 -30.418  1.00 25.42           C  
ANISOU 6366  CD1 LEU A 774     3520   3201   2938     99    143   1009       C  
ATOM   6367  CD2 LEU A 774     -20.323 -31.460 -30.022  1.00 28.10           C  
ANISOU 6367  CD2 LEU A 774     3909   3333   3434    138    119   1099       C  
ATOM   6368  N   ASN A 775     -19.532 -31.060 -25.373  1.00 35.06           N  
ANISOU 6368  N   ASN A 775     4712   4599   4010    361    158   1486       N  
ATOM   6369  CA  ASN A 775     -18.854 -30.600 -24.164  1.00 34.92           C  
ANISOU 6369  CA  ASN A 775     4663   4738   3867    461    158   1528       C  
ATOM   6370  C   ASN A 775     -18.930 -29.071 -24.094  1.00 32.72           C  
ANISOU 6370  C   ASN A 775     4349   4616   3468    488    164   1398       C  
ATOM   6371  O   ASN A 775     -18.808 -28.391 -25.122  1.00 29.13           O  
ANISOU 6371  O   ASN A 775     3918   4110   3039    463    152   1253       O  
ATOM   6372  CB  ASN A 775     -17.399 -31.077 -24.185  1.00 36.99           C  
ANISOU 6372  CB  ASN A 775     4961   4929   4166    545    123   1500       C  
ATOM   6373  CG  ASN A 775     -16.589 -30.564 -23.007  1.00 42.34           C  
ANISOU 6373  CG  ASN A 775     5598   5781   4707    655    117   1519       C  
ATOM   6374  OD1 ASN A 775     -15.854 -29.583 -23.129  1.00 46.19           O  
ANISOU 6374  OD1 ASN A 775     6072   6349   5129    700    105   1376       O  
ATOM   6375  ND2 ASN A 775     -16.712 -31.228 -21.865  1.00 42.51           N  
ANISOU 6375  ND2 ASN A 775     5597   5869   4687    693    124   1698       N  
ATOM   6376  N   TYR A 776     -19.150 -28.543 -22.895  1.00 30.36           N  
ANISOU 6376  N   TYR A 776     3991   4505   3040    539    179   1451       N  
ATOM   6377  CA  TYR A 776     -19.370 -27.107 -22.710  1.00 31.39           C  
ANISOU 6377  CA  TYR A 776     4082   4780   3065    568    181   1329       C  
ATOM   6378  C   TYR A 776     -18.233 -26.210 -23.232  1.00 29.50           C  
ANISOU 6378  C   TYR A 776     3870   4518   2819    611    153   1159       C  
ATOM   6379  O   TYR A 776     -18.488 -25.121 -23.736  1.00 30.87           O  
ANISOU 6379  O   TYR A 776     4047   4707   2975    596    147   1038       O  
ATOM   6380  CB  TYR A 776     -19.694 -26.789 -21.245  1.00 31.88           C  
ANISOU 6380  CB  TYR A 776     4065   5063   2984    628    199   1405       C  
ATOM   6381  CG  TYR A 776     -18.513 -26.835 -20.303  1.00 33.62           C  
ANISOU 6381  CG  TYR A 776     4265   5382   3128    728    182   1421       C  
ATOM   6382  CD1 TYR A 776     -17.953 -25.657 -19.808  1.00 34.17           C  
ANISOU 6382  CD1 TYR A 776     4294   5594   3093    802    168   1287       C  
ATOM   6383  CD2 TYR A 776     -17.963 -28.053 -19.894  1.00 37.22           C  
ANISOU 6383  CD2 TYR A 776     4739   5786   3616    753    178   1569       C  
ATOM   6384  CE1 TYR A 776     -16.879 -25.683 -18.936  1.00 35.10           C  
ANISOU 6384  CE1 TYR A 776     4381   5823   3133    894    151   1289       C  
ATOM   6385  CE2 TYR A 776     -16.885 -28.095 -19.018  1.00 39.47           C  
ANISOU 6385  CE2 TYR A 776     4998   6179   3819    857    159   1585       C  
ATOM   6386  CZ  TYR A 776     -16.349 -26.905 -18.545  1.00 40.04           C  
ANISOU 6386  CZ  TYR A 776     5021   6414   3779    925    147   1440       C  
ATOM   6387  OH  TYR A 776     -15.285 -26.935 -17.684  1.00 41.03           O  
ANISOU 6387  OH  TYR A 776     5108   6663   3817   1028    126   1443       O  
ATOM   6388  N   ILE A 777     -16.992 -26.667 -23.108  1.00 31.18           N  
ANISOU 6388  N   ILE A 777     4102   4698   3047    664    133   1155       N  
ATOM   6389  CA  ILE A 777     -15.833 -25.906 -23.596  1.00 32.22           C  
ANISOU 6389  CA  ILE A 777     4252   4819   3173    693    109    999       C  
ATOM   6390  C   ILE A 777     -15.845 -25.814 -25.129  1.00 30.36           C  
ANISOU 6390  C   ILE A 777     4072   4428   3037    616    103    904       C  
ATOM   6391  O   ILE A 777     -15.618 -24.745 -25.699  1.00 29.48           O  
ANISOU 6391  O   ILE A 777     3971   4323   2909    597     95    779       O  
ATOM   6392  CB  ILE A 777     -14.501 -26.481 -23.037  1.00 34.50           C  
ANISOU 6392  CB  ILE A 777     4531   5134   3443    776     89   1017       C  
ATOM   6393  CG1 ILE A 777     -14.366 -26.114 -21.555  1.00 36.05           C  
ANISOU 6393  CG1 ILE A 777     4658   5535   3504    860     91   1060       C  
ATOM   6394  CG2 ILE A 777     -13.287 -25.962 -23.819  1.00 35.47           C  
ANISOU 6394  CG2 ILE A 777     4673   5218   3588    781     67    857       C  
ATOM   6395  CD1 ILE A 777     -13.310 -26.896 -20.809  1.00 43.93           C  
ANISOU 6395  CD1 ILE A 777     5638   6582   4471    953     72   1129       C  
ATOM   6396  N   SER A 778     -16.172 -26.923 -25.784  1.00 30.49           N  
ANISOU 6396  N   SER A 778     4121   4308   3157    569    104    969       N  
ATOM   6397  CA  SER A 778     -16.234 -26.964 -27.243  1.00 29.64           C  
ANISOU 6397  CA  SER A 778     4055   4072   3136    499     97    880       C  
ATOM   6398  C   SER A 778     -17.323 -26.060 -27.827  1.00 28.28           C  
ANISOU 6398  C   SER A 778     3882   3915   2947    437    108    834       C  
ATOM   6399  O   SER A 778     -17.280 -25.749 -29.015  1.00 27.36           O  
ANISOU 6399  O   SER A 778     3795   3732   2870    389    101    745       O  
ATOM   6400  CB  SER A 778     -16.393 -28.401 -27.748  1.00 30.55           C  
ANISOU 6400  CB  SER A 778     4196   4039   3371    466     92    947       C  
ATOM   6401  OG  SER A 778     -17.748 -28.808 -27.703  1.00 31.35           O  
ANISOU 6401  OG  SER A 778     4291   4116   3506    402    112   1039       O  
ATOM   6402  N   ILE A 779     -18.284 -25.631 -27.003  1.00 28.55           N  
ANISOU 6402  N   ILE A 779     3880   4052   2916    445    125    893       N  
ATOM   6403  CA  ILE A 779     -19.362 -24.742 -27.482  1.00 28.96           C  
ANISOU 6403  CA  ILE A 779     3926   4131   2948    405    129    847       C  
ATOM   6404  C   ILE A 779     -19.367 -23.330 -26.863  1.00 27.57           C  
ANISOU 6404  C   ILE A 779     3726   4075   2676    458    122    776       C  
ATOM   6405  O   ILE A 779     -20.247 -22.508 -27.161  1.00 26.92           O  
ANISOU 6405  O   ILE A 779     3637   4017   2573    445    119    735       O  
ATOM   6406  CB  ILE A 779     -20.768 -25.394 -27.379  1.00 31.31           C  
ANISOU 6406  CB  ILE A 779     4194   4433   3268    354    150    947       C  
ATOM   6407  CG1 ILE A 779     -21.043 -25.901 -25.958  1.00 34.85           C  
ANISOU 6407  CG1 ILE A 779     4593   4990   3660    389    171   1076       C  
ATOM   6408  CG2 ILE A 779     -20.895 -26.509 -28.392  1.00 34.73           C  
ANISOU 6408  CG2 ILE A 779     4659   4717   3818    282    149    965       C  
ATOM   6409  CD1 ILE A 779     -22.346 -26.683 -25.819  1.00 40.13           C  
ANISOU 6409  CD1 ILE A 779     5226   5665   4356    320    198   1191       C  
ATOM   6410  N   ALA A 780     -18.385 -23.055 -26.012  1.00 25.44           N  
ANISOU 6410  N   ALA A 780     3438   3878   2349    523    116    753       N  
ATOM   6411  CA  ALA A 780     -18.202 -21.715 -25.461  1.00 25.82           C  
ANISOU 6411  CA  ALA A 780     3464   4025   2321    573    103    658       C  
ATOM   6412  C   ALA A 780     -17.578 -20.793 -26.495  1.00 23.53           C  
ANISOU 6412  C   ALA A 780     3224   3649   2066    540     82    536       C  
ATOM   6413  O   ALA A 780     -16.694 -21.209 -27.244  1.00 24.37           O  
ANISOU 6413  O   ALA A 780     3365   3672   2222    508     79    513       O  
ATOM   6414  CB  ALA A 780     -17.332 -21.772 -24.217  1.00 25.70           C  
ANISOU 6414  CB  ALA A 780     3404   4130   2231    649    101    665       C  
ATOM   6415  N   SER A 781     -18.037 -19.544 -26.531  1.00 21.72           N  
ANISOU 6415  N   SER A 781     2998   3442   1812    549     68    460       N  
ATOM   6416  CA  SER A 781     -17.417 -18.519 -27.364  1.00 22.01           C  
ANISOU 6416  CA  SER A 781     3083   3401   1877    516     47    357       C  
ATOM   6417  C   SER A 781     -16.133 -18.064 -26.685  1.00 23.72           C  
ANISOU 6417  C   SER A 781     3281   3673   2059    549     38    281       C  
ATOM   6418  O   SER A 781     -15.902 -18.395 -25.523  1.00 22.82           O  
ANISOU 6418  O   SER A 781     3112   3671   1887    612     43    301       O  
ATOM   6419  CB  SER A 781     -18.357 -17.326 -27.535  1.00 22.90           C  
ANISOU 6419  CB  SER A 781     3209   3508   1985    527     27    308       C  
ATOM   6420  OG  SER A 781     -19.483 -17.691 -28.309  1.00 31.68           O  
ANISOU 6420  OG  SER A 781     4335   4576   3127    493     32    366       O  
ATOM   6421  N   VAL A 782     -15.296 -17.319 -27.406  1.00 23.49           N  
ANISOU 6421  N   VAL A 782     3290   3575   2058    503     25    197       N  
ATOM   6422  CA  VAL A 782     -14.074 -16.775 -26.831  1.00 25.43           C  
ANISOU 6422  CA  VAL A 782     3512   3874   2275    519     15    107       C  
ATOM   6423  C   VAL A 782     -13.993 -15.278 -27.100  1.00 28.29           C  
ANISOU 6423  C   VAL A 782     3906   4186   2657    489     -8      6       C  
ATOM   6424  O   VAL A 782     -14.359 -14.818 -28.173  1.00 29.68           O  
ANISOU 6424  O   VAL A 782     4141   4254   2881    430    -15     13       O  
ATOM   6425  CB  VAL A 782     -12.802 -17.460 -27.391  1.00 26.46           C  
ANISOU 6425  CB  VAL A 782     3647   3982   2425    481     25     96       C  
ATOM   6426  CG1 VAL A 782     -11.562 -16.952 -26.657  1.00 28.24           C  
ANISOU 6426  CG1 VAL A 782     3829   4292   2608    504     15     -1       C  
ATOM   6427  CG2 VAL A 782     -12.892 -18.983 -27.276  1.00 22.56           C  
ANISOU 6427  CG2 VAL A 782     3137   3499   1937    511     40    197       C  
ATOM   6428  N   SER A 783     -13.529 -14.521 -26.113  1.00 30.95           N  
ANISOU 6428  N   SER A 783     4203   4600   2958    532    -24    -86       N  
ATOM   6429  CA  SER A 783     -13.294 -13.096 -26.295  1.00 32.59           C  
ANISOU 6429  CA  SER A 783     4441   4741   3201    498    -52   -193       C  
ATOM   6430  C   SER A 783     -12.128 -12.618 -25.424  1.00 34.33           C  
ANISOU 6430  C   SER A 783     4608   5047   3391    513    -62   -309       C  
ATOM   6431  O   SER A 783     -11.682 -13.337 -24.527  1.00 34.60           O  
ANISOU 6431  O   SER A 783     4573   5215   3358    572    -51   -304       O  
ATOM   6432  CB  SER A 783     -14.565 -12.298 -25.991  1.00 31.73           C  
ANISOU 6432  CB  SER A 783     4341   4615   3099    551    -77   -210       C  
ATOM   6433  OG  SER A 783     -14.426 -10.972 -26.463  1.00 33.86           O  
ANISOU 6433  OG  SER A 783     4665   4768   3431    509   -108   -291       O  
ATOM   6434  N   SER A 784     -11.641 -11.407 -25.701  1.00 34.93           N  
ANISOU 6434  N   SER A 784     4713   5042   3515    455    -84   -410       N  
ATOM   6435  CA  SER A 784     -10.576 -10.788 -24.912  1.00 34.40           C  
ANISOU 6435  CA  SER A 784     4593   5049   3430    454    -98   -545       C  
ATOM   6436  C   SER A 784     -11.153  -9.917 -23.808  1.00 36.06           C  
ANISOU 6436  C   SER A 784     4763   5314   3623    538   -131   -647       C  
ATOM   6437  O   SER A 784     -12.088  -9.156 -24.039  1.00 38.71           O  
ANISOU 6437  O   SER A 784     5147   5553   4009    549   -156   -657       O  
ATOM   6438  CB  SER A 784      -9.664  -9.948 -25.804  1.00 32.87           C  
ANISOU 6438  CB  SER A 784     4447   4737   3307    329   -103   -604       C  
ATOM   6439  OG  SER A 784      -8.754 -10.765 -26.503  1.00 31.90           O  
ANISOU 6439  OG  SER A 784     4318   4633   3169    265    -72   -558       O  
ATOM   6440  N   ALA A 785     -10.571 -10.010 -22.619  1.00 36.77           N  
ANISOU 6440  N   ALA A 785     4760   5570   3640    602   -136   -732       N  
ATOM   6441  CA  ALA A 785     -11.105  -9.337 -21.434  1.00 38.75           C  
ANISOU 6441  CA  ALA A 785     4950   5924   3851    699   -166   -841       C  
ATOM   6442  C   ALA A 785     -10.542  -7.928 -21.241  1.00 39.10           C  
ANISOU 6442  C   ALA A 785     4994   5902   3960    660   -206  -1024       C  
ATOM   6443  O   ALA A 785      -9.768  -7.683 -20.318  1.00 40.25           O  
ANISOU 6443  O   ALA A 785     5055   6179   4058    688   -219  -1153       O  
ATOM   6444  CB  ALA A 785     -10.862 -10.188 -20.193  1.00 37.63           C  
ANISOU 6444  CB  ALA A 785     4698   6020   3581    799   -153   -832       C  
ATOM   6445  N   ASN A 786     -10.948  -7.004 -22.107  1.00 40.71           N  
ANISOU 6445  N   ASN A 786     5292   5900   4276    596   -229  -1035       N  
ATOM   6446  CA  ASN A 786     -10.472  -5.623 -22.037  1.00 43.22           C  
ANISOU 6446  CA  ASN A 786     5628   6109   4683    544   -271  -1197       C  
ATOM   6447  C   ASN A 786     -11.438  -4.682 -21.337  1.00 45.72           C  
ANISOU 6447  C   ASN A 786     5934   6411   5028    643   -321  -1312       C  
ATOM   6448  O   ASN A 786     -12.652  -4.785 -21.513  1.00 45.91           O  
ANISOU 6448  O   ASN A 786     5989   6406   5050    711   -328  -1236       O  
ATOM   6449  CB  ASN A 786     -10.171  -5.083 -23.437  1.00 43.02           C  
ANISOU 6449  CB  ASN A 786     5719   5854   4774    402   -270  -1138       C  
ATOM   6450  CG  ASN A 786      -8.967  -5.746 -24.073  1.00 41.18           C  
ANISOU 6450  CG  ASN A 786     5479   5647   4520    291   -227  -1082       C  
ATOM   6451  OD1 ASN A 786      -7.961  -6.001 -23.412  1.00 43.14           O  
ANISOU 6451  OD1 ASN A 786     5642   6037   4713    289   -216  -1167       O  
ATOM   6452  ND2 ASN A 786      -9.060  -6.016 -25.365  1.00 38.92           N  
ANISOU 6452  ND2 ASN A 786     5276   5241   4272    205   -204   -947       N  
ATOM   6453  N   ASN A 787     -10.881  -3.763 -20.550  1.00 49.22           N  
ANISOU 6453  N   ASN A 787     6325   6879   5497    652   -359  -1507       N  
ATOM   6454  CA  ASN A 787     -11.639  -2.686 -19.907  1.00 51.20           C  
ANISOU 6454  CA  ASN A 787     6564   7094   5797    742   -418  -1660       C  
ATOM   6455  C   ASN A 787     -12.687  -3.125 -18.893  1.00 50.84           C  
ANISOU 6455  C   ASN A 787     6426   7257   5632    906   -422  -1673       C  
ATOM   6456  O   ASN A 787     -13.735  -2.490 -18.776  1.00 50.79           O  
ANISOU 6456  O   ASN A 787     6437   7197   5665    988   -462  -1725       O  
ATOM   6457  CB  ASN A 787     -12.303  -1.797 -20.963  1.00 53.23           C  
ANISOU 6457  CB  ASN A 787     6954   7070   6200    696   -453  -1618       C  
ATOM   6458  CG  ASN A 787     -11.352  -0.809 -21.563  1.00 56.73           C  
ANISOU 6458  CG  ASN A 787     7469   7305   6781    553   -476  -1688       C  
ATOM   6459  OD1 ASN A 787     -10.665  -0.083 -20.845  1.00 61.80           O  
ANISOU 6459  OD1 ASN A 787     8059   7964   7460    539   -507  -1877       O  
ATOM   6460  ND2 ASN A 787     -11.313  -0.758 -22.887  1.00 54.78           N  
ANISOU 6460  ND2 ASN A 787     7338   6865   6610    440   -461  -1537       N  
ATOM   6461  N   ILE A 788     -12.404  -4.195 -18.157  1.00 50.17           N  
ANISOU 6461  N   ILE A 788     6243   7419   5402    955   -381  -1624       N  
ATOM   6462  CA  ILE A 788     -13.335  -4.677 -17.136  1.00 51.75           C  
ANISOU 6462  CA  ILE A 788     6343   7849   5471   1099   -377  -1619       C  
ATOM   6463  C   ILE A 788     -13.756  -3.549 -16.182  1.00 53.60           C  
ANISOU 6463  C   ILE A 788     6509   8145   5712   1202   -437  -1848       C  
ATOM   6464  O   ILE A 788     -14.948  -3.328 -15.972  1.00 55.70           O  
ANISOU 6464  O   ILE A 788     6761   8440   5963   1298   -457  -1859       O  
ATOM   6465  CB  ILE A 788     -12.761  -5.875 -16.336  1.00 51.85           C  
ANISOU 6465  CB  ILE A 788     6251   8124   5324   1136   -332  -1548       C  
ATOM   6466  CG1 ILE A 788     -12.321  -6.999 -17.283  1.00 49.71           C  
ANISOU 6466  CG1 ILE A 788     6049   7779   5061   1045   -280  -1339       C  
ATOM   6467  CG2 ILE A 788     -13.784  -6.386 -15.316  1.00 52.24           C  
ANISOU 6467  CG2 ILE A 788     6200   8418   5232   1271   -323  -1515       C  
ATOM   6468  CD1 ILE A 788     -11.462  -8.067 -16.612  1.00 51.14           C  
ANISOU 6468  CD1 ILE A 788     6144   8171   5117   1070   -248  -1283       C  
ATOM   6469  N   ALA A 789     -12.778  -2.825 -15.641  1.00 54.49           N  
ANISOU 6469  N   ALA A 789     6572   8278   5851   1180   -468  -2043       N  
ATOM   6470  CA  ALA A 789     -13.035  -1.759 -14.666  1.00 56.49           C  
ANISOU 6470  CA  ALA A 789     6747   8603   6115   1278   -530  -2295       C  
ATOM   6471  C   ALA A 789     -13.878  -0.604 -15.216  1.00 56.84           C  
ANISOU 6471  C   ALA A 789     6885   8393   6317   1294   -589  -2374       C  
ATOM   6472  O   ALA A 789     -14.663  -0.009 -14.479  1.00 57.72           O  
ANISOU 6472  O   ALA A 789     6932   8588   6411   1423   -635  -2527       O  
ATOM   6473  CB  ALA A 789     -11.721  -1.238 -14.077  1.00 57.18           C  
ANISOU 6473  CB  ALA A 789     6766   8748   6213   1231   -551  -2493       C  
ATOM   6474  N   LYS A 790     -13.714  -0.299 -16.503  1.00 55.98           N  
ANISOU 6474  N   LYS A 790     6924   7987   6357   1172   -590  -2270       N  
ATOM   6475  CA  LYS A 790     -14.467   0.772 -17.169  1.00 56.79           C  
ANISOU 6475  CA  LYS A 790     7136   7820   6621   1181   -649  -2309       C  
ATOM   6476  C   LYS A 790     -15.983   0.571 -17.064  1.00 56.54           C  
ANISOU 6476  C   LYS A 790     7089   7860   6533   1322   -659  -2252       C  
ATOM   6477  O   LYS A 790     -16.726   1.524 -16.809  1.00 56.45           O  
ANISOU 6477  O   LYS A 790     7080   7776   6593   1421   -726  -2399       O  
ATOM   6478  CB  LYS A 790     -14.045   0.877 -18.641  1.00 57.10           C  
ANISOU 6478  CB  LYS A 790     7333   7572   6792   1020   -634  -2147       C  
ATOM   6479  CG  LYS A 790     -14.730   1.972 -19.452  1.00 57.22           C  
ANISOU 6479  CG  LYS A 790     7476   7286   6977   1018   -696  -2153       C  
ATOM   6480  CD  LYS A 790     -14.434   1.797 -20.936  1.00 58.69           C  
ANISOU 6480  CD  LYS A 790     7802   7253   7243    866   -665  -1941       C  
ATOM   6481  CE  LYS A 790     -15.030   2.916 -21.779  1.00 60.03           C  
ANISOU 6481  CE  LYS A 790     8108   7117   7583    859   -730  -1927       C  
ATOM   6482  NZ  LYS A 790     -14.281   4.193 -21.602  1.00 62.87           N  
ANISOU 6482  NZ  LYS A 790     8506   7281   8102    791   -789  -2105       N  
ATOM   6483  N   TYR A 791     -16.424  -0.673 -17.249  1.00 54.18           N  
ANISOU 6483  N   TYR A 791     6770   7706   6110   1329   -595  -2048       N  
ATOM   6484  CA  TYR A 791     -17.844  -1.021 -17.227  1.00 53.54           C  
ANISOU 6484  CA  TYR A 791     6667   7712   5965   1439   -592  -1968       C  
ATOM   6485  C   TYR A 791     -18.290  -1.649 -15.904  1.00 55.58           C  
ANISOU 6485  C   TYR A 791     6759   8324   6036   1563   -569  -2016       C  
ATOM   6486  O   TYR A 791     -19.382  -2.224 -15.818  1.00 55.07           O  
ANISOU 6486  O   TYR A 791     6654   8387   5883   1634   -547  -1916       O  
ATOM   6487  CB  TYR A 791     -18.172  -1.963 -18.389  1.00 51.60           C  
ANISOU 6487  CB  TYR A 791     6511   7378   5718   1356   -539  -1706       C  
ATOM   6488  CG  TYR A 791     -17.920  -1.362 -19.751  1.00 49.61           C  
ANISOU 6488  CG  TYR A 791     6415   6804   5629   1246   -561  -1638       C  
ATOM   6489  CD1 TYR A 791     -16.771  -1.677 -20.468  1.00 45.85           C  
ANISOU 6489  CD1 TYR A 791     6005   6223   5194   1094   -525  -1549       C  
ATOM   6490  CD2 TYR A 791     -18.830  -0.466 -20.319  1.00 50.47           C  
ANISOU 6490  CD2 TYR A 791     6603   6728   5846   1298   -620  -1662       C  
ATOM   6491  CE1 TYR A 791     -16.536  -1.122 -21.727  1.00 47.77           C  
ANISOU 6491  CE1 TYR A 791     6384   6192   5572    986   -541  -1475       C  
ATOM   6492  CE2 TYR A 791     -18.606   0.093 -21.575  1.00 50.65           C  
ANISOU 6492  CE2 TYR A 791     6772   6463   6011   1197   -641  -1579       C  
ATOM   6493  CZ  TYR A 791     -17.457  -0.240 -22.272  1.00 48.69           C  
ANISOU 6493  CZ  TYR A 791     6583   6125   5791   1036   -599  -1482       C  
ATOM   6494  OH  TYR A 791     -17.228   0.311 -23.512  1.00 49.29           O  
ANISOU 6494  OH  TYR A 791     6795   5940   5992    929   -616  -1391       O  
ATOM   6495  N   ASP A 792     -17.449  -1.537 -14.878  1.00 57.60           N  
ANISOU 6495  N   ASP A 792     6913   8750   6224   1584   -574  -2166       N  
ATOM   6496  CA  ASP A 792     -17.780  -2.078 -13.563  1.00 60.31           C  
ANISOU 6496  CA  ASP A 792     7089   9452   6374   1702   -553  -2214       C  
ATOM   6497  C   ASP A 792     -18.391  -1.012 -12.648  1.00 62.79           C  
ANISOU 6497  C   ASP A 792     7309   9868   6682   1846   -622  -2478       C  
ATOM   6498  O   ASP A 792     -17.689  -0.141 -12.116  1.00 64.09           O  
ANISOU 6498  O   ASP A 792     7436  10018   6897   1860   -671  -2706       O  
ATOM   6499  CB  ASP A 792     -16.558  -2.749 -12.909  1.00 60.47           C  
ANISOU 6499  CB  ASP A 792     7031   9657   6286   1659   -515  -2206       C  
ATOM   6500  CG  ASP A 792     -16.918  -3.550 -11.654  1.00 61.72           C  
ANISOU 6500  CG  ASP A 792     7026  10201   6224   1769   -482  -2184       C  
ATOM   6501  OD1 ASP A 792     -17.709  -3.061 -10.816  1.00 63.62           O  
ANISOU 6501  OD1 ASP A 792     7162  10618   6393   1897   -513  -2330       O  
ATOM   6502  OD2 ASP A 792     -16.394  -4.672 -11.497  1.00 61.35           O  
ANISOU 6502  OD2 ASP A 792     6951  10286   6072   1731   -425  -2018       O  
ATOM   6503  N   VAL A 793     -19.709  -1.096 -12.490  1.00 63.51           N  
ANISOU 6503  N   VAL A 793     7355  10064   6712   1953   -626  -2452       N  
ATOM   6504  CA  VAL A 793     -20.444  -0.283 -11.531  1.00 65.29           C  
ANISOU 6504  CA  VAL A 793     7461  10453   6892   2114   -684  -2692       C  
ATOM   6505  C   VAL A 793     -20.903  -1.205 -10.396  1.00 65.81           C  
ANISOU 6505  C   VAL A 793     7351  10941   6712   2201   -632  -2644       C  
ATOM   6506  O   VAL A 793     -21.903  -1.916 -10.526  1.00 65.66           O  
ANISOU 6506  O   VAL A 793     7308  11034   6607   2226   -590  -2479       O  
ATOM   6507  CB  VAL A 793     -21.648   0.447 -12.200  1.00 66.25           C  
ANISOU 6507  CB  VAL A 793     7655  10386   7131   2184   -737  -2723       C  
ATOM   6508  CG1 VAL A 793     -22.445   1.257 -11.178  1.00 69.06           C  
ANISOU 6508  CG1 VAL A 793     7875  10933   7433   2368   -800  -2986       C  
ATOM   6509  CG2 VAL A 793     -21.169   1.356 -13.329  1.00 65.96           C  
ANISOU 6509  CG2 VAL A 793     7799   9929   7333   2094   -790  -2744       C  
ATOM   6510  N   GLY A 794     -20.139  -1.208  -9.302  1.00 67.17           N  
ANISOU 6510  N   GLY A 794     7398  11352   6770   2237   -632  -2780       N  
ATOM   6511  CA  GLY A 794     -20.442  -2.011  -8.108  1.00 68.17           C  
ANISOU 6511  CA  GLY A 794     7346  11908   6650   2322   -586  -2743       C  
ATOM   6512  C   GLY A 794     -20.734  -3.486  -8.352  1.00 66.59           C  
ANISOU 6512  C   GLY A 794     7155  11815   6333   2256   -497  -2414       C  
ATOM   6513  O   GLY A 794     -21.672  -4.044  -7.776  1.00 67.11           O  
ANISOU 6513  O   GLY A 794     7111  12149   6241   2326   -463  -2334       O  
ATOM   6514  N   GLY A 795     -19.934  -4.114  -9.211  1.00 64.19           N  
ANISOU 6514  N   GLY A 795     6977  11300   6111   2119   -461  -2227       N  
ATOM   6515  CA  GLY A 795     -20.100  -5.531  -9.544  1.00 61.78           C  
ANISOU 6515  CA  GLY A 795     6699  11047   5729   2046   -383  -1919       C  
ATOM   6516  C   GLY A 795     -21.210  -5.805 -10.544  1.00 59.62           C  
ANISOU 6516  C   GLY A 795     6516  10606   5531   2009   -365  -1761       C  
ATOM   6517  O   GLY A 795     -21.564  -6.962 -10.794  1.00 57.53           O  
ANISOU 6517  O   GLY A 795     6263  10392   5205   1954   -303  -1519       O  
ATOM   6518  N   PHE A 796     -21.755  -4.737 -11.119  1.00 59.14           N  
ANISOU 6518  N   PHE A 796     6520  10343   5609   2040   -423  -1901       N  
ATOM   6519  CA  PHE A 796     -22.865  -4.837 -12.058  1.00 57.42           C  
ANISOU 6519  CA  PHE A 796     6378   9978   5462   2024   -418  -1783       C  
ATOM   6520  C   PHE A 796     -22.575  -4.070 -13.351  1.00 54.97           C  
ANISOU 6520  C   PHE A 796     6242   9275   5370   1952   -463  -1808       C  
ATOM   6521  O   PHE A 796     -21.825  -3.090 -13.329  1.00 56.10           O  
ANISOU 6521  O   PHE A 796     6424   9275   5616   1954   -517  -1987       O  
ATOM   6522  CB  PHE A 796     -24.160  -4.354 -11.401  1.00 58.53           C  
ANISOU 6522  CB  PHE A 796     6396  10325   5517   2167   -446  -1910       C  
ATOM   6523  CG  PHE A 796     -24.785  -5.367 -10.479  1.00 61.44           C  
ANISOU 6523  CG  PHE A 796     6611  11064   5669   2204   -382  -1791       C  
ATOM   6524  CD1 PHE A 796     -25.456  -6.478 -10.993  1.00 61.03           C  
ANISOU 6524  CD1 PHE A 796     6582  11028   5578   2128   -317  -1534       C  
ATOM   6525  CD2 PHE A 796     -24.711  -5.211  -9.098  1.00 63.26           C  
ANISOU 6525  CD2 PHE A 796     6671  11633   5732   2309   -387  -1934       C  
ATOM   6526  CE1 PHE A 796     -26.037  -7.421 -10.145  1.00 62.26           C  
ANISOU 6526  CE1 PHE A 796     6599  11516   5541   2146   -256  -1406       C  
ATOM   6527  CE2 PHE A 796     -25.289  -6.148  -8.241  1.00 65.04           C  
ANISOU 6527  CE2 PHE A 796     6751  12213   5746   2335   -324  -1803       C  
ATOM   6528  CZ  PHE A 796     -25.952  -7.256  -8.767  1.00 64.08           C  
ANISOU 6528  CZ  PHE A 796     6662  12089   5597   2248   -258  -1531       C  
ATOM   6529  N   PRO A 797     -23.164  -4.516 -14.483  1.00 51.69           N  
ANISOU 6529  N   PRO A 797     5928   8688   5023   1884   -441  -1625       N  
ATOM   6530  CA  PRO A 797     -22.844  -3.898 -15.773  1.00 49.60           C  
ANISOU 6530  CA  PRO A 797     5831   8068   4949   1805   -476  -1611       C  
ATOM   6531  C   PRO A 797     -23.267  -2.430 -15.847  1.00 49.52           C  
ANISOU 6531  C   PRO A 797     5850   7909   5055   1899   -566  -1824       C  
ATOM   6532  O   PRO A 797     -24.411  -2.098 -15.543  1.00 49.90           O  
ANISOU 6532  O   PRO A 797     5833   8063   5066   2019   -595  -1896       O  
ATOM   6533  CB  PRO A 797     -23.644  -4.742 -16.780  1.00 47.87           C  
ANISOU 6533  CB  PRO A 797     5673   7779   4736   1744   -435  -1387       C  
ATOM   6534  CG  PRO A 797     -23.968  -6.014 -16.059  1.00 48.86           C  
ANISOU 6534  CG  PRO A 797     5685   8188   4693   1745   -364  -1252       C  
ATOM   6535  CD  PRO A 797     -24.144  -5.609 -14.634  1.00 50.32           C  
ANISOU 6535  CD  PRO A 797     5716   8650   4753   1871   -382  -1424       C  
ATOM   6536  N   GLY A 798     -22.329  -1.570 -16.234  1.00 48.39           N  
ANISOU 6536  N   GLY A 798     5803   7526   5056   1843   -610  -1923       N  
ATOM   6537  CA  GLY A 798     -22.609  -0.165 -16.479  1.00 48.74           C  
ANISOU 6537  CA  GLY A 798     5910   7358   5252   1910   -700  -2101       C  
ATOM   6538  C   GLY A 798     -23.178   0.065 -17.870  1.00 47.99           C  
ANISOU 6538  C   GLY A 798     5960   6990   5283   1869   -720  -1965       C  
ATOM   6539  O   GLY A 798     -23.486  -0.896 -18.582  1.00 45.24           O  
ANISOU 6539  O   GLY A 798     5647   6654   4890   1799   -663  -1750       O  
ATOM   6540  N   PRO A 799     -23.331   1.346 -18.266  1.00 49.28           N  
ANISOU 6540  N   PRO A 799     6211   6905   5608   1914   -806  -2091       N  
ATOM   6541  CA  PRO A 799     -23.870   1.680 -19.586  1.00 48.97           C  
ANISOU 6541  CA  PRO A 799     6312   6605   5687   1888   -836  -1963       C  
ATOM   6542  C   PRO A 799     -22.968   1.172 -20.712  1.00 46.69           C  
ANISOU 6542  C   PRO A 799     6148   6138   5453   1699   -785  -1760       C  
ATOM   6543  O   PRO A 799     -21.743   1.268 -20.613  1.00 46.19           O  
ANISOU 6543  O   PRO A 799     6110   6011   5429   1593   -770  -1792       O  
ATOM   6544  CB  PRO A 799     -23.903   3.216 -19.581  1.00 49.93           C  
ANISOU 6544  CB  PRO A 799     6500   6489   5981   1967   -942  -2159       C  
ATOM   6545  CG  PRO A 799     -23.883   3.600 -18.134  1.00 52.72           C  
ANISOU 6545  CG  PRO A 799     6708   7052   6272   2088   -972  -2415       C  
ATOM   6546  CD  PRO A 799     -23.032   2.556 -17.477  1.00 51.84           C  
ANISOU 6546  CD  PRO A 799     6502   7181   6012   2000   -884  -2364       C  
ATOM   6547  N   LYS A 800     -23.587   0.626 -21.757  1.00 45.13           N  
ANISOU 6547  N   LYS A 800     6015   5885   5249   1663   -760  -1565       N  
ATOM   6548  CA  LYS A 800     -22.889   0.144 -22.964  1.00 44.39           C  
ANISOU 6548  CA  LYS A 800     6035   5631   5199   1496   -717  -1370       C  
ATOM   6549  C   LYS A 800     -21.989  -1.072 -22.711  1.00 41.47           C  
ANISOU 6549  C   LYS A 800     5612   5420   4726   1385   -628  -1279       C  
ATOM   6550  O   LYS A 800     -21.120  -1.383 -23.530  1.00 41.52           O  
ANISOU 6550  O   LYS A 800     5697   5308   4771   1245   -594  -1166       O  
ATOM   6551  CB  LYS A 800     -22.104   1.281 -23.646  1.00 46.39           C  
ANISOU 6551  CB  LYS A 800     6424   5578   5626   1417   -770  -1404       C  
ATOM   6552  CG  LYS A 800     -22.983   2.434 -24.123  1.00 51.32           C  
ANISOU 6552  CG  LYS A 800     7129   5998   6371   1520   -862  -1449       C  
ATOM   6553  CD  LYS A 800     -22.202   3.721 -24.331  1.00 57.22           C  
ANISOU 6553  CD  LYS A 800     7984   6461   7296   1468   -928  -1543       C  
ATOM   6554  CE  LYS A 800     -23.126   4.820 -24.862  1.00 62.84           C  
ANISOU 6554  CE  LYS A 800     8788   6954   8136   1580  -1025  -1564       C  
ATOM   6555  NZ  LYS A 800     -22.612   6.200 -24.611  1.00 65.02           N  
ANISOU 6555  NZ  LYS A 800     9134   6980   8591   1588  -1110  -1728       N  
ATOM   6556  N   CYS A 801     -22.221  -1.766 -21.596  1.00 39.85           N  
ANISOU 6556  N   CYS A 801     5270   5488   4384   1453   -593  -1324       N  
ATOM   6557  CA  CYS A 801     -21.390  -2.901 -21.200  1.00 40.48           C  
ANISOU 6557  CA  CYS A 801     5292   5727   4362   1374   -518  -1246       C  
ATOM   6558  C   CYS A 801     -21.429  -4.032 -22.233  1.00 38.48           C  
ANISOU 6558  C   CYS A 801     5092   5442   4087   1269   -458  -1022       C  
ATOM   6559  O   CYS A 801     -22.497  -4.589 -22.506  1.00 36.80           O  
ANISOU 6559  O   CYS A 801     4858   5298   3825   1306   -442   -926       O  
ATOM   6560  CB  CYS A 801     -21.779  -3.429 -19.815  1.00 41.24           C  
ANISOU 6560  CB  CYS A 801     5231   6132   4307   1476   -495  -1312       C  
ATOM   6561  SG  CYS A 801     -20.739  -4.818 -19.248  1.00 42.71           S  
ANISOU 6561  SG  CYS A 801     5346   6512   4368   1396   -413  -1206       S  
ATOM   6562  N   PRO A 802     -20.257  -4.358 -22.816  1.00 36.78           N  
ANISOU 6562  N   PRO A 802     4939   5128   3909   1139   -427   -953       N  
ATOM   6563  CA  PRO A 802     -20.153  -5.433 -23.807  1.00 33.92           C  
ANISOU 6563  CA  PRO A 802     4623   4734   3531   1039   -373   -764       C  
ATOM   6564  C   PRO A 802     -20.567  -6.779 -23.228  1.00 31.11           C  
ANISOU 6564  C   PRO A 802     4173   4598   3051   1065   -316   -671       C  
ATOM   6565  O   PRO A 802     -20.316  -7.062 -22.046  1.00 30.15           O  
ANISOU 6565  O   PRO A 802     3953   4660   2843   1118   -301   -732       O  
ATOM   6566  CB  PRO A 802     -18.666  -5.442 -24.177  1.00 31.99           C  
ANISOU 6566  CB  PRO A 802     4427   4397   3331    916   -354   -762       C  
ATOM   6567  CG  PRO A 802     -18.176  -4.077 -23.817  1.00 37.72           C  
ANISOU 6567  CG  PRO A 802     5175   5014   4141    929   -410   -929       C  
ATOM   6568  CD  PRO A 802     -18.958  -3.698 -22.590  1.00 37.60           C  
ANISOU 6568  CD  PRO A 802     5065   5148   4073   1077   -443  -1065       C  
ATOM   6569  N   PHE A 803     -21.199  -7.587 -24.073  1.00 28.92           N  
ANISOU 6569  N   PHE A 803     3924   4298   2765   1025   -286   -524       N  
ATOM   6570  CA  PHE A 803     -21.709  -8.899 -23.700  1.00 29.87           C  
ANISOU 6570  CA  PHE A 803     3970   4590   2791   1031   -234   -413       C  
ATOM   6571  C   PHE A 803     -20.704  -9.755 -22.936  1.00 30.50           C  
ANISOU 6571  C   PHE A 803     3994   4789   2805   1004   -191   -389       C  
ATOM   6572  O   PHE A 803     -21.060 -10.362 -21.921  1.00 30.73           O  
ANISOU 6572  O   PHE A 803     3927   5014   2736   1061   -167   -369       O  
ATOM   6573  CB  PHE A 803     -22.172  -9.639 -24.947  1.00 30.72           C  
ANISOU 6573  CB  PHE A 803     4135   4607   2929    956   -210   -269       C  
ATOM   6574  CG  PHE A 803     -22.922 -10.910 -24.664  1.00 31.91           C  
ANISOU 6574  CG  PHE A 803     4214   4904   3005    956   -162   -157       C  
ATOM   6575  CD1 PHE A 803     -24.278 -10.877 -24.349  1.00 32.58           C  
ANISOU 6575  CD1 PHE A 803     4235   5100   3044   1027   -169   -156       C  
ATOM   6576  CD2 PHE A 803     -22.279 -12.143 -24.753  1.00 29.59           C  
ANISOU 6576  CD2 PHE A 803     3918   4631   2694    883   -113    -52       C  
ATOM   6577  CE1 PHE A 803     -24.982 -12.056 -24.104  1.00 33.19           C  
ANISOU 6577  CE1 PHE A 803     4245   5310   3057   1008   -122    -44       C  
ATOM   6578  CE2 PHE A 803     -22.971 -13.330 -24.513  1.00 28.95           C  
ANISOU 6578  CE2 PHE A 803     3779   4660   2562    871    -72     61       C  
ATOM   6579  CZ  PHE A 803     -24.325 -13.286 -24.190  1.00 33.05           C  
ANISOU 6579  CZ  PHE A 803     4234   5291   3035    925    -73     69       C  
ATOM   6580  N   HIS A 804     -19.458  -9.800 -23.412  1.00 28.22           N  
ANISOU 6580  N   HIS A 804     3761   4396   2564    921   -183   -388       N  
ATOM   6581  CA  HIS A 804     -18.436 -10.648 -22.783  1.00 29.53           C  
ANISOU 6581  CA  HIS A 804     3878   4670   2671    901   -148   -362       C  
ATOM   6582  C   HIS A 804     -17.966 -10.102 -21.434  1.00 31.89           C  
ANISOU 6582  C   HIS A 804     4093   5118   2907    979   -166   -498       C  
ATOM   6583  O   HIS A 804     -17.590 -10.872 -20.547  1.00 33.67           O  
ANISOU 6583  O   HIS A 804     4242   5512   3041   1010   -140   -466       O  
ATOM   6584  CB  HIS A 804     -17.257 -10.932 -23.736  1.00 27.49           C  
ANISOU 6584  CB  HIS A 804     3691   4279   2473    793   -133   -325       C  
ATOM   6585  CG  HIS A 804     -16.437  -9.725 -24.083  1.00 27.39           C  
ANISOU 6585  CG  HIS A 804     3731   4140   2535    748   -167   -442       C  
ATOM   6586  ND1 HIS A 804     -16.896  -8.721 -24.911  1.00 27.68           N  
ANISOU 6586  ND1 HIS A 804     3848   4012   2657    723   -203   -467       N  
ATOM   6587  CD2 HIS A 804     -15.179  -9.369 -23.725  1.00 26.68           C  
ANISOU 6587  CD2 HIS A 804     3625   4062   2449    716   -172   -536       C  
ATOM   6588  CE1 HIS A 804     -15.965  -7.790 -25.030  1.00 27.65           C  
ANISOU 6588  CE1 HIS A 804     3879   3913   2714    671   -227   -565       C  
ATOM   6589  NE2 HIS A 804     -14.911  -8.161 -24.325  1.00 27.88           N  
ANISOU 6589  NE2 HIS A 804     3847   4052   2696    662   -207   -615       N  
ATOM   6590  N   ILE A 805     -18.016  -8.778 -21.278  1.00 33.82           N  
ANISOU 6590  N   ILE A 805     4349   5300   3200   1013   -216   -650       N  
ATOM   6591  CA  ILE A 805     -17.660  -8.124 -20.014  1.00 33.16           C  
ANISOU 6591  CA  ILE A 805     4179   5357   3064   1093   -243   -814       C  
ATOM   6592  C   ILE A 805     -18.760  -8.321 -18.974  1.00 35.19           C  
ANISOU 6592  C   ILE A 805     4329   5832   3211   1211   -240   -826       C  
ATOM   6593  O   ILE A 805     -18.480  -8.424 -17.780  1.00 38.97           O  
ANISOU 6593  O   ILE A 805     4703   6518   3586   1278   -237   -895       O  
ATOM   6594  CB  ILE A 805     -17.346  -6.610 -20.204  1.00 32.73           C  
ANISOU 6594  CB  ILE A 805     4175   5143   3118   1088   -302   -988       C  
ATOM   6595  CG1 ILE A 805     -16.238  -6.403 -21.254  1.00 30.56           C  
ANISOU 6595  CG1 ILE A 805     4000   4667   2945    954   -299   -963       C  
ATOM   6596  CG2 ILE A 805     -16.941  -5.972 -18.888  1.00 31.16           C  
ANISOU 6596  CG2 ILE A 805     3876   5097   2867   1168   -332  -1179       C  
ATOM   6597  CD1 ILE A 805     -14.878  -7.007 -20.889  1.00 26.32           C  
ANISOU 6597  CD1 ILE A 805     3418   4225   2359    901   -267   -969       C  
ATOM   6598  N   ARG A 806     -20.007  -8.372 -19.435  1.00 36.84           N  
ANISOU 6598  N   ARG A 806     4556   6009   3432   1234   -242   -760       N  
ATOM   6599  CA  ARG A 806     -21.150  -8.715 -18.587  1.00 37.01           C  
ANISOU 6599  CA  ARG A 806     4471   6250   3341   1328   -229   -743       C  
ATOM   6600  C   ARG A 806     -20.926 -10.104 -17.973  1.00 37.26           C  
ANISOU 6600  C   ARG A 806     4433   6466   3258   1310   -168   -595       C  
ATOM   6601  O   ARG A 806     -21.129 -10.303 -16.775  1.00 36.59           O  
ANISOU 6601  O   ARG A 806     4230   6624   3047   1386   -157   -621       O  
ATOM   6602  CB  ARG A 806     -22.449  -8.684 -19.406  1.00 35.35           C  
ANISOU 6602  CB  ARG A 806     4299   5960   3172   1332   -236   -675       C  
ATOM   6603  CG  ARG A 806     -23.718  -8.995 -18.609  1.00 39.59           C  
ANISOU 6603  CG  ARG A 806     4718   6731   3594   1420   -221   -661       C  
ATOM   6604  CD  ARG A 806     -24.985  -8.919 -19.475  1.00 38.42           C  
ANISOU 6604  CD  ARG A 806     4601   6508   3489   1425   -232   -607       C  
ATOM   6605  NE  ARG A 806     -25.319  -7.547 -19.871  1.00 37.69           N  
ANISOU 6605  NE  ARG A 806     4560   6273   3488   1493   -304   -756       N  
ATOM   6606  CZ  ARG A 806     -26.078  -6.710 -19.161  1.00 41.06           C  
ANISOU 6606  CZ  ARG A 806     4907   6814   3879   1622   -348   -908       C  
ATOM   6607  NH1 ARG A 806     -26.606  -7.082 -17.995  1.00 38.52           N  
ANISOU 6607  NH1 ARG A 806     4441   6781   3416   1695   -323   -936       N  
ATOM   6608  NH2 ARG A 806     -26.308  -5.488 -19.620  1.00 39.49           N  
ANISOU 6608  NH2 ARG A 806     4773   6445   3786   1682   -420  -1033       N  
ATOM   6609  N   GLY A 807     -20.484 -11.045 -18.808  1.00 35.86           N  
ANISOU 6609  N   GLY A 807     4328   6172   3126   1210   -133   -442       N  
ATOM   6610  CA  GLY A 807     -20.201 -12.411 -18.382  1.00 34.49           C  
ANISOU 6610  CA  GLY A 807     4112   6120   2873   1187    -81   -287       C  
ATOM   6611  C   GLY A 807     -19.103 -12.486 -17.343  1.00 35.25           C  
ANISOU 6611  C   GLY A 807     4142   6363   2890   1227    -81   -344       C  
ATOM   6612  O   GLY A 807     -19.171 -13.300 -16.419  1.00 37.03           O  
ANISOU 6612  O   GLY A 807     4282   6788   2999   1266    -51   -255       O  
ATOM   6613  N   ILE A 808     -18.090 -11.636 -17.490  1.00 35.10           N  
ANISOU 6613  N   ILE A 808     4157   6252   2929   1214   -115   -487       N  
ATOM   6614  CA  ILE A 808     -16.999 -11.576 -16.521  1.00 36.42           C  
ANISOU 6614  CA  ILE A 808     4252   6565   3020   1254   -121   -572       C  
ATOM   6615  C   ILE A 808     -17.504 -11.029 -15.190  1.00 38.77           C  
ANISOU 6615  C   ILE A 808     4424   7107   3199   1370   -140   -692       C  
ATOM   6616  O   ILE A 808     -17.177 -11.570 -14.130  1.00 42.12           O  
ANISOU 6616  O   ILE A 808     4750   7762   3493   1427   -124   -665       O  
ATOM   6617  CB  ILE A 808     -15.808 -10.732 -17.029  1.00 36.96           C  
ANISOU 6617  CB  ILE A 808     4379   6477   3185   1197   -153   -710       C  
ATOM   6618  CG1 ILE A 808     -15.089 -11.457 -18.168  1.00 32.75           C  
ANISOU 6618  CG1 ILE A 808     3940   5770   2731   1090   -127   -590       C  
ATOM   6619  CG2 ILE A 808     -14.822 -10.426 -15.885  1.00 33.42           C  
ANISOU 6619  CG2 ILE A 808     3834   6213   2652   1254   -170   -848       C  
ATOM   6620  CD1 ILE A 808     -14.247 -10.544 -19.030  1.00 34.31           C  
ANISOU 6620  CD1 ILE A 808     4217   5773   3046   1006   -153   -699       C  
ATOM   6621  N   LEU A 809     -18.306  -9.968 -15.250  1.00 39.34           N  
ANISOU 6621  N   LEU A 809     4496   7137   3313   1412   -177   -823       N  
ATOM   6622  CA  LEU A 809     -18.881  -9.375 -14.045  1.00 40.93           C  
ANISOU 6622  CA  LEU A 809     4571   7574   3405   1532   -200   -963       C  
ATOM   6623  C   LEU A 809     -19.776 -10.365 -13.308  1.00 41.35           C  
ANISOU 6623  C   LEU A 809     4526   7877   3309   1579   -154   -814       C  
ATOM   6624  O   LEU A 809     -19.765 -10.408 -12.076  1.00 43.51           O  
ANISOU 6624  O   LEU A 809     4670   8428   3435   1664   -151   -866       O  
ATOM   6625  CB  LEU A 809     -19.638  -8.085 -14.373  1.00 40.78           C  
ANISOU 6625  CB  LEU A 809     4582   7435   3479   1574   -254  -1129       C  
ATOM   6626  CG  LEU A 809     -18.749  -6.918 -14.811  1.00 42.13           C  
ANISOU 6626  CG  LEU A 809     4828   7391   3788   1539   -308  -1306       C  
ATOM   6627  CD1 LEU A 809     -19.580  -5.759 -15.310  1.00 40.41           C  
ANISOU 6627  CD1 LEU A 809     4665   7007   3683   1577   -364  -1426       C  
ATOM   6628  CD2 LEU A 809     -17.841  -6.469 -13.681  1.00 43.82           C  
ANISOU 6628  CD2 LEU A 809     4941   7777   3931   1593   -331  -1488       C  
ATOM   6629  N   THR A 810     -20.525 -11.168 -14.069  1.00 40.42           N  
ANISOU 6629  N   THR A 810     4465   7667   3226   1517   -118   -626       N  
ATOM   6630  CA  THR A 810     -21.349 -12.240 -13.510  1.00 41.96           C  
ANISOU 6630  CA  THR A 810     4579   8065   3297   1529    -67   -450       C  
ATOM   6631  C   THR A 810     -20.463 -13.223 -12.748  1.00 42.91           C  
ANISOU 6631  C   THR A 810     4651   8337   3314   1528    -35   -332       C  
ATOM   6632  O   THR A 810     -20.707 -13.509 -11.575  1.00 45.74           O  
ANISOU 6632  O   THR A 810     4884   8981   3513   1598    -17   -307       O  
ATOM   6633  CB  THR A 810     -22.142 -12.998 -14.605  1.00 41.87           C  
ANISOU 6633  CB  THR A 810     4651   7889   3368   1438    -35   -272       C  
ATOM   6634  OG1 THR A 810     -22.871 -12.069 -15.418  1.00 42.39           O  
ANISOU 6634  OG1 THR A 810     4772   7800   3535   1442    -72   -376       O  
ATOM   6635  CG2 THR A 810     -23.123 -13.986 -13.975  1.00 40.53           C  
ANISOU 6635  CG2 THR A 810     4387   7935   3077   1441     16   -104       C  
ATOM   6636  N   TYR A 811     -19.432 -13.717 -13.430  1.00 42.10           N  
ANISOU 6636  N   TYR A 811     4643   8052   3299   1455    -29   -263       N  
ATOM   6637  CA  TYR A 811     -18.414 -14.576 -12.836  1.00 41.20           C  
ANISOU 6637  CA  TYR A 811     4499   8045   3110   1463    -10   -168       C  
ATOM   6638  C   TYR A 811     -17.816 -13.993 -11.559  1.00 42.22           C  
ANISOU 6638  C   TYR A 811     4508   8427   3107   1564    -35   -319       C  
ATOM   6639  O   TYR A 811     -17.723 -14.693 -10.550  1.00 42.44           O  
ANISOU 6639  O   TYR A 811     4442   8696   2986   1618    -13   -218       O  
ATOM   6640  CB  TYR A 811     -17.300 -14.852 -13.848  1.00 39.07           C  
ANISOU 6640  CB  TYR A 811     4346   7530   2969   1382    -16   -145       C  
ATOM   6641  CG  TYR A 811     -16.175 -15.728 -13.332  1.00 38.90           C  
ANISOU 6641  CG  TYR A 811     4298   7599   2883   1401     -5    -58       C  
ATOM   6642  CD1 TYR A 811     -16.303 -17.114 -13.302  1.00 38.73           C  
ANISOU 6642  CD1 TYR A 811     4289   7590   2837   1380     32    174       C  
ATOM   6643  CD2 TYR A 811     -14.978 -15.170 -12.887  1.00 36.46           C  
ANISOU 6643  CD2 TYR A 811     3952   7358   2545   1439    -36   -210       C  
ATOM   6644  CE1 TYR A 811     -15.275 -17.923 -12.827  1.00 37.75           C  
ANISOU 6644  CE1 TYR A 811     4144   7541   2658   1413     34    259       C  
ATOM   6645  CE2 TYR A 811     -13.949 -15.966 -12.415  1.00 37.92           C  
ANISOU 6645  CE2 TYR A 811     4106   7639   2664   1469    -31   -134       C  
ATOM   6646  CZ  TYR A 811     -14.102 -17.343 -12.390  1.00 38.15           C  
ANISOU 6646  CZ  TYR A 811     4152   7674   2668   1463      2    104       C  
ATOM   6647  OH  TYR A 811     -13.079 -18.141 -11.923  1.00 40.01           O  
ANISOU 6647  OH  TYR A 811     4361   7997   2843   1508     -1    184       O  
ATOM   6648  N   ASN A 812     -17.399 -12.727 -11.604  1.00 43.07           N  
ANISOU 6648  N   ASN A 812     4617   8479   3268   1588    -83   -557       N  
ATOM   6649  CA  ASN A 812     -16.787 -12.092 -10.433  1.00 45.59           C  
ANISOU 6649  CA  ASN A 812     4817   9032   3473   1681   -113   -737       C  
ATOM   6650  C   ASN A 812     -17.718 -12.114  -9.220  1.00 48.65           C  
ANISOU 6650  C   ASN A 812     5058   9747   3682   1784   -102   -742       C  
ATOM   6651  O   ASN A 812     -17.278 -12.414  -8.111  1.00 50.70           O  
ANISOU 6651  O   ASN A 812     5201  10280   3781   1856    -97   -740       O  
ATOM   6652  CB  ASN A 812     -16.313 -10.665 -10.740  1.00 45.66           C  
ANISOU 6652  CB  ASN A 812     4857   8897   3593   1678   -169  -1002       C  
ATOM   6653  CG  ASN A 812     -15.122 -10.625 -11.696  1.00 45.60           C  
ANISOU 6653  CG  ASN A 812     4962   8641   3723   1579   -178  -1012       C  
ATOM   6654  OD1 ASN A 812     -14.512 -11.651 -12.007  1.00 47.25           O  
ANISOU 6654  OD1 ASN A 812     5209   8816   3929   1532   -147   -848       O  
ATOM   6655  ND2 ASN A 812     -14.787  -9.429 -12.165  1.00 43.24           N  
ANISOU 6655  ND2 ASN A 812     4713   8168   3548   1546   -222  -1206       N  
ATOM   6656  N   ARG A 813     -19.002 -11.828  -9.443  1.00 50.03           N  
ANISOU 6656  N   ARG A 813     5228   9907   3873   1792    -98   -743       N  
ATOM   6657  CA  ARG A 813     -20.012 -11.905  -8.379  1.00 52.16           C  
ANISOU 6657  CA  ARG A 813     5351  10499   3969   1880    -81   -735       C  
ATOM   6658  C   ARG A 813     -20.180 -13.322  -7.839  1.00 53.00           C  
ANISOU 6658  C   ARG A 813     5406  10792   3938   1863    -20   -460       C  
ATOM   6659  O   ARG A 813     -20.412 -13.510  -6.644  1.00 55.81           O  
ANISOU 6659  O   ARG A 813     5617  11485   4103   1942     -5   -445       O  
ATOM   6660  CB  ARG A 813     -21.370 -11.399  -8.863  1.00 51.42           C  
ANISOU 6660  CB  ARG A 813     5269  10338   3932   1885    -87   -778       C  
ATOM   6661  CG  ARG A 813     -21.486  -9.894  -9.000  1.00 51.72           C  
ANISOU 6661  CG  ARG A 813     5311  10283   4058   1947   -155  -1067       C  
ATOM   6662  CD  ARG A 813     -22.949  -9.453  -9.095  1.00 51.41           C  
ANISOU 6662  CD  ARG A 813     5229  10292   4012   1997   -163  -1116       C  
ATOM   6663  NE  ARG A 813     -23.739 -10.248 -10.039  1.00 51.11           N  
ANISOU 6663  NE  ARG A 813     5274  10108   4038   1906   -121   -897       N  
ATOM   6664  CZ  ARG A 813     -23.764 -10.062 -11.359  1.00 51.34           C  
ANISOU 6664  CZ  ARG A 813     5454   9806   4248   1829   -136   -868       C  
ATOM   6665  NH1 ARG A 813     -23.028  -9.111 -11.926  1.00 49.40           N  
ANISOU 6665  NH1 ARG A 813     5302   9323   4143   1821   -190  -1025       N  
ATOM   6666  NH2 ARG A 813     -24.527 -10.840 -12.120  1.00 49.21           N  
ANISOU 6666  NH2 ARG A 813     5236   9448   4016   1752    -97   -679       N  
ATOM   6667  N   ALA A 814     -20.077 -14.306  -8.728  1.00 50.91           N  
ANISOU 6667  N   ALA A 814     5259  10310   3774   1760     13   -243       N  
ATOM   6668  CA  ALA A 814     -20.230 -15.708  -8.355  1.00 52.06           C  
ANISOU 6668  CA  ALA A 814     5382  10570   3829   1729     67     37       C  
ATOM   6669  C   ALA A 814     -19.063 -16.210  -7.495  1.00 54.23           C  
ANISOU 6669  C   ALA A 814     5604  11011   3991   1781     65     88       C  
ATOM   6670  O   ALA A 814     -19.267 -17.008  -6.574  1.00 55.20           O  
ANISOU 6670  O   ALA A 814     5636  11383   3954   1814     98    258       O  
ATOM   6671  CB  ALA A 814     -20.396 -16.570  -9.600  1.00 49.56           C  
ANISOU 6671  CB  ALA A 814     5209   9949   3672   1607     94    222       C  
ATOM   6672  N   ILE A 815     -17.854 -15.728  -7.786  1.00 54.16           N  
ANISOU 6672  N   ILE A 815     5645  10876   4057   1788     26    -57       N  
ATOM   6673  CA  ILE A 815     -16.647 -16.172  -7.075  1.00 57.61           C  
ANISOU 6673  CA  ILE A 815     6036  11456   4398   1842     16    -26       C  
ATOM   6674  C   ILE A 815     -16.187 -15.234  -5.949  1.00 61.21           C  
ANISOU 6674  C   ILE A 815     6350  12198   4711   1954    -21   -259       C  
ATOM   6675  O   ILE A 815     -15.229 -15.546  -5.232  1.00 61.47           O  
ANISOU 6675  O   ILE A 815     6319  12401   4636   2013    -32   -249       O  
ATOM   6676  CB  ILE A 815     -15.451 -16.417  -8.038  1.00 55.52           C  
ANISOU 6676  CB  ILE A 815     5897  10911   4287   1779      0    -24       C  
ATOM   6677  CG1 ILE A 815     -14.948 -15.093  -8.628  1.00 53.85           C  
ANISOU 6677  CG1 ILE A 815     5727  10537   4197   1758    -45   -301       C  
ATOM   6678  CG2 ILE A 815     -15.819 -17.446  -9.115  1.00 55.45           C  
ANISOU 6678  CG2 ILE A 815     6019  10638   4412   1676     33    201       C  
ATOM   6679  CD1 ILE A 815     -13.481 -15.102  -9.025  1.00 52.20           C  
ANISOU 6679  CD1 ILE A 815     5567  10209   4057   1733    -69   -366       C  
ATOM   6680  N   LYS A 816     -16.864 -14.093  -5.812  1.00 64.14           N  
ANISOU 6680  N   LYS A 816     6669  12616   5084   1988    -45   -477       N  
ATOM   6681  CA  LYS A 816     -16.525 -13.078  -4.813  1.00 68.37           C  
ANISOU 6681  CA  LYS A 816     7069  13402   5506   2094    -88   -742       C  
ATOM   6682  C   LYS A 816     -16.363 -13.688  -3.419  1.00 70.89           C  
ANISOU 6682  C   LYS A 816     7229  14131   5575   2191    -71   -651       C  
ATOM   6683  O   LYS A 816     -17.206 -14.470  -2.969  1.00 70.69           O  
ANISOU 6683  O   LYS A 816     7151  14281   5429   2199    -25   -441       O  
ATOM   6684  CB  LYS A 816     -17.588 -11.971  -4.796  1.00 69.61           C  
ANISOU 6684  CB  LYS A 816     7184  13576   5688   2130   -111   -944       C  
ATOM   6685  CG  LYS A 816     -17.353 -10.857  -3.773  1.00 74.85           C  
ANISOU 6685  CG  LYS A 816     7701  14490   6247   2245   -162  -1249       C  
ATOM   6686  CD  LYS A 816     -18.574  -9.947  -3.671  1.00 78.64           C  
ANISOU 6686  CD  LYS A 816     8127  15019   6733   2300   -183  -1418       C  
ATOM   6687  CE  LYS A 816     -18.642  -9.214  -2.333  1.00 83.23           C  
ANISOU 6687  CE  LYS A 816     8512  15978   7133   2439   -217  -1662       C  
ATOM   6688  NZ  LYS A 816     -17.669  -8.088  -2.226  1.00 85.69           N  
ANISOU 6688  NZ  LYS A 816     8816  16215   7529   2469   -285  -1976       N  
ATOM   6689  N   GLY A 817     -15.260 -13.336  -2.762  1.00 72.87           N  
ANISOU 6689  N   GLY A 817     7403  14535   5748   2257   -107   -804       N  
ATOM   6690  CA  GLY A 817     -14.980 -13.796  -1.406  1.00 77.37           C  
ANISOU 6690  CA  GLY A 817     7811  15518   6067   2364   -100   -746       C  
ATOM   6691  C   GLY A 817     -14.300 -15.152  -1.339  1.00 78.71           C  
ANISOU 6691  C   GLY A 817     8020  15701   6186   2351    -72   -452       C  
ATOM   6692  O   GLY A 817     -14.171 -15.728  -0.256  1.00 80.97           O  
ANISOU 6692  O   GLY A 817     8185  16324   6258   2436    -60   -334       O  
ATOM   6693  N   ASN A 818     -13.878 -15.664  -2.495  1.00 77.90           N  
ANISOU 6693  N   ASN A 818     8085  15239   6276   2252    -64   -333       N  
ATOM   6694  CA  ASN A 818     -13.133 -16.923  -2.570  1.00 79.15           C  
ANISOU 6694  CA  ASN A 818     8297  15354   6422   2245    -49    -79       C  
ATOM   6695  C   ASN A 818     -11.748 -16.709  -3.166  1.00 78.21           C  
ANISOU 6695  C   ASN A 818     8245  15048   6422   2225    -87   -207       C  
ATOM   6696  O   ASN A 818     -11.612 -16.389  -4.350  1.00 76.17           O  
ANISOU 6696  O   ASN A 818     8117  14455   6370   2128    -92   -276       O  
ATOM   6697  CB  ASN A 818     -13.899 -17.986  -3.368  1.00 78.58           C  
ANISOU 6697  CB  ASN A 818     8351  15046   6458   2149     -1    214       C  
ATOM   6698  CG  ASN A 818     -15.246 -18.333  -2.748  1.00 82.62           C  
ANISOU 6698  CG  ASN A 818     8787  15764   6842   2155     44    371       C  
ATOM   6699  OD1 ASN A 818     -15.344 -18.616  -1.550  1.00 83.75           O  
ANISOU 6699  OD1 ASN A 818     8793  16262   6766   2241     54    450       O  
ATOM   6700  ND2 ASN A 818     -16.293 -18.321  -3.570  1.00 82.74           N  
ANISOU 6700  ND2 ASN A 818     8883  15569   6984   2061     71    418       N  
ATOM   6701  N   ILE A 819     -10.726 -16.884  -2.332  1.00 79.43           N  
ANISOU 6701  N   ILE A 819     8302  15441   6437   2319   -113   -237       N  
ATOM   6702  CA  ILE A 819      -9.332 -16.670  -2.737  1.00 80.01           C  
ANISOU 6702  CA  ILE A 819     8407  15403   6591   2312   -151   -376       C  
ATOM   6703  C   ILE A 819      -8.812 -17.697  -3.750  1.00 77.69           C  
ANISOU 6703  C   ILE A 819     8260  14815   6443   2246   -138   -173       C  
ATOM   6704  O   ILE A 819      -7.950 -17.380  -4.569  1.00 76.89           O  
ANISOU 6704  O   ILE A 819     8227  14507   6481   2189   -158   -300       O  
ATOM   6705  CB  ILE A 819      -8.375 -16.593  -1.509  1.00 83.01           C  
ANISOU 6705  CB  ILE A 819     8623  16154   6763   2441   -186   -474       C  
ATOM   6706  CG1 ILE A 819      -8.843 -17.509  -0.365  1.00 85.10           C  
ANISOU 6706  CG1 ILE A 819     8786  16750   6796   2544   -163   -228       C  
ATOM   6707  CG2 ILE A 819      -8.270 -15.160  -1.007  1.00 84.76           C  
ANISOU 6707  CG2 ILE A 819     8730  16531   6944   2471   -223   -831       C  
ATOM   6708  CD1 ILE A 819      -8.329 -18.938  -0.434  1.00 85.75           C  
ANISOU 6708  CD1 ILE A 819     8931  16786   6863   2570   -153     85       C  
ATOM   6709  N   ASP A 820      -9.362 -18.909  -3.698  1.00 77.22           N  
ANISOU 6709  N   ASP A 820     8244  14741   6355   2249   -103    135       N  
ATOM   6710  CA  ASP A 820      -8.903 -20.039  -4.518  1.00 75.02           C  
ANISOU 6710  CA  ASP A 820     8093  14211   6201   2208    -96    343       C  
ATOM   6711  C   ASP A 820      -9.356 -20.024  -5.985  1.00 70.50           C  
ANISOU 6711  C   ASP A 820     7679  13244   5863   2070    -76    353       C  
ATOM   6712  O   ASP A 820      -8.699 -20.622  -6.840  1.00 69.37           O  
ANISOU 6712  O   ASP A 820     7636  12875   5849   2032    -82    415       O  
ATOM   6713  CB  ASP A 820      -9.278 -21.377  -3.856  1.00 78.19           C  
ANISOU 6713  CB  ASP A 820     8482  14737   6489   2265    -72    676       C  
ATOM   6714  CG  ASP A 820     -10.576 -21.301  -3.052  1.00 83.69           C  
ANISOU 6714  CG  ASP A 820     9097  15653   7048   2275    -36    769       C  
ATOM   6715  OD1 ASP A 820     -11.592 -20.782  -3.573  1.00 84.46           O  
ANISOU 6715  OD1 ASP A 820     9233  15625   7232   2189    -11    708       O  
ATOM   6716  OD2 ASP A 820     -10.577 -21.770  -1.890  1.00 87.34           O  
ANISOU 6716  OD2 ASP A 820     9450  16429   7307   2372    -34    906       O  
ATOM   6717  N   ALA A 821     -10.472 -19.352  -6.270  1.00 65.95           N  
ANISOU 6717  N   ALA A 821     7121  12603   5336   2006    -55    286       N  
ATOM   6718  CA  ALA A 821     -11.027 -19.307  -7.621  1.00 60.32           C  
ANISOU 6718  CA  ALA A 821     6548  11546   4826   1881    -36    301       C  
ATOM   6719  C   ALA A 821     -10.167 -18.452  -8.547  1.00 56.88           C  
ANISOU 6719  C   ALA A 821     6171  10908   4531   1822    -65     74       C  
ATOM   6720  O   ALA A 821      -9.735 -17.369  -8.153  1.00 56.89           O  
ANISOU 6720  O   ALA A 821     6101  11023   4493   1849    -94   -162       O  
ATOM   6721  CB  ALA A 821     -12.449 -18.782  -7.592  1.00 60.33           C  
ANISOU 6721  CB  ALA A 821     6535  11565   4822   1846    -12    284       C  
ATOM   6722  N   PRO A 822      -9.907 -18.945  -9.775  1.00 53.26           N  
ANISOU 6722  N   PRO A 822     5840  10157   4238   1736    -57    144       N  
ATOM   6723  CA  PRO A 822      -9.155 -18.195 -10.779  1.00 51.62           C  
ANISOU 6723  CA  PRO A 822     5695   9749   4167   1660    -77    -43       C  
ATOM   6724  C   PRO A 822      -9.767 -16.828 -11.052  1.00 51.17           C  
ANISOU 6724  C   PRO A 822     5645   9630   4166   1607    -85   -239       C  
ATOM   6725  O   PRO A 822     -10.944 -16.735 -11.396  1.00 50.33           O  
ANISOU 6725  O   PRO A 822     5583   9435   4107   1567    -65   -180       O  
ATOM   6726  CB  PRO A 822      -9.272 -19.068 -12.031  1.00 48.42           C  
ANISOU 6726  CB  PRO A 822     5422   9062   3913   1575    -56    109       C  
ATOM   6727  CG  PRO A 822      -9.472 -20.429 -11.532  1.00 49.65           C  
ANISOU 6727  CG  PRO A 822     5572   9286   4007   1633    -41    356       C  
ATOM   6728  CD  PRO A 822     -10.238 -20.304 -10.245  1.00 53.07           C  
ANISOU 6728  CD  PRO A 822     5900   9990   4275   1708    -31    405       C  
ATOM   6729  N   GLN A 823      -8.971 -15.779 -10.880  1.00 52.06           N  
ANISOU 6729  N   GLN A 823     5709   9792   4278   1608   -117   -473       N  
ATOM   6730  CA  GLN A 823      -9.382 -14.435 -11.253  1.00 53.35           C  
ANISOU 6730  CA  GLN A 823     5896   9849   4528   1553   -134   -671       C  
ATOM   6731  C   GLN A 823      -9.241 -14.251 -12.762  1.00 52.18           C  
ANISOU 6731  C   GLN A 823     5884   9378   4564   1425   -127   -670       C  
ATOM   6732  O   GLN A 823      -8.342 -14.827 -13.384  1.00 52.19           O  
ANISOU 6732  O   GLN A 823     5928   9286   4615   1383   -122   -620       O  
ATOM   6733  CB  GLN A 823      -8.537 -13.390 -10.524  1.00 55.65           C  
ANISOU 6733  CB  GLN A 823     6086  10294   4764   1590   -173   -925       C  
ATOM   6734  CG  GLN A 823      -8.719 -13.370  -9.006  1.00 61.88           C  
ANISOU 6734  CG  GLN A 823     6723  11432   5358   1721   -185   -968       C  
ATOM   6735  CD  GLN A 823     -10.028 -12.732  -8.562  1.00 64.55           C  
ANISOU 6735  CD  GLN A 823     7025  11840   5662   1758   -186  -1022       C  
ATOM   6736  OE1 GLN A 823     -10.784 -13.320  -7.786  1.00 67.93           O  
ANISOU 6736  OE1 GLN A 823     7386  12470   5954   1834   -165   -891       O  
ATOM   6737  NE2 GLN A 823     -10.297 -11.522  -9.044  1.00 64.17           N  
ANISOU 6737  NE2 GLN A 823     7018  11631   5735   1706   -212  -1215       N  
ATOM   6738  N   VAL A 824     -10.147 -13.463 -13.342  1.00 50.22           N  
ANISOU 6738  N   VAL A 824     5698   8976   4409   1372   -130   -725       N  
ATOM   6739  CA  VAL A 824     -10.057 -13.052 -14.738  1.00 47.63           C  
ANISOU 6739  CA  VAL A 824     5490   8361   4245   1252   -129   -746       C  
ATOM   6740  C   VAL A 824      -9.027 -11.927 -14.853  1.00 48.09           C  
ANISOU 6740  C   VAL A 824     5537   8377   4359   1203   -161   -966       C  
ATOM   6741  O   VAL A 824      -9.154 -10.896 -14.192  1.00 49.46           O  
ANISOU 6741  O   VAL A 824     5652   8628   4513   1237   -192  -1142       O  
ATOM   6742  CB  VAL A 824     -11.430 -12.568 -15.283  1.00 46.20           C  
ANISOU 6742  CB  VAL A 824     5375   8040   4138   1225   -127   -723       C  
ATOM   6743  CG1 VAL A 824     -11.293 -12.004 -16.703  1.00 43.55           C  
ANISOU 6743  CG1 VAL A 824     5160   7424   3962   1106   -132   -753       C  
ATOM   6744  CG2 VAL A 824     -12.445 -13.698 -15.261  1.00 44.54           C  
ANISOU 6744  CG2 VAL A 824     5176   7864   3885   1251    -91   -507       C  
ATOM   6745  N   VAL A 825      -8.015 -12.136 -15.692  1.00 46.93           N  
ANISOU 6745  N   VAL A 825     5438   8111   4281   1119   -154   -962       N  
ATOM   6746  CA  VAL A 825      -6.947 -11.154 -15.880  1.00 47.87           C  
ANISOU 6746  CA  VAL A 825     5544   8188   4457   1047   -178  -1155       C  
ATOM   6747  C   VAL A 825      -7.272 -10.171 -17.005  1.00 46.97           C  
ANISOU 6747  C   VAL A 825     5539   7811   4496    929   -186  -1206       C  
ATOM   6748  O   VAL A 825      -7.616 -10.578 -18.116  1.00 46.11           O  
ANISOU 6748  O   VAL A 825     5529   7528   4463    861   -163  -1074       O  
ATOM   6749  CB  VAL A 825      -5.577 -11.831 -16.155  1.00 47.95           C  
ANISOU 6749  CB  VAL A 825     5530   8240   4448   1017   -168  -1140       C  
ATOM   6750  CG1 VAL A 825      -4.463 -10.788 -16.206  1.00 48.41           C  
ANISOU 6750  CG1 VAL A 825     5551   8293   4550    938   -191  -1352       C  
ATOM   6751  CG2 VAL A 825      -5.264 -12.883 -15.090  1.00 49.42           C  
ANISOU 6751  CG2 VAL A 825     5619   8674   4485   1146   -165  -1061       C  
ATOM   6752  N   GLU A 826      -7.157  -8.880 -16.701  1.00 47.91           N  
ANISOU 6752  N   GLU A 826     5637   7905   4661    907   -221  -1400       N  
ATOM   6753  CA  GLU A 826      -7.376  -7.808 -17.672  1.00 47.70           C  
ANISOU 6753  CA  GLU A 826     5712   7625   4786    797   -237  -1457       C  
ATOM   6754  C   GLU A 826      -6.555  -8.019 -18.949  1.00 46.22           C  
ANISOU 6754  C   GLU A 826     5601   7280   4679    658   -212  -1389       C  
ATOM   6755  O   GLU A 826      -5.331  -8.131 -18.904  1.00 46.19           O  
ANISOU 6755  O   GLU A 826     5547   7350   4654    611   -206  -1454       O  
ATOM   6756  CB  GLU A 826      -7.054  -6.449 -17.036  1.00 49.52           C  
ANISOU 6756  CB  GLU A 826     5895   7863   5058    789   -284  -1697       C  
ATOM   6757  CG  GLU A 826      -6.920  -5.273 -18.007  1.00 52.48           C  
ANISOU 6757  CG  GLU A 826     6372   7967   5601    655   -306  -1769       C  
ATOM   6758  CD  GLU A 826      -8.249  -4.826 -18.617  1.00 54.90           C  
ANISOU 6758  CD  GLU A 826     6783   8081   5994    667   -321  -1695       C  
ATOM   6759  OE1 GLU A 826      -8.221  -4.277 -19.740  1.00 55.92           O  
ANISOU 6759  OE1 GLU A 826     7023   7975   6249    552   -324  -1654       O  
ATOM   6760  OE2 GLU A 826      -9.313  -5.015 -17.985  1.00 54.55           O  
ANISOU 6760  OE2 GLU A 826     6707   8132   5888    791   -330  -1676       O  
ATOM   6761  N   GLY A 827      -7.245  -8.081 -20.083  1.00 43.92           N  
ANISOU 6761  N   GLY A 827     5423   6793   4470    598   -198  -1262       N  
ATOM   6762  CA  GLY A 827      -6.588  -8.223 -21.374  1.00 42.90           C  
ANISOU 6762  CA  GLY A 827     5366   6522   4411    465   -174  -1195       C  
ATOM   6763  C   GLY A 827      -6.358  -9.653 -21.828  1.00 42.50           C  
ANISOU 6763  C   GLY A 827     5315   6527   4306    478   -135  -1041       C  
ATOM   6764  O   GLY A 827      -5.861  -9.873 -22.930  1.00 42.37           O  
ANISOU 6764  O   GLY A 827     5350   6414   4336    379   -114   -986       O  
ATOM   6765  N   GLU A 828      -6.710 -10.627 -20.989  1.00 42.40           N  
ANISOU 6765  N   GLU A 828     5244   6671   4196    600   -127   -971       N  
ATOM   6766  CA  GLU A 828      -6.553 -12.035 -21.359  1.00 41.83           C  
ANISOU 6766  CA  GLU A 828     5176   6631   4086    623    -97   -823       C  
ATOM   6767  C   GLU A 828      -7.843 -12.643 -21.926  1.00 38.09           C  
ANISOU 6767  C   GLU A 828     4777   6056   3641    639    -81   -662       C  
ATOM   6768  O   GLU A 828      -8.876 -11.987 -21.972  1.00 37.03           O  
ANISOU 6768  O   GLU A 828     4682   5847   3542    643    -93   -664       O  
ATOM   6769  CB  GLU A 828      -5.951 -12.854 -20.205  1.00 45.19           C  
ANISOU 6769  CB  GLU A 828     5497   7279   4395    734    -99   -824       C  
ATOM   6770  CG  GLU A 828      -4.406 -12.759 -20.175  1.00 56.82           C  
ANISOU 6770  CG  GLU A 828     6906   8837   5846    696   -104   -939       C  
ATOM   6771  CD  GLU A 828      -3.728 -13.655 -19.133  1.00 65.64           C  
ANISOU 6771  CD  GLU A 828     7919  10177   6844    816   -110   -929       C  
ATOM   6772  OE1 GLU A 828      -2.637 -13.270 -18.651  1.00 68.98           O  
ANISOU 6772  OE1 GLU A 828     8258  10729   7223    815   -125  -1070       O  
ATOM   6773  OE2 GLU A 828      -4.267 -14.737 -18.799  1.00 68.37           O  
ANISOU 6773  OE2 GLU A 828     8266  10570   7140    908   -101   -778       O  
ATOM   6774  N   LYS A 829      -7.772 -13.886 -22.386  1.00 36.25           N  
ANISOU 6774  N   LYS A 829     4560   5816   3400    647    -57   -534       N  
ATOM   6775  CA  LYS A 829      -8.913 -14.523 -23.041  1.00 35.15           C  
ANISOU 6775  CA  LYS A 829     4486   5573   3297    643    -41   -391       C  
ATOM   6776  C   LYS A 829      -9.888 -15.147 -22.047  1.00 33.24           C  
ANISOU 6776  C   LYS A 829     4205   5437   2988    747    -37   -300       C  
ATOM   6777  O   LYS A 829      -9.493 -15.633 -20.984  1.00 30.79           O  
ANISOU 6777  O   LYS A 829     3819   5287   2592    830    -40   -293       O  
ATOM   6778  CB  LYS A 829      -8.438 -15.573 -24.053  1.00 36.41           C  
ANISOU 6778  CB  LYS A 829     4681   5663   3492    598    -20   -307       C  
ATOM   6779  CG  LYS A 829      -7.563 -15.023 -25.186  1.00 38.26           C  
ANISOU 6779  CG  LYS A 829     4949   5805   3781    484    -17   -379       C  
ATOM   6780  CD  LYS A 829      -8.379 -14.607 -26.406  1.00 38.49           C  
ANISOU 6780  CD  LYS A 829     5068   5672   3885    399    -11   -332       C  
ATOM   6781  CE  LYS A 829      -7.483 -13.964 -27.458  1.00 38.33           C  
ANISOU 6781  CE  LYS A 829     5074   5583   3905    278     -6   -394       C  
ATOM   6782  NZ  LYS A 829      -7.958 -14.266 -28.832  1.00 42.48           N  
ANISOU 6782  NZ  LYS A 829     5668   5996   4476    210      8   -312       N  
ATOM   6783  N   VAL A 830     -11.167 -15.119 -22.403  1.00 31.71           N  
ANISOU 6783  N   VAL A 830     4057   5165   2827    739    -32   -227       N  
ATOM   6784  CA  VAL A 830     -12.207 -15.758 -21.604  1.00 30.08           C  
ANISOU 6784  CA  VAL A 830     3813   5055   2560    816    -21   -124       C  
ATOM   6785  C   VAL A 830     -13.141 -16.579 -22.478  1.00 29.43           C  
ANISOU 6785  C   VAL A 830     3789   4859   2533    776      0     14       C  
ATOM   6786  O   VAL A 830     -13.432 -16.199 -23.614  1.00 28.63           O  
ANISOU 6786  O   VAL A 830     3757   4612   2508    703     -2      3       O  
ATOM   6787  CB  VAL A 830     -13.045 -14.739 -20.793  1.00 29.96           C  
ANISOU 6787  CB  VAL A 830     3758   5123   2504    871    -40   -205       C  
ATOM   6788  CG1 VAL A 830     -12.291 -14.283 -19.560  1.00 25.81           C  
ANISOU 6788  CG1 VAL A 830     3142   4774   1892    941    -58   -322       C  
ATOM   6789  CG2 VAL A 830     -13.462 -13.549 -21.664  1.00 31.33           C  
ANISOU 6789  CG2 VAL A 830     4001   5138   2766    811    -61   -290       C  
ATOM   6790  N   TYR A 831     -13.584 -17.715 -21.944  1.00 29.38           N  
ANISOU 6790  N   TYR A 831     3753   4924   2486    820     19    145       N  
ATOM   6791  CA  TYR A 831     -14.704 -18.458 -22.511  1.00 27.84           C  
ANISOU 6791  CA  TYR A 831     3593   4650   2334    787     38    271       C  
ATOM   6792  C   TYR A 831     -16.008 -17.796 -22.070  1.00 27.50           C  
ANISOU 6792  C   TYR A 831     3523   4670   2255    813     37    262       C  
ATOM   6793  O   TYR A 831     -16.093 -17.291 -20.950  1.00 27.35           O  
ANISOU 6793  O   TYR A 831     3435   4805   2151    884     29    211       O  
ATOM   6794  CB  TYR A 831     -14.693 -19.902 -22.024  1.00 28.39           C  
ANISOU 6794  CB  TYR A 831     3640   4766   2382    817     58    419       C  
ATOM   6795  CG  TYR A 831     -13.625 -20.798 -22.626  1.00 28.36           C  
ANISOU 6795  CG  TYR A 831     3669   4674   2433    798     56    445       C  
ATOM   6796  CD1 TYR A 831     -13.435 -20.865 -24.004  1.00 25.19           C  
ANISOU 6796  CD1 TYR A 831     3334   4114   2125    720     55    413       C  
ATOM   6797  CD2 TYR A 831     -12.838 -21.617 -21.807  1.00 29.24           C  
ANISOU 6797  CD2 TYR A 831     3740   4873   2496    867     53    504       C  
ATOM   6798  CE1 TYR A 831     -12.473 -21.695 -24.557  1.00 28.74           C  
ANISOU 6798  CE1 TYR A 831     3803   4498   2621    712     52    420       C  
ATOM   6799  CE2 TYR A 831     -11.872 -22.456 -22.346  1.00 32.27           C  
ANISOU 6799  CE2 TYR A 831     4150   5178   2933    866     45    518       C  
ATOM   6800  CZ  TYR A 831     -11.690 -22.491 -23.727  1.00 34.16           C  
ANISOU 6800  CZ  TYR A 831     4449   5262   3268    788     45    467       C  
ATOM   6801  OH  TYR A 831     -10.736 -23.326 -24.281  1.00 34.69           O  
ANISOU 6801  OH  TYR A 831     4532   5264   3385    794     35    463       O  
ATOM   6802  N   VAL A 832     -17.014 -17.807 -22.945  1.00 26.81           N  
ANISOU 6802  N   VAL A 832     3480   4480   2226    763     42    302       N  
ATOM   6803  CA  VAL A 832     -18.298 -17.145 -22.694  1.00 26.01           C  
ANISOU 6803  CA  VAL A 832     3353   4431   2098    790     36    283       C  
ATOM   6804  C   VAL A 832     -19.467 -18.093 -22.996  1.00 27.87           C  
ANISOU 6804  C   VAL A 832     3584   4657   2348    757     63    417       C  
ATOM   6805  O   VAL A 832     -19.527 -18.701 -24.072  1.00 26.40           O  
ANISOU 6805  O   VAL A 832     3455   4336   2239    686     71    469       O  
ATOM   6806  CB  VAL A 832     -18.478 -15.862 -23.580  1.00 27.17           C  
ANISOU 6806  CB  VAL A 832     3559   4457   2308    763      5    170       C  
ATOM   6807  CG1 VAL A 832     -19.818 -15.203 -23.299  1.00 26.27           C  
ANISOU 6807  CG1 VAL A 832     3413   4401   2167    811     -8    143       C  
ATOM   6808  CG2 VAL A 832     -17.343 -14.847 -23.366  1.00 24.59           C  
ANISOU 6808  CG2 VAL A 832     3242   4116   1987    774    -22     33       C  
ATOM   6809  N   LEU A 833     -20.403 -18.204 -22.055  1.00 28.55           N  
ANISOU 6809  N   LEU A 833     3595   4897   2356    803     76    462       N  
ATOM   6810  CA  LEU A 833     -21.616 -18.997 -22.278  1.00 29.43           C  
ANISOU 6810  CA  LEU A 833     3689   5017   2477    762    103    579       C  
ATOM   6811  C   LEU A 833     -22.900 -18.214 -21.999  1.00 31.01           C  
ANISOU 6811  C   LEU A 833     3834   5322   2628    801     96    530       C  
ATOM   6812  O   LEU A 833     -22.989 -17.490 -21.001  1.00 33.46           O  
ANISOU 6812  O   LEU A 833     4077   5785   2851    882     84    455       O  
ATOM   6813  CB  LEU A 833     -21.600 -20.296 -21.448  1.00 26.11           C  
ANISOU 6813  CB  LEU A 833     3220   4689   2011    758    138    735       C  
ATOM   6814  CG  LEU A 833     -20.786 -21.477 -21.992  1.00 27.30           C  
ANISOU 6814  CG  LEU A 833     3431   4700   2242    706    147    826       C  
ATOM   6815  CD1 LEU A 833     -20.734 -22.618 -20.983  1.00 25.01           C  
ANISOU 6815  CD1 LEU A 833     3095   4507   1902    721    173    985       C  
ATOM   6816  CD2 LEU A 833     -21.350 -21.970 -23.332  1.00 27.28           C  
ANISOU 6816  CD2 LEU A 833     3487   4527   2350    615    152    854       C  
ATOM   6817  N   PRO A 834     -23.908 -18.377 -22.873  1.00 32.19           N  
ANISOU 6817  N   PRO A 834     4002   5402   2828    749    100    562       N  
ATOM   6818  CA  PRO A 834     -25.231 -17.826 -22.577  1.00 32.92           C  
ANISOU 6818  CA  PRO A 834     4026   5616   2865    790     95    529       C  
ATOM   6819  C   PRO A 834     -25.906 -18.585 -21.441  1.00 34.71           C  
ANISOU 6819  C   PRO A 834     4147   6047   2994    799    136    635       C  
ATOM   6820  O   PRO A 834     -25.707 -19.800 -21.293  1.00 34.90           O  
ANISOU 6820  O   PRO A 834     4170   6060   3029    738    171    776       O  
ATOM   6821  CB  PRO A 834     -26.002 -18.018 -23.888  1.00 32.74           C  
ANISOU 6821  CB  PRO A 834     4049   5467   2924    721     92    552       C  
ATOM   6822  CG  PRO A 834     -25.280 -19.132 -24.611  1.00 31.82           C  
ANISOU 6822  CG  PRO A 834     3997   5204   2887    631    112    641       C  
ATOM   6823  CD  PRO A 834     -23.843 -19.012 -24.208  1.00 30.99           C  
ANISOU 6823  CD  PRO A 834     3927   5069   2780    659    104    609       C  
ATOM   6824  N   LEU A 835     -26.690 -17.859 -20.646  1.00 34.86           N  
ANISOU 6824  N   LEU A 835     4076   6251   2920    876    129    567       N  
ATOM   6825  CA  LEU A 835     -27.402 -18.421 -19.504  1.00 36.22           C  
ANISOU 6825  CA  LEU A 835     4129   6659   2974    890    168    657       C  
ATOM   6826  C   LEU A 835     -28.914 -18.263 -19.655  1.00 37.20           C  
ANISOU 6826  C   LEU A 835     4179   6889   3067    885    176    650       C  
ATOM   6827  O   LEU A 835     -29.401 -17.174 -19.989  1.00 37.01           O  
ANISOU 6827  O   LEU A 835     4153   6860   3050    951    135    508       O  
ATOM   6828  CB  LEU A 835     -26.914 -17.756 -18.208  1.00 37.69           C  
ANISOU 6828  CB  LEU A 835     4241   7038   3043    998    156    572       C  
ATOM   6829  CG  LEU A 835     -25.973 -18.491 -17.236  1.00 38.01           C  
ANISOU 6829  CG  LEU A 835     4254   7176   3013   1005    181    670       C  
ATOM   6830  CD1 LEU A 835     -25.130 -19.599 -17.871  1.00 35.86           C  
ANISOU 6830  CD1 LEU A 835     4079   6708   2840    919    197    804       C  
ATOM   6831  CD2 LEU A 835     -25.092 -17.506 -16.477  1.00 38.39           C  
ANISOU 6831  CD2 LEU A 835     4275   7312   2998   1111    145    514       C  
ATOM   6832  N   ARG A 836     -29.645 -19.354 -19.417  1.00 37.85           N  
ANISOU 6832  N   ARG A 836     4200   7062   3118    805    226    804       N  
ATOM   6833  CA  ARG A 836     -31.114 -19.355 -19.498  1.00 39.23           C  
ANISOU 6833  CA  ARG A 836     4285   7367   3252    785    242    810       C  
ATOM   6834  C   ARG A 836     -31.738 -18.442 -18.450  1.00 40.78           C  
ANISOU 6834  C   ARG A 836     4354   7831   3307    902    232    701       C  
ATOM   6835  O   ARG A 836     -31.198 -18.285 -17.354  1.00 39.22           O  
ANISOU 6835  O   ARG A 836     4106   7783   3012    966    238    691       O  
ATOM   6836  CB  ARG A 836     -31.685 -20.761 -19.317  1.00 39.39           C  
ANISOU 6836  CB  ARG A 836     4258   7443   3267    661    303   1007       C  
ATOM   6837  CG  ARG A 836     -31.346 -21.735 -20.416  1.00 38.28           C  
ANISOU 6837  CG  ARG A 836     4223   7047   3273    542    311   1099       C  
ATOM   6838  CD  ARG A 836     -32.357 -22.862 -20.478  1.00 40.29           C  
ANISOU 6838  CD  ARG A 836     4417   7350   3542    414    360   1245       C  
ATOM   6839  NE  ARG A 836     -32.544 -23.531 -19.190  1.00 43.46           N  
ANISOU 6839  NE  ARG A 836     4725   7954   3836    390    410   1395       N  
ATOM   6840  CZ  ARG A 836     -31.780 -24.523 -18.751  1.00 44.20           C  
ANISOU 6840  CZ  ARG A 836     4858   7982   3953    342    435   1553       C  
ATOM   6841  NH1 ARG A 836     -30.766 -24.958 -19.488  1.00 43.96           N  
ANISOU 6841  NH1 ARG A 836     4955   7693   4053    318    412   1563       N  
ATOM   6842  NH2 ARG A 836     -32.025 -25.078 -17.575  1.00 42.51           N  
ANISOU 6842  NH2 ARG A 836     4554   7969   3629    322    479   1702       N  
ATOM   6843  N   GLU A 837     -32.879 -17.855 -18.801  1.00 40.74           N  
ANISOU 6843  N   GLU A 837     4294   7898   3288    935    214    613       N  
ATOM   6844  CA  GLU A 837     -33.628 -16.974 -17.910  1.00 45.93           C  
ANISOU 6844  CA  GLU A 837     4820   8816   3816   1055    199    488       C  
ATOM   6845  C   GLU A 837     -33.966 -17.648 -16.569  1.00 46.89           C  
ANISOU 6845  C   GLU A 837     4798   9238   3781   1039    259    598       C  
ATOM   6846  O   GLU A 837     -34.417 -18.796 -16.537  1.00 46.84           O  
ANISOU 6846  O   GLU A 837     4756   9278   3764    916    317    778       O  
ATOM   6847  CB  GLU A 837     -34.905 -16.505 -18.613  1.00 47.22           C  
ANISOU 6847  CB  GLU A 837     4940   9006   3995   1076    175    408       C  
ATOM   6848  CG  GLU A 837     -35.603 -15.322 -17.954  1.00 57.93           C  
ANISOU 6848  CG  GLU A 837     6185  10575   5252   1233    135    224       C  
ATOM   6849  CD  GLU A 837     -36.427 -14.508 -18.944  1.00 62.01           C  
ANISOU 6849  CD  GLU A 837     6723  11003   5834   1294     78    102       C  
ATOM   6850  OE1 GLU A 837     -37.667 -14.456 -18.795  1.00 63.45           O  
ANISOU 6850  OE1 GLU A 837     6779  11390   5940   1322     85     70       O  
ATOM   6851  OE2 GLU A 837     -35.829 -13.930 -19.878  1.00 64.60           O  
ANISOU 6851  OE2 GLU A 837     7191  11067   6286   1314     26     43       O  
ATOM   6852  N   GLY A 838     -33.730 -16.929 -15.473  1.00 46.92           N  
ANISOU 6852  N   GLY A 838     4718   9445   3664   1160    243    490       N  
ATOM   6853  CA  GLY A 838     -34.091 -17.410 -14.137  1.00 50.20           C  
ANISOU 6853  CA  GLY A 838     4980  10194   3902   1164    296    577       C  
ATOM   6854  C   GLY A 838     -33.004 -18.220 -13.455  1.00 50.95           C  
ANISOU 6854  C   GLY A 838     5104  10294   3962   1122    329    730       C  
ATOM   6855  O   GLY A 838     -33.240 -18.840 -12.416  1.00 53.79           O  
ANISOU 6855  O   GLY A 838     5350  10910   4179   1101    380    858       O  
ATOM   6856  N   ASN A 839     -31.812 -18.210 -14.048  1.00 47.82           N  
ANISOU 6856  N   ASN A 839     4857   9623   3691   1113    299    720       N  
ATOM   6857  CA  ASN A 839     -30.630 -18.859 -13.487  1.00 45.62           C  
ANISOU 6857  CA  ASN A 839     4617   9325   3392   1096    316    835       C  
ATOM   6858  C   ASN A 839     -30.164 -18.157 -12.206  1.00 46.40           C  
ANISOU 6858  C   ASN A 839     4615   9679   3335   1228    300    722       C  
ATOM   6859  O   ASN A 839     -30.455 -16.976 -12.016  1.00 47.01           O  
ANISOU 6859  O   ASN A 839     4639   9848   3375   1339    257    507       O  
ATOM   6860  CB  ASN A 839     -29.507 -18.867 -14.530  1.00 41.67           C  
ANISOU 6860  CB  ASN A 839     4289   8480   3063   1065    281    811       C  
ATOM   6861  CG  ASN A 839     -29.011 -17.471 -14.860  1.00 38.44           C  
ANISOU 6861  CG  ASN A 839     3929   7973   2704   1168    215    571       C  
ATOM   6862  OD1 ASN A 839     -28.130 -16.942 -14.186  1.00 38.57           O  
ANISOU 6862  OD1 ASN A 839     3933   8053   2669   1249    190    476       O  
ATOM   6863  ND2 ASN A 839     -29.578 -16.868 -15.899  1.00 31.17           N  
ANISOU 6863  ND2 ASN A 839     3064   6896   1883   1163    183    475       N  
ATOM   6864  N   PRO A 840     -29.434 -18.877 -11.331  1.00 47.95           N  
ANISOU 6864  N   PRO A 840     4784   9992   3442   1222    329    861       N  
ATOM   6865  CA  PRO A 840     -28.979 -18.346 -10.040  1.00 49.23           C  
ANISOU 6865  CA  PRO A 840     4834  10436   3435   1343    318    770       C  
ATOM   6866  C   PRO A 840     -27.822 -17.340 -10.114  1.00 48.69           C  
ANISOU 6866  C   PRO A 840     4830  10250   3420   1439    253    555       C  
ATOM   6867  O   PRO A 840     -27.476 -16.722  -9.100  1.00 48.92           O  
ANISOU 6867  O   PRO A 840     4759  10510   3318   1549    234    428       O  
ATOM   6868  CB  PRO A 840     -28.527 -19.606  -9.296  1.00 50.62           C  
ANISOU 6868  CB  PRO A 840     4987  10722   3525   1288    368   1028       C  
ATOM   6869  CG  PRO A 840     -28.108 -20.534 -10.377  1.00 48.10           C  
ANISOU 6869  CG  PRO A 840     4826  10060   3390   1168    377   1181       C  
ATOM   6870  CD  PRO A 840     -29.107 -20.309 -11.464  1.00 47.37           C  
ANISOU 6870  CD  PRO A 840     4772   9812   3415   1103    374   1125       C  
ATOM   6871  N   PHE A 841     -27.235 -17.176 -11.295  1.00 46.94           N  
ANISOU 6871  N   PHE A 841     4764   9687   3385   1394    222    511       N  
ATOM   6872  CA  PHE A 841     -26.148 -16.212 -11.485  1.00 46.06           C  
ANISOU 6872  CA  PHE A 841     4719   9440   3341   1461    163    313       C  
ATOM   6873  C   PHE A 841     -26.694 -14.798 -11.675  1.00 46.94           C  
ANISOU 6873  C   PHE A 841     4808   9547   3481   1547    110     62       C  
ATOM   6874  O   PHE A 841     -25.945 -13.817 -11.612  1.00 46.58           O  
ANISOU 6874  O   PHE A 841     4788   9438   3473   1616     58   -131       O  
ATOM   6875  CB  PHE A 841     -25.254 -16.622 -12.659  1.00 42.27           C  
ANISOU 6875  CB  PHE A 841     4406   8616   3038   1373    154    375       C  
ATOM   6876  CG  PHE A 841     -24.584 -17.957 -12.470  1.00 41.44           C  
ANISOU 6876  CG  PHE A 841     4330   8492   2921   1309    193    597       C  
ATOM   6877  CD1 PHE A 841     -23.474 -18.083 -11.637  1.00 43.43           C  
ANISOU 6877  CD1 PHE A 841     4553   8855   3093   1367    185    598       C  
ATOM   6878  CD2 PHE A 841     -25.070 -19.090 -13.114  1.00 38.76           C  
ANISOU 6878  CD2 PHE A 841     4046   8026   2656   1197    232    800       C  
ATOM   6879  CE1 PHE A 841     -22.852 -19.322 -11.450  1.00 42.99           C  
ANISOU 6879  CE1 PHE A 841     4527   8778   3029   1324    213    808       C  
ATOM   6880  CE2 PHE A 841     -24.460 -20.331 -12.940  1.00 40.59           C  
ANISOU 6880  CE2 PHE A 841     4311   8218   2893   1146    261   1004       C  
ATOM   6881  CZ  PHE A 841     -23.346 -20.448 -12.105  1.00 41.86           C  
ANISOU 6881  CZ  PHE A 841     4447   8484   2972   1215    250   1014       C  
ATOM   6882  N   GLY A 842     -28.003 -14.712 -11.903  1.00 46.70           N  
ANISOU 6882  N   GLY A 842     4726   9581   3436   1543    121     66       N  
ATOM   6883  CA  GLY A 842     -28.704 -13.435 -12.001  1.00 49.61           C  
ANISOU 6883  CA  GLY A 842     5056   9975   3819   1642     69   -161       C  
ATOM   6884  C   GLY A 842     -28.385 -12.596 -13.227  1.00 50.16           C  
ANISOU 6884  C   GLY A 842     5274   9706   4078   1636     10   -283       C  
ATOM   6885  O   GLY A 842     -28.540 -11.373 -13.186  1.00 52.21           O  
ANISOU 6885  O   GLY A 842     5522   9948   4366   1737    -50   -498       O  
ATOM   6886  N   ASP A 843     -27.938 -13.240 -14.310  1.00 48.24           N  
ANISOU 6886  N   ASP A 843     5168   9196   3964   1520     26   -147       N  
ATOM   6887  CA  ASP A 843     -27.695 -12.551 -15.588  1.00 47.07           C  
ANISOU 6887  CA  ASP A 843     5161   8735   3987   1497    -22   -227       C  
ATOM   6888  C   ASP A 843     -27.750 -13.477 -16.810  1.00 46.12           C  
ANISOU 6888  C   ASP A 843     5149   8399   3974   1365      8    -51       C  
ATOM   6889  O   ASP A 843     -27.908 -14.692 -16.668  1.00 47.13           O  
ANISOU 6889  O   ASP A 843     5252   8594   4061   1287     64    130       O  
ATOM   6890  CB  ASP A 843     -26.368 -11.790 -15.563  1.00 46.18           C  
ANISOU 6890  CB  ASP A 843     5120   8488   3940   1524    -65   -360       C  
ATOM   6891  CG  ASP A 843     -26.472 -10.424 -16.217  1.00 47.07           C  
ANISOU 6891  CG  ASP A 843     5302   8415   4167   1578   -136   -545       C  
ATOM   6892  OD1 ASP A 843     -27.249 -10.269 -17.187  1.00 44.40           O  
ANISOU 6892  OD1 ASP A 843     5021   7941   3908   1557   -150   -519       O  
ATOM   6893  OD2 ASP A 843     -25.774  -9.499 -15.747  1.00 52.96           O  
ANISOU 6893  OD2 ASP A 843     6045   9152   4927   1642   -180   -717       O  
ATOM   6894  N   LYS A 844     -27.607 -12.898 -18.004  1.00 44.07           N  
ANISOU 6894  N   LYS A 844     5010   7883   3853   1341    -31   -107       N  
ATOM   6895  CA  LYS A 844     -27.797 -13.649 -19.251  1.00 41.97           C  
ANISOU 6895  CA  LYS A 844     4835   7430   3684   1228    -10     28       C  
ATOM   6896  C   LYS A 844     -26.559 -14.396 -19.778  1.00 38.86           C  
ANISOU 6896  C   LYS A 844     4540   6863   3363   1133     10    125       C  
ATOM   6897  O   LYS A 844     -26.657 -15.162 -20.741  1.00 34.37           O  
ANISOU 6897  O   LYS A 844     4035   6158   2867   1039     31    236       O  
ATOM   6898  CB  LYS A 844     -28.404 -12.759 -20.342  1.00 43.09           C  
ANISOU 6898  CB  LYS A 844     5043   7410   3920   1249    -60    -58       C  
ATOM   6899  CG  LYS A 844     -27.447 -11.743 -20.960  1.00 43.79           C  
ANISOU 6899  CG  LYS A 844     5247   7277   4114   1262   -113   -168       C  
ATOM   6900  CD  LYS A 844     -28.179 -10.901 -21.996  1.00 44.79           C  
ANISOU 6900  CD  LYS A 844     5436   7261   4323   1291   -164   -226       C  
ATOM   6901  CE  LYS A 844     -27.404  -9.638 -22.347  1.00 45.31           C  
ANISOU 6901  CE  LYS A 844     5596   7138   4482   1327   -226   -355       C  
ATOM   6902  NZ  LYS A 844     -27.996  -8.948 -23.534  1.00 42.11           N  
ANISOU 6902  NZ  LYS A 844     5274   6561   4166   1338   -274   -367       N  
ATOM   6903  N   CYS A 845     -25.405 -14.168 -19.154  1.00 38.25           N  
ANISOU 6903  N   CYS A 845     4467   6802   3264   1162      2     70       N  
ATOM   6904  CA  CYS A 845     -24.177 -14.860 -19.547  1.00 36.96           C  
ANISOU 6904  CA  CYS A 845     4381   6504   3157   1088     18    148       C  
ATOM   6905  C   CYS A 845     -23.145 -14.903 -18.437  1.00 36.75           C  
ANISOU 6905  C   CYS A 845     4305   6608   3052   1135     21    116       C  
ATOM   6906  O   CYS A 845     -23.199 -14.119 -17.493  1.00 37.67           O  
ANISOU 6906  O   CYS A 845     4342   6880   3088   1226     -1     -8       O  
ATOM   6907  CB  CYS A 845     -23.555 -14.227 -20.798  1.00 36.06           C  
ANISOU 6907  CB  CYS A 845     4391   6139   3172   1042    -16     80       C  
ATOM   6908  SG  CYS A 845     -23.146 -12.487 -20.604  1.00 38.49           S  
ANISOU 6908  SG  CYS A 845     4717   6400   3510   1122    -81   -139       S  
ATOM   6909  N   ILE A 846     -22.206 -15.834 -18.574  1.00 34.98           N  
ANISOU 6909  N   ILE A 846     4121   6322   2850   1080     45    221       N  
ATOM   6910  CA  ILE A 846     -21.089 -15.977 -17.659  1.00 33.38           C  
ANISOU 6910  CA  ILE A 846     3878   6226   2577   1122     45    203       C  
ATOM   6911  C   ILE A 846     -19.816 -16.253 -18.466  1.00 32.99           C  
ANISOU 6911  C   ILE A 846     3924   5987   2623   1061     39    209       C  
ATOM   6912  O   ILE A 846     -19.846 -16.982 -19.458  1.00 34.59           O  
ANISOU 6912  O   ILE A 846     4200   6031   2911    982     55    308       O  
ATOM   6913  CB  ILE A 846     -21.361 -17.081 -16.578  1.00 33.88           C  
ANISOU 6913  CB  ILE A 846     3851   6503   2520   1143     87    362       C  
ATOM   6914  CG1 ILE A 846     -20.368 -16.953 -15.410  1.00 34.33           C  
ANISOU 6914  CG1 ILE A 846     3837   6738   2469   1222     78    310       C  
ATOM   6915  CG2 ILE A 846     -21.395 -18.488 -17.212  1.00 29.23           C  
ANISOU 6915  CG2 ILE A 846     3320   5790   1996   1053    123    562       C  
ATOM   6916  CD1 ILE A 846     -20.665 -17.830 -14.202  1.00 35.16           C  
ANISOU 6916  CD1 ILE A 846     3839   7094   2428   1261    113    458       C  
ATOM   6917  N   ALA A 847     -18.714 -15.635 -18.051  1.00 33.65           N  
ANISOU 6917  N   ALA A 847     3997   6100   2690   1098     14     87       N  
ATOM   6918  CA  ALA A 847     -17.411 -15.833 -18.679  1.00 33.49           C  
ANISOU 6918  CA  ALA A 847     4043   5942   2738   1047      8     74       C  
ATOM   6919  C   ALA A 847     -16.389 -16.261 -17.629  1.00 34.62           C  
ANISOU 6919  C   ALA A 847     4119   6247   2789   1104     10     79       C  
ATOM   6920  O   ALA A 847     -16.496 -15.873 -16.469  1.00 35.20           O  
ANISOU 6920  O   ALA A 847     4097   6524   2751   1185      2     17       O  
ATOM   6921  CB  ALA A 847     -16.956 -14.549 -19.372  1.00 31.73           C  
ANISOU 6921  CB  ALA A 847     3880   5577   2601   1018    -29    -92       C  
ATOM   6922  N   TRP A 848     -15.410 -17.063 -18.041  1.00 33.75           N  
ANISOU 6922  N   TRP A 848     4048   6058   2716   1069     18    145       N  
ATOM   6923  CA  TRP A 848     -14.315 -17.488 -17.164  1.00 33.27           C  
ANISOU 6923  CA  TRP A 848     3928   6138   2573   1129     14    148       C  
ATOM   6924  C   TRP A 848     -12.995 -17.614 -17.947  1.00 32.38           C  
ANISOU 6924  C   TRP A 848     3871   5896   2537   1083      3    100       C  
ATOM   6925  O   TRP A 848     -13.030 -17.752 -19.163  1.00 32.37           O  
ANISOU 6925  O   TRP A 848     3955   5702   2644   1001      9    120       O  
ATOM   6926  CB  TRP A 848     -14.676 -18.796 -16.454  1.00 33.88           C  
ANISOU 6926  CB  TRP A 848     3966   6332   2576   1168     42    347       C  
ATOM   6927  CG  TRP A 848     -14.666 -20.033 -17.320  1.00 32.19           C  
ANISOU 6927  CG  TRP A 848     3829   5945   2455   1107     61    506       C  
ATOM   6928  CD1 TRP A 848     -13.681 -20.982 -17.378  1.00 30.18           C  
ANISOU 6928  CD1 TRP A 848     3593   5655   2219   1122     57    581       C  
ATOM   6929  CD2 TRP A 848     -15.692 -20.466 -18.227  1.00 30.05           C  
ANISOU 6929  CD2 TRP A 848     3620   5521   2275   1029     81    597       C  
ATOM   6930  NE1 TRP A 848     -14.027 -21.973 -18.271  1.00 27.83           N  
ANISOU 6930  NE1 TRP A 848     3369   5179   2026   1058     73    705       N  
ATOM   6931  CE2 TRP A 848     -15.254 -21.681 -18.805  1.00 27.48           C  
ANISOU 6931  CE2 TRP A 848     3351   5065   2027    995     89    716       C  
ATOM   6932  CE3 TRP A 848     -16.936 -19.946 -18.610  1.00 30.97           C  
ANISOU 6932  CE3 TRP A 848     3746   5605   2416    990     89    579       C  
ATOM   6933  CZ2 TRP A 848     -16.019 -22.384 -19.738  1.00 27.71           C  
ANISOU 6933  CZ2 TRP A 848     3441   4932   2156    916    106    810       C  
ATOM   6934  CZ3 TRP A 848     -17.692 -20.646 -19.545  1.00 27.86           C  
ANISOU 6934  CZ3 TRP A 848     3411   5062   2114    912    108    680       C  
ATOM   6935  CH2 TRP A 848     -17.229 -21.854 -20.095  1.00 26.75           C  
ANISOU 6935  CH2 TRP A 848     3322   4793   2049    872    117    791       C  
ATOM   6936  N   PRO A 849     -11.830 -17.548 -17.259  1.00 33.78           N  
ANISOU 6936  N   PRO A 849     3990   6197   2648   1135    -13     28       N  
ATOM   6937  CA  PRO A 849     -10.544 -17.619 -17.966  1.00 35.16           C  
ANISOU 6937  CA  PRO A 849     4199   6276   2883   1092    -23    -34       C  
ATOM   6938  C   PRO A 849     -10.448 -18.804 -18.927  1.00 36.22           C  
ANISOU 6938  C   PRO A 849     4406   6256   3099   1048     -6    104       C  
ATOM   6939  O   PRO A 849     -10.805 -19.926 -18.576  1.00 38.16           O  
ANISOU 6939  O   PRO A 849     4646   6532   3321   1088      7    263       O  
ATOM   6940  CB  PRO A 849      -9.527 -17.757 -16.832  1.00 34.68           C  
ANISOU 6940  CB  PRO A 849     4042   6425   2709   1183    -39    -80       C  
ATOM   6941  CG  PRO A 849     -10.149 -17.009 -15.708  1.00 34.85           C  
ANISOU 6941  CG  PRO A 849     3982   6629   2630   1248    -48   -150       C  
ATOM   6942  CD  PRO A 849     -11.639 -17.283 -15.819  1.00 35.76           C  
ANISOU 6942  CD  PRO A 849     4128   6701   2758   1236    -25    -24       C  
ATOM   6943  N   SER A 850      -9.985 -18.536 -20.142  1.00 35.23           N  
ANISOU 6943  N   SER A 850     4346   5968   3072    962     -8     40       N  
ATOM   6944  CA  SER A 850      -9.898 -19.562 -21.172  1.00 35.92           C  
ANISOU 6944  CA  SER A 850     4498   5909   3243    916      5    137       C  
ATOM   6945  C   SER A 850      -8.783 -20.577 -20.903  1.00 37.47           C  
ANISOU 6945  C   SER A 850     4663   6158   3414    976     -4    176       C  
ATOM   6946  O   SER A 850      -7.870 -20.322 -20.114  1.00 36.81           O  
ANISOU 6946  O   SER A 850     4511   6219   3254   1037    -20    101       O  
ATOM   6947  CB  SER A 850      -9.709 -18.917 -22.540  1.00 33.26           C  
ANISOU 6947  CB  SER A 850     4227   5413   2997    810      5     52       C  
ATOM   6948  OG  SER A 850      -8.413 -18.365 -22.657  1.00 33.93           O  
ANISOU 6948  OG  SER A 850     4286   5534   3074    790     -7    -79       O  
ATOM   6949  N   GLY A 851      -8.879 -21.726 -21.571  1.00 41.15           N  
ANISOU 6949  N   GLY A 851     5179   6506   3951    964      3    285       N  
ATOM   6950  CA  GLY A 851      -7.911 -22.820 -21.435  1.00 45.22           C  
ANISOU 6950  CA  GLY A 851     5677   7039   4466   1031    -12    333       C  
ATOM   6951  C   GLY A 851      -8.172 -23.708 -20.238  1.00 49.30           C  
ANISOU 6951  C   GLY A 851     6157   7660   4916   1133    -16    484       C  
ATOM   6952  O   GLY A 851      -7.515 -24.737 -20.059  1.00 52.59           O  
ANISOU 6952  O   GLY A 851     6568   8075   5339   1203    -33    556       O  
ATOM   6953  N   THR A 852      -9.141 -23.312 -19.419  1.00 50.86           N  
ANISOU 6953  N   THR A 852     6326   7952   5046   1144     -2    537       N  
ATOM   6954  CA  THR A 852      -9.399 -23.989 -18.155  1.00 51.82           C  
ANISOU 6954  CA  THR A 852     6397   8218   5074   1237     -2    683       C  
ATOM   6955  C   THR A 852     -10.833 -24.494 -18.077  1.00 53.07           C  
ANISOU 6955  C   THR A 852     6585   8324   5257   1197     26    844       C  
ATOM   6956  O   THR A 852     -11.747 -23.945 -18.713  1.00 49.83           O  
ANISOU 6956  O   THR A 852     6207   7829   4896   1114     44    805       O  
ATOM   6957  CB  THR A 852      -9.144 -23.063 -16.931  1.00 49.75           C  
ANISOU 6957  CB  THR A 852     6037   8200   4665   1306    -11    594       C  
ATOM   6958  OG1 THR A 852     -10.030 -21.947 -16.996  1.00 47.43           O  
ANISOU 6958  OG1 THR A 852     5739   7917   4364   1250      2    503       O  
ATOM   6959  CG2 THR A 852      -7.702 -22.550 -16.894  1.00 50.44           C  
ANISOU 6959  CG2 THR A 852     6080   8364   4720   1341    -39    427       C  
ATOM   6960  N   GLU A 853     -10.999 -25.566 -17.306  1.00 54.86           N  
ANISOU 6960  N   GLU A 853     6796   8603   5447   1256     28   1029       N  
ATOM   6961  CA  GLU A 853     -12.285 -25.934 -16.753  1.00 55.18           C  
ANISOU 6961  CA  GLU A 853     6823   8688   5454   1234     57   1190       C  
ATOM   6962  C   GLU A 853     -12.654 -24.816 -15.782  1.00 54.60           C  
ANISOU 6962  C   GLU A 853     6660   8849   5235   1271     65   1107       C  
ATOM   6963  O   GLU A 853     -11.794 -24.284 -15.061  1.00 53.22           O  
ANISOU 6963  O   GLU A 853     6420   8844   4959   1351     43   1010       O  
ATOM   6964  CB  GLU A 853     -12.191 -27.270 -15.999  1.00 57.74           C  
ANISOU 6964  CB  GLU A 853     7143   9040   5756   1296     54   1414       C  
ATOM   6965  CG  GLU A 853     -11.802 -28.483 -16.858  1.00 61.26           C  
ANISOU 6965  CG  GLU A 853     7675   9244   6356   1278     37   1496       C  
ATOM   6966  CD  GLU A 853     -12.986 -29.114 -17.593  1.00 63.70           C  
ANISOU 6966  CD  GLU A 853     8048   9364   6790   1165     64   1601       C  
ATOM   6967  OE1 GLU A 853     -14.104 -29.159 -17.029  1.00 63.48           O  
ANISOU 6967  OE1 GLU A 853     7991   9416   6711   1125     96   1720       O  
ATOM   6968  OE2 GLU A 853     -12.794 -29.582 -18.736  1.00 64.67           O  
ANISOU 6968  OE2 GLU A 853     8242   9272   7058   1116     52   1557       O  
ATOM   6969  N   ILE A 854     -13.928 -24.447 -15.788  1.00 54.46           N  
ANISOU 6969  N   ILE A 854     6634   8850   5209   1214     92   1128       N  
ATOM   6970  CA  ILE A 854     -14.453 -23.465 -14.857  1.00 55.65           C  
ANISOU 6970  CA  ILE A 854     6693   9225   5225   1255     98   1052       C  
ATOM   6971  C   ILE A 854     -14.403 -24.049 -13.437  1.00 56.83           C  
ANISOU 6971  C   ILE A 854     6755   9615   5221   1344    105   1200       C  
ATOM   6972  O   ILE A 854     -14.645 -25.244 -13.252  1.00 58.45           O  
ANISOU 6972  O   ILE A 854     6983   9785   5443   1336    120   1415       O  
ATOM   6973  CB  ILE A 854     -15.881 -23.007 -15.286  1.00 56.05           C  
ANISOU 6973  CB  ILE A 854     6753   9233   5310   1178    124   1042       C  
ATOM   6974  CG1 ILE A 854     -16.373 -21.841 -14.423  1.00 57.62           C  
ANISOU 6974  CG1 ILE A 854     6857   9656   5381   1231    122    917       C  
ATOM   6975  CG2 ILE A 854     -16.874 -24.185 -15.310  1.00 57.01           C  
ANISOU 6975  CG2 ILE A 854     6893   9304   5464   1121    158   1267       C  
ATOM   6976  CD1 ILE A 854     -17.451 -21.011 -15.085  1.00 57.91           C  
ANISOU 6976  CD1 ILE A 854     6912   9618   5472   1175    127    822       C  
ATOM   6977  N   THR A 855     -14.046 -23.218 -12.456  1.00 56.69           N  
ANISOU 6977  N   THR A 855     6640   9840   5060   1428     91   1083       N  
ATOM   6978  CA  THR A 855     -13.947 -23.648 -11.049  1.00 58.87           C  
ANISOU 6978  CA  THR A 855     6816  10391   5162   1524     94   1206       C  
ATOM   6979  C   THR A 855     -15.132 -24.510 -10.597  1.00 60.38           C  
ANISOU 6979  C   THR A 855     6990  10642   5310   1489    135   1448       C  
ATOM   6980  O   THR A 855     -16.284 -24.202 -10.903  1.00 58.20           O  
ANISOU 6980  O   THR A 855     6713  10338   5060   1418    163   1441       O  
ATOM   6981  CB  THR A 855     -13.739 -22.452 -10.074  1.00 58.65           C  
ANISOU 6981  CB  THR A 855     6667  10641   4976   1607     77   1014       C  
ATOM   6982  OG1 THR A 855     -13.732 -22.928  -8.723  1.00 59.78           O  
ANISOU 6982  OG1 THR A 855     6705  11075   4934   1699     84   1149       O  
ATOM   6983  CG2 THR A 855     -14.827 -21.392 -10.226  1.00 57.72           C  
ANISOU 6983  CG2 THR A 855     6523  10547   4860   1565     90    877       C  
ATOM   6984  N   ASP A 856     -14.829 -25.591  -9.877  1.00 64.46           N  
ANISOU 6984  N   ASP A 856     7489  11242   5761   1540    138   1665       N  
ATOM   6985  CA  ASP A 856     -15.836 -26.584  -9.462  1.00 68.04           C  
ANISOU 6985  CA  ASP A 856     7936  11730   6187   1492    178   1933       C  
ATOM   6986  C   ASP A 856     -16.955 -26.023  -8.577  1.00 69.26           C  
ANISOU 6986  C   ASP A 856     7972  12166   6179   1492    214   1940       C  
ATOM   6987  O   ASP A 856     -18.006 -26.655  -8.421  1.00 69.43           O  
ANISOU 6987  O   ASP A 856     7983  12206   6192   1419    255   2129       O  
ATOM   6988  CB  ASP A 856     -15.171 -27.794  -8.789  1.00 71.36           C  
ANISOU 6988  CB  ASP A 856     8362  12189   6562   1560    166   2171       C  
ATOM   6989  CG  ASP A 856     -14.491 -28.726  -9.789  1.00 74.12           C  
ANISOU 6989  CG  ASP A 856     8843  12211   7110   1533    140   2233       C  
ATOM   6990  OD1 ASP A 856     -13.443 -29.312  -9.437  1.00 76.70           O  
ANISOU 6990  OD1 ASP A 856     9178  12549   7415   1628    105   2303       O  
ATOM   6991  OD2 ASP A 856     -14.999 -28.876 -10.925  1.00 75.83           O  
ANISOU 6991  OD2 ASP A 856     9147  12167   7497   1424    152   2205       O  
ATOM   6992  N   LEU A 857     -16.726 -24.837  -8.014  1.00 69.74           N  
ANISOU 6992  N   LEU A 857     7937  12446   6115   1569    196   1723       N  
ATOM   6993  CA  LEU A 857     -17.755 -24.103  -7.273  1.00 71.81           C  
ANISOU 6993  CA  LEU A 857     8079  12976   6231   1582    222   1662       C  
ATOM   6994  C   LEU A 857     -19.017 -23.853  -8.111  1.00 70.18           C  
ANISOU 6994  C   LEU A 857     7910  12622   6131   1471    250   1634       C  
ATOM   6995  O   LEU A 857     -20.139 -24.014  -7.619  1.00 72.28           O  
ANISOU 6995  O   LEU A 857     8102  13054   6308   1439    290   1739       O  
ATOM   6996  CB  LEU A 857     -17.198 -22.763  -6.763  1.00 72.97           C  
ANISOU 6996  CB  LEU A 857     8136  13315   6274   1681    185   1376       C  
ATOM   6997  CG  LEU A 857     -16.319 -22.749  -5.503  1.00 77.27           C  
ANISOU 6997  CG  LEU A 857     8569  14167   6625   1810    163   1372       C  
ATOM   6998  CD1 LEU A 857     -15.499 -21.460  -5.423  1.00 76.69           C  
ANISOU 6998  CD1 LEU A 857     8450  14157   6532   1880    116   1051       C  
ATOM   6999  CD2 LEU A 857     -17.149 -22.945  -4.232  1.00 79.43           C  
ANISOU 6999  CD2 LEU A 857     8699  14805   6676   1853    198   1506       C  
ATOM   7000  N   ILE A 858     -18.824 -23.476  -9.374  1.00 65.66           N  
ANISOU 7000  N   ILE A 858     7448  11757   5743   1414    230   1496       N  
ATOM   7001  CA  ILE A 858     -19.928 -23.029 -10.229  1.00 62.22           C  
ANISOU 7001  CA  ILE A 858     7044  11191   5404   1327    246   1425       C  
ATOM   7002  C   ILE A 858     -20.163 -23.904 -11.468  1.00 59.00           C  
ANISOU 7002  C   ILE A 858     6766  10461   5190   1211    258   1543       C  
ATOM   7003  O   ILE A 858     -21.144 -23.709 -12.189  1.00 58.06           O  
ANISOU 7003  O   ILE A 858     6671  10242   5149   1133    274   1515       O  
ATOM   7004  CB  ILE A 858     -19.760 -21.538 -10.637  1.00 60.87           C  
ANISOU 7004  CB  ILE A 858     6873  10991   5265   1364    209   1126       C  
ATOM   7005  CG1 ILE A 858     -18.401 -21.305 -11.303  1.00 60.04           C  
ANISOU 7005  CG1 ILE A 858     6857  10690   5267   1375    168   1007       C  
ATOM   7006  CG2 ILE A 858     -19.935 -20.630  -9.419  1.00 63.49           C  
ANISOU 7006  CG2 ILE A 858     7060  11654   5409   1469    200    992       C  
ATOM   7007  CD1 ILE A 858     -18.180 -19.887 -11.784  1.00 61.03           C  
ANISOU 7007  CD1 ILE A 858     6996  10748   5445   1391    132    736       C  
ATOM   7008  N   LYS A 859     -19.276 -24.870 -11.699  1.00 57.19           N  
ANISOU 7008  N   LYS A 859     6612  10082   5036   1206    248   1666       N  
ATOM   7009  CA  LYS A 859     -19.358 -25.737 -12.882  1.00 54.80           C  
ANISOU 7009  CA  LYS A 859     6429   9470   4924   1105    252   1756       C  
ATOM   7010  C   LYS A 859     -20.725 -26.404 -13.048  1.00 54.09           C  
ANISOU 7010  C   LYS A 859     6333   9351   4869    998    296   1917       C  
ATOM   7011  O   LYS A 859     -21.331 -26.309 -14.117  1.00 53.12           O  
ANISOU 7011  O   LYS A 859     6265   9046   4871    912    301   1859       O  
ATOM   7012  CB  LYS A 859     -18.245 -26.793 -12.881  1.00 54.84           C  
ANISOU 7012  CB  LYS A 859     6496   9354   4985   1137    232   1882       C  
ATOM   7013  CG  LYS A 859     -18.149 -27.564 -14.187  1.00 53.17           C  
ANISOU 7013  CG  LYS A 859     6407   8816   4980   1050    224   1916       C  
ATOM   7014  CD  LYS A 859     -17.114 -28.667 -14.139  1.00 53.35           C  
ANISOU 7014  CD  LYS A 859     6487   8722   5063   1094    199   2042       C  
ATOM   7015  CE  LYS A 859     -17.168 -29.476 -15.429  1.00 54.10           C  
ANISOU 7015  CE  LYS A 859     6691   8499   5365   1005    193   2067       C  
ATOM   7016  NZ  LYS A 859     -16.061 -30.459 -15.545  1.00 54.99           N  
ANISOU 7016  NZ  LYS A 859     6865   8471   5557   1062    157   2142       N  
ATOM   7017  N   ASP A 860     -21.193 -27.068 -11.990  1.00 53.88           N  
ANISOU 7017  N   ASP A 860     6232   9515   4725   1000    329   2121       N  
ATOM   7018  CA  ASP A 860     -22.472 -27.786 -11.994  1.00 53.63           C  
ANISOU 7018  CA  ASP A 860     6179   9487   4712    887    376   2299       C  
ATOM   7019  C   ASP A 860     -23.641 -26.893 -12.383  1.00 50.36           C  
ANISOU 7019  C   ASP A 860     5712   9138   4284    840    394   2155       C  
ATOM   7020  O   ASP A 860     -24.520 -27.310 -13.137  1.00 48.55           O  
ANISOU 7020  O   ASP A 860     5515   8770   4162    727    416   2205       O  
ATOM   7021  CB  ASP A 860     -22.742 -28.433 -10.624  1.00 58.35           C  
ANISOU 7021  CB  ASP A 860     6682  10344   5145    906    410   2531       C  
ATOM   7022  CG  ASP A 860     -22.173 -29.843 -10.511  1.00 63.99           C  
ANISOU 7022  CG  ASP A 860     7472  10905   5938    883    407   2783       C  
ATOM   7023  OD1 ASP A 860     -21.627 -30.360 -11.510  1.00 67.62           O  
ANISOU 7023  OD1 ASP A 860     8052  11055   6586    851    379   2766       O  
ATOM   7024  OD2 ASP A 860     -22.276 -30.442  -9.416  1.00 70.41           O  
ANISOU 7024  OD2 ASP A 860     8220  11910   6621    901    431   3001       O  
ATOM   7025  N   ASP A 861     -23.636 -25.666 -11.872  1.00 48.98           N  
ANISOU 7025  N   ASP A 861     5455   9173   3981    934    380   1968       N  
ATOM   7026  CA  ASP A 861     -24.695 -24.699 -12.155  1.00 49.51           C  
ANISOU 7026  CA  ASP A 861     5467   9320   4026    921    386   1812       C  
ATOM   7027  C   ASP A 861     -24.592 -24.069 -13.541  1.00 47.65           C  
ANISOU 7027  C   ASP A 861     5333   8818   3955    893    352   1628       C  
ATOM   7028  O   ASP A 861     -25.603 -23.661 -14.109  1.00 47.53           O  
ANISOU 7028  O   ASP A 861     5304   8781   3974    847    359   1559       O  
ATOM   7029  CB  ASP A 861     -24.732 -23.614 -11.081  1.00 51.12           C  
ANISOU 7029  CB  ASP A 861     5544   9839   4042   1040    376   1667       C  
ATOM   7030  CG  ASP A 861     -25.263 -24.129  -9.755  1.00 55.34           C  
ANISOU 7030  CG  ASP A 861     5945  10696   4386   1053    420   1844       C  
ATOM   7031  OD1 ASP A 861     -24.579 -23.950  -8.724  1.00 57.54           O  
ANISOU 7031  OD1 ASP A 861     6155  11189   4519   1153    409   1838       O  
ATOM   7032  OD2 ASP A 861     -26.364 -24.719  -9.752  1.00 55.56           O  
ANISOU 7032  OD2 ASP A 861     5932  10774   4404    957    466   1990       O  
ATOM   7033  N   VAL A 862     -23.380 -23.981 -14.083  1.00 45.81           N  
ANISOU 7033  N   VAL A 862     5195   8399   3812    922    314   1551       N  
ATOM   7034  CA  VAL A 862     -23.205 -23.454 -15.437  1.00 44.06           C  
ANISOU 7034  CA  VAL A 862     5073   7929   3741    887    285   1400       C  
ATOM   7035  C   VAL A 862     -23.719 -24.474 -16.451  1.00 44.08           C  
ANISOU 7035  C   VAL A 862     5149   7711   3889    765    304   1523       C  
ATOM   7036  O   VAL A 862     -24.487 -24.121 -17.345  1.00 42.45           O  
ANISOU 7036  O   VAL A 862     4964   7412   3753    710    303   1448       O  
ATOM   7037  CB  VAL A 862     -21.739 -23.029 -15.729  1.00 42.87           C  
ANISOU 7037  CB  VAL A 862     4989   7665   3636    944    243   1275       C  
ATOM   7038  CG1 VAL A 862     -21.533 -22.751 -17.213  1.00 41.19           C  
ANISOU 7038  CG1 VAL A 862     4884   7186   3582    885    220   1170       C  
ATOM   7039  CG2 VAL A 862     -21.374 -21.790 -14.921  1.00 42.01           C  
ANISOU 7039  CG2 VAL A 862     4806   7751   3406   1051    218   1100       C  
ATOM   7040  N   LEU A 863     -23.324 -25.737 -16.281  1.00 45.25           N  
ANISOU 7040  N   LEU A 863     5331   7783   4080    728    319   1708       N  
ATOM   7041  CA  LEU A 863     -23.738 -26.823 -17.186  1.00 46.31           C  
ANISOU 7041  CA  LEU A 863     5535   7696   4364    611    333   1823       C  
ATOM   7042  C   LEU A 863     -25.246 -27.064 -17.186  1.00 45.88           C  
ANISOU 7042  C   LEU A 863     5419   7717   4298    517    373   1903       C  
ATOM   7043  O   LEU A 863     -25.806 -27.521 -18.185  1.00 44.82           O  
ANISOU 7043  O   LEU A 863     5330   7410   4290    418    379   1911       O  
ATOM   7044  CB  LEU A 863     -23.027 -28.143 -16.841  1.00 48.64           C  
ANISOU 7044  CB  LEU A 863     5874   7900   4708    602    335   2015       C  
ATOM   7045  CG  LEU A 863     -21.498 -28.273 -16.815  1.00 50.76           C  
ANISOU 7045  CG  LEU A 863     6202   8086   5001    690    296   1980       C  
ATOM   7046  CD1 LEU A 863     -21.082 -29.717 -17.100  1.00 54.07           C  
ANISOU 7046  CD1 LEU A 863     6697   8298   5551    648    290   2146       C  
ATOM   7047  CD2 LEU A 863     -20.828 -27.339 -17.789  1.00 46.92           C  
ANISOU 7047  CD2 LEU A 863     5768   7486   4574    717    261   1751       C  
ATOM   7048  N   HIS A 864     -25.884 -26.778 -16.055  1.00 46.55           N  
ANISOU 7048  N   HIS A 864     5388   8076   4222    549    402   1955       N  
ATOM   7049  CA  HIS A 864     -27.322 -26.963 -15.902  1.00 49.10           C  
ANISOU 7049  CA  HIS A 864     5627   8524   4504    465    444   2029       C  
ATOM   7050  C   HIS A 864     -28.103 -25.785 -16.488  1.00 47.11           C  
ANISOU 7050  C   HIS A 864     5340   8320   4239    484    429   1824       C  
ATOM   7051  O   HIS A 864     -29.209 -25.966 -16.998  1.00 46.37           O  
ANISOU 7051  O   HIS A 864     5217   8217   4184    397    450   1839       O  
ATOM   7052  CB  HIS A 864     -27.682 -27.173 -14.422  1.00 52.05           C  
ANISOU 7052  CB  HIS A 864     5879   9203   4695    491    483   2176       C  
ATOM   7053  CG  HIS A 864     -29.143 -27.394 -14.177  1.00 56.75           C  
ANISOU 7053  CG  HIS A 864     6369   9962   5231    398    533   2261       C  
ATOM   7054  ND1 HIS A 864     -30.009 -26.367 -13.864  1.00 58.28           N  
ANISOU 7054  ND1 HIS A 864     6450  10394   5301    446    539   2122       N  
ATOM   7055  CD2 HIS A 864     -29.891 -28.523 -14.202  1.00 60.55           C  
ANISOU 7055  CD2 HIS A 864     6837  10405   5764    256    577   2464       C  
ATOM   7056  CE1 HIS A 864     -31.227 -26.854 -13.705  1.00 61.67           C  
ANISOU 7056  CE1 HIS A 864     6792  10944   5696    340    588   2234       C  
ATOM   7057  NE2 HIS A 864     -31.183 -28.159 -13.906  1.00 63.34           N  
ANISOU 7057  NE2 HIS A 864     7062  10989   6014    216    614   2446       N  
ATOM   7058  N   TRP A 865     -27.523 -24.588 -16.409  1.00 45.38           N  
ANISOU 7058  N   TRP A 865     5124   8149   3970    600    390   1635       N  
ATOM   7059  CA  TRP A 865     -28.184 -23.375 -16.897  1.00 44.84           C  
ANISOU 7059  CA  TRP A 865     5029   8117   3891    641    366   1439       C  
ATOM   7060  C   TRP A 865     -27.668 -22.846 -18.247  1.00 43.12           C  
ANISOU 7060  C   TRP A 865     4931   7638   3816    638    321   1295       C  
ATOM   7061  O   TRP A 865     -28.126 -21.804 -18.719  1.00 44.32           O  
ANISOU 7061  O   TRP A 865     5077   7792   3970    679    294   1139       O  
ATOM   7062  CB  TRP A 865     -28.159 -22.281 -15.822  1.00 43.85           C  
ANISOU 7062  CB  TRP A 865     4805   8250   3605    769    352   1315       C  
ATOM   7063  CG  TRP A 865     -29.046 -22.603 -14.659  1.00 44.51           C  
ANISOU 7063  CG  TRP A 865     4745   8635   3530    767    398   1426       C  
ATOM   7064  CD1 TRP A 865     -28.670 -23.173 -13.466  1.00 44.43           C  
ANISOU 7064  CD1 TRP A 865     4671   8813   3398    789    427   1568       C  
ATOM   7065  CD2 TRP A 865     -30.461 -22.398 -14.575  1.00 45.02           C  
ANISOU 7065  CD2 TRP A 865     4704   8870   3532    740    423   1412       C  
ATOM   7066  NE1 TRP A 865     -29.760 -23.327 -12.653  1.00 44.58           N  
ANISOU 7066  NE1 TRP A 865     4551   9110   3278    769    471   1649       N  
ATOM   7067  CE2 TRP A 865     -30.874 -22.861 -13.303  1.00 47.40           C  
ANISOU 7067  CE2 TRP A 865     4875   9465   3668    738    470   1550       C  
ATOM   7068  CE3 TRP A 865     -31.423 -21.869 -15.448  1.00 46.50           C  
ANISOU 7068  CE3 TRP A 865     4886   9003   3777    720    409   1299       C  
ATOM   7069  CZ2 TRP A 865     -32.209 -22.806 -12.881  1.00 46.68           C  
ANISOU 7069  CZ2 TRP A 865     4645   9623   3469    711    507   1569       C  
ATOM   7070  CZ3 TRP A 865     -32.751 -21.816 -15.027  1.00 45.73           C  
ANISOU 7070  CZ3 TRP A 865     4651   9146   3577    702    441   1312       C  
ATOM   7071  CH2 TRP A 865     -33.129 -22.282 -13.752  1.00 47.34           C  
ANISOU 7071  CH2 TRP A 865     4722   9649   3617    694    491   1443       C  
ATOM   7072  N   MET A 866     -26.724 -23.563 -18.859  1.00 42.88           N  
ANISOU 7072  N   MET A 866     5002   7391   3898    595    313   1350       N  
ATOM   7073  CA  MET A 866     -26.244 -23.260 -20.215  1.00 40.23           C  
ANISOU 7073  CA  MET A 866     4774   6816   3694    572    279   1240       C  
ATOM   7074  C   MET A 866     -27.409 -23.156 -21.177  1.00 38.80           C  
ANISOU 7074  C   MET A 866     4591   6580   3572    505    281   1206       C  
ATOM   7075  O   MET A 866     -28.243 -24.063 -21.232  1.00 39.63           O  
ANISOU 7075  O   MET A 866     4662   6695   3700    416    314   1325       O  
ATOM   7076  CB  MET A 866     -25.389 -24.413 -20.736  1.00 41.93           C  
ANISOU 7076  CB  MET A 866     5076   6832   4024    512    281   1339       C  
ATOM   7077  CG  MET A 866     -23.929 -24.391 -20.402  1.00 41.34           C  
ANISOU 7077  CG  MET A 866     5044   6720   3942    579    259   1317       C  
ATOM   7078  SD  MET A 866     -23.193 -25.898 -21.059  1.00 41.18           S  
ANISOU 7078  SD  MET A 866     5112   6469   4065    510    260   1439       S  
ATOM   7079  CE  MET A 866     -23.208 -25.533 -22.807  1.00 40.17           C  
ANISOU 7079  CE  MET A 866     5066   6130   4068    451    235   1295       C  
ATOM   7080  N   ASP A 867     -27.452 -22.075 -21.958  1.00 37.60           N  
ANISOU 7080  N   ASP A 867     4476   6363   3448    543    243   1049       N  
ATOM   7081  CA  ASP A 867     -28.515 -21.898 -22.958  1.00 35.03           C  
ANISOU 7081  CA  ASP A 867     4149   5988   3172    494    236   1006       C  
ATOM   7082  C   ASP A 867     -28.102 -22.423 -24.335  1.00 32.80           C  
ANISOU 7082  C   ASP A 867     3966   5473   3025    416    224   1005       C  
ATOM   7083  O   ASP A 867     -27.569 -21.675 -25.167  1.00 29.31           O  
ANISOU 7083  O   ASP A 867     3593   4917   2625    443    187    897       O  
ATOM   7084  CB  ASP A 867     -28.958 -20.435 -23.042  1.00 32.97           C  
ANISOU 7084  CB  ASP A 867     3867   5797   2862    587    198    849       C  
ATOM   7085  CG  ASP A 867     -30.305 -20.267 -23.723  1.00 33.83           C  
ANISOU 7085  CG  ASP A 867     3935   5938   2981    559    194    822       C  
ATOM   7086  OD1 ASP A 867     -30.695 -21.125 -24.550  1.00 34.10           O  
ANISOU 7086  OD1 ASP A 867     3988   5877   3090    459    210    888       O  
ATOM   7087  OD2 ASP A 867     -30.986 -19.264 -23.425  1.00 36.54           O  
ANISOU 7087  OD2 ASP A 867     4221   6406   3257    644    171    724       O  
ATOM   7088  N   TYR A 868     -28.359 -23.711 -24.559  1.00 32.00           N  
ANISOU 7088  N   TYR A 868     3864   5306   2988    317    253   1124       N  
ATOM   7089  CA  TYR A 868     -28.062 -24.373 -25.833  1.00 32.32           C  
ANISOU 7089  CA  TYR A 868     3981   5142   3156    238    243   1118       C  
ATOM   7090  C   TYR A 868     -28.814 -23.774 -27.022  1.00 32.10           C  
ANISOU 7090  C   TYR A 868     3960   5077   3157    220    219   1016       C  
ATOM   7091  O   TYR A 868     -28.249 -23.665 -28.109  1.00 30.21           O  
ANISOU 7091  O   TYR A 868     3795   4696   2988    206    193    949       O  
ATOM   7092  CB  TYR A 868     -28.377 -25.867 -25.753  1.00 34.21           C  
ANISOU 7092  CB  TYR A 868     4207   5325   3467    134    276   1259       C  
ATOM   7093  CG  TYR A 868     -27.464 -26.670 -24.850  1.00 36.54           C  
ANISOU 7093  CG  TYR A 868     4521   5599   3765    147    291   1378       C  
ATOM   7094  CD1 TYR A 868     -26.316 -27.284 -25.349  1.00 37.63           C  
ANISOU 7094  CD1 TYR A 868     4742   5556   3998    143    273   1378       C  
ATOM   7095  CD2 TYR A 868     -27.767 -26.838 -23.502  1.00 41.34           C  
ANISOU 7095  CD2 TYR A 868     5056   6380   4273    167    322   1492       C  
ATOM   7096  CE1 TYR A 868     -25.483 -28.040 -24.517  1.00 40.84           C  
ANISOU 7096  CE1 TYR A 868     5165   5944   4408    169    280   1490       C  
ATOM   7097  CE2 TYR A 868     -26.946 -27.587 -22.663  1.00 45.41           C  
ANISOU 7097  CE2 TYR A 868     5586   6884   4782    187    332   1617       C  
ATOM   7098  CZ  TYR A 868     -25.808 -28.183 -23.173  1.00 43.95           C  
ANISOU 7098  CZ  TYR A 868     5491   6507   4700    192    309   1616       C  
ATOM   7099  OH  TYR A 868     -25.008 -28.918 -22.329  1.00 46.71           O  
ANISOU 7099  OH  TYR A 868     5855   6851   5042    225    312   1742       O  
ATOM   7100  N   THR A 869     -30.083 -23.401 -26.823  1.00 33.07           N  
ANISOU 7100  N   THR A 869     4002   5342   3221    223    226   1005       N  
ATOM   7101  CA  THR A 869     -30.906 -22.816 -27.898  1.00 31.61           C  
ANISOU 7101  CA  THR A 869     3813   5147   3051    219    199    913       C  
ATOM   7102  C   THR A 869     -30.306 -21.498 -28.410  1.00 30.31           C  
ANISOU 7102  C   THR A 869     3716   4926   2874    311    151    794       C  
ATOM   7103  O   THR A 869     -30.200 -21.289 -29.621  1.00 29.16           O  
ANISOU 7103  O   THR A 869     3626   4670   2782    291    124    739       O  
ATOM   7104  CB  THR A 869     -32.379 -22.593 -27.463  1.00 33.93           C  
ANISOU 7104  CB  THR A 869     3991   5632   3267    224    213    916       C  
ATOM   7105  OG1 THR A 869     -32.957 -23.836 -27.045  1.00 37.00           O  
ANISOU 7105  OG1 THR A 869     4316   6068   3674    116    261   1037       O  
ATOM   7106  CG2 THR A 869     -33.213 -22.010 -28.618  1.00 31.20           C  
ANISOU 7106  CG2 THR A 869     3640   5279   2936    232    178    821       C  
ATOM   7107  N   VAL A 870     -29.902 -20.627 -27.488  1.00 30.12           N  
ANISOU 7107  N   VAL A 870     3684   4980   2781    407    140    755       N  
ATOM   7108  CA  VAL A 870     -29.270 -19.357 -27.859  1.00 33.02           C  
ANISOU 7108  CA  VAL A 870     4118   5280   3148    486     94    646       C  
ATOM   7109  C   VAL A 870     -27.923 -19.610 -28.543  1.00 34.76           C  
ANISOU 7109  C   VAL A 870     4437   5330   3442    446     87    644       C  
ATOM   7110  O   VAL A 870     -27.610 -19.009 -29.575  1.00 34.02           O  
ANISOU 7110  O   VAL A 870     4410   5130   3386    445     56    584       O  
ATOM   7111  CB  VAL A 870     -29.138 -18.405 -26.652  1.00 32.87           C  
ANISOU 7111  CB  VAL A 870     4059   5384   3046    594     81    588       C  
ATOM   7112  CG1 VAL A 870     -28.154 -17.274 -26.950  1.00 31.53           C  
ANISOU 7112  CG1 VAL A 870     3972   5105   2902    651     38    488       C  
ATOM   7113  CG2 VAL A 870     -30.518 -17.828 -26.296  1.00 32.63           C  
ANISOU 7113  CG2 VAL A 870     3936   5515   2946    655     71    545       C  
ATOM   7114  N   LEU A 871     -27.153 -20.527 -27.969  1.00 35.41           N  
ANISOU 7114  N   LEU A 871     4522   5395   3536    414    117    715       N  
ATOM   7115  CA  LEU A 871     -25.881 -20.952 -28.520  1.00 35.73           C  
ANISOU 7115  CA  LEU A 871     4637   5296   3641    379    114    714       C  
ATOM   7116  C   LEU A 871     -26.015 -21.425 -29.969  1.00 36.39           C  
ANISOU 7116  C   LEU A 871     4764   5259   3804    303    106    703       C  
ATOM   7117  O   LEU A 871     -25.280 -20.975 -30.845  1.00 36.65           O  
ANISOU 7117  O   LEU A 871     4860   5201   3866    298     84    642       O  
ATOM   7118  CB  LEU A 871     -25.339 -22.088 -27.662  1.00 38.35           C  
ANISOU 7118  CB  LEU A 871     4951   5643   3979    361    145    812       C  
ATOM   7119  CG  LEU A 871     -23.851 -22.122 -27.357  1.00 40.85           C  
ANISOU 7119  CG  LEU A 871     5311   5909   4302    392    139    796       C  
ATOM   7120  CD1 LEU A 871     -23.642 -23.006 -26.139  1.00 40.75           C  
ANISOU 7120  CD1 LEU A 871     5254   5972   4255    408    166    906       C  
ATOM   7121  CD2 LEU A 871     -23.051 -22.613 -28.577  1.00 44.21           C  
ANISOU 7121  CD2 LEU A 871     5805   6175   4817    338    128    768       C  
ATOM   7122  N   LEU A 872     -26.952 -22.338 -30.212  1.00 38.10           N  
ANISOU 7122  N   LEU A 872     4938   5487   4051    238    126    759       N  
ATOM   7123  CA  LEU A 872     -27.169 -22.887 -31.543  1.00 38.17           C  
ANISOU 7123  CA  LEU A 872     4971   5402   4131    164    118    737       C  
ATOM   7124  C   LEU A 872     -27.577 -21.798 -32.529  1.00 39.34           C  
ANISOU 7124  C   LEU A 872     5140   5553   4255    191     83    655       C  
ATOM   7125  O   LEU A 872     -26.992 -21.687 -33.604  1.00 41.50           O  
ANISOU 7125  O   LEU A 872     5467   5741   4561    168     65    609       O  
ATOM   7126  CB  LEU A 872     -28.216 -24.006 -31.513  1.00 37.69           C  
ANISOU 7126  CB  LEU A 872     4848   5365   4108     85    144    804       C  
ATOM   7127  CG  LEU A 872     -28.593 -24.618 -32.871  1.00 40.93           C  
ANISOU 7127  CG  LEU A 872     5264   5695   4591      5    134    764       C  
ATOM   7128  CD1 LEU A 872     -27.442 -25.452 -33.448  1.00 41.63           C  
ANISOU 7128  CD1 LEU A 872     5412   5639   4765    -32    131    750       C  
ATOM   7129  CD2 LEU A 872     -29.862 -25.448 -32.770  1.00 42.54           C  
ANISOU 7129  CD2 LEU A 872     5390   5953   4820    -73    157    813       C  
ATOM   7130  N   GLU A 873     -28.565 -20.991 -32.151  1.00 40.17           N  
ANISOU 7130  N   GLU A 873     5199   5765   4298    245     72    639       N  
ATOM   7131  CA  GLU A 873     -29.061 -19.917 -33.011  1.00 42.15           C  
ANISOU 7131  CA  GLU A 873     5468   6020   4525    286     31    573       C  
ATOM   7132  C   GLU A 873     -28.030 -18.844 -33.364  1.00 40.87           C  
ANISOU 7132  C   GLU A 873     5391   5776   4361    332      0    523       C  
ATOM   7133  O   GLU A 873     -27.996 -18.370 -34.501  1.00 41.19           O  
ANISOU 7133  O   GLU A 873     5476   5762   4412    323    -28    493       O  
ATOM   7134  CB  GLU A 873     -30.319 -19.274 -32.409  1.00 44.46           C  
ANISOU 7134  CB  GLU A 873     5688   6451   4752    353     20    559       C  
ATOM   7135  CG  GLU A 873     -31.574 -20.140 -32.545  1.00 51.29           C  
ANISOU 7135  CG  GLU A 873     6465   7406   5618    292     42    592       C  
ATOM   7136  CD  GLU A 873     -32.048 -20.299 -33.991  1.00 56.87           C  
ANISOU 7136  CD  GLU A 873     7180   8073   6355    246     20    559       C  
ATOM   7137  OE1 GLU A 873     -32.827 -21.243 -34.256  1.00 57.99           O  
ANISOU 7137  OE1 GLU A 873     7258   8257   6521    167     41    579       O  
ATOM   7138  OE2 GLU A 873     -31.644 -19.483 -34.857  1.00 59.00           O  
ANISOU 7138  OE2 GLU A 873     7517   8278   6624    284    -19    515       O  
ATOM   7139  N   LYS A 874     -27.188 -18.474 -32.404  1.00 39.37           N  
ANISOU 7139  N   LYS A 874     5219   5584   4156    374      5    516       N  
ATOM   7140  CA  LYS A 874     -26.263 -17.354 -32.590  1.00 39.31           C  
ANISOU 7140  CA  LYS A 874     5282   5505   4148    412    -24    462       C  
ATOM   7141  C   LYS A 874     -24.951 -17.706 -33.281  1.00 38.38           C  
ANISOU 7141  C   LYS A 874     5225   5285   4072    350    -16    460       C  
ATOM   7142  O   LYS A 874     -24.494 -16.961 -34.149  1.00 39.67           O  
ANISOU 7142  O   LYS A 874     5448   5381   4245    339    -40    430       O  
ATOM   7143  CB  LYS A 874     -25.980 -16.654 -31.254  1.00 40.68           C  
ANISOU 7143  CB  LYS A 874     5436   5737   4282    490    -28    430       C  
ATOM   7144  CG  LYS A 874     -26.864 -15.440 -30.990  1.00 43.19           C  
ANISOU 7144  CG  LYS A 874     5737   6105   4567    581    -68    373       C  
ATOM   7145  CD  LYS A 874     -26.872 -14.998 -29.527  1.00 44.00           C  
ANISOU 7145  CD  LYS A 874     5786   6313   4619    662    -67    332       C  
ATOM   7146  CE  LYS A 874     -25.488 -15.040 -28.880  1.00 44.07           C  
ANISOU 7146  CE  LYS A 874     5819   6294   4631    653    -53    316       C  
ATOM   7147  NZ  LYS A 874     -25.522 -14.457 -27.505  1.00 44.96           N  
ANISOU 7147  NZ  LYS A 874     5872   6523   4685    742    -61    254       N  
ATOM   7148  N   THR A 875     -24.340 -18.824 -32.898  1.00 36.01           N  
ANISOU 7148  N   THR A 875     4908   4978   3794    312     17    494       N  
ATOM   7149  CA  THR A 875     -22.994 -19.137 -33.379  1.00 34.70           C  
ANISOU 7149  CA  THR A 875     4789   4736   3661    270     23    476       C  
ATOM   7150  C   THR A 875     -23.002 -20.094 -34.558  1.00 32.97           C  
ANISOU 7150  C   THR A 875     4574   4465   3486    198     30    482       C  
ATOM   7151  O   THR A 875     -22.013 -20.198 -35.290  1.00 31.58           O  
ANISOU 7151  O   THR A 875     4434   4238   3329    163     28    450       O  
ATOM   7152  CB  THR A 875     -22.073 -19.704 -32.262  1.00 34.52           C  
ANISOU 7152  CB  THR A 875     4749   4732   3636    291     44    495       C  
ATOM   7153  OG1 THR A 875     -22.366 -21.091 -32.044  1.00 36.20           O  
ANISOU 7153  OG1 THR A 875     4927   4945   3882    260     69    560       O  
ATOM   7154  CG2 THR A 875     -22.246 -18.923 -30.960  1.00 34.57           C  
ANISOU 7154  CG2 THR A 875     4726   4824   3586    366     40    484       C  
ATOM   7155  N   PHE A 876     -24.116 -20.791 -34.740  1.00 32.31           N  
ANISOU 7155  N   PHE A 876     4448   4408   3419    173     37    513       N  
ATOM   7156  CA  PHE A 876     -24.203 -21.773 -35.806  1.00 31.77           C  
ANISOU 7156  CA  PHE A 876     4375   4295   3400    105     41    503       C  
ATOM   7157  C   PHE A 876     -25.216 -21.404 -36.888  1.00 32.14           C  
ANISOU 7157  C   PHE A 876     4410   4372   3430     86     20    478       C  
ATOM   7158  O   PHE A 876     -24.835 -21.194 -38.040  1.00 31.94           O  
ANISOU 7158  O   PHE A 876     4412   4323   3399     60      5    438       O  
ATOM   7159  CB  PHE A 876     -24.487 -23.164 -35.242  1.00 30.59           C  
ANISOU 7159  CB  PHE A 876     4185   4132   3307     71     67    553       C  
ATOM   7160  CG  PHE A 876     -24.481 -24.234 -36.276  1.00 29.87           C  
ANISOU 7160  CG  PHE A 876     4087   3977   3285      2     66    523       C  
ATOM   7161  CD1 PHE A 876     -23.287 -24.655 -36.846  1.00 26.34           C  
ANISOU 7161  CD1 PHE A 876     3672   3463   2874    -11     62    475       C  
ATOM   7162  CD2 PHE A 876     -25.669 -24.816 -36.694  1.00 28.95           C  
ANISOU 7162  CD2 PHE A 876     3923   3880   3198    -49     68    527       C  
ATOM   7163  CE1 PHE A 876     -23.282 -25.641 -37.822  1.00 31.04           C  
ANISOU 7163  CE1 PHE A 876     4254   4005   3534    -66     57    425       C  
ATOM   7164  CE2 PHE A 876     -25.669 -25.807 -37.665  1.00 31.28           C  
ANISOU 7164  CE2 PHE A 876     4206   4116   3563   -113     64    479       C  
ATOM   7165  CZ  PHE A 876     -24.478 -26.221 -38.228  1.00 30.94           C  
ANISOU 7165  CZ  PHE A 876     4197   4001   3557   -118     56    424       C  
ATOM   7166  N   ILE A 877     -26.497 -21.327 -36.524  1.00 32.55           N  
ANISOU 7166  N   ILE A 877     4413   4494   3462    102     19    503       N  
ATOM   7167  CA  ILE A 877     -27.560 -21.144 -37.519  1.00 32.56           C  
ANISOU 7167  CA  ILE A 877     4386   4541   3445     88     -2    479       C  
ATOM   7168  C   ILE A 877     -27.467 -19.804 -38.261  1.00 32.06           C  
ANISOU 7168  C   ILE A 877     4371   4480   3329    135    -40    453       C  
ATOM   7169  O   ILE A 877     -27.562 -19.766 -39.489  1.00 32.93           O  
ANISOU 7169  O   ILE A 877     4490   4593   3429    107    -58    429       O  
ATOM   7170  CB  ILE A 877     -28.980 -21.409 -36.933  1.00 33.85           C  
ANISOU 7170  CB  ILE A 877     4470   4797   3594     92      6    505       C  
ATOM   7171  CG1 ILE A 877     -29.113 -22.886 -36.528  1.00 35.46           C  
ANISOU 7171  CG1 ILE A 877     4630   4979   3865     15     42    541       C  
ATOM   7172  CG2 ILE A 877     -30.080 -21.048 -37.954  1.00 32.56           C  
ANISOU 7172  CG2 ILE A 877     4272   4702   3399     95    -23    470       C  
ATOM   7173  CD1 ILE A 877     -30.465 -23.272 -35.930  1.00 39.97           C  
ANISOU 7173  CD1 ILE A 877     5112   5649   4424     -7     60    577       C  
ATOM   7174  N   LYS A 878     -27.251 -18.717 -37.530  1.00 31.63           N  
ANISOU 7174  N   LYS A 878     4350   4423   3245    205    -54    460       N  
ATOM   7175  CA  LYS A 878     -27.150 -17.408 -38.171  1.00 34.48           C  
ANISOU 7175  CA  LYS A 878     4767   4760   3573    247    -94    449       C  
ATOM   7176  C   LYS A 878     -26.028 -17.343 -39.231  1.00 32.39           C  
ANISOU 7176  C   LYS A 878     4560   4432   3314    191    -95    441       C  
ATOM   7177  O   LYS A 878     -26.284 -16.911 -40.354  1.00 33.03           O  
ANISOU 7177  O   LYS A 878     4660   4523   3366    184   -121    444       O  
ATOM   7178  CB  LYS A 878     -27.036 -16.267 -37.148  1.00 35.80           C  
ANISOU 7178  CB  LYS A 878     4961   4916   3726    330   -112    442       C  
ATOM   7179  CG  LYS A 878     -27.883 -15.067 -37.530  1.00 41.18           C  
ANISOU 7179  CG  LYS A 878     5660   5608   4378    405   -163    436       C  
ATOM   7180  CD  LYS A 878     -27.322 -13.757 -37.016  1.00 48.75           C  
ANISOU 7180  CD  LYS A 878     6683   6496   5345    467   -192    416       C  
ATOM   7181  CE  LYS A 878     -27.921 -12.581 -37.800  1.00 51.31           C  
ANISOU 7181  CE  LYS A 878     7053   6785   5657    527   -251    425       C  
ATOM   7182  NZ  LYS A 878     -27.575 -11.256 -37.216  1.00 51.88           N  
ANISOU 7182  NZ  LYS A 878     7184   6773   5755    597   -290    397       N  
ATOM   7183  N   PRO A 879     -24.793 -17.778 -38.884  1.00 32.05           N  
ANISOU 7183  N   PRO A 879     4537   4340   3298    155    -68    431       N  
ATOM   7184  CA  PRO A 879     -23.724 -17.800 -39.885  1.00 30.72           C  
ANISOU 7184  CA  PRO A 879     4406   4139   3127     97    -65    414       C  
ATOM   7185  C   PRO A 879     -24.008 -18.722 -41.069  1.00 29.41           C  
ANISOU 7185  C   PRO A 879     4205   4009   2961     41    -61    392       C  
ATOM   7186  O   PRO A 879     -23.776 -18.330 -42.208  1.00 28.12           O  
ANISOU 7186  O   PRO A 879     4062   3863   2759     14    -76    388       O  
ATOM   7187  CB  PRO A 879     -22.520 -18.316 -39.097  1.00 30.64           C  
ANISOU 7187  CB  PRO A 879     4400   4094   3148     82    -36    397       C  
ATOM   7188  CG  PRO A 879     -22.804 -17.944 -37.704  1.00 30.68           C  
ANISOU 7188  CG  PRO A 879     4397   4105   3155    145    -35    412       C  
ATOM   7189  CD  PRO A 879     -24.267 -18.099 -37.540  1.00 31.94           C  
ANISOU 7189  CD  PRO A 879     4512   4317   3306    175    -43    433       C  
ATOM   7190  N   LEU A 880     -24.498 -19.933 -40.802  1.00 29.48           N  
ANISOU 7190  N   LEU A 880     4158   4030   3011     21    -43    378       N  
ATOM   7191  CA  LEU A 880     -24.875 -20.861 -41.879  1.00 30.53           C  
ANISOU 7191  CA  LEU A 880     4248   4196   3156    -32    -44    336       C  
ATOM   7192  C   LEU A 880     -25.947 -20.285 -42.829  1.00 30.01           C  
ANISOU 7192  C   LEU A 880     4164   4205   3034    -20    -76    338       C  
ATOM   7193  O   LEU A 880     -25.841 -20.436 -44.051  1.00 30.75           O  
ANISOU 7193  O   LEU A 880     4246   4342   3097    -55    -87    303       O  
ATOM   7194  CB  LEU A 880     -25.318 -22.212 -41.304  1.00 30.41           C  
ANISOU 7194  CB  LEU A 880     4179   4161   3214    -60    -23    328       C  
ATOM   7195  CG  LEU A 880     -25.730 -23.312 -42.289  1.00 30.39           C  
ANISOU 7195  CG  LEU A 880     4124   4174   3248   -121    -25    266       C  
ATOM   7196  CD1 LEU A 880     -24.540 -23.783 -43.107  1.00 33.80           C  
ANISOU 7196  CD1 LEU A 880     4569   4579   3693   -152    -23    200       C  
ATOM   7197  CD2 LEU A 880     -26.345 -24.480 -41.554  1.00 26.34           C  
ANISOU 7197  CD2 LEU A 880     3566   3625   2818   -153     -6    278       C  
ATOM   7198  N   GLU A 881     -26.964 -19.631 -42.268  1.00 31.44           N  
ANISOU 7198  N   GLU A 881     4336   4416   3194     37    -92    374       N  
ATOM   7199  CA  GLU A 881     -27.990 -18.945 -43.069  1.00 34.32           C  
ANISOU 7199  CA  GLU A 881     4686   4856   3499     71   -129    382       C  
ATOM   7200  C   GLU A 881     -27.322 -17.894 -43.954  1.00 32.37           C  
ANISOU 7200  C   GLU A 881     4506   4595   3197     81   -155    408       C  
ATOM   7201  O   GLU A 881     -27.685 -17.728 -45.118  1.00 32.54           O  
ANISOU 7201  O   GLU A 881     4515   4684   3165     74   -179    406       O  
ATOM   7202  CB  GLU A 881     -29.032 -18.271 -42.167  1.00 37.02           C  
ANISOU 7202  CB  GLU A 881     5011   5228   3828    149   -147    409       C  
ATOM   7203  CG  GLU A 881     -30.492 -18.391 -42.636  1.00 48.10           C  
ANISOU 7203  CG  GLU A 881     6340   6740   5197    170   -170    393       C  
ATOM   7204  CD  GLU A 881     -30.809 -17.627 -43.919  1.00 55.65           C  
ANISOU 7204  CD  GLU A 881     7313   7747   6085    201   -216    400       C  
ATOM   7205  OE1 GLU A 881     -31.406 -18.233 -44.839  1.00 61.83           O  
ANISOU 7205  OE1 GLU A 881     8034   8616   6843    166   -224    363       O  
ATOM   7206  OE2 GLU A 881     -30.477 -16.424 -44.016  1.00 60.83           O  
ANISOU 7206  OE2 GLU A 881     8043   8359   6712    260   -247    445       O  
ATOM   7207  N   GLY A 882     -26.338 -17.197 -43.386  1.00 30.76           N  
ANISOU 7207  N   GLY A 882     4369   4312   3006     93   -148    434       N  
ATOM   7208  CA  GLY A 882     -25.506 -16.258 -44.131  1.00 28.70           C  
ANISOU 7208  CA  GLY A 882     4176   4023   2706     78   -164    469       C  
ATOM   7209  C   GLY A 882     -24.789 -16.909 -45.302  1.00 27.60           C  
ANISOU 7209  C   GLY A 882     4018   3932   2537      0   -147    439       C  
ATOM   7210  O   GLY A 882     -24.782 -16.352 -46.402  1.00 26.58           O  
ANISOU 7210  O   GLY A 882     3906   3850   2342    -12   -169    472       O  
ATOM   7211  N   PHE A 883     -24.187 -18.080 -45.069  1.00 25.35           N  
ANISOU 7211  N   PHE A 883     3696   3640   2297    -46   -113    379       N  
ATOM   7212  CA  PHE A 883     -23.481 -18.814 -46.128  1.00 24.68           C  
ANISOU 7212  CA  PHE A 883     3579   3609   2190   -110    -99    324       C  
ATOM   7213  C   PHE A 883     -24.445 -19.227 -47.218  1.00 26.09           C  
ANISOU 7213  C   PHE A 883     3699   3889   2324   -119   -120    293       C  
ATOM   7214  O   PHE A 883     -24.179 -19.009 -48.398  1.00 26.35           O  
ANISOU 7214  O   PHE A 883     3724   4005   2283   -147   -130    289       O  
ATOM   7215  CB  PHE A 883     -22.780 -20.094 -45.621  1.00 22.09           C  
ANISOU 7215  CB  PHE A 883     3218   3242   1934   -140    -67    254       C  
ATOM   7216  CG  PHE A 883     -21.815 -19.879 -44.484  1.00 20.96           C  
ANISOU 7216  CG  PHE A 883     3115   3017   1830   -126    -47    272       C  
ATOM   7217  CD1 PHE A 883     -21.289 -18.617 -44.200  1.00 20.31           C  
ANISOU 7217  CD1 PHE A 883     3095   2907   1717   -114    -52    324       C  
ATOM   7218  CD2 PHE A 883     -21.406 -20.963 -43.712  1.00 21.53           C  
ANISOU 7218  CD2 PHE A 883     3163   3042   1976   -126    -25    233       C  
ATOM   7219  CE1 PHE A 883     -20.397 -18.430 -43.143  1.00 20.10           C  
ANISOU 7219  CE1 PHE A 883     3094   2821   1723   -102    -35    325       C  
ATOM   7220  CE2 PHE A 883     -20.504 -20.794 -42.660  1.00 23.62           C  
ANISOU 7220  CE2 PHE A 883     3457   3253   2266   -106     -9    247       C  
ATOM   7221  CZ  PHE A 883     -20.001 -19.523 -42.368  1.00 18.31           C  
ANISOU 7221  CZ  PHE A 883     2835   2568   1554    -94    -13    286       C  
ATOM   7222  N   THR A 884     -25.564 -19.820 -46.803  1.00 25.41           N  
ANISOU 7222  N   THR A 884     3565   3811   2279    -98   -125    272       N  
ATOM   7223  CA  THR A 884     -26.479 -20.491 -47.719  1.00 24.43           C  
ANISOU 7223  CA  THR A 884     3365   3786   2133   -117   -141    214       C  
ATOM   7224  C   THR A 884     -27.288 -19.515 -48.577  1.00 27.48           C  
ANISOU 7224  C   THR A 884     3751   4269   2420    -76   -181    261       C  
ATOM   7225  O   THR A 884     -27.509 -19.775 -49.765  1.00 28.39           O  
ANISOU 7225  O   THR A 884     3818   4498   2473    -99   -197    219       O  
ATOM   7226  CB  THR A 884     -27.404 -21.499 -46.988  1.00 23.36           C  
ANISOU 7226  CB  THR A 884     3169   3629   2078   -126   -130    175       C  
ATOM   7227  OG1 THR A 884     -28.067 -20.850 -45.900  1.00 23.30           O  
ANISOU 7227  OG1 THR A 884     3183   3590   2081    -70   -134    243       O  
ATOM   7228  CG2 THR A 884     -26.596 -22.666 -46.441  1.00 22.07           C  
ANISOU 7228  CG2 THR A 884     2998   3375   2011   -172    -97    125       C  
ATOM   7229  N   SER A 885     -27.715 -18.397 -47.993  1.00 28.11           N  
ANISOU 7229  N   SER A 885     3884   4312   2486     -9   -202    344       N  
ATOM   7230  CA  SER A 885     -28.380 -17.348 -48.773  1.00 31.57           C  
ANISOU 7230  CA  SER A 885     4339   4822   2836     46   -249    407       C  
ATOM   7231  C   SER A 885     -27.420 -16.744 -49.803  1.00 33.47           C  
ANISOU 7231  C   SER A 885     4627   5088   3002     13   -254    454       C  
ATOM   7232  O   SER A 885     -27.806 -16.500 -50.945  1.00 34.54           O  
ANISOU 7232  O   SER A 885     4738   5338   3046     20   -282    474       O  
ATOM   7233  CB  SER A 885     -28.985 -16.262 -47.878  1.00 32.09           C  
ANISOU 7233  CB  SER A 885     4454   4823   2916    136   -276    475       C  
ATOM   7234  OG  SER A 885     -28.031 -15.758 -46.965  1.00 35.60           O  
ANISOU 7234  OG  SER A 885     4974   5141   3412    135   -257    507       O  
ATOM   7235  N   ALA A 886     -26.164 -16.539 -49.412  1.00 32.74           N  
ANISOU 7235  N   ALA A 886     4593   4906   2940    -27   -225    473       N  
ATOM   7236  CA  ALA A 886     -25.149 -16.078 -50.359  1.00 33.01           C  
ANISOU 7236  CA  ALA A 886     4660   4979   2904    -80   -219    514       C  
ATOM   7237  C   ALA A 886     -24.961 -17.091 -51.490  1.00 31.77           C  
ANISOU 7237  C   ALA A 886     4418   4964   2689   -137   -206    427       C  
ATOM   7238  O   ALA A 886     -24.851 -16.710 -52.649  1.00 32.89           O  
ANISOU 7238  O   ALA A 886     4551   5220   2727   -155   -221    465       O  
ATOM   7239  CB  ALA A 886     -23.824 -15.809 -49.652  1.00 31.71           C  
ANISOU 7239  CB  ALA A 886     4554   4706   2788   -122   -186    526       C  
ATOM   7240  N   ALA A 887     -24.938 -18.376 -51.144  1.00 31.60           N  
ANISOU 7240  N   ALA A 887     4333   4935   2737   -161   -182    313       N  
ATOM   7241  CA  ALA A 887     -24.739 -19.445 -52.131  1.00 32.13           C  
ANISOU 7241  CA  ALA A 887     4313   5121   2773   -210   -173    199       C  
ATOM   7242  C   ALA A 887     -26.021 -19.875 -52.857  1.00 33.77           C  
ANISOU 7242  C   ALA A 887     4440   5451   2941   -190   -204    147       C  
ATOM   7243  O   ALA A 887     -25.968 -20.729 -53.746  1.00 34.56           O  
ANISOU 7243  O   ALA A 887     4459   5662   3009   -227   -204     38       O  
ATOM   7244  CB  ALA A 887     -24.083 -20.636 -51.478  1.00 29.97           C  
ANISOU 7244  CB  ALA A 887     4014   4768   2606   -243   -140     96       C  
ATOM   7245  N   LYS A 888     -27.158 -19.281 -52.476  1.00 35.70           N  
ANISOU 7245  N   LYS A 888     4699   5683   3184   -129   -233    212       N  
ATOM   7246  CA  LYS A 888     -28.488 -19.593 -53.042  1.00 37.33           C  
ANISOU 7246  CA  LYS A 888     4823   6011   3351   -103   -266    166       C  
ATOM   7247  C   LYS A 888     -28.858 -21.059 -52.812  1.00 37.33           C  
ANISOU 7247  C   LYS A 888     4736   6005   3443   -150   -248     25       C  
ATOM   7248  O   LYS A 888     -29.352 -21.747 -53.716  1.00 38.81           O  
ANISOU 7248  O   LYS A 888     4830   6320   3595   -175   -263    -76       O  
ATOM   7249  CB  LYS A 888     -28.586 -19.242 -54.534  1.00 37.08           C  
ANISOU 7249  CB  LYS A 888     4751   6163   3173   -100   -296    174       C  
ATOM   7250  CG  LYS A 888     -27.812 -18.012 -54.968  1.00 43.37           C  
ANISOU 7250  CG  LYS A 888     5635   6963   3882    -90   -303    311       C  
ATOM   7251  CD  LYS A 888     -28.679 -16.783 -55.136  1.00 48.18           C  
ANISOU 7251  CD  LYS A 888     6289   7594   4422     -6   -353    442       C  
ATOM   7252  CE  LYS A 888     -27.898 -15.706 -55.880  1.00 50.56           C  
ANISOU 7252  CE  LYS A 888     6663   7924   4624    -17   -362    578       C  
ATOM   7253  NZ  LYS A 888     -28.736 -14.540 -56.259  1.00 55.80           N  
ANISOU 7253  NZ  LYS A 888     7371   8618   5213     72   -421    713       N  
ATOM   7254  N   LEU A 889     -28.600 -21.518 -51.594  1.00 36.54           N  
ANISOU 7254  N   LEU A 889     4665   5755   3463   -164   -218     22       N  
ATOM   7255  CA  LEU A 889     -28.912 -22.875 -51.161  1.00 37.99           C  
ANISOU 7255  CA  LEU A 889     4785   5890   3759   -213   -199    -82       C  
ATOM   7256  C   LEU A 889     -29.875 -22.817 -49.990  1.00 37.55           C  
ANISOU 7256  C   LEU A 889     4730   5770   3766   -188   -195    -31       C  
ATOM   7257  O   LEU A 889     -29.977 -21.798 -49.306  1.00 36.76           O  
ANISOU 7257  O   LEU A 889     4692   5632   3643   -128   -200     71       O  
ATOM   7258  CB  LEU A 889     -27.631 -23.595 -50.713  1.00 37.27           C  
ANISOU 7258  CB  LEU A 889     4727   5681   3754   -254   -165   -122       C  
ATOM   7259  CG  LEU A 889     -26.882 -24.617 -51.581  1.00 39.23           C  
ANISOU 7259  CG  LEU A 889     4922   5965   4020   -305   -160   -256       C  
ATOM   7260  CD1 LEU A 889     -27.436 -24.792 -52.987  1.00 44.45           C  
ANISOU 7260  CD1 LEU A 889     5495   6804   4589   -318   -189   -348       C  
ATOM   7261  CD2 LEU A 889     -25.401 -24.286 -51.629  1.00 37.93           C  
ANISOU 7261  CD2 LEU A 889     4813   5771   3828   -305   -141   -237       C  
ATOM   7262  N   ASP A 890     -30.579 -23.919 -49.762  1.00 37.76           N  
ANISOU 7262  N   ASP A 890     4683   5790   3875   -237   -186   -108       N  
ATOM   7263  CA  ASP A 890     -31.372 -24.076 -48.558  1.00 38.40           C  
ANISOU 7263  CA  ASP A 890     4753   5814   4025   -233   -171    -62       C  
ATOM   7264  C   ASP A 890     -30.733 -25.131 -47.655  1.00 36.87           C  
ANISOU 7264  C   ASP A 890     4576   5471   3961   -289   -133    -75       C  
ATOM   7265  O   ASP A 890     -30.328 -26.199 -48.122  1.00 34.00           O  
ANISOU 7265  O   ASP A 890     4182   5071   3666   -349   -128   -168       O  
ATOM   7266  CB  ASP A 890     -32.829 -24.411 -48.914  1.00 41.11           C  
ANISOU 7266  CB  ASP A 890     4991   6276   4352   -251   -191   -117       C  
ATOM   7267  CG  ASP A 890     -33.646 -23.166 -49.280  1.00 45.76           C  
ANISOU 7267  CG  ASP A 890     5574   6994   4817   -162   -230    -63       C  
ATOM   7268  OD1 ASP A 890     -33.624 -22.177 -48.506  1.00 50.02           O  
ANISOU 7268  OD1 ASP A 890     6179   7492   5333    -89   -233     36       O  
ATOM   7269  OD2 ASP A 890     -34.318 -23.173 -50.334  1.00 48.43           O  
ANISOU 7269  OD2 ASP A 890     5840   7477   5083   -158   -263   -123       O  
ATOM   7270  N   TYR A 891     -30.601 -24.815 -46.369  1.00 36.47           N  
ANISOU 7270  N   TYR A 891     4575   5337   3943   -260   -111     18       N  
ATOM   7271  CA  TYR A 891     -30.041 -25.776 -45.426  1.00 36.55           C  
ANISOU 7271  CA  TYR A 891     4603   5215   4069   -302    -78     29       C  
ATOM   7272  C   TYR A 891     -31.138 -26.663 -44.842  1.00 38.67           C  
ANISOU 7272  C   TYR A 891     4801   5477   4414   -361    -63     28       C  
ATOM   7273  O   TYR A 891     -30.861 -27.618 -44.122  1.00 38.48           O  
ANISOU 7273  O   TYR A 891     4783   5343   4496   -409    -38     45       O  
ATOM   7274  CB  TYR A 891     -29.201 -25.088 -44.334  1.00 37.58           C  
ANISOU 7274  CB  TYR A 891     4816   5270   4191   -246    -60    124       C  
ATOM   7275  CG  TYR A 891     -29.970 -24.155 -43.425  1.00 37.03           C  
ANISOU 7275  CG  TYR A 891     4751   5246   4072   -187    -60    206       C  
ATOM   7276  CD1 TYR A 891     -30.065 -22.798 -43.710  1.00 38.57           C  
ANISOU 7276  CD1 TYR A 891     4982   5501   4173   -114    -87    236       C  
ATOM   7277  CD2 TYR A 891     -30.589 -24.630 -42.274  1.00 37.77           C  
ANISOU 7277  CD2 TYR A 891     4811   5325   4215   -203    -35    254       C  
ATOM   7278  CE1 TYR A 891     -30.771 -21.940 -42.880  1.00 41.17           C  
ANISOU 7278  CE1 TYR A 891     5311   5868   4463    -46    -95    292       C  
ATOM   7279  CE2 TYR A 891     -31.298 -23.778 -41.437  1.00 40.07           C  
ANISOU 7279  CE2 TYR A 891     5093   5682   4451   -142    -36    313       C  
ATOM   7280  CZ  TYR A 891     -31.381 -22.437 -41.742  1.00 39.86           C  
ANISOU 7280  CZ  TYR A 891     5100   5707   4337    -58    -68    322       C  
ATOM   7281  OH  TYR A 891     -32.083 -21.593 -40.915  1.00 39.74           O  
ANISOU 7281  OH  TYR A 891     5072   5753   4275     16    -76    362       O  
ATOM   7282  N   GLU A 892     -32.383 -26.333 -45.166  1.00 41.46           N  
ANISOU 7282  N   GLU A 892     5086   5955   4711   -358    -80     14       N  
ATOM   7283  CA  GLU A 892     -33.534 -27.153 -44.810  1.00 44.52           C  
ANISOU 7283  CA  GLU A 892     5386   6370   5160   -431    -66     -1       C  
ATOM   7284  C   GLU A 892     -34.327 -27.451 -46.070  1.00 45.72           C  
ANISOU 7284  C   GLU A 892     5449   6637   5286   -470    -96   -117       C  
ATOM   7285  O   GLU A 892     -34.604 -26.547 -46.861  1.00 45.23           O  
ANISOU 7285  O   GLU A 892     5377   6698   5109   -406   -129   -135       O  
ATOM   7286  CB  GLU A 892     -34.407 -26.446 -43.770  1.00 45.03           C  
ANISOU 7286  CB  GLU A 892     5429   6507   5173   -385    -55     89       C  
ATOM   7287  CG  GLU A 892     -33.744 -26.330 -42.405  1.00 46.52           C  
ANISOU 7287  CG  GLU A 892     5683   6601   5391   -358    -23    193       C  
ATOM   7288  CD  GLU A 892     -34.681 -25.840 -41.319  1.00 49.37           C  
ANISOU 7288  CD  GLU A 892     6000   7052   5706   -325     -8    264       C  
ATOM   7289  OE1 GLU A 892     -34.844 -26.568 -40.317  1.00 50.29           O  
ANISOU 7289  OE1 GLU A 892     6093   7132   5883   -382     29    325       O  
ATOM   7290  OE2 GLU A 892     -35.251 -24.735 -41.462  1.00 50.07           O  
ANISOU 7290  OE2 GLU A 892     6075   7252   5696   -240    -35    262       O  
ATOM   7291  N   LYS A 893     -34.675 -28.719 -46.267  1.00 48.55           N  
ANISOU 7291  N   LYS A 893     5743   6952   5752   -576    -87   -195       N  
ATOM   7292  CA  LYS A 893     -35.383 -29.122 -47.476  1.00 52.76           C  
ANISOU 7292  CA  LYS A 893     6181   7597   6269   -622   -117   -329       C  
ATOM   7293  C   LYS A 893     -36.762 -28.475 -47.553  1.00 53.89           C  
ANISOU 7293  C   LYS A 893     6239   7922   6315   -597   -133   -322       C  
ATOM   7294  O   LYS A 893     -37.624 -28.718 -46.705  1.00 55.81           O  
ANISOU 7294  O   LYS A 893     6430   8182   6594   -640   -109   -277       O  
ATOM   7295  CB  LYS A 893     -35.503 -30.644 -47.579  1.00 54.60           C  
ANISOU 7295  CB  LYS A 893     6361   7725   6659   -748   -106   -423       C  
ATOM   7296  CG  LYS A 893     -35.872 -31.109 -48.980  1.00 57.53           C  
ANISOU 7296  CG  LYS A 893     6642   8197   7019   -790   -142   -597       C  
ATOM   7297  CD  LYS A 893     -36.292 -32.568 -49.009  1.00 62.67           C  
ANISOU 7297  CD  LYS A 893     7223   8751   7838   -925   -136   -699       C  
ATOM   7298  CE  LYS A 893     -36.672 -32.986 -50.421  1.00 64.81           C  
ANISOU 7298  CE  LYS A 893     7393   9143   8090   -961   -176   -894       C  
ATOM   7299  NZ  LYS A 893     -37.339 -34.314 -50.442  1.00 68.21           N  
ANISOU 7299  NZ  LYS A 893     7738   9494   8684  -1104   -174  -1004       N  
ATOM   7300  N   LYS A 894     -36.949 -27.640 -48.568  1.00 54.94           N  
ANISOU 7300  N   LYS A 894     6353   8201   6319   -522   -173   -361       N  
ATOM   7301  CA  LYS A 894     -38.242 -27.015 -48.835  1.00 57.04           C  
ANISOU 7301  CA  LYS A 894     6532   8659   6484   -480   -201   -372       C  
ATOM   7302  C   LYS A 894     -39.238 -28.070 -49.317  1.00 57.49           C  
ANISOU 7302  C   LYS A 894     6453   8797   6595   -591   -204   -500       C  
ATOM   7303  O   LYS A 894     -38.842 -29.083 -49.903  1.00 58.10           O  
ANISOU 7303  O   LYS A 894     6508   8809   6760   -677   -203   -607       O  
ATOM   7304  CB  LYS A 894     -38.098 -25.898 -49.876  1.00 57.25           C  
ANISOU 7304  CB  LYS A 894     6581   8810   6360   -368   -249   -371       C  
ATOM   7305  CG  LYS A 894     -37.250 -26.281 -51.085  1.00 60.82           C  
ANISOU 7305  CG  LYS A 894     7044   9267   6800   -393   -265   -462       C  
ATOM   7306  CD  LYS A 894     -37.712 -25.562 -52.342  1.00 66.19           C  
ANISOU 7306  CD  LYS A 894     7674  10152   7326   -322   -317   -500       C  
ATOM   7307  CE  LYS A 894     -37.063 -26.160 -53.588  1.00 68.68           C  
ANISOU 7307  CE  LYS A 894     7958  10515   7623   -364   -331   -622       C  
ATOM   7308  NZ  LYS A 894     -37.835 -25.842 -54.823  1.00 69.59           N  
ANISOU 7308  NZ  LYS A 894     7975  10869   7599   -324   -381   -694       N  
ATOM   7309  N   ALA A 895     -40.522 -27.837 -49.058  1.00 56.51           N  
ANISOU 7309  N   ALA A 895     6232   8817   6424   -588   -210   -499       N  
ATOM   7310  CA  ALA A 895     -41.574 -28.745 -49.508  1.00 57.63           C  
ANISOU 7310  CA  ALA A 895     6228   9060   6607   -698   -214   -625       C  
ATOM   7311  C   ALA A 895     -41.670 -28.777 -51.035  1.00 57.61           C  
ANISOU 7311  C   ALA A 895     6162   9197   6529   -683   -264   -767       C  
ATOM   7312  O   ALA A 895     -41.387 -27.777 -51.706  1.00 57.60           O  
ANISOU 7312  O   ALA A 895     6202   9291   6394   -561   -301   -740       O  
ATOM   7313  CB  ALA A 895     -42.909 -28.354 -48.894  1.00 58.19           C  
ANISOU 7313  CB  ALA A 895     6201   9287   6621   -685   -210   -592       C  
ATOM   7314  N   SER A 896     -42.048 -29.931 -51.578  1.00 58.01           N  
ANISOU 7314  N   SER A 896     6112   9260   6669   -809   -265   -916       N  
ATOM   7315  CA  SER A 896     -42.294 -30.064 -53.018  1.00 59.42           C  
ANISOU 7315  CA  SER A 896     6199   9607   6771   -803   -314  -1076       C  
ATOM   7316  C   SER A 896     -43.549 -30.893 -53.313  1.00 59.64           C  
ANISOU 7316  C   SER A 896     6057   9761   6843   -920   -321  -1221       C  
ATOM   7317  O   SER A 896     -44.094 -31.557 -52.425  1.00 58.76           O  
ANISOU 7317  O   SER A 896     5907   9569   6852  -1032   -283  -1201       O  
ATOM   7318  CB  SER A 896     -41.068 -30.651 -53.737  1.00 59.30           C  
ANISOU 7318  CB  SER A 896     6241   9477   6812   -827   -319  -1161       C  
ATOM   7319  OG  SER A 896     -41.044 -32.066 -53.653  1.00 61.25           O  
ANISOU 7319  OG  SER A 896     6443   9586   7243   -975   -301  -1281       O  
ATOM   7320  N   LEU A 897     -43.992 -30.851 -54.568  1.00 60.21           N  
ANISOU 7320  N   LEU A 897     6024  10040   6814   -897   -370  -1366       N  
ATOM   7321  CA  LEU A 897     -45.159 -31.609 -55.028  1.00 60.89           C  
ANISOU 7321  CA  LEU A 897     5932  10275   6928  -1005   -386  -1535       C  
ATOM   7322  C   LEU A 897     -45.053 -33.118 -54.787  1.00 61.08           C  
ANISOU 7322  C   LEU A 897     5924  10109   7176  -1195   -355  -1647       C  
ATOM   7323  O   LEU A 897     -46.068 -33.804 -54.679  1.00 61.36           O  
ANISOU 7323  O   LEU A 897     5829  10202   7283  -1320   -348  -1740       O  
ATOM   7324  CB  LEU A 897     -45.425 -31.321 -56.510  1.00 61.79           C  
ANISOU 7324  CB  LEU A 897     5947  10644   6886   -936   -448  -1679       C  
ATOM   7325  CG  LEU A 897     -46.462 -30.262 -56.925  1.00 61.55           C  
ANISOU 7325  CG  LEU A 897     5828  10906   6653   -811   -494  -1655       C  
ATOM   7326  CD1 LEU A 897     -46.550 -29.059 -55.982  1.00 58.10           C  
ANISOU 7326  CD1 LEU A 897     5488  10447   6140   -683   -483  -1440       C  
ATOM   7327  CD2 LEU A 897     -46.183 -29.807 -58.357  1.00 62.36           C  
ANISOU 7327  CD2 LEU A 897     5900  11208   6587   -709   -553  -1734       C  
ATOM   7328  N   PHE A 898     -43.824 -33.619 -54.685  1.00 61.08           N  
ANISOU 7328  N   PHE A 898     6041   9878   7290  -1215   -339  -1637       N  
ATOM   7329  CA  PHE A 898     -43.566 -35.036 -54.421  1.00 63.42           C  
ANISOU 7329  CA  PHE A 898     6332   9947   7815  -1377   -316  -1729       C  
ATOM   7330  C   PHE A 898     -44.001 -35.526 -53.035  1.00 65.25           C  
ANISOU 7330  C   PHE A 898     6585  10015   8194  -1491   -261  -1599       C  
ATOM   7331  O   PHE A 898     -44.244 -36.726 -52.854  1.00 65.73           O  
ANISOU 7331  O   PHE A 898     6598   9933   8442  -1652   -247  -1682       O  
ATOM   7332  CB  PHE A 898     -42.093 -35.369 -54.674  1.00 63.58           C  
ANISOU 7332  CB  PHE A 898     6475   9777   7908  -1342   -320  -1749       C  
ATOM   7333  CG  PHE A 898     -41.761 -35.535 -56.126  1.00 64.17           C  
ANISOU 7333  CG  PHE A 898     6483   9987   7912  -1308   -370  -1954       C  
ATOM   7334  CD1 PHE A 898     -41.833 -36.790 -56.726  1.00 66.79           C  
ANISOU 7334  CD1 PHE A 898     6728  10257   8393  -1427   -391  -2178       C  
ATOM   7335  CD2 PHE A 898     -41.402 -34.437 -56.901  1.00 63.03           C  
ANISOU 7335  CD2 PHE A 898     6358  10040   7552  -1159   -399  -1924       C  
ATOM   7336  CE1 PHE A 898     -41.540 -36.957 -58.075  1.00 67.22           C  
ANISOU 7336  CE1 PHE A 898     6706  10463   8372  -1391   -439  -2385       C  
ATOM   7337  CE2 PHE A 898     -41.108 -34.591 -58.252  1.00 67.07           C  
ANISOU 7337  CE2 PHE A 898     6796  10707   7979  -1129   -444  -2108       C  
ATOM   7338  CZ  PHE A 898     -41.177 -35.858 -58.840  1.00 67.18           C  
ANISOU 7338  CZ  PHE A 898     6713  10678   8133  -1242   -464  -2347       C  
ATOM   7339  N   ASP A 899     -44.108 -34.600 -52.077  1.00 64.86           N  
ANISOU 7339  N   ASP A 899     6599   9988   8056  -1408   -232  -1400       N  
ATOM   7340  CA  ASP A 899     -44.611 -34.898 -50.729  1.00 67.36           C  
ANISOU 7340  CA  ASP A 899     6919  10209   8466  -1501   -178  -1260       C  
ATOM   7341  C   ASP A 899     -46.092 -35.292 -50.746  1.00 71.38           C  
ANISOU 7341  C   ASP A 899     7251  10886   8983  -1624   -173  -1343       C  
ATOM   7342  O   ASP A 899     -46.859 -34.890 -49.870  1.00 72.53           O  
ANISOU 7342  O   ASP A 899     7356  11125   9078  -1631   -142  -1229       O  
ATOM   7343  CB  ASP A 899     -44.429 -33.686 -49.803  1.00 64.64           C  
ANISOU 7343  CB  ASP A 899     6664   9899   7995  -1363   -157  -1056       C  
ATOM   7344  CG  ASP A 899     -42.979 -33.279 -49.636  1.00 62.60           C  
ANISOU 7344  CG  ASP A 899     6577   9474   7735  -1255   -155   -963       C  
ATOM   7345  OD1 ASP A 899     -42.724 -32.060 -49.521  1.00 59.76           O  
ANISOU 7345  OD1 ASP A 899     6280   9197   7229  -1105   -166   -867       O  
ATOM   7346  OD2 ASP A 899     -42.097 -34.168 -49.613  1.00 62.81           O  
ANISOU 7346  OD2 ASP A 899     6671   9284   7909  -1320   -145   -990       O  
ATOM   7347  N   MET A 900     -46.488 -36.085 -51.735  1.00 75.08           N  
ANISOU 7347  N   MET A 900     7607  11406   9513  -1723   -204  -1551       N  
ATOM   7348  CA  MET A 900     -47.896 -36.374 -51.958  1.00 79.22           C  
ANISOU 7348  CA  MET A 900     7945  12132  10021  -1831   -209  -1661       C  
ATOM   7349  C   MET A 900     -48.115 -37.844 -52.296  1.00 82.66           C  
ANISOU 7349  C   MET A 900     8303  12434  10672  -2040   -208  -1830       C  
ATOM   7350  O   MET A 900     -49.248 -38.276 -52.503  1.00 85.02           O  
ANISOU 7350  O   MET A 900     8438  12875  10991  -2165   -210  -1944       O  
ATOM   7351  CB  MET A 900     -48.416 -35.480 -53.082  1.00 78.86           C  
ANISOU 7351  CB  MET A 900     7803  12401   9761  -1695   -268  -1775       C  
ATOM   7352  CG  MET A 900     -49.610 -34.637 -52.700  1.00 80.06           C  
ANISOU 7352  CG  MET A 900     7848  12812   9759  -1640   -265  -1713       C  
ATOM   7353  SD  MET A 900     -49.415 -32.936 -53.267  1.00 78.60           S  
ANISOU 7353  SD  MET A 900     7717  12842   9306  -1363   -320  -1643       S  
ATOM   7354  CE  MET A 900     -51.017 -32.257 -52.833  1.00 80.40           C  
ANISOU 7354  CE  MET A 900     7781  13373   9395  -1327   -323  -1622       C  
ATOM   7355  N   PHE A 901     -47.024 -38.605 -52.326  1.00 85.55           N  
ANISOU 7355  N   PHE A 901     8783  12521  11202  -2076   -208  -1849       N  
ATOM   7356  CA  PHE A 901     -47.047 -39.998 -52.766  1.00 90.82           C  
ANISOU 7356  CA  PHE A 901     9396  13023  12090  -2251   -221  -2031       C  
ATOM   7357  C   PHE A 901     -46.418 -40.949 -51.742  1.00 94.40           C  
ANISOU 7357  C   PHE A 901     9969  13115  12782  -2367   -179  -1904       C  
ATOM   7358  O   PHE A 901     -45.771 -40.509 -50.786  1.00 92.54           O  
ANISOU 7358  O   PHE A 901     9870  12764  12526  -2290   -144  -1686       O  
ATOM   7359  CB  PHE A 901     -46.314 -40.135 -54.109  1.00 89.97           C  
ANISOU 7359  CB  PHE A 901     9287  12939  11958  -2171   -283  -2244       C  
ATOM   7360  CG  PHE A 901     -46.936 -39.349 -55.235  1.00 88.32           C  
ANISOU 7360  CG  PHE A 901     8948  13087  11522  -2070   -330  -2383       C  
ATOM   7361  CD1 PHE A 901     -47.904 -39.926 -56.053  1.00 89.12           C  
ANISOU 7361  CD1 PHE A 901     8865  13354  11644  -2181   -363  -2615       C  
ATOM   7362  CD2 PHE A 901     -46.542 -38.037 -55.488  1.00 85.24           C  
ANISOU 7362  CD2 PHE A 901     8620  12866  10901  -1865   -346  -2280       C  
ATOM   7363  CE1 PHE A 901     -48.477 -39.210 -57.096  1.00 88.27           C  
ANISOU 7363  CE1 PHE A 901     8631  13590  11317  -2078   -411  -2739       C  
ATOM   7364  CE2 PHE A 901     -47.110 -37.312 -56.527  1.00 84.35           C  
ANISOU 7364  CE2 PHE A 901     8394  13079  10578  -1765   -395  -2388       C  
ATOM   7365  CZ  PHE A 901     -48.079 -37.900 -57.334  1.00 86.54           C  
ANISOU 7365  CZ  PHE A 901     8483  13535  10864  -1866   -428  -2617       C  
ATOM   7366  N   ASP A 902     -46.620 -42.252 -51.966  1.00 60.44           N  
ATOM   7367  CA  ASP A 902     -45.986 -43.338 -51.197  1.00 63.86           C  
ATOM   7368  C   ASP A 902     -46.351 -43.307 -49.709  1.00 64.47           C  
ATOM   7369  O   ASP A 902     -46.372 -44.344 -49.042  1.00 64.47           O  
ATOM   7370  CB  ASP A 902     -44.454 -43.339 -51.395  1.00 65.73           C  
ATOM   7371  CG  ASP A 902     -43.806 -44.683 -51.046  1.00 70.05           C  
ATOM   7372  OD1 ASP A 902     -44.216 -45.720 -51.620  1.00 70.81           O  
ATOM   7373  OD2 ASP A 902     -42.871 -44.697 -50.209  1.00 71.27           O  
TER    7374      ASP A 902                                                      
ATOM   7375  P    DC T   3      10.359   0.903 -27.800  1.00 78.81           P  
ANISOU 7375  P    DC T   3     9488  10191  10267    864    -42   -282       P  
ATOM   7376  OP1  DC T   3      10.641   2.327 -28.116  1.00 76.98           O  
ANISOU 7376  OP1  DC T   3     9217   9892  10138    859   -123   -301       O  
ATOM   7377  OP2  DC T   3       9.808   0.549 -26.468  1.00 79.07           O  
ANISOU 7377  OP2  DC T   3     9497  10296  10252    927    -24   -341       O  
ATOM   7378  O5'  DC T   3       9.375   0.277 -28.911  1.00 73.65           O  
ANISOU 7378  O5'  DC T   3     8871   9528   9583    804    -10   -218       O  
ATOM   7379  C5'  DC T   3       8.225   1.032 -29.293  1.00 65.77           C  
ANISOU 7379  C5'  DC T   3     7851   8504   8634    792    -57   -223       C  
ATOM   7380  C4'  DC T   3       7.346   0.446 -30.397  1.00 58.21           C  
ANISOU 7380  C4'  DC T   3     6928   7543   7646    732    -28   -161       C  
ATOM   7381  O4'  DC T   3       6.011   0.985 -30.240  1.00 59.26           O  
ANISOU 7381  O4'  DC T   3     7033   7675   7807    746    -63   -186       O  
ATOM   7382  C3'  DC T   3       7.641   0.871 -31.830  1.00 49.71           C  
ANISOU 7382  C3'  DC T   3     5862   6414   6611    660    -52    -95       C  
ATOM   7383  O3'  DC T   3       6.857   0.101 -32.762  1.00 34.78           O  
ANISOU 7383  O3'  DC T   3     4004   4538   4671    606    -11    -43       O  
ATOM   7384  C2'  DC T   3       7.171   2.328 -31.802  1.00 52.23           C  
ANISOU 7384  C2'  DC T   3     6129   6685   7030    672   -138   -119       C  
ATOM   7385  C1'  DC T   3       5.944   2.249 -30.888  1.00 58.28           C  
ANISOU 7385  C1'  DC T   3     6877   7487   7778    722   -137   -176       C  
ATOM   7386  N1   DC T   3       5.845   3.287 -29.798  1.00 62.82           N  
ANISOU 7386  N1   DC T   3     7395   8054   8421    787   -197   -259       N  
ATOM   7387  C2   DC T   3       4.587   3.572 -29.232  1.00 63.96           C  
ANISOU 7387  C2   DC T   3     7509   8217   8576    821   -217   -308       C  
ATOM   7388  O2   DC T   3       3.576   2.981 -29.644  1.00 63.46           O  
ANISOU 7388  O2   DC T   3     7469   8175   8468    796   -187   -275       O  
ATOM   7389  N3   DC T   3       4.512   4.503 -28.241  1.00 65.16           N  
ANISOU 7389  N3   DC T   3     7603   8367   8790    881   -270   -393       N  
ATOM   7390  C4   DC T   3       5.615   5.130 -27.812  1.00 65.73           C  
ANISOU 7390  C4   DC T   3     7648   8416   8912    907   -303   -431       C  
ATOM   7391  N4   DC T   3       5.489   6.037 -26.835  1.00 65.12           N  
ANISOU 7391  N4   DC T   3     7508   8339   8896    966   -355   -524       N  
ATOM   7392  C5   DC T   3       6.902   4.852 -28.368  1.00 64.97           C  
ANISOU 7392  C5   DC T   3     7583   8297   8804    873   -283   -377       C  
ATOM   7393  C6   DC T   3       6.965   3.939 -29.345  1.00 63.73           C  
ANISOU 7393  C6   DC T   3     7484   8146   8586    814   -230   -293       C  
HETATM 7394  P   2PR T   4       7.307  -1.303 -33.382  1.00 25.94           P  
ANISOU 7394  P   2PR T   4     2935   3449   3471    564     70      1       P  
HETATM 7395  OP1 2PR T   4       9.092  -1.025 -33.227  1.00 29.18           O  
ANISOU 7395  OP1 2PR T   4     3343   3838   3905    573     62     -2       O  
HETATM 7396  OP2 2PR T   4       6.343  -2.295 -32.202  1.00 32.52           O  
ANISOU 7396  OP2 2PR T   4     3776   4339   4241    620    121    -41       O  
HETATM 7397  O5' 2PR T   4       6.537  -0.926 -34.860  1.00 31.79           O  
ANISOU 7397  O5' 2PR T   4     3677   4168   4233    488     45     61       O  
HETATM 7398  C5' 2PR T   4       5.141  -1.074 -35.049  1.00 25.20           C  
ANISOU 7398  C5' 2PR T   4     2842   3348   3384    478     48     65       C  
HETATM 7399  C4' 2PR T   4       4.995  -0.604 -36.480  1.00 27.76           C  
ANISOU 7399  C4' 2PR T   4     3163   3653   3734    404     19    129       C  
HETATM 7400  O4' 2PR T   4       5.662  -1.506 -37.361  1.00 27.71           O  
ANISOU 7400  O4' 2PR T   4     3189   3669   3672    350     74    168       O  
HETATM 7401  C3' 2PR T   4       3.564  -0.506 -36.934  1.00 26.44           C  
ANISOU 7401  C3' 2PR T   4     2989   3492   3566    380      7    147       C  
HETATM 7402  O3' 2PR T   4       3.092   0.809 -36.637  1.00 27.12           O  
ANISOU 7402  O3' 2PR T   4     3029   3537   3737    405    -72    133       O  
HETATM 7403  C2' 2PR T   4       3.712  -0.715 -38.417  1.00 28.80           C  
ANISOU 7403  C2' 2PR T   4     3299   3800   3843    297     18    215       C  
HETATM 7404  C1' 2PR T   4       4.879  -1.681 -38.533  1.00 28.15           C  
ANISOU 7404  C1' 2PR T   4     3249   3740   3705    285     80    215       C  
HETATM 7405  N9  2PR T   4       4.302  -3.048 -38.593  1.00 23.67           N  
ANISOU 7405  N9  2PR T   4     2716   3215   3063    275    155    205       N  
HETATM 7406  C8  2PR T   4       4.343  -4.013 -37.653  1.00 21.69           C  
ANISOU 7406  C8  2PR T   4     2486   2982   2772    321    209    165       C  
HETATM 7407  N7  2PR T   4       3.664  -5.089 -38.119  1.00 25.84           N  
ANISOU 7407  N7  2PR T   4     3035   3539   3245    290    265    174       N  
HETATM 7408  C5  2PR T   4       3.207  -4.789 -39.365  1.00 22.88           C  
ANISOU 7408  C5  2PR T   4     2655   3170   2870    224    246    216       C  
HETATM 7409  C6  2PR T   4       2.471  -5.480 -40.325  1.00 21.60           C  
ANISOU 7409  C6  2PR T   4     2504   3039   2665    168    281    238       C  
HETATM 7410  N1  2PR T   4       2.159  -4.875 -41.489  1.00 21.13           N  
ANISOU 7410  N1  2PR T   4     2427   2987   2613    105    246    284       N  
HETATM 7411  C2  2PR T   4       2.566  -3.603 -41.737  1.00 24.30           C  
ANISOU 7411  C2  2PR T   4     2800   3363   3071     96    177    315       C  
HETATM 7412  N2  2PR T   4       2.251  -3.007 -42.911  1.00 24.46           N  
ANISOU 7412  N2  2PR T   4     2798   3397   3101     31    141    371       N  
HETATM 7413  N3  2PR T   4       3.296  -2.911 -40.825  1.00 20.35           N  
ANISOU 7413  N3  2PR T   4     2288   2824   2621    151    142    292       N  
HETATM 7414  C4  2PR T   4       3.611  -3.490 -39.643  1.00 22.18           C  
ANISOU 7414  C4  2PR T   4     2537   3052   2840    215    176    240       C  
ATOM   7415  P    DT T   5       1.536   1.085 -36.484  1.00 24.12           P  
ANISOU 7415  P    DT T   5     2631   3159   3374    416    -95    120       P  
ATOM   7416  OP1  DT T   5       1.379   2.423 -35.876  1.00 28.58           O  
ANISOU 7416  OP1  DT T   5     3144   3678   4038    459   -174     84       O  
ATOM   7417  OP2  DT T   5       0.892  -0.092 -35.873  1.00 26.83           O  
ANISOU 7417  OP2  DT T   5     3006   3551   3638    443    -29     88       O  
ATOM   7418  O5'  DT T   5       1.019   1.144 -38.001  1.00 24.59           O  
ANISOU 7418  O5'  DT T   5     2694   3220   3430    332   -103    199       O  
ATOM   7419  C5'  DT T   5       1.476   2.110 -38.973  1.00 24.83           C  
ANISOU 7419  C5'  DT T   5     2694   3217   3523    282   -161    260       C  
ATOM   7420  C4'  DT T   5       0.802   1.847 -40.316  1.00 20.60           C  
ANISOU 7420  C4'  DT T   5     2164   2709   2953    203   -151    331       C  
ATOM   7421  O4'  DT T   5       1.203   0.534 -40.780  1.00 24.37           O  
ANISOU 7421  O4'  DT T   5     2688   3239   3333    170    -70    339       O  
ATOM   7422  C3'  DT T   5      -0.716   1.763 -40.257  1.00 22.45           C  
ANISOU 7422  C3'  DT T   5     2395   2954   3181    208   -153    324       C  
ATOM   7423  O3'  DT T   5      -1.305   3.052 -40.409  1.00 24.45           O  
ANISOU 7423  O3'  DT T   5     2597   3161   3532    206   -235    347       O  
ATOM   7424  C2'  DT T   5      -1.065   0.853 -41.426  1.00 20.67           C  
ANISOU 7424  C2'  DT T   5     2197   2781   2874    135   -103    374       C  
ATOM   7425  C1'  DT T   5       0.126  -0.086 -41.467  1.00 23.08           C  
ANISOU 7425  C1'  DT T   5     2539   3114   3117    128    -40    363       C  
ATOM   7426  N1   DT T   5      -0.182  -1.435 -40.901  1.00 22.80           N  
ANISOU 7426  N1   DT T   5     2546   3114   3005    154     38    315       N  
ATOM   7427  C2   DT T   5      -0.818  -2.321 -41.737  1.00 20.54           C  
ANISOU 7427  C2   DT T   5     2279   2871   2654    102     85    337       C  
ATOM   7428  O2   DT T   5      -1.126  -2.055 -42.880  1.00 23.44           O  
ANISOU 7428  O2   DT T   5     2632   3256   3017     37     67    391       O  
ATOM   7429  N3   DT T   5      -1.071  -3.552 -41.193  1.00 22.70           N  
ANISOU 7429  N3   DT T   5     2587   3170   2870    128    154    296       N  
ATOM   7430  C4   DT T   5      -0.768  -3.977 -39.912  1.00 23.76           C  
ANISOU 7430  C4   DT T   5     2734   3295   2999    198    180    243       C  
ATOM   7431  O4   DT T   5      -1.054  -5.109 -39.534  1.00 25.69           O  
ANISOU 7431  O4   DT T   5     3003   3564   3194    213    241    219       O  
ATOM   7432  C5   DT T   5      -0.109  -3.003 -39.065  1.00 24.13           C  
ANISOU 7432  C5   DT T   5     2758   3305   3105    250    129    220       C  
ATOM   7433  C7   DT T   5       0.255  -3.372 -37.648  1.00 19.12           C  
ANISOU 7433  C7   DT T   5     2130   2672   2463    326    153    163       C  
ATOM   7434  C6   DT T   5       0.153  -1.785 -39.593  1.00 22.77           C  
ANISOU 7434  C6   DT T   5     2554   3101   2996    227     61    253       C  
ATOM   7435  P    DC T   6      -2.863   3.242 -40.142  1.00 26.54           P  
ANISOU 7435  P    DC T   6     2847   3424   3815    225   -254    329       P  
ATOM   7436  OP1  DC T   6      -3.124   4.696 -40.079  1.00 26.93           O  
ANISOU 7436  OP1  DC T   6     2835   3410   3989    237   -345    339       O  
ATOM   7437  OP2  DC T   6      -3.260   2.356 -39.020  1.00 26.09           O  
ANISOU 7437  OP2  DC T   6     2821   3396   3698    285   -199    252       O  
ATOM   7438  O5'  DC T   6      -3.569   2.634 -41.444  1.00 27.26           O  
ANISOU 7438  O5'  DC T   6     2955   3561   3842    145   -224    398       O  
ATOM   7439  C5'  DC T   6      -3.378   3.150 -42.767  1.00 27.71           C  
ANISOU 7439  C5'  DC T   6     2987   3621   3920     68   -259    488       C  
ATOM   7440  C4'  DC T   6      -4.312   2.440 -43.745  1.00 25.06           C  
ANISOU 7440  C4'  DC T   6     2669   3342   3511      7   -223    531       C  
ATOM   7441  O4'  DC T   6      -4.141   0.996 -43.677  1.00 26.32           O  
ANISOU 7441  O4'  DC T   6     2883   3555   3563      5   -133    495       O  
ATOM   7442  C3'  DC T   6      -5.797   2.656 -43.511  1.00 24.93           C  
ANISOU 7442  C3'  DC T   6     2639   3317   3518     24   -244    520       C  
ATOM   7443  O3'  DC T   6      -6.431   2.573 -44.769  1.00 25.59           O  
ANISOU 7443  O3'  DC T   6     2712   3441   3571    -53   -246    594       O  
ATOM   7444  C2'  DC T   6      -6.171   1.491 -42.591  1.00 25.35           C  
ANISOU 7444  C2'  DC T   6     2739   3398   3496     74   -172    443       C  
ATOM   7445  C1'  DC T   6      -5.321   0.376 -43.190  1.00 23.32           C  
ANISOU 7445  C1'  DC T   6     2522   3191   3148     32   -101    455       C  
ATOM   7446  N1   DC T   6      -4.982  -0.737 -42.249  1.00 23.57           N  
ANISOU 7446  N1   DC T   6     2597   3239   3120     82    -31    387       N  
ATOM   7447  C2   DC T   6      -5.240  -2.069 -42.640  1.00 23.59           C  
ANISOU 7447  C2   DC T   6     2637   3292   3033     52     44    382       C  
ATOM   7448  O2   DC T   6      -5.744  -2.325 -43.748  1.00 26.44           O  
ANISOU 7448  O2   DC T   6     2996   3688   3360    -14     54    425       O  
ATOM   7449  N3   DC T   6      -4.930  -3.071 -41.779  1.00 21.63           N  
ANISOU 7449  N3   DC T   6     2421   3054   2742     97    105    328       N  
ATOM   7450  C4   DC T   6      -4.388  -2.808 -40.577  1.00 23.65           C  
ANISOU 7450  C4   DC T   6     2674   3282   3028    167     94    282       C  
ATOM   7451  N4   DC T   6      -4.113  -3.862 -39.789  1.00 21.25           N  
ANISOU 7451  N4   DC T   6     2399   2997   2678    205    156    240       N  
ATOM   7452  C5   DC T   6      -4.105  -1.465 -40.155  1.00 19.86           C  
ANISOU 7452  C5   DC T   6     2158   2757   2632    199     20    278       C  
ATOM   7453  C6   DC T   6      -4.418  -0.476 -41.019  1.00 22.68           C  
ANISOU 7453  C6   DC T   6     2482   3094   3042    154    -41    331       C  
ATOM   7454  P    DG T   7      -7.987   2.846 -45.011  1.00 27.85           P  
ANISOU 7454  P    DG T   7     2977   3728   3876    -65   -273    615       P  
ATOM   7455  OP1  DG T   7      -8.111   3.523 -46.316  1.00 28.77           O  
ANISOU 7455  OP1  DG T   7     3052   3859   4020   -144   -321    716       O  
ATOM   7456  OP2  DG T   7      -8.583   3.482 -43.818  1.00 32.72           O  
ANISOU 7456  OP2  DG T   7     3575   4288   4571     12   -312    554       O  
ATOM   7457  O5'  DG T   7      -8.568   1.364 -45.139  1.00 31.26           O  
ANISOU 7457  O5'  DG T   7     3462   4226   4190    -79   -185    584       O  
ATOM   7458  C5'  DG T   7      -8.172   0.557 -46.251  1.00 31.19           C  
ANISOU 7458  C5'  DG T   7     3473   4282   4096   -151   -137    624       C  
ATOM   7459  C4'  DG T   7      -9.123  -0.604 -46.488  1.00 31.48           C  
ANISOU 7459  C4'  DG T   7     3542   4371   4047   -170    -73    603       C  
ATOM   7460  O4'  DG T   7      -8.861  -1.694 -45.557  1.00 31.80           O  
ANISOU 7460  O4'  DG T   7     3629   4415   4039   -118     -5    526       O  
ATOM   7461  C3'  DG T   7     -10.600  -0.300 -46.328  1.00 34.29           C  
ANISOU 7461  C3'  DG T   7     3882   4716   4428   -159   -100    605       C  
ATOM   7462  O3'  DG T   7     -11.300  -1.104 -47.282  1.00 35.38           O  
ANISOU 7462  O3'  DG T   7     4033   4920   4490   -220    -59    630       O  
ATOM   7463  C2'  DG T   7     -10.880  -0.687 -44.866  1.00 31.19           C  
ANISOU 7463  C2'  DG T   7     3516   4294   4042    -71    -75    520       C  
ATOM   7464  C1'  DG T   7      -9.941  -1.872 -44.655  1.00 27.49           C  
ANISOU 7464  C1'  DG T   7     3091   3853   3500    -65      1    481       C  
ATOM   7465  N9   DG T   7      -9.353  -2.017 -43.318  1.00 29.54           N  
ANISOU 7465  N9   DG T   7     3366   4081   3776     14     16    416       N  
ATOM   7466  C8   DG T   7      -8.754  -1.047 -42.542  1.00 29.73           C  
ANISOU 7466  C8   DG T   7     3367   4056   3873     65    -35    396       C  
ATOM   7467  N7   DG T   7      -8.300  -1.488 -41.397  1.00 29.66           N  
ANISOU 7467  N7   DG T   7     3377   4040   3852    129     -4    335       N  
ATOM   7468  C5   DG T   7      -8.599  -2.847 -41.419  1.00 26.99           C  
ANISOU 7468  C5   DG T   7     3077   3745   3432    120     72    318       C  
ATOM   7469  C6   DG T   7      -8.362  -3.859 -40.458  1.00 23.63           C  
ANISOU 7469  C6   DG T   7     2680   3334   2962    168    132    267       C  
ATOM   7470  O6   DG T   7      -7.813  -3.738 -39.359  1.00 27.55           O  
ANISOU 7470  O6   DG T   7     3175   3816   3477    230    130    225       O  
ATOM   7471  N1   DG T   7      -8.832  -5.114 -40.860  1.00 21.72           N  
ANISOU 7471  N1   DG T   7     2468   3132   2654    138    198    270       N  
ATOM   7472  C2   DG T   7      -9.475  -5.344 -42.058  1.00 25.51           C  
ANISOU 7472  C2   DG T   7     2949   3637   3107     68    206    309       C  
ATOM   7473  N2   DG T   7      -9.876  -6.603 -42.326  1.00 24.49           N  
ANISOU 7473  N2   DG T   7     2844   3541   2918     46    272    300       N  
ATOM   7474  N3   DG T   7      -9.700  -4.395 -42.961  1.00 26.15           N  
ANISOU 7474  N3   DG T   7     3004   3713   3220     22    151    358       N  
ATOM   7475  C4   DG T   7      -9.250  -3.180 -42.585  1.00 25.20           C  
ANISOU 7475  C4   DG T   7     2854   3550   3170     50     85    363       C  
ATOM   7476  P    DC T   8     -12.889  -1.020 -47.455  1.00 34.81           P  
ANISOU 7476  P    DC T   8     3948   4857   4420   -230    -75    645       P  
ATOM   7477  OP1  DC T   8     -13.178  -1.495 -48.829  1.00 33.66           O  
ANISOU 7477  OP1  DC T   8     3797   4784   4207   -318    -52    697       O  
ATOM   7478  OP2  DC T   8     -13.389   0.298 -47.001  1.00 32.37           O  
ANISOU 7478  OP2  DC T   8     3597   4487   4216   -196   -156    662       O  
ATOM   7479  O5'  DC T   8     -13.392  -2.076 -46.365  1.00 33.69           O  
ANISOU 7479  O5'  DC T   8     3850   4713   4238   -168    -12    561       O  
ATOM   7480  C5'  DC T   8     -13.219  -3.471 -46.559  1.00 33.82           C  
ANISOU 7480  C5'  DC T   8     3907   4776   4168   -187     70    530       C  
ATOM   7481  C4'  DC T   8     -13.863  -4.207 -45.406  1.00 31.55           C  
ANISOU 7481  C4'  DC T   8     3647   4476   3865   -121    110    465       C  
ATOM   7482  O4'  DC T   8     -13.020  -4.062 -44.237  1.00 31.62           O  
ANISOU 7482  O4'  DC T   8     3665   4445   3905    -51    110    420       O  
ATOM   7483  C3'  DC T   8     -15.238  -3.675 -45.004  1.00 32.66           C  
ANISOU 7483  C3'  DC T   8     3769   4599   4042    -95     72    465       C  
ATOM   7484  O3'  DC T   8     -16.145  -4.766 -44.901  1.00 31.69           O  
ANISOU 7484  O3'  DC T   8     3672   4508   3863    -95    129    439       O  
ATOM   7485  C2'  DC T   8     -15.000  -3.001 -43.654  1.00 30.69           C  
ANISOU 7485  C2'  DC T   8     3509   4298   3855    -11     39    420       C  
ATOM   7486  C1'  DC T   8     -13.876  -3.890 -43.130  1.00 31.71           C  
ANISOU 7486  C1'  DC T   8     3672   4434   3942     14     97    381       C  
ATOM   7487  N1   DC T   8     -13.085  -3.393 -41.951  1.00 30.04           N  
ANISOU 7487  N1   DC T   8     3454   4185   3776     86     77    338       N  
ATOM   7488  C2   DC T   8     -12.594  -4.344 -41.033  1.00 28.91           C  
ANISOU 7488  C2   DC T   8     3339   4053   3592    132    135    289       C  
ATOM   7489  O2   DC T   8     -12.821  -5.549 -41.219  1.00 24.55           O  
ANISOU 7489  O2   DC T   8     2816   3534   2979    114    199    284       O  
ATOM   7490  N3   DC T   8     -11.871  -3.913 -39.967  1.00 25.04           N  
ANISOU 7490  N3   DC T   8     2840   3538   3135    196    117    250       N  
ATOM   7491  C4   DC T   8     -11.651  -2.604 -39.791  1.00 29.67           C  
ANISOU 7491  C4   DC T   8     3390   4084   3797    215     45    251       C  
ATOM   7492  N4   DC T   8     -10.942  -2.234 -38.718  1.00 27.36           N  
ANISOU 7492  N4   DC T   8     3088   3773   3535    278     31    204       N  
ATOM   7493  C5   DC T   8     -12.143  -1.617 -40.711  1.00 30.05           C  
ANISOU 7493  C5   DC T   8     3408   4113   3898    169    -16    301       C  
ATOM   7494  C6   DC T   8     -12.850  -2.053 -41.768  1.00 27.29           C  
ANISOU 7494  C6   DC T   8     3068   3793   3508    105      2    347       C  
ATOM   7495  P    DC T   9     -17.710  -4.599 -45.192  1.00 30.29           P  
ANISOU 7495  P    DC T   9     3479   4343   3687   -112    109    459       P  
ATOM   7496  OP1  DC T   9     -17.946  -4.728 -46.644  1.00 31.51           O  
ANISOU 7496  OP1  DC T   9     3624   4544   3805   -199    111    514       O  
ATOM   7497  OP2  DC T   9     -18.266  -3.429 -44.483  1.00 30.25           O  
ANISOU 7497  OP2  DC T   9     3442   4293   3760    -62     42    456       O  
ATOM   7498  O5'  DC T   9     -18.234  -5.919 -44.475  1.00 28.74           O  
ANISOU 7498  O5'  DC T   9     3316   4165   3437    -78    181    407       O  
ATOM   7499  C5'  DC T   9     -17.641  -7.169 -44.782  1.00 29.53           C  
ANISOU 7499  C5'  DC T   9     3447   4296   3478   -103    252    389       C  
ATOM   7500  C4'  DC T   9     -17.375  -7.960 -43.510  1.00 30.16           C  
ANISOU 7500  C4'  DC T   9     3549   4361   3548    -35    299    336       C  
ATOM   7501  O4'  DC T   9     -16.299  -7.381 -42.738  1.00 29.63           O  
ANISOU 7501  O4'  DC T   9     3478   4262   3517     14    276    319       O  
ATOM   7502  C3'  DC T   9     -18.544  -7.987 -42.553  1.00 29.62           C  
ANISOU 7502  C3'  DC T   9     3477   4288   3490     19    295    314       C  
ATOM   7503  O3'  DC T   9     -19.428  -9.006 -42.980  1.00 31.23           O  
ANISOU 7503  O3'  DC T   9     3694   4522   3649    -14    342    315       O  
ATOM   7504  C2'  DC T   9     -17.875  -8.297 -41.219  1.00 31.71           C  
ANISOU 7504  C2'  DC T   9     3750   4538   3759     92    317    271       C  
ATOM   7505  C1'  DC T   9     -16.483  -7.704 -41.371  1.00 29.60           C  
ANISOU 7505  C1'  DC T   9     3480   4249   3516     88    294    277       C  
ATOM   7506  N1   DC T   9     -16.172  -6.478 -40.535  1.00 29.56           N  
ANISOU 7506  N1   DC T   9     3449   4211   3569    144    232    260       N  
ATOM   7507  C2   DC T   9     -15.598  -6.635 -39.262  1.00 29.75           C  
ANISOU 7507  C2   DC T   9     3476   4230   3598    214    246    218       C  
ATOM   7508  O2   DC T   9     -15.392  -7.772 -38.807  1.00 32.54           O  
ANISOU 7508  O2   DC T   9     3851   4604   3908    230    307    201       O  
ATOM   7509  N3   DC T   9     -15.294  -5.525 -38.537  1.00 30.18           N  
ANISOU 7509  N3   DC T   9     3503   4258   3707    263    190    194       N  
ATOM   7510  C4   DC T   9     -15.519  -4.308 -39.037  1.00 29.14           C  
ANISOU 7510  C4   DC T   9     3343   4097   3633    245    121    215       C  
ATOM   7511  N4   DC T   9     -15.191  -3.268 -38.267  1.00 29.29           N  
ANISOU 7511  N4   DC T   9     3330   4086   3712    296     68    184       N  
ATOM   7512  C5   DC T   9     -16.100  -4.118 -40.332  1.00 27.94           C  
ANISOU 7512  C5   DC T   9     3187   3947   3482    174    105    268       C  
ATOM   7513  C6   DC T   9     -16.404  -5.220 -41.038  1.00 27.49           C  
ANISOU 7513  C6   DC T   9     3158   3926   3361    125    162    288       C  
ATOM   7514  P    DG T  10     -20.908  -9.143 -42.397  1.00 34.43           P  
ANISOU 7514  P    DG T  10     4094   4936   4054     17    341    305       P  
ATOM   7515  OP1  DG T  10     -21.567 -10.263 -43.110  1.00 36.59           O  
ANISOU 7515  OP1  DG T  10     4381   5240   4281    -32    394    310       O  
ATOM   7516  OP2  DG T  10     -21.545  -7.812 -42.347  1.00 33.13           O  
ANISOU 7516  OP2  DG T  10     3898   4752   3936     29    268    321       O  
ATOM   7517  O5'  DG T  10     -20.601  -9.567 -40.883  1.00 35.48           O  
ANISOU 7517  O5'  DG T  10     4233   5060   4189     98    368    264       O  
ATOM   7518  C5'  DG T  10     -20.184 -10.874 -40.528  1.00 31.52           C  
ANISOU 7518  C5'  DG T  10     3752   4570   3654    107    437    247       C  
ATOM   7519  C4'  DG T  10     -20.337 -11.028 -39.022  1.00 34.02           C  
ANISOU 7519  C4'  DG T  10     4061   4890   3974    187    445    219       C  
ATOM   7520  O4'  DG T  10     -19.480 -10.082 -38.331  1.00 33.73           O  
ANISOU 7520  O4'  DG T  10     4011   4836   3969    233    404    202       O  
ATOM   7521  C3'  DG T  10     -21.748 -10.805 -38.487  1.00 33.40           C  
ANISOU 7521  C3'  DG T  10     3966   4828   3898    216    427    215       C  
ATOM   7522  O3'  DG T  10     -22.029 -11.858 -37.575  1.00 34.22           O  
ANISOU 7522  O3'  DG T  10     4073   4954   3976    254    478    204       O  
ATOM   7523  C2'  DG T  10     -21.697  -9.420 -37.834  1.00 31.58           C  
ANISOU 7523  C2'  DG T  10     3707   4582   3708    263    360    196       C  
ATOM   7524  C1'  DG T  10     -20.228  -9.246 -37.472  1.00 30.93           C  
ANISOU 7524  C1'  DG T  10     3630   4484   3638    285    359    182       C  
ATOM   7525  N9   DG T  10     -19.727  -7.873 -37.610  1.00 30.59           N  
ANISOU 7525  N9   DG T  10     3566   4410   3645    291    292    178       N  
ATOM   7526  C8   DG T  10     -19.887  -7.028 -38.679  1.00 26.89           C  
ANISOU 7526  C8   DG T  10     3089   3920   3209    241    245    208       C  
ATOM   7527  N7   DG T  10     -19.322  -5.861 -38.508  1.00 28.23           N  
ANISOU 7527  N7   DG T  10     3235   4058   3433    261    187    200       N  
ATOM   7528  C5   DG T  10     -18.746  -5.934 -37.249  1.00 26.99           C  
ANISOU 7528  C5   DG T  10     3072   3907   3275    329    197    155       C  
ATOM   7529  C6   DG T  10     -18.000  -4.973 -36.518  1.00 29.13           C  
ANISOU 7529  C6   DG T  10     3318   4156   3595    377    151    121       C  
ATOM   7530  O6   DG T  10     -17.693  -3.824 -36.864  1.00 29.20           O  
ANISOU 7530  O6   DG T  10     3303   4126   3667    369     90    127       O  
ATOM   7531  N1   DG T  10     -17.599  -5.449 -35.265  1.00 29.32           N  
ANISOU 7531  N1   DG T  10     3340   4206   3592    440    181     79       N  
ATOM   7532  C2   DG T  10     -17.895  -6.709 -34.784  1.00 29.79           C  
ANISOU 7532  C2   DG T  10     3420   4308   3591    453    247     78       C  
ATOM   7533  N2   DG T  10     -17.455  -7.029 -33.552  1.00 26.89           N  
ANISOU 7533  N2   DG T  10     3042   3971   3203    514    268     44       N  
ATOM   7534  N3   DG T  10     -18.592  -7.608 -35.470  1.00 28.86           N  
ANISOU 7534  N3   DG T  10     3325   4203   3437    408    288    111       N  
ATOM   7535  C4   DG T  10     -18.986  -7.164 -36.685  1.00 27.75           C  
ANISOU 7535  C4   DG T  10     3188   4039   3316    348    261    144       C  
ATOM   7536  P    DC T  11     -23.318 -11.906 -36.631  1.00 34.02           P  
ANISOU 7536  P    DC T  11     4027   4958   3942    301    475    194       P  
ATOM   7537  OP1  DC T  11     -23.570 -13.343 -36.386  1.00 37.88           O  
ANISOU 7537  OP1  DC T  11     4526   5466   4401    298    542    206       O  
ATOM   7538  OP2  DC T  11     -24.398 -11.072 -37.212  1.00 35.24           O  
ANISOU 7538  OP2  DC T  11     4170   5109   4113    278    428    202       O  
ATOM   7539  O5'  DC T  11     -22.812 -11.195 -35.291  1.00 32.99           O  
ANISOU 7539  O5'  DC T  11     3872   4838   3824    378    445    162       O  
ATOM   7540  C5'  DC T  11     -21.915 -11.868 -34.401  1.00 33.62           C  
ANISOU 7540  C5'  DC T  11     3953   4934   3888    416    483    154       C  
ATOM   7541  C4'  DC T  11     -21.924 -11.244 -33.015  1.00 37.19           C  
ANISOU 7541  C4'  DC T  11     4372   5419   4342    493    455    119       C  
ATOM   7542  O4'  DC T  11     -21.272  -9.949 -33.037  1.00 40.15           O  
ANISOU 7542  O4'  DC T  11     4734   5767   4755    507    396     91       O  
ATOM   7543  C3'  DC T  11     -23.302 -11.005 -32.404  1.00 40.54           C  
ANISOU 7543  C3'  DC T  11     4767   5880   4756    525    438    106       C  
ATOM   7544  O3'  DC T  11     -23.264 -11.459 -31.044  1.00 44.68           O  
ANISOU 7544  O3'  DC T  11     5266   6460   5250    586    462     92       O  
ATOM   7545  C2'  DC T  11     -23.529  -9.498 -32.551  1.00 38.08           C  
ANISOU 7545  C2'  DC T  11     4433   5545   4489    535    365     74       C  
ATOM   7546  C1'  DC T  11     -22.113  -8.930 -32.532  1.00 38.53           C  
ANISOU 7546  C1'  DC T  11     4494   5574   4572    543    344     58       C  
ATOM   7547  N1   DC T  11     -21.868  -7.709 -33.390  1.00 40.14           N  
ANISOU 7547  N1   DC T  11     4694   5725   4833    514    282     56       N  
ATOM   7548  C2   DC T  11     -21.132  -6.610 -32.891  1.00 40.62           C  
ANISOU 7548  C2   DC T  11     4728   5768   4938    552    231     17       C  
ATOM   7549  O2   DC T  11     -20.689  -6.630 -31.734  1.00 42.38           O  
ANISOU 7549  O2   DC T  11     4931   6024   5148    611    237    -22       O  
ATOM   7550  N3   DC T  11     -20.919  -5.533 -33.698  1.00 38.19           N  
ANISOU 7550  N3   DC T  11     4413   5409   4690    522    175     24       N  
ATOM   7551  C4   DC T  11     -21.397  -5.524 -34.947  1.00 37.56           C  
ANISOU 7551  C4   DC T  11     4349   5304   4619    456    168     70       C  
ATOM   7552  N4   DC T  11     -21.170  -4.446 -35.703  1.00 35.49           N  
ANISOU 7552  N4   DC T  11     4072   4995   4417    427    110     86       N  
ATOM   7553  C5   DC T  11     -22.142  -6.623 -35.474  1.00 37.16           C  
ANISOU 7553  C5   DC T  11     4325   5276   4516    417    220    105       C  
ATOM   7554  C6   DC T  11     -22.344  -7.680 -34.673  1.00 38.59           C  
ANISOU 7554  C6   DC T  11     4516   5500   4647    447    276     94       C  
ATOM   7555  P    DC T  12     -24.515 -11.337 -30.054  1.00 44.28           P  
ANISOU 7555  P    DC T  12     5177   6470   5177    634    453     73       P  
ATOM   7556  OP1  DC T  12     -24.231 -12.237 -28.913  1.00 47.62           O  
ANISOU 7556  OP1  DC T  12     5582   6954   5559    677    497     84       O  
ATOM   7557  OP2  DC T  12     -25.758 -11.481 -30.834  1.00 45.74           O  
ANISOU 7557  OP2  DC T  12     5372   6643   5365    594    453     94       O  
ATOM   7558  O5'  DC T  12     -24.430  -9.821 -29.542  1.00 42.15           O  
ANISOU 7558  O5'  DC T  12     4872   6203   4941    679    383     12       O  
ATOM   7559  C5'  DC T  12     -23.347  -9.441 -28.706  1.00 37.74           C  
ANISOU 7559  C5'  DC T  12     4294   5662   4383    724    371    -22       C  
ATOM   7560  C4'  DC T  12     -23.440  -7.975 -28.351  1.00 38.06           C  
ANISOU 7560  C4'  DC T  12     4296   5697   4469    761    301    -86       C  
ATOM   7561  O4'  DC T  12     -23.091  -7.179 -29.503  1.00 38.60           O  
ANISOU 7561  O4'  DC T  12     4385   5686   4596    715    261    -78       O  
ATOM   7562  C3'  DC T  12     -24.830  -7.517 -27.926  1.00 39.24           C  
ANISOU 7562  C3'  DC T  12     4408   5883   4620    788    275   -116       C  
ATOM   7563  O3'  DC T  12     -24.789  -7.285 -26.533  1.00 37.85           O  
ANISOU 7563  O3'  DC T  12     4182   5782   4418    858    268   -170       O  
ATOM   7564  C2'  DC T  12     -25.086  -6.240 -28.726  1.00 37.91           C  
ANISOU 7564  C2'  DC T  12     4232   5646   4525    766    209   -138       C  
ATOM   7565  C1'  DC T  12     -23.750  -5.941 -29.398  1.00 38.85           C  
ANISOU 7565  C1'  DC T  12     4378   5704   4679    737    197   -124       C  
ATOM   7566  N1   DC T  12     -23.852  -5.349 -30.776  1.00 37.51           N  
ANISOU 7566  N1   DC T  12     4229   5459   4564    675    162    -91       N  
ATOM   7567  C2   DC T  12     -23.251  -4.105 -31.046  1.00 36.69           C  
ANISOU 7567  C2   DC T  12     4106   5302   4534    676     99   -116       C  
ATOM   7568  O2   DC T  12     -22.649  -3.511 -30.141  1.00 35.53           O  
ANISOU 7568  O2   DC T  12     3925   5167   4408    730     74   -172       O  
ATOM   7569  N3   DC T  12     -23.349  -3.588 -32.303  1.00 36.08           N  
ANISOU 7569  N3   DC T  12     4040   5162   4504    618     67    -75       N  
ATOM   7570  C4   DC T  12     -24.008  -4.260 -33.260  1.00 37.44           C  
ANISOU 7570  C4   DC T  12     4246   5332   4648    560     96    -18       C  
ATOM   7571  N4   DC T  12     -24.078  -3.718 -34.482  1.00 38.76           N  
ANISOU 7571  N4   DC T  12     4419   5450   4858    501     62     24       N  
ATOM   7572  C5   DC T  12     -24.627  -5.523 -33.006  1.00 36.77           C  
ANISOU 7572  C5   DC T  12     4182   5297   4490    558    160     -1       C  
ATOM   7573  C6   DC T  12     -24.519  -6.024 -31.766  1.00 36.75           C  
ANISOU 7573  C6   DC T  12     4166   5349   4447    616    190    -35       C  
ATOM   7574  P    DG T  13     -26.068  -6.819 -25.697  1.00 37.82           P  
ANISOU 7574  P    DG T  13     4123   5843   4404    904    244   -221       P  
ATOM   7575  OP1  DG T  13     -25.871  -7.316 -24.317  1.00 37.84           O  
ANISOU 7575  OP1  DG T  13     4087   5949   4343    961    273   -242       O  
ATOM   7576  OP2  DG T  13     -27.303  -7.147 -26.447  1.00 36.52           O  
ANISOU 7576  OP2  DG T  13     3977   5659   4239    864    253   -181       O  
ATOM   7577  O5'  DG T  13     -25.915  -5.234 -25.685  1.00 35.39           O  
ANISOU 7577  O5'  DG T  13     3778   5494   4174    928    167   -297       O  
ATOM   7578  C5'  DG T  13     -24.744  -4.628 -25.149  1.00 34.84           C  
ANISOU 7578  C5'  DG T  13     3688   5424   4127    962    142   -345       C  
ATOM   7579  C4'  DG T  13     -24.926  -3.121 -25.081  1.00 37.26           C  
ANISOU 7579  C4'  DG T  13     3946   5693   4518    988     66   -423       C  
ATOM   7580  O4'  DG T  13     -24.843  -2.557 -26.414  1.00 35.32           O  
ANISOU 7580  O4'  DG T  13     3731   5341   4346    931     31   -386       O  
ATOM   7581  C3'  DG T  13     -26.252  -2.625 -24.511  1.00 36.43           C  
ANISOU 7581  C3'  DG T  13     3788   5635   4421   1024     39   -479       C  
ATOM   7582  O3'  DG T  13     -25.968  -1.462 -23.734  1.00 39.36           O  
ANISOU 7582  O3'  DG T  13     4093   6017   4843   1079    -17   -579       O  
ATOM   7583  C2'  DG T  13     -27.100  -2.353 -25.757  1.00 36.41           C  
ANISOU 7583  C2'  DG T  13     3811   5552   4471    968     16   -434       C  
ATOM   7584  C1'  DG T  13     -26.043  -1.901 -26.760  1.00 35.21           C  
ANISOU 7584  C1'  DG T  13     3693   5303   4381    925     -8   -401       C  
ATOM   7585  N9   DG T  13     -26.249  -2.249 -28.163  1.00 37.09           N  
ANISOU 7585  N9   DG T  13     3986   5476   4631    849      3   -316       N  
ATOM   7586  C8   DG T  13     -26.715  -3.426 -28.705  1.00 36.19           C  
ANISOU 7586  C8   DG T  13     3920   5378   4454    806     60   -246       C  
ATOM   7587  N7   DG T  13     -26.754  -3.423 -30.015  1.00 35.36           N  
ANISOU 7587  N7   DG T  13     3851   5208   4376    740     54   -186       N  
ATOM   7588  C5   DG T  13     -26.273  -2.166 -30.362  1.00 36.06           C  
ANISOU 7588  C5   DG T  13     3915   5232   4552    738    -12   -209       C  
ATOM   7589  C6   DG T  13     -26.084  -1.565 -31.632  1.00 35.11           C  
ANISOU 7589  C6   DG T  13     3809   5036   4496    679    -50   -162       C  
ATOM   7590  O6   DG T  13     -26.314  -2.056 -32.738  1.00 37.79           O  
ANISOU 7590  O6   DG T  13     4187   5355   4817    615    -30    -93       O  
ATOM   7591  N1   DG T  13     -25.588  -0.263 -31.540  1.00 33.97           N  
ANISOU 7591  N1   DG T  13     3622   4840   4443    700   -119   -202       N  
ATOM   7592  C2   DG T  13     -25.302   0.380 -30.351  1.00 34.59           C  
ANISOU 7592  C2   DG T  13     3651   4939   4551    771   -147   -289       C  
ATOM   7593  N2   DG T  13     -24.823   1.629 -30.421  1.00 34.02           N  
ANISOU 7593  N2   DG T  13     3538   4806   4581    783   -215   -322       N  
ATOM   7594  N3   DG T  13     -25.471  -0.170 -29.158  1.00 34.25           N  
ANISOU 7594  N3   DG T  13     3594   4977   4443    826   -111   -339       N  
ATOM   7595  C4   DG T  13     -25.958  -1.435 -29.235  1.00 36.19           C  
ANISOU 7595  C4   DG T  13     3881   5273   4598    806    -45   -291       C  
ATOM   7596  P    DC T  14     -27.106  -0.615 -23.003  1.00 42.75           P  
ANISOU 7596  P    DC T  14     4448   6491   5304   1129    -60   -671       P  
ATOM   7597  OP1  DC T  14     -26.493   0.097 -21.859  1.00 46.32           O  
ANISOU 7597  OP1  DC T  14     4834   6997   5768   1195    -90   -775       O  
ATOM   7598  OP2  DC T  14     -28.268  -1.500 -22.764  1.00 40.96           O  
ANISOU 7598  OP2  DC T  14     4226   6338   5001   1128    -16   -637       O  
ATOM   7599  O5'  DC T  14     -27.506   0.443 -24.132  1.00 42.88           O  
ANISOU 7599  O5'  DC T  14     4466   6388   5439   1092   -123   -666       O  
ATOM   7600  C5'  DC T  14     -26.635   1.480 -24.550  1.00 40.65           C  
ANISOU 7600  C5'  DC T  14     4172   6016   5256   1086   -179   -691       C  
ATOM   7601  C4'  DC T  14     -27.270   2.253 -25.698  1.00 42.89           C  
ANISOU 7601  C4'  DC T  14     4458   6198   5640   1041   -231   -659       C  
ATOM   7602  O4'  DC T  14     -27.433   1.392 -26.847  1.00 40.51           O  
ANISOU 7602  O4'  DC T  14     4230   5864   5298    970   -190   -546       O  
ATOM   7603  C3'  DC T  14     -28.662   2.820 -25.438  1.00 44.20           C  
ANISOU 7603  C3'  DC T  14     4570   6378   5845   1065   -264   -711       C  
ATOM   7604  O3'  DC T  14     -28.569   4.228 -25.499  1.00 47.68           O  
ANISOU 7604  O3'  DC T  14     4952   6745   6418   1083   -344   -776       O  
ATOM   7605  C2'  DC T  14     -29.546   2.272 -26.563  1.00 42.67           C  
ANISOU 7605  C2'  DC T  14     4428   6150   5636   1001   -244   -613       C  
ATOM   7606  C1'  DC T  14     -28.521   1.867 -27.612  1.00 41.76           C  
ANISOU 7606  C1'  DC T  14     4379   5973   5515    939   -225   -522       C  
ATOM   7607  N1   DC T  14     -28.898   0.766 -28.582  1.00 41.59           N  
ANISOU 7607  N1   DC T  14     4427   5949   5426    873   -171   -418       N  
ATOM   7608  C2   DC T  14     -28.759   0.964 -29.971  1.00 39.94           C  
ANISOU 7608  C2   DC T  14     4252   5659   5263    803   -190   -340       C  
ATOM   7609  O2   DC T  14     -28.360   2.046 -30.418  1.00 41.24           O  
ANISOU 7609  O2   DC T  14     4390   5750   5528    793   -252   -346       O  
ATOM   7610  N3   DC T  14     -29.078  -0.049 -30.815  1.00 40.93           N  
ANISOU 7610  N3   DC T  14     4435   5791   5324    745   -140   -257       N  
ATOM   7611  C4   DC T  14     -29.517  -1.215 -30.330  1.00 43.92           C  
ANISOU 7611  C4   DC T  14     4838   6243   5607    755    -76   -247       C  
ATOM   7612  N4   DC T  14     -29.826  -2.171 -31.211  1.00 44.57           N  
ANISOU 7612  N4   DC T  14     4973   6325   5638    696    -30   -171       N  
ATOM   7613  C5   DC T  14     -29.663  -1.448 -28.926  1.00 43.33           C  
ANISOU 7613  C5   DC T  14     4728   6249   5485    825    -56   -315       C  
ATOM   7614  C6   DC T  14     -29.339  -0.442 -28.102  1.00 42.16           C  
ANISOU 7614  C6   DC T  14     4525   6104   5392    881   -104   -399       C  
ATOM   7615  P    DG T  15     -29.669   5.184 -24.841  1.00 49.83           P  
ANISOU 7615  P    DG T  15     5138   7032   6762   1134   -397   -879       P  
ATOM   7616  OP1  DG T  15     -28.921   6.309 -24.232  1.00 50.71           O  
ANISOU 7616  OP1  DG T  15     5183   7116   6970   1182   -455   -982       O  
ATOM   7617  OP2  DG T  15     -30.620   4.387 -24.028  1.00 46.21           O  
ANISOU 7617  OP2  DG T  15     4671   6690   6197   1165   -348   -903       O  
ATOM   7618  O5'  DG T  15     -30.470   5.706 -26.114  1.00 47.08           O  
ANISOU 7618  O5'  DG T  15     4799   6581   6507   1078   -439   -811       O  
ATOM   7619  C5'  DG T  15     -29.819   6.342 -27.206  1.00 48.17           C  
ANISOU 7619  C5'  DG T  15     4953   6606   6742   1028   -482   -750       C  
ATOM   7620  C4'  DG T  15     -30.763   6.311 -28.389  1.00 45.88           C  
ANISOU 7620  C4'  DG T  15     4689   6263   6481    966   -493   -659       C  
ATOM   7621  O4'  DG T  15     -30.762   4.967 -28.919  1.00 43.79           O  
ANISOU 7621  O4'  DG T  15     4507   6041   6091    918   -418   -564       O  
ATOM   7622  C3'  DG T  15     -32.217   6.615 -28.026  1.00 47.72           C  
ANISOU 7622  C3'  DG T  15     4873   6521   6739    994   -512   -708       C  
ATOM   7623  O3'  DG T  15     -32.727   7.656 -28.852  1.00 49.23           O  
ANISOU 7623  O3'  DG T  15     5028   6613   7066    965   -583   -684       O  
ATOM   7624  C2'  DG T  15     -32.955   5.291 -28.235  1.00 46.69           C  
ANISOU 7624  C2'  DG T  15     4804   6461   6475    964   -439   -639       C  
ATOM   7625  C1'  DG T  15     -32.079   4.683 -29.324  1.00 45.92           C  
ANISOU 7625  C1'  DG T  15     4783   6322   6341    895   -409   -528       C  
ATOM   7626  N9   DG T  15     -32.220   3.246 -29.534  1.00 43.10           N  
ANISOU 7626  N9   DG T  15     4497   6028   5851    863   -328   -460       N  
ATOM   7627  C8   DG T  15     -32.464   2.260 -28.604  1.00 43.96           C  
ANISOU 7627  C8   DG T  15     4617   6237   5850    899   -267   -487       C  
ATOM   7628  N7   DG T  15     -32.529   1.062 -29.117  1.00 40.82           N  
ANISOU 7628  N7   DG T  15     4284   5866   5361    854   -204   -406       N  
ATOM   7629  C5   DG T  15     -32.315   1.269 -30.475  1.00 40.23           C  
ANISOU 7629  C5   DG T  15     4243   5709   5333    785   -223   -327       C  
ATOM   7630  C6   DG T  15     -32.279   0.347 -31.548  1.00 39.38           C  
ANISOU 7630  C6   DG T  15     4201   5592   5170    714   -179   -231       C  
ATOM   7631  O6   DG T  15     -32.433  -0.877 -31.490  1.00 42.80           O  
ANISOU 7631  O6   DG T  15     4677   6078   5507    701   -112   -198       O  
ATOM   7632  N1   DG T  15     -32.041   0.973 -32.775  1.00 38.47           N  
ANISOU 7632  N1   DG T  15     4093   5398   5125    656   -221   -172       N  
ATOM   7633  C2   DG T  15     -31.855   2.335 -32.937  1.00 39.26           C  
ANISOU 7633  C2   DG T  15     4143   5430   5345    665   -299   -196       C  
ATOM   7634  N2   DG T  15     -31.623   2.788 -34.180  1.00 37.45           N  
ANISOU 7634  N2   DG T  15     3923   5136   5171    601   -332   -122       N  
ATOM   7635  N3   DG T  15     -31.887   3.208 -31.937  1.00 37.26           N  
ANISOU 7635  N3   DG T  15     3828   5175   5155    731   -342   -289       N  
ATOM   7636  C4   DG T  15     -32.124   2.608 -30.745  1.00 40.68           C  
ANISOU 7636  C4   DG T  15     4254   5691   5512    789   -300   -353       C  
ATOM   7637  P    DC T  16     -34.032   8.470 -28.413  1.00 51.09           P  
ANISOU 7637  P    DC T  16     5183   6842   7386   1005   -633   -762       P  
ATOM   7638  OP1  DC T  16     -34.090   9.698 -29.242  1.00 53.30           O  
ANISOU 7638  OP1  DC T  16     5418   7000   7834    977   -716   -736       O  
ATOM   7639  OP2  DC T  16     -34.070   8.587 -26.936  1.00 51.14           O  
ANISOU 7639  OP2  DC T  16     5133   6931   7366   1088   -626   -899       O  
ATOM   7640  O5'  DC T  16     -35.210   7.465 -28.842  1.00 51.04           O  
ANISOU 7640  O5'  DC T  16     5227   6888   7277    969   -580   -690       O  
ATOM   7641  C5'  DC T  16     -35.869   7.581 -30.105  1.00 49.61           C  
ANISOU 7641  C5'  DC T  16     5067   6642   7141    902   -600   -589       C  
ATOM   7642  C4'  DC T  16     -35.068   6.968 -31.246  1.00 47.71           C  
ANISOU 7642  C4'  DC T  16     4903   6371   6852    828   -570   -467       C  
ATOM   7643  O4'  DC T  16     -34.723   5.591 -30.938  1.00 46.93           O  
ANISOU 7643  O4'  DC T  16     4873   6360   6600    825   -484   -446       O  
ATOM   7644  C3'  DC T  16     -35.795   6.933 -32.588  1.00 47.74           C  
ANISOU 7644  C3'  DC T  16     4932   6330   6878    753   -583   -356       C  
ATOM   7645  O3'  DC T  16     -34.915   7.375 -33.618  1.00 46.75           O  
ANISOU 7645  O3'  DC T  16     4819   6130   6815    698   -615   -277       O  
ATOM   7646  C2'  DC T  16     -36.163   5.461 -32.759  1.00 45.99           C  
ANISOU 7646  C2'  DC T  16     4785   6189   6502    724   -497   -302       C  
ATOM   7647  C1'  DC T  16     -35.006   4.771 -32.051  1.00 43.77           C  
ANISOU 7647  C1'  DC T  16     4538   5957   6136    752   -446   -334       C  
ATOM   7648  N1   DC T  16     -35.274   3.355 -31.600  1.00 41.07           N  
ANISOU 7648  N1   DC T  16     4247   5710   5648    757   -361   -326       N  
ATOM   7649  C2   DC T  16     -35.264   2.305 -32.538  1.00 38.83           C  
ANISOU 7649  C2   DC T  16     4034   5436   5283    691   -308   -229       C  
ATOM   7650  O2   DC T  16     -35.043   2.549 -33.730  1.00 37.50           O  
ANISOU 7650  O2   DC T  16     3885   5209   5153    628   -330   -153       O  
ATOM   7651  N3   DC T  16     -35.502   1.035 -32.112  1.00 38.75           N  
ANISOU 7651  N3   DC T  16     4064   5504   5155    697   -234   -221       N  
ATOM   7652  C4   DC T  16     -35.732   0.787 -30.817  1.00 38.52           C  
ANISOU 7652  C4   DC T  16     4008   5547   5081    764   -212   -296       C  
ATOM   7653  N4   DC T  16     -35.962  -0.480 -30.445  1.00 35.70           N  
ANISOU 7653  N4   DC T  16     3687   5264   4615    765   -141   -275       N  
ATOM   7654  C5   DC T  16     -35.746   1.841 -29.850  1.00 38.69           C  
ANISOU 7654  C5   DC T  16     3957   5570   5173    831   -264   -397       C  
ATOM   7655  C6   DC T  16     -35.517   3.089 -30.280  1.00 39.26           C  
ANISOU 7655  C6   DC T  16     3991   5559   5368    826   -337   -412       C  
ATOM   7656  P    DG T  17     -35.459   8.134 -34.917  1.00 47.20           P  
ANISOU 7656  P    DG T  17     4852   6106   6975    633   -676   -182       P  
ATOM   7657  OP1  DG T  17     -34.297   8.308 -35.818  1.00 46.04           O  
ANISOU 7657  OP1  DG T  17     4728   5913   6853    579   -690   -102       O  
ATOM   7658  OP2  DG T  17     -36.238   9.314 -34.470  1.00 46.54           O  
ANISOU 7658  OP2  DG T  17     4681   5972   7031    677   -749   -250       O  
ATOM   7659  O5'  DG T  17     -36.518   7.121 -35.566  1.00 47.82           O  
ANISOU 7659  O5'  DG T  17     4982   6238   6948    584   -624   -110       O  
ATOM   7660  C5'  DG T  17     -36.300   6.479 -36.822  1.00 45.14           C  
ANISOU 7660  C5'  DG T  17     4701   5903   6546    501   -594      6       C  
ATOM   7661  C4'  DG T  17     -37.341   5.399 -37.077  1.00 42.06           C  
ANISOU 7661  C4'  DG T  17     4356   5578   6046    475   -535     39       C  
ATOM   7662  O4'  DG T  17     -37.337   4.427 -36.007  1.00 42.43           O  
ANISOU 7662  O4'  DG T  17     4434   5701   5986    525   -468    -30       O  
ATOM   7663  C3'  DG T  17     -38.782   5.881 -37.163  1.00 43.71           C  
ANISOU 7663  C3'  DG T  17     4522   5775   6312    478   -572     37       C  
ATOM   7664  O3'  DG T  17     -39.016   6.226 -38.521  1.00 41.52           O  
ANISOU 7664  O3'  DG T  17     4240   5456   6078    402   -607    144       O  
ATOM   7665  C2'  DG T  17     -39.601   4.659 -36.741  1.00 42.60           C  
ANISOU 7665  C2'  DG T  17     4424   5718   6043    489   -498     20       C  
ATOM   7666  C1'  DG T  17     -38.631   3.857 -35.875  1.00 42.05           C  
ANISOU 7666  C1'  DG T  17     4393   5701   5884    528   -439    -32       C  
ATOM   7667  N9   DG T  17     -38.934   3.823 -34.444  1.00 39.33           N  
ANISOU 7667  N9   DG T  17     4018   5405   5522    610   -426   -138       N  
ATOM   7668  C8   DG T  17     -39.275   4.873 -33.619  1.00 40.13           C  
ANISOU 7668  C8   DG T  17     4045   5485   5718    672   -482   -227       C  
ATOM   7669  N7   DG T  17     -39.463   4.514 -32.375  1.00 39.39           N  
ANISOU 7669  N7   DG T  17     3937   5462   5568    738   -451   -314       N  
ATOM   7670  C5   DG T  17     -39.230   3.146 -32.374  1.00 37.35           C  
ANISOU 7670  C5   DG T  17     3747   5270   5175    718   -371   -273       C  
ATOM   7671  C6   DG T  17     -39.282   2.201 -31.316  1.00 39.86           C  
ANISOU 7671  C6   DG T  17     4078   5681   5385    762   -308   -317       C  
ATOM   7672  O6   DG T  17     -39.553   2.393 -30.115  1.00 40.62           O  
ANISOU 7672  O6   DG T  17     4128   5833   5474    831   -311   -408       O  
ATOM   7673  N1   DG T  17     -38.974   0.913 -31.761  1.00 38.92           N  
ANISOU 7673  N1   DG T  17     4032   5596   5161    719   -238   -245       N  
ATOM   7674  C2   DG T  17     -38.653   0.578 -33.058  1.00 38.18           C  
ANISOU 7674  C2   DG T  17     3988   5456   5060    642   -228   -152       C  
ATOM   7675  N2   DG T  17     -38.383  -0.716 -33.311  1.00 40.65           N  
ANISOU 7675  N2   DG T  17     4363   5810   5273    610   -157   -102       N  
ATOM   7676  N3   DG T  17     -38.601   1.457 -34.046  1.00 34.62           N  
ANISOU 7676  N3   DG T  17     3525   4931   4700    600   -285   -110       N  
ATOM   7677  C4   DG T  17     -38.899   2.711 -33.638  1.00 36.29           C  
ANISOU 7677  C4   DG T  17     3668   5102   5019    640   -354   -170       C  
ATOM   7678  P    DG T  18     -40.384   6.844 -39.037  1.00 36.88           P  
ANISOU 7678  P    DG T  18     3607   4840   5567    380   -656    181       P  
ATOM   7679  OP1  DG T  18     -41.327   5.741 -39.303  1.00 39.01           O  
ANISOU 7679  OP1  DG T  18     3925   5178   5719    352   -595    210       O  
ATOM   7680  OP2  DG T  18     -40.054   7.799 -40.121  1.00 41.62           O  
ANISOU 7680  OP2  DG T  18     4171   5369   6276    324   -725    270       O  
ATOM   7681  O5'  DG T  18     -40.899   7.702 -37.788  1.00 39.27           O  
ANISOU 7681  O5'  DG T  18     3839   5117   5966    468   -700     63       O  
ATOM   7682  C5'  DG T  18     -42.262   8.068 -37.688  1.00 28.55           C  
ANISOU 7682  C5'  DG T  18     2438   3753   4657    481   -728     47       C  
ATOM   7683  C4'  DG T  18     -42.783   7.721 -36.304  1.00 31.52           C  
ANISOU 7683  C4'  DG T  18     2804   4189   4985    561   -695    -73       C  
ATOM   7684  O4'  DG T  18     -44.139   8.227 -36.179  1.00 30.19           O  
ANISOU 7684  O4'  DG T  18     2582   4007   4881    579   -731    -96       O  
ATOM   7685  C3'  DG T  18     -42.876   6.228 -35.980  1.00 30.44           C  
ANISOU 7685  C3'  DG T  18     2742   4150   4676    560   -600    -73       C  
ATOM   7686  O3'  DG T  18     -42.514   6.016 -34.616  1.00 32.66           O  
ANISOU 7686  O3'  DG T  18     3012   4480   4916    637   -573   -182       O  
ATOM   7687  C2'  DG T  18     -44.349   5.903 -36.244  1.00 29.47           C  
ANISOU 7687  C2'  DG T  18     2617   4055   4525    543   -590    -48       C  
ATOM   7688  C1'  DG T  18     -44.996   7.187 -35.754  1.00 27.36           C  
ANISOU 7688  C1'  DG T  18     2261   3735   4400    591   -666   -116       C  
ATOM   7689  N9   DG T  18     -46.310   7.516 -36.282  1.00 26.76           N  
ANISOU 7689  N9   DG T  18     2154   3639   4373    567   -697    -78       N  
ATOM   7690  C8   DG T  18     -47.405   7.817 -35.520  1.00 27.02           C  
ANISOU 7690  C8   DG T  18     2138   3690   4439    619   -713   -155       C  
ATOM   7691  N7   DG T  18     -48.450   8.109 -36.227  1.00 27.46           N  
ANISOU 7691  N7   DG T  18     2173   3718   4543    583   -743    -99       N  
ATOM   7692  C5   DG T  18     -48.021   7.999 -37.542  1.00 27.79           C  
ANISOU 7692  C5   DG T  18     2251   3726   4581    501   -749     24       C  
ATOM   7693  C6   DG T  18     -48.737   8.205 -38.746  1.00 27.18           C  
ANISOU 7693  C6   DG T  18     2168   3618   4540    432   -778    131       C  
ATOM   7694  O6   DG T  18     -49.919   8.532 -38.877  1.00 29.97           O  
ANISOU 7694  O6   DG T  18     2485   3961   4941    431   -806    138       O  
ATOM   7695  N1   DG T  18     -47.947   7.999 -39.873  1.00 29.04           N  
ANISOU 7695  N1   DG T  18     2444   3841   4750    358   -774    238       N  
ATOM   7696  C2   DG T  18     -46.616   7.643 -39.841  1.00 30.50           C  
ANISOU 7696  C2   DG T  18     2670   4035   4885    352   -745    239       C  
ATOM   7697  N2   DG T  18     -46.026   7.492 -41.038  1.00 33.27           N  
ANISOU 7697  N2   DG T  18     3050   4377   5214    275   -745    347       N  
ATOM   7698  N3   DG T  18     -45.924   7.448 -38.716  1.00 28.26           N  
ANISOU 7698  N3   DG T  18     2394   3773   4571    418   -717    140       N  
ATOM   7699  C4   DG T  18     -46.694   7.642 -37.602  1.00 27.31           C  
ANISOU 7699  C4   DG T  18     2234   3671   4471    490   -721     37       C  
TER    7700       DG T  18                                                      
ATOM   7701  O5'  DC P 103     -35.460 -12.763 -36.260  1.00110.22           O  
ANISOU 7701  O5'  DC P 103    13574  14789  13514    296    453    253       O  
ATOM   7702  C5'  DC P 103     -35.992 -11.930 -35.227  1.00111.51           C  
ANISOU 7702  C5'  DC P 103    13702  14978  13689    359    415    222       C  
ATOM   7703  C4'  DC P 103     -36.446 -10.578 -35.763  1.00111.37           C  
ANISOU 7703  C4'  DC P 103    13668  14934  13715    348    346    212       C  
ATOM   7704  O4'  DC P 103     -37.052  -9.777 -34.706  1.00112.73           O  
ANISOU 7704  O4'  DC P 103    13798  15132  13903    413    309    171       O  
ATOM   7705  C3'  DC P 103     -35.335  -9.712 -36.354  1.00110.35           C  
ANISOU 7705  C3'  DC P 103    13545  14759  13623    329    308    209       C  
ATOM   7706  O3'  DC P 103     -35.767  -9.150 -37.588  1.00107.88           O  
ANISOU 7706  O3'  DC P 103    13236  14418  13337    269    273    238       O  
ATOM   7707  C2'  DC P 103     -35.143  -8.634 -35.293  1.00111.95           C  
ANISOU 7707  C2'  DC P 103    13709  14966  13860    398    260    159       C  
ATOM   7708  C1'  DC P 103     -36.594  -8.448 -34.867  1.00113.58           C  
ANISOU 7708  C1'  DC P 103    13887  15202  14066    422    245    147       C  
ATOM   7709  N1   DC P 103     -36.809  -7.594 -33.633  1.00115.43           N  
ANISOU 7709  N1   DC P 103    14073  15462  14324    498    208     87       N  
ATOM   7710  C2   DC P 103     -38.109  -7.178 -33.270  1.00116.11           C  
ANISOU 7710  C2   DC P 103    14124  15571  14420    522    183     67       C  
ATOM   7711  O2   DC P 103     -39.092  -7.521 -33.946  1.00114.99           O  
ANISOU 7711  O2   DC P 103    13994  15427  14269    482    192    102       O  
ATOM   7712  N3   DC P 103     -38.260  -6.400 -32.159  1.00116.50           N  
ANISOU 7712  N3   DC P 103    14125  15648  14491    591    149      3       N  
ATOM   7713  C4   DC P 103     -37.196  -6.031 -31.435  1.00116.30           C  
ANISOU 7713  C4   DC P 103    14084  15629  14475    634    139    -39       C  
ATOM   7714  N4   DC P 103     -37.406  -5.268 -30.357  1.00115.61           N  
ANISOU 7714  N4   DC P 103    13943  15576  14408    700    105   -110       N  
ATOM   7715  C5   DC P 103     -35.869  -6.435 -31.786  1.00116.36           C  
ANISOU 7715  C5   DC P 103    14129  15610  14472    610    163    -14       C  
ATOM   7716  C6   DC P 103     -35.728  -7.204 -32.877  1.00115.99           C  
ANISOU 7716  C6   DC P 103    14131  15536  14406    543    197     48       C  
ATOM   7717  P    DG P 104     -34.718  -8.491 -38.604  1.00106.58           P  
ANISOU 7717  P    DG P 104    13081  14211  13204    222    241    258       P  
ATOM   7718  OP1  DG P 104     -33.969  -9.597 -39.245  1.00105.73           O  
ANISOU 7718  OP1  DG P 104    13010  14107  13054    176    298    280       O  
ATOM   7719  OP2  DG P 104     -33.985  -7.419 -37.889  1.00106.73           O  
ANISOU 7719  OP2  DG P 104    13075  14208  13271    274    194    224       O  
ATOM   7720  O5'  DG P 104     -35.649  -7.786 -39.704  1.00104.13           O  
ANISOU 7720  O5'  DG P 104    12757  13885  12922    169    196    294       O  
ATOM   7721  C5'  DG P 104     -36.840  -7.088 -39.328  1.00100.08           C  
ANISOU 7721  C5'  DG P 104    12211  13374  12441    197    155    283       C  
ATOM   7722  C4'  DG P 104     -36.773  -5.578 -39.530  1.00 97.23           C  
ANISOU 7722  C4'  DG P 104    11813  12971  12159    203     75    283       C  
ATOM   7723  O4'  DG P 104     -37.414  -4.947 -38.391  1.00 96.37           O  
ANISOU 7723  O4'  DG P 104    11666  12866  12085    274     44    232       O  
ATOM   7724  C3'  DG P 104     -35.390  -4.938 -39.626  1.00 95.80           C  
ANISOU 7724  C3'  DG P 104    11629  12755  12014    205     48    280       C  
ATOM   7725  O3'  DG P 104     -34.994  -4.848 -40.997  1.00 94.55           O  
ANISOU 7725  O3'  DG P 104    11483  12582  11857    128     38    338       O  
ATOM   7726  C2'  DG P 104     -35.592  -3.554 -39.015  1.00 95.06           C  
ANISOU 7726  C2'  DG P 104    11485  12627  12005    255    -25    246       C  
ATOM   7727  C1'  DG P 104     -36.776  -3.724 -38.070  1.00 93.42           C  
ANISOU 7727  C1'  DG P 104    11259  12452  11786    307    -16    205       C  
ATOM   7728  N9   DG P 104     -36.406  -3.722 -36.652  1.00 89.34           N  
ANISOU 7728  N9   DG P 104    10725  11958  11263    386     -6    136       N  
ATOM   7729  C8   DG P 104     -36.335  -4.808 -35.812  1.00 87.75           C  
ANISOU 7729  C8   DG P 104    10543  11809  10989    418     56    114       C  
ATOM   7730  N7   DG P 104     -35.984  -4.502 -34.595  1.00 86.12           N  
ANISOU 7730  N7   DG P 104    10309  11623  10789    488     49     53       N  
ATOM   7731  C5   DG P 104     -35.809  -3.126 -34.620  1.00 84.49           C  
ANISOU 7731  C5   DG P 104    10063  11370  10671    505    -24     26       C  
ATOM   7732  C6   DG P 104     -35.428  -2.233 -33.587  1.00 81.18           C  
ANISOU 7732  C6   DG P 104     9596  10949  10299    572    -64    -48       C  
ATOM   7733  O6   DG P 104     -35.165  -2.505 -32.408  1.00 78.81           O  
ANISOU 7733  O6   DG P 104     9282  10699   9964    632    -41   -102       O  
ATOM   7734  N1   DG P 104     -35.366  -0.910 -34.029  1.00 79.42           N  
ANISOU 7734  N1   DG P 104     9337  10661  10179    566   -138    -55       N  
ATOM   7735  C2   DG P 104     -35.642  -0.505 -35.317  1.00 80.93           C  
ANISOU 7735  C2   DG P 104     9534  10800  10414    500   -170     12       C  
ATOM   7736  N2   DG P 104     -35.534   0.805 -35.575  1.00 78.54           N  
ANISOU 7736  N2   DG P 104     9186  10435  10219    502   -245      4       N  
ATOM   7737  N3   DG P 104     -36.001  -1.333 -36.294  1.00 84.26           N  
ANISOU 7737  N3   DG P 104     9999  11234  10781    435   -132     82       N  
ATOM   7738  C4   DG P 104     -36.066  -2.627 -35.881  1.00 86.46           C  
ANISOU 7738  C4   DG P 104    10316  11570  10965    442    -59     80       C  
ATOM   7739  P    DC P 105     -33.463  -4.663 -41.445  1.00 92.79           P  
ANISOU 7739  P    DC P 105    11274  12339  11644    104     34    353       P  
ATOM   7740  OP1  DC P 105     -33.430  -4.721 -42.926  1.00 91.96           O  
ANISOU 7740  OP1  DC P 105    11176  12241  11523     17     30    418       O  
ATOM   7741  OP2  DC P 105     -32.617  -5.583 -40.651  1.00 92.09           O  
ANISOU 7741  OP2  DC P 105    11215  12268  11507    141     92    315       O  
ATOM   7742  O5'  DC P 105     -33.114  -3.176 -40.971  1.00 91.09           O  
ANISOU 7742  O5'  DC P 105    11013  12074  11522    147    -43    334       O  
ATOM   7743  C5'  DC P 105     -33.734  -2.046 -41.582  1.00 87.41           C  
ANISOU 7743  C5'  DC P 105    10506  11575  11129    122   -113    370       C  
ATOM   7744  C4'  DC P 105     -33.257  -0.758 -40.935  1.00 84.16           C  
ANISOU 7744  C4'  DC P 105    10049  11111  10814    173   -180    337       C  
ATOM   7745  O4'  DC P 105     -33.831  -0.604 -39.612  1.00 82.04           O  
ANISOU 7745  O4'  DC P 105     9760  10849  10563    253   -184    262       O  
ATOM   7746  C3'  DC P 105     -31.756  -0.668 -40.706  1.00 81.61           C  
ANISOU 7746  C3'  DC P 105     9738  10771  10497    187   -176    322       C  
ATOM   7747  O3'  DC P 105     -31.114  -0.408 -41.969  1.00 81.26           O  
ANISOU 7747  O3'  DC P 105     9698  10714  10465    114   -195    394       O  
ATOM   7748  C2'  DC P 105     -31.715   0.459 -39.678  1.00 80.41           C  
ANISOU 7748  C2'  DC P 105     9536  10579  10437    259   -234    261       C  
ATOM   7749  C1'  DC P 105     -32.929   0.139 -38.806  1.00 80.03           C  
ANISOU 7749  C1'  DC P 105     9479  10563  10366    307   -216    210       C  
ATOM   7750  N1   DC P 105     -32.620  -0.614 -37.519  1.00 77.07           N  
ANISOU 7750  N1   DC P 105     9122  10232   9930    372   -164    140       N  
ATOM   7751  C2   DC P 105     -32.293   0.092 -36.341  1.00 73.84           C  
ANISOU 7751  C2   DC P 105     8672   9813   9569    447   -195     63       C  
ATOM   7752  O2   DC P 105     -32.248   1.329 -36.349  1.00 72.15           O  
ANISOU 7752  O2   DC P 105     8410   9547   9457    461   -266     46       O  
ATOM   7753  N3   DC P 105     -32.028  -0.609 -35.204  1.00 72.28           N  
ANISOU 7753  N3   DC P 105     8486   9667   9309    502   -147      7       N  
ATOM   7754  C4   DC P 105     -32.079  -1.946 -35.203  1.00 72.44           C  
ANISOU 7754  C4   DC P 105     8553   9738   9233    486    -74     31       C  
ATOM   7755  N4   DC P 105     -31.812  -2.588 -34.061  1.00 69.73           N  
ANISOU 7755  N4   DC P 105     8213   9446   8834    540    -31    -16       N  
ATOM   7756  C5   DC P 105     -32.408  -2.684 -36.381  1.00 73.84           C  
ANISOU 7756  C5   DC P 105     8771   9917   9368    412    -42    103       C  
ATOM   7757  C6   DC P 105     -32.666  -1.986 -37.496  1.00 75.51           C  
ANISOU 7757  C6   DC P 105     8972  10086   9631    358    -87    152       C  
ATOM   7758  P    DG P 106     -29.713   0.352 -42.162  1.00 79.83           P  
ANISOU 7758  P    DG P 106     9502  10492  10339    109   -233    408       P  
ATOM   7759  OP1  DG P 106     -29.356   0.272 -43.598  1.00 80.90           O  
ANISOU 7759  OP1  DG P 106     9645  10640  10452     21   -234    493       O  
ATOM   7760  OP2  DG P 106     -28.757  -0.144 -41.148  1.00 80.83           O  
ANISOU 7760  OP2  DG P 106     9654  10626  10433    164   -192    345       O  
ATOM   7761  O5'  DG P 106     -30.099   1.866 -41.812  1.00 77.79           O  
ANISOU 7761  O5'  DG P 106     9176  10170  10209    144   -322    397       O  
ATOM   7762  C5'  DG P 106     -29.136   2.895 -41.936  1.00 73.07           C  
ANISOU 7762  C5'  DG P 106     8545   9519   9699    145   -380    411       C  
ATOM   7763  C4'  DG P 106     -28.691   3.449 -40.592  1.00 68.84           C  
ANISOU 7763  C4'  DG P 106     7984   8950   9221    231   -402    321       C  
ATOM   7764  O4'  DG P 106     -29.185   2.676 -39.467  1.00 64.99           O  
ANISOU 7764  O4'  DG P 106     7518   8507   8669    291   -350    243       O  
ATOM   7765  C3'  DG P 106     -27.178   3.496 -40.437  1.00 68.34           C  
ANISOU 7765  C3'  DG P 106     7934   8873   9160    239   -396    311       C  
ATOM   7766  O3'  DG P 106     -26.820   4.845 -40.196  1.00 71.57           O  
ANISOU 7766  O3'  DG P 106     8284   9214   9698    266   -475    297       O  
ATOM   7767  C2'  DG P 106     -26.868   2.584 -39.248  1.00 63.85           C  
ANISOU 7767  C2'  DG P 106     7401   8347   8512    301   -332    230       C  
ATOM   7768  C1'  DG P 106     -28.178   2.629 -38.474  1.00 60.20           C  
ANISOU 7768  C1'  DG P 106     6916   7901   8057    348   -336    177       C  
ATOM   7769  N9   DG P 106     -28.422   1.472 -37.608  1.00 53.50           N  
ANISOU 7769  N9   DG P 106     6104   7116   7109    387   -264    127       N  
ATOM   7770  C8   DG P 106     -28.682   0.179 -38.004  1.00 50.48           C  
ANISOU 7770  C8   DG P 106     5774   6784   6622    350   -193    161       C  
ATOM   7771  N7   DG P 106     -28.869  -0.653 -37.017  1.00 48.39           N  
ANISOU 7771  N7   DG P 106     5526   6568   6291    398   -141    111       N  
ATOM   7772  C5   DG P 106     -28.723   0.144 -35.886  1.00 48.51           C  
ANISOU 7772  C5   DG P 106     5498   6573   6362    470   -179     36       C  
ATOM   7773  C6   DG P 106     -28.818  -0.199 -34.516  1.00 45.36           C  
ANISOU 7773  C6   DG P 106     5087   6222   5926    542   -152    -38       C  
ATOM   7774  O6   DG P 106     -29.059  -1.311 -34.043  1.00 45.73           O  
ANISOU 7774  O6   DG P 106     5162   6327   5885    555    -89    -43       O  
ATOM   7775  N1   DG P 106     -28.605   0.890 -33.666  1.00 45.31           N  
ANISOU 7775  N1   DG P 106     5025   6193   5996    602   -207   -110       N  
ATOM   7776  C2   DG P 106     -28.335   2.168 -34.103  1.00 47.72           C  
ANISOU 7776  C2   DG P 106     5290   6427   6413    593   -282   -108       C  
ATOM   7777  N2   DG P 106     -28.162   3.102 -33.154  1.00 43.12           N  
ANISOU 7777  N2   DG P 106     4651   5830   5903    657   -329   -191       N  
ATOM   7778  N3   DG P 106     -28.245   2.505 -35.393  1.00 48.84           N  
ANISOU 7778  N3   DG P 106     5441   6519   6596    524   -309    -28       N  
ATOM   7779  C4   DG P 106     -28.449   1.452 -36.228  1.00 49.46           C  
ANISOU 7779  C4   DG P 106     5574   6628   6590    465   -254     40       C  
ATOM   7780  P    DC P 107     -25.319   5.347 -40.406  1.00 74.10           P  
ANISOU 7780  P    DC P 107     8596   9496  10061    255   -500    316       P  
ATOM   7781  OP1  DC P 107     -25.377   6.680 -41.052  1.00 74.15           O  
ANISOU 7781  OP1  DC P 107     8539   9434  10202    228   -588    371       O  
ATOM   7782  OP2  DC P 107     -24.533   4.247 -41.023  1.00 73.36           O  
ANISOU 7782  OP2  DC P 107     8565   9453   9855    207   -432    357       O  
ATOM   7783  O5'  DC P 107     -24.820   5.507 -38.894  1.00 71.37           O  
ANISOU 7783  O5'  DC P 107     8239   9142   9736    347   -497    202       O  
ATOM   7784  C5'  DC P 107     -25.361   6.509 -38.036  1.00 66.84           C  
ANISOU 7784  C5'  DC P 107     7602   8527   9267    409   -556    130       C  
ATOM   7785  C4'  DC P 107     -24.766   6.370 -36.645  1.00 64.89           C  
ANISOU 7785  C4'  DC P 107     7353   8300   9001    489   -535     23       C  
ATOM   7786  O4'  DC P 107     -25.263   5.159 -36.015  1.00 61.73           O  
ANISOU 7786  O4'  DC P 107     6999   7980   8477    514   -458    -14       O  
ATOM   7787  C3'  DC P 107     -23.243   6.275 -36.601  1.00 64.28           C  
ANISOU 7787  C3'  DC P 107     7298   8215   8911    488   -522     25       C  
ATOM   7788  O3'  DC P 107     -22.756   7.194 -35.629  1.00 67.63           O  
ANISOU 7788  O3'  DC P 107     7669   8602   9427    553   -570    -61       O  
ATOM   7789  C2'  DC P 107     -22.961   4.817 -36.228  1.00 60.27           C  
ANISOU 7789  C2'  DC P 107     6859   7786   8256    494   -429     12       C  
ATOM   7790  C1'  DC P 107     -24.193   4.474 -35.396  1.00 56.60           C  
ANISOU 7790  C1'  DC P 107     6384   7366   7755    540   -408    -48       C  
ATOM   7791  N1   DC P 107     -24.559   3.014 -35.319  1.00 49.88           N  
ANISOU 7791  N1   DC P 107     5593   6589   6769    529   -322    -34       N  
ATOM   7792  C2   DC P 107     -24.796   2.412 -34.065  1.00 45.31           C  
ANISOU 7792  C2   DC P 107     5016   6071   6127    594   -281   -108       C  
ATOM   7793  O2   DC P 107     -24.694   3.075 -33.023  1.00 44.96           O  
ANISOU 7793  O2   DC P 107     4925   6027   6131    659   -313   -190       O  
ATOM   7794  N3   DC P 107     -25.133   1.095 -34.029  1.00 41.53           N  
ANISOU 7794  N3   DC P 107     4586   5654   5539    581   -206    -86       N  
ATOM   7795  C4   DC P 107     -25.240   0.388 -35.161  1.00 40.19           C  
ANISOU 7795  C4   DC P 107     4462   5486   5323    510   -173     -7       C  
ATOM   7796  N4   DC P 107     -25.576  -0.902 -35.059  1.00 37.51           N  
ANISOU 7796  N4   DC P 107     4164   5201   4885    502   -101      7       N  
ATOM   7797  C5   DC P 107     -25.008   0.975 -36.445  1.00 40.41           C  
ANISOU 7797  C5   DC P 107     4489   5462   5404    444   -212     63       C  
ATOM   7798  C6   DC P 107     -24.676   2.276 -36.471  1.00 45.39           C  
ANISOU 7798  C6   DC P 107     5071   6033   6143    456   -286     51       C  
ATOM   7799  P    DG P 108     -21.208   7.608 -35.582  1.00 70.65           P  
ANISOU 7799  P    DG P 108     8047   8947   9849    557   -589    -64       P  
ATOM   7800  OP1  DG P 108     -21.148   9.047 -35.222  1.00 70.38           O  
ANISOU 7800  OP1  DG P 108     7931   8836   9973    593   -677   -112       O  
ATOM   7801  OP2  DG P 108     -20.537   7.115 -36.811  1.00 68.45           O  
ANISOU 7801  OP2  DG P 108     7816   8670   9521    479   -563     44       O  
ATOM   7802  O5'  DG P 108     -20.674   6.736 -34.355  1.00 65.81           O  
ANISOU 7802  O5'  DG P 108     7467   8404   9135    618   -524   -148       O  
ATOM   7803  C5'  DG P 108     -21.072   7.070 -33.030  1.00 63.09           C  
ANISOU 7803  C5'  DG P 108     7078   8081   8814    698   -538   -262       C  
ATOM   7804  C4'  DG P 108     -20.601   6.013 -32.049  1.00 59.54           C  
ANISOU 7804  C4'  DG P 108     6665   7714   8242    740   -465   -313       C  
ATOM   7805  O4'  DG P 108     -21.241   4.749 -32.360  1.00 54.90           O  
ANISOU 7805  O4'  DG P 108     6136   7188   7535    710   -394   -263       O  
ATOM   7806  C3'  DG P 108     -19.095   5.758 -32.058  1.00 58.41           C  
ANISOU 7806  C3'  DG P 108     6553   7568   8073    734   -444   -299       C  
ATOM   7807  O3'  DG P 108     -18.622   5.827 -30.708  1.00 60.54           O  
ANISOU 7807  O3'  DG P 108     6795   7878   8330    808   -438   -400       O  
ATOM   7808  C2'  DG P 108     -18.964   4.374 -32.698  1.00 54.77           C  
ANISOU 7808  C2'  DG P 108     6169   7153   7486    683   -364   -221       C  
ATOM   7809  C1'  DG P 108     -20.285   3.718 -32.308  1.00 52.38           C  
ANISOU 7809  C1'  DG P 108     5874   6910   7120    699   -329   -239       C  
ATOM   7810  N9   DG P 108     -20.748   2.651 -33.192  1.00 49.21           N  
ANISOU 7810  N9   DG P 108     5529   6534   6634    639   -273   -159       N  
ATOM   7811  C8   DG P 108     -20.791   2.664 -34.565  1.00 47.67           C  
ANISOU 7811  C8   DG P 108     5357   6303   6452    563   -281    -70       C  
ATOM   7812  N7   DG P 108     -21.265   1.565 -35.086  1.00 46.44           N  
ANISOU 7812  N7   DG P 108     5249   6187   6208    523   -222    -22       N  
ATOM   7813  C5   DG P 108     -21.555   0.769 -33.986  1.00 43.98           C  
ANISOU 7813  C5   DG P 108     4948   5938   5825    576   -172    -76       C  
ATOM   7814  C6   DG P 108     -22.098  -0.536 -33.927  1.00 42.99           C  
ANISOU 7814  C6   DG P 108     4864   5871   5601    565   -101    -57       C  
ATOM   7815  O6   DG P 108     -22.431  -1.271 -34.866  1.00 42.97           O  
ANISOU 7815  O6   DG P 108     4899   5875   5554    506    -65      5       O  
ATOM   7816  N1   DG P 108     -22.240  -0.983 -32.613  1.00 42.87           N  
ANISOU 7816  N1   DG P 108     4836   5912   5539    631    -71   -119       N  
ATOM   7817  C2   DG P 108     -21.898  -0.254 -31.498  1.00 44.48           C  
ANISOU 7817  C2   DG P 108     4995   6125   5781    699   -104   -197       C  
ATOM   7818  N2   DG P 108     -22.104  -0.845 -30.313  1.00 43.43           N  
ANISOU 7818  N2   DG P 108     4851   6064   5586    754    -67   -245       N  
ATOM   7819  N3   DG P 108     -21.390   0.975 -31.541  1.00 45.90           N  
ANISOU 7819  N3   DG P 108     5136   6248   6056    710   -171   -225       N  
ATOM   7820  C4   DG P 108     -21.246   1.423 -32.814  1.00 45.63           C  
ANISOU 7820  C4   DG P 108     5113   6150   6074    647   -202   -158       C  
ATOM   7821  P    DG P 109     -17.080   5.619 -30.306  1.00 64.11           P  
ANISOU 7821  P    DG P 109     7265   8338   8755    825   -418   -416       P  
ATOM   7822  OP1  DG P 109     -16.786   6.587 -29.221  1.00 61.16           O  
ANISOU 7822  OP1  DG P 109     6822   7957   8458    894   -469   -526       O  
ATOM   7823  OP2  DG P 109     -16.256   5.607 -31.538  1.00 62.26           O  
ANISOU 7823  OP2  DG P 109     7069   8050   8538    756   -421   -321       O  
ATOM   7824  O5'  DG P 109     -17.063   4.127 -29.714  1.00 60.06           O  
ANISOU 7824  O5'  DG P 109     6806   7923   8091    839   -327   -415       O  
ATOM   7825  C5'  DG P 109     -17.961   3.745 -28.660  1.00 59.09           C  
ANISOU 7825  C5'  DG P 109     6662   7878   7913    892   -302   -479       C  
ATOM   7826  C4'  DG P 109     -17.699   2.338 -28.134  1.00 57.63           C  
ANISOU 7826  C4'  DG P 109     6523   7778   7595    902   -218   -462       C  
ATOM   7827  O4'  DG P 109     -18.405   1.331 -28.916  1.00 55.49           O  
ANISOU 7827  O4'  DG P 109     6305   7521   7258    850   -168   -382       O  
ATOM   7828  C3'  DG P 109     -16.235   1.917 -28.117  1.00 57.75           C  
ANISOU 7828  C3'  DG P 109     6571   7792   7579    895   -189   -442       C  
ATOM   7829  O3'  DG P 109     -15.962   1.275 -26.873  1.00 59.94           O  
ANISOU 7829  O3'  DG P 109     6840   8158   7778    950   -147   -491       O  
ATOM   7830  C2'  DG P 109     -16.110   0.988 -29.327  1.00 55.65           C  
ANISOU 7830  C2'  DG P 109     6374   7505   7265    821   -142   -338       C  
ATOM   7831  C1'  DG P 109     -17.501   0.362 -29.422  1.00 53.02           C  
ANISOU 7831  C1'  DG P 109     6052   7211   6883    810   -113   -318       C  
ATOM   7832  N9   DG P 109     -17.896  -0.001 -30.789  1.00 48.30           N  
ANISOU 7832  N9   DG P 109     5496   6575   6281    735   -100   -232       N  
ATOM   7833  C8   DG P 109     -17.751   0.772 -31.919  1.00 48.18           C  
ANISOU 7833  C8   DG P 109     5479   6487   6339    684   -147   -187       C  
ATOM   7834  N7   DG P 109     -18.191   0.196 -33.008  1.00 47.10           N  
ANISOU 7834  N7   DG P 109     5380   6343   6171    619   -121   -114       N  
ATOM   7835  C5   DG P 109     -18.661  -1.037 -32.588  1.00 42.97           C  
ANISOU 7835  C5   DG P 109     4888   5885   5556    629    -53   -113       C  
ATOM   7836  C6   DG P 109     -19.250  -2.089 -33.335  1.00 41.89           C  
ANISOU 7836  C6   DG P 109     4793   5767   5355    578      0    -55       C  
ATOM   7837  O6   DG P 109     -19.490  -2.139 -34.554  1.00 43.49           O  
ANISOU 7837  O6   DG P 109     5016   5944   5564    512     -3      4       O  
ATOM   7838  N1   DG P 109     -19.583  -3.171 -32.526  1.00 38.54           N  
ANISOU 7838  N1   DG P 109     4383   5406   4855    609     60    -71       N  
ATOM   7839  C2   DG P 109     -19.370  -3.228 -31.169  1.00 41.78           C  
ANISOU 7839  C2   DG P 109     4768   5863   5245    679     68   -130       C  
ATOM   7840  N2   DG P 109     -19.760  -4.354 -30.561  1.00 41.25           N  
ANISOU 7840  N2   DG P 109     4713   5856   5102    697    128   -126       N  
ATOM   7841  N3   DG P 109     -18.818  -2.251 -30.454  1.00 44.82           N  
ANISOU 7841  N3   DG P 109     5112   6238   5679    727     21   -189       N  
ATOM   7842  C4   DG P 109     -18.483  -1.179 -31.223  1.00 46.17           C  
ANISOU 7842  C4   DG P 109     5271   6339   5934    699    -39   -179       C  
ATOM   7843  P    DC P 110     -14.499   0.734 -26.503  1.00 61.23           P  
ANISOU 7843  P    DC P 110     7027   8341   7895    960   -111   -484       P  
ATOM   7844  OP1  DC P 110     -14.457   0.672 -25.024  1.00 62.31           O  
ANISOU 7844  OP1  DC P 110     7118   8568   7988   1033   -102   -564       O  
ATOM   7845  OP2  DC P 110     -13.473   1.497 -27.259  1.00 60.36           O  
ANISOU 7845  OP2  DC P 110     6923   8146   7864    930   -153   -465       O  
ATOM   7846  O5'  DC P 110     -14.495  -0.752 -27.099  1.00 57.95           O  
ANISOU 7846  O5'  DC P 110     6682   7949   7389    912    -33   -393       O  
ATOM   7847  C5'  DC P 110     -15.517  -1.679 -26.733  1.00 54.21           C  
ANISOU 7847  C5'  DC P 110     6215   7541   6840    919     15   -378       C  
ATOM   7848  C4'  DC P 110     -15.443  -2.924 -27.600  1.00 49.39           C  
ANISOU 7848  C4'  DC P 110     5669   6922   6174    861     78   -290       C  
ATOM   7849  O4'  DC P 110     -15.832  -2.622 -28.955  1.00 47.77           O  
ANISOU 7849  O4'  DC P 110     5489   6647   6014    797     57   -241       O  
ATOM   7850  C3'  DC P 110     -14.053  -3.539 -27.717  1.00 47.21           C  
ANISOU 7850  C3'  DC P 110     5427   6638   5872    846    115   -258       C  
ATOM   7851  O3'  DC P 110     -14.025  -4.620 -26.781  1.00 43.57           O  
ANISOU 7851  O3'  DC P 110     4967   6256   5333    879    173   -255       O  
ATOM   7852  C2'  DC P 110     -13.922  -3.931 -29.201  1.00 45.68           C  
ANISOU 7852  C2'  DC P 110     5286   6383   5687    768    132   -184       C  
ATOM   7853  C1'  DC P 110     -15.316  -3.654 -29.766  1.00 43.22           C  
ANISOU 7853  C1'  DC P 110     4968   6059   5395    744    111   -172       C  
ATOM   7854  N1   DC P 110     -15.452  -3.233 -31.220  1.00 39.53           N  
ANISOU 7854  N1   DC P 110     4522   5525   4973    674     84   -122       N  
ATOM   7855  C2   DC P 110     -16.070  -4.094 -32.157  1.00 37.28           C  
ANISOU 7855  C2   DC P 110     4274   5240   4650    617    125    -63       C  
ATOM   7856  O2   DC P 110     -16.482  -5.209 -31.809  1.00 35.36           O  
ANISOU 7856  O2   DC P 110     4049   5043   4344    623    182    -52       O  
ATOM   7857  N3   DC P 110     -16.196  -3.687 -33.448  1.00 36.09           N  
ANISOU 7857  N3   DC P 110     4136   5043   4535    554     99    -18       N  
ATOM   7858  C4   DC P 110     -15.744  -2.487 -33.825  1.00 37.38           C  
ANISOU 7858  C4   DC P 110     4275   5155   4772    546     35    -21       C  
ATOM   7859  N4   DC P 110     -15.892  -2.133 -35.112  1.00 35.22           N  
ANISOU 7859  N4   DC P 110     4009   4846   4528    480     11     34       N  
ATOM   7860  C5   DC P 110     -15.118  -1.598 -32.894  1.00 36.22           C  
ANISOU 7860  C5   DC P 110     4091   4998   4675    604     -8    -79       C  
ATOM   7861  C6   DC P 110     -15.007  -2.000 -31.620  1.00 36.33           C  
ANISOU 7861  C6   DC P 110     4093   5063   4649    667     18   -132       C  
ATOM   7862  P    DG P 111     -12.725  -5.495 -26.474  1.00 44.80           P  
ANISOU 7862  P    DG P 111     5147   6430   5447    882    222   -228       P  
ATOM   7863  OP1  DG P 111     -13.010  -6.259 -25.238  1.00 42.37           O  
ANISOU 7863  OP1  DG P 111     4813   6216   5071    931    261   -238       O  
ATOM   7864  OP2  DG P 111     -11.528  -4.627 -26.571  1.00 45.32           O  
ANISOU 7864  OP2  DG P 111     5205   6450   5562    888    182   -256       O  
ATOM   7865  O5'  DG P 111     -12.673  -6.510 -27.722  1.00 42.75           O  
ANISOU 7865  O5'  DG P 111     4946   6126   5171    810    271   -148       O  
ATOM   7866  C5'  DG P 111     -13.797  -7.341 -27.998  1.00 39.42           C  
ANISOU 7866  C5'  DG P 111     4539   5724   4715    787    307   -112       C  
ATOM   7867  C4'  DG P 111     -13.577  -8.206 -29.226  1.00 38.27           C  
ANISOU 7867  C4'  DG P 111     4445   5534   4563    718    349    -50       C  
ATOM   7868  O4'  DG P 111     -13.806  -7.457 -30.446  1.00 35.96           O  
ANISOU 7868  O4'  DG P 111     4167   5181   4317    666    310    -39       O  
ATOM   7869  C3'  DG P 111     -12.183  -8.790 -29.351  1.00 37.27           C  
ANISOU 7869  C3'  DG P 111     4342   5391   4428    705    383    -29       C  
ATOM   7870  O3'  DG P 111     -12.381 -10.165 -29.562  1.00 38.88           O  
ANISOU 7870  O3'  DG P 111     4570   5607   4595    680    448     16       O  
ATOM   7871  C2'  DG P 111     -11.566  -8.063 -30.551  1.00 34.84           C  
ANISOU 7871  C2'  DG P 111     4055   5015   4167    655    349    -19       C  
ATOM   7872  C1'  DG P 111     -12.800  -7.753 -31.387  1.00 33.53           C  
ANISOU 7872  C1'  DG P 111     3893   4830   4016    617    328     -5       C  
ATOM   7873  N9   DG P 111     -12.751  -6.591 -32.277  1.00 33.34           N  
ANISOU 7873  N9   DG P 111     3864   4755   4047    584    268     -4       N  
ATOM   7874  C8   DG P 111     -12.206  -5.350 -32.035  1.00 29.30           C  
ANISOU 7874  C8   DG P 111     3325   4217   3591    609    207    -37       C  
ATOM   7875  N7   DG P 111     -12.361  -4.521 -33.038  1.00 34.32           N  
ANISOU 7875  N7   DG P 111     3959   4807   4276    566    161    -17       N  
ATOM   7876  C5   DG P 111     -13.063  -5.243 -34.006  1.00 31.64           C  
ANISOU 7876  C5   DG P 111     3647   4469   3905    508    194     30       C  
ATOM   7877  C6   DG P 111     -13.523  -4.879 -35.306  1.00 32.43           C  
ANISOU 7877  C6   DG P 111     3754   4541   4029    443    170     73       C  
ATOM   7878  O6   DG P 111     -13.402  -3.798 -35.911  1.00 33.57           O  
ANISOU 7878  O6   DG P 111     3878   4646   4230    420    112     87       O  
ATOM   7879  N1   DG P 111     -14.188  -5.931 -35.943  1.00 32.19           N  
ANISOU 7879  N1   DG P 111     3751   4533   3948    400    222    105       N  
ATOM   7880  C2   DG P 111     -14.389  -7.182 -35.396  1.00 32.02           C  
ANISOU 7880  C2   DG P 111     3747   4548   3871    417    287     99       C  
ATOM   7881  N2   DG P 111     -15.055  -8.076 -36.152  1.00 23.95           N  
ANISOU 7881  N2   DG P 111     2747   3538   2814    369    328    129       N  
ATOM   7882  N3   DG P 111     -13.969  -7.525 -34.178  1.00 28.71           N  
ANISOU 7882  N3   DG P 111     3321   4154   3434    477    308     68       N  
ATOM   7883  C4   DG P 111     -13.311  -6.521 -33.544  1.00 31.83           C  
ANISOU 7883  C4   DG P 111     3691   4536   3869    520    260     34       C  
ATOM   7884  P    DG P 112     -11.156 -11.181 -29.628  1.00 41.24           P  
ANISOU 7884  P    DG P 112     4892   5897   4881    666    501     46       P  
ATOM   7885  OP1  DG P 112     -11.650 -12.478 -29.108  1.00 40.78           O  
ANISOU 7885  OP1  DG P 112     4829   5877   4787    676    559     78       O  
ATOM   7886  OP2  DG P 112      -9.933 -10.541 -29.089  1.00 39.37           O  
ANISOU 7886  OP2  DG P 112     4643   5658   4659    700    476     19       O  
ATOM   7887  O5'  DG P 112     -10.933 -11.304 -31.203  1.00 39.18           O  
ANISOU 7887  O5'  DG P 112     4670   5575   4642    590    508     72       O  
ATOM   7888  C5'  DG P 112     -11.991 -11.716 -32.073  1.00 37.07           C  
ANISOU 7888  C5'  DG P 112     4417   5298   4369    543    523     94       C  
ATOM   7889  C4'  DG P 112     -11.550 -11.488 -33.510  1.00 36.59           C  
ANISOU 7889  C4'  DG P 112     4383   5191   4329    475    515    109       C  
ATOM   7890  O4'  DG P 112     -11.640 -10.079 -33.835  1.00 30.62           O  
ANISOU 7890  O4'  DG P 112     3615   4414   3606    472    446     94       O  
ATOM   7891  C3'  DG P 112     -10.103 -11.886 -33.795  1.00 34.93           C  
ANISOU 7891  C3'  DG P 112     4190   4959   4124    458    541    116       C  
ATOM   7892  O3'  DG P 112     -10.107 -12.974 -34.701  1.00 37.74           O  
ANISOU 7892  O3'  DG P 112     4568   5303   4467    404    593    139       O  
ATOM   7893  C2'  DG P 112      -9.481 -10.632 -34.400  1.00 35.09           C  
ANISOU 7893  C2'  DG P 112     4209   4948   4175    440    484    107       C  
ATOM   7894  C1'  DG P 112     -10.715  -9.860 -34.855  1.00 32.75           C  
ANISOU 7894  C1'  DG P 112     3902   4650   3892    423    440    109       C  
ATOM   7895  N9   DG P 112     -10.490  -8.432 -35.064  1.00 33.09           N  
ANISOU 7895  N9   DG P 112     3928   4667   3979    425    370     99       N  
ATOM   7896  C8   DG P 112      -9.842  -7.543 -34.237  1.00 33.84           C  
ANISOU 7896  C8   DG P 112     4000   4754   4104    475    328     68       C  
ATOM   7897  N7   DG P 112      -9.786  -6.326 -34.722  1.00 37.40           N  
ANISOU 7897  N7   DG P 112     4433   5172   4604    461    265     68       N  
ATOM   7898  C5   DG P 112     -10.430  -6.419 -35.956  1.00 34.88           C  
ANISOU 7898  C5   DG P 112     4127   4844   4282    395    266    107       C  
ATOM   7899  C6   DG P 112     -10.683  -5.436 -36.951  1.00 33.06           C  
ANISOU 7899  C6   DG P 112     3884   4585   4093    350    211    135       C  
ATOM   7900  O6   DG P 112     -10.373  -4.245 -36.944  1.00 33.38           O  
ANISOU 7900  O6   DG P 112     3898   4594   4193    360    148    131       O  
ATOM   7901  N1   DG P 112     -11.371  -5.946 -38.051  1.00 33.10           N  
ANISOU 7901  N1   DG P 112     3904   4601   4070    287    233    173       N  
ATOM   7902  C2   DG P 112     -11.762  -7.260 -38.177  1.00 34.95           C  
ANISOU 7902  C2   DG P 112     4164   4866   4249    270    301    177       C  
ATOM   7903  N2   DG P 112     -12.407  -7.586 -39.304  1.00 34.15           N  
ANISOU 7903  N2   DG P 112     4073   4777   4128    206    313    209       N  
ATOM   7904  N3   DG P 112     -11.531  -8.195 -37.257  1.00 34.33           N  
ANISOU 7904  N3   DG P 112     4097   4806   4140    311    351    153       N  
ATOM   7905  C4   DG P 112     -10.863  -7.711 -36.178  1.00 32.61           C  
ANISOU 7905  C4   DG P 112     3864   4582   3942    373    330    122       C  
ATOM   7906  P    DC P 113      -8.841 -13.926 -34.882  1.00 38.69           P  
ANISOU 7906  P    DC P 113     4704   5409   4589    388    644    146       P  
ATOM   7907  OP1  DC P 113      -9.122 -15.225 -34.277  1.00 41.14           O  
ANISOU 7907  OP1  DC P 113     5008   5734   4888    406    701    159       O  
ATOM   7908  OP2  DC P 113      -7.594 -13.169 -34.638  1.00 42.21           O  
ANISOU 7908  OP2  DC P 113     5148   5841   5050    408    614    134       O  
ATOM   7909  O5'  DC P 113      -8.826 -14.190 -36.427  1.00 44.81           O  
ANISOU 7909  O5'  DC P 113     5497   6164   5364    309    658    154       O  
ATOM   7910  C5'  DC P 113      -8.457 -13.083 -37.147  1.00 43.76           C  
ANISOU 7910  C5'  DC P 113     5366   6018   5242    282    609    154       C  
ATOM   7911  C4'  DC P 113      -9.473 -12.911 -38.230  1.00 39.91           C  
ANISOU 7911  C4'  DC P 113     4880   5537   4746    226    597    166       C  
ATOM   7912  O4'  DC P 113      -9.924 -11.538 -38.227  1.00 41.54           O  
ANISOU 7912  O4'  DC P 113     5073   5740   4971    236    527    170       O  
ATOM   7913  C3'  DC P 113      -8.778 -13.145 -39.541  1.00 38.95           C  
ANISOU 7913  C3'  DC P 113     4770   5412   4618    157    613    173       C  
ATOM   7914  O3'  DC P 113      -9.669 -13.739 -40.465  1.00 34.64           O  
ANISOU 7914  O3'  DC P 113     4227   4882   4052    104    638    178       O  
ATOM   7915  C2'  DC P 113      -8.293 -11.747 -39.925  1.00 38.03           C  
ANISOU 7915  C2'  DC P 113     4644   5284   4520    147    548    185       C  
ATOM   7916  C1'  DC P 113      -9.330 -10.825 -39.289  1.00 38.08           C  
ANISOU 7916  C1'  DC P 113     4635   5290   4544    186    496    185       C  
ATOM   7917  N1   DC P 113      -8.745  -9.543 -38.781  1.00 33.79           N  
ANISOU 7917  N1   DC P 113     4075   4725   4037    222    434    181       N  
ATOM   7918  C2   DC P 113      -9.015  -8.364 -39.491  1.00 35.12           C  
ANISOU 7918  C2   DC P 113     4228   4883   4235    192    372    202       C  
ATOM   7919  O2   DC P 113      -9.739  -8.421 -40.495  1.00 39.64           O  
ANISOU 7919  O2   DC P 113     4800   5469   4794    136    371    228       O  
ATOM   7920  N3   DC P 113      -8.492  -7.186 -39.055  1.00 32.79           N  
ANISOU 7920  N3   DC P 113     3911   4561   3985    224    313    197       N  
ATOM   7921  C4   DC P 113      -7.726  -7.163 -37.963  1.00 31.21           C  
ANISOU 7921  C4   DC P 113     3710   4353   3796    283    317    165       C  
ATOM   7922  N4   DC P 113      -7.237  -5.978 -37.580  1.00 26.57           N  
ANISOU 7922  N4   DC P 113     3099   3739   3259    313    257    155       N  
ATOM   7923  C5   DC P 113      -7.428  -8.360 -37.225  1.00 34.06           C  
ANISOU 7923  C5   DC P 113     4088   4734   4120    314    381    146       C  
ATOM   7924  C6   DC P 113      -7.950  -9.519 -37.666  1.00 31.89           C  
ANISOU 7924  C6   DC P 113     3831   4478   3806    282    437    157       C  
ATOM   7925  P    DG P 114      -8.976 -14.441 -41.707  1.00 37.61           P  
ANISOU 7925  P    DG P 114     4610   5268   4414     35    677    172       P  
ATOM   7926  OP1  DG P 114      -9.968 -15.367 -42.299  1.00 43.12           O  
ANISOU 7926  OP1  DG P 114     5307   5983   5094     -4    716    165       O  
ATOM   7927  OP2  DG P 114      -7.642 -14.925 -41.303  1.00 36.81           O  
ANISOU 7927  OP2  DG P 114     4514   5149   4324     55    708    158       O  
ATOM   7928  O5'  DG P 114      -8.735 -13.219 -42.699  1.00 31.85           O  
ANISOU 7928  O5'  DG P 114     3872   4550   3681    -11    621    195       O  
ATOM   7929  C5'  DG P 114      -9.858 -12.537 -43.226  1.00 34.72           C  
ANISOU 7929  C5'  DG P 114     4225   4929   4039    -38    581    217       C  
ATOM   7930  C4'  DG P 114      -9.421 -11.719 -44.422  1.00 34.49           C  
ANISOU 7930  C4'  DG P 114     4183   4920   4003    -99    543    245       C  
ATOM   7931  O4'  DG P 114      -8.989 -10.415 -43.967  1.00 33.84           O  
ANISOU 7931  O4'  DG P 114     4089   4810   3957    -67    479    265       O  
ATOM   7932  C3'  DG P 114      -8.266 -12.317 -45.212  1.00 33.05           C  
ANISOU 7932  C3'  DG P 114     4002   4755   3799   -145    581    233       C  
ATOM   7933  O3'  DG P 114      -8.652 -12.259 -46.584  1.00 35.40           O  
ANISOU 7933  O3'  DG P 114     4285   5100   4064   -223    577    251       O  
ATOM   7934  C2'  DG P 114      -7.056 -11.472 -44.808  1.00 33.35           C  
ANISOU 7934  C2'  DG P 114     4039   4768   3865   -117    546    244       C  
ATOM   7935  C1'  DG P 114      -7.673 -10.140 -44.389  1.00 31.36           C  
ANISOU 7935  C1'  DG P 114     3773   4496   3647    -88    473    273       C  
ATOM   7936  N9   DG P 114      -7.007  -9.475 -43.270  1.00 28.37           N  
ANISOU 7936  N9   DG P 114     3394   4078   3308    -21    442    264       N  
ATOM   7937  C8   DG P 114      -6.530 -10.074 -42.128  1.00 27.69           C  
ANISOU 7937  C8   DG P 114     3322   3973   3227     40    475    231       C  
ATOM   7938  N7   DG P 114      -5.983  -9.239 -41.290  1.00 25.72           N  
ANISOU 7938  N7   DG P 114     3064   3695   3012     91    435    226       N  
ATOM   7939  C5   DG P 114      -6.102  -8.004 -41.910  1.00 25.22           C  
ANISOU 7939  C5   DG P 114     2980   3625   2978     63    369    257       C  
ATOM   7940  C6   DG P 114      -5.684  -6.719 -41.474  1.00 26.17           C  
ANISOU 7940  C6   DG P 114     3079   3713   3151     95    303    264       C  
ATOM   7941  O6   DG P 114      -5.111  -6.440 -40.419  1.00 24.65           O  
ANISOU 7941  O6   DG P 114     2885   3498   2984    155    291    236       O  
ATOM   7942  N1   DG P 114      -5.984  -5.705 -42.393  1.00 23.39           N  
ANISOU 7942  N1   DG P 114     2703   3359   2826     48    246    308       N  
ATOM   7943  C2   DG P 114      -6.616  -5.931 -43.597  1.00 25.03           C  
ANISOU 7943  C2   DG P 114     2907   3601   3002    -22    254    344       C  
ATOM   7944  N2   DG P 114      -6.837  -4.854 -44.361  1.00 19.73           N  
ANISOU 7944  N2   DG P 114     2205   2927   2364    -61    192    394       N  
ATOM   7945  N3   DG P 114      -7.016  -7.135 -44.012  1.00 26.65           N  
ANISOU 7945  N3   DG P 114     3132   3842   3151    -52    317    331       N  
ATOM   7946  C4   DG P 114      -6.731  -8.126 -43.129  1.00 25.04           C  
ANISOU 7946  C4   DG P 114     2952   3631   2929     -6    372    286       C  
HETATM 7947  P   2DA P 115      -7.679 -12.489 -47.830  1.00 36.24           P  
ANISOU 7947  P   2DA P 115     4380   5252   4139   -293    597    250       P  
HETATM 7948  OP1 2DA P 115      -8.541 -12.490 -49.081  1.00 37.04           O  
ANISOU 7948  OP1 2DA P 115     4460   5414   4200   -367    592    267       O  
HETATM 7949  OP2 2DA P 115      -6.758 -13.646 -47.544  1.00 33.83           O  
ANISOU 7949  OP2 2DA P 115     4087   4934   3832   -279    662    202       O  
HETATM 7950  O5' 2DA P 115      -6.882 -11.095 -47.829  1.00 36.11           O  
ANISOU 7950  O5' 2DA P 115     4350   5222   4148   -287    530    295       O  
HETATM 7951  C5' 2DA P 115      -5.529 -10.947 -48.226  1.00 31.63           C  
ANISOU 7951  C5' 2DA P 115     3777   4665   3577   -308    532    298       C  
HETATM 7952  C4' 2DA P 115      -5.302  -9.444 -48.278  1.00 28.77           C  
ANISOU 7952  C4' 2DA P 115     3396   4289   3248   -306    453    354       C  
HETATM 7953  O4' 2DA P 115      -5.552  -8.857 -46.997  1.00 27.49           O  
ANISOU 7953  O4' 2DA P 115     3243   4066   3137   -230    419    350       O  
HETATM 7954  C3' 2DA P 115      -3.862  -9.127 -48.628  1.00 26.82           C  
ANISOU 7954  C3' 2DA P 115     3140   4049   3002   -325    446    366       C  
HETATM 7955  C2' 2DA P 115      -3.567  -7.868 -47.834  1.00 28.08           C  
ANISOU 7955  C2' 2DA P 115     3293   4153   3224   -274    379    395       C  
HETATM 7956  C1' 2DA P 115      -4.629  -7.795 -46.752  1.00 25.18           C  
ANISOU 7956  C1' 2DA P 115     2937   3743   2886   -211    368    376       C  
HETATM 7957  N9  2DA P 115      -3.998  -7.944 -45.414  1.00 26.25           N  
ANISOU 7957  N9  2DA P 115     3093   3830   3051   -133    380    337       N  
HETATM 7958  C8  2DA P 115      -3.838  -9.090 -44.718  1.00 21.89           C  
ANISOU 7958  C8  2DA P 115     2565   3270   2481    -98    442    290       C  
HETATM 7959  N7  2DA P 115      -3.230  -8.808 -43.541  1.00 22.28           N  
ANISOU 7959  N7  2DA P 115     2621   3279   2564    -30    430    271       N  
HETATM 7960  C5  2DA P 115      -3.005  -7.470 -43.512  1.00 23.26           C  
ANISOU 7960  C5  2DA P 115     2725   3383   2732    -22    359    299       C  
HETATM 7961  C6  2DA P 115      -2.420  -6.609 -42.579  1.00 24.78           C  
ANISOU 7961  C6  2DA P 115     2908   3534   2973     35    316    291       C  
HETATM 7962  N6  2DA P 115      -1.930  -7.095 -41.397  1.00 18.85           N  
ANISOU 7962  N6  2DA P 115     2172   2765   2224     99    345    250       N  
HETATM 7963  N1  2DA P 115      -2.352  -5.276 -42.871  1.00 22.09           N  
ANISOU 7963  N1  2DA P 115     2538   3172   2681     24    243    326       N  
HETATM 7964  C2  2DA P 115      -2.839  -4.785 -44.023  1.00 23.03           C  
ANISOU 7964  C2  2DA P 115     2638   3314   2800    -40    212    376       C  
HETATM 7965  N3  2DA P 115      -3.395  -5.597 -44.939  1.00 23.27           N  
ANISOU 7965  N3  2DA P 115     2676   3391   2774    -97    254    387       N  
HETATM 7966  C4  2DA P 115      -3.491  -6.935 -44.699  1.00 23.96           C  
ANISOU 7966  C4  2DA P 115     2792   3497   2813    -88    328    344       C  
TER    7967      2DA P 115                                                      
HETATM 7968  PA  TTP A 903      -0.175 -10.420 -49.140  1.00 45.82           P  
ANISOU 7968  PA  TTP A 903     5556   6481   5373   -353    542    303       P  
HETATM 7969  O1A TTP A 903      -0.733 -11.303 -48.057  1.00 48.65           O  
ANISOU 7969  O1A TTP A 903     5942   6794   5747   -292    584    257       O  
HETATM 7970  O2A TTP A 903      -0.765 -10.805 -50.473  1.00 51.41           O  
ANISOU 7970  O2A TTP A 903     6240   7267   6025   -433    561    307       O  
HETATM 7971  O3A TTP A 903       1.420 -10.591 -49.142  1.00 49.55           O  
ANISOU 7971  O3A TTP A 903     6030   6950   5847   -351    563    288       O  
HETATM 7972  PB  TTP A 903       2.570 -10.094 -50.158  1.00 45.11           P  
ANISOU 7972  PB  TTP A 903     5440   6436   5263   -409    546    318       P  
HETATM 7973  O1B TTP A 903       3.292  -8.932 -49.533  1.00 43.32           O  
ANISOU 7973  O1B TTP A 903     5212   6161   5087   -370    487    358       O  
HETATM 7974  O2B TTP A 903       2.099  -9.806 -51.561  1.00 44.04           O  
ANISOU 7974  O2B TTP A 903     5269   6386   5080   -493    530    356       O  
HETATM 7975  O3B TTP A 903       3.511 -11.387 -50.074  1.00 45.32           O  
ANISOU 7975  O3B TTP A 903     5480   6465   5273   -403    622    251       O  
HETATM 7976  PG  TTP A 903       3.295 -12.720 -50.959  1.00 43.14           P  
ANISOU 7976  PG  TTP A 903     5194   6248   4948   -456    694    195       P  
HETATM 7977  O1G TTP A 903       2.031 -12.667 -51.747  1.00 39.30           O  
ANISOU 7977  O1G TTP A 903     4691   5815   4428   -505    684    210       O  
HETATM 7978  O2G TTP A 903       4.458 -12.745 -51.917  1.00 42.46           O  
ANISOU 7978  O2G TTP A 903     5083   6222   4830   -511    706    191       O  
HETATM 7979  O3G TTP A 903       3.339 -13.940 -50.067  1.00 43.79           O  
ANISOU 7979  O3G TTP A 903     5302   6277   5057   -405    754    132       O  
HETATM 7980  O5' TTP A 903      -0.407  -8.868 -48.772  1.00 46.30           O  
ANISOU 7980  O5' TTP A 903     5604   6508   5481   -329    456    363       O  
HETATM 7981  C5' TTP A 903      -0.435  -7.895 -49.808  1.00 40.53           C  
ANISOU 7981  C5' TTP A 903     4837   5818   4744   -389    403    427       C  
HETATM 7982  C4' TTP A 903       0.035  -6.555 -49.279  1.00 42.06           C  
ANISOU 7982  C4' TTP A 903     5017   5960   5002   -355    331    471       C  
HETATM 7983  O4' TTP A 903      -0.742  -6.192 -48.133  1.00 44.98           O  
ANISOU 7983  O4' TTP A 903     5400   6268   5420   -286    305    456       O  
HETATM 7984  C3' TTP A 903       1.471  -6.577 -48.785  1.00 42.62           C  
ANISOU 7984  C3' TTP A 903     5099   6003   5091   -324    342    451       C  
HETATM 7985  O3' TTP A 903       2.439  -6.392 -49.825  1.00 44.48           O  
ANISOU 7985  O3' TTP A 903     5311   6289   5300   -386    339    484       O  
HETATM 7986  C2' TTP A 903       1.469  -5.443 -47.779  1.00 42.43           C  
ANISOU 7986  C2' TTP A 903     5070   5908   5142   -262    277    468       C  
HETATM 7987  C1' TTP A 903       0.068  -5.521 -47.161  1.00 41.68           C  
ANISOU 7987  C1' TTP A 903     4985   5790   5059   -226    272    450       C  
HETATM 7988  N1  TTP A 903       0.243  -6.281 -45.916  1.00 41.26           N  
ANISOU 7988  N1  TTP A 903     4966   5702   5011   -154    315    387       N  
HETATM 7989  C2  TTP A 903       0.734  -5.578 -44.792  1.00 38.84           C  
ANISOU 7989  C2  TTP A 903     4659   5339   4760    -87    278    374       C  
HETATM 7990  O2  TTP A 903       0.956  -4.350 -44.878  1.00 39.10           O  
ANISOU 7990  O2  TTP A 903     4664   5348   4845    -88    210    411       O  
HETATM 7991  N3  TTP A 903       0.958  -6.205 -43.632  1.00 40.95           N  
ANISOU 7991  N3  TTP A 903     4949   5581   5027    -22    314    323       N  
HETATM 7992  C4  TTP A 903       0.729  -7.514 -43.490  1.00 40.11           C  
ANISOU 7992  C4  TTP A 903     4868   5495   4877    -19    384    288       C  
HETATM 7993  O4  TTP A 903       0.951  -8.072 -42.391  1.00 42.73           O  
ANISOU 7993  O4  TTP A 903     5217   5807   5213     41    415    251       O  
HETATM 7994  C5  TTP A 903       0.223  -8.288 -44.647  1.00 38.89           C  
ANISOU 7994  C5  TTP A 903     4715   5389   4673    -87    424    296       C  
HETATM 7995  C5M TTP A 903      -0.047  -9.774 -44.520  1.00 36.88           C  
ANISOU 7995  C5M TTP A 903     4482   5150   4382    -85    502    255       C  
HETATM 7996  C6  TTP A 903       0.002  -7.607 -45.839  1.00 39.21           C  
ANISOU 7996  C6  TTP A 903     4731   5463   4706   -154    387    344       C  
HETATM 7997 CA    CA A 904       0.708 -11.110 -52.747  1.00 27.75          CA  
HETATM 7998 CA    CA A 905      -2.891 -11.671 -51.544  1.00 53.52          CA  
HETATM 7999 CA    CA A 906       3.254 -48.457 -52.863  1.00 56.40          CA  
HETATM 8000 CA    CA A 907       2.432 -16.065 -55.222  1.00 75.70          CA  
HETATM 8001 CA    CA A 908       3.395 -24.675 -13.046  1.00 59.86          CA  
HETATM 8002  O   HOH A 909     -18.817  -8.411 -10.512  1.00 30.02           O  
HETATM 8003  O   HOH A 910      10.704   8.322 -45.907  1.00 13.37           O  
HETATM 8004  O   HOH A 911      -4.573  -4.204 -47.252  1.00 13.14           O  
HETATM 8005  O   HOH A 912      29.241   7.077 -32.414  1.00 14.80           O  
HETATM 8006  O   HOH A 913      15.133 -21.936 -32.856  1.00 13.25           O  
HETATM 8007  O   HOH A 914     -28.659 -34.346 -26.358  1.00 33.98           O  
HETATM 8008  O   HOH A 915      25.395  21.330 -44.644  1.00 21.10           O  
HETATM 8009  O   HOH A 916     -27.749 -31.820 -53.866  1.00 20.39           O  
HETATM 8010  O   HOH A 917       9.470  -6.206  -2.426  1.00 40.60           O  
HETATM 8011  O   HOH A 918      13.400   4.917 -36.038  1.00 24.57           O  
HETATM 8012  O   HOH A 919       5.273 -33.685 -23.296  1.00 26.63           O  
HETATM 8013  O   HOH A 920      22.154 -21.112 -18.127  1.00 12.09           O  
HETATM 8014  O   HOH A 921       7.772  -4.723  -9.008  1.00 40.76           O  
HETATM 8015  O   HOH A 922      24.592 -11.474 -40.178  1.00 16.09           O  
HETATM 8016  O   HOH A 923       5.069   9.191 -65.680  1.00 23.84           O  
HETATM 8017  O   HOH A 924     -21.009  -7.736 -51.269  1.00 12.88           O  
HETATM 8018  O   HOH A 925      21.940  -6.882 -25.693  1.00 14.05           O  
HETATM 8019  O   HOH A 926       4.927  -2.685 -63.644  1.00 25.57           O  
HETATM 8020  O   HOH A 927     -14.890 -23.180 -27.859  1.00 11.73           O  
HETATM 8021  O   HOH A 928      -0.699 -16.130 -31.293  1.00 19.79           O  
HETATM 8022  O   HOH A 929     -14.561  -7.032 -62.713  1.00 21.03           O  
HETATM 8023  O   HOH A 930      25.215 -20.863 -35.931  1.00 25.01           O  
HETATM 8024  O   HOH A 931       4.622 -29.923 -38.759  1.00 29.79           O  
HETATM 8025  O   HOH A 932      18.896  -2.766 -29.985  1.00 13.87           O  
HETATM 8026  O   HOH A 933       9.419 -30.781 -31.504  1.00 18.59           O  
HETATM 8027  O   HOH A 934      28.752 -17.126 -16.871  1.00 29.10           O  
HETATM 8028  O   HOH A 935      -9.643 -28.570 -45.871  1.00 14.62           O  
HETATM 8029  O   HOH A 936      19.005  22.184 -38.561  1.00 21.55           O  
HETATM 8030  O   HOH A 937       0.460   9.124 -38.581  1.00 13.55           O  
HETATM 8031  O   HOH A 938      10.241 -10.978 -23.900  1.00 18.84           O  
HETATM 8032  O   HOH A 939      20.440  12.603 -43.135  1.00 28.01           O  
HETATM 8033  O   HOH A 940     -14.981 -30.828 -42.740  1.00 17.79           O  
HETATM 8034  O   HOH A 941     -16.987 -18.418 -61.222  1.00 21.79           O  
HETATM 8035  O   HOH A 942     -12.733 -20.756 -13.298  1.00 24.69           O  
HETATM 8036  O   HOH A 943       0.741 -21.881 -18.525  1.00 16.02           O  
HETATM 8037  O   HOH A 944     -18.735 -30.259 -34.202  1.00 14.67           O  
HETATM 8038  O   HOH A 945      21.085  -4.931  -0.348  1.00 19.97           O  
HETATM 8039  O   HOH A 946     -12.291 -26.267 -34.784  1.00 16.37           O  
HETATM 8040  O   HOH A 947      -2.751  -1.120 -47.273  1.00 25.56           O  
HETATM 8041  O   HOH A 948      33.239  16.060 -24.863  1.00 27.73           O  
HETATM 8042  O   HOH A 949      29.944 -19.410 -21.841  1.00 23.76           O  
HETATM 8043  O   HOH A 950     -10.127 -10.361 -48.811  1.00 21.90           O  
HETATM 8044  O   HOH A 951      26.042  -6.652 -21.932  1.00 14.40           O  
HETATM 8045  O   HOH A 952       6.585  -9.478 -66.113  1.00 32.86           O  
HETATM 8046  O   HOH A 953      16.326  -1.632 -55.514  1.00 28.39           O  
HETATM 8047  O   HOH A 954       7.029  11.429 -32.507  1.00 36.20           O  
HETATM 8048  O   HOH A 955     -12.419 -22.291 -28.254  1.00  4.18           O  
HETATM 8049  O   HOH A 956      -9.084 -26.436 -15.788  1.00 35.66           O  
HETATM 8050  O  AHOH A 957      13.358 -25.058 -44.458  0.50  2.00           O  
HETATM 8051  O  BHOH A 957      14.197 -22.917 -44.277  0.50  3.55           O  
HETATM 8052  O   HOH A 958     -20.248 -19.566 -61.293  1.00 18.74           O  
HETATM 8053  O   HOH A 959      22.891  -4.137 -39.953  1.00 15.63           O  
HETATM 8054  O   HOH A 960      28.778  -2.247 -39.312  1.00 14.83           O  
HETATM 8055  O   HOH A 961       5.208 -22.766 -13.273  1.00 31.36           O  
HETATM 8056  O   HOH A 962       2.786  -9.498 -63.838  1.00 16.87           O  
HETATM 8057  O   HOH A 963      21.487   1.828 -57.845  1.00 25.22           O  
HETATM 8058  O   HOH A 964     -10.729 -20.369 -15.140  1.00 43.45           O  
HETATM 8059  O   HOH A 965     -32.801 -23.277 -45.424  1.00 43.40           O  
HETATM 8060  O   HOH A 966       4.877  -7.930 -57.526  1.00  5.57           O  
HETATM 8061  O   HOH A 967      -3.978 -34.807 -27.642  1.00 42.99           O  
HETATM 8062  O   HOH A 968     -28.392 -26.258 -19.913  1.00 36.74           O  
HETATM 8063  O   HOH A 969       1.394 -26.860  -4.336  1.00 15.30           O  
HETATM 8064  O   HOH A 970      23.241 -23.133 -27.548  1.00 19.26           O  
HETATM 8065  O   HOH A 971     -15.813 -30.042 -61.961  1.00 14.84           O  
HETATM 8066  O   HOH A 972      21.789  -8.364  -0.631  1.00 20.52           O  
HETATM 8067  O   HOH A 973      16.607 -39.737 -59.979  1.00 20.40           O  
HETATM 8068  O   HOH A 974       4.679 -10.447 -29.209  1.00 21.61           O  
HETATM 8069  O   HOH A 975       5.094 -31.147 -45.923  1.00 14.93           O  
HETATM 8070  O   HOH A 976      19.730 -37.784 -15.122  1.00 35.91           O  
HETATM 8071  O   HOH A 977     -31.379 -24.700 -23.679  1.00 11.51           O  
HETATM 8072  O   HOH A 978       5.441 -21.498  -1.674  1.00 15.69           O  
HETATM 8073  O   HOH A 979      33.834 -19.618 -22.520  1.00 23.22           O  
HETATM 8074  O   HOH A 980      13.138  18.528 -60.674  1.00 23.55           O  
HETATM 8075  O   HOH A 981     -16.229  -2.201 -55.894  1.00 13.93           O  
HETATM 8076  O   HOH A 982      37.875  -8.183 -29.319  1.00 27.01           O  
HETATM 8077  O   HOH A 983      20.411  -1.119 -10.678  1.00 20.88           O  
HETATM 8078  O   HOH A 984      -4.559  13.360 -41.688  1.00 39.16           O  
HETATM 8079  O   HOH A 985      19.826 -11.256 -49.743  1.00 17.23           O  
HETATM 8080  O   HOH A 986      37.179  -4.687 -19.847  1.00 20.35           O  
HETATM 8081  O   HOH A 987       3.423  -9.399 -43.644  1.00  9.75           O  
HETATM 8082  O   HOH A 988       5.242  -4.609 -33.991  1.00 19.49           O  
HETATM 8083  O   HOH A 989      12.637 -23.293   3.195  1.00 15.36           O  
HETATM 8084  O   HOH A 990      -4.262   4.460 -51.035  1.00 19.77           O  
HETATM 8085  O   HOH A 991       3.748 -11.816 -43.021  1.00 10.83           O  
HETATM 8086  O   HOH A 992      -5.482 -31.516 -56.520  1.00  9.11           O  
HETATM 8087  O   HOH A 993      18.775  -5.053 -45.548  1.00 20.12           O  
HETATM 8088  O   HOH A 994       6.936  -6.672 -37.234  1.00 16.14           O  
HETATM 8089  O   HOH A 995      26.003 -18.596 -42.078  1.00 35.96           O  
HETATM 8090  O   HOH A 996      14.652  -0.464 -18.613  1.00 34.01           O  
HETATM 8091  O   HOH A 997      18.532   4.794 -39.232  1.00 23.07           O  
HETATM 8092  O   HOH A 998      30.282  -6.598 -15.956  1.00 17.21           O  
HETATM 8093  O   HOH A 999      26.908 -13.413 -13.993  1.00 27.13           O  
HETATM 8094  O   HOH A1000      -4.355  14.248 -66.496  1.00 31.58           O  
HETATM 8095  O   HOH A1001      17.982  10.975 -33.399  1.00 25.76           O  
HETATM 8096  O   HOH A1002      -6.302 -31.209 -30.553  1.00 43.79           O  
HETATM 8097  O   HOH A1003      14.969  14.064 -51.569  1.00 22.39           O  
HETATM 8098  O   HOH A1004       4.294  12.981 -42.950  1.00 17.39           O  
HETATM 8099  O   HOH A1005       6.132 -36.398  -0.332  1.00 14.59           O  
HETATM 8100  O   HOH A1006     -31.473 -29.861 -43.088  1.00 24.10           O  
HETATM 8101  O   HOH A1007      18.450  17.926 -30.345  1.00 19.96           O  
HETATM 8102  O   HOH A1008     -18.690 -10.082 -57.971  1.00 19.23           O  
HETATM 8103  O   HOH A1009      10.179  -7.313 -53.561  1.00 18.50           O  
HETATM 8104  O   HOH A1010      22.556  -4.423 -44.640  1.00 28.21           O  
HETATM 8105  O   HOH A1011     -21.620 -23.294 -58.493  1.00 19.33           O  
HETATM 8106  O   HOH A1012      21.345  22.254 -39.518  1.00 23.68           O  
HETATM 8107  O   HOH A1013       1.010 -28.061  -1.943  1.00 14.74           O  
HETATM 8108  O   HOH A1014       6.789 -18.232 -16.120  1.00 19.76           O  
HETATM 8109  O   HOH A1015      -1.942  -0.317 -44.789  1.00 11.49           O  
HETATM 8110  O   HOH A1016     -20.290 -30.515 -20.909  1.00 13.32           O  
HETATM 8111  O   HOH A1017     -27.812 -13.945 -25.682  1.00 23.47           O  
HETATM 8112  O   HOH A1018      10.710  17.167 -33.068  1.00 32.29           O  
HETATM 8113  O   HOH A1019       5.748 -27.957   7.658  1.00 28.31           O  
HETATM 8114  O   HOH A1020       8.420 -48.188 -57.826  1.00 38.56           O  
HETATM 8115  O   HOH A1021       0.390  12.513 -71.464  1.00 18.71           O  
HETATM 8116  O   HOH A1022      12.650 -47.278 -59.915  1.00 25.98           O  
HETATM 8117  O   HOH A1023       4.644 -15.250 -64.017  1.00 30.56           O  
HETATM 8118  O   HOH A1024       2.053   6.640 -35.707  1.00 12.75           O  
HETATM 8119  O   HOH A1025       8.466  15.882 -64.207  1.00 14.38           O  
HETATM 8120  O   HOH A1026     -12.260 -20.736 -30.457  1.00  6.83           O  
HETATM 8121  O   HOH A1027       5.826 -21.355 -38.605  1.00  7.83           O  
HETATM 8122  O   HOH A1028      15.408  -3.245  -7.444  1.00 43.58           O  
HETATM 8123  O   HOH A1029       5.048 -18.809 -38.594  1.00 13.50           O  
HETATM 8124  O   HOH A1030      -3.639 -30.950  -5.873  1.00 16.71           O  
HETATM 8125  O   HOH A1031       9.407 -33.915 -57.427  1.00 11.57           O  
HETATM 8126  O   HOH A1032      -9.476 -19.502 -35.139  1.00 15.75           O  
HETATM 8127  O   HOH A1033      21.819 -27.368 -27.040  1.00 27.63           O  
HETATM 8128  O   HOH A1034     -25.320  -3.964 -21.651  1.00 17.42           O  
HETATM 8129  O   HOH A1035      -7.376   8.393 -44.794  1.00 28.60           O  
HETATM 8130  O   HOH A1036       3.532 -32.805 -55.421  1.00 19.25           O  
HETATM 8131  O   HOH A1037       1.404 -28.924 -46.452  1.00 26.65           O  
HETATM 8132  O   HOH A1038     -19.394 -31.747 -62.781  1.00 41.32           O  
HETATM 8133  O   HOH A1039     -10.912  -1.644 -62.470  1.00 22.54           O  
HETATM 8134  O   HOH A1040     -22.692 -15.845 -42.413  1.00 26.62           O  
HETATM 8135  O   HOH A1041      27.381 -17.756 -20.145  1.00 19.43           O  
HETATM 8136  O   HOH A1042       4.445 -51.783 -13.426  1.00 22.75           O  
HETATM 8137  O   HOH A1043      19.526  18.475 -45.356  1.00 29.96           O  
HETATM 8138  O   HOH A1044      19.143  15.107 -42.368  1.00 19.16           O  
HETATM 8139  O   HOH A1045      17.174   6.122 -31.349  1.00 19.59           O  
HETATM 8140  O   HOH A1046      27.321 -17.553 -24.315  1.00 18.34           O  
HETATM 8141  O   HOH A1047      21.729  -9.202 -27.236  1.00 17.93           O  
HETATM 8142  O   HOH A1048      28.632 -24.578 -19.374  1.00 22.71           O  
HETATM 8143  O   HOH A1049     -12.131 -24.007 -38.869  1.00 16.67           O  
HETATM 8144  O   HOH A1050      17.681  19.434 -32.428  1.00 26.60           O  
HETATM 8145  O   HOH A1051      -3.115 -16.961 -19.803  1.00 29.79           O  
HETATM 8146  O   HOH A1052      19.912  -4.608 -52.743  1.00 17.79           O  
HETATM 8147  O   HOH A1053     -22.418 -34.660 -55.669  1.00 24.34           O  
HETATM 8148  O   HOH A1054      16.275  -8.421 -22.064  1.00 17.83           O  
HETATM 8149  O   HOH A1055      17.477 -23.393 -24.145  1.00 26.08           O  
HETATM 8150  O   HOH A1056      -6.453 -36.452 -65.819  1.00 28.84           O  
HETATM 8151  O   HOH A1057      13.180 -21.863 -39.594  1.00 17.80           O  
HETATM 8152  O   HOH A1058      24.286 -12.534 -13.927  1.00 34.61           O  
HETATM 8153  O   HOH A1059      14.760   3.343 -28.974  1.00 25.96           O  
HETATM 8154  O   HOH A1060     -25.072 -24.922  -6.226  1.00 22.42           O  
HETATM 8155  O   HOH A1061     -18.537 -31.067 -37.047  1.00 35.35           O  
HETATM 8156  O   HOH A1062     -14.534 -29.557 -31.466  1.00 31.41           O  
HETATM 8157  O   HOH A1063     -21.285 -10.881 -45.868  1.00 18.32           O  
HETATM 8158  O   HOH A1064      20.548  -7.100 -23.398  1.00 16.02           O  
HETATM 8159  O   HOH A1065       5.849  -8.865 -48.828  1.00 21.07           O  
HETATM 8160  O   HOH A1066      19.665 -19.723 -39.433  1.00 38.61           O  
HETATM 8161  O   HOH A1067      28.584  -9.147  -7.493  1.00 30.46           O  
HETATM 8162  O   HOH A1068      10.397 -27.748 -37.920  1.00 17.26           O  
HETATM 8163  O   HOH A1069     -30.226 -16.928 -22.480  1.00 19.90           O  
HETATM 8164  O   HOH A1070      24.025  -1.304 -35.223  1.00 18.25           O  
HETATM 8165  O   HOH A1071     -11.606 -30.164 -46.388  1.00 22.14           O  
HETATM 8166  O   HOH A1072       3.738  -5.090 -11.625  1.00 36.14           O  
HETATM 8167  O   HOH A1073      -1.968  17.360 -56.969  1.00 14.56           O  
HETATM 8168  O   HOH A1074      -6.746 -23.382 -31.601  1.00 30.11           O  
HETATM 8169  O   HOH A1075      23.196  20.684 -37.753  1.00 19.67           O  
HETATM 8170  O   HOH A1076       4.426 -14.917 -55.390  1.00 50.10           O  
HETATM 8171  O   HOH A1077     -18.678  -8.874  -7.718  1.00 29.60           O  
HETATM 8172  O   HOH A1078       9.145 -28.692  -3.847  1.00 21.01           O  
HETATM 8173  O   HOH A1079       9.270 -26.950   7.206  1.00 18.72           O  
HETATM 8174  O   HOH A1080      10.928  10.343 -35.273  1.00 47.35           O  
HETATM 8175  O   HOH A1081      22.203 -28.574  -0.876  1.00 33.62           O  
HETATM 8176  O   HOH A1082     -20.751  -6.800 -26.798  1.00 19.77           O  
HETATM 8177  O   HOH A1083       3.889 -35.227  -1.660  1.00 15.00           O  
HETATM 8178  O   HOH A1084      13.897 -48.137 -46.680  1.00 40.52           O  
HETATM 8179  O   HOH A1085       1.196  14.462 -53.721  1.00 22.44           O  
HETATM 8180  O   HOH A1086     -36.206 -24.145 -46.348  1.00 32.55           O  
HETATM 8181  O   HOH A1087       2.919   6.104 -71.104  1.00 25.52           O  
HETATM 8182  O   HOH A1088      17.733 -39.880 -21.535  1.00 40.48           O  
HETATM 8183  O   HOH A1089      35.446  -3.204 -28.078  1.00 28.96           O  
HETATM 8184  O   HOH A1090       4.165 -28.543 -11.381  1.00 28.45           O  
HETATM 8185  O   HOH A1091     -24.993 -13.743 -46.547  1.00 18.14           O  
HETATM 8186  O   HOH A1092      10.518   8.766 -70.047  1.00 32.70           O  
HETATM 8187  O   HOH A1093     -10.145   1.395 -49.872  1.00 22.35           O  
HETATM 8188  O   HOH A1094     -22.365 -14.292 -40.193  1.00 17.08           O  
HETATM 8189  O   HOH A1095       2.796 -16.030 -46.595  1.00 22.41           O  
HETATM 8190  O   HOH A1096     -15.036 -30.045 -40.026  1.00 15.61           O  
HETATM 8191  O   HOH A1097       0.247  -9.724 -40.617  1.00 26.63           O  
HETATM 8192  O   HOH A1098      11.629  11.122 -43.144  1.00 31.31           O  
HETATM 8193  O   HOH A1099       2.553 -30.539 -56.526  1.00 13.99           O  
HETATM 8194  O   HOH A1100      30.024 -20.123 -24.991  1.00 20.11           O  
HETATM 8195  O   HOH A1101     -27.615 -14.563 -40.773  1.00 24.57           O  
HETATM 8196  O   HOH A1102      12.661  12.873 -46.935  1.00 17.21           O  
HETATM 8197  O   HOH A1103      32.625   4.951 -17.772  1.00 24.15           O  
HETATM 8198  O   HOH A1104      11.349  -6.947 -36.058  1.00 16.53           O  
HETATM 8199  O   HOH A1105       1.892 -30.960 -48.343  1.00 24.82           O  
HETATM 8200  O   HOH A1106       2.677  -4.313 -34.422  1.00 15.46           O  
HETATM 8201  O   HOH A1107      13.747 -26.145 -53.326  1.00 28.62           O  
HETATM 8202  O   HOH A1108      -0.150 -24.679 -18.572  1.00 32.61           O  
HETATM 8203  O   HOH A1109      14.043 -38.458 -43.803  1.00 26.16           O  
HETATM 8204  O   HOH A1110      -3.548 -31.028 -31.678  1.00 45.04           O  
HETATM 8205  O   HOH A1111      16.056  26.879 -35.529  1.00 35.86           O  
HETATM 8206  O   HOH A1112       6.217 -24.121  -0.759  1.00 20.50           O  
HETATM 8207  O   HOH A1113     -32.152 -37.487 -53.668  1.00 31.02           O  
HETATM 8208  O   HOH A1114     -16.908 -31.437 -28.427  1.00 29.35           O  
HETATM 8209  O   HOH A1115      -5.738 -17.439 -53.536  1.00 18.66           O  
HETATM 8210  O   HOH A1116      -9.313   9.689 -56.840  1.00 23.66           O  
HETATM 8211  O   HOH A1117      24.729 -17.073  -3.741  1.00 26.46           O  
HETATM 8212  O   HOH A1118     -15.294  -1.141 -53.214  1.00 24.18           O  
HETATM 8213  O   HOH A1119     -19.210  -1.129 -51.698  1.00 31.67           O  
HETATM 8214  O   HOH A1120       2.533 -24.457 -37.779  1.00 23.39           O  
HETATM 8215  O   HOH A1121      -9.558 -29.417 -29.395  1.00 26.43           O  
HETATM 8216  O   HOH A1122      16.045 -39.022  -8.318  1.00 17.78           O  
HETATM 8217  O   HOH A1123      25.743 -16.508 -39.365  1.00 30.97           O  
HETATM 8218  O   HOH A1124       3.684 -40.404 -10.236  1.00 24.39           O  
HETATM 8219  O   HOH A1125       3.941 -22.971 -39.572  1.00 16.48           O  
HETATM 8220  O   HOH A1126       1.958  -6.704 -12.187  1.00 38.34           O  
HETATM 8221  O   HOH A1127      -4.873  -2.072 -53.289  1.00 19.73           O  
HETATM 8222  O   HOH A1128      -2.794  -0.602 -52.083  1.00 14.74           O  
HETATM 8223  O   HOH A1129      16.834 -32.221 -25.081  1.00 27.62           O  
HETATM 8224  O   HOH A1130      18.857 -22.098 -31.869  1.00 32.16           O  
HETATM 8225  O   HOH A1131      -0.936 -30.353 -23.726  1.00 37.15           O  
HETATM 8226  O   HOH A1132      17.043 -23.794 -44.707  1.00 29.60           O  
HETATM 8227  O   HOH A1133      19.110 -21.745 -44.874  1.00 36.07           O  
HETATM 8228  O   HOH A1134      15.052 -17.883 -39.940  1.00 19.37           O  
HETATM 8229  O   HOH A1135      13.901 -19.695 -38.044  1.00 20.99           O  
HETATM 8230  O   HOH A1136      19.990 -13.662 -42.065  1.00 30.07           O  
HETATM 8231  O   HOH A1137      17.833 -12.329 -41.363  1.00 33.25           O  
HETATM 8232  O   HOH A1138       8.857 -14.818 -52.738  1.00  8.76           O  
HETATM 8233  O   HOH A1139      13.995 -31.225 -28.679  1.00 38.32           O  
HETATM 8234  O   HOH A1140      26.827   7.927 -32.033  1.00 15.01           O  
HETATM 8235  O  AHOH A1141      11.786   2.656 -67.658  0.50  2.00           O  
HETATM 8236  O  BHOH A1141       9.952   2.340 -66.977  0.50  3.42           O  
HETATM 8237  O   HOH A1142       9.525  -7.630 -68.359  1.00 32.68           O  
HETATM 8238  O   HOH A1143     -25.803 -33.004 -52.491  1.00 23.48           O  
HETATM 8239  O   HOH A1144      11.105  11.035 -45.924  1.00 22.03           O  
HETATM 8240  O   HOH A1145     -11.957  -1.153 -70.625  1.00 17.44           O  
HETATM 8241  O   HOH A1146      -5.996  -1.550 -72.267  1.00 17.03           O  
HETATM 8242  O   HOH A1147      -1.778  -4.487 -72.205  1.00 23.15           O  
HETATM 8243  O   HOH A1148      -6.314  -4.979 -72.896  1.00 16.33           O  
HETATM 8244  O   HOH A1149     -15.500  -6.270 -69.116  1.00 37.11           O  
HETATM 8245  O   HOH A1150     -13.371  -5.333 -70.232  1.00 26.46           O  
HETATM 8246  O   HOH A1151      23.978   9.247 -22.472  1.00 19.41           O  
HETATM 8247  O   HOH A1152      16.987  15.660 -60.391  1.00 41.10           O  
HETATM 8248  O   HOH A1153     -23.260 -12.817 -68.564  1.00 24.62           O  
HETATM 8249  O   HOH A1154     -10.655 -23.768 -27.018  1.00 17.66           O  
HETATM 8250  O   HOH A1155     -10.673 -26.487 -26.734  1.00 22.81           O  
HETATM 8251  O   HOH A1156     -12.971 -27.854 -27.311  1.00 20.95           O  
HETATM 8252  O   HOH A1157       9.424 -10.566 -38.523  1.00 18.01           O  
HETATM 8253  O   HOH A1158       8.301  15.682 -67.130  1.00 14.79           O  
HETATM 8254  O   HOH A1159       9.893  18.079 -63.156  1.00 20.79           O  
HETATM 8255  O   HOH A1160       5.871  16.292 -63.852  1.00  9.97           O  
HETATM 8256  O   HOH A1161       5.506  18.193 -61.821  1.00 12.67           O  
HETATM 8257  O   HOH A1162      20.171  12.047 -34.168  1.00 25.22           O  
HETATM 8258  O   HOH A1163       3.342 -13.346  -3.733  1.00 23.42           O  
HETATM 8259  O   HOH A1164      10.360 -47.441 -40.296  1.00 15.47           O  
HETATM 8260  O   HOH A1165      22.373 -13.002 -39.430  1.00 21.21           O  
HETATM 8261  O   HOH A1166      -9.061 -24.164 -36.509  1.00 34.21           O  
HETATM 8262  O   HOH A1167      -3.943 -27.308 -35.924  1.00 39.49           O  
HETATM 8263  O   HOH A1168      11.287  13.203 -30.721  1.00 35.69           O  
HETATM 8264  O   HOH A1169      11.251  11.390 -37.729  1.00 23.95           O  
HETATM 8265  O   HOH A1170       9.929  14.644 -43.748  1.00 25.70           O  
HETATM 8266  O   HOH A1171      17.832  14.142 -52.205  1.00 32.55           O  
HETATM 8267  O   HOH A1172       7.338  -8.050 -26.509  1.00 29.78           O  
HETATM 8268  O   HOH A1173       9.386  -8.130 -37.658  1.00 25.99           O  
HETATM 8269  O   HOH T  19     -11.773  -0.362 -50.976  1.00 12.89           O  
HETATM 8270  O   HOH T  20       3.055   3.786 -32.191  1.00 24.57           O  
HETATM 8271  O   HOH T  41     -19.119  -6.534 -48.199  1.00 21.65           O  
HETATM 8272  O   HOH T  64     -17.982 -10.333 -34.924  1.00 15.29           O  
HETATM 8273  O   HOH T  71      -5.456   5.548 -40.886  1.00 18.28           O  
HETATM 8274  O   HOH T  75     -41.487   7.986 -32.815  1.00  3.18           O  
HETATM 8275  O   HOH T 200     -24.346 -14.682 -38.626  1.00 34.01           O  
HETATM 8276  O   HOH T 205     -39.611  -1.189 -30.246  1.00 10.60           O  
HETATM 8277  O   HOH T 220     -26.593 -12.865 -33.094  1.00 23.37           O  
HETATM 8278  O   HOH T 224     -18.672  -2.733 -48.200  1.00 24.81           O  
HETATM 8279  O   HOH T 231     -21.483  -2.119 -47.039  1.00 32.19           O  
HETATM 8280  O   HOH T 232     -22.791  -4.202 -48.690  1.00 32.06           O  
HETATM 8281  O   HOH T 237      -5.119  -1.851 -46.424  1.00 18.12           O  
HETATM 8282  O   HOH T 284       7.350  -3.686 -30.490  1.00 24.09           O  
HETATM 8283  O   HOH P  12      -8.408 -17.636 -42.503  1.00 16.44           O  
HETATM 8284  O   HOH P  84     -17.762   1.208 -35.114  1.00 25.99           O  
HETATM 8285  O   HOH P 188     -10.331  -4.395 -29.156  1.00 26.34           O  
HETATM 8286  O   HOH P 195      -7.423  -4.967 -47.062  1.00 26.45           O  
HETATM 8287  O   HOH P 248      -7.355 -12.257 -51.412  1.00 24.85           O  
HETATM 8288  O   HOH P 250     -20.598  -0.535 -38.806  1.00 39.45           O  
CONECT  977 8001                                                                
CONECT  978 8001                                                                
CONECT 3419 7997                                                                
CONECT 3420 7997 7998                                                           
CONECT 3424 7997                                                                
CONECT 4161 7999                                                                
CONECT 4179 7999                                                                
CONECT 4379 7999                                                                
CONECT 5121 7997                                                                
CONECT 5122 7998                                                                
CONECT 7383 7394                                                                
CONECT 7394 7383 7395 7396 7397                                                 
CONECT 7395 7394                                                                
CONECT 7396 7394                                                                
CONECT 7397 7394 7398                                                           
CONECT 7398 7397 7399                                                           
CONECT 7399 7398 7400 7401                                                      
CONECT 7400 7399 7404                                                           
CONECT 7401 7399 7402 7403                                                      
CONECT 7402 7401 7415                                                           
CONECT 7403 7401 7404                                                           
CONECT 7404 7400 7403 7405                                                      
CONECT 7405 7404 7406 7414                                                      
CONECT 7406 7405 7407                                                           
CONECT 7407 7406 7408                                                           
CONECT 7408 7407 7409 7414                                                      
CONECT 7409 7408 7410                                                           
CONECT 7410 7409 7411                                                           
CONECT 7411 7410 7412 7413                                                      
CONECT 7412 7411                                                                
CONECT 7413 7411 7414                                                           
CONECT 7414 7405 7408 7413                                                      
CONECT 7415 7402                                                                
CONECT 7933 7947                                                                
CONECT 7947 7933 7948 7949 7950                                                 
CONECT 7948 7947                                                                
CONECT 7949 7947                                                                
CONECT 7950 7947 7951                                                           
CONECT 7951 7950 7952                                                           
CONECT 7952 7951 7953 7954                                                      
CONECT 7953 7952 7956                                                           
CONECT 7954 7952 7955                                                           
CONECT 7955 7954 7956                                                           
CONECT 7956 7953 7955 7957                                                      
CONECT 7957 7956 7958 7966                                                      
CONECT 7958 7957 7959                                                           
CONECT 7959 7958 7960                                                           
CONECT 7960 7959 7961 7966                                                      
CONECT 7961 7960 7962 7963                                                      
CONECT 7962 7961                                                                
CONECT 7963 7961 7964                                                           
CONECT 7964 7963 7965                                                           
CONECT 7965 7964 7966                                                           
CONECT 7966 7957 7960 7965                                                      
CONECT 7968 7969 7970 7971 7980                                                 
CONECT 7969 7968                                                                
CONECT 7970 7968 7997 7998                                                      
CONECT 7971 7968 7972                                                           
CONECT 7972 7971 7973 7974 7975                                                 
CONECT 7973 7972                                                                
CONECT 7974 7972 7997                                                           
CONECT 7975 7972 7976                                                           
CONECT 7976 7975 7977 7978 7979                                                 
CONECT 7977 7976 7997                                                           
CONECT 7978 7976                                                                
CONECT 7979 7976                                                                
CONECT 7980 7968 7981                                                           
CONECT 7981 7980 7982                                                           
CONECT 7982 7981 7983 7984                                                      
CONECT 7983 7982 7987                                                           
CONECT 7984 7982 7985 7986                                                      
CONECT 7985 7984                                                                
CONECT 7986 7984 7987                                                           
CONECT 7987 7983 7986 7988                                                      
CONECT 7988 7987 7989 7996                                                      
CONECT 7989 7988 7990 7991                                                      
CONECT 7990 7989                                                                
CONECT 7991 7989 7992                                                           
CONECT 7992 7991 7993 7994                                                      
CONECT 7993 7992                                                                
CONECT 7994 7992 7995 7996                                                      
CONECT 7995 7994                                                                
CONECT 7996 7988 7994                                                           
CONECT 7997 3419 3420 3424 5121                                                 
CONECT 7997 7970 7974 7977                                                      
CONECT 7998 3420 5122 7970                                                      
CONECT 7999 4161 4179 4379                                                      
CONECT 8000 8170                                                                
CONECT 8001  977  978 8055                                                      
CONECT 8055 8001                                                                
CONECT 8170 8000                                                                
MASTER      516    0    8   38   36    0   10    6 8273    3   91   73          
END

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Related entries of code: 3sq4

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
3suo	RCSB PDB PDBbind	13aa, >3SUO_3\|Chain... at 100%
3sup	RCSB PDB PDBbind	13aa, >3SUP_3\|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
3suo	RCSB PDB PDBbind	dTTP Opposite 2AP (GC rich sequence) DNA

Entry Information

PDB ID	3sq4
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	RB69 DNA Polymerase
Ligand Name	dTTP Opposite 2AP (GC rich sequence) DNA
EC.Number	E.C.2.7.7.7
Resolution	2.23(Å)
Affinity (Kd/Ki/IC50)	Kd=30uM
Release Year	2011
Protein/NA Sequence	Check fasta file
Primary Reference	(2011) Biochemistry Vol. 50: pp. 10136-10149

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): Q38087
Entrez Gene ID	NCBI Entrez Gene ID: 1494172
ASD	Information of known allosteric effects of PDB entries

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